Human Metabolome Database Version 2.5

Showing metabocard for Adenosine monophosphate (HMDB00045)

Legend: metabolite field enzyme field

Version

2.5

Creation Date

2005-11-16 15:48:42

Update Date

2009-05-29 16:25:53

Accession Number

HMDB00045

Secondary Accession Numbers

Not Available

Common Name

Adenosine monophosphate

Description

Adenosine monophosphate, also known as 5'-adenylic acid and abbreviated AMP, is a nucleotide that is found in RNA. It is an ester of phosphoric acid with the nucleoside adenosine. AMP consists of the phosphate group, the pentose sugar ribose, and the nucleobase adenine. AMP can be produced during ATP synthesis by the enzyme adenylate kinase. AMP has recently been approved as a 'Bitter Blocker' additive to foodstuffs. When AMP is added to bitter foods or foods with a bitter aftertaste it makes them seem 'sweeter'. This potentially makes lower calorie food products more palatable

Synonyms

5'-AMP
5'-adenosine monophosphate
5'-adenylate
5'-adenylic acid
AMP
Adenosine 5'-monophosphate
Adenosine 5'-phosphate
Adenosine 5'-phosphorate
Adenosine 5'-phosphoric acid
Adenosine phosphate
Adenosine-5'-monophosphorate
Adenosine-5'-monophosphoric acid
Adenosine-5-monophosphorate
Adenosine-5-monophosphoric acid
Adenovite
Adenylate
Adenylic acid
Cardiomone
Lycedan
Muscle adenylate
Muscle adenylic acid
My-B-Den
Phosaden
Phosphaden
Phosphentaside
adenosine-monophosphate
adenosine-phosphate
My-beta-Den

Chemical IUPAC Name

[(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxyphosphonic acid

Chemical Formula

C₁₀H₁₄N₅O₇P

Chemical Structure

Chemical Taxonomy

Kingdom
Organic
Super Class
Nucleosides and Nucleoside conjugates
Class
Nucleotides
Sub Class
Nucleotide monophosphates
Family
Mammalian Metabolite
Species
secondary alcohol 1,2-diol primary amine primary aromatic amine phosphoric acid ester aromatic compound heterocyclic compound
Biofunction
Component of Alanine and aspartate metabolism Component of Aminoacyl-tRNA biosynthesis Component of Arginine and proline metabolism Component of Biotin metabolism Component of Fatty acid metabolism Component of Glutamate metabolism Component of Glycine, serine and threonine metabolism Component of Histidine metabolism Component of Lysine biosynthesis Component of Methionine metabolism Component of Nitrogen metabolism Component of Phenylalanine, tyrosine and tryptophan biosynthesis Component of Porphyrin and chlorophyll metabolism Component of Propanoate metabolism Component of Purine metabolism Component of Pyrimidine metabolism Component of Pyruvate metabolism Component of Selenoamino acid metabolism Component of Sulfur metabolism Component of Thiamine metabolism Component of Tryptophan metabolism Component of Valine, leucine and isoleucine biosynthesis
Application
—
Source
Endogenous

Average Molecular Weight

347.221

Monoisotopic Molecular Weight

347.063080

Isomeric SMILES

NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O

Canonical SMILES

NC1=NC=NC2=C1N=CN2C1OC(COP(O)(O)=O)C(O)C1O

KEGG Compound ID

C00020

BioCyc ID

AMP

BiGG ID

33534

Wikipedia Link

Adenosine monophosphate Link Image

NuGOwiki Link

Metagene Link

METLIN ID

PubChem Compound

PubChem Substance

ChEBI ID

CAS Registry Number

61-19-8

InChI Identifier

InChI=1/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1

Synthesis Reference

Not Available

Melting Point (Experimental)

195 oC

Experimental Water Solubility

10 mg/mL at 20 oC [BEILSTEIN]; 801 mg/mL (sodium salt, HMP expt) Source: PhysProp

Predicted Water Solubility

3.31 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS

Physiological Charge

-2

State

Solid

Experimental LogP/Hydrophobicity

Not Available Source: PhysProp

Predicted LogP/Hydrophobicity

-3.13 [Predicted by ALOGPS]; -3.1 [Predicted by PubChem via XLOGP]; -1.68 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS

Material Safety Data Sheet (MSDS)

Show PDF/HTML

MOL File

Show

SDF File

Show

PDB File

Show

2D Structure

3D Structure

Experimental PDB ID

12AS

Experimental PDB File

Show

Experimental PDB Structure

Experimental ¹H NMR Spectrum

Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image

Experimental ¹³C NMR Spectrum

Not Available

Experimental ¹³C HSQC Spectrum

Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image

Predicted ¹H NMR Spectrum

Show Image
Show Peaklist

Predicted ¹³C NMR Spectrum

Show Image
Show Peaklist

Mass Spectrum

Not Available

Simplified TOCSY Spectrum

Show Image
Show Peaklist

BMRB Spectrum

Show Image
Show Peaklist

Cellular Location

Cytoplasm (Predicted from LogP)
Nucleus
endoplasmic reticulum
Extracellular
golgi apparatus
lysosome
mitochondria
peroxisome

Biofluid Location

Blood
Cellular Cytoplasm
Cerebrospinal Fluid

Tissue Location

Tissue	References
All Tissues	—

Concentrations (Normal)

Biofluid	Blood
Value	51.0 (10.0-92.0) uM
Age	Adult:>18 yrs old
Sex	Both
Patient information	Normal
Comments	Not Available
References	Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.

Biofluid	Blood
Value	14.0 +/- 3.0 uM
Age	Adult:>18 yrs old
Sex	Male
Patient information	Normal
Comments	Not Available
References	Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.

Biofluid	Blood
Value	6.2 +/- 3.1 uM
Age	Adult:>18 yrs old
Sex	Male
Patient information	Normal
Comments	Not Available
References	BISHOP C, RANKINE DM, TALBOTT JH: The nucleotides in normal human blood. J Biol Chem. 1959 May;234(5):1233-7. [PubMed ]

Biofluid	Blood
Value	5.1+/- 1.3 uM
Age	Adult:>18 yrs old
Sex	Female
Patient information	Normal
Comments	Not Available
References	BISHOP C, RANKINE DM, TALBOTT JH: The nucleotides in normal human blood. J Biol Chem. 1959 May;234(5):1233-7. [PubMed ]

Biofluid	Cellular Cytoplasm
Value	23 uM
Age	Children:1-13 yrs old
Sex	Both
Patient information	Normal
Comments	Not Available
References	Pagani R, Tabucchi A, Carlucci F, Leoncini R, Consolmagno E, Molinelli M, Valerio P: Some aspects of purine nucleotide metabolism in human lymphocytes before and after infection with HIV-1 virus: nucleotide content. Adv Exp Med Biol. 1991;309B:43-6. [PubMed ]

Biofluid	Cellular Cytoplasm
Value	80.0 (71.0-89.0) uM
Age	Children:1-13 yrs old
Sex	Both
Patient information	Normal
Comments	Not Available
References	Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed ]

Biofluid	CSF
Value	< 0.2 uM
Age	Adult:>18 yrs old
Sex	Both
Patient information	Normal
Comments	Not Available
References	Eells JT, Spector R: Purine and pyrimidine base and nucleoside concentrations in human cerebrospinal fluid and plasma. Neurochem Res. 1983 Nov;8(11):1451-7. [PubMed ]

Concentrations (Abnormal)

Not Available

Associated Disorders

Not Available

OMIM ID

Not Available

Pathways

Name	SMPDB Link	KEGG Link
Ammonia Recycling	SMP00009	map00910
Ethanol Degradation	SMP00449
Glycine and Serine Metabolism	SMP00004	map00260
Histidine Metabolism	SMP00044	map00340
Mitochondrial Beta-Oxidation of Long Chain Saturated Fatty Acids	SMP00482
Mitochondrial Beta-Oxidation of Medium Chain Saturated Fatty Acids	SMP00481
Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids	SMP00480
Purine Metabolism	SMP00050	map00230
Transcription/Translation	SMP00019
Urea Cycle	SMP00059	map00330

General References

Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed ]
BISHOP C, RANKINE DM, TALBOTT JH: The nucleotides in normal human blood. J Biol Chem. 1959 May;234(5):1233-7. [PubMed ]
Lin CY, Ishida M: Elevation of cAMP levels in cerebrospinal fluid of patients with neonatal meningitis. Pediatrics. 1983 Jun;71(6):932-4. [PubMed ]
Pagani R, Tabucchi A, Carlucci F, Leoncini R, Consolmagno E, Molinelli M, Valerio P: Some aspects of purine nucleotide metabolism in human lymphocytes before and after infection with HIV-1 virus: nucleotide content. Adv Exp Med Biol. 1991;309B:43-6. [PubMed ]
Drezner MK, Neelon FA, Curtis HB, Lebovitz HE: Renal cyclic adenosine monophosphate: an accurate index of parathyroid function. Metabolism. 1976 Oct;25(10):1103-12. [PubMed ]
Aschenbach WG, Sakamoto K, Goodyear LJ: 5' adenosine monophosphate-activated protein kinase, metabolism and exercise. Sports Med. 2004;34(2):91-103. [PubMed ]
Subramanian GM, Cronin PW, Poley G, Weinstein A, Stoughton SM, Zhong J, Ou Y, Zmuda JF, Osborn BL, Freimuth WW: A phase 1 study of PAmAb, a fully human monoclonal antibody against Bacillus anthracis protective antigen, in healthy volunteers. Clin Infect Dis. 2005 Jul 1;41(1):12-20. Epub 2005 May 24. [PubMed ]
Aurbach GD: Genetic disorders involving parathyroid hormone and calcitonin. Birth Defects Orig Artic Ser. 1971 May;7(6):48-54. [PubMed ]
Eells JT, Spector R: Purine and pyrimidine base and nucleoside concentrations in human cerebrospinal fluid and plasma. Neurochem Res. 1983 Nov;8(11):1451-7. [PubMed ]
Post RM, Cramer H, Goodwin FK: Cyclic AMP in cerebrospinal fluid of manic and depressive patients. Psychol Med. 1977 Nov;7(4):599-605. [PubMed ]
Wikipedia

Metabolic Enzymes

Enzyme 1 [top]

Enzyme 1 ID

5232

Enzyme 1 Name

Cytosolic 5'-nucleotidase 1B

Enzyme 1 Synonyms

cN1B
Autoimmune infertility-related protein
Cytosolic 5'-nucleotidase IB
cN-IB

Enzyme 1 Gene Name

NT5C1B

Enzyme 1 Protein Sequence

>Cytosolic 5'-nucleotidase 1B

MSQTSLKQKKNEPGMRSSKESLEAEKRKESDKTGVRLSNQMRRAVNPNHSLRCCPFQGHS
SCRRCLCAAEGTALGPCHTIRIYIHMCLLWEQGQQITMMRGSQESSLRKTDSRGYLVRSQ
WSRISRSPSTKAPSIDEPRSRNTSAKLPSSSTSSRTPSTSPSLHDSSPPPLSGQPSLQPP
ASPQLPRSLDSRPPTPPEPDPGSRRSTKMQENPEAWAQGIVREIRQTRDSQPLEYSRTSP
TEWKSSSQRRGIYPASTQLDRNSLSEQQQQQREDEDDYEAAYWASMRSFYEKNPSCSRPW
PPKPKNAITIALSSCALFNMVDGRKIYEQEGLEKYMEYQLTNENVILTPGPAFRFVKALQ
YVNARLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKDPIGYLK
AYLTNLYIAADSEKVQEAIQEGIASATMFDGAKDMAYCDTQLRVAFDGDAVLFSDESEHF
TKEHGLDKFFQYDTLCESKPLAQGPLKGFLEDLGRLQKKFYAKNERLLCPIRTYLVTARS
AASSGARVLKTLRRWGLEIDEALFLAGAPKSPILVKIRPHIFFDDHMFHIEGAQRLGSIA
AYGFNKKFSS

Enzyme 1 Number of Residues

610

Enzyme 1 Molecular Weight

68803.1

Enzyme 1 Theoretical pI

9.03

Enzyme 1 GO Classification

Function
5'-nucleotidase activity binding catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding magnesium ion binding metal ion binding nucleotidase activity nucleotide binding phosphatase activity phosphoric ester hydrolase activity
Process
cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside phosphate metabolic process nucleotide metabolic process
Component
cell part cytoplasm intracellular part

Enzyme 1 General Function

Involved in nucleotide binding

Enzyme 1 Specific Function

Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels

Enzyme 1 Pathways

Nicotinate and Nicotinamide Metabolism (map00760 )
Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 1 Reactions

a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]

Enzyme 1 Pfam Domain Function

5-nucleotidase (PF06189 )

Enzyme 1 Signals

None

Enzyme 1 Transmembrane Regions

None

Enzyme 1 Essentiality

Not Available

Enzyme 1 GenBank ID Protein

50593110

Enzyme 1 UniProtKB/Swiss-Prot ID

Q96P26

Enzyme 1 UniProtKB/Swiss-Prot Entry Name

5NT1B_HUMAN Link Image

Enzyme 1 PDB ID

Not Available

Enzyme 1 Cellular Location

Not Available

Enzyme 1 Gene Sequence

>1833 bp

ATGAGTCAAACATCTCTCAAACAGAAAAAGAATGAGCCTGGAATGAGGTCCTCAAAAGAG
AGTCTAGAAGCAGAAAAAAGAAAGGAATCTGACAAAACAGGAGTTCGTCTGAGCAATCAG
ATGAGGCGTGCAGTCAATCCGAATCACTCGCTGAGATGTTGCCCCTTCCAGGGTCACTCG
TCGTGTAGACGCTGCCTTTGTGCAGCTGAGGGAACAGCCCTTGGCCCCTGCCACACAATA
CGTATTTATATTCACATGTGCCTGTTGTGGGAGCAGGGCCAGCAGATCACCATGATGAGG
GGATCACAAGAATCATCACTGCGGAAGACAGACTCTCGAGGGTACCTTGTGCGCAGTCAA
TGGTCTAGAATATCCCGGAGCCCATCCACCAAGGCTCCATCCATAGATGAGCCTAGAAGC
AGGAACACCAGTGCTAAGCTCCCCAGCAGCTCCACGAGCTCCCGGACTCCATCCACCTCC
CCAAGCCTGCATGACTCCTCACCGCCGCCGCTGTCCGGGCAGCCCTCGCTCCAGCCACCC
GCGTCGCCCCAGCTGCCCCGGTCGCTGGACTCGCGGCCTCCCACGCCCCCAGAGCCCGAT
CCTGGCTCCCGGCGCAGCACCAAAATGCAAGAGAATCCGGAGGCCTGGGCCCAAGGCATC
GTGCGGGAAATCCGCCAGACCCGGGACTCGCAGCCGCTGGAATATTCGCGCACGTCCCCC
ACCGAGTGGAAGTCCTCCAGCCAGCGCAGGGGGATCTACCCCGCCTCCACCCAGCTGGAC
CGCAACTCTCTGTCCGAGCAGCAGCAGCAGCAGCGGGAGGACGAGGACGACTACGAGGCT
GCCTACTGGGCATCCATGAGGTCGTTCTACGAGAAGAACCCGAGCTGCTCGCGCCCCTGG
CCGCCCAAACCCAAGAACGCCATCACCATTGCTCTCTCATCCTGCGCGCTCTTCAACATG
GTGGACGGCAGGAAAATCTACGAGCAAGAGGGTCTGGAAAAGTACATGGAGTATCAGCTC
ACCAATGAGAACGTCATCCTGACCCCGGGCCCGGCGTTCCGCTTCGTCAAGGCACTACAG
TATGTCAATGCTAGACTCCGTGATCTATATCCTGATGAACAGGACTTATTTGATATTGTA
CTGATGACTAATAACCATGCCCAAGTGGGAGTGCGGCTTATAAACAGCGTCAATCACTAC
GGCTTACTGATTGACCGCTTCTGTCTGACCGGGGGAAAAGACCCCATTGGCTATTTGAAG
GCATATCTTACCAACTTGTATATTGCTGCAGATTCTGAAAAAGTGCAAGAGGCAATACAA
GAAGGTATTGCCTCTGCGACAATGTTTGATGGAGCCAAAGACATGGCTTACTGTGACACT
CAGCTCCGTGTAGCCTTTGATGGGGATGCTGTCCTCTTCTCTGATGAGTCTGAACATTTT
ACCAAGGAGCATGGGCTCGACAAATTCTTCCAGTATGATACATTATGTGAAAGTAAGCCT
CTTGCTCAGGGTCCCCTAAAAGGCTTTCTGGAAGATTTAGGCAGACTGCAAAAGAAGTTC
TATGCCAAAAATGAACGGTTACTTTGTCCTATCAGGACCTACCTGGTTACAGCTAGGAGT
GCAGCCAGTTCAGGCGCCCGTGTGCTGAAGACCCTTCGACGCTGGGGTCTAGAGATAGAC
GAAGCTCTTTTCCTTGCTGGAGCCCCCAAAAGTCCCATCTTGGTGAAGATCCGGCCCCAC
ATCTTCTTTGATGACCACATGTTCCACATTGAAGGGGCACAGAGGTTAGGTTCCATCGCA
GCTTATGGCTTTAATAAAAAATTCAGTAGTTAG

Enzyme 1 GenBank Gene ID

NM_001002006.2 Link Image

Enzyme 1 GeneCard ID

NT5C1B

Enzyme 1 GenAtlas ID

NT5C1B

Enzyme 1 HGNC ID

HGNC:17818 Link Image

Enzyme 1 Chromosome Location

Enzyme 1 Locus

2p24.2

Enzyme 1 SNPs

SNPJam Report Link Image

Enzyme 1 General References

Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Sala-Newby GB, Newby AC: Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene related to human autoimmune infertility-related protein. Biochim Biophys Acta. 2001 Oct 31;1521(1-3):12-8. [PubMed ]

Enzyme 1 Metabolite References

Not Available

Enzyme 2 [top]

Enzyme 2 ID

5233

Enzyme 2 Name

Cytosolic 5'-nucleotidase 1A

Enzyme 2 Synonyms

cN1A
Cytosolic 5'-nucleotidase IA
cN-I
cN-IA

Enzyme 2 Gene Name

NT5C1A

Enzyme 2 Protein Sequence

>Cytosolic 5'-nucleotidase 1A

MEPGQPREPQEPREPGPGAETAAAPVWEEAKIFYDNLAPKKKPKSPKPQNAVTIAVSSRA
LFRMDEEQQIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNRRLRELYPDSEDV
FDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVR
EAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAH
ENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWG
LETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQTPRRTAP
AKQAPSAQ

Enzyme 2 Number of Residues

368

Enzyme 2 Molecular Weight

41020.1

Enzyme 2 Theoretical pI

6.52

Enzyme 2 GO Classification

Function
5'-nucleotidase activity binding catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding magnesium ion binding metal ion binding nucleotidase activity nucleotide binding phosphatase activity phosphoric ester hydrolase activity
Process
cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside phosphate metabolic process nucleotide metabolic process
Component
cell part cytoplasm intracellular part

Enzyme 2 General Function

Involved in nucleotide binding

Enzyme 2 Specific Function

Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia

Enzyme 2 Pathways

Nicotinate and Nicotinamide Metabolism (map00760 )
Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 2 Reactions

a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]

Enzyme 2 Pfam Domain Function

5-nucleotidase (PF06189 )

Enzyme 2 Signals

None

Enzyme 2 Transmembrane Regions

None

Enzyme 2 Essentiality

Not Available

Enzyme 2 GenBank ID Protein

12659324

Enzyme 2 UniProtKB/Swiss-Prot ID

Q9BXI3

Enzyme 2 UniProtKB/Swiss-Prot Entry Name

5NT1A_HUMAN Link Image

Enzyme 2 PDB ID

Not Available

Enzyme 2 Cellular Location

Not Available

Enzyme 2 Gene Sequence

>1107 bp

ATGGAACCTGGGCAGCCCCGGGAGCCCCAGGAGCCCCGCGAGCCCGGGCCAGGAGCGGAG
ACCGCTGCGGCCCCGGTCTGGGAGGAAGCCAAGATTTTCTACGACAACCTCGCGCCCAAG
AAGAAACCCAAATCGCCCAAGCCTCAGAATGCAGTCACCATCGCTGTGTCCTCCCGAGCC
TTGTTTCGCATGGACGAGGAGCAGCAGATCTACACGGAGCAGGGCGTGGAGGAGTACGTG
CGCTACCAGCTGGAACATGAGAACGAACCCTTCAGTCCCGGGCCAGCCTTCCCTTTTGTG
AAGGCTCTGGAGGCCGTGAACAGGCGGCTGCGGGAGCTGTACCCTGATAGTGAGGACGTC
TTCGACATCGTCCTCATGACTAACAACCATGCTCAAGTGGGTGTCCGCCTCATCAACAGT
ATCAACCACTATGACCTGTTCATCGAGAGGTTCTGCATGACAGGTGGGAACAGCCCGATC
TGCTACCTCAAGGCCTATCACACCAACCTCTACTTGTCAGCCGATGCGGAAAAAGTGCGA
GAAGCCATTGATGAGGGGATCGCAGCTGCCACCATCTTCAGCCCCAGCAGGGATGTGGTT
GTGTCCCAGAGTCAGCTGCGCGTGGCCTTCGATGGGGACGCCGTGCTCTTCTCGGACGAG
TCGGAGCGCATCGTCAAGGCCCACGGGCTGGACCGATTCTTCGAGCATGAGAAGGCCCAC
GAGAACAAGCCTCTGGCTCAGGGCCCCTTAAAGGGCTTTCTGGAGGCACTGGGTAGGTTG
CAGAAGAAGTTCTACTCCAAAGGCCTGCGGCTGGAGTGCCCAATTCGTACCTACTTGGTG
ACAGCACGCAGTGCAGCCAGTTCCGGGGCCCGGGCTCTCAAGACCCTGCGCAGCTGGGGC
CTGGAGACAGATGAAGCCTTGTTCCTTGCTGGAGCGCCCAAGGGCCCTCTCCTTGAGAAG
ATCCGCCCACACATCTTCTTTGATGACCAGATGTTCCATGTGGCTGGGGCTCAGGAGATG
GGCACTGTGGCCGCCCATGTGCCTTATGGTGTGGCACAGACACCCCGGCGGACTGCACCT
GCAAAGCAGGCCCCATCTGCACAGTAG

Enzyme 2 GenBank Gene ID

AF331801

Enzyme 2 GeneCard ID

NT5C1A

Enzyme 2 GenAtlas ID

NT5C1A

Enzyme 2 HGNC ID

HGNC:17819 Link Image

Enzyme 2 Chromosome Location

Enzyme 2 Locus

1p34.3-p33

Enzyme 2 SNPs

SNPJam Report Link Image

Enzyme 2 General References

Hunsucker SA, Spychala J, Mitchell BS: Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside analog resistance. J Biol Chem. 2001 Mar 30;276(13):10498-504. Epub 2000 Dec 22. [PubMed ]
Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 2 Metabolite References

Not Available

Enzyme 3 [top]

Enzyme 3 ID

5234

Enzyme 3 Name

5'(3')-deoxyribonucleotidase, cytosolic type

Enzyme 3 Synonyms

Cytosolic 5',3'-pyrimidine nucleotidase
Deoxy-5'-nucleotidase 1
dNT-1

Enzyme 3 Gene Name

NT5C

Enzyme 3 Protein Sequence

>5'(3')-deoxyribonucleotidase, cytosolic type

MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADK
VASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHL
GPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRL
LSWSDNWREILDSKRGAAQRE

Enzyme 3 Number of Residues

201

Enzyme 3 Molecular Weight

23382.5

Enzyme 3 Theoretical pI

6.63

Enzyme 3 GO Classification

Function
catalytic activity hydrolase activity hydrolase activity, acting on ester bonds phosphatase activity phosphoric ester hydrolase activity
Process
—
Component
—

Enzyme 3 General Function

Involved in metal ion binding

Enzyme 3 Specific Function

Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP

Enzyme 3 Pathways

Not Available

Enzyme 3 Reactions

Not Available

Enzyme 3 Pfam Domain Function

NT5C (PF06941 )

Enzyme 3 Signals

None

Enzyme 3 Transmembrane Regions

None

Enzyme 3 Essentiality

Not Available

Enzyme 3 GenBank ID Protein

7524492

Enzyme 3 UniProtKB/Swiss-Prot ID

Q8TCD5

Enzyme 3 UniProtKB/Swiss-Prot Entry Name

NT5C_HUMAN Link Image

Enzyme 3 PDB ID

Not Available

Enzyme 3 Cellular Location

Not Available

Enzyme 3 Gene Sequence

>606 bp

ATGGCGCGGAGCGTGCGCGTGCTGGTGGACATGGACGGCGTCCTGGCCGACTTCGAGGCC
GGCCTCCTGCGGGGCTTCCGCCGCCGCTTCCCTGAGGAGCCGCACGTGCCGCTGGAGCAA
CGCCGCGGCTTCCTGGCCCGCGAGCAGTACCGCGCCCTGCGGCCCGACCTGGCGGATAAA
GTGGCCAGTGTGTACGAAGCCCCGGGCTTTTTCCTGGACCTGGAGCCCATCCCGGGAGCC
TTGGACGCTGTGCGGGAGATGAACGACCTACCGGACACGCAGGTCTTCATCTGCACCAGC
CCCCTGCTGAAGTACCACCACTGTGTGGGTGAGAAGTACCGCTGGGTGGAGCAGCACCTG
GGGCCCCAGTTCGTAGAACGAATTATCCTGACAAGGGACAAGACGGTGGTCTTGGGGGAC
CTGCTCATTGATGACAAGGACACAGTTCGAGGCCAGGAGGAGACCCCAAGCTGGGAGCAC
ATCTTGTTCACCTGCTGCCACAATCGGCACCTGGTCCTGCCCCCGACAAGGAGACGGCTG
CTCTCCTGGAGTGACAACTGGAGGGAGATCTTAGATAGCAAGCGCGGAGCTGCGCAGCGG
GAATGA

Enzyme 3 GenBank Gene ID

AF154829

Enzyme 3 GeneCard ID

NT5C

Enzyme 3 GenAtlas ID

Not Available

Enzyme 3 HGNC ID

Not Available

Enzyme 3 Chromosome Location

Enzyme 3 Locus

17q25.1

Enzyme 3 SNPs

SNPJam Report Link Image

Enzyme 3 General References

Rampazzo C, Johansson M, Gallinaro L, Ferraro P, Hellman U, Karlsson A, Reichard P, Bianchi V: Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression of the enzyme in Escherichia coli and mammalian cells. J Biol Chem. 2000 Feb 25;275(8):5409-15. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Rampazzo C, Kost-Alimova M, Ruzzenente B, Dumanski JP, Bianchi V: Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of the mitochondrial enzyme, gene structures, chromosomal mapping and comparison with the human orthologs. Gene. 2002 Jul 10;294(1-2):109-17. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
Wallden K, Rinaldo-Matthis A, Ruzzenente B, Rampazzo C, Bianchi V, Nordlund P: Crystal structures of human and murine deoxyribonucleotidases: insights into recognition of substrates and nucleotide analogues. Biochemistry. 2007 Dec 4;46(48):13809-18. Epub 2007 Nov 7. [PubMed ]

Enzyme 3 Metabolite References

Not Available

Enzyme 4 [top]

Enzyme 4 ID

5235

Enzyme 4 Name

Deoxycytidine kinase

Enzyme 4 Synonyms

Enzyme 4 Gene Name

DCK

Enzyme 4 Protein Sequence

>Deoxycytidine kinase

MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCN
VQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAE
KPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQA
TPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNE
DFKDKYESLVEKVKEFLSTL

Enzyme 4 Number of Residues

260

Enzyme 4 Molecular Weight

30518.3

Enzyme 4 Theoretical pI

4.88

Enzyme 4 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity nucleoside binding phosphotransferase activity, alcohol group as acceptor purine nucleoside binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
Component
—

Enzyme 4 General Function

Involved in ATP binding

Enzyme 4 Specific Function

Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents

Enzyme 4 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 4 Reactions

NTP + deoxycytidine = NDP + dCMP [RN:R02321]

Enzyme 4 Pfam Domain Function

dNK (PF01712 )

Enzyme 4 Signals

None

Enzyme 4 Transmembrane Regions

None

Enzyme 4 Essentiality

Not Available

Enzyme 4 GenBank ID Protein

Not Available

Enzyme 4 UniProtKB/Swiss-Prot ID

P27707

Enzyme 4 UniProtKB/Swiss-Prot Entry Name

DCK_HUMAN

Enzyme 4 PDB ID

1P62

Enzyme 4 PDB File

Show

Enzyme 4 3D Structure

Enzyme 4 Cellular Location

Not Available

Enzyme 4 Gene Sequence

>783 bp

ATGGCCACCCCGCCCAAGAGAAGCTGCCCGTCTTTCTCAGCCAGCTCTGAGGGGACCCGC
ATCAAGAAAATCTCCATCGAAGGGAACATCGCTGCAGGGAAGTCAACATTTGTGAATATC
CTTAAACAATTGTGTGAAGATTGGGAAGTGGTTCCTGAACCTGTTGCCAGATGGTGCAAT
GTTCAAAGTACTCAAGATGAATTTGAGGAACTTACAATGTCTCAGAAAAATGGTGGGAAT
GTTCTTCAGATGATGTATGAGAAACCTGAACGATGGTCTTTTACCTTCCAAACATATGCC
TGTCTCAGTCGAATAAGAGCTCAGCTTGCCTCTCTGAATGGCAAGCTCAAAGATGCAGAG
AAACCTGTATTATTTTTTGAACGATCTGTGTATAGTGACAGGTATATTTTTGCATCTAAT
TTGTATGAATCTGAATGCATGAATGAGACAGAGTGGACAATTTATCAAGACTGGCATGAC
TGGATGAATAACCAATTTGGCCAAAGCCTTGAATTGGATGGAATCATTTATCTTCAAGCC
ACTCCAGAGACATGCTTACATAGAATATATTTACGGGGAAGAAATGAAGAGCAAGGCATT
CCTCTTGAATATTTAGAGAAGCTTCATTATAAACATGAAAGCTGGCTCCTGCATAGGACA
CTGAAAACCAACTTCGATTATCTTCAAGAGGTGCCTATCTTAACACTGGATGTTAATGAA
GACTTTAAAGACAAATATGAAAGTCTGGTTGAAAAGGTCAAAGAGTTTTTGAGTACTTTG
TGA

Enzyme 4 GenBank Gene ID

Enzyme 4 GeneCard ID

Enzyme 4 GenAtlas ID

Enzyme 4 HGNC ID

Enzyme 4 Chromosome Location

Enzyme 4 Locus

4q13.3-q21.1

Enzyme 4 SNPs

SNPJam Report Link Image

Enzyme 4 General References

Chottiner EG, Shewach DS, Datta NS, Ashcraft E, Gribbin D, Ginsburg D, Fox IH, Mitchell BS: Cloning and expression of human deoxycytidine kinase cDNA. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1531-5. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Eriksson S, Cederlund E, Bergman T, Jornvall H, Bohman C: Characterization of human deoxycytidine kinase. Correlation with cDNA sequences. FEBS Lett. 1991 Mar 25;280(2):363-6. [PubMed ]
Johansson M, Brismar S, Karlsson A: Human deoxycytidine kinase is located in the cell nucleus. Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11941-5. [PubMed ]
Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
Sabini E, Ort S, Monnerjahn C, Konrad M, Lavie A: Structure of human dCK suggests strategies to improve anticancer and antiviral therapy. Nat Struct Biol. 2003 Jul;10(7):513-9. [PubMed ]

Enzyme 4 Metabolite References

Not Available

Enzyme 5 [top]

Enzyme 5 ID

5236

Enzyme 5 Name

5'(3')-deoxyribonucleotidase, mitochondrial

Enzyme 5 Synonyms

5',3'-nucleotidase, mitochondrial
Deoxy-5'-nucleotidase 2
dNT-2

Enzyme 5 Gene Name

NT5M

Enzyme 5 Protein Sequence

>5'(3')-deoxyribonucleotidase, mitochondrial

MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC

Enzyme 5 Number of Residues

228

Enzyme 5 Molecular Weight

25861.5

Enzyme 5 Theoretical pI

8.12

Enzyme 5 GO Classification

Function
catalytic activity hydrolase activity hydrolase activity, acting on ester bonds phosphatase activity phosphoric ester hydrolase activity
Process
—
Component
—

Enzyme 5 General Function

Involved in phosphatase activity

Enzyme 5 Specific Function

Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP

Enzyme 5 Pathways

Not Available

Enzyme 5 Reactions

Not Available

Enzyme 5 Pfam Domain Function

NT5C (PF06941 )

Enzyme 5 Signals

None

Enzyme 5 Transmembrane Regions

None

Enzyme 5 Essentiality

Not Available

Enzyme 5 GenBank ID Protein

Not Available

Enzyme 5 UniProtKB/Swiss-Prot ID

Q9NPB1

Enzyme 5 UniProtKB/Swiss-Prot Entry Name

NT5M_HUMAN Link Image

Enzyme 5 PDB ID

1Q92

Enzyme 5 PDB File

Show

Enzyme 5 3D Structure

Enzyme 5 Cellular Location

Not Available

Enzyme 5 Gene Sequence

>687 bp

ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA

Enzyme 5 GenBank Gene ID

AF210652

Enzyme 5 GeneCard ID

NT5M

Enzyme 5 GenAtlas ID

NT5M

Enzyme 5 HGNC ID

HGNC:15769 Link Image

Enzyme 5 Chromosome Location

Enzyme 5 Locus

17p11.2

Enzyme 5 SNPs

SNPJam Report Link Image

Enzyme 5 General References

Rampazzo C, Gallinaro L, Milanesi E, Frigimelica E, Reichard P, Bianchi V: A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8239-44. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P: Crystal structure of a human mitochondrial deoxyribonucleotidase. Nat Struct Biol. 2002 Oct;9(10):779-87. [PubMed ]

Enzyme 5 Metabolite References

Not Available

Enzyme 6 [top]

Enzyme 6 ID

5237

Enzyme 6 Name

Cytosolic purine 5'-nucleotidase

Enzyme 6 Synonyms

Cytosolic 5'-nucleotidase II

Enzyme 6 Gene Name

NT5C2

Enzyme 6 Protein Sequence

>Cytosolic purine 5'-nucleotidase

MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
PQEITHCHDEDDDEEEEEEEE

Enzyme 6 Number of Residues

561

Enzyme 6 Molecular Weight

64969.2

Enzyme 6 Theoretical pI

6.05

Enzyme 6 GO Classification

Not Available

Enzyme 6 General Function

Involved in 5'-nucleotidase activity

Enzyme 6 Specific Function

May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides

Enzyme 6 Pathways

Nicotinate and Nicotinamide Metabolism (map00760 )
Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 6 Reactions

a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]

Enzyme 6 Pfam Domain Function

5_nucleotid (PF05761 )

Enzyme 6 Signals

None

Enzyme 6 Transmembrane Regions

None

Enzyme 6 Essentiality

Not Available

Enzyme 6 GenBank ID Protein

Not Available

Enzyme 6 UniProtKB/Swiss-Prot ID

P49902

Enzyme 6 UniProtKB/Swiss-Prot Entry Name

5NTC_HUMAN Link Image

Enzyme 6 PDB ID

Not Available

Enzyme 6 Cellular Location

Not Available

Enzyme 6 Gene Sequence

>1686 bp

ATGTCGACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
CCCCAGGAAATTACACACTGCCATGACGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA

Enzyme 6 GenBank Gene ID

Enzyme 6 GeneCard ID

Enzyme 6 GenAtlas ID

Enzyme 6 HGNC ID

Enzyme 6 Chromosome Location

Enzyme 6 Locus

10q24.32

Enzyme 6 SNPs

SNPJam Report Link Image

Enzyme 6 General References

Oka J, Matsumoto A, Hosokawa Y, Inoue S: Molecular cloning of human cytosolic purine 5'-nucleotidase. Biochem Biophys Res Commun. 1994 Nov 30;205(1):917-22. [PubMed ]
Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Wallden K, Stenmark P, Nyman T, Flodin S, Graslund S, Loppnau P, Bianchi V, Nordlund P: Crystal structure of human cytosolic 5'-nucleotidase II: insights into allosteric regulation and substrate recognition. J Biol Chem. 2007 Jun 15;282(24):17828-36. Epub 2007 Apr 3. [PubMed ]

Enzyme 6 Metabolite References

Not Available

Enzyme 7 [top]

Enzyme 7 ID

5271

Enzyme 7 Name

Acetyl-coenzyme A synthetase 2-like, mitochondrial

Enzyme 7 Synonyms

Acetate--CoA ligase 2
Acetyl-CoA synthetase 2
AceCS2
Acyl-CoA synthetase short-chain family member 1

Enzyme 7 Gene Name

ACSS1

Enzyme 7 Protein Sequence

>Acetyl-coenzyme A synthetase 2-like, mitochondrial

MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPA
LSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVR
KSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVA
AMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVK
HCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM
PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF
ESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPI
NCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVL
MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG
GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD
SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG
DTTTLEDPSIIAEILSVYQKCKDKQAAAK

Enzyme 7 Number of Residues

689

Enzyme 7 Molecular Weight

74856.1

Enzyme 7 Theoretical pI

7.11

Enzyme 7 GO Classification

Function
AMP binding CoA-ligase activity acetate-CoA ligase activity adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity ligase activity ligase activity, forming carbon-sulfur bonds nucleoside binding purine nucleoside binding
Process
metabolic process
Component
—

Enzyme 7 General Function

Involved in acetate-CoA ligase activity

Enzyme 7 Specific Function

Important for maintaining normal body temperature during fasting and for energy homeostasis. Essential for energy expenditure under ketogenic conditions. Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2)

Enzyme 7 Pathways

Gluconeogenesis (map00010 )
Propanoate Metabolism (map00640 )
Pyruvate Metabolism (map00620 )

Enzyme 7 Reactions

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA [RN:R00235]

Enzyme 7 Pfam Domain Function

AMP-binding (PF00501 )

Enzyme 7 Signals

None

Enzyme 7 Transmembrane Regions

None

Enzyme 7 Essentiality

Not Available

Enzyme 7 GenBank ID Protein

24659677

Enzyme 7 UniProtKB/Swiss-Prot ID

Q9NUB1

Enzyme 7 UniProtKB/Swiss-Prot Entry Name

ACS2L_HUMAN Link Image

Enzyme 7 PDB ID

Not Available

Enzyme 7 Cellular Location

Not Available

Enzyme 7 Gene Sequence

>2070 bp

ATGGCGGCGCGCACCCTGGGCCGCGGCGTCGGGAGGCTGCTGGGCAGCCTGCGAGGGCTC
TCGGGGCAGCCCGCGCGGCCGCCGTGCGGGGTGAGCGCGCCGCGCAGGGCGGCCTCGGGA
CCCTCGGGCAGCGCTCCCGCAGTTGCAGCAGCAGCAGCACAGCCAGGCTCGTATCCCGCG
CTGAGTGCACAGGCAGCCCGGGAGCCGGCCGCCTTCTGGGGGCCTCTGGCGCGGGACACT
CTCGTGTGGGACACCCCCTACCACACCGTCTGGGACTGCGACTTCAGCACTGGCAAGATC
GGCTGGTTCCTGGGAGGCCAGTTAAATGTCTCTGTCAACTGCTTGGACCAGCATGTTCGG
AAGTCCCCCGAGAGCGTTGCTTTGATCTGGGAGCGCGATGAGCCTGGAACGGAAGTGAGG
ATCACCTACAGGGAACTACTGGAGACCACGTGCCGCCTGGCCAACACGCTGAAGAGGCAT
GGAGTCCACCGTGGGGACCGTGTTGCCATCTACATGCCCGTGTCCCCATTGGCTGTGGCA
GCAATGCTGGCCTGTGCCAGGATCGGAGCTGTCCACACAGTCATCTTTGCTGGCTTCAGT
GCGGAGTCCTTGGCTGGGAGGATCAATGATGCCAAGTGCAAGGTGGTTATCACCTTCAAC
CAAGGACTCCGGGGTGGGCGCGTGGTGGAGCTGAAGAAAATAGTGGATGAGGCTGTGAAG
CACTGCCCCACCGTGCAGCATGTCCTGGTGGCTCACAGGACAGACAACAAGGTCCACATG
GGGGATCTGGACGTCCCGCTGGAGCAGGAAATGGCCAAGGAGGACCCTGTTTGCGCCCCA
GAGAGCATGGGCAGTGAGGACATGCTCTTCATGCTGTACACCTCAGGGAGCACCGGAATG
CCCAAGGGCATCGTCCATACCCAGGCAGGCTACCTGCTCTATGCCGCCCTGACTCACAAG
CTTGTGTTTGACCACCAGCCAGGTGACATCTTTGGCTGTGTGGCCGACATCGGTTGGATT
ACAGGACACAGCTACGTGGTGTATGGGCCTCTCTGCAATGGTGCCACCAGCGTCCTTTTT
GAGAGCACCCCAGTTTATCCCAATGCTGGTCGGTACTGGGAGACAGTAGAGAGGTTGAAG
ATCAATCAGTTCTATGGCGCCCCAACGGCTGTCCGGCTGTTGCTGAAATACGGTGATGCC
TGGGTGAAGAAGTATGATCGCTCCTCCCTGCGGACCCTGGGGTCAGTGGGAGAGCCCATC
AACTGTGAGGCCTGGGAGTGGCTTCACAGGGTGGTGGGGGACAGCAGGTGCACGCTGGTG
GACACCTGGTGGCAGACAGAAACAGGTGGCATCTGCATCGCACCACGGCCCTCGGAAGAA
GGGGCGGAAATCCTCCCTGCCATGGCGATGAGGCCCTTCTTTGGCATCGTCCCCGTCCTC
ATGGATGAGAAGGGCAGCGTCATGGAGGGCAGCAACGTCTCCGGGGCCCTGTGCATCTCC
CAGGCCTGGCCGGGCATGGCCAGGACCATCTATGGCGACCACCAGCGATTTGTGGACGCC
TACTTCAAGGCCTACCCAGGCTATTACTTCACTGGAGACGGGGCTTACCGAACTGAGGGC
GGCTATTACCAGATCACAGGGCGGATGGATGATGTCATCAACATCAGTGGCCACCGGCTG
GGGACCGCAGAGATTGAGGACGCCATCGCCGACCACCCTGCAGTACCAGAAAGTGCTGTC
ATTGGCTACCCCCACGACATCAAAGGAGAAGCTGCCTTTGCCTTCATTGTGGTGAAAGAT
AGTGCGGGTGACTCAGATGTGGTGGTGCAGGAGCTCAAGTCCATGGTGGCCACCAAGATC
GCCAAATATGCTGTGCCTGATGAGATCCTGGTGGTGAAACGTCTTCCAAAAACCAGGTCT
GGGAAGGTCATGCGGCGGCTCCTGAGGAAGATCATCACTAGTGAGGCCCAGGAGCTGGGA
GACACTACCACCTTGGAGGACCCCAGCATCATCGCAGAGATCCTGAGTGTCTACCAGAAG
TGCAAGGACAAGCAGGCTGCTGCTAAGTGA

Enzyme 7 GenBank Gene ID

BC039261

Enzyme 7 GeneCard ID

ACSS1

Enzyme 7 GenAtlas ID

ACSS1

Enzyme 7 HGNC ID

HGNC:16091 Link Image

Enzyme 7 Chromosome Location

Enzyme 7 Locus

20p11.23-p11.21

Enzyme 7 SNPs

SNPJam Report Link Image

Enzyme 7 General References

Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed ]
Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed ]
Schwer B, Bunkenborg J, Verdin RO, Andersen JS, Verdin E: Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10224-9. Epub 2006 Jun 20. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Jin L, Wei W, Jiang Y, Peng H, Cai J, Mao C, Dai H, Choy W, Bemis JE, Jirousek MR, Milne JC, Westphal CH, Perni RB: Crystal structures of human SIRT3 displaying substrate-induced conformational changes. J Biol Chem. 2009 Sep 4;284(36):24394-405. Epub 2009 Jun 16. [PubMed ]

Enzyme 7 Metabolite References

Not Available

Enzyme 8 [top]

Enzyme 8 ID

5313

Enzyme 8 Name

Ectonucleoside triphosphate diphosphohydrolase 1

Enzyme 8 Synonyms

NTPDase 1
Ecto-ATP diphosphohydrolase 1
Ecto-ATPDase 1
Ecto-ATPase 1
Ecto-apyrase
Lymphoid cell activation antigen
CD39 antigen

Enzyme 8 Gene Name

ENTPD1

Enzyme 8 Protein Sequence

>Ectonucleoside triphosphate diphosphohydrolase 1

MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV

Enzyme 8 Number of Residues

510

Enzyme 8 Molecular Weight

57964.1

Enzyme 8 Theoretical pI

6.29

Enzyme 8 GO Classification

Function
catalytic activity hydrolase activity
Process
—
Component
—

Enzyme 8 General Function

Involved in hydrolase activity

Enzyme 8 Specific Function

In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well

Enzyme 8 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 8 Reactions

ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]

Enzyme 8 Pfam Domain Function

GDA1_CD39 (PF01150 )

Enzyme 8 Signals

None

Enzyme 8 Transmembrane Regions

17-37 479-499

Enzyme 8 Essentiality

Not Available

Enzyme 8 GenBank ID Protein

45580700

Enzyme 8 UniProtKB/Swiss-Prot ID

P49961

Enzyme 8 UniProtKB/Swiss-Prot Entry Name

ENTP1_HUMAN Link Image

Enzyme 8 PDB ID

Not Available

Enzyme 8 Cellular Location

Not Available

Enzyme 8 Gene Sequence

>1533 bp

ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG

Enzyme 8 GenBank Gene ID

NM_001776.5 Link Image

Enzyme 8 GeneCard ID

ENTPD1

Enzyme 8 GenAtlas ID

ENTPD1

Enzyme 8 HGNC ID

HGNC:3363

Enzyme 8 Chromosome Location

Enzyme 8 Locus

10q24

Enzyme 8 SNPs

SNPJam Report Link Image

Enzyme 8 General References

Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed ]
Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed ]
Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed ]
Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed ]
Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed ]
Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed ]
Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed ]
Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed ]
Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]

Enzyme 8 Metabolite References

Not Available

Enzyme 9 [top]

Enzyme 9 ID

5314

Enzyme 9 Name

Soluble calcium-activated nucleotidase 1

Enzyme 9 Synonyms

SCAN-1
Apyrase homolog
Putative MAPK-activating protein PM09
Putative NF-kappa-B-activating protein 107

Enzyme 9 Gene Name

CANT1

Enzyme 9 Protein Sequence

>Soluble calcium-activated nucleotidase 1

MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI

Enzyme 9 Number of Residues

401

Enzyme 9 Molecular Weight

44839.2

Enzyme 9 Theoretical pI

5.98

Enzyme 9 GO Classification

Function
binding calcium ion binding catalytic activity cation binding hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion binding metal ion binding pyrophosphatase activity
Process
—
Component
—

Enzyme 9 General Function

Involved in calcium ion binding

Enzyme 9 Specific Function

Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP

Enzyme 9 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 9 Reactions

a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]

Enzyme 9 Pfam Domain Function

Apyrase (PF06079 )

Enzyme 9 Signals

None

Enzyme 9 Transmembrane Regions

45-62

Enzyme 9 Essentiality

Not Available

Enzyme 9 GenBank ID Protein

229577440

Enzyme 9 UniProtKB/Swiss-Prot ID

Q8WVQ1

Enzyme 9 UniProtKB/Swiss-Prot Entry Name

CANT1_HUMAN Link Image

Enzyme 9 PDB ID

1S1D

Enzyme 9 PDB File

Show

Enzyme 9 3D Structure

Enzyme 9 Cellular Location

Not Available

Enzyme 9 Gene Sequence

>1206 bp

ATGCCCGTGCAGCTGTCTGAGCACCCGGAATGGAATGAGTCTATGCACTCCCTCCGGATC
AGTGTGGGGGGCCTTCCTGTGCTGGCGTCCATGACCAAGGCCGCGGACCCCCGCTTCCGC
CCCCGCTGGAAGGTGATCCTGACGTTCTTTGTGGGTGCTGCCATCCTCTGGCTGCTCTGC
TCCCACCGCCCGGCCCCCGGCAGGCCCCCCACCCACAATGCACACAACTGGAGGCTCGGC
CAGGCGCCCGCCAACTGGTACAATGACACCTACCCCCTGTCTCCCCCACAAAGGACACCG
GCTGGGATTCGGTATCGAATCGCAGTTATCGCAGACCTGGACACAGAGTCAAGGGCCCAA
GAGGAAAACACCTGGTTCAGTTACCTGAAAAAGGGCTACCTGACCCTGTCAGACAGTGGG
GACAAGGTGGCCGTGGAATGGGACAAAGACCATGGGGTCCTGGAGTCCCACCTGGCGGAG
AAGGGGAGAGGCATGGAGCTATCCGACCTGATTGTTTTCAATGGGAAACTCTACTCCGTG
GATGACCGGACGGGGGTCGTCTACCAGATCGAAGGCAGCAAAGCCGTGCCCTGGGTGATT
CTGTCCGACGGCGACGGCACCGTGGAGAAAGGCTTCAAGGCCGAATGGCTGGCAGTGAAG
GACGAGCGTCTGTACGTGGGCGGCCTGGGCAAGGAGTGGACGACCACTACGGGTGATGTG
GTGAACGAGAACCCGGAGTGGGTGAAGGTGGTGGGCTACAAGGGCAGCGTGGACCACGAG
AACTGGGTGTCCAACTACAACGCCCTGCGGGCTGCTGCCGGCATCCAGCCGCCAGGCTAC
CTCATCCATGAGTCTGCCTGCTGGAGTGACACGCTGCAGCGCTGGTTCTTCCTGCCGCGC
CGCGCCAGCCAGGAGCGCTACAGCGAGAAGGACGACGAGCGCAAGGGCGCCAACCTGCTG
CTGAGCGCCTCCCCTGACTTCGGCGACATCGCTGTGAGCCACGTCGGGGCGGTGGTCCCC
ACTCACGGCTTCTCGTCCTTCAAGTTCATCCCCAACACCGACGACCAGATCATTGTGGCC
CTCAAATCCGAGGAGGACAGCGGCAGAGTCGCCTCCTACATCATGGCCTTCACGCTGGAC
GGGCGCTTCCTGTTGCCGGAGACCAAGATCGGAAGCGTGAAATACGAAGGCATCGAGTTC
ATTTAA

Enzyme 9 GenBank Gene ID

NM_001159772.1 Link Image

Enzyme 9 GeneCard ID

CANT1

Enzyme 9 GenAtlas ID

CANT1

Enzyme 9 HGNC ID

HGNC:19721 Link Image

Enzyme 9 Chromosome Location

Enzyme 9 Locus

17q25.3

Enzyme 9 SNPs

SNPJam Report Link Image

Enzyme 9 General References

Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed ]
Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed ]
Yang M, Kirley TL: Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change. Biochemistry. 2004 Jul 20;43(28):9185-94. [PubMed ]
Dai J, Liu J, Deng Y, Smith TM, Lu M: Structure and protein design of a human platelet function inhibitor. Cell. 2004 Mar 5;116(5):649-59. [PubMed ]
Huber C, Oules B, Bertoli M, Chami M, Fradin M, Alanay Y, Al-Gazali LI, Ausems MG, Bitoun P, Cavalcanti DP, Krebs A, Le Merrer M, Mortier G, Shafeghati Y, Superti-Furga A, Robertson SP, Le Goff C, Muda AO, Paterlini-Brechot P, Munnich A, Cormier-Daire V: Identification of CANT1 mutations in Desbuquois dysplasia. Am J Hum Genet. 2009 Nov;85(5):706-10. Epub 2009 Oct 22. [PubMed ]

Enzyme 9 Metabolite References

Not Available

Enzyme 10 [top]

Enzyme 10 ID

5318

Enzyme 10 Name

Ectonucleoside triphosphate diphosphohydrolase 3

Enzyme 10 Synonyms

NTPDase 3
CD39 antigen-like 3
Ecto-ATP diphosphohydrolase 3
Ecto-ATPDase 3
Ecto-ATPase 3
Ecto-apyrase 3
HB6

Enzyme 10 Gene Name

ENTPD3

Enzyme 10 Protein Sequence

>Ectonucleoside triphosphate diphosphohydrolase 3

MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD

Enzyme 10 Number of Residues

529

Enzyme 10 Molecular Weight

59104.8

Enzyme 10 Theoretical pI

6.40

Enzyme 10 GO Classification

Function
catalytic activity hydrolase activity
Process
—
Component
—

Enzyme 10 General Function

Involved in hydrolase activity

Enzyme 10 Specific Function

Has a threefold preference for the hydrolysis of ATP over ADP

Enzyme 10 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 10 Reactions

ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]

Enzyme 10 Pfam Domain Function

GDA1_CD39 (PF01150 )

Enzyme 10 Signals

None

Enzyme 10 Transmembrane Regions

23-43 486-506

Enzyme 10 Essentiality

Not Available

Enzyme 10 GenBank ID Protein

13817037

Enzyme 10 UniProtKB/Swiss-Prot ID

O75355

Enzyme 10 UniProtKB/Swiss-Prot Entry Name

ENTP3_HUMAN Link Image

Enzyme 10 PDB ID

Not Available

Enzyme 10 Cellular Location

Not Available

Enzyme 10 Gene Sequence

>1590 bp

ATGTTCACTGTGCTGACCCGCCAACCATGTGAGCAAGCAGGCCTCAAGGCCCTCTACCGA
ACTCCAACCATCATTGCCTTGGTGGTCTTGCTTGTGAGTATTGTGGTACTTGTGAGTATC
ACTGTCATCCAGATCCACAAGCAAGAGGTCCTCCCTCCAGGACTGAAGTATGGTATTGTG
CTGGATGCCGGGTCTTCAAGAACCACAGTCTACGTGTATCAATGGCCAGCAGAAAAAGAG
AATAATACCGGAGTGGTCAGTCAAACCTTCAAATGTAGTGTGAAAGGCTCTGGAATCTCC
AGCTATGGAAATAACCCCCAAGATGTCCCCAGAGCCTTTGAGGAGTGTATGCAAAAAGTC
AAGGGGCAGGTTCCATCCCACCTCCACGGATCCACCCCCATTCACCTGGGAGCCACGGCT
GGGATGCGCTTGCTGAGGTTGCAAAATGAAACAGCAGCTAATGAAGTCCTTGAAAGCATC
CAAAGCTACTTCAAGTCCCAGCCCTTTGACTTTAGGGGTGCTCAAATCATTTCTGGGCAA
GAAGAAGGGGTATATGGATGGATTACAGCCAACTATTTAATGGGAAATTTCCTGGAGAAG
AACCTGTGGCACATGTGGGTGCACCCGCATGGAGTGGAAACCACGGGTGCCCTGGACTTA
GGTGGTGCCTCCACCCAAATATCCTTCGTGGCAGGAGAGAAGATGGATCTGAACACCAGC
GACATCATGCAGGTGTCCCTGTATGGCTACGTATACACGCTCTACACACACAGCTTCCAG
TGCTATGGCCGGAATGAGGCTGAGAAGAAGTTTCTGGCAATGCTCCTGCAGAATTCTCCT
ACCAAAAACCATCTCACCAATCCCTGTTACCCTCGGGATTATAGCATCAGCTTCACCATG
GGCCATGTATTTGATAGCCTGTGCACTGTGGACCAGAGGCCAGAAAGTTATAACCCCAAT
GATGTCATCACTTTTGAAGGAACTGGGGACCCATCTCTGTGTAAGGAGAAGGTGGCTTCC
ATATTTGACTTCAAAGCTTGCCATGATCAAGAAACCTGTTCTTTTGATGGGGTTTATCAG
CCAAAGATTAAAGGGCCATTTGTGGCTTTTGCAGGATTCTACTACACAGCCAGTGCTTTA
AATCTTTCAGGTAGCTTTTCCCTGGACACCTTCAACTCCAGCACCTGGAATTTCTGCTCA
CAGAATTGGAGTCAGCTCCCACTGCTGCTCCCCAAATTTGATGAGGTATATGCCCGCTCT
TACTGCTTCTCAGCCAACTACATCTACCACTTGTTTGTGAACGGTTACAAATTCACAGAG
GAGACTTGGCCCCAAATACACTTTGAAAAAGAAGTGGGGAATAGCAGCATAGCCTGGTCT
CTTGGCTACATGCTCAGCCTGACCAACCAGATCCCAGCTGAAAGCCCTCTGATCCGTCTG
CCCATAGAACCACCTGTCTTTGTGGGCACCCTCGCTTTCTTCACAGCGGCAGCCTTGCTG
TGTCTGGCATTTCTTGCATACCTGTGTTCAGCAACCAGAAGAAAGAGGCACTCCGAGCAT
GCCTTTGACCATGCAGTGGATTCTGACTGA

Enzyme 10 GenBank Gene ID

AF034840

Enzyme 10 GeneCard ID

ENTPD3

Enzyme 10 GenAtlas ID

ENTPD3

Enzyme 10 HGNC ID

HGNC:3365

Enzyme 10 Chromosome Location

Enzyme 10 Locus

3p21.3

Enzyme 10 SNPs

SNPJam Report Link Image

Enzyme 10 General References

Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed ]
Smith TM, Kirley TL: Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1. Biochim Biophys Acta. 1998 Jul 28;1386(1):65-78. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Smith TM, Lewis Carl SA, Kirley TL: Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase. Biochemistry. 1999 May 4;38(18):5849-57. [PubMed ]
Yang F, Hicks-Berger CA, Smith TM, Kirley TL: Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry. 2001 Apr 3;40(13):3943-50. [PubMed ]

Enzyme 10 Metabolite References

Not Available

Enzyme 11 [top]

Enzyme 11 ID

5321

Enzyme 11 Name

Serum paraoxonase/lactonase 3

Enzyme 11 Synonyms

Not Available

Enzyme 11 Gene Name

PON3

Enzyme 11 Protein Sequence

>Serum paraoxonase/lactonase 3

MGKLVALVLLGVGLSLVGEMFLAFRERVNASREVEPVEPENCHLIEELESGSEDIDILPS
GLAFISSGLKYPGMPNFAPDEPGKIFLMDLNEQNPRAQALEISGGFDKELFNPHGISIFI
DKDNTVYLYVVNHPHMKSTVEIFKFEEQQRSLVYLKTIKHELLKSVNDIVVLGPEQFYAT
RDHYFTNSLLSFFEMILDLRWTYVLFYSPREVKVVAKGFCSANGITVSADQKYVYVADVA
AKNIHIMEKHDNWDLTQLKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLNYNPEDPPG
SEVLRIQNVLSEKPRVSTVYANNGSVLQGTSVASVYHGKILIGTVFHKTLYCEL

Enzyme 11 Number of Residues

354

Enzyme 11 Molecular Weight

39607.2

Enzyme 11 Theoretical pI

5.10

Enzyme 11 GO Classification

Function
arylesterase activity carboxylesterase activity catalytic activity hydrolase activity hydrolase activity, acting on ester bonds
Process
—
Component
extracellular region

Enzyme 11 General Function

Involved in arylesterase activity

Enzyme 11 Specific Function

Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents

Enzyme 11 Pathways

Not Available

Enzyme 11 Reactions

an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol [RN:R03979]

Enzyme 11 Pfam Domain Function

Arylesterase (PF01731 )

Enzyme 11 Signals

Enzyme 11 Transmembrane Regions

None

Enzyme 11 Essentiality

Not Available

Enzyme 11 GenBank ID Protein

29788996

Enzyme 11 UniProtKB/Swiss-Prot ID

Q15166

Enzyme 11 UniProtKB/Swiss-Prot Entry Name

PON3_HUMAN Link Image

Enzyme 11 PDB ID

Not Available

Enzyme 11 Cellular Location

Not Available

Enzyme 11 Gene Sequence

>1065 bp

ATGGGGAAGCTCGTGGCGCTGGTCCTGCTGGGGGTCGGCCTGTCCTTAGTCGGGGAGATG
TTCCTGGCGTTTAGAGAAAGGGTGAATGCCTCTCGAGAAGTGGAGCCAGTAGAACCTGAA
AACTGCCACCTTATTGAGGAACTTGAAAGTGGCTCTGAAGATATTGATATACTTCCTAGT
GGGCTGGCTTTTATCTCCAGTGGATTAAAATATCCAGGCATGCCAAACTTTGCGCCAGAT
GAACCAGGAAAAATCTTCTTGATGGATCTGAATGAACAAAACCCAAGGGCACAAGCGCTA
GAAATCAGTGGTGGATTTGACAAAGAATTATTTAATCCACATGGGATCAGTATTTTCATC
GACAAAGACAATACTGTGTATCTTTATGTTGTGAATCATCCCCACATGAAGTCCACTGTG
GAGATATTTAAATTTGAGGAACAACAACGTTCTCTGGTATACCTGAAAACTATAAAACAT
GAACTTCTCAAAAGTGTGAATGACATTGTGGTTCTTGGACCAGAACAGTTCTATGCCACC
AGAGACCACTATTTTACCAACTCCCTCCTGTCATTTTTTGAGATGATCTTGGATCTTCGC
TGGACTTATGTTCTTTTCTACAGCCCAAGGGAGGTTAAAGTGGTGGCCAAAGGATTTTGT
AGTGCCAATGGGATCACAGTCTCAGCAGACCAGAAGTATGTCTATGTAGCTGATGTAGCA
GCTAAGAACATTCACATAATGGAAAAACATGATAACTGGGATTTAACTCAACTGAAGGTG
ATACAGTTGGGCACCTTAGTGGATAACCTGACTGTCGATCCTGCCACAGGAGACATTTTG
GCAGGATGCCATCCTAATCCTATGAAGCTACTGAACTATAACCCTGAGGACCCTCCAGGA
TCAGAAGTACTTCGCATCCAGAATGTTTTGTCTGAGAAGCCCAGGGTGAGCACCGTGTAT
GCCAACAATGGCTCTGTGCTTCAGGGCACCTCTGTGGCTTCTGTGTACCATGGGAAAATT
CTCATAGGCACCGTATTTCACAAAACTCTGTACTGTGAGCTCTAG

Enzyme 11 GenBank Gene ID

NM_000940.2 Link Image

Enzyme 11 GeneCard ID

PON3

Enzyme 11 GenAtlas ID

PON3

Enzyme 11 HGNC ID

HGNC:9206

Enzyme 11 Chromosome Location

Enzyme 11 Locus

7q21.3

Enzyme 11 SNPs

SNPJam Report Link Image

Enzyme 11 General References

Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Primo-Parmo SL, Sorenson RC, Teiber J, La Du BN: The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics. 1996 May 1;33(3):498-507. [PubMed ]
Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN: Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J Lipid Res. 2005 Jun;46(6):1239-47. Epub 2005 Mar 16. [PubMed ]
Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]

Enzyme 11 Metabolite References

Not Available

Enzyme 12 [top]

Enzyme 12 ID

5351

Enzyme 12 Name

Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

Enzyme 12 Synonyms

E-NPP 1
Membrane component chromosome 6 surface marker 1
Phosphodiesterase I/nucleotide pyrophosphatase 1
Plasma-cell membrane glycoprotein PC-1
Alkaline phosphodiesterase I
Nucleotide pyrophosphatase
NPPase

Enzyme 12 Gene Name

ENPP1

Enzyme 12 Protein Sequence

>Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED

Enzyme 12 Number of Residues

925

Enzyme 12 Molecular Weight

104923.6

Enzyme 12 Theoretical pI

7.14

Enzyme 12 GO Classification

Function
binding catalytic activity cation binding hydrolase activity ion binding metal ion binding molecular transducer activity nucleic acid binding pattern binding polysaccharide binding receptor activity scavenger receptor activity signal transducer activity transmembrane receptor activity
Process
immune response immune system process metabolic process
Component
—

Enzyme 12 General Function

Involved in catalytic activity

Enzyme 12 Specific Function

Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity

Enzyme 12 Pathways

Nicotinate and Nicotinamide Metabolism (map00760 )
Pantothenate and CoA Biosynthesis (map00770 )
Purine Metabolism (map00230 )
Riboflavin Metabolism (map00740 )
Starch and Sucrose Metabolism (map00500 )

Enzyme 12 Reactions

a dinucleotide + H2O = 2 mononucleotides [RN:R00056]

Enzyme 12 Pfam Domain Function

Endonuclease_NS (PF01223 )
Phosphodiest (PF01663 )
Somatomedin_B (PF01033 )

Enzyme 12 Signals

None

Enzyme 12 Transmembrane Regions

77-97

Enzyme 12 Essentiality

Not Available

Enzyme 12 GenBank ID Protein

170650661

Enzyme 12 UniProtKB/Swiss-Prot ID

P22413

Enzyme 12 UniProtKB/Swiss-Prot Entry Name

ENPP1_HUMAN Link Image

Enzyme 12 PDB ID

Not Available

Enzyme 12 Cellular Location

Not Available

Enzyme 12 Gene Sequence

>2778 bp

ATGGAGCGCGACGGCTGCGCGGGGGGCGGGAGCCGCGGCGGCGAGGGCGGGCGCGCTCCC
CGGGAGGGCCCGGCGGGGAACGGCCGCGATCGGGGCCGCAGCCACGCTGCCGAGGCGCCC
GGGGACCCGCAGGCGGCCGCGTCCTTGCTGGCCCCTATGGACGTGGGGGAGGAGCCGCTG
GAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCCAACACCTATAAAGTACTCTCGCTG
GTATTGTCAGTATGTGTGTTAACAACAATACTTGGTTGTATATTTGGGTTGAAACCAAGC
TGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGTTTCGAGAGAACATTTGGGAACTGT
CGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGCTGTTTAGATTACCAGGAGACGTGC
ATAGAACCAGAACATATATGGACTTGCAACAAATTCAGGTGTGGTGAGAAAAGGTTGACC
AGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGACAAGGGCGACTGCTGCATCAACTAC
AGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAAGAACCATGTGAGAGCATTAATGAG
CCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACCCTCTTATTTTCTTTGGATGGATTC
AGGGCAGAATATTTACACACTTGGGGTGGACTTCTTCCTGTTATTAGCAAACTAAAAAAA
TGTGGAACATATACTAAAAACATGAGACCGGTATATCCAACAAAAACTTTCCCCAATCAC
TACAGCATTGTCACCGGATTGTATCCAGAATCTCATGGCATAATCGACAATAAAATGTAT
GATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGTAAAGAGAAATTTAATCCTGAGTGG
TACAAAGGAGAACCAATTTGGGTCACAGCTAAGTATCAAGGCCTCAAGTCTGGCACATTT
TTCTGGCCAGGATCAGATGTGGAAATTAACGGAATTTTCCCAGACATCTATAAAATGTAT
AATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCTGTTCTTCAGTGGCTACAGCTTCCT
AAAGATGAAAGACCACACTTTTACACTCTGTATTTAGAAGAACCAGATTCTTCAGGTCAT
TCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCCTTGCAGAGGGTTGATGGTATGGTT
GGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTGCACAGATGCCTGAACCTCATCCTT
ATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAGAAATACATATATCTGAATAAATAT
TTGGGGGATGTTAAAAATATTAAAGTTATCTATGGACCTGCAGCTCGATTGAGACCCTCT
GATGTCCCAGATAAATACTATTCATTTAACTATGAAGGCATTGCCCGAAATCTTTCTTGC
CGGGAACCAAACCAGCACTTCAAACCTTACCTGAAACATTTCTTACCTAAGCGTTTGCAC
TTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTCTATTTGGACCCTCAGTGGCAACTT
GCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGTGGATTTCATGGCTCTGACAATGTA
TTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGACCTGGATTCAAGCATGGCATTGAG
GCTGACACCTTTGAAAACATTGAAGTCTATAACTTAATGTGTGATTTACTGAATTTGACA
CCGGCTCCTAATAACGGAACTCATGGAAGTCTTAACCACCTTCTAAAGAATCCTGTTTAT
ACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTACAGTGCCCCTTCACAAGAAACCCC
AGAGATAACCTTGGCTGCTCATGTAACCCTTCGATTTTGCCGATTGAGGATTTTCAAACA
CAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATTAAGCATGAAACTTTACCCTATGGA
AGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGTCTTCTTTCCCAGCACCAGTTTATG
AGTGGATACAGCCAAGACATCTTAATGCCCCTTTGGACATCCTATACCGTGGACAGAAAT
GACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTGTACCAGGACTTTAGAATTCCTCTT
AGTCCTGTCCATAAATGTTCATTTTATAAAAATAACACCAAAGTGAGTTACGGGTTCCTC
TCCCCACCACAACTAAATAAAAATTCAAGTGGAATATATTCTGAAGCTTTGCTTACTACA
AATATAGTGCCAATGTACCAGAGTTTTCAAGTTATATGGCGCTACTTTCATGACACCCTA
CTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAATGTCGTCAGTGGTCCTGTGTTTGAC
TTTGATTATGATGGACGTTGTGATTCCTTAGAGAATCTGAGGCAAAAAAGAAGAGTCATC
CGTAACCAAGAAATTTTGATTCCAACTCACTTCTTTATTGTGCTAACAAGCTGTAAAGAT
ACATCTCAGACGCCTTTGCACTGTGAAAACCTAGACACCTTAGCTTTCATTTTGCCTCAC
AGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAGCATGACTCCTCATGGGTTGAAGAA
TTGTTAATGTTACACAGAGCACGGATCACAGATGTTGAGCACATCACTGGACTCAGCTTC
TATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTAAAGTTGAAAACACATTTGCCAACC
TTTAGCCAAGAAGACTGA

Enzyme 12 GenBank Gene ID

NM_006208.2 Link Image

Enzyme 12 GeneCard ID

ENPP1

Enzyme 12 GenAtlas ID

ENPP1

Enzyme 12 HGNC ID

HGNC:3356

Enzyme 12 Chromosome Location

Enzyme 12 Locus

6q22-q23

Enzyme 12 SNPs

SNPJam Report Link Image

Enzyme 12 General References

Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed ]
Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed ]
Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed ]
Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed ]
Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed ]
Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed ]
Bello V, Goding JW, Greengrass V, Sali A, Dubljevic V, Lenoir C, Trugnan G, Maurice M: Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis. Mol Biol Cell. 2001 Oct;12(10):3004-15. [PubMed ]
Yano Y, Hayashi Y, Sano K, Nagano H, Nakaji M, Seo Y, Ninomiya T, Yoon S, Yokozaki H, Kasuga M: Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases. Cancer Lett. 2004 Apr 30;207(2):139-47. [PubMed ]
Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed ]
Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed ]
Rutsch F, Ruf N, Vaingankar S, Toliat MR, Suk A, Hohne W, Schauer G, Lehmann M, Roscioli T, Schnabel D, Epplen JT, Knisely A, Superti-Furga A, McGill J, Filippone M, Sinaiko AR, Vallance H, Hinrichs B, Smith W, Ferre M, Terkeltaub R, Nurnberg P: Mutations in ENPP1 are associated with 'idiopathic' infantile arterial calcification. Nat Genet. 2003 Aug;34(4):379-81. [PubMed ]
Cheng KS, Chen MR, Ruf N, Lin SP, Rutsch F: Generalized arterial calcification of infancy: different clinical courses in two affected siblings. Am J Med Genet A. 2005 Jul 15;136(2):210-3. [PubMed ]
Bacci S, Ludovico O, Prudente S, Zhang YY, Di Paola R, Mangiacotti D, Rauseo A, Nolan D, Duffy J, Fini G, Salvemini L, Amico C, Vigna C, Pellegrini F, Menzaghi C, Doria A, Trischitta V: The K121Q polymorphism of the ENPP1/PC-1 gene is associated with insulin resistance/atherogenic phenotypes, including earlier onset of type 2 diabetes and myocardial infarction. Diabetes. 2005 Oct;54(10):3021-5. [PubMed ]

Enzyme 12 Metabolite References

Not Available

Enzyme 13 [top]

Enzyme 13 ID

5426

Enzyme 13 Name

Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

Enzyme 13 Synonyms

E-NPP 3
Phosphodiesterase I beta
PD-Ibeta
Phosphodiesterase I/nucleotide pyrophosphatase 3
CD203c antigen
Alkaline phosphodiesterase I
Nucleotide pyrophosphatase
NPPase

Enzyme 13 Gene Name

ENPP3

Enzyme 13 Protein Sequence

>Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFD
ASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCL
QRKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTL
MPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLS
SKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERIS
TLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRN
LHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNS
EEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGG
GNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLN
HLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEI
TATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPT
VPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEE
FRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHY
FVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVR
DVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI

Enzyme 13 Number of Residues

875

Enzyme 13 Molecular Weight

100123.5

Enzyme 13 Theoretical pI

6.55

Enzyme 13 GO Classification

Function
binding catalytic activity cation binding hydrolase activity ion binding metal ion binding molecular transducer activity nucleic acid binding pattern binding polysaccharide binding receptor activity scavenger receptor activity signal transducer activity transmembrane receptor activity
Process
immune response immune system process metabolic process
Component
—

Enzyme 13 General Function

Involved in catalytic activity

Enzyme 13 Specific Function

Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD

Enzyme 13 Pathways

Nicotinate and Nicotinamide Metabolism (map00760 )
Pantothenate and CoA Biosynthesis (map00770 )
Purine Metabolism (map00230 )
Riboflavin Metabolism (map00740 )
Starch and Sucrose Metabolism (map00500 )

Enzyme 13 Reactions

a dinucleotide + H2O = 2 mononucleotides [RN:R00056]

Enzyme 13 Pfam Domain Function

Endonuclease_NS (PF01223 )
Phosphodiest (PF01663 )
Somatomedin_B (PF01033 )

Enzyme 13 Signals

None

Enzyme 13 Transmembrane Regions

12-30

Enzyme 13 Essentiality

Not Available

Enzyme 13 GenBank ID Protein

2465540

Enzyme 13 UniProtKB/Swiss-Prot ID

O14638

Enzyme 13 UniProtKB/Swiss-Prot Entry Name

ENPP3_HUMAN Link Image

Enzyme 13 PDB ID

Not Available

Enzyme 13 Cellular Location

Not Available

Enzyme 13 Gene Sequence

>2628 bp

ATGGAATCTACGTTGACTTTAGCAACGGAACAACCTGTTAAGAAGAACACTCTTAAGAAA
TATAAAATAGCTTGCATTGTTCTTCTTGCTTTGCTGGTGATCATGTCACTTGGATTAGGC
CTGGGGCTTGGACTCAGGAAACTGGAAAAGCAAGGCAGCTGCAGGAAGAAGTGCTTTGAT
GCATCATTTAGAGGACTGGAGAACTGCCGGTGTGATGTGGCATGTAAAGACCGAGGTGAT
TGCTGCTGGGATTTTGAAGACACCTGTGTGGAATCAACTCGAATATGGATGTGCAATAAA
TTTCGTTGTGGAGAGACCAGATTAGAGGCCAGCCTTTGCTCTTGTTCAGATGACTGTTTG
CAGAAGAAAGATTGCTGTGCTGACTATAAGAGTGTTTGCCAAGGAGAAACCTCATGGCTG
GAAGAAAACTGTGACACAGCCCAGCAGTCTCAGTGCCCAGAAGGGTTTGACCTGCCACCA
GTTATCTTGTTTTCTATGGATGGATTTAGAGCTGAATATTTATACACATGGGATACTTTA
ATGCCAAATATCAATAAACTGAAAACATGTGGAATTCATTCAAAATACATGAGAGCTATG
TATCCTACCAAAACCTTCCCAAATCATTACACCATTGTCACGGGCTTGTATCCAGAGTCA
CATGGCATCATTGACAATAATATGTATGATGTAAATCTCAACAAGAATTTTTCACTTTCT
TCAAAGGAACAAAATAATCCAGCCTGGTGGCATGGGCAACCAATGTGGCTGACAGCAATG
TATCAAGGTTTAAAAGCCGCTACCTACTTTTGGCCCGGATCAGAAGTGGCTATAAATGGC
TCCTTTCCTTCCATATACATGCCTTACAACGGAAGTGTCCCATTTGAAGAGAGGATTTCT
ACACTGTTAAAATGGCTGGACCTGCCCAAAGCTGAAAGACCCAGGTTTTATACCATGTAT
TTTGAAGAACCTGATTCCTCTGGACATGCAGGTGGACCAGTCAGTGCCAGAGTAATTAAA
GCCTTACAGGTAGTAGATCATGCTTTTGGGATGTTGATGGAAGGCCTGAAGCAGCGGAAT
TTGCACAACTGTGTCAATATCATCCTTCTGGCTGACCATGGAATGGACCAGACTTATTGT
AACAAGATGGAATACATGACTGATTATTTTCCCAGAATAAACTTCTTCTACATGTACGAA
GGGCCTGCCCCCCGCATCCGAGCTCATAATATACCTCATGACTTTTTTAGTTTTAATTCT
GAGGAAATTGTTAGAAACCTCAGTTGCCGAAAACCTGATCAGCATTTCAAGCCCTATTTG
ACTCCTGATTTGCCAAAGCGACTGCACTATGCCAAGAACGTCAGAATCGACAAAGTTCAT
CTCTTTGTGGATCAACAGTGGCTGGCTGTTAGGAGTAAATCAAATACAAATTGTGGAGGA
GGCAACCATGGTTATAACAATGAGTTTAGGAGCATGGAGGCTATCTTTCTGGCACATGGA
CCCAGTTTTAAAGAGAAGACTGAAGTTGAACCATTTGAAAATATTGAAGTCTATAACCTA
ATGTGTGATCTTCTACGCATTCAACCAGCACCAAACAATGGAACCCATGGTAGTTTAAAC
CATCTTCTGAAGGTGCCTTTTTATGAGCCATCCCATGCAGAGGAGGTGTCAAAGTTTTCT
GTTTGTGGCTTTGCTAATCCATTGCCCACAGAGTCTCTTGACTGTTTCTGCCCTCACCTA
CAAAATAGTACTCAGCTGGAACAAGTGAATCAGATGCTAAATCTCACCCAAGAAGAAATA
ACAGCAACAGTGAAAGTAAATTTGCCATTTGGGAGGCCTAGGGTACTGCAGAAGAACGTG
GACCACTGTCTCCTTTACCACAGGGAATATGTCAGTGGATTTGGAAAAGCTATGAGGATG
CCCATGTGGAGTTCATACACAGTCCCCCAGTTGGGAGACACATCGCCTCTGCCTCCCACT
GTCCCAGACTGTCTGCGGGCTGATGTCAGGGTTCCTCCTTCTGAGAGCCAAAAATGTTCC
TTCTATTTAGCAGACAAGAATATCACCCACGGCTTCCTCTATCCTCCTGCCAGCAATAGA
ACATCAGATAGCCAATATGATGCTTTAATTACTAGCAATTTGGTACCTATGTATGAAGAA
TTCAGAAAAATGTGGGACTACTTCCACAGTGTTCTTCTTATAAAACATGCCACAGAAAGA
AATGGAGTAAATGTGGTTAGTGGACCAATATTTGATTATAATTATGATGGCCATTTTGAT
GCTCCAGATGAAATTACCAAACATTTAGCCAACACTGATGTTCCCATCCCAACACACTAC
TTTGTGGTGCTGACCAGTTGTAAAAACAAGAGCCACACACCGGAAAACTGCCCTGGGTGG
CTGGATGTCCTACCCTTTATCATCCCTCACCGACCTACCAACGTGGAGAGCTGTCCTGAA
GGTAAACCAGAAGCTCTTTGGGTTGAAGAAAGATTTACAGCTCACATTGCCCGGGTCCGT
GATGTAGAACTTCTCACTGGGCTTGACTTCTATCAGGATAAAGTGCAGCCTGTCTCTGAA
ATTTTGCAACTAAAGACATATTTACCAACATTTGAAACCACTATTTAA

Enzyme 13 GenBank Gene ID

AF005632

Enzyme 13 GeneCard ID

ENPP3

Enzyme 13 GenAtlas ID

ENPP3

Enzyme 13 HGNC ID

HGNC:3358

Enzyme 13 Chromosome Location

Enzyme 13 Locus

6q22

Enzyme 13 SNPs

SNPJam Report Link Image

Enzyme 13 General References

Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed ]
Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
Buhring HJ, Seiffert M, Giesert C, Marxer A, Kanz L, Valent P, Sano K: The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3. Blood. 2001 May 15;97(10):3303-5. [PubMed ]
Yano Y, Hayashi Y, Sano K, Nagano H, Nakaji M, Seo Y, Ninomiya T, Yoon S, Yokozaki H, Kasuga M: Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases. Cancer Lett. 2004 Apr 30;207(2):139-47. [PubMed ]
Buhring HJ, Streble A, Valent P: The basophil-specific ectoenzyme E-NPP3 (CD203c) as a marker for cell activation and allergy diagnosis. Int Arch Allergy Immunol. 2004 Apr;133(4):317-29. Epub 2004 Mar 17. [PubMed ]

Enzyme 13 Metabolite References

Not Available

Enzyme 14 [top]

Enzyme 14 ID

5507

Enzyme 14 Name

Phenylalanyl-tRNA synthetase, mitochondrial

Enzyme 14 Synonyms

Phenylalanine--tRNA ligase
PheRS

Enzyme 14 Gene Name

FARS2

Enzyme 14 Protein Sequence

>Phenylalanyl-tRNA synthetase, mitochondrial

MVGSALRRGAHAYVYLVSKASHISRGHQHQAWGSRPPAAECATQRAPGSVVELLGKSYPQ
DDHSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVV
TTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRR
DQIDSQHYPIFHQLEAVRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVE
FDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVN
SAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKY
PAVINDISFWLPSENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKTHKTSHCYRITYRH
MERTLSQREVRHIHQALQEAAVQLLGVEGRF

Enzyme 14 Number of Residues

451

Enzyme 14 Molecular Weight

52356.2

Enzyme 14 Theoretical pI

7.48

Enzyme 14 GO Classification

Function
ATP binding RNA binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity cation binding ion binding ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds magnesium ion binding metal ion binding nucleic acid binding nucleoside binding nucleotide binding phenylalanine-tRNA ligase activity purine nucleoside binding tRNA binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process phenylalanyl-tRNA aminoacylation tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process tRNA processing translation
Component
cell part cytoplasm intracellular part

Enzyme 14 General Function

Involved in nucleotide binding

Enzyme 14 Specific Function

Catalyzes direct attachment of p-Tyr (Tyr) to tRNAPhe. Permits also, with a lower efficiency, the attachment of m-Tyr to tRNAPhe, thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins

Enzyme 14 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Phenylalanine and Tyrosine Metabolism (map00400 )

Enzyme 14 Reactions

ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe [RN:R03660]

Enzyme 14 Pfam Domain Function

FDX-ACB (PF03147 )
tRNA-synt_2d (PF01409 )

Enzyme 14 Signals

None

Enzyme 14 Transmembrane Regions

None

Enzyme 14 Essentiality

Not Available

Enzyme 14 GenBank ID Protein

Not Available

Enzyme 14 UniProtKB/Swiss-Prot ID

O95363

Enzyme 14 UniProtKB/Swiss-Prot Entry Name

SYFM_HUMAN Link Image

Enzyme 14 PDB ID

Not Available

Enzyme 14 Cellular Location

Not Available

Enzyme 14 Gene Sequence

>1356 bp

ATGGTGGGCTCAGCTCTCAGGAGAGGTGCCCATGCATATGTCTACCTGGTGAGTAAGGCC
AGTCACATCTCCAGAGGCCATCAGCACCAGGCCTGGGGATCGAGGCCTCCTGCAGCAGAG
TGTGCCACCCAAAGAGCTCCAGGCAGTGTGGTGGAGCTGCTGGGCAAATCCTACCCTCAG
GACGACCACAGCAACCTCACCCGGAAGGTCCTCACCAGAGTTGGCAGGAACCTGCACAAC
CAGCAGCATCACCCTCTGTGGCTGATCAAGGAGAGGGTGAAGGAGCACTTCTACAAGCAG
TATGTGGGCCGCTTTGGGACCCCGTTGTTCTCGGTCTACGACAACCTTTCTCCAGTGGTC
ACGACCTGGCAGAACTTTGACAGCCTGCTCATCCCAGCTGATCACCCCAGCAGGAAGAAG
GGGGACAACTATTACCTGAATCGGACTCACATGCTGAGAGCGCACACGTCTGCACACCAG
TGGGACTTGCTGCACGCGGGACTGGATGCCTTCCTGGTGGTGGGTGATGTCTACAGGCGT
GACCAGATCGACTCCCAGCACTACCCTATTTTCCACCAGCTGGAGGCCGTGCGGCTCTTC
TCCAAGCATGAGTTATTTGCTGGTATAAAGGATGGAGAAAGCCTGCAGCTCTTTGAACAA
AGTTCTCGCTCTGCGCATAAACAAGAGACACACACCATGGAGGCCGTGAAGCTTGTAGAG
TTTGATCTTAAGCAAACGCTTACCAGGCTCATGGCACATCTTTTTGGAGATGAGCTGGAG
ATAAGATGGGTAGACTGCTACTTCCCTTTTACACATCCTTCCTTTGAGATGGAGATCAAC
TTTCATGGAGAATGGCTGGAAGTTCTTGGCTGCGGGGTGATGGAACAACAACTGGTCAAT
TCAGCTGGTGCTCAAGACCGAATCGGCTGGGCTTTTGGCCTAGGATTAGAAAGGCTAGCC
ATGATCCTCTACGACATCCCTGATATCCGTCTCTTCTGGTGTGAGGACGAGCGCTTCCTG
AAGCAGTTCTGTGTATCCAACATTAATCAGAAGGTGAAGTTTCAGCCTCTTAGCAAATAT
CCGGCTGTGATCAATGATATTTCATTCTGGTTGCCCTCTGAGAATTACGCAGAAAATGAT
TTCTATGACTTAGTCCGAACAATTGGAGGAGACCTGGTGGAAAAGGTTGATCTCATAGAC
AAGTTTGTACATCCAAAGACGCACAAGACCAGCCACTGCTACCGCATCACGTACCGCCAC
ATGGAACGGACTCTGTCCCAGAGAGAGGTCAGGCACATCCACCAGGCCTTGCAGGAGGCT
GCAGTCCAGCTGTTGGGTGTGGAGGGCAGGTTCTGA

Enzyme 14 GenBank Gene ID

AF097441

Enzyme 14 GeneCard ID

FARS2

Enzyme 14 GenAtlas ID

FARS2

Enzyme 14 HGNC ID

HGNC:21062 Link Image

Enzyme 14 Chromosome Location

Enzyme 14 Locus

6p25.1

Enzyme 14 SNPs

SNPJam Report Link Image

Enzyme 14 General References

Bullard JM, Cai YC, Demeler B, Spremulli LL: Expression and characterization of a human mitochondrial phenylalanyl-tRNA synthetase. J Mol Biol. 1999 May 14;288(4):567-77. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Klipcan L, Levin I, Kessler N, Moor N, Finarov I, Safro M: The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase. Structure. 2008 Jul;16(7):1095-104. [PubMed ]
Klipcan L, Moor N, Kessler N, Safro MG: Eukaryotic cytosolic and mitochondrial phenylalanyl-tRNA synthetases catalyze the charging of tRNA with the meta-tyrosine. Proc Natl Acad Sci U S A. 2009 Jul 7;106(27):11045-8. Epub 2009 Jun 22. [PubMed ]

Enzyme 14 Metabolite References

Not Available

Enzyme 15 [top]

Enzyme 15 ID

5578

Enzyme 15 Name

3'(2'),5'-bisphosphate nucleotidase 1

Enzyme 15 Synonyms

Bisphosphate 3'-nucleotidase 1
PAP-inositol-1,4-phosphatase
PIP

Enzyme 15 Gene Name

BPNT1

Enzyme 15 Protein Sequence

>3'(2'),5'-bisphosphate nucleotidase 1

MASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICS
SLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLD
GTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGF
QLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFAS
PGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPE
SIKNALVP

Enzyme 15 Number of Residues

308

Enzyme 15 Molecular Weight

33392.0

Enzyme 15 Theoretical pI

5.41

Enzyme 15 GO Classification

Function
catalytic activity hydrolase activity hydrolase activity, acting on ester bonds inositol or phosphatidylinositol phosphatase activity phosphatase activity phosphoric ester hydrolase activity
Process
—
Component
—

Enzyme 15 General Function

Involved in inositol or phosphatidylinositol phosphatase activity

Enzyme 15 Specific Function

Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4- trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6

Enzyme 15 Pathways

Sulfate and Sulfite Metabolism (map00920 )

Enzyme 15 Reactions

adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate [RN:R00188]

Enzyme 15 Pfam Domain Function

Inositol_P (PF00459 )

Enzyme 15 Signals

None

Enzyme 15 Transmembrane Regions

None

Enzyme 15 Essentiality

Not Available

Enzyme 15 GenBank ID Protein

Not Available

Enzyme 15 UniProtKB/Swiss-Prot ID

O95861

Enzyme 15 UniProtKB/Swiss-Prot Entry Name

BPNT1_HUMAN Link Image

Enzyme 15 PDB ID

1JP4

Enzyme 15 PDB File

Show

Enzyme 15 3D Structure

Enzyme 15 Cellular Location

Not Available

Enzyme 15 Gene Sequence

>927 bp

ATGGCTTCCAGTAACACTGTGTTGATGCGGTTGGTAGCCTCCGCATATTCTATTGCTCAA
AAGGCAGGAATGATAGTCAGACGTGTTATTGCTGAAGGAGACCTGGGTATTGTGGAGAAG
ACCTGTGCAACAGACCTGCAGACCAAAGCTGACCGATTGGCACAGATGAGCATATGTTCT
TCATTGGCCCGGAAATTCCCCAAACTCACAATTATAGGGGAAGAGGATCTGCCTTCTGAG
GAAGTGGATCAAGAGCTGATTGAAGACAGTCAGTGGGAAGAAATACTGAAGCAACCATGC
CCATCGCAGTACAGTGCTATTAAAGAAGAAGATCTCGTGGTCTGGGTTGATCCTCTGGAT
GGAACCAAGGAATATACCGAAGGTCTTCTTGACAATGTAACAGTTCTTATTGGAATTGCT
TATGAAGGAAAAGCCATAGCAGGAGTTATTAACCAGCCATATTACAACTATGAGGCAGGA
CCAGATGCTGTGTTGGGGAGGACAATCTGGGGAGTTTTAGGTTTAGGCGCCTTTGGGTTT
CAGCTGAAAGAAGTCCCTGCTGGGAAACACATTATCACAACTACTCGATCCCATAGCAAC
AAGTTGGTTACTGACTGTGTTGCTGCTATGAACCCCGATGCTGTGCTGCGAGTAGGAGGA
GCAGGAAATAAGATTATTCAGCTGATTGAAGGCAAAGCCTCTGCTTATGTATTTGCAAGT
CCTGGTTGTAAGAAGTGGGATACTTGTGCTCCAGAAGTTATTTTACATGCTGTGGGAGGC
AAGTTAACCGATATCCATGGGAATGTTCTTCAGTACCACAAGGATGTGAAGCATATGAAC
TCTGCAGGAGTCCTGGCCACACTGAGGAATTATGACTACTATGCAAGCCGAGTTCCAGAA
TCTATTAAAAATGCACTTGTTCCTTAA

Enzyme 15 GenBank Gene ID

AF125042

Enzyme 15 GeneCard ID

BPNT1

Enzyme 15 GenAtlas ID

BPNT1

Enzyme 15 HGNC ID

HGNC:1096

Enzyme 15 Chromosome Location

Enzyme 15 Locus

1q41

Enzyme 15 SNPs

SNPJam Report Link Image

Enzyme 15 General References

Spiegelberg BD, Xiong JP, Smith JJ, Gu RF, York JD: Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate. J Biol Chem. 1999 May 7;274(19):13619-28. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]

Enzyme 15 Metabolite References

Not Available

Enzyme 16 [top]

Enzyme 16 ID

5605

Enzyme 16 Name

ADP-dependent glucokinase

Enzyme 16 Synonyms

ADP-GK
ADPGK
RbBP-35

Enzyme 16 Gene Name

ADPGK

Enzyme 16 Protein Sequence

>ADP-dependent glucokinase

MALWRGSAYAGFLALAVGCVFLLEPELPGSALRSLWSSLCLGPAPAPPGPVSPEGRLAAA
WDALIVRPVRRWRRVAVGVNACVDVVLSGVKLLQALGLSPGNGKDHSILHSRNDLEEAFI
HFMGKGAAAERFFSDKETFHDIAQVASEFPGAQHYVGGNAALIGQKFAANSDLKVLLCGP
VGPKLHELLDDNVFVPPESLQEVDEFHLILEYQAGEEWGQLKAPHANRFIFSHDLSNGAM
NMLEVFVSSLEEFQPDLVVLSGLHMMEGQSKELQRKRLLEVVTSISDIPTGIPVHLELAS
MTNRELMSSIVHQQVFPAVTSLGLNEQELLFLTQSASGPHSSLSSWNGVPDVGMVSDILF
WILKEHGRSKSRASDLTRIHFHTLVYHILATVDGHWANQLAAVAAGARVAGTQACATETI
DTSRVSLRAPQEFMTSHSEAGSRIVLNPNKPVVEWHREGISFHFTPVLVCKDPIRTVGLG
DAISAEGLFYSEVHPHY

Enzyme 16 Number of Residues

497

Enzyme 16 Molecular Weight

54088.3

Enzyme 16 Theoretical pI

6.17

Enzyme 16 GO Classification

Function
catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity transferase activity, transferring phosphorus-containing groups
Process
carbohydrate metabolic process metabolic process primary metabolic process
Component
—

Enzyme 16 General Function

Involved in phosphotransferase activity, alcohol group as acceptor

Enzyme 16 Specific Function

Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. GDP and CDP can replace ADP, but with reduced efficiency

Enzyme 16 Pathways

Not Available

Enzyme 16 Reactions

ADP + D-glucose = AMP + D-glucose 6-phosphate [RN:R05804]

Enzyme 16 Pfam Domain Function

ADP_PFK_GK (PF04587 )

Enzyme 16 Signals

1-22

Enzyme 16 Transmembrane Regions

None

Enzyme 16 Essentiality

Not Available

Enzyme 16 GenBank ID Protein

13543940

Enzyme 16 UniProtKB/Swiss-Prot ID

Q9BRR6

Enzyme 16 UniProtKB/Swiss-Prot Entry Name

ADPGK_HUMAN Link Image

Enzyme 16 PDB ID

Not Available

Enzyme 16 Cellular Location

Not Available

Enzyme 16 Gene Sequence

>1494 bp

ATGGCGCTGTGGCGCGGCTCCGCGTACGCGGGCTTCCTGGCGCTGGCCGTGGGCTGCGTC
TTCCTGCTGGAGCCAGAGCTGCCAGGCTCGGCGCTGCGCTCTCTCTGGAGCTCGCTGTGT
CTGGGGCCCGCGCCTGCGCCCCCGGGACCCGTCTCCCCCGAGGGCCGGTTGGCGGCAGCC
TGGGACGCGCTTATCGTGCGGCCAGTCCGGCGCTGGCGCCGCGTGGCAGTGGGAGTCAAT
GCATGTGTTGATGTGGTGCTCTCAGGGGTGAAGCTCTTGCAGGCACTTGGCCTTAGTCCT
GGGAATGGGAAAGATCACAGCATTCTGCATTCAAGGAATGATCTGGAAGAAGCCTTCATT
CACTTCATGGGGAAGGGAGCAGCTGCTGAGCGCTTCTTCAGTGATAAGGAAACTTTTCAC
GACATTGCCCAGGTTGCGTCAGAGTTCCCAGGAGCCCAGCACTATGTAGGAGGAAATGCA
GCTTTAATTGGACAGAAATTTGCAGCCAACTCAGATTTAAAGGTTCTTCTTTGCGGTCCA
GTTGGTCCAAAGCTACATGAGCTTCTTGATGACAATGTCTTTGTTCCACCAGAGTCATTG
CAGGAAGTGGATGAGTTCCACCTCATTTTAGAGTATCAAGCAGGGGAGGAGTGGGGCCAG
TTAAAAGCTCCCCATGCCAACCGATTCATCTTCTCTCACGACCTCTCCAACGGGGCCATG
AATATGCTGGAGGTGTTTGTGTCTAGCCTGGAGGAGTTTCAGCCAGACCTGGTGGTCCTC
TCTGGATTGCACATGATGGAGGGACAAAGCAAGGAGCTCCAGAGGAAGAGACTCTTGGAG
GTTGTAACCTCCATTTCTGACATCCCCACTGGTATTCCAGTTCACCTAGAGCTGGCCAGT
ATGACTAACAGGGAGCTCATGAGCAGCATTGTCCATCAGCAGGTCTTTCCCGCGGTGACT
TCCCTTGGGCTGAATGAACAGGAGCTGTTATTTCTCACCCAGTCAGCCTCTGGACCTCAC
TCTTCTCTCTCTTCCTGGAACGGTGTTCCTGATGTGGGCATGGTCAGTGACATCCTCTTC
TGGATCTTGAAAGAACATGGGAGGAGTAAAAGCAGAGCCTCGGATCTCACCAGGATCCAT
TTCCACACGCTGGTCTACCACATCCTGGCAACTGTGGATGGACACTGGGCCAACCAGCTG
GCAGCCGTGGCTGCAGGAGCTCGTGTGGCTGGGACACAGGCCTGCGCCACAGAAACCATA
GACACCAGCCGAGTGTCTCTGAGGGCACCCCAAGAGTTCATGACTTCCCATTCGGAGGCA
GGCTCCAGGATTGTATTAAACCCAAACAAGCCAGTAGTAGAATGGCACAGAGAGGGAATA
TCCTTCCACTTCACACCAGTATTGGTGTGTAAAGACCCCATTCGAACTGTAGGCCTTGGA
GATGCCATTTCAGCCGAAGGACTCTTCTATTCGGAAGTACACCCTCACTATTAG

Enzyme 16 GenBank Gene ID

BC006112

Enzyme 16 GeneCard ID

ADPGK

Enzyme 16 GenAtlas ID

ADPGK

Enzyme 16 HGNC ID

HGNC:25250 Link Image

Enzyme 16 Chromosome Location

Enzyme 16 Locus

15q24.1

Enzyme 16 SNPs

SNPJam Report Link Image

Enzyme 16 General References

Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 16 Metabolite References

Not Available

Enzyme 17 [top]

Enzyme 17 ID

5606

Enzyme 17 Name

Glycogen phosphorylase, liver form

Enzyme 17 Synonyms

Not Available

Enzyme 17 Gene Name

PYGL

Enzyme 17 Protein Sequence

>Glycogen phosphorylase, liver form

MAKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTV
RDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDI
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRDGWQVEEA
DDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVN
TMRLWSARAPNDFNLRDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKASKFGSTRGAGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKL
PWSKAWELTQKTFAYTNHTVLPEALERWPVDLVEKLLPRHLEIIYEINQKHLDRIVALFP
KDVDRLRRMSLIEEEGSKRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKF
QNKTNGITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQ
ENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRIKKDPKKLFV
PRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKLKVIFLENYRVSLAEKVIPA
TDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRIDDVA
ALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEA
YVKCQDKVSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSDLKISLSNE
SNKVNGN

Enzyme 17 Number of Residues

847

Enzyme 17 Molecular Weight

97147.8

Enzyme 17 Theoretical pI

7.17

Enzyme 17 GO Classification

Function
binding catalytic activity cofactor binding phosphorylase activity pyridoxal phosphate binding transferase activity transferase activity, transferring glycosyl groups transferase activity, transferring hexosyl groups
Process
carbohydrate metabolic process metabolic process primary metabolic process
Component
—

Enzyme 17 General Function

Involved in phosphorylase activity

Enzyme 17 Specific Function

Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties

Enzyme 17 Pathways

Starch and Sucrose Metabolism (map00500 )

Enzyme 17 Reactions

[(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate [RN:R01821 R06050]

Enzyme 17 Pfam Domain Function

Phosphorylase (PF00343 )

Enzyme 17 Signals

None

Enzyme 17 Transmembrane Regions

None

Enzyme 17 Essentiality

Not Available

Enzyme 17 GenBank ID Protein

183353

Enzyme 17 UniProtKB/Swiss-Prot ID

P06737

Enzyme 17 UniProtKB/Swiss-Prot Entry Name

PYGL_HUMAN Link Image

Enzyme 17 PDB ID

1L7X

Enzyme 17 PDB File

Show

Enzyme 17 3D Structure

Enzyme 17 Cellular Location

Not Available

Enzyme 17 Gene Sequence

>2544 bp

ATGGGCGAACCGCTGACAGACCAGGAGAAGCGGCGGCAGATCAGCATCCGCGGCATCGTG
GGCGTGGAGAACGTGGCAGAGCTGAAGAAGAGTTTCAACCGGCACCTGCACTTCACGCTG
GTCAAGGACCGCAACGTGGCCACCACCCGCGACTACTACTTCGCGCTGGCGCACACGGTG
CGGGACCACCTGGTGGGGCGCTGGATCCGCACGCAGCAGCACTACTACGACAAGTGCCCC
AAGAGGGAATATTACCTCTCTCTGGAATTTTACATGGGCCGAACATTACAGAACACCATG
ATCAACCTCGGTCTGCAAAATGCCTGTGATGAGGCCATTTACCAGCTTGGATTGGATATA
GAAGAGTTAGAAGAAATTGAAGAAGATGCTGGACTTGGCAATGGTGGTCTTGGGAGACTT
GCTGCCTGCTTCTTGGATTCCATGGCAACCCTGGGACTTGCAGCCTATGGATACGGCATT
CGGTATGAATATGGGATTTTCAATCAGAAGATCCGAGATGGATGGCAGGTAGAAGAAGCA
GATGATTGGCTCAGATATGGAAACCCTTGGGAGAAGTCCCGCCCAGAATTCATGCTGCCT
GTGCACTTCTATGGAAAAGTAGAACACACCAACACCGGGACCAAGTGGATTGACACTCAA
GTGGTCCTGGCTCTGCCATATGACACCCCCGAGCCCGGCTACATGAATAACACTGTCAAC
ACCATGCGCCTCTGGTCTGCTCGGGCACCAAATGACTTTAACCTCAGAGACTTTAATGTT
GGAGACTACATTCAGGCTGTGCTGGACCGAAACCTGGCCGAGAACATCTCCCGGGTCCTC
TATCCCAATGACAATTTTTTTGAAGGGAAGGAGCTAAGATTGAAGCAGGAATACTTTGTG
GTGGCTGCAACCTTGCAAGATATCATCCGCCGTTTCAAAGCCTCCAAGTTTGGCTCCACC
CGTGGTCAAGGAACTGTGTTTGATGCCTTCCCGGATCAGGTGGCCATCCAGCTGAATGAT
ACTCACCCTCGCATCGCGATCCCTGAGCTGATGAGGATTTTTGTGGATATTGAAAAACTG
CCCTGGTCCAAGGCATGGGAGCTCAACCAGAAGACCTTCGCCTACACCAACCACACAGTG
CTCCCGGAAGCCCTGGAGCGCTGGCCCGTGGACCTGGTGGAGAAGCTGCTCCCTCGACAT
TTGGAAATCATTTATGAGATAAATCAGAAGCATTTAGATAGAATTGTGGCCTTGTTTCCT
AAAGATGTGGACCCTCTGAGAAGGATGTCTCTGATAGAAGAGGAAGGAAGCAAAAGGATC
AACATGGCCCATCTCTGCATTGTCGGTTCCCATGCTGTGAATGGCGTGGCTAAAATCCAC
TCAGACATCGTGAAGACTAAAGTATTCAAGGACTTCAGTGAGCTAGAACCTGACAAGTTT
CAGAATAAAACCAATGGGATCACTCCAAGGCGCTGGCTCCTACTCTGCAACCCAGGACTT
GCAGAGCTCATAGCAGAGAAAATTGGAGAAGACTATGTGAAAGACCTGAGCCAGCTGACG
AAGCTCCACAGCTTCCTGGGTGATGATGTCTTCCTCCGGGAACTCGCCAAGGTGAAGCAG
GAGAATAAGCTGAAGTTTTCTCAGTTCCTGGAGACGGAGTACAAAGTGAAGATCAACCCA
TCCTCCATGTTTGATGTCCAGGTGAAGAGGATACATGAGTACAAGCGACAGCTCTTGAAC
TGTCTGCATGTGATCACGATGTACAACCGCATTAAGAAAGACCCTAAGAAGTTATTCGTG
CCAAGGACAGTTATCATTGGTGGTAAAGCTGCCCCAGGATATCACATGGCCAAAATGATC
ATAAAGCTGATCACTTCAGTGGCAGATGTGGTGAACAATGACCCTATGGTTGGAAGCAAG
TTGAAAGTCATCTTCTTGGAGAACTACAGAGTATCTCTTGCTGAAAAAGTCATTCCAGCC
ACAGATCTGTCAGAGCAGATTTCCACTGCAGGCACCGAAGCCTCGGGGACAGGCAATATG
AAGTTCATGCTAAATGGGGCCCTAACTATCGGGACCATGGATGGGGCCAATGTGGAAATG
GCAGAAGAAGCTGGGGAAGAGAACCTGTTCATCTTTGGCATGAGCATAGATGATGTGGCT
GCTTTGGACAAGAAAGGGTACGAGGCAAAAGAATACTATGAGGCACTTCCAGAGCTGAAG
CTGGTCATTGATCAAATTGACAATGGCTTTTTTTCTCCCAAGCAGCCTGACCTCTTCAAA
GATATCATCAACATGCTATTTTATCATGACAGGTTTAAAGTCTTTGCAGACTACGAAGCC
TATGTCAAGTGTCAAGATAAAGTGAGTCAGCTGTACATGAATCCAAAGGCCTGGAACACA
ATGGTACTCAAAAACATAGCTGCCTCGGGGAAATTCTCCAGTGACCGAACAATTAAAGAA
TATGCCCAAAACATCTGGAACGTGGAACCTTCAGATCTAAAGATTTCTCTATCCAATGAA
TCTAACAAAGTCAATGGAAATTGA

Enzyme 17 GenBank Gene ID

M14636

Enzyme 17 GeneCard ID

PYGL

Enzyme 17 GenAtlas ID

PYGL

Enzyme 17 HGNC ID

HGNC:9725

Enzyme 17 Chromosome Location

Enzyme 17 Locus

14q21-q22

Enzyme 17 SNPs

SNPJam Report Link Image

Enzyme 17 General References

Newgard CB, Nakano K, Hwang PK, Fletterick RJ: Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8132-6. [PubMed ]
Chang S, Rosenberg MJ, Morton H, Francomano CA, Biesecker LG: Identification of a mutation in liver glycogen phosphorylase in glycogen storage disease type VI. Hum Mol Genet. 1998 May;7(5):865-70. [PubMed ]
Burwinkel B, Bakker HD, Herschkovitz E, Moses SW, Shin YS, Kilimann MW: Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI. Am J Hum Genet. 1998 Apr;62(4):785-91. [PubMed ]
Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gorin FA, Mullinax RL, Ignacio PC, Neve RL, Kurnit DM: McArdle's & Hers' diseases: glycogen phosphorylase transcriptional expression in human tissues. J Neurogenet. 1987 Dec;4(6):293-308. [PubMed ]
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Rath VL, Ammirati M, Danley DE, Ekstrom JL, Gibbs EM, Hynes TR, Mathiowetz AM, McPherson RK, Olson TV, Treadway JL, Hoover DJ: Human liver glycogen phosphorylase inhibitors bind at a new allosteric site. Chem Biol. 2000 Sep;7(9):677-82. [PubMed ]
Rath VL, Ammirati M, LeMotte PK, Fennell KF, Mansour MN, Danley DE, Hynes TR, Schulte GK, Wasilko DJ, Pandit J: Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core. Mol Cell. 2000 Jul;6(1):139-48. [PubMed ]
Ekstrom JL, Pauly TA, Carty MD, Soeller WC, Culp J, Danley DE, Hoover DJ, Treadway JL, Gibbs EM, Fletterick RJ, Day YS, Myszka DG, Rath VL: Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase. Chem Biol. 2002 Aug;9(8):915-24. [PubMed ]

Enzyme 17 Metabolite References

Not Available

Enzyme 18 [top]

Enzyme 18 ID

5610

Enzyme 18 Name

Glycogen phosphorylase, muscle form

Enzyme 18 Synonyms

Myophosphorylase

Enzyme 18 Gene Name

PYGM

Enzyme 18 Protein Sequence

>Glycogen phosphorylase, muscle form

MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTV
RDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDM
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEA
DDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVN
TMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERM
DWDKAWDVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFP
GDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKF
QNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQ
ENKLKFAAYLEREYKVHINPNSLFDIQVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFV
PRTVMIGGKAAPGYHMAKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPA
ADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVD
KLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYED
YIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDE
AI

Enzyme 18 Number of Residues

842

Enzyme 18 Molecular Weight

97091.3

Enzyme 18 Theoretical pI

7.03

Enzyme 18 GO Classification

Function
binding catalytic activity cofactor binding phosphorylase activity pyridoxal phosphate binding transferase activity transferase activity, transferring glycosyl groups transferase activity, transferring hexosyl groups
Process
carbohydrate metabolic process metabolic process primary metabolic process
Component
—

Enzyme 18 General Function

Involved in phosphorylase activity

Enzyme 18 Specific Function

Enzyme 18 Pathways

Starch and Sucrose Metabolism (map00500 )

Enzyme 18 Reactions

[(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate [RN:R01821 R06050]

Enzyme 18 Pfam Domain Function

Phosphorylase (PF00343 )

Enzyme 18 Signals

None

Enzyme 18 Transmembrane Regions

None

Enzyme 18 Essentiality

Not Available

Enzyme 18 GenBank ID Protein

3153910

Enzyme 18 UniProtKB/Swiss-Prot ID

P11217

Enzyme 18 UniProtKB/Swiss-Prot Entry Name

PYGM_HUMAN Link Image

Enzyme 18 PDB ID

1XL1

Enzyme 18 PDB File

Show

Enzyme 18 3D Structure

Enzyme 18 Cellular Location

Not Available

Enzyme 18 Gene Sequence

>2529 bp

ATGTCCCGGCCCCTGTCAGACCAAGAGAAAAGAAAGCAAATCAGTGTGCGTGGCCTGGCC
GGCGTGGAGAACGTGACTGAGCTGAAAAAGAACTTCAACCGGCACCTGCATTTCACACTC
GTAAAGGACCGCAATGTGGCCACCCCACGAGACTACTACTTTGCTCTGGCCCATACCGTG
CGCGACCACCTCGTGGGGCGCTGGATCCGCACGCAGCAGCACTACTATGAGAAGGACCCC
AAGAGGATCTACTACCTGTCTTTAGAGTTCTATATGGGACGGACGCTACAGAACACCATG
GTGAACCTGGCCTTAGAGAATGCCTGTGACGAGGCCACCTACCAGCTGGGCCTGGACATG
GAGGAGCTGGAGGAAATTGAGGAGGATGCGGGGCTGGGCAACGGGGGCCTGGGCCGGCTG
GCAGCCTGCTTTCTTGACTCCATGGCAACACTGGGCCTGGCCGCCTATGGCTACGGGATT
CGCTATGAGTTTGGGATTTTTAACCAGAAGATCTCCGGGGGCTGGCAGATGGAGGAGGCC
GATGACTGGCTTCGCTACGGCAACCCCTGGGAGAAGGCCCGGCCCGAGTTCACGCTACCT
GTGCACTTCTACGGCCATGTGGAGCACACCAGCCAGGGTGCCAAGTGGGTGGACACACAG
GTGGTACTGGCCATGCCCTACGATACGCCCGTGCCTGGCTATCGCAACAATGTTGTCAAC
ACCATGCGCCTCTGGTCTGCCAAGGCTCCCAATGACTTCAACCTCAAGGACTTCAATGTC
GGTGGCTACATCCAGGCTGTGTTGGACCGAAACCTGGCGGAGAACATCTCTCGTGTCCTG
TACCCCAATGATAATTTCTTCGAAGGGAAGGAGCTGCGGCTGAAGCAGGAGTATTTCGTG
GTGGCTGCCACCCTCCAGGACATCATCCGTCGCTTCAAGTCTTCCAAGTTCGGCTGCCGT
GATCCCGTGCGCACGAACTTCGATGCCTTCCCAGATAAGGTGGCCATCCAGCTCAATGAC
ACCCACCCCTCCCTGGCCATCCCCGAGCTGATGAGGATCCTGGTGGACCTGGAACGGATG
GACTGGGACAAGGCGTGGGATGTGACAGTGAGGACCTGTGCCTACACCAACCACACGGTG
CTGCCCGAGGCCCTGGAGCGCTGGCCGGTGCACCTCTTGGAGACGCTGCTGCCGCGGCAC
CTCCAGATCATCTACGAGATCAACCAGCGCTTCCTCAACCGGGTGGCGGCCGCATTCCCA
GGGGACGTAGACCGGCTGCGGCGCATGTCGCTGGTGGAGGAGGGCGCAGTGAAGCGCATC
AACATGGCACACCTGTGCATCGCGGGGTCGCACGCCGTCAACGGCGTGGCGCGCATCCAC
TCCGAGATCCTCAAGAAGACCATCTTCAAAGACTTCTATGAGCTGGAGCCTCATAAGTTC
CAGAATAAGACCAACGGCATCACCCCTCGGCGCTGGCTGGTTCTGTGTAACCCCGGGCTG
GCAGAGGTCATTGCTGAGCGCATCGGGGAGGACTTCATCTCTGACCTGGACCAGCTGCGC
AAACTGCTCTCCTTTGTGGATGATGAAGCTTTCATTCGGGATGTGGCCAAAGTGAAGCAG
GAAAACAAGTTGAAGTTTGCTGCCTACCTAGAGAGGGAATACAAAGTCCACATCAACCCC
AACTCACTCTTCGACATCCAGGTGAAGCGGATTCACGAATATAAACGACAGCTCCTCAAC
TGCCTCCATGTCATCACCCTGTACAACCGCATCAAGAGGGAGCCCAATAAGTTTTTTGTG
CCTCGGACTGTGATGATTGGAGGGAAGGCTGCACCTGGGTACCACATGGCCAAGATGATC
ATCAGACTCGTCACAGCCATCGGGGATGTGGTCAACCATGACCCGGCAGTGGGTGACCGC
CTCCGTGTCATCTTCCTGGAGAACTACCGAGTCTCACTGGCCGAGAAAGTGATCCCAGCT
GCAGACCTCTCTGAGCAGATCTCCACTGCGGGCACTGAAGCCTCAGGCACCGGCAACATG
AAGTTCATGCTCAACGGGGCTCTGACCATTGGCACCATGGACGGGGCCAATGTGGAGATG
GCAGAAGAGGCGGGAGAGGAAAACTTCTTCATCTTTGGCATGCGGGTGGAGGATGTGGAT
AAGCTTGACCAAAGAGGGTACAATGCCCAGGAGTACTACGATCGCATTCCTGAGCTTCGG
CAGGTCATTGAGCAGCTGAGCAGTGGCTTCTTCTCCCCCAAACAGCCCGACCTGTTCAAG
GACATTGTCAATATGCTCATGCACCATGACCGGTTTAAAGTCTTCGCAGATTATGAAGAC
TACATTAAATGCCAGGAGAAAGTCAGCGCCTTGTACAAGAACCCAAGAGAGTGGACGCGG
ATGGTGATCCGGAACATAGCCACCTCTGGCAAGTTCTCCAGTGACCGCACCATTGCCCAG
TATGCCCGGGAGATCTGGGGTGTGGAGCCTTCCCGCCAGCGCCTGCCAGCCCCGGATGAG
GCCATCTGA

Enzyme 18 GenBank Gene ID

AF066859

Enzyme 18 GeneCard ID

PYGM

Enzyme 18 GenAtlas ID

PYGM

Enzyme 18 HGNC ID

HGNC:9726

Enzyme 18 Chromosome Location

Enzyme 18 Locus

11q12-q13.2

Enzyme 18 SNPs

SNPJam Report Link Image

Enzyme 18 General References

Burke J, Hwang P, Anderson L, Lebo R, Gorin F, Fletterick R: Intron/exon structure of the human gene for the muscle isozyme of glycogen phosphorylase. Proteins. 1987;2(3):177-87. [PubMed ]
Kubisch C, Wicklein EM, Jentsch TJ: Molecular diagnosis of McArdle disease: revised genomic structure of the myophosphorylase gene and identification of a novel mutation. Hum Mutat. 1998;12(1):27-32. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Hwang PK, See YP, Vincentini AM, Powers MA, Fletterick RJ, Crerar MM: Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs. Eur J Biochem. 1985 Oct 15;152(2):267-74. [PubMed ]
Gautron S, Daegelen D, Mennecier F, Dubocq D, Kahn A, Dreyfus JC: Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis. J Clin Invest. 1987 Jan;79(1):275-81. [PubMed ]
Carty TJ, Tu J-I, Graves DJ: Regulation of glycogen phosphorylase. Role of the peptide region surrounding the phosphoserine residue in determining enzyme properties. J Biol Chem. 1975 Jul 10;250(13):4980-5. [PubMed ]
Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Tsujino S, Shanske S, DiMauro S: Molecular genetic heterogeneity of myophosphorylase deficiency (McArdle's disease). N Engl J Med. 1993 Jul 22;329(4):241-5. [PubMed ]
Tsujino S, Shanske S, Martinuzzi A, Heiman-Patterson T, DiMauro S: Two novel missense mutations (E654K, L396P) in Caucasian patients with myophosphorylase deficiency (McArdle's disease). Hum Mutat. 1995;6(3):276-7. [PubMed ]
Tsujino S, Shanske S, Nonaka I, DiMauro S: The molecular genetic basis of myophosphorylase deficiency (McArdle's disease). Muscle Nerve. 1995;3:S23-7. [PubMed ]
Vorgerd M, Kubisch C, Burwinkel B, Reichmann H, Mortier W, Tettenborn B, Pongratz D, Lindemuth R, Tegenthoff M, Malin JP, Kilimann MW: Mutation analysis in myophosphorylase deficiency (McArdle's disease). Ann Neurol. 1998 Mar;43(3):326-31. [PubMed ]
Gamez J, Fernandez R, Bruno C, Andreu AL, Cervera C, Navarro C, Schwartz S, Dimauro S: A new mutation in the regulatory domain of the myophosphorylase gene affecting protein dimer contact. Muscle Nerve. 1999 Aug;22(8):1136-8. [PubMed ]
Andreu AL, Bruno C, Tamburino L, Gamez J, Shanske S, Cervera C, Navarro C, DiMauro S: A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish patient with McArdle's disease. Neuromuscul Disord. 1999 May;9(3):171-3. [PubMed ]
Rubio JC, Martin MA, Garcia A, Campos Y, Cabello A, Culebras JM, Arenas J: McArdle's disease associated with homozygosity for the missense mutation Gly204Ser of the myophosphorylase gene in a Spanish patient. Neuromuscul Disord. 1999 May;9(3):174-5. [PubMed ]
Fernandez R, Navarro C, Andreu AL, Bruno C, Shanske S, Gamez J, Teijeira S, Hernandez I, Teijeiro A, Fernandez JM, Musumeci O, DiMauro S: A novel missense mutation (W797R) in the myophosphorylase gene in Spanish patients with McArdle disease. Arch Neurol. 2000 Feb;57(2):217-9. [PubMed ]
Rubio JC, Martin MA, Campos Y, Auciello R, Cabello A, Arenas J: A missense mutation W797R in the myophosphorylase gene in a Spanish patient with McArdle's disease. Muscle Nerve. 2000 Jan;23(1):129-31. [PubMed ]
Rubio JC, Martin MA, Campos Y, Cabello A, Arenas J: A missense mutation T487N in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Feb;10(2):138-40. [PubMed ]
Martin MA, Rubio JC, Campos Y, Ricoy JR, Cabello A, Arenas J: A homozygous missense mutation (A659D) in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Aug;10(6):447-9. [PubMed ]
Martin MA, Rubio JC, Buchbinder J, Fernandez-Hojas R, del Hoyo P, Teijeira S, Gamez J, Navarro C, Fernandez JM, Cabello A, Campos Y, Cervera C, Culebras JM, Andreu AL, Fletterick R, Arenas J: Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study. Ann Neurol. 2001 Nov;50(5):574-81. [PubMed ]
Bruno C, Lanzillo R, Biedi C, Iadicicco L, Minetti C, Santoro L: Two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease. Neuromuscul Disord. 2002 Jun;12(5):498-500. [PubMed ]

Enzyme 18 Metabolite References

Not Available

Enzyme 19 [top]

Enzyme 19 ID

5612

Enzyme 19 Name

Glycogen phosphorylase, brain form

Enzyme 19 Synonyms

Not Available

Enzyme 19 Gene Name

PYGB

Enzyme 19 Protein Sequence

>Glycogen phosphorylase, brain form

MAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTV
RDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDL
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEA
DDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLDTQVVLAMPYDTPVPGYKNNTVN
TMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKV
DWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFP
GDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKF
QNKTNGITPRRWLLLCNPGLADTIVEKIGEEFLTDLSQLKKLLPLVSDEVFIRDVAKVKQ
ENKLKFSAFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVVTLYNRIKRDPAKAFV
PRTVMIGGKAAPGYHMAKLIIKLVTSIGDVVNHDPVVGDRLKVIFLENYRVSLAEKVIPA
ADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGAENLFIFGLRVEDVE
ALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDCFKDIVNMLMHHDRFKVFADYEA
YMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPPNI
PRD

Enzyme 19 Number of Residues

843

Enzyme 19 Molecular Weight

96695.2

Enzyme 19 Theoretical pI

6.85

Enzyme 19 GO Classification

Function
binding catalytic activity cofactor binding phosphorylase activity pyridoxal phosphate binding transferase activity transferase activity, transferring glycosyl groups transferase activity, transferring hexosyl groups
Process
carbohydrate metabolic process metabolic process primary metabolic process
Component
—

Enzyme 19 General Function

Involved in phosphorylase activity

Enzyme 19 Specific Function

Enzyme 19 Pathways

Starch and Sucrose Metabolism (map00500 )

Enzyme 19 Reactions

[(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate [RN:R01821 R06050]

Enzyme 19 Pfam Domain Function

Phosphorylase (PF00343 )

Enzyme 19 Signals

None

Enzyme 19 Transmembrane Regions

None

Enzyme 19 Essentiality

Not Available

Enzyme 19 GenBank ID Protein

9650807

Enzyme 19 UniProtKB/Swiss-Prot ID

P11216

Enzyme 19 UniProtKB/Swiss-Prot Entry Name

PYGB_HUMAN Link Image

Enzyme 19 PDB ID

Not Available

Enzyme 19 Cellular Location

Not Available

Enzyme 19 Gene Sequence

>2532 bp

ATGGCGAAGCCGCTGACGGACAGCGAGAAGCGGAAGCAGATCAGCGTGCGCGGCCTGGCG
GGGCTAGGCGACGTGGCCGAGGTGCGGAAGAGCTTCAACCGGCACTTGCACTTCACGCTG
GTCAAGGACCGCAATGTGGCCACGCCCCGCGACTACTTCTTCGCGCTGGCGCACACGGTG
CGCGACCACCTCGTGGGCCGCTGGATCCGCACGCAGCAGCACTACTACGAGCGCGACCCC
AAGCGCATTTATTATCTTTCCCTGGAATTCTACATGGGTCGCACGCTGCAGAACACGATG
GTGAACCTGGGCCTTCAGAATGCCTGCGATGAAGCCATCTATCAGTTGGGGTTAGACTTG
GAGGAACTCGAGGAGATAGAAGAAGATGCTGGCCTTGGGAATGGAGGCCTGGGGAGGCTG
GCAGCGTGTTTCCTTGACTCAATGGCTACCTTGGGCCTGGCAGCATACGGCTATGGAATC
CGCTATGAATTTGGGATTTTTAACCAGAAGATTGTCAATGGCTGGCAGGTAGAGGAGGCC
GATGACTGGCTGCGCTACGGCAACCCCTGGGAGAAAGCGCGGCCTGAGTATATGCTTCCC
GTGCACTTCTACGGACGCGTGGAGCACACCCCCGACGGCGTGAAGTGGCTGGACACACAG
GTGGTGCTGGCCATGCCCTACGACACCCCAGTGCCCGGCTACAAGAACAACACCGTCAAC
ACCATGCGGCTGTGGTCCGCCAAGGCTCCCAACGACTTCAAGCTGCAGGACTTCAACGTG
GGAGACTACATCGAGGCGGTCCTGGACCGGAACTTGGCTGAGAACATCTCCAGGGTCCTG
TATCCAAATGATAACTTCTTTGAGGGGAAGGAGCTGCGGCTGAAGCAGGAGTACTTCGTG
GTGGCCGCCACGCTCCAGGACATCATCCGCCGCTTCAAGTCGTCCAAGTTCGGCTGCCGG
GACCCTGTGAGAACCTGTTTCGAGACGTTCCCAGACAAGGTGGCCATCCAGCTGAACGAC
ACCCACCCCGCCCTCTCCATCCCTGAGCTCATGCGGATCCTGGTGGACGTGGAGAAGGTG
GACTGGGACAAGGCCTGGGAAATCACGAAGAAGACCTGTGCATACACCAACCACACTGTG
CTGCCTGAGGCCTTGGAGCGCTGGCCCGTGTCCATGTTTGAGAAGCTGCTGCCGCGGCAC
CTGGAGATAATCTATGCCATCAACCAGCGGCACCTGGACCACGTGGCCGCGCTGTTTCCC
GGCGATGTGGACCGCCTGCGCAGGATGTCTGTGATCGAGGAGGGGGACTGCAAGCGGATC
AACATGGCCCACCTGTGTGTGATTGGGTCCCATGCTGTCAATGGTGTGGCGAGGATCCAC
TCGGAGATCGTGAAACAGTCGGTCTTTAAGGATTTTTATGAACTGGAGCCAGAGAAGTTC
CAGAATAAGACCAATGGCATCACCCCCCGCCGGTGGCTGCTGCTGTGCAACCCGGGGCTG
GCCGATACCATCGTGGAGAAAATTGGGGAGGAGTTCCTGACTGACCTGAGCCAGCTGAAG
AAGCTGCTGCCGCTGGTCAGTGACGAGGTGTTCATCAGGGACGTGGCCAAGGTCAAACAG
GAGAACAAGCTCAAGTTCTCGGCCTTCCTGGAGAAGGAGTACAAGGTGAAGATCAACCCC
TCCTCCATGTTCGATGTGCATGTGAAGAGGATCCACGAGTACAAGCGGCAGCTGCTCAAC
TGCCTGCACGTCGTCACCCTGTACAATCGAATCAAGAGAGACCCGGCCAAGGCTTTTGTG
CCCAGGACTGTTATGATTGGGGGCAAGGCAGCGCCCGGTTACCACATGGCCAAGCTGATC
ATCAAGTTGGTCACCTCCATCGGCGACGTCGTCAATCATGACCCAGTTGTGGGTGACAGG
TTGAAAGTGATCTTCCTGGAGAACTACCGTGTGTCCTTGGCTGAGAAAGTGATCCCGGCC
GCTGATCTGTCGCAGCAGATCTCCACTGCAGGCACCGAGGCCTCAGGCACAGGCAACATG
AAGTTCATGCTCAACGGGGCCCTCACCATCGGCACCATGGACGGCGCCAACGTGGAGATG
GCCGAGGAGGCCGGGGCCGAGAACCTCTTCATCTTCGGCCTGCGGGTGGAGGATGTCGAG
GCCTTGGACCGGAAAGGGTACAATGCCAGGGAGTACTACGACCACCTGCCCGAGCTGAAG
CAGGCCGTGGACCAGATCAGCAGTGGCTTTTTTTCTCCCAAGGAGCCAGACTGCTTCAAG
GACATCGTGAACATGCTGATGCACCATGACAGGTTCAAGGTGTTTGCAGACTATGAAGCC
TACATGCAGTGCCAGGCACAGGTGGACCAGCTGTACCGGAACCCCAAGGAGTGGACCAAG
AAGGTCATCAGGAACATCGCCTGCTCGGGCAAGTTCTCCAGTGACCGGACCATCACGGAG
TATGCACGGGAGATCTGGGGTGTGGAGCCCTCCGACCTGCAGATCCCGCCCCCCAACATC
CCCCGGGACTAG

Enzyme 19 GenBank Gene ID

AL121772

Enzyme 19 GeneCard ID

PYGB

Enzyme 19 GenAtlas ID

PYGB

Enzyme 19 HGNC ID

HGNC:9723

Enzyme 19 Chromosome Location

Enzyme 19 Locus

20p11.2-p11.1

Enzyme 19 SNPs

SNPJam Report Link Image

Enzyme 19 General References

Newgard CB, Littman DR, van Genderen C, Smith M, Fletterick RJ: Human brain glycogen phosphorylase. Cloning, sequence analysis, chromosomal mapping, tissue expression, and comparison with the human liver and muscle isozymes. J Biol Chem. 1988 Mar 15;263(8):3850-7. [PubMed ]
Gelinas RP, Froman BE, McElroy F, Tait RC, Gorin FA: Human brain glycogen phosphorylase: characterization of fetal cDNA and genomic sequences. Brain Res Mol Brain Res. 1989 Nov;6(2-3):177-85. [PubMed ]
Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed ]
Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]

Enzyme 19 Metabolite References

Not Available

Enzyme 20 [top]

Enzyme 20 ID

5676

Enzyme 20 Name

Adenine phosphoribosyltransferase

Enzyme 20 Synonyms

APRT

Enzyme 20 Gene Name

APRT

Enzyme 20 Protein Sequence

>Adenine phosphoribosyltransferase

MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDY
IAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPG
QRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE

Enzyme 20 Number of Residues

180

Enzyme 20 Molecular Weight

19607.5

Enzyme 20 Theoretical pI

5.82

Enzyme 20 GO Classification

Function
adenine phosphoribosyltransferase activity catalytic activity transferase activity transferase activity, transferring glycosyl groups transferase activity, transferring pentosyl groups
Process
adenine salvage cellular aromatic compound metabolic process cellular metabolic process cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside metabolic process purine base biosynthetic process purine base metabolic process purine base salvage
Component
cell part cytoplasm intracellular part

Enzyme 20 General Function

Involved in adenine phosphoribosyltransferase activity

Enzyme 20 Specific Function

Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis

Enzyme 20 Pathways

Purine Metabolism (map00230 )

Enzyme 20 Reactions

AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate [RN:R00190]

Enzyme 20 Pfam Domain Function

Pribosyltran (PF00156 )

Enzyme 20 Signals

None

Enzyme 20 Transmembrane Regions

None

Enzyme 20 Essentiality

Not Available

Enzyme 20 GenBank ID Protein

51476557

Enzyme 20 UniProtKB/Swiss-Prot ID

P07741

Enzyme 20 UniProtKB/Swiss-Prot Entry Name

APT_HUMAN

Enzyme 20 PDB ID

1ORE

Enzyme 20 PDB File

Show

Enzyme 20 3D Structure

Enzyme 20 Cellular Location

Not Available

Enzyme 20 Gene Sequence

>543 bp

ATGGCCGACTCCGAGCTGCAGCTGGTTGAGCAGCGGATCCGCAGCTTCCCCGACTTCCCC
ACCCCAGGCGTGGTATTCAGGGACATCTCGCCCGTCCTGAAGGACCCCGCCTCCTTCCGC
GCCGCCATCGGCCTCCTGGCGCGACACCTGAAGGCGACCCACGGGGGCCGCATCGACTAC
ATCGCAGGCCTAGACTCCCGAGGCTTCCTCTTTGGCCCCTCCCTGGCCCAGGAGCTTGGA
CTGGGCTGCGTGCTCATCCGAAAGCGGGGGAAGCTGCCAGGCCCCACTCTGTGGGCCTCC
TATTCCCTGGAGTACGGGAAGGCTGAGCTGGAGATTCAGAAAGACGCCCTGGAGCCAGGA
CAGAGGGTGGTCGTCGTGGATGATCTGCTGGCCACTGGTGGAACCATGAACGCTGCCTGT
GAGCTGCTGGGCCGCCTGCAGGCTGAGGTCCTGGAGTGCGTGAGCCTGGTGGAGCTGACC
TCGCTTAAGGGCAGGGAGAAGCTGGCACCTGTACCCTTCTTCTCTCTCCTGCAGTATGAG
TGA

Enzyme 20 GenBank Gene ID

CR749423

Enzyme 20 GeneCard ID

APRT

Enzyme 20 GenAtlas ID

APRT

Enzyme 20 HGNC ID

HGNC:626

Enzyme 20 Chromosome Location

Enzyme 20 Locus

16q24

Enzyme 20 SNPs

SNPJam Report Link Image

Enzyme 20 General References

Hidaka Y, Tarle SA, O'Toole TE, Kelley WN, Palella TD: Nucleotide sequence of the human APRT gene. Nucleic Acids Res. 1987 Nov 11;15(21):9086. [PubMed ]
Broderick TP, Schaff DA, Bertino AM, Dush MK, Tischfield JA, Stambrook PJ: Comparative anatomy of the human APRT gene and enzyme: nucleotide sequence divergence and conservation of a nonrandom CpG dinucleotide arrangement. Proc Natl Acad Sci U S A. 1987 May;84(10):3349-53. [PubMed ]
Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Wilson JM, O'Toole TE, Argos P, Shewach DS, Daddona PE, Kelley WN: Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J Biol Chem. 1986 Oct 15;261(29):13677-83. [PubMed ]
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Silva M, Silva CH, Iulek J, Thiemann OH: Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis. Biochemistry. 2004 Jun 22;43(24):7663-71. [PubMed ]
Chen J, Sahota A, Laxdal T, Scrine M, Bowman S, Cui C, Stambrook PJ, Tischfield JA: Identification of a single missense mutation in the adenine phosphoribosyltransferase (APRT) gene from five Icelandic patients and a British patient. Am J Hum Genet. 1991 Dec;49(6):1306-11. [PubMed ]
Sahota A, Chen J, Boyadjiev SA, Gault MH, Tischfield JA: Missense mutation in the adenine phosphoribosyltransferase gene causing 2,8-dihydroxyadenine urolithiasis. Hum Mol Genet. 1994 May;3(5):817-8. [PubMed ]
Hidaka Y, Palella TD, O'Toole TE, Tarle SA, Kelley WN: Human adenine phosphoribosyltransferase. Identification of allelic mutations at the nucleotide level as a cause of complete deficiency of the enzyme. J Clin Invest. 1987 Nov;80(5):1409-15. [PubMed ]
Hidaka Y, Tarle SA, Fujimori S, Kamatani N, Kelley WN, Palella TD: Human adenine phosphoribosyltransferase deficiency. Demonstration of a single mutant allele common to the Japanese. J Clin Invest. 1988 Mar;81(3):945-50. [PubMed ]
Kamatani N, Hakoda M, Otsuka S, Yoshikawa H, Kashiwazaki S: Only three mutations account for almost all defective alleles causing adenine phosphoribosyltransferase deficiency in Japanese patients. J Clin Invest. 1992 Jul;90(1):130-5. [PubMed ]
Deng L, Yang M, Frund S, Wessel T, De Abreu RA, Tischfield JA, Sahota A: 2,8-Dihydroxyadenine urolithiasis in a patient with considerable residual adenine phosphoribosyltransferase activity in cell extracts but with mutations in both copies of APRT. Mol Genet Metab. 2001 Mar;72(3):260-4. [PubMed ]

Enzyme 20 Metabolite References

Not Available

Enzyme 21 [top]

Enzyme 21 ID

5715

Enzyme 21 Name

Hypoxanthine-guanine phosphoribosyltransferase

Enzyme 21 Synonyms

HGPRT
HGPRTase

Enzyme 21 Gene Name

HPRT1

Enzyme 21 Protein Sequence

>Hypoxanthine-guanine phosphoribosyltransferase

MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGH
HIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGD
DLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVG
FEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA

Enzyme 21 Number of Residues

218

Enzyme 21 Molecular Weight

24579.2

Enzyme 21 Theoretical pI

6.67

Enzyme 21 GO Classification

Function
catalytic activity hypoxanthine phosphoribosyltransferase activity transferase activity transferase activity, transferring glycosyl groups transferase activity, transferring pentosyl groups
Process
biosynthetic process cellular biosynthetic process cellular nitrogen compound metabolic process heterocycle biosynthetic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside metabolic process purine ribonucleoside salvage purine salvage
Component
cell part cytoplasm intracellular part

Enzyme 21 General Function

Involved in hypoxanthine phosphoribosyltransferase activity

Enzyme 21 Specific Function

IMP + diphosphate = hypoxanthine + 5-phospho- alpha-D-ribose 1-diphosphate

Enzyme 21 Pathways

Purine Metabolism (map00230 )

Enzyme 21 Reactions

IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate [RN:R01132]

Enzyme 21 Pfam Domain Function

Pribosyltran (PF00156 )

Enzyme 21 Signals

None

Enzyme 21 Transmembrane Regions

None

Enzyme 21 Essentiality

Not Available

Enzyme 21 GenBank ID Protein

306885

Enzyme 21 UniProtKB/Swiss-Prot ID

P00492

Enzyme 21 UniProtKB/Swiss-Prot Entry Name

HPRT_HUMAN Link Image

Enzyme 21 PDB ID

1BZY

Enzyme 21 PDB File

Show

Enzyme 21 3D Structure

Enzyme 21 Cellular Location

Not Available

Enzyme 21 Gene Sequence

>657 bp

ATGGCGACCCGCAGCCCTGGCGTCGTGATTAGTGATGATGAACCAGGTTATGACCTTGAT
TTATTTTGCATACCTAATCATTATGCTGAGGATTTGGAAAGGGTGTTTATTCCTCATGGA
CTAATTATGGACAGGACTGAACGTCTTGCTCGAGATGTGATGAAGGAGATGGGAGGCCAT
CACATTGTAGCCCTCTGTGTGCTCAAGGGGGGCTATAAATTCTTTGCTGACCTGCTGGAT
TACATCAAAGCACTGAATAGAAATAGTGATAGATCCATTCCTATGACTGTAGATTTTATC
AGACTGAAGAGCTATTGTAATGACCAGTCAACAGGGGACATAAAAGTAATTGGTGGAGAT
GATCTCTCAACTTTAACTGGAAAGAATGTCTTGATTGTGGAAGATATAATTGACACTGGC
AAAACAATGCAGACTTTGCTTTCCTTGGTCAGGCAGTATAATCCAAAGATGGTCAAGGTC
GCAAGCTTGCTGGTGAAAAGGACCCCACGAAGTGTTGGATATAAGCCAGACTTTGTTGGA
TTTGAAATTCCAGACAAGTTTGTTGTAGGATATGCCCTTGACTATAATGAATACTTCAGG
GATTTGAATCATGTTTGTGTCATTAGTGAAACTGGAAAAGCAAAATACAAAGCCTAA

Enzyme 21 GenBank Gene ID

M31642

Enzyme 21 GeneCard ID

HPRT1

Enzyme 21 GenAtlas ID

HPRT1

Enzyme 21 HGNC ID

HGNC:5157

Enzyme 21 Chromosome Location

Not Available

Enzyme 21 Locus

Not Available

Enzyme 21 SNPs

SNPJam Report Link Image

Enzyme 21 General References

Jolly DJ, Okayama H, Berg P, Esty AC, Filpula D, Bohlen P, Johnson GG, Shively JE, Hunkapillar T, Friedmann T: Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase. Proc Natl Acad Sci U S A. 1983 Jan;80(2):477-81. [PubMed ]
Edwards A, Voss H, Rice P, Civitello A, Stegemann J, Schwager C, Zimmermann J, Erfle H, Caskey CT, Ansorge W: Automated DNA sequencing of the human HPRT locus. Genomics. 1990 Apr;6(4):593-608. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Wilson JM, Tarr GE, Mahoney WC, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J Biol Chem. 1982 Sep 25;257(18):10978-85. [PubMed ]
Patel PI, Framson PE, Caskey CT, Chinault AC: Fine structure of the human hypoxanthine phosphoribosyltransferase gene. Mol Cell Biol. 1986 Feb;6(2):393-403. [PubMed ]
Eads JC, Scapin G, Xu Y, Grubmeyer C, Sacchettini JC: The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell. 1994 Jul 29;78(2):325-34. [PubMed ]
Shi W, Li CM, Tyler PC, Furneaux RH, Grubmeyer C, Schramm VL, Almo SC: The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor. Nat Struct Biol. 1999 Jun;6(6):588-93. [PubMed ]
Balendiran GK, Molina JA, Xu Y, Torres-Martinez J, Stevens R, Focia PJ, Eakin AE, Sacchettini JC, Craig SP 3rd: Ternary complex structure of human HGPRTase, PRPP, Mg2+, and the inhibitor HPP reveals the involvement of the flexible loop in substrate binding. Protein Sci. 1999 May;8(5):1023-31. [PubMed ]
Sculley DG, Dawson PA, Emmerson BT, Gordon RB: A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Hum Genet. 1992 Nov;90(3):195-207. [PubMed ]
Wilson JM, Kobayashi R, Fox IH, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. J Biol Chem. 1983 May 25;258(10):6458-60. [PubMed ]
Wilson JM, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome. J Clin Invest. 1983 May;71(5):1331-5. [PubMed ]
Wilson JM, Tarr GE, Kelley WN: Human hypoxanthine (guanine) phosphoribosyltransferase: an amino acid substitution in a mutant form of the enzyme isolated from a patient with gout. Proc Natl Acad Sci U S A. 1983 Feb;80(3):870-3. [PubMed ]
Wilson JM, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Structural alteration in a dysfunctional enzyme variant (HPRTMunich) isolated from a patient with gout. J Biol Chem. 1984 Jan 10;259(1):27-30. [PubMed ]
Cariello NF, Scott JK, Kat AG, Thilly WG, Keohavong P: Resolution of a missense mutant in human genomic DNA by denaturing gradient gel electrophoresis and direct sequencing using in vitro DNA amplification: HPRT Munich. Am J Hum Genet. 1988 May;42(5):726-34. [PubMed ]
Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Genetic basis of hypoxanthine guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome (HPRTFlint). Gene. 1988 Mar 31;63(2):331-6. [PubMed ]
Davidson BL, Palella TD, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland). Gene. 1988 Aug 15;68(1):85-91. [PubMed ]
Fujimori S, Hidaka Y, Davidson BL, Palella TD, Kelley WN: Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRT Ann Arbor). Hum Genet. 1988 May;79(1):39-43. [PubMed ]
Davidson BL, Chin SJ, Wilson JM, Kelley WN, Palella TD: Hypoxanthine-guanine phosphoribosyltransferase. Genetic evidence for identical mutations in two partially deficient subjects. J Clin Invest. 1988 Dec;82(6):2164-7. [PubMed ]
Keough DT, Gordon RB, de Jersey J, Emmerson BT: Biochemical basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in nine families. J Inherit Metab Dis. 1988;11(3):229-38. [PubMed ]
Igarashi T, Minami M, Nishida Y: Molecular analysis of hypoxanthine-guanine phosphoribosyltransferase mutations in five unrelated Japanese patients. Acta Paediatr Jpn. 1989 Jun;31(3):303-13. [PubMed ]
Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Human hypoxanthine-guanine phosphoribosyltransferase deficiency. The molecular defect in a patient with gout (HPRTAshville). J Biol Chem. 1989 Jan 5;264(1):520-5. [PubMed ]
Fujimori S, Davidson BL, Kelley WN, Palella TD: Identification of a single nucleotide change in the hypoxanthine-guanine phosphoribosyltransferase gene (HPRTYale) responsible for Lesch-Nyhan syndrome. J Clin Invest. 1989 Jan;83(1):11-3. [PubMed ]
Davidson BL, Tarle SA, Palella TD, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in ten subjects determined by direct sequencing of amplified transcripts. J Clin Invest. 1989 Jul;84(1):342-6. [PubMed ]
Gibbs RA, Nguyen PN, McBride LJ, Koepf SM, Caskey CT: Identification of mutations leading to the Lesch-Nyhan syndrome by automated direct DNA sequencing of in vitro amplified cDNA. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1919-23. [PubMed ]
Gibbs RA, Nguyen PN, Edwards A, Civitello AB, Caskey CT: Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families. Genomics. 1990 Jun;7(2):235-44. [PubMed ]
Skopek TR, Recio L, Simpson D, Dallaire L, Melancon SB, Ogier H, O'Neill JP, Falta MT, Nicklas JA, Albertini RJ: Molecular analyses of a Lesch-Nyhan syndrome mutation (hprtMontreal) by use of T-lymphocyte cultures. Hum Genet. 1990 Jun;85(1):111-6. [PubMed ]
Gordon RB, Sculley DG, Dawson PA, Beacham IR, Emmerson BT: Identification of a single nucleotide substitution in the coding sequence of in vitro amplified cDNA from a patient with partial HPRT deficiency (HPRTBRISBANE). J Inherit Metab Dis. 1990;13(5):692-700. [PubMed ]
Davidson BL, Tarle SA, Van Antwerp M, Gibbs DA, Watts RW, Kelley WN, Palella TD: Identification of 17 independent mutations responsible for human hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Am J Hum Genet. 1991 May;48(5):951-8. [PubMed ]
Tarle SA, Davidson BL, Wu VC, Zidar FJ, Seegmiller JE, Kelley WN, Palella TD: Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects. Genomics. 1991 Jun;10(2):499-501. [PubMed ]
Sculley DG, Dawson PA, Beacham IR, Emmerson BT, Gordon RB: Hypoxanthine-guanine phosphoribosyltransferase deficiency: analysis of HPRT mutations by direct sequencing and allele-specific amplification. Hum Genet. 1991 Oct;87(6):688-92. [PubMed ]
Yamada Y, Goto H, Ogasawara N: Identification of two independent Japanese mutant HPRT genes using the PCR technique. Adv Exp Med Biol. 1991;309B:121-4. [PubMed ]
Lightfoot T, Joshi R, Nuki G, Snyder FF: The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction. Hum Genet. 1992 Mar;88(6):695-6. [PubMed ]
Sege-Peterson K, Chambers J, Page T, Jones OW, Nyhan WL: Characterization of mutations in phenotypic variants of hypoxanthine phosphoribosyltransferase deficiency. Hum Mol Genet. 1992 Sep;1(6):427-32. [PubMed ]
Burgemeister R, Rotzer E, Gutensohn W, Gehrke M, Schiel W: Identification of a new missense mutation in exon 2 of the human hypoxanthine phosphoribosyltransferase gene (HPRTIsar): a further example of clinical heterogeneity in HPRT deficiencies. Hum Mutat. 1995;5(4):341-4. [PubMed ]
Fujimori S, Sakuma R, Yamaoka N, Hakoda M, Yamanaka H, Kamatani N: An asymptomatic germline missense base substitution in the hypoxanthine phosphoribosyltransferase (HPRT) gene that reduces the amount of enzyme in humans. Hum Genet. 1997 Jan;99(1):8-10. [PubMed ]
Liu G, Aral B, Zabot MT, Kamoun P, Ceballos-Picot I: The molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in French families; report of two novel mutations. Hum Mutat. 1998;Suppl 1:S88-90. [PubMed ]

Enzyme 21 Metabolite References

Not Available

Enzyme 22 [top]

Enzyme 22 ID

5756

Enzyme 22 Name

Biotin--protein ligase

Enzyme 22 Synonyms

Biotin apo-protein ligase
Biotin--[methylmalonyl-CoA-carboxytransferase] ligase
Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase
Holocarboxylase synthetase
HCS
Biotin--[methylcrotonoyl-CoA-carboxylase] ligase
Biotin--[acetyl-CoA-carboxylase] ligase

Enzyme 22 Gene Name

HLCS

Enzyme 22 Protein Sequence

>Biotin--protein ligase

MEDRLHMDNGLVPQKIVSVHLQDSTLKEVKDQVSNKQAQILEPKPEPSLEIKPEQDGMEH
VGRDDPKALGEEPKQRRGSASGSEPAGDSDRGGGPVEHYHLHLSSCHECLELENSTIESV
KFASAENIPDLPYDYSSSLESVADETSPEREGRRVNLTGKAPNILLYVGSDSQEALGRFH
EVRSVLADCVDIDSYILYHLLEDSALRDPWTDNCLLLVIATRESIPEDLYQKFMAYLSQG
GKVLGLSSSFTFGGFQVTSKGALHKTVQNLVFSKADQSEVKLSVLSSGCRYQEGPVRLSP
GRLQGHLENEDKDRMIVHVPFGTRGGEAVLCQVHLELPPSSNIVQTPEDFNLLKSSNFRR
YEVLREILTTLGLSCDMKQVPALTPLYLLSAAEEIRDPLMQWLGKHVDSEGEIKSGQLSL
RFVSSYVSEVEITPSCIPVVTNMEAFSSEHFNLEIYRQNLQTKQLGKVILFAEVTPTTMR
LLDGLMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPF
VQHLMSVAVVEAVRSIPEYQDINLRVKWPNDIYYSDLMKIGGVLVNSTLMGETFYILIGC
GFNVTNSNPTICINDLITEYNKQHKAELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVL
PLYYRYWVHSGQQVHLGSAEGPKVSIVGLDDSGFLQVHQEGGEVVTVHPDGNSFDMLRNL
ILPKRR

Enzyme 22 Number of Residues

726

Enzyme 22 Molecular Weight

80759.3

Enzyme 22 Theoretical pI

5.34

Enzyme 22 GO Classification

Function
biotin-[acetyl-CoA-carboxylase] ligase activity biotin-protein ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds
Process
macromolecule metabolic process macromolecule modification metabolic process protein modification process
Component
—

Enzyme 22 General Function

Involved in biotin-[acetyl-CoA-carboxylase] ligase activity

Enzyme 22 Specific Function

Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl- CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase

Enzyme 22 Pathways

Biotin metabolism (map00780 )

Enzyme 22 Reactions

ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)] [RN:R04562]

Enzyme 22 Pfam Domain Function

BPL_C (PF02237 )
BPL_LipA_LipB (PF03099 )

Enzyme 22 Signals

None

Enzyme 22 Transmembrane Regions

None

Enzyme 22 Essentiality

Not Available

Enzyme 22 GenBank ID Protein

Not Available

Enzyme 22 UniProtKB/Swiss-Prot ID

P50747

Enzyme 22 UniProtKB/Swiss-Prot Entry Name

BPL1_HUMAN Link Image

Enzyme 22 PDB ID

Not Available

Enzyme 22 Cellular Location

Not Available

Enzyme 22 Gene Sequence

>2181 bp

ATGGAAGATAGACTCCACATGGATAATGGACTGGTACCCCAAAAGATTGTGTCGGTGCAC
TTGCAGGACTCCACTCTGAAGGAAGTTAAGGATCAGGTCTCAAACAAGCAAGCCCAGATC
CTAGAGCCGAAGCCTGAACCTTCTCTTGAGATTAAGCCTGAGCAGGACGGTATGGAGCAT
GTTGGCAGAGATGACCCAAAGGCTCTTGGTGAAGAACCCAAACAAAGGAGAGGCAGTGCC
TCTGGGAGTGAGCCTGCTGGGGACAGTGACAGGGGAGGGGGCCCCGTTGAGCATTATCAC
CTCCATCTGTCTAGTTGCCACGAGTGTCTGGAACTTGAGAACAGCACCATTGAGTCAGTC
AAGTTTGCGTCTGCCGAGAACATTCCAGACCTTCCCTACGATTATAGCAGCAGTTTGGAG
AGTGTTGCTGATGAGACCTCCCCCGAAAGAGAAGGGAGGAGAGTCAACCTCACGGGAAAG
GCACCCAACATCCTCCTCTATGTGGGCTCCGACTCCCAGGAAGCCCTCGGCCGGTTCCAC
GAGGTCCGGTCTGTGCTGGCCGACTGTGTGGACATTGACAGTTATATTCTCTACCACCTG
CTGGAGGACAGTGCTCTCAGAGACCCGTGGACGGACAACTGTCTGCTGTTGGTCATTGCT
ACCAGGGAGTCCATTCCCGAAGACCTGTACCAGAAGTTCATGGCCTATCTTTCTCAGGGA
GGGAAGGTGTTGGGCCTGTCTTCATCCTTCACCTTTGGTGGCTTTCAGGTGACAAGCAAG
GGTGCACTGCACAAGACAGTCCAGAACTTGGTTTTCTCCAAGGCTGACCAGAGCGAGGTG
AAGCTCAGCGTCTTGAGCAGTGGCTGCAGGTACCAGGAAGGCCCCGTCCGGCTCAGCCCC
GGCAGGCTCCAGGGCCACCTGGAGAATGAGGACAAGGACAGGATGATTGTGCATGTGCCT
TTTGGAACTCGCGGGGGAGAAGCTGTTCTTTGCCAGGTGCACTTAGAACTACCTCCCAGC
TCCAACATAGTGCAAACTCCAGAAGATTTTAACTTGCTCAAGTCAAGCAATTTTAGAAGA
TACGAAGTCCTTAGAGAGATTCTGACAACCCTTGGCCTCAGCTGTGACATGAAACAAGTT
CCTGCCTTAACTCCTCTTTACTTGCTGTCAGCTGCGGAGGAAATCAGGGATCCTCTTATG
CAGTGGCTTGGGAAACATGTGGACTCCGAGGGAGAAATAAAATCCGGCCAGCTCTCTCTT
AGATTTGTTTCATCCTACGTGTCTGAAGTAGAAATAACCCCATCTTGTATACCTGTGGTG
ACCAACATGGAGGCCTTCTCATCAGAACATTTCAACTTAGAGATCTATCGCCAAAATCTG
CAGACCAAGCAGTTGGGGAAAGTAATTTTGTTTGCCGAAGTGACCCCCACAACGATGCGT
CTCCTGGATGGGCTGATGTTTCAGACACCGCAGGAAATGGGCTTAATAGTGATCGCGGCC
CGGCAGACCGAGGGCAAAGGACGGGGAGGGAATGTGTGGCTGAGCCCTGTGGGATGTGCT
CTTTCTACTCTGCTCATCTCCATTCCACTGAGATCCCAGCTGGGACAGAGGATCCCGTTT
GTCCAGCATCTGATGTCCGTGGCTGTCGTGGAAGCAGTGAGGTCCATTCCCGAGTATCAG
GATATCAACTTACGAGTGAAGTGGCCCAACGATATTTATTACAGTGACCTCATGAAGATC
GGCGGAGTTCTGGTTAACTCAACACTCATGGGAGAAACATTTTATATACTTATTGGCTGT
GGATTTAATGTGACTAACAGTAACCCTACCATCTGCATCAACGACCTCATCACAGAATAC
AATAAACAACACAAGGCAGAACTGAAGCCCTTAAGAGCCGATTATCTCATCGCCAGAGTC
GTGACTGTGCTGGAGAAACTGATCAAAGAGTTTCAGGACAAAGGGCCCAACAGCGTCCTT
CCCCTTTATTACCGATACTGGGTCCACAGTGGTCAGCAAGTCCATCTGGGCAGCGCAGAG
GGACCAAAGGTGTCCATCGTTGGCCTGGACGATTCTGGCTTCCTCCAGGTTCACCAGGAG
GGCGGCGAGGTTGTGACTGTGCACCCGGACGGCAACTCCTTCGACATGCTGAGAAACCTC
ATCCTCCCCAAACGGCGGTAA

Enzyme 22 GenBank Gene ID

D23672

Enzyme 22 GeneCard ID

HLCS

Enzyme 22 GenAtlas ID

HLCS

Enzyme 22 HGNC ID

HGNC:4976

Enzyme 22 Chromosome Location

Enzyme 22 Locus

21q22.1|21q22.13

Enzyme 22 SNPs

SNPJam Report Link Image

Enzyme 22 General References

Suzuki Y, Aoki Y, Ishida Y, Chiba Y, Iwamatsu A, Kishino T, Niikawa N, Matsubara Y, Narisawa K: Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA. Nat Genet. 1994 Oct;8(2):122-8. [PubMed ]
Yang X, Aoki Y, Li X, Sakamoto O, Hiratsuka M, Kure S, Taheri S, Christensen E, Inui K, Kubota M, Ohira M, Ohki M, Kudoh J, Kawasaki K, Shibuya K, Shintani A, Asakawa S, Minoshima S, Shimizu N, Narisawa K, Matsubara Y, Suzuki Y: Structure of human holocarboxylase synthetase gene and mutation spectrum of holocarboxylase synthetase deficiency. Hum Genet. 2001 Nov;109(5):526-34. Epub 2001 Oct 5. [PubMed ]
Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Dahmane N, Ghezala GA, Gosset P, Chamoun Z, Dufresne-Zacharia MC, Lopes C, Rabatel N, Gassanova-Maugenre S, Chettouh Z, Abramowski V, Fayet E, Yaspo ML, Korn B, Blouin JL, Lehrach H, Poutska A, Antonarakis SE, Sinet PM, Creau N, Delabar JM: Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21 involved in Down syndrome. Genomics. 1998 Feb 15;48(1):12-23. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Aoki Y, Suzuki Y, Sakamoto O, Li X, Takahashi K, Ohtake A, Sakuta R, Ohura T, Miyabayashi S, Narisawa K: Molecular analysis of holocarboxylase synthetase deficiency: a missense mutation and a single base deletion are predominant in Japanese patients. Biochim Biophys Acta. 1995 Dec 12;1272(3):168-74. [PubMed ]
Dupuis L, Leon-Del-Rio A, Leclerc D, Campeau E, Sweetman L, Saudubray JM, Herman G, Gibson KM, Gravel RA: Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency. Hum Mol Genet. 1996 Jul;5(7):1011-6. [PubMed ]
Aoki Y, Suzuki Y, Li X, Sakamoto O, Chikaoka H, Takita S, Narisawa K: Characterization of mutant holocarboxylase synthetase (HCS): a Km for biotin was not elevated in a patient with HCS deficiency. Pediatr Res. 1997 Dec;42(6):849-54. [PubMed ]
Aoki Y, Li X, Sakamoto O, Hiratsuka M, Akaishi H, Xu L, Briones P, Suormala T, Baumgartner ER, Suzuki Y, Narisawa K: Identification and characterization of mutations in patients with holocarboxylase synthetase deficiency. Hum Genet. 1999 Feb;104(2):143-8. [PubMed ]
Sakamoto O, Suzuki Y, Li X, Aoki Y, Hiratsuka M, Suormala T, Baumgartner ER, Gibson KM, Narisawa K: Relationship between kinetic properties of mutant enzyme and biochemical and clinical responsiveness to biotin in holocarboxylase synthetase deficiency. Pediatr Res. 1999 Dec;46(6):671-6. [PubMed ]
Morrone A, Malvagia S, Donati MA, Funghini S, Ciani F, Pela I, Boneh A, Peters H, Pasquini E, Zammarchi E: Clinical findings and biochemical and molecular analysis of four patients with holocarboxylase synthetase deficiency. Am J Med Genet. 2002 Jul 22;111(1):10-8. [PubMed ]
Tang NL, Hui J, Yong CK, Wong LT, Applegarth DA, Vallance HD, Law LK, Fung SL, Mak TW, Sung YM, Cheung KL, Fok TF: A genomic approach to mutation analysis of holocarboxylase synthetase gene in three Chinese patients with late-onset holocarboxylase synthetase deficiency. Clin Biochem. 2003 Mar;36(2):145-9. [PubMed ]
Suzuki Y, Yang X, Aoki Y, Kure S, Matsubara Y: Mutations in the holocarboxylase synthetase gene HLCS. Hum Mutat. 2005 Oct;26(4):285-90. [PubMed ]
Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
Bailey LM, Ivanov RA, Jitrapakdee S, Wilson CJ, Wallace JC, Polyak SW: Reduced half-life of holocarboxylase synthetase from patients with severe multiple carboxylase deficiency. Hum Mutat. 2008 Jun;29(6):E47-57. [PubMed ]

Enzyme 22 Metabolite References

Not Available

Enzyme 23 [top]

Enzyme 23 ID

5770

Enzyme 23 Name

Phenylalanyl-tRNA synthetase beta chain

Enzyme 23 Synonyms

Phenylalanine--tRNA ligase beta chain
PheRS

Enzyme 23 Gene Name

FARSB

Enzyme 23 Protein Sequence

>Phenylalanyl-tRNA synthetase beta chain

MPTVSVKRDLLFQALGRTYTDEEFDELCFEFGLELDEITSEKEIISKEQGNVKAAGASDV
VLYKIDVPANRYDLLCLEGLVRGLQVFKERIKAPVYKRVMPDGKIQKLIITEETAKIRPF
AVAAVLRNIKFTKDRYDSFIELQEKLHQNICRKRALVAIGTHDLDTLSGPFTYTAKRPSD
IKFKPLNKTKEYTACELMNIYKTDNHLKHYLHIIENKPLYPVIYDSNGVVLSMPPIINGD
HSRITVNTRNIFIECTGTDFTKAKIVLDIIVTMFSEYCENQFTVEAAEVVFPNGKSHTFP
ELAYRKEMVRADLINKKVGIRETPENLAKLLTRMYLKSEVIGDGNQIEIEIPPTRADIIH
ACDIVEDAAIAYGYNNIQMTLPKTYTIANQFPLNKLTELLRHDMAAAGFTEALTFALCSQ
EDIADKLGVDISATKAVHISNPKTAEFQVARTTLLPGLLKTIAANRKMPLPLKLFEISDI
VIKDSNTDVGAKNYRHLCAVYYNKNPGFEIIHGLLDRIMQLLDVPPGEDKGGYVIKASEG
PAFFPGRCAEIFARGQSVGKLGVLHPDVITKFELTMPCSSLEINVGPFL

Enzyme 23 Number of Residues

589

Enzyme 23 Molecular Weight

66114.9

Enzyme 23 Theoretical pI

6.83

Enzyme 23 GO Classification

Function
ATP binding RNA binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity cation binding ion binding ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds magnesium ion binding metal ion binding nucleic acid binding nucleoside binding nucleotide binding phenylalanine-tRNA ligase activity purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process phenylalanyl-tRNA aminoacylation tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 23 General Function

Involved in RNA binding

Enzyme 23 Specific Function

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)

Enzyme 23 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Phenylalanine and Tyrosine Metabolism (map00400 )

Enzyme 23 Reactions

ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe [RN:R03660]

Enzyme 23 Pfam Domain Function

B3_4 (PF03483 )
B5 (PF03484 )

Enzyme 23 Signals

None

Enzyme 23 Transmembrane Regions

None

Enzyme 23 Essentiality

Not Available

Enzyme 23 GenBank ID Protein

124028525

Enzyme 23 UniProtKB/Swiss-Prot ID

Q9NSD9

Enzyme 23 UniProtKB/Swiss-Prot Entry Name

SYFB_HUMAN Link Image

Enzyme 23 PDB ID

Not Available

Enzyme 23 Cellular Location

Not Available

Enzyme 23 Gene Sequence

>1770 bp

ATGCCGACTGTCAGCGTGAAGCGTGATCTGCTCTTCCAAGCCCTGGGCCGCACCTACACT
GACGAAGAATTTGATGAACTATGTTTTGAATTTGGTCTGGAGCTTGATGAAATTACATCT
GAGAAGGAAATAATAAGTAAAGAACAAGGTAATGTAAAGGCAGCAGGAGCCTCTGATGTT
GTTCTTTACAAAATTGACGTCCCTGCCAATAGATATGATCTCCTGTGTCTGGAAGGATTG
GTTCGAGGACTTCAGGTCTTCAAAGAAAGGATAAAGGCTCCAGTGTATAAACGGGTAATG
CCTGATGGAAAAATCCAGAAATTGATTATCACAGAAGAGACAGCTAAGATACGTCCTTTT
GCGGTAGCAGCAGTTCTCCGTAATATAAAGTTTACTAAAGATCGATATGACAGCTTCATT
GAACTTCAGGAGAAATTACATCAGAATATTTGCAGGAAAAGAGCACTGGTTGCCATTGGT
ACCCATGATTTGGACACTTTGTCGGGCCCATTTACTTATACTGCAAAGCGTCCTTCAGAT
ATCAAATTCAAGCCTCTAAATAAGACCAAGGAGTATACAGCCTGTGAACTGATGAACATA
TACAAGACTGACAATCACCTGAAACATTATTTACATATCATTGAAAACAAACCCCTGTAT
CCAGTTATCTATGATAGCAATGGTGTCGTCCTTTCAATGCCTCCCATCATCAATGGGGAT
CATTCCAGAATAACAGTAAATACTAGAAATATTTTTATTGAATGCACGGGAACTGACTTT
ACTAAGGCAAAAATAGTTCTTGATATTATTGTCACCATGTTCAGTGAATATTGTGAGAAT
CAATTTACGGTCGAAGCTGCTGAAGTGGTTTTTCCTAATGGAAAATCACATACCTTTCCA
GAATTAGCTTACCGAAAGGAGATGGTGAGAGCTGACCTAATTAACAAAAAAGTTGGAATC
AGAGAAACTCCAGAAAATCTTGCCAAACTTCTGACCAGGATGTATTTAAAATCAGAAGTC
ATAGGTGATGGGAATCAGATTGAGATTGAAATCCCTCCAACCAGAGCTGACATTATCCAT
GCATGTGATATTGTAGAAGATGCAGCTATTGCTTATGGATATAACAACATTCAGATGACT
CTCCCGAAAACTTACACCATAGCTAATCAATTTCCTCTTAATAAGCTCACTGAACTTCTC
CGACATGACATGGCAGCCGCTGGCTTCACTGAAGCACTTACCTTTGCCCTGTGCTCCCAA
GAAGATATTGCTGATAAACTAGGTGTGGATATCTCTGCAACAAAGGCAGTCCACATAAGT
AATCCTAAAACAGCTGAATTTCAGGTGGCACGCACTACCCTTCTTCCTGGCCTCCTGAAG
ACCATAGCAGCAAATCGTAAGATGCCCCTTCCACTGAAACTGTTTGAAATCTCTGACATT
GTAATAAAAGATTCTAATACAGATGTAGGTGCAAAAAACTACAGACATCTCTGTGCTGTT
TATTACAACAAGAATCCTGGGTTTGAGATCATTCATGGGCTGCTGGACAGAATTATGCAG
TTGCTCGATGTGCCTCCTGGTGAAGACAAGGGGGGATATGTGATCAAAGCATCAGAAGGG
CCTGCTTTCTTCCCCGGGCGATGTGCAGAGATCTTTGCCAGGGGTCAAAGCGTCGGGAAG
CTTGGGGTCCTTCATCCTGACGTTATCACCAAATTTGAGCTGACCATGCCCTGCTCCTCC
CTAGAAATCAATGTTGGACCCTTTTTGTGA

Enzyme 23 GenBank Gene ID

NM_005687.3 Link Image

Enzyme 23 GeneCard ID

FARSB

Enzyme 23 GenAtlas ID

FARSB

Enzyme 23 HGNC ID

HGNC:17800 Link Image

Enzyme 23 Chromosome Location

Enzyme 23 Locus

2q36.1

Enzyme 23 SNPs

SNPJam Report Link Image

Enzyme 23 General References

Rodova M, Ankilova V, Safro MG: Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells. Biochem Biophys Res Commun. 1999 Feb 24;255(3):765-73. [PubMed ]
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]
Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 23 Metabolite References

Not Available

Enzyme 24 [top]

Enzyme 24 ID

5832

Enzyme 24 Name

Ubiquitin-conjugating enzyme E2 A

Enzyme 24 Synonyms

RAD6 homolog A
HR6A
hHR6A
Ubiquitin carrier protein A
Ubiquitin-protein ligase A

Enzyme 24 Gene Name

UBE2A

Enzyme 24 Protein Sequence

>Ubiquitin-conjugating enzyme E2 A

MSTPARRRLMRDFKRLQEDPPAGVSGAPSENNIMVWNAVIFGPEGTPFEDGTFKLTIEFT
EEYPNKPPTVRFVSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNS
PANSQAAQLYQENKREYEKRVSAIVEQSWRDC

Enzyme 24 Number of Residues

152

Enzyme 24 Molecular Weight

17315.3

Enzyme 24 Theoretical pI

4.79

Enzyme 24 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 24 General Function

Involved in acid-amino acid ligase activity

Enzyme 24 Specific Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11', as well as 'Lys-48'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA

Enzyme 24 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 24 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 24 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 24 Signals

None

Enzyme 24 Transmembrane Regions

None

Enzyme 24 Essentiality

Not Available

Enzyme 24 GenBank ID Protein

32967280

Enzyme 24 UniProtKB/Swiss-Prot ID

P49459

Enzyme 24 UniProtKB/Swiss-Prot Entry Name

UBE2A_HUMAN Link Image

Enzyme 24 PDB ID

1JAS

Enzyme 24 PDB File

Show

Enzyme 24 3D Structure

Enzyme 24 Cellular Location

Not Available

Enzyme 24 Gene Sequence

>459 bp

ATGTCCACCCCGGCTCGGCGGCGCCTCATGCGGGACTTCAAGAGGTTGCAGGAGGATCCT
CCAGCCGGAGTCAGCGGGGCTCCGTCCGAGAACAACATAATGGTGTGGAACGCGGTCATT
TTCGGGCCTGAAGGGACCCCGTTTGAGGATGGAACATTTAAACTTACAATAGAATTCACT
GAAGAATATCCAAATAAACCACCTACAGTTAGATTTGTCTCTAAGATGTTCCATCCAAAT
GTCTATGCAGATGGTAGTATATGTCTGGACATACTTCAGAACCGTTGGAGTCCAACCTAT
GATGTGTCTTCCATTCTAACATCCATACAGTCTCTGTTGGATGAACCCAATCCCAATAGT
CCAGCAAACAGCCAGGCTGCTCAGCTGTACCAGGAGAACAAACGGGAATATGAAAAGCGT
GTTTCTGCAATAGTAGAACAAAGCTGGCGTGATTGTTGA

Enzyme 24 GenBank Gene ID

NM_003336.2 Link Image

Enzyme 24 GeneCard ID

UBE2A

Enzyme 24 GenAtlas ID

UBE2A

Enzyme 24 HGNC ID

HGNC:12472 Link Image

Enzyme 24 Chromosome Location

Not Available

Enzyme 24 Locus

Not Available

Enzyme 24 SNPs

SNPJam Report Link Image

Enzyme 24 General References

Koken MH, Reynolds P, Jaspers-Dekker I, Prakash L, Prakash S, Bootsma D, Hoeijmakers JH: Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6. Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):8865-9. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]

Enzyme 24 Metabolite References

Not Available

Enzyme 25 [top]

Enzyme 25 ID

5833

Enzyme 25 Name

Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma

Enzyme 25 Synonyms

GMP-PDE gamma

Enzyme 25 Gene Name

PDE6H

Enzyme 25 Protein Sequence

>Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma

MSDNTTLPAPASNQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDI
TVICPWEAFSHLELHELAQFGII

Enzyme 25 Number of Residues

Enzyme 25 Molecular Weight

9074.4

Enzyme 25 Theoretical pI

9.98

Enzyme 25 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity GMP binding binding cGMP binding catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds nucleoside binding phosphoric diester hydrolase activity phosphoric ester hydrolase activity purine nucleoside binding
Process
multicellular organismal process neurological system process sensory perception sensory perception of light stimulus system process visual perception
Component
—

Enzyme 25 General Function

Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity

Enzyme 25 Specific Function

Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones

Enzyme 25 Pathways

Purine Metabolism (map00230 )

Enzyme 25 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 25 Pfam Domain Function

PDE6_gamma (PF04868 )

Enzyme 25 Signals

None

Enzyme 25 Transmembrane Regions

None

Enzyme 25 Essentiality

Not Available

Enzyme 25 GenBank ID Protein

Not Available

Enzyme 25 UniProtKB/Swiss-Prot ID

Q13956

Enzyme 25 UniProtKB/Swiss-Prot Entry Name

CNCG_HUMAN Link Image

Enzyme 25 PDB ID

1FQJ

Enzyme 25 PDB File

Show

Enzyme 25 3D Structure

Enzyme 25 Cellular Location

Not Available

Enzyme 25 Gene Sequence

>252 bp

ATGAGTGACAACACTACTCTGCCTGCTCCAGCTTCAAACCAGGGTCCTACCACCCCACGC
AAAGGCCCTCCCAAGTTCAAGCAGAGGCAGACTCGCCAATTCAAGAGTAAACCTCCAAAG
AAAGGTGTGAAAGGATTTGGAGATGACATTCCAGGAATGGAGGGGCTAGGAACAGATATC
ACAGTGATTTGTCCATGGGAGGCATTCAGCCACCTGGAATTGCATGAGCTCGCTCAGTTT
GGGATTATCTGA

Enzyme 25 GenBank Gene ID

D45399

Enzyme 25 GeneCard ID

PDE6H

Enzyme 25 GenAtlas ID

PDE6H

Enzyme 25 HGNC ID

HGNC:8790

Enzyme 25 Chromosome Location

Enzyme 25 Locus

12p13

Enzyme 25 SNPs

SNPJam Report Link Image

Enzyme 25 General References

Shimizu-Matsumoto A, Itoh K, Inazawa J, Nishida K, Matsumoto Y, Kinoshita S, Matsubara K, Okubo K: Isolation and chromosomal localization of the human cone cGMP phosphodiesterase gamma cDNA (PDE6H). Genomics. 1996 Feb 15;32(1):121-4. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Piri N, Gao YQ, Danciger M, Mendoza E, Fishman GA, Farber DB: A substitution of G to C in the cone cGMP-phosphodiesterase gamma subunit gene found in a distinctive form of cone dystrophy. Ophthalmology. 2005 Jan;112(1):159-66. [PubMed ]

Enzyme 25 Metabolite References

Not Available

Enzyme 26 [top]

Enzyme 26 ID

5834

Enzyme 26 Name

Adenylate kinase isoenzyme 1

Enzyme 26 Synonyms

AK 1
ATP-AMP transphosphorylase 1
Myokinase

Enzyme 26 Gene Name

AK1

Enzyme 26 Protein Sequence

>Adenylate kinase isoenzyme 1

MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRSEVSSGSARGKKLSEI
MEKGQLVPLETVLDMLRDAMVAKVNTSKGFLIDGYPREVQQGEEFERRIGQPTLLLYVDA
GPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVD
SVFSQVCTHLDALK

Enzyme 26 Number of Residues

194

Enzyme 26 Molecular Weight

21634.7

Enzyme 26 Theoretical pI

8.99

Enzyme 26 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding adenylate kinase activity binding catalytic activity kinase activity nucleobase, nucleoside, nucleotide kinase activity nucleoside binding phosphotransferase activity, phosphate group as acceptor purine nucleoside binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
ATP metabolic process cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside phosphate metabolic process nucleotide metabolic process purine nucleoside triphosphate metabolic process purine nucleotide metabolic process purine ribonucleoside triphosphate metabolic process
Component
cell part cytoplasm intracellular part

Enzyme 26 General Function

Involved in ATP binding

Enzyme 26 Specific Function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth

Enzyme 26 Pathways

Purine Metabolism (map00230 )

Enzyme 26 Reactions

ATP + AMP = 2 ADP [RN:R00127]

Enzyme 26 Pfam Domain Function

ADK (PF00406 )

Enzyme 26 Signals

None

Enzyme 26 Transmembrane Regions

None

Enzyme 26 Essentiality

Not Available

Enzyme 26 GenBank ID Protein

Not Available

Enzyme 26 UniProtKB/Swiss-Prot ID

P00568

Enzyme 26 UniProtKB/Swiss-Prot Entry Name

KAD1_HUMAN Link Image

Enzyme 26 PDB ID

1Z83

Enzyme 26 PDB File

Show

Enzyme 26 3D Structure

Enzyme 26 Cellular Location

Not Available

Enzyme 26 Gene Sequence

>585 bp

ATGGAAGAGAAGCTGAAGAAAACCAAGATCATCTTTGTGGTGGGTGGGCCTGGCTCAGGG
AAGGGCACCCAGTGTGAGAAGATCGTGCAGAAGTATGGCTACACCCACCTCTCCACCGGG
GACCTCCTGCGGTCCGAGGTCAGCTCAGGCTCGGCCAGGGGCAAGAAGCTGTCGGAAATC
ATGGAGAAGGGGCAGCTGGTTCCACTGGAGACAGTGTTGGACATGCTCCGGGATGCCATG
GTGGCCAAAGTCAATACTTCCAAAGGCTTCCTGATTGATGGCTACCCGCGGGAGGTGCAG
CAAGGAGAAGAGTTTGAGCGACGGATTGGACAGCCCACACTGCTGCTGTATGTGGACGCA
GGCCCTGAGACCATGACCCAGCGGCTCTTGAAACGTGGAGAGACCAGCGGGCGTGTGGAC
GACAATGAGGAGACCATCAAAAAGCGGCTGGAGACCTATTACAAGGCCACAGAACCCGTC
ATCGCCTTCTATGAGAAACGTGGCATTGTGCGCAAGGTCAACGCTGAGGGCTCCGTGGAC
AGTGTCTTCTCCCAGGTCTGCACCCACCTGGACGCCCTAAAGTAG

Enzyme 26 GenBank Gene ID

AB021871

Enzyme 26 GeneCard ID

AK1

Enzyme 26 GenAtlas ID

AK1

Enzyme 26 HGNC ID

HGNC:361

Enzyme 26 Chromosome Location

Enzyme 26 Locus

9q34.1

Enzyme 26 SNPs

SNPJam Report Link Image

Enzyme 26 General References

Von Zabern I, Wittmann-Liebold B, Untucht-Grau R, Schirmer RH, Pai EF: Primary and tertiary structure of the principal human adenylate kinase. Eur J Biochem. 1976 Sep;68(1):281-90. [PubMed ]
Matsuura S, Igarashi M, Tanizawa Y, Yamada M, Kishi F, Kajii T, Fujii H, Miwa S, Sakurai M, Nakazawa A: Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase. J Biol Chem. 1989 Jun 15;264(17):10148-55. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Qualtieri A, Pedace V, Bisconte MG, Bria M, Gulino B, Andreoli V, Brancati C: Severe erythrocyte adenylate kinase deficiency due to homozygous A-->G substitution at codon 164 of human AK1 gene associated with chronic haemolytic anaemia. Br J Haematol. 1997 Dec;99(4):770-6. [PubMed ]
Corrons JL, Garcia E, Tusell JJ, Varughese KI, West C, Beutler E: Red cell adenylate kinase deficiency: molecular study of 3 new mutations (118G>A, 190G>A, and GAC deletion) associated with hereditary nonspherocytic hemolytic anemia. Blood. 2003 Jul 1;102(1):353-6. Epub 2003 Mar 20. [PubMed ]

Enzyme 26 Metabolite References

Not Available

Enzyme 27 [top]

Enzyme 27 ID

5835

Enzyme 27 Name

NEDD8-conjugating enzyme Ubc12

Enzyme 27 Synonyms

NEDD8 carrier protein
NEDD8 protein ligase
Ubiquitin-conjugating enzyme E2 M

Enzyme 27 Gene Name

UBE2M

Enzyme 27 Protein Sequence

>NEDD8-conjugating enzyme Ubc12

MIKLFSLKQQKKEEESAGGTKGSSKKASAAQLRIQKDINELNLPKTCDISFSDPDDLLNF
KLVICPDEGFYKSGKFVFSFKVGQGYPHDPPKVKCETMVYHPNIDLEGNVCLNILREDWK
PVLTINSIIYGLQYLFLEPNPEDPLNKEAAEVLQNNRRLFEQNVQRSMRGGYIGSTYFER
CLK

Enzyme 27 Number of Residues

183

Enzyme 27 Molecular Weight

20899.8

Enzyme 27 Theoretical pI

7.84

Enzyme 27 GO Classification

Function
ATP binding acid-amino acid ligase activity adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds nucleoside binding purine nucleoside binding small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 27 General Function

Involved in ATP binding

Enzyme 27 Specific Function

Accepts the ubiquitin-like protein NEDD8 from the UBA3- NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation

Enzyme 27 Pathways

Not Available

Enzyme 27 Reactions

Not Available

Enzyme 27 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 27 Signals

None

Enzyme 27 Transmembrane Regions

None

Enzyme 27 Essentiality

Not Available

Enzyme 27 GenBank ID Protein

3599674

Enzyme 27 UniProtKB/Swiss-Prot ID

P61081

Enzyme 27 UniProtKB/Swiss-Prot Entry Name

UBC12_HUMAN Link Image

Enzyme 27 PDB ID

1Y8X

Enzyme 27 PDB File

Show

Enzyme 27 3D Structure

Enzyme 27 Cellular Location

Not Available

Enzyme 27 Gene Sequence

>552 bp

ATGATCAAGCTGTTCTCGCTGAAGCAGCAGAAGAAGGAGGAGGAGTCGGCGGGCGGCACC
AAGGGCAGCAGCAAGAAGGCGTCGGCGGCGCAGCTGCGGATCCAGAAGGACATAAACGAG
CTGAACCTGCCCAAGACGTGTGATATCAGCTTCTCAGATCCAGACGACCTCCTCAACTTC
AAGCTGGTCATCTGTCCTGATGAGGGCTTCTACAAGAGTGGGAAGTTTGTGTTCAGTTTT
AAGGTGGGCCAGGGTTACCCGCATGATCCCCCCAAGGTGAAGTGTGAGACAATGGTCTAT
CACCCCAACATTGACCTCGAGGGCAACGTCTGCCTCAACATCCTCAGAGAGGACTGGAAG
CCAGTCCTTACGATAAACTCCATAATTTATGGCCTGCAGTATCTCTTCTTGGAGCCCAAC
CCCGAGGACCCACTGAACAAGGAGGCCGCAGAGGTCCTGCAGAACAACCGGCGGCTGTTT
GAGCAGAACGTGCAGCGCTCCATGCGGGGTGGCTACATCGGCTCCACCTACTTTGAGCGC
TGCCTGAAATAG

Enzyme 27 GenBank Gene ID

AB012191

Enzyme 27 GeneCard ID

UBE2M

Enzyme 27 GenAtlas ID

UBE2M

Enzyme 27 HGNC ID

HGNC:12491 Link Image

Enzyme 27 Chromosome Location

Enzyme 27 Locus

19q13.43

Enzyme 27 SNPs

SNPJam Report Link Image

Enzyme 27 General References

Osaka F, Kawasaki H, Aida N, Saeki M, Chiba T, Kawashima S, Tanaka K, Kato S: A new NEDD8-ligating system for cullin-4A. Genes Dev. 1998 Aug 1;12(15):2263-8. [PubMed ]
Gong L, Yeh ET: Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway. J Biol Chem. 1999 Apr 23;274(17):12036-42. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Wada H, Yeh ET, Kamitani T: A dominant-negative UBC12 mutant sequesters NEDD8 and inhibits NEDD8 conjugation in vivo. J Biol Chem. 2000 Jun 2;275(22):17008-15. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Huang DT, Ayrault O, Hunt HW, Taherbhoy AM, Duda DM, Scott DC, Borg LA, Neale G, Murray PJ, Roussel MF, Schulman BA: E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification. Mol Cell. 2009 Feb 27;33(4):483-95. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Huang DT, Miller DW, Mathew R, Cassell R, Holton JM, Roussel MF, Schulman BA: A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8. Nat Struct Mol Biol. 2004 Oct;11(10):927-35. Epub 2004 Sep 7. [PubMed ]
Huang DT, Paydar A, Zhuang M, Waddell MB, Holton JM, Schulman BA: Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1. Mol Cell. 2005 Feb 4;17(3):341-50. [PubMed ]

Enzyme 27 Metabolite References

Not Available

Enzyme 28 [top]

Enzyme 28 ID

5836

Enzyme 28 Name

Ubiquitin/ISG15-conjugating enzyme E2 L6

Enzyme 28 Synonyms

Retinoic acid-induced gene B protein
RIG-B
UbcH8
Ubiquitin carrier protein L6
Ubiquitin-protein ligase L6

Enzyme 28 Gene Name

UBE2L6

Enzyme 28 Protein Sequence

>Ubiquitin/ISG15-conjugating enzyme E2 L6

MMASMRVVKELEDLQKKPPPYLRNLSSDDANVLVWHALLLPDQPPYHLKAFNLRISFPPE
YPFKPPMIKFTTKIYHPNVDENGQICLPIISSENWKPCTKTCQVLEALNVLVNRPNIREP
LRMDLADLLTQNPELFRKNAEEFTLRFGVDRPS

Enzyme 28 Number of Residues

153

Enzyme 28 Molecular Weight

17768.5

Enzyme 28 Theoretical pI

8.06

Enzyme 28 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 28 General Function

Involved in acid-amino acid ligase activity

Enzyme 28 Specific Function

Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53

Enzyme 28 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 28 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 28 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 28 Signals

None

Enzyme 28 Transmembrane Regions

None

Enzyme 28 Essentiality

Not Available

Enzyme 28 GenBank ID Protein

4759282

Enzyme 28 UniProtKB/Swiss-Prot ID

O14933

Enzyme 28 UniProtKB/Swiss-Prot Entry Name

UB2L6_HUMAN Link Image

Enzyme 28 PDB ID

1WZW

Enzyme 28 PDB File

Show

Enzyme 28 3D Structure

Enzyme 28 Cellular Location

Not Available

Enzyme 28 Gene Sequence

>462 bp

ATGATGGCGAGCATGCGAGTGGTGAAGGAGCTGGAGGATCTTCAGAAGAAGCCTCCCCCA
TACCTGCGGAACCTGTCCAGCGATGATGCCAATGTCCTGGTGTGGCACGCTCTCCTCCTA
CCCGACCAACCTCCCTACCACCTGAAAGCCTTCAACCTGCGCATCAGCTTCCCGCCGGAG
TATCCGTTCAAGCCTCCCATGATCAAATTCACAACCAAGATCTACCACCCCAACGTGGAC
GAGAACGGACAGATTTGCCTGCCCATCATCAGCAGTGAGAACTGGAAGCCTTGCACCAAG
ACTTGCCAAGTCCTGGAGGCCCTCAATGTGCTGGTGAATAGACCGAATATCAGGGAGCCC
CTGCGGATGGACCTCGCTGACCTGCTGACACAGAATCCGGAGCTGTTCAGAAAGAATGCC
GAAGAGTTCACCCTCCGATTCGGAGTGGACCGGCCCTCCTAA

Enzyme 28 GenBank Gene ID

NM_004223.3 Link Image

Enzyme 28 GeneCard ID

UBE2L6

Enzyme 28 GenAtlas ID

UBE2L6

Enzyme 28 HGNC ID

HGNC:12490 Link Image

Enzyme 28 Chromosome Location

Enzyme 28 Locus

11q12

Enzyme 28 SNPs

SNPJam Report Link Image

Enzyme 28 General References

Ardley HC, Rose SA, Tan N, Leek JP, Markham AF, Robinson PA: Genomic organization of the human ubiquitin-conjugating enzyme gene, UBE2L6 on chromosome 11q12. Cytogenet Cell Genet. 2000;89(1-2):137-40. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Kumar S, Kao WH, Howley PM: Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity. J Biol Chem. 1997 May 23;272(21):13548-54. [PubMed ]
Zhao C, Beaudenon SL, Kelley ML, Waddell MB, Yuan W, Schulman BA, Huibregtse JM, Krug RM: The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein. Proc Natl Acad Sci U S A. 2004 May 18;101(20):7578-82. Epub 2004 May 6. [PubMed ]
Niwa J, Ishigaki S, Doyu M, Suzuki T, Tanaka K, Sobue G: A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity. Biochem Biophys Res Commun. 2001 Mar 2;281(3):706-13. [PubMed ]
Takeuchi T, Iwahara S, Saeki Y, Sasajima H, Yokosawa H: Link between the ubiquitin conjugation system and the ISG15 conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme. J Biochem. 2005 Dec;138(6):711-9. [PubMed ]
Huang J, Xu LG, Liu T, Zhai Z, Shu HB: The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis. FEBS Lett. 2006 Feb 6;580(3):940-7. Epub 2006 Jan 18. [PubMed ]
Fortier JM, Kornbluth J: NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase. J Immunol. 2006 Jun 1;176(11):6454-63. [PubMed ]
Serniwka SA, Shaw GS: The structure of the UbcH8-ubiquitin complex shows a unique ubiquitin interaction site. Biochemistry. 2009 Dec 29;48(51):12169-79. [PubMed ]

Enzyme 28 Metabolite References

Not Available

Enzyme 29 [top]

Enzyme 29 ID

5837

Enzyme 29 Name

Glycyl-tRNA synthetase

Enzyme 29 Synonyms

Diadenosine tetraphosphate synthetase
AP-4-A synthetase
Glycine--tRNA ligase
GlyRS

Enzyme 29 Gene Name

GARS

Enzyme 29 Protein Sequence

>Glycyl-tRNA synthetase

MPSPRPVLLRGARAALLLLLPPRLLARPSLLLRRSLSAASCAPISLPAAASRSSMDGAGA
EEVLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIVD
RAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDC
TMLTPEPVLKTSGHVDKFADFMVKDVKNGECFRADHLLKAHLQKLMSDKKCSVEKKSEME
SVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFNLMFKTFIGPGGNMPGYLRPET
AQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEK
DHPKFQNVADLHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKV
GISPDKLRFRQHMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPL
VAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYLAICDECYITEMEMLLNEKGEF
TIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVREGDE
QRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYAR
TDEIGVAFGVTIDFDTVNKTPHTATLRDRDSMRQIRAEISELPSIVQDLANGNITWADVE
ARYPLFEGQETGKKETIEE

Enzyme 29 Number of Residues

739

Enzyme 29 Molecular Weight

83138.8

Enzyme 29 Theoretical pI

7.04

Enzyme 29 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity glycine-tRNA ligase activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process glycyl-tRNA aminoacylation macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 29 General Function

Involved in nucleotide binding

Enzyme 29 Specific Function

Catalyzes the attachment of glycine to tRNA(Gly). Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs

Enzyme 29 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Glycine, Serine and Threonine Metabolism (map00260 )

Enzyme 29 Reactions

ATP + glycine + tRNAGly = AMP + diphosphate + glycyl-tRNAGly [RN:R03654]

Enzyme 29 Pfam Domain Function

HGTP_anticodon (PF03129 )
tRNA-synt_2b (PF00587 )
WHEP-TRS (PF00458 )

Enzyme 29 Signals

None

Enzyme 29 Transmembrane Regions

None

Enzyme 29 Essentiality

Not Available

Enzyme 29 GenBank ID Protein

Not Available

Enzyme 29 UniProtKB/Swiss-Prot ID

P41250

Enzyme 29 UniProtKB/Swiss-Prot Entry Name

SYG_HUMAN

Enzyme 29 PDB ID

Not Available

Enzyme 29 Cellular Location

Not Available

Enzyme 29 Gene Sequence

>2220 bp

ATGCCCTCTCCGCGTCCAGTGCTGCTTAGAGGTGCTCGCGCCGCTCTGCTGCTGCTGCTG
CCGCCCCGGCTCTTAGCCCGACCCTCGCTCCTGCTCCGCCGGTCCCTCAGCGCGGCCTCC
TGCGCCCCGATCTCCTTGCCCGCCGCCGCCTCCCGGAGCAGCATGGACGGCGCGGGGGCT
GAGGAGGTGCTGGCACCTCTGAGGCTAGCAGTGCGCCAGCAGGGAGATCTTGTGCGAAAA
CTCAAAGAAGATAAAGCACCCCAAGTAGACGTAGACAAAGCAGTGGCTGAGCTCAAAGCC
CGCAAGAGGGTTCTGGAAGCAAAGGAGCTGGCGTTACAGCCCAAAGATGATATTGTAGAC
CGAGCAAAAATGGAAGATACCCTGAAGAGGAGGTTTTTCTATGATCAAGCTTTTGCTATT
TATGGAGGTGTTAGTGGTCTGTATGACTTTGGGCCAGTTGGCTGTGCTTTGAAGAACAAT
ATTATTCAGACCTGGAGGCAGCACTTTATCCAAGAGGAACAGATCCTGGAGATCGATTGC
ACCATGCTCACCCCTGAGCCAGTTTTAAAGACCTCTGGCCATGTAGACAAATTTGCTGAC
TTCATGGTGAAAGACGTAAAAAATGGAGAATGTTTTCGTGCTGACCATCTATTAAAAGCT
CATTTACAGAAATTGATGTCTGATAAGAAGTGTTCTGTCGAAAAGAAATCAGAAATGGAA
AGTGTTTTGGCCCAGCTTGATAACTATGGACAGCAAGAACTTGCGGATCTTTTTGTGAAC
TATAATGTAAAATCTCCCATTACTGGAAATGATCTATCCCCTCCAGTGTCTTTTAACTTA
ATGTTCAAGACTTTCATTGGGCCTGGAGGAAACATGCCTGGGTACTTGAGACCAGAAACT
GCACAGGGGATTTTCTTGAATTTCAAACGACTTTTGGAGTTCAACCAAGGAAAGTTGCCT
TTTGCTGCTGCCCAGATTGGAAATTCTTTTAGAAATGAGATCTCCCCTCGATCTGGACTG
ATCAGAGTCAGAGAATTCACAATGGCAGAAATTGAGCACTTTGTAGATCCCAGTGAGAAA
GACCACCCCAAGTTCCAGAATGTGGCAGACCTTCACCTTTATTTGTATTCAGCAAAAGCC
CAGGTCAGCGGACAGTCCGCTCGGAAAATGCGCCTGGGAGATGCTGTTGAACAGGGTGTG
ATTAATAACACAGTATTAGGCTATTTCATTGGCCGCATCTACCTCTACCTCACGAAGGTT
GGAATATCTCCAGATAAACTCCGCTTCCGGCAGCACATGGAGAATGAGATGGCCCATTAT
GCCTGTGACTGTTGGGATGCAGAATCCAAAACATCCTACGGTTGGATTGAGATTGTTGGA
TGTGCTGATCGTTCCTGTTATGACCTCTCCTGTCATGCACGAGCCACCAAAGTCCCACTT
GTAGCTGAGAAACCTCTGAAAGAACCCAAAACAGTCAATGTTGTTCAGTTTGAACCCAGT
AAGGGAGCAATTGGTAAGGCATATAAGAAGGATGCAAAACTGGTGATGGAGTATCTTGCC
ATTTGTGATGAGTGCTACATTACAGAAATGGAGATGCTGCTGAATGAGAAAGGGGAATTC
ACAATTGAAACTGAAGGGAAAACATTTCAGTTAACAAAAGACATGATCAATGTGAAGAGA
TTCCAGAAAACACTATATGTGGAAGAAGTTGTTCCGAATGTAATTGAACCTTCCTTCGGC
CTGGGTAGGATCATGTATACGGTATTTGAACATACATTCCATGTACGAGAAGGAGATGAA
CAGAGAACATTCTTCAGTTTCCCTGCTGTAGTTGCTCCATTCAAATGTTCCGTCCTCCCA
CTGAGCCAAAACCAGGAGTTCATGCCATTTGTCAAGGAATTATCGGAAGCCCTGACCAGG
CATGGAGTATCTCACAAAGTAGACGATTCCTCTGGGTCAATCGGAAGGCGCTATGCCAGG
ACTGATGAGATTGGCGTGGCTTTTGGTGTCACCATTGACTTTGACACAGTGAACAAGACC
CCCCACACTGCAACTCTGAGGGACCGTGACTCAATGCGGCAGATAAGAGCAGAGATCTCT
GAGCTGCCCAGCATAGTCCAAGACCTAGCCAATGGCAACATCACATGGGCTGATGTGGAG
GCCAGGTATCCTCTGTTTGAAGGGCAAGAGACTGGTAAAAAAGAGACAATCGAGGAATGA

Enzyme 29 GenBank Gene ID

D30658

Enzyme 29 GeneCard ID

GARS

Enzyme 29 GenAtlas ID

GARS

Enzyme 29 HGNC ID

HGNC:4162

Enzyme 29 Chromosome Location

Enzyme 29 Locus

7p15

Enzyme 29 SNPs

SNPJam Report Link Image

Enzyme 29 General References

Shiba K, Schimmel P, Motegi H, Noda T: Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation. J Biol Chem. 1994 Nov 25;269(47):30049-55. [PubMed ]
Williams J, Osvath S, Khong TF, Pearse M, Power D: Cloning, sequencing and bacterial expression of human glycine tRNA synthetase. Nucleic Acids Res. 1995 Apr 25;23(8):1307-10. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Ge Q, Trieu EP, Targoff IN: Primary structure and functional expression of human Glycyl-tRNA synthetase, an autoantigen in myositis. J Biol Chem. 1994 Nov 18;269(46):28790-7. [PubMed ]
Mudge SJ, Williams JH, Eyre HJ, Sutherland GR, Cowan PJ, Power DA: Complex organisation of the 5'-end of the human glycine tRNA synthetase gene. Gene. 1998 Mar 16;209(1-2):45-50. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Cader MZ, Ren J, James PA, Bird LE, Talbot K, Stammers DK: Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy. FEBS Lett. 2007 Jun 26;581(16):2959-64. Epub 2007 May 29. [PubMed ]
Xie W, Nangle LA, Zhang W, Schimmel P, Yang XL: Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase. Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):9976-81. Epub 2007 Jun 1. [PubMed ]
Guo RT, Chong YE, Guo M, Yang XL: Crystal structures and biochemical analyses suggest a unique mechanism and role for human glycyl-tRNA synthetase in Ap4A homeostasis. J Biol Chem. 2009 Oct 16;284(42):28968-76. Epub 2009 Aug 26. [PubMed ]
Antonellis A, Ellsworth RE, Sambuughin N, Puls I, Abel A, Lee-Lin SQ, Jordanova A, Kremensky I, Christodoulou K, Middleton LT, Sivakumar K, Ionasescu V, Funalot B, Vance JM, Goldfarb LG, Fischbeck KH, Green ED: Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V. Am J Hum Genet. 2003 May;72(5):1293-9. Epub 2003 Apr 10. [PubMed ]

Enzyme 29 Metabolite References

Not Available

Enzyme 30 [top]

Enzyme 30 ID

5838

Enzyme 30 Name

Ribose-phosphate pyrophosphokinase 3

Enzyme 30 Synonyms

Phosphoribosyl pyrophosphate synthase 1-like 1
PRPS1-like 1
Phosphoribosyl pyrophosphate synthase III
PRS-III

Enzyme 30 Gene Name

PRPS1L1

Enzyme 30 Protein Sequence

>Ribose-phosphate pyrophosphokinase 3

MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIDESVRGEDVYIVQSGC
GEINDSLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRSPISAKLVANMLSIAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPTVLKWIRENIPEWKNCIIVSPDAGGAKRVTS
IADQLNVDFALIHKERKKANEVDCIVLVGDVNDRVAILVDDMADTCVTICLAADKLLSAG
ATRVYAILTHGIFSGPAISRINTACFEAVVVTNTIPQDEKMKHCSKIRVIDISMILAEAI
RRTHNGESVSYLFSHVPL

Enzyme 30 Number of Residues

318

Enzyme 30 Molecular Weight

34838.9

Enzyme 30 Theoretical pI

6.31

Enzyme 30 GO Classification

Function
binding catalytic activity cation binding diphosphotransferase activity ion binding magnesium ion binding metal ion binding ribose phosphate diphosphokinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
biosynthetic process cellular biosynthetic process cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside metabolic process nucleoside monophosphate biosynthetic process nucleoside monophosphate metabolic process nucleoside phosphate metabolic process nucleotide biosynthetic process nucleotide metabolic process ribonucleoside monophosphate biosynthetic process
Component
—

Enzyme 30 General Function

Involved in magnesium ion binding

Enzyme 30 Specific Function

Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis

Enzyme 30 Pathways

Pentose Pathway (map00030 )
Purine Metabolism (map00230 )

Enzyme 30 Reactions

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate [RN:R01049]

Enzyme 30 Pfam Domain Function

Pribosyltran (PF00156 )

Enzyme 30 Signals

None

Enzyme 30 Transmembrane Regions

None

Enzyme 30 Essentiality

Not Available

Enzyme 30 GenBank ID Protein

110611809

Enzyme 30 UniProtKB/Swiss-Prot ID

P21108

Enzyme 30 UniProtKB/Swiss-Prot Entry Name

PRPS3_HUMAN Link Image

Enzyme 30 PDB ID

Not Available

Enzyme 30 Cellular Location

Not Available

Enzyme 30 Gene Sequence

>957 bp

ACGCCGAATATCAAAATCTTCAGCGGCAGCTCCCACCAGGACTTATCCCAGAAAATTGCT
GACCGCCTGGGCCTGGAGCTAGGCAAGGTGGTGACTAAGAAATTCAGCAACCAGGAGACC
TGCGTGGAAATTGATGAGAGTGTGCGTGGAGAGGATGTCTACATCGTTCAGAGTGGTTGT
GGCGAAATCAACGACAGTCTAATGGAGCTTTTGATCATGATTAATGCCTGCAAGATTGCT
TCAGCTAGCCGAGTTACTGCAGTCATCCCATGCTTCCCTTATGCCCGACAGGATAAGAAG
GATAAGAGCCGGTCCCCAATCTCTGCCAAGCTTGTTGCAAATATGCTCTCTATAGCAGGT
GCGGATCATATCATCACCATGGACCTACATGCTTCTCAAATTCAGGGCTTTTTTGATATC
CCAGTAGACAACTTGTATGCAGAGCCAACTGTCCTGAAGTGGATAAGGGAGAATATCCCT
GAGTGGAAGAACTGCATTATTGTCTCGCCAGATGCTGGTGGAGCTAAAAGAGTGACCTCC
ATTGCAGACCAGTTGAATGTGGACTTTGCTTTGATTCATAAAGAACGGAAGAAGGCCAAT
GAAGTGGACTGCATAGTGCTAGTGGGAGATGTGAATGATCGTGTGGCTATCCTTGTAGAT
GACATGGCAGACACTTGTGTTACAATCTGCCTCGCAGCTGACAAACTTCTCTCAGCTGGA
GCAACCAGAGTTTATGCTATCTTGACTCATGGAATCTTTTCTGGCCCAGCCATTTCTCGC
ATCAACACTGCATGCTTTGAAGCAGTGGTAGTCACCAATACCATACCTCAAGATGATAAG
ATGAAGCATTGCTCCAAAATACGAGTAATTGACATCTCCATGATCCTTGCAGAAGCCATA
AGGAGAACTCATAATGGGGAATCTGTTTCCTACCTGTTCAGCCATGTTCCTTTATAA

Enzyme 30 GenBank Gene ID

BC062797

Enzyme 30 GeneCard ID

PRPS1L1

Enzyme 30 GenAtlas ID

PRPS1L1

Enzyme 30 HGNC ID

HGNC:9463

Enzyme 30 Chromosome Location

Enzyme 30 Locus

7p21.1

Enzyme 30 SNPs

SNPJam Report Link Image

Enzyme 30 General References

Taira M, Iizasa T, Shimada H, Kudoh J, Shimizu N, Tatibana M: A human testis-specific mRNA for phosphoribosylpyrophosphate synthetase that initiates from a non-AUG codon. J Biol Chem. 1990 Sep 25;265(27):16491-7. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 30 Metabolite References

Not Available

Enzyme 31 [top]

Enzyme 31 ID

5839

Enzyme 31 Name

Bifunctional aminoacyl-tRNA synthetase

Enzyme 31 Synonyms

Cell proliferation-inducing gene 32 protein
Glutamyl-tRNA synthetase
Glutamate--tRNA ligase
GluRS
Prolyl-tRNA synthetase
Proline--tRNA ligase

Enzyme 31 Gene Name

EPRS

Enzyme 31 Protein Sequence

>Bifunctional aminoacyl-tRNA synthetase

MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLAR
VATTAGLYGSNLMEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLA
DLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEK
KQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTN
PEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMK
AEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCK
IQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYI
WEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGS
SRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVG
LKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENKD
YKKTTKVTWLAETTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPC
LKDLKKGDIIQLQRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTK
VEATKNETSAPFKERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAA
VKQLLSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKL
KAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPE
AKVLFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAED
KDKKKKEKENKSEKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKK
EENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPM
FVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDL
PIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEEL
LAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPK
IPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDK
EALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFV
AVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSG
KIVQIPFCGEIDCEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKN
PAKYYTLFGRSY

Enzyme 31 Number of Residues

1512

Enzyme 31 Molecular Weight

170589.7

Enzyme 31 Theoretical pI

7.34

Enzyme 31 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity glutamate-tRNA ligase activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding proline-tRNA ligase activity purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process glutamyl-tRNA aminoacylation macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process prolyl-tRNA aminoacylation tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 31 General Function

Involved in nucleotide binding

Enzyme 31 Specific Function

Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction:the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA

Enzyme 31 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Glutamate Metabolism (map00251 )
Porphyrin Metabolism (map00860 )

Enzyme 31 Reactions

ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu [RN:R05578]

Enzyme 31 Pfam Domain Function

HGTP_anticodon (PF03129 )
ProRS-C_1 (PF09180 )
tRNA-synt_1c (PF00749 )
tRNA-synt_1c_C (PF03950 )
tRNA-synt_2b (PF00587 )
WHEP-TRS (PF00458 )

Enzyme 31 Signals

None

Enzyme 31 Transmembrane Regions

None

Enzyme 31 Essentiality

Not Available

Enzyme 31 GenBank ID Protein

Not Available

Enzyme 31 UniProtKB/Swiss-Prot ID

P07814

Enzyme 31 UniProtKB/Swiss-Prot Entry Name

SYEP_HUMAN Link Image

Enzyme 31 PDB ID

Not Available

Enzyme 31 Cellular Location

Not Available

Enzyme 31 Gene Sequence

>4539 bp

ATGGCGACGCTCTCTCTGACCGTGAATTCAGGAGACCCTCCGCTAGGAGCTTTGCTGGCA
GTAGAACACGTGAAAGACGATGTCAGCATTTCCGTTGAAGAAGGGAAAGAGAATATTCTT
CATGTTTCTGAAAATGTGATATTCACAGATGTGAATTCTATACTTCGCTACTTGGCTAGA
GTTGCAACTACAGCTGGGTTATATGGCTCTAATCTGATGGAACATACTGAGATTGATCAC
TGGTTGGAGTTCAGTGCTACAAAATTATCTTCATGTGATTCCTTTACTTCTACAATTAAT
GAACTCAATCATTGCCTGTCTCTGAGAACATACTTAGTTGGAAACTCCTTGAGTTTAGCA
GATTTATGTGTTTGGGCCACCCTAAAAGGAAATGCTGCCTGGCAAGAACAGTTGAAACAG
AAGAAAGCTCCAGTTCATGTAAAACGTTGGTTTGGCTTTCTTGAAGCCCAGCAGGCCTTC
CAGTCAGTAGGTACCAAGTGGGATGTTTCAACAACCAAAGCTCGAGTGGCACCTGAGAAA
AAGCAAGATGTTGGGAAATTTGTTGAGCTTCCAGGTGCGGAGATGGGAAAGGTTACCGTC
AGATTTCCTCCAGAGGCCAGTGGTTACTTACACATTGGGCATGCAAAAGCTGCTCTTCTG
AACCAGCACTACCAGGTTAACTTTAAAGGGAAACTGATCATGAGATTTGATGACACAAAT
CCTGAAAAAGAAAAGGAAGATTTTGAGAAGGTTATCTTGGAAGATGTTGCAATGTTGCAT
ATCAAACCAGATCAATTTACTTATACTTCGGATCATTTTGAAACTATAATGAAGTATGCA
GAGAAGCTAATTCAAGAAGGGAAGGCTTATGTGGATGATACTCCTGCTGAACAGATGAAA
GCAGAACGTGAGCAGAGGATAGAATCTAAACATAGAAAAAACCCTATTGAGAAGAATCTA
CAAATGTGGGAAGAAATGAAAAAAGGGAGCCAGTTTGGTCAGTCCTGTTGTTTGCGAGCA
AAAATTGACATGAGTAGTAACAATGGATGCATGAGAGATCCAACCCTTTATCGCTGCAAA
ATTCAACCACATCCAAGAACTGGAAATAAATACAATGTTTATCCAACATATGATTTTGCC
TGCCCCATAGTTGACAGCATCGAAGGTGTTACACATGCCCTGAGAACAACAGAATACCAT
GACAGAGATGAGCAGTTTTACTGGATTATTGAAGCTTTAGGCATAAGAAAACCATATATT
TGGGAATATAGTCGGCTAAATCTCAACAACACAGTGCTATCCAAAAGAAAACTCACATGG
TTTGTCAATGAAGGACTAGTAGATGGATGGGATGACCCAAGATTTCCTACGGTTCGTGGT
GTACTGAGAAGAGGGATGACAGTTGAAGGACTGAAACAGTTTATTGCTGCTCAGGGCTCC
TCACGTTCAGTCGTGAACATGGAGTGGGACAAAATCTGGGCGTTTAACAAAAAGGTTATT
GACCCAGTGGCTCCACGATATGTTGCATTACTGAAGAAAGAAGTGATCCCAGTGAATGTA
CCTGAAGCTCAGGAGGAGATGAAAGAAGTAGCCAGACACCCAAAGAATCCTGAGGTTGGC
TTGAAGCCTGTGTGGTATAGTCCCAAAGTTTTCATTGAAGGTGCTGATGCAGAGACTTTT
TCGGAGGGTGAGATGGTTACATTTATAAATTGGGGCAACCTCAACATTACAAAAATACAC
AAAAATGCAGATGGAAAAATCATATCTCTTGATGCAAAGTTGAATTTGGAAAACAAAGAC
TACAAGAAAACCACTAAGGTCACTTGGCTTGCAGAGACTACACATGCTCTTCCTATTCCA
GTAATCTGTGTCACTTATGAGCACTTGATCACAAAGCCAGTGCTAGGAAAAGACGAGGAC
TTTAAGCAGTATGTCAACAAGAACAGTAAGCATGAAGAGCTAATGCTAGGGGATCCCTGC
CTTAAGGATTTGAAAAAAGGAGATATTATACAACTCCAGAGAAGAGGATTCTTCATATGT
GATCAACCTTATGAACCTGTTAGCCCATATAGTTGCAAGGAAGCCCCGTGTGTTTTGATA
TACATTCCTGATGGGCACACAAAGGAAATGCCAACATCAGGGTCAAAGGAAAAGACCAAA
GTAGAAGCCACAAAAAATGAGACCTCTGCTCCTTTTAAGGAAAGACCAACACCTTCTCTG
AATAATAATTGTACTACATCTGAGGATTCCTTGGTCCTTTACAATAGAGTGGCTGTTCAA
GGAGATGTGGTTCGTGAATTAAAAGCCAAGAAAGCACCAAAGGAAGATGTAGATGCAGCT
GTAAAACAGCTTTTGTCTTTGAAAGCTGAATATAAGGAGAAAACTGGCCAGGAATATAAA
CCTGGAAACCCTCCTGCTGAAATAGGACAGAATATTTCTTCTAATTCCTCAGCAAGTATT
CTGGAAAGTAAATCTCTGTATGATGAAGTTGCTGCACAAGGGGAGGTGGTTCGTAAGCTA
AAAGCTGAAAAATCCCCTAAGGCTAAAATAAATGAAGCTGTAGAATGCTTACTGTCCCTG
AAGGCTCAGTATAAAGAAAAAACTGGGAAGGAGTACATACCTGGTCAGCCCCCATTATCT
CAAAGTTCGGATTCAAGCCCAACCAGAAATTCTGAACCTGCTGGTTTAGAAACACCAGAA
GCGAAAGTACTTTTTGACAAAGTAGCTTCTCAAGGGGAAGTAGTTCGGAAACTTAAAACT
GAAAAAGCCCCTAAGGATCAAGTAGATATAGCTGTTCAAGAACTCCTTCAGCTAAAGGCA
CAGTACGAGTCTTTGATAGGAGTAGAGTATAAGCCTGTGTCGGCCACTGGAGCTGAGGAC
AAAGATAAGAAGAAGAAAGAAAAAGAAAATAAATCTGAAAAGCAGAATAAGCCTCAGAAA
CAAAATGATGGCCAAAGGAAAGACCCTTCTAAAAACCAAGGAGGTGGGCTCTCATCAAGT
GGAGCAGGAGAAGGGCAGGGGCCTAAGAAACAGACCAGGTTGGGTCTTGAGGCAAAAAAA
GAAGAAAATCTTGCTGATTGGTATTCTCAGGTCATCACAAAATCAGAAATGATTGAATAC
CATGACGTAAGTGGCTGTTATATTCTTCGTCCCTGGGCCTATGCCATTTGGGAAGCCATC
AAGGACTTTTTTGATGCTGAGATCAAGAAACTTGGTGTTGAAAACTGCTACTTCCCCATG
TTTGTGTCTCAAAGTGCATTAGAGAAAGAGAAGACTCATGTTGCTGACTTTGCCCCAGAG
GTTGCTTGGGTTACAAGATCTGGCAAAACCGAGCTGGCAGAACCAATTGCCATTCGTCCT
ACTAGTGAAACAGTAATGTATCCTGCATATGCAAAATGGGTACAATCACACAGAGACCTG
CCCATCAAGCTCAATCAGTGGTGCAATGTGGTGCGTTGGGAATTCAAGCATCCTCAGCCT
TTCCTACGTACTCGTGAATTTCTTTGGCAGGAAGGGCACAGTGCTTTTGTTACCGTGGAA
GAGGCAGCGGAAGAGGTCTTGCAGATACTTGACTTATATGCTCAGGTATATGAAGAACTC
CTGGCAATTCCTGTTGTTAAAGGAAGAAAGACGGAAAAGGAAAAATTTGCAGGAGGAGAC
TATACAACTACAATAGAAGCATTTATATCTGCTAGTGGAAGAGCTATCCAGGGAGGAACA
TCACATCATTTAGGGCAGAATTTTTCCAAAATGTTTGAAATCGTTTTTGAAGATCCAAAG
ATACCAGGAGAGAAGCAATTTGCCTATCAAAACTCCTGGGGCCTGACAACTCGAACTATT
GGTGTTATGACCATGGTTCATGGGGACAACATGGGTTTAGTATTACCACCCCGTGTAGCA
TGTGTTCAGGTGGTGATTATTCCTTGTGGCATTACCAATGCACTTTCTGAAGAAGACAAA
GAAGCGCTGATTGCAAAATGCAATGATTATCGAAGGCGATTACTCAGTGTTAACATCCGC
GTTAGAGCTGATTTACGAGATAATTATTCTCCAGGTTGGAAATTCAATCACTGGGAGCTC
AAGGGAGTTCCCATTAGACTTGAAGTTGGGCCACGTGATATGAAGAGCTGTCAGTTTGTA
GCCGTCAGACGAGATACTGGAGAAAAGCTGACAGTTGCTGAAAATGAGGCAGAGACTAAA
CTTCAAGCTATTTTGGAAGACATCCAGGTCACCCTTTTCACAAGGGCTTCTGAAGACCTT
AAGACTCATATGGTTGTGGCTAATACAATGGAAGACTTTCAGAAGATACTAGATTCTGGA
AGGATTGTTCAGATTCCATTCTGTGGGGAAATTGACTGTGAGGACTGGATCAAAAAGACC
ACTGCCAGGGATCAAGATCTTGAACCTGGTGCTCCATCCATGGGAGCTAAAAGCCTTTGC
ATCCCCTTCAAACCACTCTGTGAACTGCAGCCTGGAGCCAAATGTGTCTGTGGCAAGAAC
CCTGCCAAGTACTACACCTTATTTGGTCGCAGCTACTGA

Enzyme 31 GenBank Gene ID

CR933648

Enzyme 31 GeneCard ID

EPRS

Enzyme 31 GenAtlas ID

EPRS

Enzyme 31 HGNC ID

HGNC:3418

Enzyme 31 Chromosome Location

Enzyme 31 Locus

1q41-q42

Enzyme 31 SNPs

SNPJam Report Link Image

Enzyme 31 General References

Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Fett R, Knippers R: The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors. J Biol Chem. 1991 Jan 25;266(3):1448-55. [PubMed ]
Thommes P, Fett R, Schray B, Kunze N, Knippers R: The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes. Nucleic Acids Res. 1988 Jun 24;16(12):5391-406. [PubMed ]
Cerini C, Kerjan P, Astier M, Gratecos D, Mirande M, Semeriva M: A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 1991 Dec;10(13):4267-77. [PubMed ]
Kaiser E, Eberhard D, Knippers R: Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase. J Mol Evol. 1992 Jan;34(1):45-53. [PubMed ]
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
Kato T, Daigo Y, Hayama S, Ishikawa N, Yamabuki T, Ito T, Miyamoto M, Kondo S, Nakamura Y: A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis. Cancer Res. 2005 Jul 1;65(13):5638-46. [PubMed ]
Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed ]
Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS: Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats. Biochemistry. 2000 Dec 26;39(51):15775-82. [PubMed ]

Enzyme 31 Metabolite References

Not Available

Enzyme 32 [top]

Enzyme 32 ID

5842

Enzyme 32 Name

Long-chain-fatty-acid--CoA ligase 4

Enzyme 32 Synonyms

Long-chain acyl-CoA synthetase 4
LACS 4

Enzyme 32 Gene Name

ACSL4

Enzyme 32 Protein Sequence

>Long-chain-fatty-acid--CoA ligase 4

MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYR
SVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLIL
GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTL
YATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPE
GFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT
GQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSK
GDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLC
NLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEV
TDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAED
YSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDN
ICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAM
KLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK

Enzyme 32 Number of Residues

711

Enzyme 32 Molecular Weight

79187.4

Enzyme 32 Theoretical pI

8.51

Enzyme 32 GO Classification

Function
catalytic activity
Process
metabolic process
Component
—

Enzyme 32 General Function

Involved in catalytic activity

Enzyme 32 Specific Function

Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates

Enzyme 32 Pathways

Fatty Acid Metabolism (map00071 )

Enzyme 32 Reactions

ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]

Enzyme 32 Pfam Domain Function

AMP-binding (PF00501 )

Enzyme 32 Signals

None

Enzyme 32 Transmembrane Regions

8-28

Enzyme 32 Essentiality

Not Available

Enzyme 32 GenBank ID Protein

12669909

Enzyme 32 UniProtKB/Swiss-Prot ID

O60488

Enzyme 32 UniProtKB/Swiss-Prot Entry Name

ACSL4_HUMAN Link Image

Enzyme 32 PDB ID

Not Available

Enzyme 32 Cellular Location

Not Available

Enzyme 32 Gene Sequence

>2136 bp

ATGAAACTTAAGCTAAATGTGCTCACCATTATTTTGCTGCCTGTCCACTTGTTAATAACA
ATATACAGTGCCCTTATATTTATTCCATGGTATTTTCTTACCAATGCCAAGAAGAAAAAC
GCTATGGCAAAGAGAATAAAAGCTAAGCCCACTTCAGACAAACCTGGAAGTCCATATCGC
TCTGTCACACACTTCGACTCACTAGCTGTAATAGACATCCCTGGAGCAGATACTCTGGAT
AAATTATTTGACCATGCTGTATCCAAGTTTGGGAAGAAGGACAGCCTTGGGACCAGGGAA
ATCCTAAGTGAAGAAAATGAAATGCAGCCAAATGGAAAAGTTTTTAAGAAGTTAATTCTT
GGGAATTATAAATGGATGAACTATCTTGAAGTGAATCGCAGAGTGAATAACTTTGGTAGT
GGACTCACTGCACTGGGACTAAAACCAAAGAACACCATTGCCATCTTCTGTGAGACCAGG
GCCGAATGGATGATTGCAGCACAGACCTGCTTTAAGTACAACTTTCCTCTTGTGACTTTA
TATGCCACACTTGGCAAAGAAGCAGTAGTTCATGGGCTAAATGAATCTGAGGCTTCCTAT
CTGATTACCAGTGTTGAACTTCTGGAAAGTAAACTTAAGACTGCATTGTTAGATATCAGT
TGTGTTAAACATATCATTTATGTGGACAATAAGGCTATCAATAAAGCAGAGTACCCTGAA
GGATTTGAGATTCACAGCATGCAATCAGTAGAAGAGTTGGGATCTAACCCAGAAAACTTG
GGCATTCCTCCAAGTAGACCAACGCCTTCAGACATGGCCATTGTTATGTATACTAGTGGT
TCTACTGGCCGACCTAAGGGAGTGATGATGCATCATAGCAATTTGATAGCTGGAATGACA
GGCCAGTGTGAAAGAATACCTGGACTGGGACCGAAGGACACATATATTGGCTACTTGCCT
TTGGCTCATGTGCTAGAACTGACAGCAGAGATATCTTGCTTTACCTATGGCTGCAGGATT
GGATATTCTTCTCCGCTTACACTCTCTGACCAGTCCAGCAAAATTAAAAAAGGAAGCAAA
GGAGACTGTACTGTACTGAAGCCCACACTTATGGCTGCTGTTCCGGAAATCATGGATAGA
ATTTATAAGAATGTTATGAGCAAAGTCCAAGAGATGAATTATATTCAGAAAACTCTGTTC
AAGATAGGGTATGATTACAAATTGGAACAGATCAAAAAGGGATATGATGCACCTCTTTGC
AATCTGTTACTGTTTAAAAAGGTCAAGGCCCTGCTGGGAGGGAATGTCCGCATGATGCTG
TCTGGAGGGGCCCCGCTATCTCCTCAGACACACCGATTCATGAATGTCTGCTTCTGCTGC
CCAATTGGCCAGGGTTATGGACTGACAGAATCATGTGGTGCTGGGACAGTTACTGAAGTA
ACTGACTATACTACTGGCAGAGTTGGAGCACCTCTTATTTGCTGTGAAATTAAGCTAAAA
GACTGGCAAGAAGGCGGTTATACAATTAATGACAAGCCAAACCCCAGAGGTGAAATCGTA
ATTGGTGGACAGAACATCTCCATGGGATATTTTAAAAATGAAGAGAAAACAGCAGAAGAT
TATTCTGTGGATGAAAATGGACAAAGGTGGTTTTGCACTGGTGATATTGGAGAATTCCAT
CCCGATGGATGTTTACAGATTATAGATCGTAAGAAAGATCTAGTGAAGTTACAAGCAGGA
GAGTATGTATCTCTTGGGAAAGTAGAAGCTGCACTGAAGAATTGTCCACTTATTGACAAC
ATCTGTGCTTTTGCCAAAAGTGATCAGTCCTATGTGATCAGTTTTGTGGTTCCTAACCAG
AAAAGGTTGACACTTTTGGCACAACAGAAAGGGGTAGAAGGAACTTGGGTTGATATCTGC
AATAATCCTGCTATGGAAGCTGAAATACTGAAAGAAATTCGAGAAGCTGCAAATGCCATG
AAATTGGAGCGATTTGAAATTCCAATCAAGGTTCGATTAAGCCCAGAGCCATGGACCCCT
GAAACTGGTTTGGTAACTGATGCTTTCAAACTGAAAAGGAAGGAGCTGAGGAACCATTAC
CTCAAAGACATTGAACGAATGTATGGGGGCAAATAA

Enzyme 32 GenBank Gene ID

NM_022977.2 Link Image

Enzyme 32 GeneCard ID

ACSL4

Enzyme 32 GenAtlas ID

ACSL4

Enzyme 32 HGNC ID

HGNC:3571

Enzyme 32 Chromosome Location

Not Available

Enzyme 32 Locus

Not Available

Enzyme 32 SNPs

SNPJam Report Link Image

Enzyme 32 General References

Cao Y, Traer E, Zimmerman GA, McIntyre TM, Prescott SM: Cloning, expression, and chromosomal localization of human long-chain fatty acid-CoA ligase 4 (FACL4). Genomics. 1998 Apr 15;49(2):327-30. [PubMed ]
Piccini M, Vitelli F, Bruttini M, Pober BR, Jonsson JJ, Villanova M, Zollo M, Borsani G, Ballabio A, Renieri A: FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation. Genomics. 1998 Feb 1;47(3):350-8. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Meloni I, Muscettola M, Raynaud M, Longo I, Bruttini M, Moizard MP, Gomot M, Chelly J, des Portes V, Fryns JP, Ropers HH, Magi B, Bellan C, Volpi N, Yntema HG, Lewis SE, Schaffer JE, Renieri A: FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation. Nat Genet. 2002 Apr;30(4):436-40. Epub 2002 Mar 11. [PubMed ]
Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]

Enzyme 32 Metabolite References

Not Available

Enzyme 33 [top]

Enzyme 33 ID

5843

Enzyme 33 Name

Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A

Enzyme 33 Synonyms

Cam-PDE 1A
61 kDa Cam-PDE
hCam-1

Enzyme 33 Gene Name

PDE1A

Enzyme 33 Protein Sequence

>Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A

MGSSATEIEELENTTFKYLTGEQTEKMWQRLKGILRCLVKQLERGDVNVVDLKKNIEYAA
SVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMTKKKPEEKPKFRS
IVHAVQAGIFVERMYRKTYHMVGLAYPAAVIVTLKDVDKWSFDVFALNEASGEHSLKFMI
YELFTRYDLINRFKIPVSCLITFAEALEVGYSKYKNPYHNLIHAADVTQTVHYIMLHTGI
MHWLTELEILAMVFAAAIHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLM
QEEEMNILINLSKDDWRDLRNLVIEMVLSTDMSGHFQQIKNIRNSLQQPEGIDRAKTMSL
ILHAADISHPAKSWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGF
IDFIVEPTFSLLTDSTEKIVIPLIEEASKAETSSYVASSSTTIVGLHIADALRRSNTKGS
MSDGSYSPDYSLAAVDLKSFKNNLVDIIQQNKERWKELAAQEARTSSQKCEFIHQ

Enzyme 33 Number of Residues

535

Enzyme 33 Molecular Weight

61251.4

Enzyme 33 Theoretical pI

6.02

Enzyme 33 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 33 General Function

Involved in catalytic activity

Enzyme 33 Specific Function

Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a higher affinity for cGMP than for cAMP

Enzyme 33 Pathways

Purine Metabolism (map00230 )

Enzyme 33 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 33 Pfam Domain Function

PDEase_I (PF00233 )
PDEase_I_N (PF08499 )

Enzyme 33 Signals

None

Enzyme 33 Transmembrane Regions

None

Enzyme 33 Essentiality

Not Available

Enzyme 33 GenBank ID Protein

1151109

Enzyme 33 UniProtKB/Swiss-Prot ID

P54750

Enzyme 33 UniProtKB/Swiss-Prot Entry Name

PDE1A_HUMAN Link Image

Enzyme 33 PDB ID

Not Available

Enzyme 33 Cellular Location

Not Available

Enzyme 33 Gene Sequence

>1608 bp

ATGGGGTCTAGTGCCACAGAGATTGAAGAATTGGAAAACACCACTTTTAAGTATCTTACA
GGAGAACAGACTGAAAAAATGTGGCAGCGCCTGAAAGGAATACTAAGATGCTTGGTGAAG
CAGCTGGAAAGAGGTGATGTTAACGTCGTCGACTTAAAGAAGAATATTGAATATGCGGCA
TCTGTGCTGGAAGCAGTTTATATCGATGAAACAAGAAGACTTCTGGATACTGAAGATGAG
CTCAGTGACATTCAGACTGACTCAGTCCCATCTGAAGTCCGGGACTGGTTGGCTTCTACC
TTTACACGGAAAATGGGGATGACAAAAAAGAAACCTGAGGAAAAACCAAAATTTCGGAGC
ATTGTGCATGCTGTTCAAGCTGGAATTTTTGTGGAAAGAATGTACCGAAAAACATATCAT
ATGGTTGGTTTGGCATATCCAGCAGCTGTCATCGTAACATTAAAGGATGTTGATAAATGG
TCTTTCGATGTATTTGCCCTAAATGAAGCAAGTGGAGAGCATAGTCTGAAGTTTATGATT
TATGAACTGTTTACCAGATATGATCTTATCAACCGTTTCAAGATTCCTGTTTCTTGCCTA
ATCACCTTTGCAGAAGCTTTAGAAGTTGGTTACAGCAAGTACAAAAATCCATATCACAAT
TTGATTCATGCAGCTGATGTCACTCAAACTGTGCATTACATAATGCTTCATACAGGTATC
ATGCACTGGCTCACTGAACTGGAAATTTTAGCAATGGTCTTTGCTGCTGCCATTCATGAT
TATGAGCATACAGGGACAACAAACAACTTTCACATTCAGACAAGGTCAGATGTTGCCATT
TTGTATAATGATCGCTCTGTCCTTGAGAATCACCACGTGAGTGCAGCTTATCGACTTATG
CAAGAAGAAGAAATGAATATCTTGATAAATTTATCCAAAGATGACTGGAGGGATCTTCGG
AACCTAGTGATTGAAATGGTTTTATCTACAGACATGTCAGGTCACTTCCAGCAAATTAAA
AATATAAGAAACAGTTTGCAGCAGCCTGAAGGGATTGACAGAGCCAAAACCATGTCCCTG
ATTCTCCACGCAGCAGACATCAGCCACCCAGCCAAATCCTGGAAGCTGCATTATCGGTGG
ACCATGGCCCTAATGGAGGAGTTTTTCCTGCAGGGAGATAAAGAAGCTGAATTAGGGCTT
CCATTTTCCCCACTTTGTGATCGGAAGTCAACCATGGTGGCCCAGTCACAAATAGGTTTC
ATCGATTTCATAGTAGAGCCAACATTTTCTCTTCTGACAGACTCAACAGAGAAAATTGTT
ATTCCTCTTATAGAGGAAGCCTCAAAAGCCGAAACTTCTTCCTATGTGGCAAGCAGCTCA
ACCACCATTGTGGGGTTACACATTGCTGATGCACTAAGACGATCAAATACAAAAGGCTCC
ATGAGTGATGGGTCCTATTCCCCAGACTACTCCCTTGCAGCAGTGGACCTGAAGAGTTTC
AAGAACAACCTGGTGGACATCATTCAGCAGAACAAAGAGAGGTGGAAAGAGTTAGCTGCA
CAAGAAGCAAGAACCAGTTCACAGAAGTGTGAGTTTATTCATCAGTAA

Enzyme 33 GenBank Gene ID

U40370

Enzyme 33 GeneCard ID

PDE1A

Enzyme 33 GenAtlas ID

PDE1A

Enzyme 33 HGNC ID

HGNC:8774

Enzyme 33 Chromosome Location

Enzyme 33 Locus

2q32.1

Enzyme 33 SNPs

SNPJam Report Link Image

Enzyme 33 General References

Loughney K, Martins TJ, Harris EA, Sadhu K, Hicks JB, Sonnenburg WK, Beavo JA, Ferguson K: Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. J Biol Chem. 1996 Jan 12;271(2):796-806. [PubMed ]
Michibata H, Yanaka N, Kanoh Y, Okumura K, Omori K: Human Ca2+/calmodulin-dependent phosphodiesterase PDE1A: novel splice variants, their specific expression, genomic organization, and chromosomal localization. Biochim Biophys Acta. 2001 Jan 26;1517(2):278-87. [PubMed ]
Fidock M, Miller M, Lanfear J: Isolation and differential tissue distribution of two human cDNAs encoding PDE1 splice variants. Cell Signal. 2002 Jan;14(1):53-60. [PubMed ]
Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 33 Metabolite References

Not Available

Enzyme 34 [top]

Enzyme 34 ID

5845

Enzyme 34 Name

GTP:AMP phosphotransferase, mitochondrial

Enzyme 34 Synonyms

Adenylate kinase 3
AK 3
Adenylate kinase 3 alpha-like 1

Enzyme 34 Gene Name

AK3

Enzyme 34 Protein Sequence

>GTP:AMP phosphotransferase, mitochondrial

MGASARLLRAVIMGAPGSGKGTVSSRITTHFELKHLSSGDLLRDNMLRGTEIGVLAKAFI
DQGKLIPDDVMTRLALHELKNLTQYSWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEV
IKQRLTARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDDKPETVIKRLKAYEDQT
KPVLEYYQKKGVLETFSGTETNKIWPYVYAFLQTKVPQRSQKASVTP

Enzyme 34 Number of Residues

227

Enzyme 34 Molecular Weight

25565.2

Enzyme 34 Theoretical pI

9.64

Enzyme 34 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding adenylate kinase activity binding catalytic activity kinase activity nucleobase, nucleoside, nucleotide kinase activity nucleoside binding nucleotide kinase activity phosphotransferase activity, phosphate group as acceptor purine nucleoside binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
Component
—

Enzyme 34 General Function

Involved in ATP binding

Enzyme 34 Specific Function

NTP + AMP = NDP + ADP

Enzyme 34 Pathways

Pyrimidine Metabolism (map00240 )

Enzyme 34 Reactions

nucleoside triphosphate + AMP = nucleoside diphosphate + ADP [RN:R00333]

Enzyme 34 Pfam Domain Function

ADK (PF00406 )
ADK_lid (PF05191 )

Enzyme 34 Signals

None

Enzyme 34 Transmembrane Regions

None

Enzyme 34 Essentiality

Not Available

Enzyme 34 GenBank ID Protein

6518533

Enzyme 34 UniProtKB/Swiss-Prot ID

Q9UIJ7

Enzyme 34 UniProtKB/Swiss-Prot Entry Name

KAD3_HUMAN Link Image

Enzyme 34 PDB ID

2AK3

Enzyme 34 PDB File

Show

Enzyme 34 3D Structure

Enzyme 34 Cellular Location

Not Available

Enzyme 34 Gene Sequence

>684 bp

ATGGGGGCGTCGGGGCGGCTGCTGCGAGCGGTGATCATGGGGGCCCCGGGCTCGGGCAAG
GGCACCGTGTCGTCCCGCATCACTACACACTTCGAGCTGAAGCACCTCTCCCGCGGGGAC
CTGCTCCGGGACAACATGCTGCGGGGCACAGAAATTGGCGTGTTAGCCCAGGCTTTCATT
GACCAAGGGAAACTCATCCCAGATTATGTCACGACTCGGCTGGCCCTTCATGAGCTGAAA
AACCTCACCCAGTATAGCTGGCTGTTGGATGGTTTTCCAAGGACACTTCCACAGGCAGAA
GCCCTAGATAGAGCTTATCAGATCGACACAGTGATTAACCTGAATGTGCCCTTTGAGGTC
ATTAAACAACGCCTTACTGCTCGCTGGATTCATCCCGCCAGTGGCCGAGTCTATAACATT
GAATTCAACCCTCCCAAAACTGTGGGCATTGATGACCTGACTGGGGAGCCTCTCATTCAG
CGTGAGGATGATAAACCAGAGACGGTTATCAAGAGACTAAAGGCTTATGAAGACCAAACA
AAGCCAGTCCTGGAATATTACCAGAAAAAAGGGGTGTTGGAAACATTCTCCGGAACAGAA
ACCAACAAGATTTGGCCCTATGTATATGCTTTCCTACAAACTAAAGTTCCACAAAGAAGC
CAGAAAGCTTCAGTTACTCCATGA

Enzyme 34 GenBank Gene ID

AB021870

Enzyme 34 GeneCard ID

AK3

Enzyme 34 GenAtlas ID

AK3

Enzyme 34 HGNC ID

HGNC:17376 Link Image

Enzyme 34 Chromosome Location

Enzyme 34 Locus

9p24.1

Enzyme 34 SNPs

SNPJam Report Link Image

Enzyme 34 General References

Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 34 Metabolite References

Not Available

Enzyme 35 [top]

Enzyme 35 ID

5846

Enzyme 35 Name

Tryptophanyl-tRNA synthetase, cytoplasmic

Enzyme 35 Synonyms

Interferon-induced protein 53
IFP53
Tryptophan--tRNA ligase
TrpRS
hWRS
T1-TrpRS
T2-TrpRS

Enzyme 35 Gene Name

WARS

Enzyme 35 Protein Sequence

>Tryptophanyl-tRNA synthetase, cytoplasmic

MPNSEPASLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKA
DCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRI
ERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFT
KWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDY
MGMSSGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDR
TDIQCLIPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIF
LTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDY
TSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKLSFDFQ

Enzyme 35 Number of Residues

471

Enzyme 35 Molecular Weight

53164.9

Enzyme 35 Theoretical pI

6.15

Enzyme 35 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding tryptophan-tRNA ligase activity
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation tryptophanyl-tRNA aminoacylation
Component
cell part cytoplasm intracellular part

Enzyme 35 General Function

Involved in nucleotide binding

Enzyme 35 Specific Function

Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression

Enzyme 35 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Tryptophan Metabolism (map00380 )

Enzyme 35 Reactions

ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp [RN:R03664]

Enzyme 35 Pfam Domain Function

tRNA-synt_1b (PF00579 )
WHEP-TRS (PF00458 )

Enzyme 35 Signals

None

Enzyme 35 Transmembrane Regions

None

Enzyme 35 Essentiality

Not Available

Enzyme 35 GenBank ID Protein

184657

Enzyme 35 UniProtKB/Swiss-Prot ID

P23381

Enzyme 35 UniProtKB/Swiss-Prot Entry Name

SYWC_HUMAN Link Image

Enzyme 35 PDB ID

1R6T

Enzyme 35 PDB File

Show

Enzyme 35 3D Structure

Enzyme 35 Cellular Location

Not Available

Enzyme 35 Gene Sequence

>1416 bp

ATGCCCAACAGTGAGCCCGCATCTCTGCTGGAGCTGTTCAACAGCATCGCCACACAAGGG
GAGCTCGTAAGGTCCCTCAAAGCGGGAAATGCGTCAAAGGATGAAATTGATTCTGCAGTA
AAGATGTTGGTGTCATTAAAAATGAGCTACAAAGCTGCCGCGGGGGAGGATTACAAGGCT
GACTGTCCTCCAGGGAACCCAGCACCTACCAGTAATCATGGCCCAGATGCCACAGAAGCT
GAAGAGGATTTTGTGGACCCATGGACAGTACAGACAAGCAGTGCAAAAGGCATAGACTAC
GATAAGCTCATTGTTCGGTTTGGAAGTAGTAAAATTGACAAAGAGCTAATAAACCGAATA
GAGAGAGCCACCGGCCAAAGACCACACCACTTCCTGCGCAGAGGCATCTTCTTCTCACAC
AGAGATATGAATCAGGTTCTTGATGCCTATGAAAATAAGAAGCCATTTTATCTGTACACG
GGCCGGGGCCCCTCTTCTGAAGCAATGCATGTAGGTCACCTCATTCCATTTATTTTCACA
AAGTGGCTCCAGGATGTATTTAACGTGCCCTTGGTGATCCAGATGACGGATGACGAGAAG
TATCTGTGGAAGGACCTGACCCTGGACCAGGCCTATAGCTATGCTGTGGAGAATGCCAAG
GACATCATCGCCTGTGGCTTTGACATCAACAAGACTTTCATATTCTCTGACCTGGACTAC
ATGGGGATGAGCTCAGGTTTCTACAAAAATGTGGTGAAGATTCAAAAGCATGTTACCTTC
AACCAAGTGAAAGGCATTTTCGGCTTCACTGACAGCGACTGCATTGGGAAGATCAGTTTT
CCTGCCATCCAGGCTGCTCCCTCCTTCAGCAACTCATTCCCACAGATCTTCCGAGACAGG
ACGGATATCCAGTGCCTTATCCCATGTGCCATTGACCAGGATCCTTACTTTAGAATGACA
AGGGACGTCGCCCCCAGGATCGGCTATCCTAAACCAGCCCTGTTGCACTCCACCTTCTTC
CCAGCCCTGCAGGGCGCCCAGACCAAAATGAGTGCCAGCGACCCCAACTCCTCCATCTTC
CTCACCGACACGGCCAAGCAGATCAAAACCAAGGTCAATAAGCATGCGTTTTCTGGAGGG
AGAGACACCATCGAGGAGCACAGGCAGTTTGGGGGCAACTGTGATGTGGACGTGTCTTTC
ATGTACCTGACCTTCTTCCTCGAGGACGACGACAAGCTCGAGCAGATCAGGAAGGATTAC
ACCAGCGGAGCCATGCTCACCGGTGAGCTCAAGAAGGCACTCATAGAGGTTCTGCAGCCC
TTGATCGCAGAGCACCAGGCCCGGCGCAAGGAGGTCACGGATGAGATAGTGAAAGAGTTC
ATGACTCCCCGGAAGCTGTCCTTCGACTTTCAGTAG

Enzyme 35 GenBank Gene ID

M77804

Enzyme 35 GeneCard ID

WARS

Enzyme 35 GenAtlas ID

WARS

Enzyme 35 HGNC ID

HGNC:12729 Link Image

Enzyme 35 Chromosome Location

Enzyme 35 Locus

14q32.31

Enzyme 35 SNPs

SNPJam Report Link Image

Enzyme 35 General References

Rubin BY, Anderson SL, Xing L, Powell RJ, Tate WP: Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts. J Biol Chem. 1991 Dec 25;266(36):24245-8. [PubMed ]
Fleckner J, Rasmussen HH, Justesen J: Human interferon gamma potently induces the synthesis of a 55-kDa protein (gamma 2) highly homologous to rabbit peptide chain release factor and bovine tryptophanyl-tRNA synthetase. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11520-4. [PubMed ]
Frolova LYu, Sudomoina MA, Grigorieva AYu, Zinovieva OL, Kisselev LL: Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase. Gene. 1991 Dec 30;109(2):291-6. [PubMed ]
Buwitt U, Flohr T, Bottger EC: Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor. EMBO J. 1992 Feb;11(2):489-96. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Sokolova IV, Narovlianskii AN, Amchenkova AM, Turpaev KT: [Alternative splicing of 5'-terminal exons of the human tryptophanyl-tRNA synthetase gene] Mol Biol (Mosk). 1996 Mar-Apr;30(2):319-29. [PubMed ]
Frolova LY, Grigorieva AY, Sudomoina MA, Kisselev LL: The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization. Gene. 1993 Jun 30;128(2):237-45. [PubMed ]
Reano A, Richard MH, Denoroy L, Viac J, Benedetto JP, Schmitt D: Gamma interferon potently induces tryptophanyl-tRNA synthetase expression in human keratinocytes. J Invest Dermatol. 1993 Jun;100(6):775-9. [PubMed ]
Wakasugi K, Slike BM, Hood J, Otani A, Ewalt KL, Friedlander M, Cheresh DA, Schimmel P: A human aminoacyl-tRNA synthetase as a regulator of angiogenesis. Proc Natl Acad Sci U S A. 2002 Jan 8;99(1):173-7. Epub 2002 Jan 2. [PubMed ]
Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed ]
Bange FC, Flohr T, Buwitt U, Bottger EC: An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase. FEBS Lett. 1992 Mar 30;300(2):162-6. [PubMed ]
Tolstrup AB, Bejder A, Fleckner J, Justesen J: Transcriptional regulation of the interferon-gamma-inducible tryptophanyl-tRNA synthetase includes alternative splicing. J Biol Chem. 1995 Jan 6;270(1):397-403. [PubMed ]
Otani A, Slike BM, Dorrell MI, Hood J, Kinder K, Ewalt KL, Cheresh D, Schimmel P, Friedlander M: A fragment of human TrpRS as a potent antagonist of ocular angiogenesis. Proc Natl Acad Sci U S A. 2002 Jan 8;99(1):178-83. Epub 2002 Jan 2. [PubMed ]
Tzima E, Reader JS, Irani-Tehrani M, Ewalt KL, Schwartz MA, Schimmel P: Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells. Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14903-7. Epub 2003 Nov 20. [PubMed ]
Wakasugi K, Nakano T, Morishima I: Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase. Biochemistry. 2005 Jan 11;44(1):225-32. [PubMed ]
Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Yang XL, Otero FJ, Skene RJ, McRee DE, Schimmel P, Ribas de Pouplana L: Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15376-80. Epub 2003 Dec 11. [PubMed ]
Yu Y, Liu Y, Shen N, Xu X, Xu F, Jia J, Jin Y, Arnold E, Ding J: Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity. J Biol Chem. 2004 Feb 27;279(9):8378-88. Epub 2003 Dec 5. [PubMed ]
Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]

Enzyme 35 Metabolite References

Not Available

Enzyme 36 [top]

Enzyme 36 ID

5847

Enzyme 36 Name

High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A

Enzyme 36 Synonyms

Not Available

Enzyme 36 Gene Name

PDE8A

Enzyme 36 Protein Sequence

>High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A

MGCAPSIHISERLVAEDAPSPAAPPLSSGGPRLPQGQKTAALPRTRGAGLLESELRDGSG
KKVAVADVQFGPMRFHQDQLQVLLVFTKEDNQCNGFCRACEKAGFKCTVTKEAQAVLACF
LDKHHDIIIIDHRNPRQLDAEALCRSIRSSKLSENTVIVGVVRRVDREELSVMPFISAGF
TRRYVENPNIMACYNELLQLEFGEVRSQLKLRACNSVFTALENSEDAIEITSEDRFIQYA
NPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNI
QQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKAEKISECVQSDTHTDNQTGKHKDRRKGSL
DVKAVASRATEVSSQRRHSSMARIHSMTIEAPITKVINIINAAQESSPMPVTEALDRVLE
ILRTTELYSPQFGAKDDDPHANDLVGGLMSDGLRRLSGNEYVLSTKNTQMVSSNIITPIS
LDDVPPRIARAMENEEYWDFDIFELEAATHNRPLIYLGLKMFARFGICEFLHCSESTLRS
WLQIIEANYHSSNPYHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDH
PGRTNSFLCNAGSELAILYNDTAVLESHHAALAFQLTTGDDKCNIFKNMERNDYRTLRQG
IIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKNQEVINTMLRTPENRTLIKRM
LIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPVVMPVFDRNTCSIPKSQIS
FIDYFITDMFDAWDAFVDLPDLMQHLDNNFKYWKGLDEMKLRNLRPPPE

Enzyme 36 Number of Residues

829

Enzyme 36 Molecular Weight

93303.1

Enzyme 36 Theoretical pI

6.03

Enzyme 36 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds molecular transducer activity phosphoric diester hydrolase activity phosphoric ester hydrolase activity signal transducer activity two-component response regulator activity
Process
biological regulation regulation of biological process regulation of cellular process regulation of gene expression regulation of macromolecule metabolic process regulation of metabolic process regulation of transcription regulation of transcription, DNA-dependent signal transduction signal transmission signaling process two-component signal transduction system (phosphorelay)
Component
—

Enzyme 36 General Function

Involved in catalytic activity

Enzyme 36 Specific Function

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development

Enzyme 36 Pathways

Purine Metabolism (map00230 )

Enzyme 36 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 36 Pfam Domain Function

PAS (PF00989 )
PDEase_I (PF00233 )
Response_reg (PF00072 )

Enzyme 36 Signals

None

Enzyme 36 Transmembrane Regions

None

Enzyme 36 Essentiality

Not Available

Enzyme 36 GenBank ID Protein

Not Available

Enzyme 36 UniProtKB/Swiss-Prot ID

O60658

Enzyme 36 UniProtKB/Swiss-Prot Entry Name

PDE8A_HUMAN Link Image

Enzyme 36 PDB ID

Not Available

Enzyme 36 Cellular Location

Not Available

Enzyme 36 Gene Sequence

>2490 bp

ATGGGCTGTGCCCCGAGCATCCACATTTCCGAGCGCCTGGTGGCCGAGGACGCGCCTAGC
CCCGCGGCACCGCCGCTGTCGTCCGGCGGGCCGCGCCTCCCGCAGGGCCAGAAGACGGCC
GCCTTGCCCCGGACCCGCGGCGCCGGCCTCTTGGAGTCGGAGCTTCGCGACGGCAGCGGC
AAGAAGGTAGCAGTAGCTGATGTGCAGTTTGGCCCCATGAGATTTCATCAAGATCAACTT
CAGGTACTTTTAGTGTTTACCAAAGAAGATAACCAATGTAATGGATTCTGCAGGGCATGT
GAAAAAGCAGGGTTTAAGTGTACAGTTACCAAGGAGGCTCAGGCTGTCCTTGCCTGTTTC
CTGGACAAACATCATGACATTATCATCATAGACCACAGAAATCCTCGACAGCTGGATGCA
GAGGCACTGTGCAGGTCTATCAGATCATCAAAACTCTCAGAAAACACAGTTATTGTTGGT
GTAGTACGCAGGGTGGATAGAGAAGAGTTGTCCGTAATGCCTTTCATTTCTGCTGGATTT
ACAAGGAGGTATGTAGAAAACCCCAACATCATGGCCTGCTACAATGAACTGCTCCAGCTG
GAGTTTGGAGAGGTGCGATCACAACTGAAACTCAGGGCTTGTAACTCAGTATTCACTGCA
TTAGAAAACAGTGAAGATGCAATTGAAATTACAAGCGAAGACCGTTTTATACAGTATGCA
AATCCTGCATTTGAAACAACAATGGGCTATCAGTCAGGTGAATTAATAGGGAAGGAGTTA
GGAGAAGTGCCTATAAATGAAAAAAAGGCTGACTTGCTCGATACTATAAATTCATGCATC
AGGATAGGCAAGGAGTGGCAAGGAATTTACTATGCAAAAAAGAAAAACGGAGATAATATA
CAACAAAATGTGAAGATAATACCTGTCATTGGACAGGGAGGAAAAATTAGACACTATGTG
TCCATTATCAGAGTGTGCAATGGCAACAATAAGGCTGAGAAAATATCCGAATGTGTTCAG
TCTGACACTCATACAGATAATCAGACAGGCAAACATAAAGACAGGAGAAAAGGCTCACTA
GACGTCAAAGCTGTTGCCTCCCGTGCAACTGAAGTTTCCAGCCAGAGACGACACTCTTCC
ATGGCCCGGATACATTCCATGACAATTGAGGCGCCCATCACCAAGGTAATCAATATTATC
AATGCTGCCCAGGAAAGTAGTCCCATGCCTGTGACAGAAGCCCTAGACCGTGTGCTGGAA
ATTCTAAGAACCACTGAGTTATATTCACCACAGTTTGGTGCTAAAGATGATGATCCCCAT
GCCAATGACCTTGTTGGGGGCTTAATGTCTGATGGTTTGCGAAGACTATCAGGGAATGAA
TATGTTCTTTCAACAAAAAACACTCAAATGGTTTCAAGCAATATAATCACTCCCATCTCC
CTTGATGATGTCCCACCACGGATAGCTCGGGCCATGGAAAATGAGGAATACTGGGACTTT
GATATTTTTGAACTGGAGGCTGCCACCCACAATAGGCCTTTGATTTATCTTGGTCTCAAA
ATGTTTGCTCGCTTTGGAATCTGTGAATTCTTACACTGCTCCGAGTCAACGCTAAGATCA
TGGTTACAAATTATCGAAGCCAATTATCATTCCTCCAATCCCTACCACAATTCTACACAT
TCTGCTGATGTGCTTCATGCCACTGCCTATTTTCTCTCCAAGGAGAGGATAAAGGAAACT
TTAGATCCAATTGATGAGGTCGCTGCACTCATCGCAGCCACCATTCATGATGTGGATCAC
CCTGGGAGAACCAACTCCTTCCTGTGTAATGCTGGAAGTGAGCTGGCCATTTTGTACAAT
GACACTGCTGTGCTGGAGAGCCACCATGCGGCCTTGGCCTTCCAGCTGACCACTGGAGAT
GATAAATGCAATATATTTAAAAACATGGAGAGGAATGATTATCGGACACTGCGCCAGGGG
ATTATCGACATGGTCTTAGCCACAGAAATGACAAAGCACTTTGAGCATGTCAACAAATTT
GTCAACAGCATCAACAAACCCTTGGCAACACTAGAAGAAAATGGGGAAACTGATAAAAAC
CAGGAAGTGATAAACACTATGCTTAGGACTCCAGAGAACCGGACCCTAATCAAACGAATG
CTGATTAAATGTGCTGATGTGTCCAATCCCTGCCGACCCCTGCAGTACTGCATCGAGTGG
GCTGCACGCATTTCGGAAGAATATTTTTCTCAGACTGATGAAGAGAAGCAGCAGGGCTTA
CCTGTGGTGATGCCAGTGTTTGACAGAAATACCTGCAGCATCCCCAAATCCCAAATCTCT
TTCATTGATTACTTCATCACAGACATGTTTGATGCTTGGGATGCCTTTGTAGACCTGCCT
GATTTAATGCAGCATCTTGACAACAACTTTAAATACTGGAAAGGACTGGACGAAATGAAG
CTGCGGAACCTCCGACCACCTCCTGAATAG

Enzyme 36 GenBank Gene ID

AF388183

Enzyme 36 GeneCard ID

PDE8A

Enzyme 36 GenAtlas ID

PDE8A

Enzyme 36 HGNC ID

HGNC:8793

Enzyme 36 Chromosome Location

Enzyme 36 Locus

15q25.3

Enzyme 36 SNPs

SNPJam Report Link Image

Enzyme 36 General References

Wang P, Wu P, Egan RW, Billah MM: Human phosphodiesterase 8A splice variants: cloning, gene organization, and tissue distribution. Gene. 2001 Dec 12;280(1-2):183-94. [PubMed ]
Glavas NA, Ostenson C, Schaefer JB, Vasta V, Beavo JA: T cell activation up-regulates cyclic nucleotide phosphodiesterases 8A1 and 7A3. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6319-24. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Fisher DA, Smith JF, Pillar JS, St Denis SH, Cheng JB: Isolation and characterization of PDE8A, a novel human cAMP-specific phosphodiesterase. Biochem Biophys Res Commun. 1998 May 29;246(3):570-7. [PubMed ]
Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Wang H, Yan Z, Yang S, Cai J, Robinson H, Ke H: Kinetic and structural studies of phosphodiesterase-8A and implication on the inhibitor selectivity. Biochemistry. 2008 Dec 2;47(48):12760-8. [PubMed ]

Enzyme 36 Metabolite References

Not Available

Enzyme 37 [top]

Enzyme 37 ID

5848

Enzyme 37 Name

Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B

Enzyme 37 Synonyms

Cam-PDE 1B
63 kDa Cam-PDE

Enzyme 37 Gene Name

PDE1B

Enzyme 37 Protein Sequence

>Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B

MELSPRSPPEMLEESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEINIEELKKNL
EYTASLLEAVYIDETRQILDTEDELQELRSDAVPSEVRDWLASTFTQQARAKGRRAEEKP
KFRSIVHAVQAGIFVERMFRRTYTSVGPTYSTAVLNCLKNLDLWCFDVFSLNQAADDHAL
RTIVFELLTRHNLISRFKIPTVFLMSFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLL
RTGMVHCLSEIELLAIIFAAAIHDYEHTGTTNSFHIQTKSECAIVYNDRSVLENHHISSV
FRLMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKTMKTALQQLERIDKPK
ALSLLLHAADISHPTKQWLVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQS
QIGFIDFIVEPTFSVLTDVAEKSVQPLADEDSKSKNQPSFQWRQPSLDVEVGDPNPDVVS
FRSTWVKRIQENKQKWKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD

Enzyme 37 Number of Residues

536

Enzyme 37 Molecular Weight

61379.2

Enzyme 37 Theoretical pI

5.22

Enzyme 37 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 37 General Function

Involved in catalytic activity

Enzyme 37 Specific Function

Enzyme 37 Pathways

Purine Metabolism (map00230 )

Enzyme 37 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 37 Pfam Domain Function

PDEase_I (PF00233 )
PDEase_I_N (PF08499 )

Enzyme 37 Signals

None

Enzyme 37 Transmembrane Regions

None

Enzyme 37 Essentiality

Not Available

Enzyme 37 GenBank ID Protein

Not Available

Enzyme 37 UniProtKB/Swiss-Prot ID

Q01064

Enzyme 37 UniProtKB/Swiss-Prot Entry Name

PDE1B_HUMAN Link Image

Enzyme 37 PDB ID

1TAZ

Enzyme 37 PDB File

Show

Enzyme 37 3D Structure

Enzyme 37 Cellular Location

Not Available

Enzyme 37 Gene Sequence

>1611 bp

ATGGAGCTGTCCCCCCGCAGTCCTCCGGAGATGCTGGAGGAGTCGGATTGCCCGTCACCC
CTGGAGCTGAAGTCAGCCCCCAGCAAGAAGATGTGGATTAAGCTTCGGTCTCTGCTGCGC
TACATGGTGAAGCAGTTGGAGAATGGGGAGATAAACATTGAGGAGCTGAAGAAAAATCTG
GAGTACACAGCTTCTCTGCTGGAAGCCGTCTACATAGATGAGACACGGCAAATCTTGGAC
ACGGAGGACGAGCTGCAGGAGCTGCGGTCAGATGCCGTGCCTTCGGAGGTGCGGGACTGG
CTGGCCTCCACCTTCACCCAGCAGGCCCGGGCCAAAGGCCGCCGAGCAGAGGAGAAGCCC
AAGTTCCGAAGCATTGTGCACGCTGTGCAGGCTGGGATCTTCGTGGAACGGATGTTCCGG
AGAACATACACCTCTGTGGGCCCCACTTACTCTACTGCGGTTCTCAACTGTCTCAAGAAC
CTGGATCTCTGGTGCTTTGATGTCTTTTCCTTGAACCAGGCAGCAGATGACCATGCCCTG
AGGACCATTGTTTTTGAGTTGCTGACTCGGCATAACCTCATCAGCCGCTTCAAGATTCCC
ACTGTGTTTTTGATGAGTTTCCTGGATGCCTTGGAGACAGGCTATGGGAAGTACAAGAAT
CCTTACCACAACCAGATCCACGCAGCCGATGTTACCCAGACAGTCCATTGCTTCTTGCTC
CGCACAGGGATGGTGCACTGCCTGTCGGAGATTGAGCTCCTGGCCATCATCTTTGCTGCA
GCTATCCATGATTATGAGCACACGGGCACTACCAACAGCTTCCACATCCAGACCAAGTCA
GAATGTGCCATCGTGTACAATGATCGTTCAGTGCTGGAGAATCACCACATCAGCTCTGTT
TTCCGATTGATGCAGGATGATGAGATGAACATTTTCATCAACCTCACCAAGGATGAGTTT
GTAGAACTCCGAGCCCTGGTCATTGAGATGGTGTTGGCCACAGACATGTCCTGCCATTTC
CAGCAAGTGAAGACCATGAAGACAGCCTTGCAACAGCTGGAGAGGATTGACAAGCCCAAG
GCCCTGTCTCTACTGCTCCATGCTGCTGACATCAGCCACCCAACCAAGCAGTGGTTGGTC
CACAGCCGTTGGACCAAGGCCCTCATGGAGGAATTCTTCCGTCAGGGTGACAAGGAGGCA
GAGTTGGGCCTGCCCTTTTCTCCACTCTGTGACCGCACTTCCACTCTAGTGGCACAGTCT
CAGATAGGGTTCATCGACTTCATTGTGGAGCCCACATTCTCTGTGCTGACTGACGTGGCA
GAGAAGAGTGTTCAGCCCCTGGCGGATGAGGACTCCAAGTCTAAAAACCAGCCCAGCTTT
CAGTGGCGCCAGCCCTCTCTGGATGTGGAAGTGGGAGACCCCAACCCTGATGTGGTCAGC
TTTCGTTCCACCTGGGTCAAGCGCATTCAGGAGAACAAGCAGAAATGGAAGGAACGGGCA
GCAAGTGGCATCACCAACCAGATGTCCATTGACGAGCTGTCCCCCTGTGAAGAAGAGGCC
CCCCCATCCCCTGCCGAAGATGAACACAACCAGAATGGGAATCTGGATTAG

Enzyme 37 GenBank Gene ID

U56976

Enzyme 37 GeneCard ID

PDE1B

Enzyme 37 GenAtlas ID

PDE1B

Enzyme 37 HGNC ID

HGNC:8775

Enzyme 37 Chromosome Location

Enzyme 37 Locus

12q13

Enzyme 37 SNPs

SNPJam Report Link Image

Enzyme 37 General References

Jiang X, Li J, Paskind M, Epstein PM: Inhibition of calmodulin-dependent phosphodiesterase induces apoptosis in human leukemic cells. Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):11236-41. [PubMed ]
Yu J, Wolda SL, Frazier AL, Florio VA, Martins TJ, Snyder PB, Harris EA, McCaw KN, Farrell CA, Steiner B, Bentley JK, Beavo JA, Ferguson K, Gelinas R: Identification and characterisation of a human calmodulin-stimulated phosphodiesterase PDE1B1. Cell Signal. 1997 Nov;9(7):519-29. [PubMed ]
Fidock M, Miller M, Lanfear J: Isolation and differential tissue distribution of two human cDNAs encoding PDE1 splice variants. Cell Signal. 2002 Jan;14(1):53-60. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Repaske DR, Swinnen JV, Jin SL, Van Wyk JJ, Conti M: A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding the 63-kDa calmodulin-dependent phosphodiesterase. J Biol Chem. 1992 Sep 15;267(26):18683-8. [PubMed ]
Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G: A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases. Mol Cell. 2004 Jul 23;15(2):279-86. [PubMed ]

Enzyme 37 Metabolite References

Not Available

Enzyme 38 [top]

Enzyme 38 ID

5849

Enzyme 38 Name

Long-chain-fatty-acid--CoA ligase 1

Enzyme 38 Synonyms

Acyl-CoA synthetase 1
ACS1
Long-chain acyl-CoA synthetase 1
LACS 1
Long-chain acyl-CoA synthetase 2
LACS 2
Long-chain fatty acid-CoA ligase 2
Palmitoyl-CoA ligase 1
Palmitoyl-CoA ligase 2

Enzyme 38 Gene Name

ACSL1

Enzyme 38 Protein Sequence

>Long-chain-fatty-acid--CoA ligase 1

MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQ
SVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEW
LSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT
LGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQR
CGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAF
VKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQP
TVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKV
QSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV
GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGD
IGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAI
VVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHP
ELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV

Enzyme 38 Number of Residues

698

Enzyme 38 Molecular Weight

77942.7

Enzyme 38 Theoretical pI

7.16

Enzyme 38 GO Classification

Function
catalytic activity
Process
metabolic process
Component
—

Enzyme 38 General Function

Involved in catalytic activity

Enzyme 38 Specific Function

Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate

Enzyme 38 Pathways

Fatty Acid Metabolism (map00071 )

Enzyme 38 Reactions

ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]

Enzyme 38 Pfam Domain Function

AMP-binding (PF00501 )

Enzyme 38 Signals

None

Enzyme 38 Transmembrane Regions

25-45

Enzyme 38 Essentiality

Not Available

Enzyme 38 GenBank ID Protein

Not Available

Enzyme 38 UniProtKB/Swiss-Prot ID

P33121

Enzyme 38 UniProtKB/Swiss-Prot Entry Name

ACSL1_HUMAN Link Image

Enzyme 38 PDB ID

Not Available

Enzyme 38 Cellular Location

Not Available

Enzyme 38 Gene Sequence

>2097 bp

ATGCAAGCCCATGAGCTGTTCCGGTATTTTCGAATGCCAGAGCTGGTTGACTTCCGACAG
TACGTGCGTACTCTTCCGACCAACACGCTTATGGGCTTCGGAGCTTTTGCAGCACTCACC
ACCTTCTGGTACGCCACGAGACCCAAACCCCTGAAGCCGCCATGCGACCTCTCCATGCAG
TCAGTGGAAGTGGCGGGTAGTGGTGGTGCACGAAGATCCGCACTACTTGACAGCGACGAG
CCCTTGGTGTATTTCTATGATGATGTCACAACATTATACGAAGGTTTCCAGAGGGGAATA
CAGGTGTCAAATAATGGCCCTTGTTTAGGCTCTCGGAAACCAGACCAACCCTATGAATGG
CTTTCATATAAACAGGTTGCAGAATTGTCGGAGTGCATAGGCTCAGCACTGATCCAGAAG
GGCTTCAAGACTGCCCCAGATCAGTTCATTGGCATCTTTGCTCAAAATAGACCTGAGTGG
GTGATTATTGAACAAGGATGCTTTGCTTATTCGATGGTGATCGTTCCACTTTATGATACC
CTTGGAAATGAAGCCATCACGTACATAGTCAACAAAGCTGAACTCTCTCTGGTTTTTGTT
GACAAGCCAGAGAAGGCCAAACTCTTATTAGAGGGTGTAGAAAATAAGTTAATACCAGGC
CTTAAAATCATAGTTGTCATGGATGCCTACGGCAGTGAACTGGTGGAACGAGGCCAGAGG
TGTGGGGTGGAAGTCACCAGCATGAAGGCGATGGAGGACCTGGGAAGAGCCAACAGACGG
AAGCCCAAGCCTCCAGCACCTGAAGATCTTGCAGTAATTTGTTTCACAAGTGGAACTACA
GGCAACCCCAAAGGAGCAATGGTCACTCACCGAAACATAGTGAGCGATTGTTCAGCTTTT
GTGAAAGCAACAGAGAATACAGTCAATCCTTGCCCAGATGATACTTTGATATCTTTCTTG
CCTCTCGCCCATATGTTTGAGAGAGTTGTAGAGTGTGTAATGCTGTGTCATGGAGCTAAA
ATCGGATTTTTCCAAGGAGATATCAGGCTGCTCATGGATGACCTCAAGGTGCTTCAACCC
ACTGTCTTCCCCGTGGTTCCAAGACTGCTGAACCGGATGTTTGACCGAATTTTCGGACAA
GCAAACACCACGCTGAAGCGATGGCTCTTGGACTTTGCCTCCAAGAGGAAAGAAGCAGAG
CTTCGCAGCGGCATCATCAGAAACAACAGCCTGTGGGACCGGCTGATCTTCCACAAAGTA
CAGTCGAGCCTGGGCGGAAGAGTCCGGCTGATGGTGACAGGAGCCGCCCCGGTGTCTGCC
ACTGTGCTGACGTTCCTCAGAGCAGCCCTGGGCTGTCAGTTTTATGAAGGATACGGACAG
ACAGAGTGCACTGCCGGGTGCTGCCTAACCATGCCTGGAGACTGGACCGCAGGCCATGTT
GGGGCCCCGATGCCGTGCAATTTGATAAAACTTGTTGATGTGGAAGAAATGAATTACATG
GCTGCCGAGGGCGAGGGCGAGGTGTGTGTGAAAGGGCCAAATGTATTTCAGGGCTACTTG
AAGGACCCAGCGAAAACAGCAGAAGCTTTGGACAAAGACGGCTGGTTACACACAGGGGAC
ATTGGAAAATGGTTACCAAATGGCACCTTGAAAATTATCGACCGGAAAAAGCACATATTT
AAGCTGGCACAAGGAGAATACATAGCCCCTGAAAAGATTGAAAATATCTACATGCGAAGT
GAGCCTGTTGCTCAGGTGTTTGTCCACGGAGAAAGCCTGCAGGCATTTCTCATTGCAATT
GTGGTACCAGATGTTGAGACATTATGTTCCTGGGCCCAAAAGAGAGGATTTGAAGGGTCG
TTTGAGGAACTGTGCAGAAATAAGGATGTCAAAAAAGCTATCCTCGAAGATATGGTGAGA
CTTGGGAAGGATTCTGGTCTGAAACCATTTGAACAGGTCAAAGGCATCACATTGCACCCT
GAATTATTTTCTATCGACAATGGCCTTCTGACTCCAACAATGAAGGCGAAAAGGCCAGAG
CTGCGGAACTATTTCAGGTCGCAGATAGATGACCTCTATTCCACTATCAAGGTTTAG

Enzyme 38 GenBank Gene ID

D10040

Enzyme 38 GeneCard ID

ACSL1

Enzyme 38 GenAtlas ID

ACSL1

Enzyme 38 HGNC ID

HGNC:3569

Enzyme 38 Chromosome Location

Enzyme 38 Locus

4q35

Enzyme 38 SNPs

SNPJam Report Link Image

Enzyme 38 General References

Abe T, Fujino T, Fukuyama R, Minoshima S, Shimizu N, Toh H, Suzuki H, Yamamoto T: Human long-chain acyl-CoA synthetase: structure and chromosomal location. J Biochem (Tokyo). 1992 Jan;111(1):123-8. [PubMed ]
Ghosh B, Barbosa E, Singh I: Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression. Mol Cell Biochem. 1995 Oct 4;151(1):77-81. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed ]

Enzyme 38 Metabolite References

Not Available

Enzyme 39 [top]

Enzyme 39 ID

5850

Enzyme 39 Name

cGMP-inhibited 3',5'-cyclic phosphodiesterase B

Enzyme 39 Synonyms

CGIPDE1
CGIP1
Cyclic GMP-inhibited phosphodiesterase B
CGI-PDE B

Enzyme 39 Gene Name

PDE3B

Enzyme 39 Protein Sequence

>cGMP-inhibited 3',5'-cyclic phosphodiesterase B

MRRDERDAKAMRSLQPPDGAGSPPESLRNGYVKSCVSPLRQDPPRGFFFHLCRFCNVELR
PPPASPQQPRRCSPFCRARLSLGALAAFVLALLLGAEPESWAAGAAWLRTLLSVCSHSLS
PLFSIACAFFFLTCFLTRTKRGPGPGRSCGSWWLLALPACCYLGDFLVWQWWSWPWGDGD
AGSAAPHTPPEAAAGRLLLVLSCVGLLLTLAHPLRLRHCVLVLLLASFVWWVSFTSLGSL
PSALRPLLSGLVGGAGCLLALGLDHFFQIREAPLHPRLSSAAEEKVPVIRPRRRSSCVSL
GETAASYYGSCKIFRRPSLPCISREQMILWDWDLKQWYKPHYQNSGGGNGVDLSVLNEAR
NMVSDLLTDPSLPPQVISSLRSISSLMGAFSGSCRPKINPLTPFPGFYPCSEIEDPAEKG
DRKLNKGLNRNSLPTPQLRRSSGTSGLLPVEQSSRWDRNNGKRPHQEFGISSQGCYLNGP
FNSNLLTIPKQRSSSVSLTHHVGLRRAGVLSSLSPVNSSNHGPVSTGSLTNRSPIEFPDT
ADFLNKPSVILQRSLGNAPNTPDFYQQLRNSDSNLCNSCGHQMLKYVSTSESDGTDCCSG
KSGEEENIFSKESFKLMETQQEEETEKKDSRKLFQEGDKWLTEEAQSEQQTNIEQEVSLD
LILVEEYDSLIEKMSNWNFPIFELVEKMGEKSGRILSQVMYTLFQDTGLLEIFKIPTQQF
MNYFRALENGYRDIPYHNRIHATDVLHAVWYLTTRPVPGLQQIHNGCGTGNETDSDGRIN
HGRIAYISSKSCSNPDESYGCLSSNIPALELMALYVAAAMHDYDHPGRTNAFLVATNAPQ
AVLYNDRSVLENHHAASAWNLYLSRPEYNFLLHLDHVEFKRFRFLVIEAILATDLKKHFD
FLAEFNAKANDVNSNGIEWSNENDRLLVCQVCIKLADINGPAKVRDLHLKWTEGIVNEFY
EQGDEEANLGLPISPFMDRSSPQLAKLQESFITHIVGPLCNSYDAAGLLPGQWLEAEEDN
DTESGDDEDGEELDTEDEEMENNLNPKPPRRKSRRRIFCQLMHHLTENHKIWKEIVEEEE
KCKADGNKLQVENSSLPQADEIQVIEEADEEE

Enzyme 39 Number of Residues

1112

Enzyme 39 Molecular Weight

124332.1

Enzyme 39 Theoretical pI

5.75

Enzyme 39 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 39 General Function

Involved in catalytic activity

Enzyme 39 Specific Function

Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. May play a role in fat metabolism

Enzyme 39 Pathways

Purine Metabolism (map00230 )

Enzyme 39 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 39 Pfam Domain Function

PDEase_I (PF00233 )

Enzyme 39 Signals

None

Enzyme 39 Transmembrane Regions

88-108 117-137 152-172 192-212 220-240 247-267

Enzyme 39 Essentiality

Not Available

Enzyme 39 GenBank ID Protein

1246755

Enzyme 39 UniProtKB/Swiss-Prot ID

Q13370

Enzyme 39 UniProtKB/Swiss-Prot Entry Name

PDE3B_HUMAN Link Image

Enzyme 39 PDB ID

1SOJ

Enzyme 39 PDB File

Show

Enzyme 39 3D Structure

Enzyme 39 Cellular Location

Not Available

Enzyme 39 Gene Sequence

>3339 bp

ATGAGGAGGGACGAGCGAGACGCCAAAGCCATGCGGTCCCTGCAGCCGCCGGATGGGGCC
GGCTCGCCCCCCGAGAGTCTGAGGAACGGCTACGTGAAGAGCTGCGTGAGCCCCTTGCGG
CAGGACCCTCCGCGCGGCTTCTTCTTCCACCTCTGCCGCTTCTGCAACGTGGAGCTGCGG
CCGCCGCCGGCCTCTCCCCAGCAGCCGCGGCGCTGCTCCCCCTTCTGCCGGGCGCGCCTC
TCGCTGGGCGCCCTGGCTGTCTTTGTCCTCGCCCTGCTGCTGGGCGCGGAACCCGAGAGC
TGGGCTGCCGGGGCCGCCTGGCTGCGGACGCTGCTGAGCGTGTGTTCGCACAGCTTGAGC
CCCCTCTTCAGCATCGCCTGTGCCTTCTTCTTCCTCACCTGCTTCCTCACCCGGACCAAG
CGGGGACCCGGCCCGGGCCGGAGCTGCGGCTCCTGGTGGCTGCTGGCGCTGCCCGCCTGC
TGTTACCTGGGGGACTTCTTGGTGTGGCAGTGGTGGTCTTGGCCTTGGGGGGATGGCGAC
GCAGGGTCCGCGGCCCCGCACACGCCCCCGGAGGCGGCAGCGGGCAGGTTGCTGCTGGTG
CTGAGCTGCGTAGGGCTGCTGCTGACGCTCGCGCACCCGCTGCGGCTCCGGCACTGCGTT
CTGGTGCTGCTCCTGGCCAGCTTCGTCTGGTGGGTCTCCTTCACCAGCCTCGGGTCGCTG
CCCTCCGCCCTCAGGCCGCTGCTCTCCGGCCTGGTGGGGGGCGCTGGCTGCCTGCTGGCC
CTGGGGTTGGATCACTTCTTTCAAATCAGGGAAGCGCCTCTTCATCCTCGACTGTCCAGT
GCCGCCGAAGAAAAAGTGCCTGTGATCCGACCCCGGAGGAGGTCCAGCTGCGTGTCGTTA
GGAGAAACTGCAGCCAGTTACTATGGCAGTTGCAAAATATTCAGGAGACCGTCGTTGCCT
TGTATTTCCAGAGAACAGATGATTCTTTGGGATTGGGACTTAAAACAATGGTATAAGCCT
CATTATCAAAATTCTGGAGGTGGAAATGGAGTTGATCTTTCAGTGCTAAATGAGGCTCGC
AATATGGTGTCAGATCTTCTGACTGATCCAAGCCTTCCACCACAAGTCATTTCCTCTCTA
CGGAGTATTAGTAGCTTAATGGGTGCTTTCTCAGGTTCCTGTAGGCCAAAGATTAATCCT
CTCACACCATTTCCTGGATTTTACCCCTGTTCTGAAATAGAGGACCCAGCTGAGAAAGGG
GATAGAAAACTTAACAAGGGACTAAATAGGAATAGTTTGCCAACTCCACAGCTGAGGAGA
AGCTCAGGAACTTCAGGATTGCTACCTGTTGAACAGTCTTCAAGGTGGGATCGTAATAAT
GGCAAAAGGCCTCACCAAGAATTTGGCATTTCAAGTCAAGGATGCTATCTAAATGGGCCT
TTTAATTCAAATCTACTGACTATCCCGAAGCAAAGGTCATCTTCTGTATCACTGACTCAC
CATGTAGGTCTCAGAAGAGCTGGTGTTTTGTCCAGTCTGAGTCCTGTGAATTCTTCCAAC
CATGGACCAGTGTCTACTGGCTCTCTAACTAATCGATCACCCATAGAATTTCCTGATACT
GCTGATTTTCTTAATAAGCCAAGCGTTATCTTGCAGAGATCTCTGGGCAATGCACCTAAT
ACTCCAGATTTTTATCAGCAACTTAGAAATTCTGATAGCAATCTGTGTAACAGCTGTGGA
CATCAAATGCTGAAATATGTTTCAACATCTGAATCAGATGGTACAGATTGCTGCAGTGGA
AAATCAGGTGAAGAAGAAAACATTTTCTCGAAAGAATCATTCAAACTTATGGAAACTCAA
CAAGAAGAGGAAACAGAGAAGAAAGACAGCAGAAAATTATTTCAGGAAGGTGATAAGTGG
CTAACAGAAGAGGCACAGAGTGAACAGCAAACAAATATTGAACAGGAAGTATCACTGGAC
CTGATTTTAGTAGAAGAGTATGACTCATTAATAGAAAAGATGAGCAACTGGAATTTTCCA
ATTTTTGAACTTGTAGAAAAGATGGGAGAGAAATCAGGAAGGATTCTCAGTCAGGTTATG
TATACCTTATTTCAAGACACTGGTTTATTGGAAATATTTAAAATTCCCACTCAACAATTT
ATGAACTATTTTCGTGCATTAGAAAATGGCTATCGAGACATTCCTTATCACAATCGTATA
CATGCCACAGATGTGCTACATGCAGTTTGGTATCTGACAACGCGGCCAGTTCCTGGCTTA
CAGCAGATCCACAATGGTTGTGGAACAGGAAATGAAACAGATTCTGATGGTAGAATTAAC
CATGGGCGAATTGCTTATATTTCTTCGAAGAGCTGCTCTAATCCTGATGAGAGTTATGGC
TGCCTGTCTTCAAACATTCCTGCATTAGAATTGATGGCTCTATACGTGGCAGCTGCCATG
CATGATTATGATCACCCAGGGAGGACAAATGCATTTCTAGTGGCTACAAATGCCCCTCAG
GCAGTTTTATACAATGACAGATCTGTTCTGGAAAATCATCATGCTGCGTCAGCTTGGAAT
CTATATCTTTCTCGCCCAGAATACAACTTCCTTCTTCATCTTGATCATGTGGAATTCAAG
CGCTTTCGTTTTTTAGTCATTGAAGCAATCCTTGCTACGGATCTTAAAAAGCATTTTGAT
TTTCTCGCAGAATTCAATGCCAAGGCAAATGATGTAAATAGTAATGGCATAGAATGGAGT
AATGAAAATGATCGCCTCTTGGTATGCCAGGTGTGCATCAAACTGGCAGATATAAATGGC
CCAGCAAAAGTTCGAGACTTGCATTTGAAATGGACAGAAGGCATTGTCAATGAATTTTAT
GAGCAGGGAGATGAAGAAGCAAATCTTGGTCTGCCCATCAGTCCATTCATGGATCGTTCT
TCTCCTCAACTAGCAAAACTCCAAGAATCTTTTATCACCCACATAGTGGGTCCCCTGTGT
AACTCCTATGATGCTGCTGGTTTGCTACCAGGTCAGTGGTTAGAAGCAGAAGAGGATAAT
GATACTGAAAGTGGTGATGATGAAGACGGTGAAGAATTAGATACAGAAGATGAAGAAATG
GAAAACAATCTAAATCCAAAACCACCAAGAAGGAAAAGCAGACGGCGAATATTTTGTCAG
CTAATGCACCACCTCACTGAAAACCACAAGATATGGAAGGAAATCGTAGAGGAAGAAGAA
AAATGTAAAGCTGATGGGAATAAACTGCAGGTGGAGAATTCCTCCTTACCTCAAGCAGAT
GAGATTCAGGTAATTGAAGAGGCAGATGAAGAGGAATAG

Enzyme 39 GenBank Gene ID

X95520

Enzyme 39 GeneCard ID

PDE3B

Enzyme 39 GenAtlas ID

PDE3B

Enzyme 39 HGNC ID

HGNC:8779

Enzyme 39 Chromosome Location

Enzyme 39 Locus

11p15.1

Enzyme 39 SNPs

SNPJam Report Link Image

Enzyme 39 General References

Miki T, Taira M, Hockman S, Shimada F, Lieman J, Napolitano M, Ward D, Taira M, Makino H, Manganiello VC: Characterization of the cDNA and gene encoding human PDE3B, the cGIP1 isoform of the human cyclic GMP-inhibited cyclic nucleotide phosphodiesterase family. Genomics. 1996 Sep 15;36(3):476-85. [PubMed ]
Murata T, Taira M, Manganiello VC: Differential expression of cGMP-inhibited cyclic nucleotide phosphodiesterases in human hepatoma cell lines. FEBS Lett. 1996 Jul 15;390(1):29-33. [PubMed ]
Lobbert RW, Winterpacht A, Seipel B, Zabel BU: Molecular cloning and chromosomal assignment of the human homologue of the rat cGMP-inhibited phosphodiesterase 1 (PDE3A)--a gene involved in fat metabolism located at 11p 15.1. Genomics. 1996 Oct 15;37(2):211-8. [PubMed ]
Liu H, Tang JR, Choi YH, Napolitano M, Hockman S, Taira M, Degerman E, Manganiello VC: Importance of cAMP-response element-binding protein in regulation of expression of the murine cyclic nucleotide phosphodiesterase 3B (Pde3b) gene in differentiating 3T3-L1 preadipocytes. J Biol Chem. 2006 Jul 28;281(30):21096-113. Epub 2006 May 15. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Scapin G, Patel SB, Chung C, Varnerin JP, Edmondson SD, Mastracchio A, Parmee ER, Singh SB, Becker JW, Van der Ploeg LH, Tota MR: Crystal structure of human phosphodiesterase 3B: atomic basis for substrate and inhibitor specificity. Biochemistry. 2004 May 25;43(20):6091-100. [PubMed ]

Enzyme 39 Metabolite References

Not Available

Enzyme 40 [top]

Enzyme 40 ID

5851

Enzyme 40 Name

Ubiquitin-conjugating enzyme E2 G1

Enzyme 40 Synonyms

E217K
UBC7
Ubiquitin carrier protein G1
Ubiquitin-protein ligase G1

Enzyme 40 Gene Name

UBE2G1

Enzyme 40 Protein Sequence

>Ubiquitin-conjugating enzyme E2 G1

MTELQSALLLRRQLAELNKNPVEGFSAGLIDDNDLYRWEVLIIGPPDTLYEGGVFKAHLT
FPKDYPLRPPKMKFITEIWHPNVDKNGDVCISILHEPGEDKYGYEKPEERWLPIHTVETI
MISVISMLADPNGDSPANVDAAKEWREDRNGEFKRKVARCVRKSQETAFE

Enzyme 40 Number of Residues

170

Enzyme 40 Molecular Weight

19509.0

Enzyme 40 Theoretical pI

4.95

Enzyme 40 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 40 General Function

Involved in acid-amino acid ligase activity

Enzyme 40 Specific Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-, as well as 'Lys-63'-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4

Enzyme 40 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 40 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 40 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 40 Signals

None

Enzyme 40 Transmembrane Regions

None

Enzyme 40 Essentiality

Not Available

Enzyme 40 GenBank ID Protein

Not Available

Enzyme 40 UniProtKB/Swiss-Prot ID

P62253

Enzyme 40 UniProtKB/Swiss-Prot Entry Name

UB2G1_HUMAN Link Image

Enzyme 40 PDB ID

Not Available

Enzyme 40 Cellular Location

Not Available

Enzyme 40 Gene Sequence

>513 bp

ATGACGGAGCTGCAGTCGGCACTGCTACTGCGAAGACAGCTGGCAGAACTCAACAAAAAT
CCAGTGGAAGGCTTTTCTGCAGGTTTAATAGATGACAATGATCTCTACCGATGGGAAGTC
CTTATTATTGGCCCTCCAGATACACTTTATGAAGGTGGTGTTTTTAAGGCTCATCTTACT
TTCCCAAAAGATTATCCCCTCCGACCTCCTAAAATGAAATTCATTACAGAAATCTGGCAC
CCAAATGTTGATAAAAATGGTGATGTGTGCATTTCTATTCTTCATGAGCCTGGGGAAGAT
AAGTATGGTTATGAAAAGCCAGAGGAACGCTGGCTCCCTATCCACACTGTGGAAACCATC
ATGATTAGTGTCATTTCTATGCTGGCAGACCCTAATGGAGACTCACCTGCTAATGTTGAT
GCTGCGAAAGAATGGAGGGAAGATAGAAATGGAGAATTTAAAAGAAAAGTTGCCCGCTGT
GTAAGAAAAAGCCAAGAGACTGCTTTTGAGTGA

Enzyme 40 GenBank Gene ID

D78514

Enzyme 40 GeneCard ID

UBE2G1

Enzyme 40 GenAtlas ID

UBE2G1

Enzyme 40 HGNC ID

HGNC:12482 Link Image

Enzyme 40 Chromosome Location

Enzyme 40 Locus

1q42|17p13.2

Enzyme 40 SNPs

SNPJam Report Link Image

Enzyme 40 General References

Watanabe TK, Kawai A, Fujiwara T, Maekawa H, Hirai Y, Nakamura Y, Takahashi E: Molecular cloning of UBE2G, encoding a human skeletal muscle-specific ubiquitin-conjugating enzyme homologous to UBC7 of C. elegans. Cytogenet Cell Genet. 1996;74(1-2):146-8. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
Pabarcus MK, Hoe N, Sadeghi S, Patterson C, Wiertz E, Correia MA: CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases. Arch Biochem Biophys. 2009 Mar 1;483(1):66-74. Epub 2008 Dec 10. [PubMed ]
David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]

Enzyme 40 Metabolite References

Not Available

Enzyme 41 [top]

Enzyme 41 ID

5852

Enzyme 41 Name

Glutaminyl-tRNA synthetase

Enzyme 41 Synonyms

Glutamine--tRNA ligase
GlnRS

Enzyme 41 Gene Name

QARS

Enzyme 41 Protein Sequence

>Glutaminyl-tRNA synthetase

MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLA
SRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPE
QIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPK
LEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKT
PGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFL
RFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQ
RGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRV
KYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPV
QWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVG
VTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADET
KGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVES
LEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASL
HVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV

Enzyme 41 Number of Residues

775

Enzyme 41 Molecular Weight

87798.0

Enzyme 41 Theoretical pI

7.16

Enzyme 41 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity glutamine-tRNA ligase activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process glutaminyl-tRNA aminoacylation macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 41 General Function

Involved in nucleotide binding

Enzyme 41 Specific Function

ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)

Enzyme 41 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Glutamate Metabolism (map00251 )

Enzyme 41 Reactions

ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln [RN:R03652]

Enzyme 41 Pfam Domain Function

tRNA-synt_1c (PF00749 )
tRNA-synt_1c_C (PF03950 )
tRNA_synt_1c_R1 (PF04558 )
tRNA_synt_1c_R2 (PF04557 )

Enzyme 41 Signals

None

Enzyme 41 Transmembrane Regions

None

Enzyme 41 Essentiality

Not Available

Enzyme 41 GenBank ID Protein

558586

Enzyme 41 UniProtKB/Swiss-Prot ID

P47897

Enzyme 41 UniProtKB/Swiss-Prot Entry Name

SYQ_HUMAN

Enzyme 41 PDB ID

Not Available

Enzyme 41 Cellular Location

Not Available

Enzyme 41 Gene Sequence

>2328 bp

ATGGCGGCTCTAGACTCCCTGTCGCTCTTCACTAGCCTCGGCCTGAGCGAGCAGAAGGCC
CGCGAGACGCTCAAGAACTCGGCTCTGAGCGCGCAGCTGCGCGAGGCCGCTACTCAGGCT
CAGCAGACCCTGGGTTCCACCATTGACAAAGCTACCGGGATCCTGTTATATGGCTTGGCC
TCCCGACTCAGGGATACCCGGCGTCTCTCCTTCCTTGTAAGCTACATAGCCAGTAAGAAG
ATCCACACTGAGCCCCAGCTAAGCGCTGCCCTTGAGTATGTGCGGAGTCACCCCTTGGAC
CCCATCGACACTGTGGACTTCGAGCGGGAATGTGGCGTGGGTGTCATTGTGACCCCAGAG
CAGATTGAGGAGGCTGTGGAGGCTGCTATTAACAGGCACCGGCCCCAGCTCCTGGTGGAA
CGTTACCATTTCAACATGGGGCTGCTGATGGGAGAGGCTCGGGCTGTGCTGAAGTGGGCA
GATGGCAAAATGATCAAGAATGAAGTGGACATGCAGGTCCTCCACCTTCTGGGCCCCAAG
TTGGAGGCTGATCTGGAGAAGAAGTTCAAGGTGGCAAAAGCTCGGCTAGAAGAAACAGAC
CGGAGGACGGCAAAGGATGTGGTGGAGAATGGCGAGACTGCTGACCAGACCCTGTCTCTG
ATGGAGCAGCTCCGGGGGGAGGCCCTTAAGTTCCACAAGCCTGGTGAGAACTACAAGACC
CCAGGCTATGTGGTCACTCCACACACCATGAATCTACTAAAGCAGCACCTGGAGATTACT
GGTGGGCAGGTACGTACCCGGTTCCCGCCAGAACCCAATGGAATCCTGCATATTGGACAT
GCCAAAGCCATCAATTTCAACTTTGGCTATGCCAAGGCCAACAATGGCATCTGTTTTCTG
CGTTTTGATGACACCAACCCTGAGAAGGAGGAAGCAAAGTTCTTCACGGCCATCTGTGAC
ATGGTAGCCTGGCTAGGCTACACACCTTACAAAGTCACATATGCGTCTGACTATTTTGAC
CAGCTATATGCGTGGGCTGTGGAGCTCATCCGCAGGGGTCTGGCTTATGTGTGCCACCAG
CGAGGAGAGGAGCTCAAAGGCCATAATACTCTGCCTTCACCCTGGAGAGACCGTCCCATG
GAGGAGTCACTGCTGCTCTTTGAGGCAATGCGCAAGGGCAAGTTTTCAGAGGGCGAGGCC
ACACTACGGATGAAGCTGGTGATGGAGGATGGCAAGATGGACCCTGTAGCCTATCGAGTC
AAGTATACACCACACCACCGCACAGGGGACAAATGGTGCATCTATCCCACCTACGACTAC
ACACACTGCCTCTGTGACTCCATCGAGCACATCACTCACTCACTCTGCACCAAGGAATTC
CAGGCCCGACGCTCTTCCTACTTCTGGCTTTGCAATGCACTGGACGTCTATTGCCCTGTG
CAGTGGGAGTATGGCCGCCTCAACCTGCACTATGCTGTTGTCTCTAAGAGGAAGATCCTC
CAGCTTGTAGCAACTGGTGCTGTGCGGGACTGGGATGACCCACGGCTCTTTACACTCACG
GCCCTGCGACGGCGGGGCTTCCCACCTGAGGCCATCAACAACTTCTGTGCCCGGGTGGGA
GTGACTGTGGCACAAACCACAATGGAGCCACATCTTCTAGAAGCCTGTGTGCGTGATGTG
CTGAATGACACAGCCCCACGAGCCATGGCTGTGCTGGAGTCACTACGGGTCATCATCACC
AACTTTCCTGCTGCCAAGTCCTTGGACATCCAGGTGCCCAACTTCCCAGCTGATGAGACC
AAAGGCTTCCATCAGGTTCCCTTTGCACCCATTGTCTTCATTGAGAGGACTGACTTCAAG
GAGGAGCCAGAGCCAGGATTTAAGCGCCTGGCTTGGGGCCAGCCTGTGGGCCTGAGGCAT
ACAGGCTACGTCATTGAGCTGCAGCATGTTGTCAAGGGCCCCAGTGGTTGTGTAGAGAGT
CTGGAGGTGACCTGCAGACGGGCAGATGCTGGAGAGAAGCCAAAGGCCTTTATTCACTGG
GTGTCACAGCCTTTGATGTGTGAGGTTCGCCTCTATGAGCGACTATTCCAGCACAAGAAC
CCTGAAGATCCTACTGAGGTGCCTGGTGGATTTTTAAGTGACCTGAACCTGGCATCACTA
CACGTGGTGGATGCAGCATTAGTGGACTGCTCTGTGGCCCTGGCAAAACCCTTCGACAAG
TTCCAGTTTGAGCGTCTTGGATATTTCTCCGTGGATCCAGACAGCCATCAGGGAAAGCTT
GTCTTTAACCGAACTGTCACACTGAAGGAAGACCCAGGAAAGGTGTGA

Enzyme 41 GenBank Gene ID

X76013

Enzyme 41 GeneCard ID

QARS

Enzyme 41 GenAtlas ID

QARS

Enzyme 41 HGNC ID

HGNC:9751

Enzyme 41 Chromosome Location

Enzyme 41 Locus

3p21.31

Enzyme 41 SNPs

SNPJam Report Link Image

Enzyme 41 General References

Lamour V, Quevillon S, Diriong S, N'Guyen VC, Lipinski M, Mirande M: Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8670-4. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 41 Metabolite References

Not Available

Enzyme 42 [top]

Enzyme 42 ID

5853

Enzyme 42 Name

Threonyl-tRNA synthetase, cytoplasmic

Enzyme 42 Synonyms

Threonine--tRNA ligase
ThrRS

Enzyme 42 Gene Name

TARS

Enzyme 42 Protein Sequence

>Threonyl-tRNA synthetase, cytoplasmic

MFEEKASSPSGKMGGEEKPIGAGEEKQKEGGKKKNKEGSGDGGRAELNPWPEYIYTRLEM
YNILKAEHDSILAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIA
KVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIE
NGFYYDMYLEEGGVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRIL
NEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGI
SFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFI
RSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMF
DHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL
DFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFY
GPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERM
IAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGCTLNK
KIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRSKQAE
EEF

Enzyme 42 Number of Residues

723

Enzyme 42 Molecular Weight

83434.5

Enzyme 42 Theoretical pI

6.64

Enzyme 42 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding threonine-tRNA ligase activity
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process threonyl-tRNA aminoacylation translation
Component
cell part cytoplasm intracellular part

Enzyme 42 General Function

Involved in nucleotide binding

Enzyme 42 Specific Function

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)

Enzyme 42 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Glycine, Serine and Threonine Metabolism (map00260 )

Enzyme 42 Reactions

ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr [RN:R03663]

Enzyme 42 Pfam Domain Function

HGTP_anticodon (PF03129 )
TGS (PF02824 )
tRNA-synt_2b (PF00587 )
tRNA_SAD (PF07973 )

Enzyme 42 Signals

None

Enzyme 42 Transmembrane Regions

None

Enzyme 42 Essentiality

Not Available

Enzyme 42 GenBank ID Protein

158258124

Enzyme 42 UniProtKB/Swiss-Prot ID

P26639

Enzyme 42 UniProtKB/Swiss-Prot Entry Name

SYTC_HUMAN Link Image

Enzyme 42 PDB ID

Not Available

Enzyme 42 Cellular Location

Not Available

Enzyme 42 Gene Sequence

>2172 bp

ATGTTTGAGGAGAAGGCCAGCAGTCCTTCAGGGAAGATGGGAGGCGAGGAGAAGCCGATT
GGTGCTGGTGAAGAGAAGCAAAAGGAAGGAGGCAAAAAGAAGAACAAAGAAGGATCTGGA
GATGGAGGTCGAGCTGAGTTGAATCCTTGGCCTGAATATATTTACACACGTCTTGAGATG
TATAATATACTAAAAGCAGAACATGATTCCATTCTGGCAGAAAAGGCAGAAAAAGATAGC
AAGCCAATTAAAGTCACTTTGCCTGATGGTAAACAGGTTGATGCGGAATCTTGGAAAACT
ACACCATATCAAATTGCCTGTGGAATTAGTCAAGGCCTGGCCGACAACACCGTTATTGCT
AAAGTAAATAATGTTGTGTGGGACCTGGACCGCCCTCTGGAAGAAGATTGTACCTTGGAG
CTTCTCAAGTTTGAGGATGAGGAAGCTCAGGCAGTGTATTGGCACTCTAGTGCTCACATA
ATGGGTGAAGCCATGGAAAGAGTCTATGGTGGATGTTTATGCTACGGTCCGCCAATAGAA
AATGGATTCTATTATGACATGTACCTCGAAGAAGGGGGTGTGTCTAGCAATGATTTCTCT
TCTCTGGAGGCTTTGTGTAAGAAAATCATTAAAGAAAAACAAGCTTTTGAAAGACTGGAA
GTTAAGAAAGAAACTTTACTGGCAATGTTTAAGTACAACAAGTTCAAATGCCGGATATTG
AATGAAAAGGTGAATACTCCAACTACCACAGTCTATAGATGTGGCCCTTTGATAGATCTC
TGCCGGGGTCCTCATGTTAGACACACGGGCAAAATTAAGGCTTTAAAAATACACAAAAAT
TCCTCCACGTACTGGGAAGGCAAAGCAGATATGGAGACTCTCCAGAGAATTTATGGCATT
TCATTCCCAGATCCTAAAATGTTGAAAGAGTGGGAGAAGTTCCAAGAGGAAGCTAAAAAC
CGAGATCATAGGAAAATTGGCAGGGACCAAGAACTATATTTCTTTCATGAACTCAGCCCT
GGAAGTTGCTTTTTTCTGCCAAAAGGAGCCTACATTTATAATGCACTTATTGAATTCATT
AGGAGCGAATATAGGAAAAGAGGATTCCAGGAGGTAGTCACCCCAAACATCTTCAACAGC
CGACTCTGGATGACCTCGGGCCACTGGCAGCACTACAGCGAGAACATGTTCTCCTTTGAG
GTGGAGAAGGAGCTGTTTGCCCTGAAACCCATGAACTGCCCAGGACACTGCCTTATGTTT
GATCATCGGCCAAGGTCCTGGCGAGAACTGCCTCTGCGGCTAGCTGATTTTGGGGTACTT
CATAGGAACGAGCTGTCTGGAGCACTCACAGGACTCACCCGGGTACGAAGATTCCAACAG
GATGATGCTCACATATTCTGTGCCATGGAGCAGATTGAAGATGAAATAAAAGGTTGTTTG
GATTTTCTACGTACGGTATATAGCGTATTTGGATTTTCTTTTAAACTAAACCTTTCTACT
CGCCCGGAAAAATTCCTTGGAGATATCGAAGTATGGGATCAAGCTGAGAAACAACTTGAA
AACAGTCTGAATGAATTTGGTGAAAAGTGGGAGTTAAACTCTGGAGATGGAGCTTTCTAT
GGCCCAAAGATTGACATACAGATTAAAGATGCGATTGGGCGGTACCACCAGTGTGCAACC
ATCCAGCTGGATTTCCAGTTGCCCATCAGATTTAATCTTACTTATGTAAGCCATGATGGT
GATGATAAGAAAAGGCCAGTGATTGTTCATCGAGCCATCTTGGGATCAGTGGAAAGAATG
ATTGCTATCCTCACAGAAAACTATGGGGGCAAATGGCCCTTTTGGCTGTCCCCTCGCCAG
GTAATGGTAGTTCCAGTGGGACCAACCTGTGATGAATATGCCCAAAAGGTACGACAACAA
TTCCACGATGCCAAATTCATGGCAGACATTGATCTGGATCCAGGCTGTACATTGAATAAA
AAGATTCGAAATGCACAGTTAGCACAGTATAACTTCATTTTAGTTGTTGGTGAAAAAGAG
AAAATCAGTGGCACTGTTAATATCCGCACAAGAGACAATAAGGTCCACGGGGAACGCACC
ATTTCTGAAACTATCGAGCGGCTACAGCAGCTCAAAGAGTTCCGCAGCAAACAGGCAGAA
GAAGAATTTTAA

Enzyme 42 GenBank Gene ID

AK292346

Enzyme 42 GeneCard ID

TARS

Enzyme 42 GenAtlas ID

TARS

Enzyme 42 HGNC ID

HGNC:11572 Link Image

Enzyme 42 Chromosome Location

Enzyme 42 Locus

5p13.2

Enzyme 42 SNPs

SNPJam Report Link Image

Enzyme 42 General References

Cruzen ME, Arfin SM: Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes. J Biol Chem. 1991 May 25;266(15):9919-23. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
Vasilescu J, Zweitzig DR, Denis NJ, Smith JC, Ethier M, Haines DS, Figeys D: The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells. J Proteome Res. 2007 Jan;6(1):298-305. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 42 Metabolite References

Not Available

Enzyme 43 [top]

Enzyme 43 ID

5855

Enzyme 43 Name

Asparagine synthetase [glutamine-hydrolyzing]

Enzyme 43 Synonyms

Cell cycle control protein TS11
Glutamine-dependent asparagine synthetase

Enzyme 43 Gene Name

ASNS

Enzyme 43 Protein Sequence

>Asparagine synthetase [glutamine-hydrolyzing]

MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQ
PIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGV
FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPF
LPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFN
NAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAAR
KVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVV
IFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPF
LDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNS
WFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPK
WINATDPSARTLTHYKSAVKA

Enzyme 43 Number of Residues

561

Enzyme 43 Molecular Weight

64369.4

Enzyme 43 Theoretical pI

6.85

Enzyme 43 GO Classification

Function
asparagine synthase (glutamine-hydrolyzing) activity asparagine synthase (glutamine-hydrolyzing) activity carbon-nitrogen ligase activity, with glutamine as amido-N-donor catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds
Process
asparagine biosynthetic process asparagine metabolic process aspartate family amino acid metabolic process cellular amino acid and derivative metabolic process cellular amino acid metabolic process cellular metabolic process metabolic process
Component
—

Enzyme 43 General Function

Involved in asparagine synthase (glutamine-hydrolyzing) activity

Enzyme 43 Specific Function

ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate

Enzyme 43 Pathways

Nitrogen Metabolism (map00910 )

Enzyme 43 Reactions

(1) ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate [RN:R00578]
(2) (1a) L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
(3) (1b) ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine [RN:R00483]

Enzyme 43 Pfam Domain Function

Asn_synthase (PF00733 )
GATase_2 (PF00310 )

Enzyme 43 Signals

None

Enzyme 43 Transmembrane Regions

None

Enzyme 43 Essentiality

Not Available

Enzyme 43 GenBank ID Protein

179100

Enzyme 43 UniProtKB/Swiss-Prot ID

P08243

Enzyme 43 UniProtKB/Swiss-Prot Entry Name

ASNS_HUMAN Link Image

Enzyme 43 PDB ID

Not Available

Enzyme 43 Cellular Location

Not Available

Enzyme 43 Gene Sequence

>1686 bp

ATGTGTGGCATTTGGGCGCTGTTTGGCAGTGATGATTGCCTTTCTGTTCAGTGTCTGAGT
GCTATGAAGATTGCACACAGAGGTCCAGATGCATTCCGTTTTGAGAATGTCAATGGATAC
ACCAACTGCTGCTTTGGATTTCACCGGTTGGCGGTAGTTGACCCGCTGTTTGGAATGCAG
CCAATTCGAGTGAAGAAATATCCGTATTTGTGGCTCTGTTACAATGGTGAAATCTACAAC
CATAAGAAGATGCAACAGCATTTTGAATTTGAATACCAGACCAAAGTGGATGGTGAGATA
ATCCTTCATCTTTATGACAAAGGAGGAATTGAGCAAACAATTTGTATGTTGGATGGTGTG
TTTGCATTTGTTTTACTGGATACTGCCAATAAGAAAGTGTTCCTGGGTAGAGATACATAT
GGAGTCAGACCTTTGTTTAAAGCAATGACAGAAGATGGATTTTTGGCTGTATGTTCAGAA
GCTAAAGGTCTTGTTACATTGAAGCACTCCGCGACTCCCTTTTTAAAAGTGGAGCCTTTT
CTTCCTGGACACTATGAAGTTTTGGATTTAAAGCCAAATGGCAAAGTTGCATCCGTGGAA
ATGGTTAAATATCATCACTGTCGGGATGTACCCCTGCACGCCCTCTATGACAATGTGGAG
AAACTCTTTCCAGGTTTTGAGATAGAAACTGTGAAGAACAACCTCAGGATCCTTTTTAAT
AATGCTGTAAAGAAACGTTTGATGACAGACAGAAGGATTGGCTGCCTTTTATCAGGGGGC
TTGGACTCCAGCTTGGTTGCTGCCACTCTGTTGAAGCAGCTGAAAGAAGCCCAAGTACAG
TATCCTCTCCAGACATTTGCAATTGGCATGGAAGACAGCCCCGATTTACTGGCTGCTAGA
AAGGTGGCAGATCATATTGGAAGTGAACATTATGAAGTCCTTTTTAACTCTGAGGAAGGC
ATTCAGGCTCTGGATGAAGTCATATTTTCCTTGGAAACTTATGACATTACAACAGTTCGT
GCTTCAGTAGGTATGTATTTAATTTCCAAGTATATTCGGAAGAACACAGATAGCGTGGTG
ATCTTCTCTGGAGAAGGATCAGATGAACTTACGCAGGGTTACATATATTTTCACAAGGCT
CCTTCTCCTGAAAAAGCCGAGGAGGAGAGTGAGAGGCTTCTGAGGGAACTCTATTTGTTT
GATGTTCTCCGCGCAGATCGAACTACTGCTGCCCATGGTCTTGAACTGAGAGTCCCATTT
CTAGATCATCGATTTTTTTCCTATTACTTGTCTCTGCCACCAGAAATGAGAATTCCAAAG
AATGGGATAGAAAAACATCTCCTGAGAGAGACGTTTGAGGATTCCAATCTGATACCCAAA
GAGATTCTCTGGCGACCAAAAGAAGCCTTCAGTGATGGAATAACTTCAGTTAAGAATTCC
TGGTTTAAGATTTTACAGGAATACGTTGAACATCAGGTTGATGATGCAATGATGGCAAAT
GCAGCCCAGAAATTTCCCTTCAATACTCCTAAAACCAAAGAAGGATATTACTACCGTCAA
GTCTTTGAACGCCATTACCCAGGCCGGGCTGACTGGCTGAGCCATTACTGGATGCCCAAG
TGGATCAATGCCACTGACCCTTCTGCCCGCACGCTGACCCACTACAAGTCAGCTGTCAAA
GCTTAG

Enzyme 43 GenBank Gene ID

M27396

Enzyme 43 GeneCard ID

ASNS

Enzyme 43 GenAtlas ID

ASNS

Enzyme 43 HGNC ID

HGNC:753

Enzyme 43 Chromosome Location

Enzyme 43 Locus

7q21.3

Enzyme 43 SNPs

SNPJam Report Link Image

Enzyme 43 General References

Andrulis IL, Chen J, Ray PN: Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells. Mol Cell Biol. 1987 Jul;7(7):2435-43. [PubMed ]
Zhang YP, Lambert MA, Cairney AE, Wills D, Ray PN, Andrulis IL: Molecular structure of the human asparagine synthetase gene. Genomics. 1989 Apr;4(3):259-65. [PubMed ]
Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Greco A, Ittmann M, Basilico C: Molecular cloning of a gene that is necessary for G1 progression in mammalian cells. Proc Natl Acad Sci U S A. 1987 Mar;84(6):1565-9. [PubMed ]
Greco A, Gong SS, Ittmann M, Basilico C: Organization and expression of the cell cycle gene, ts11, that encodes asparagine synthetase. Mol Cell Biol. 1989 Jun;9(6):2350-9. [PubMed ]
Van Heeke G, Schuster SM: Expression of human asparagine synthetase in Escherichia coli. J Biol Chem. 1989 Apr 5;264(10):5503-9. [PubMed ]
Van Heeke G, Schuster SM: The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity. J Biol Chem. 1989 Nov 25;264(33):19475-7. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 43 Metabolite References

Not Available

Enzyme 44 [top]

Enzyme 44 ID

5856

Enzyme 44 Name

Ubiquitin-conjugating enzyme E2 E2

Enzyme 44 Synonyms

UbcH8
Ubiquitin carrier protein E2
Ubiquitin-protein ligase E2

Enzyme 44 Gene Name

UBE2E2

Enzyme 44 Protein Sequence

>Ubiquitin-conjugating enzyme E2 E2

MSTEAQRVDDSPSTSGGSSDGDQRESVQQEPEREQVQPKKKEGKISSKTAAKLSTSAKRI
QKELAEITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFSPDYPFKPPK
VTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQ
YMTNRAEHDRMARQWTKRYAT

Enzyme 44 Number of Residues

201

Enzyme 44 Molecular Weight

22254.9

Enzyme 44 Theoretical pI

7.84

Enzyme 44 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 44 General Function

Involved in acid-amino acid ligase activity

Enzyme 44 Specific Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination

Enzyme 44 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 44 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 44 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 44 Signals

None

Enzyme 44 Transmembrane Regions

None

Enzyme 44 Essentiality

Not Available

Enzyme 44 GenBank ID Protein

16553859

Enzyme 44 UniProtKB/Swiss-Prot ID

Q96LR5

Enzyme 44 UniProtKB/Swiss-Prot Entry Name

UB2E2_HUMAN Link Image

Enzyme 44 PDB ID

1Y6L

Enzyme 44 PDB File

Show

Enzyme 44 3D Structure

Enzyme 44 Cellular Location

Not Available

Enzyme 44 Gene Sequence

>606 bp

ATGTCCACTGAGGCACAAAGAGTTGATGACAGTCCAAGCACTAGTGGAGGAAGTTCCGAT
GGAGATCAACGTGAAAGTGTTCAGCAAGAACCAGAAAGAGAACAAGTTCAGCCCAAGAAA
AAGGAGGGAAAAATATCCAGCAAAACCGCTGCTAAATTGTCAACTAGTGCTAAAAGAATT
CAGAAGGAACTTGCAGAAATCACATTGGACCCTCCTCCCAACTGTAGTGCTGGACCCAAA
GGAGACAACATTTATGAATGGAGGTCAACTATATTGGGACCCCCAGGATCTGTCTATGAA
GGAGGGGTGTTCTTTCTTGACATTACCTTTTCACCAGACTATCCGTTTAAACCCCCTAAG
GTTACCTTCCGAACAAGAATCTATCACTGTAATATTAACAGCCAAGGTGTGATCTGTCTG
GACATCTTAAAGGACAACTGGAGTCCGGCTTTAACTATTTCTAAAGTTCTCCTCTCCATC
TGCTCACTTCTTACAGATTGCAACCCTGCTGACCCTCTGGTGGGCAGCATCGCCACACAG
TACATGACCAACAGAGCAGAGCATGACCGGATGGCCAGACAGTGGACCAAGCGGTACGCC
ACATAG

Enzyme 44 GenBank Gene ID

AK057886

Enzyme 44 GeneCard ID

UBE2E2

Enzyme 44 GenAtlas ID

UBE2E2

Enzyme 44 HGNC ID

HGNC:12478 Link Image

Enzyme 44 Chromosome Location

Enzyme 44 Locus

3p24.2

Enzyme 44 SNPs

SNPJam Report Link Image

Enzyme 44 General References

Kimura M, Hattori T, Matsuda Y, Yoshioka T, Sumi N, Umeda Y, Nakashima S, Okano Y: cDNA cloning, characterization, and chromosome mapping of UBE2E2 encoding a human ubiquitin-conjugating E2 enzyme. Cytogenet Cell Genet. 1997;78(2):107-11. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]

Enzyme 44 Metabolite References

Not Available

Enzyme 45 [top]

Enzyme 45 ID

5857

Enzyme 45 Name

Adenylosuccinate lyase

Enzyme 45 Synonyms

ASL
Adenylosuccinase
ASase

Enzyme 45 Gene Name

ADSL

Enzyme 45 Protein Sequence

>Adenylosuccinate lyase

MAAGGDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDE
QIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTD
LIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLC
MDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITG
QTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMR
SERCCSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISE
GLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGD
NDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLLKPYESVMKVKA
ELCL

Enzyme 45 Number of Residues

484

Enzyme 45 Molecular Weight

54888.7

Enzyme 45 Theoretical pI

7.12

Enzyme 45 GO Classification

Function
N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity amidine-lyase activity carbon-nitrogen lyase activity catalytic activity lyase activity
Process
cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside phosphate metabolic process nucleotide metabolic process purine nucleotide biosynthetic process purine nucleotide metabolic process purine ribonucleotide biosynthetic process
Component
—

Enzyme 45 General Function

Involved in catalytic activity

Enzyme 45 Specific Function

N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP

Enzyme 45 Pathways

Purine Metabolism (map00230 )

Enzyme 45 Reactions

(1) N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP [RN:R01083]
(2) (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide [RN:R04559]

Enzyme 45 Pfam Domain Function

ADSL_C (PF10397 )
Lyase_1 (PF00206 )

Enzyme 45 Signals

None

Enzyme 45 Transmembrane Regions

None

Enzyme 45 Essentiality

Not Available

Enzyme 45 GenBank ID Protein

28904

Enzyme 45 UniProtKB/Swiss-Prot ID

P30566

Enzyme 45 UniProtKB/Swiss-Prot Entry Name

PUR8_HUMAN Link Image

Enzyme 45 PDB ID

Not Available

Enzyme 45 Cellular Location

Not Available

Enzyme 45 Gene Sequence

>1455 bp

ATGGCGGCTGGAGGCGATCATGGTTCGCCCGACAGCTACCGCTCACCTCTTGCCTCCCGC
TATGCCAGCCCGGAGATGTGCTTCGTGTTTAGCGACAGGTATAAATTCCGGACATGGCGG
CAGCTGTGGCTGTGGCTGGCGGAGGCCGAGCAGACATTGGGTTTGCCTATCACAGATGAA
CAAATCCAGGAGATGAAATCAAACCTGGAGAACATAGACTTCAAGATGGCAGCTGAGGAA
GAGAAACGTTTACGACATGATGTGATGGCTCACGTGCACACATTTGGCCACTGCTGTCCA
AAAGCTGCAGGCATTATTCACCTTGGTGCTACTTCTTGCTATGTTGGAGACAATACTGAC
TTGATTATTCTTAGAAATGCACTTGACCTGCTTTTGCCAAAGCTTGCCAGAGTGATCTCT
CGGCTTGCCGACTTTGCTAAGGAACGAGCCAGTCTACCCACATTAGGTTTCACACATTTC
CAGCCTGCACAGCTGACCACAGTTGGGAAACGTTGCTGTCTTTGGATTCAGGATCTTTGC
ATGGATCTCCAGAACTTGAAGCGTGTCCGAGATGACCTGCGCTTCCGGGGAGTAAAGGGT
ACCACTGGCACTCAGGCCAGTTTCCTGCAGCTCTTTGAGGGAGATGACCATAAGGTAGAG
CAGCTTGACAAGATGGTGACAGAAAAGGCAGGATTTAAGAGAGCTTTCATCATCACAGGG
CAGACATATACACGAAAAGTGGATATTGAAGTACTGTCTGTGCTGGCTAGCTTGGGGGCA
TCAGTGCACAAGATTTGCACCGACATACGCCTCCTGGCAAACCTCAAGGAGATGGAGGAA
CCCTTTGAAAAACAGCAGATTGGCTCAAGTGCGATGCCATATAAGCGGAATCCCATGCGT
TCAGAACGTTGCTGCAGTCTTGCCCGCCACCTGATGACCCTTGTCATGGACCCGCTACAG
ACAGCATCTGTCCAGTGGTTTGAACGCACACTGGATGATAGTGCCAACCGACGGATCTGT
TTGGCCGAGGCATTTCTTACCGCAGATACTATATTGAATACGCTGCAGAACATTTCTGAA
GGATTGGTCGTGTACCCCAAAGTAATTGAACGGCGCATTCGGCAAGAGCTGCCTTTCATG
GCCACAGAGAACATCATCATGGCCATGGTCAAAGCTGGAGGTAGCCGCCAGGATTGCCAT
GAGAAAATCAGAGTGCTTTCTCAGCAGGCAGCTTCTGTGGTTAAGCAGGAAGGGGGTGAC
AATGACCTCATAGAGCGTATCCAGGTTGATGCCTACTTCAGTCCCATTCACTCCCAGTTG
GATCATTTACTGGATCCTTCTTCTTTCACTGGTCGTGCCTCCCAGCAGGTGCAGAGATTC
TTAGAAGAGGAGGTGTATCCCCTGTTAAAACCATATGAAAGCGTGATGAAGGTGAAAGCA
GAATTATGTCTGTAG

Enzyme 45 GenBank Gene ID

X65867

Enzyme 45 GeneCard ID

ADSL

Enzyme 45 GenAtlas ID

ADSL

Enzyme 45 HGNC ID

HGNC:291

Enzyme 45 Chromosome Location

Enzyme 45 Locus

22q13.1|22q13.2

Enzyme 45 SNPs

SNPJam Report Link Image

Enzyme 45 General References

Fon EA, Demczuk S, Delattre O, Thomas G, Rouleau GA: Mapping of the human adenylosuccinate lyase (ADSL) gene to chromosome 22q13.1-->q13.2. Cytogenet Cell Genet. 1993;64(3-4):201-3. [PubMed ]
Kmoch S, Hartmannova H, Stiburkova B, Krijt J, Zikanova M, Sebesta I: Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients. Hum Mol Genet. 2000 Jun 12;9(10):1501-13. [PubMed ]
Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed ]
Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Stone RL, Aimi J, Barshop BA, Jaeken J, Van den Berghe G, Zalkin H, Dixon JE: A mutation in adenylosuccinate lyase associated with mental retardation and autistic features. Nat Genet. 1992 Apr;1(1):59-63. [PubMed ]
Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Maaswinkel-Mooij PD, Laan LA, Onkenhout W, Brouwer OF, Jaeken J, Poorthuis BJ: Adenylosuccinase deficiency presenting with epilepsy in early infancy. J Inherit Metab Dis. 1997 Aug;20(4):606-7. [PubMed ]
Verginelli D, Luckow B, Crifo C, Salerno C, Gross M: Identification of new mutations in the adenylosuccinate lyase gene associated with impaired enzyme activity in lymphocytes and red blood cells. Biochim Biophys Acta. 1998 Feb 27;1406(1):81-4. [PubMed ]
Marie S, Cuppens H, Heuterspreute M, Jaspers M, Tola EZ, Gu XX, Legius E, Vincent MF, Jaeken J, Cassiman JJ, Van den Berghe G: Mutation analysis in adenylosuccinate lyase deficiency: eight novel mutations in the re-evaluated full ADSL coding sequence. Hum Mutat. 1999;13(3):197-202. [PubMed ]
Race V, Marie S, Vincent MF, Van den Berghe G: Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency. Hum Mol Genet. 2000 Sep 1;9(14):2159-65. [PubMed ]
Castro M, Perez-Cerda C, Merinero B, Garcia MJ, Bernar J, Gil Nagel A, Torres J, Bermudez M, Garavito P, Marie S, Vincent F, Van den Berghe G, Ugarte M: Screening for adenylosuccinate lyase deficiency: clinical, biochemical and molecular findings in four patients. Neuropediatrics. 2002 Aug;33(4):186-9. [PubMed ]
Edery P, Chabrier S, Ceballos-Picot I, Marie S, Vincent MF, Tardieu M: Intrafamilial variability in the phenotypic expression of adenylosuccinate lyase deficiency: a report on three patients. Am J Med Genet A. 2003 Jul 15;120A(2):185-90. [PubMed ]

Enzyme 45 Metabolite References

Not Available

Enzyme 46 [top]

Enzyme 46 ID

5858

Enzyme 46 Name

Adenylate kinase isoenzyme 4, mitochondrial

Enzyme 46 Synonyms

ATP-AMP transphosphorylase
Adenylate kinase 3-like

Enzyme 46 Gene Name

AK4

Enzyme 46 Protein Sequence

>Adenylate kinase isoenzyme 4, mitochondrial

MASKLLRAVILGPPGSGKGTVCQRIAQNFGLQHLSSGHFLRENIKASTEVGEMAKQYIEK
SLLVPDHVITRLMMSELENRRGQHWLLDGFPRTLGQAEALDKICEVDLVISLNIPFETLK
DRLSRRWIHPPSGRVYNLDFNPPHVHGIDDVTGEPLVQQEDDKPEAVAARLRQYKDVAKP
VIELYKSRGVLHQFSGTETNKIWPYVYTLFSNKITPIQSKEAY

Enzyme 46 Number of Residues

223

Enzyme 46 Molecular Weight

25267.8

Enzyme 46 Theoretical pI

8.66

Enzyme 46 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding adenylate kinase activity binding catalytic activity kinase activity nucleobase, nucleoside, nucleotide kinase activity nucleoside binding nucleotide kinase activity phosphotransferase activity, phosphate group as acceptor purine nucleoside binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
Component
—

Enzyme 46 General Function

Involved in ATP binding

Enzyme 46 Specific Function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. May also be active with GTP

Enzyme 46 Pathways

Purine Metabolism (map00230 )

Enzyme 46 Reactions

ATP + AMP = 2 ADP [RN:R00127]

Enzyme 46 Pfam Domain Function

ADK (PF00406 )
ADK_lid (PF05191 )

Enzyme 46 Signals

None

Enzyme 46 Transmembrane Regions

None

Enzyme 46 Essentiality

Not Available

Enzyme 46 GenBank ID Protein

189069342

Enzyme 46 UniProtKB/Swiss-Prot ID

P27144

Enzyme 46 UniProtKB/Swiss-Prot Entry Name

KAD4_HUMAN Link Image

Enzyme 46 PDB ID

Not Available

Enzyme 46 Cellular Location

Not Available

Enzyme 46 Gene Sequence

>672 bp

ATGGCTTCCAAACTCCTGCGCGCGGTCATCCTCGGGCCGCCCGGCTCGGGCAAGGGCACC
GTGTGCCAGAGGATCGCCCAGAACTTTGGTCTCCAGCATCTCTCCAGCGGCCACTTCTTG
CGGGAGAACATCAAGGCCAGCACCGAAGTTGGTGAGATGGCAAAGCAGTATATAGAGAAA
AGTCTTTTGGTTCCAGACCATGTGATCACACGCCTAATGATGTCCGAGTTGGAGAACAGG
CGTGGCCAGCACTGGCTCCTTGATGGTTTTCCTAGGACATTAGGACAAGCCGAAGCCCTG
GACAAAATCTGTGAAGTGGATCTAGTGATCAGTTTGAATATTCCATTTGAAACACTTAAA
GATCGTCTCAGCCGCCGTTGGATTCACCCTCCTAGCGGAAGGGTATATAACCTGGACTTC
AATCCACCTCATGTACATGGTATTGATGACGTCACTGGTGAACCATTAGTCCAGCAGGAG
GATGATAAACCCGAAGCAGTTGCTGCCAGGCTAAGACAGTACAAAGACGTGGCAAAGCCA
GTCATTGAATTATACAAGAGCCGAGGAGTGCTCCACCAATTTTCCGGAACGGAGACGAAC
AAAATCTGGCCCTACGTTTACACACTTTTCTCAAACAAGATCACACCTATTCAGTCCAAA
GAAGCATATTGA

Enzyme 46 GenBank Gene ID

AK313611

Enzyme 46 GeneCard ID

AK4

Enzyme 46 GenAtlas ID

AK4

Enzyme 46 HGNC ID

HGNC:363

Enzyme 46 Chromosome Location

Enzyme 46 Locus

1p31.3

Enzyme 46 SNPs

SNPJam Report Link Image

Enzyme 46 General References

Xu G, O'Connell P, Stevens J, White R: Characterization of human adenylate kinase 3 (AK3) cDNA and mapping of the AK3 pseudogene to an intron of the NF1 gene. Genomics. 1992 Jul;13(3):537-42. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 46 Metabolite References

Not Available

Enzyme 47 [top]

Enzyme 47 ID

5859

Enzyme 47 Name

Ubiquitin-conjugating enzyme E2 D2

Enzyme 47 Synonyms

Ubiquitin carrier protein D2
Ubiquitin-conjugating enzyme E2(17)KB 2
Ubiquitin-conjugating enzyme E2-17 kDa 2
Ubiquitin-protein ligase D2

Enzyme 47 Gene Name

UBE2D2

Enzyme 47 Protein Sequence

>Ubiquitin-conjugating enzyme E2 D2

MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDY
PFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLV
PEIARIYKTDREKYNRIAREWTQKYAM

Enzyme 47 Number of Residues

147

Enzyme 47 Molecular Weight

16735.1

Enzyme 47 Theoretical pI

7.96

Enzyme 47 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 47 General Function

Involved in acid-amino acid ligase activity

Enzyme 47 Specific Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP- induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of CHIP and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of TP53/p53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3

Enzyme 47 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 47 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 47 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 47 Signals

None

Enzyme 47 Transmembrane Regions

None

Enzyme 47 Essentiality

Not Available

Enzyme 47 GenBank ID Protein

Not Available

Enzyme 47 UniProtKB/Swiss-Prot ID

P62837

Enzyme 47 UniProtKB/Swiss-Prot Entry Name

UB2D2_HUMAN Link Image

Enzyme 47 PDB ID

1UR6

Enzyme 47 PDB File

Show

Enzyme 47 3D Structure

Enzyme 47 Cellular Location

Not Available

Enzyme 47 Gene Sequence

>444 bp

ATGGCTCTGAAGAGAATCCACAAGGAATTGAATGATCTGGCACGGGACCCTCCAGCACAG
TGTTCAGCAGGTCCTGTTGGAGATGATATGTTCCATTGGCAAGCTACAATAATGGGGCCA
AATGACAGTCCCTATCAGGGTGGAGTATTTTTCTTGACAATTCATTTCCCAACAGATTAC
CCCTTCAAACCACCTAAGGTTGCATTTACAACAAGAATTTATCATCCAAATATTAACAGT
AATGGCAGCATTTGTCTTGATATTCTACGATCACAGTGGTCTCCAGCACTAACTATTTCA
AAAGTACTCTTGTCCATCTGTTCTCTGTTGTGTGATCCCAATCCAGATGATCCTTTAGTG
CCTGAGATTGCTCGGATCTACAAAACAGATAGAGAAAAGTACAACAGAATAGCTCGGGAA
TGGACTCAGAAGTATGCGATGTAA

Enzyme 47 GenBank Gene ID

U39317

Enzyme 47 GeneCard ID

UBE2D2

Enzyme 47 GenAtlas ID

UBE2D2

Enzyme 47 HGNC ID

HGNC:12475 Link Image

Enzyme 47 Chromosome Location

Enzyme 47 Locus

5q31.2

Enzyme 47 SNPs

SNPJam Report Link Image

Enzyme 47 General References

Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM: Identification of a family of closely related human ubiquitin conjugating enzymes. J Biol Chem. 1995 Dec 22;270(51):30408-14. [PubMed ]
Rolfe M, Beer-Romero P, Glass S, Eckstein J, Berdo I, Theodoras A, Pagano M, Draetta G: Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP). Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3264-8. [PubMed ]
Guinn BA, Bland EA, Lodi U, Liggins AP, Tobal K, Petters S, Wells JW, Banham AH, Mufti GJ: Humoral detection of leukaemia-associated antigens in presentation acute myeloid leukaemia. Biochem Biophys Res Commun. 2005 Oct 7;335(4):1293-304. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gonen H, Bercovich B, Orian A, Carrano A, Takizawa C, Yamanaka K, Pagano M, Iwai K, Ciechanover A: Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha. J Biol Chem. 1999 May 21;274(21):14823-30. [PubMed ]
Strack P, Caligiuri M, Pelletier M, Boisclair M, Theodoras A, Beer-Romero P, Glass S, Parsons T, Copeland RA, Auger KR, Benfield P, Brizuela L, Rolfe M: SCF(beta-TRCP) and phosphorylation dependent ubiquitinationof I kappa B alpha catalyzed by Ubc3 and Ubc4. Oncogene. 2000 Jul 20;19(31):3529-36. [PubMed ]
Saville MK, Sparks A, Xirodimas DP, Wardrop J, Stevenson LF, Bourdon JC, Woods YL, Lane DP: Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in vivo. J Biol Chem. 2004 Oct 1;279(40):42169-81. Epub 2004 Jul 26. [PubMed ]
Winkler GS, Albert TK, Dominguez C, Legtenberg YI, Boelens R, Timmers HT: An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair. J Mol Biol. 2004 Mar 12;337(1):157-65. [PubMed ]
Windheim M, Peggie M, Cohen P: Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology. Biochem J. 2008 Feb 1;409(3):723-9. [PubMed ]
Chiang MH, Chen LF, Chen H: Ubiquitin-conjugating enzyme UBE2D2 is responsible for FBXW2 (F-box and WD repeat domain containing 2)-mediated human GCM1 (glial cell missing homolog 1) ubiquitination and degradation. Biol Reprod. 2008 Nov;79(5):914-20. Epub 2008 Aug 13. [PubMed ]
Grou CP, Carvalho AF, Pinto MP, Wiese S, Piechura H, Meyer HE, Warscheid B, Sa-Miranda C, Azevedo JE: Members of the E2D (UbcH5) family mediate the ubiquitination of the conserved cysteine of Pex5p, the peroxisomal import receptor. J Biol Chem. 2008 May 23;283(21):14190-7. Epub 2008 Mar 22. [PubMed ]
Zeng W, Xu M, Liu S, Sun L, Chen ZJ: Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3. Mol Cell. 2009 Oct 23;36(2):315-25. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Zeng W, Sun L, Jiang X, Chen X, Hou F, Adhikari A, Xu M, Chen ZJ: Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell. 2010 Apr 16;141(2):315-30. [PubMed ]
David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
Houben K, Dominguez C, van Schaik FM, Timmers HT, Bonvin AM, Boelens R: Solution structure of the ubiquitin-conjugating enzyme UbcH5B. J Mol Biol. 2004 Nov 19;344(2):513-26. [PubMed ]
Sakata E, Satoh T, Yamamoto S, Yamaguchi Y, Yagi-Utsumi M, Kurimoto E, Tanaka K, Wakatsuki S, Kato K: Crystal structure of UbcH5b~ubiquitin intermediate: insight into the formation of the self-assembled E2~Ub conjugates. Structure. 2010 Jan 13;18(1):138-47. [PubMed ]

Enzyme 47 Metabolite References

Not Available

Enzyme 48 [top]

Enzyme 48 ID

5860

Enzyme 48 Name

DNA ligase 4

Enzyme 48 Synonyms

DNA ligase IV
Polydeoxyribonucleotide synthase [ATP] 4

Enzyme 48 Gene Name

LIG4

Enzyme 48 Protein Sequence

>DNA ligase 4

MAASQTSQTVASHVPFADLCSTLERIQKSKGRAEKIRHFREFLDSWRKFHDALHKNHKDV
TDSFYPAMRLILPQLERERMAYGIKETMLAKLYIELLNLPRDGKDALKLLNYRTPTGTHG
DAGDFAMIAYFVLKPRCLQKGSLTIQQVNDLLDSIASNNSAKRKDLIKKSLLQLITQSSA
LEQKWLIRMIIKDLKLGVSQQTIFSVFHNDAAELHNVTTDLEKVCRQLHDPSVGLSDISI
TLFSAFKPMLAAIADIEHIEKDMKHQSFYIETKLDGERMQMHKDGDVYKYFSRNGYNYTD
QFGASPTEGSLTPFIHNAFKADIQICILDGEMMAYNPNTQTFMQKGTKFDIKRMVEDSDL
QTCYCVFDVLMVNNKKLGHETLRKRYEILSSIFTPIPGRIEIVQKTQAHTKNEVIDALNE
AIDKREEGIMVKQPLSIYKPDKRGEGWLKIKPEYVSGLMDELDILIVGGYWGKGSRGGMM
SHFLCAVAEKPPPGEKPSVFHTLSRVGSGCTMKELYDLGLKLAKYWKPFHRKAPPSSILC
GTEKPEVYIEPCNSVIVQIKAAEIVPSDMYKTGCTLRFPRIEKIRDDKEWHECMTLDDLE
QLRGKASGKLASKHLYIGGDDEPQEKKRKAAPKMKKVIGIIEHLKAPNLTNVNKISNIFE
DVEFCVMSGTDSQPKPDLENRIAEFGGYIVQNPGPDTYCVIAGSENIRVKNIILSNKHDV
VKPAWLLECFKTKSFVPWQPRFMIHMCPSTKEHFAREYDCYGDSYFIDTDLNQLKEVFSG
IKNSNEQTPEEMASLIADLEYRYSWDCSPLSMFRRHTVYLDSYAVINDLSTKNEGTRLAI
KALELRFHGAKVVSCLAEGVSHVIIGEDHSRVADFKAFRRTFKRKFKILKESWVTDSIDK
CELQEENQYLI

Enzyme 48 Number of Residues

911

Enzyme 48 Molecular Weight

103969.9

Enzyme 48 Theoretical pI

8.04

Enzyme 48 GO Classification

Function
ATP binding DNA binding DNA ligase (ATP) activity DNA ligase (ATP) activity DNA ligase (ATP) activity DNA ligase (ATP) activity DNA ligase activity adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity ligase activity ligase activity, forming phosphoric ester bonds nucleic acid binding nucleoside binding purine nucleoside binding
Process
DNA ligation DNA ligation involved in DNA repair DNA metabolic process DNA recombination DNA repair DNA replication cellular macromolecule metabolic process macromolecule metabolic process metabolic process
Component
cell part intracellular

Enzyme 48 General Function

Involved in DNA ligase (ATP) activity

Enzyme 48 Specific Function

Efficiently joins single-strand breaks in a double- stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA- dependent protein kinase complex DNA-PK to these DNA ends

Enzyme 48 Pathways

Not Available

Enzyme 48 Reactions

ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = AMP + diphosphate + (deoxyribonucleotide)n+m [RN:R00381]

Enzyme 48 Pfam Domain Function

BRCT (PF00533 )
DNA_ligase_A_C (PF04679 )
DNA_ligase_A_M (PF01068 )
DNA_ligase_A_N (PF04675 )
DNA_ligase_IV (PF11411 )

Enzyme 48 Signals

None

Enzyme 48 Transmembrane Regions

None

Enzyme 48 Essentiality

Not Available

Enzyme 48 GenBank ID Protein

148539894

Enzyme 48 UniProtKB/Swiss-Prot ID

P49917

Enzyme 48 UniProtKB/Swiss-Prot Entry Name

DNLI4_HUMAN Link Image

Enzyme 48 PDB ID

Not Available

Enzyme 48 Cellular Location

Not Available

Enzyme 48 Gene Sequence

>2736 bp

ATGGCTGCCTCACAAACTTCACAAACTGTTGCATCTCACGTTCCTTTTGCAGATTTGTGT
TCAACTTTAGAACGAATACAGAAAAGTAAAGGACGTGCAGAAAAAATCAGACACTTCAGG
GAATTTTTAGATTCTTGGAGAAAATTTCATGATGCTCTTCATAAGAACCACAAAGATGTC
ACAGACTCTTTTTATCCAGCAATGAGACTAATTCTTCCTCAGCTAGAAAGAGAGAGAATG
GCCTATGGAATTAAAGAAACTATGCTTGCTAAGCTTTATATTGAGTTGCTTAATTTACCT
AGAGATGGAAAAGATGCCCTCAAACTTTTAAACTACAGAACACCCACTGGAACTCATGGA
GATGCTGGAGACTTTGCAATGATTGCATATTTTGTGTTGAAGCCAAGATGTTTACAGAAA
GGAAGTTTAACCATACAGCAAGTAAACGACCTTTTAGACTCAATTGCCAGCAATAATTCT
GCTAAAAGAAAAGACCTAATAAAAAAGAGCCTTCTTCAACTTATAACTCAGAGTTCAGCA
CTTGAGCAAAAGTGGCTTATACGGATGATCATAAAGGATTTAAAGCTTGGTGTTAGTCAG
CAAACTATCTTTTCTGTTTTTCATAATGATGCTGCTGAGTTGCATAATGTCACTACAGAT
CTGGAAAAAGTCTGTAGGCAACTGCATGATCCTTCTGTAGGACTCAGTGATATTTCTATC
ACTTTATTTTCTGCATTTAAACCAATGCTAGCTGCTATTGCAGATATTGAGCACATTGAG
AAGGATATGAAACATCAGAGTTTCTACATAGAAACCAAGCTAGATGGTGAACGTATGCAA
ATGCACAAAGATGGAGATGTATATAAATACTTCTCTCGAAATGGATATAACTACACTGAT
CAGTTTGGTGCTTCTCCTACTGAAGGTTCTCTTACCCCATTCATTCATAATGCATTCAAA
GCAGATATACAAATCTGTATTCTTGATGGTGAGATGATGGCCTATAATCCTAATACACAA
ACTTTCATGCAAAAGGGAACTAAGTTTGATATTAAAAGAATGGTAGAGGATTCTGATCTG
CAAACTTGTTATTGTGTTTTTGATGTATTGATGGTTAATAATAAAAAGCTAGGGCATGAG
ACTCTGAGAAAGAGGTATGAGATTCTTAGTAGTATTTTTACACCAATTCCAGGTAGAATA
GAAATAGTGCAGAAAACACAAGCTCATACTAAGAATGAAGTAATTGATGCATTGAATGAA
GCAATAGATAAAAGAGAAGAGGGAATTATGGTAAAACAACCTCTATCCATCTACAAGCCA
GACAAAAGAGGTGAAGGGTGGTTAAAAATTAAACCAGAGTATGTCAGTGGACTAATGGAT
GAATTGGACATTTTAATTGTTGGAGGATATTGGGGTAAAGGATCACGGGGTGGAATGATG
TCTCATTTTCTGTGTGCAGTAGCAGAGAAGCCCCCTCCTGGTGAGAAGCCATCTGTGTTT
CATACTCTCTCTCGTGTTGGGTCTGGCTGCACCATGAAAGAACTGTATGATCTGGGTTTG
AAATTGGCCAAGTATTGGAAGCCTTTTCATAGAAAAGCTCCACCAAGCAGCATTTTATGT
GGAACAGAGAAGCCAGAAGTATACATTGAACCTTGTAATTCTGTCATTGTTCAGATTAAA
GCAGCAGAGATCGTACCCAGTGATATGTATAAAACTGGCTGCACCTTGCGTTTTCCACGA
ATTGAAAAGATAAGAGATGACAAGGAGTGGCATGAGTGCATGACCCTGGACGACCTAGAA
CAACTTAGGGGGAAGGCATCTGGTAAGCTCGCATCTAAACACCTTTATATAGGTGGTGAT
GATGAACCACAAGAAAAAAAGCGGAAAGCTGCCCCAAAGATGAAGAAAGTTATTGGAATT
ATTGAGCACTTAAAAGCACCTAACCTTACTAACGTTAACAAAATTTCTAATATATTTGAA
GATGTAGAGTTTTGTGTTATGAGTGGAACAGATAGCCAGCCAAAGCCTGACCTGGAGAAC
AGAATTGCAGAATTTGGTGGTTATATAGTACAAAATCCAGGCCCAGACACGTACTGTGTA
ATTGCAGGGTCTGAGAACATCAGAGTGAAAAACATAATTTTGTCAAATAAACATGATGTT
GTCAAGCCTGCATGGCTTTTAGAATGTTTTAAGACCAAAAGCTTTGTACCATGGCAGCCT
CGCTTTATGATTCATATGTGCCCATCAACCAAAGAACATTTTGCCCGTGAATATGATTGC
TATGGTGATAGTTATTTCATTGATACAGACTTGAACCAACTGAAGGAAGTATTCTCAGGA
ATTAAAAATTCTAACGAGCAGACTCCTGAAGAAATGGCTTCTCTGATTGCTGATTTAGAA
TATCGGTATTCCTGGGATTGCTCTCCTCTCAGTATGTTTCGACGCCACACCGTTTATTTG
GACTCGTATGCTGTTATTAATGACCTGAGTACCAAAAATGAGGGGACAAGGTTAGCTATT
AAAGCCTTGGAGCTTCGGTTTCATGGAGCAAAAGTAGTTTCTTGTTTAGCTGAGGGAGTG
TCTCATGTAATAATTGGGGAAGATCATAGTCGTGTTGCAGATTTTAAAGCTTTTAGAAGA
ACTTTTAAGAGAAAGTTTAAAATCCTAAAAGAAAGTTGGGTAACTGATTCAATAGACAAG
TGTGAATTACAAGAAGAAAACCAGTATTTGATTTAA

Enzyme 48 GenBank Gene ID

NM_001098268.1 Link Image

Enzyme 48 GeneCard ID

LIG4

Enzyme 48 GenAtlas ID

LIG4

Enzyme 48 HGNC ID

HGNC:6601

Enzyme 48 Chromosome Location

Enzyme 48 Locus

13q33-q34

Enzyme 48 SNPs

SNPJam Report Link Image

Enzyme 48 General References

Wei YF, Robins P, Carter K, Caldecott K, Pappin DJ, Yu GL, Wang RP, Shell BK, Nash RA, Schar P, et al.: Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination. Mol Cell Biol. 1995 Jun;15(6):3206-16. [PubMed ]
Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Robins P, Lindahl T: DNA ligase IV from HeLa cell nuclei. J Biol Chem. 1996 Sep 27;271(39):24257-61. [PubMed ]
Grawunder U, Zimmer D, Fugmann S, Schwarz K, Lieber MR: DNA ligase IV is essential for V(D)J recombination and DNA double-strand break repair in human precursor lymphocytes. Mol Cell. 1998 Oct;2(4):477-84. [PubMed ]
Critchlow SE, Bowater RP, Jackson SP: Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV. Curr Biol. 1997 Aug 1;7(8):588-98. [PubMed ]
Chen L, Trujillo K, Sung P, Tomkinson AE: Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase. J Biol Chem. 2000 Aug 25;275(34):26196-205. [PubMed ]
Calsou P, Delteil C, Frit P, Drouet J, Salles B: Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein kinase on DNA ends is necessary for XRCC4-ligase IV recruitment. J Mol Biol. 2003 Feb 7;326(1):93-103. [PubMed ]
Kanno S, Kuzuoka H, Sasao S, Hong Z, Lan L, Nakajima S, Yasui A: A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. EMBO J. 2007 Apr 18;26(8):2094-103. Epub 2007 Mar 29. [PubMed ]
Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L: Crystal structure of an Xrcc4-DNA ligase IV complex. Nat Struct Biol. 2001 Dec;8(12):1015-9. [PubMed ]
Riballo E, Critchlow SE, Teo SH, Doherty AJ, Priestley A, Broughton B, Kysela B, Beamish H, Plowman N, Arlett CF, Lehmann AR, Jackson SP, Jeggo PA: Identification of a defect in DNA ligase IV in a radiosensitive leukaemia patient. Curr Biol. 1999 Jul 1;9(13):699-702. [PubMed ]
Riballo E, Doherty AJ, Dai Y, Stiff T, Oettinger MA, Jeggo PA, Kysela B: Cellular and biochemical impact of a mutation in DNA ligase IV conferring clinical radiosensitivity. J Biol Chem. 2001 Aug 17;276(33):31124-32. Epub 2001 May 10. [PubMed ]
O'Driscoll M, Cerosaletti KM, Girard PM, Dai Y, Stumm M, Kysela B, Hirsch B, Gennery A, Palmer SE, Seidel J, Gatti RA, Varon R, Oettinger MA, Neitzel H, Jeggo PA, Concannon P: DNA ligase IV mutations identified in patients exhibiting developmental delay and immunodeficiency. Mol Cell. 2001 Dec;8(6):1175-85. [PubMed ]
Roddam PL, Rollinson S, O'Driscoll M, Jeggo PA, Jack A, Morgan GJ: Genetic variants of NHEJ DNA ligase IV can affect the risk of developing multiple myeloma, a tumour characterised by aberrant class switch recombination. J Med Genet. 2002 Dec;39(12):900-5. [PubMed ]
van der Burg M, van Veelen LR, Verkaik NS, Wiegant WW, Hartwig NG, Barendregt BH, Brugmans L, Raams A, Jaspers NG, Zdzienicka MZ, van Dongen JJ, van Gent DC: A new type of radiosensitive T-B-NK+ severe combined immunodeficiency caused by a LIG4 mutation. J Clin Invest. 2006 Jan;116(1):137-45. Epub 2005 Dec 15. [PubMed ]

Enzyme 48 Metabolite References

Not Available

Enzyme 49 [top]

Enzyme 49 ID

5863

Enzyme 49 Name

Arginyl-tRNA synthetase, cytoplasmic

Enzyme 49 Synonyms

Arginine--tRNA ligase
ArgRS

Enzyme 49 Gene Name

RARS

Enzyme 49 Protein Sequence

>Arginyl-tRNA synthetase, cytoplasmic

MDVLVSECSARLLQQEEEIKSLTAEIDRLKNCGCLGASPNLEQLQEENLKLKYRLNILRK
SLQAERNKPTKNMINIISRLQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDYQCNSAMG
ISQMLKTKEQKVNPREIAENITKHLPDNECIEKVEIAGPGFINVHLRKDFVSEQLTSLLV
NGVQLPALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGD
WGTQFGMLIAHLQDKFPDYLTVSPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGK
NPDITKAWKLICDVSRQELNKIYDALDVSLIERGESFYQDRMNDIVKEFEDRGFVQVDDG
RKIVFVPGCSIPLTIVKSDGGYTYDTSDLAAIKQRLFEEKADMIIYVVDNGQSVHFQTIF
AAAQMIGWYDPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRSMDKLKEK
ERDKVLTAEELNAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTR
IRSIARLANIDEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDY
IYELATAFTEFYDSCYCVEKDRQTGKILKVNMWRMLLCEAVAAVMAKGFDILGIKPVQRM

Enzyme 49 Number of Residues

660

Enzyme 49 Molecular Weight

75378.3

Enzyme 49 Theoretical pI

6.65

Enzyme 49 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity arginine-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process arginyl-tRNA aminoacylation biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 49 General Function

Involved in nucleotide binding

Enzyme 49 Specific Function

Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1

Enzyme 49 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Arginine and Proline Metabolism (map00330 )

Enzyme 49 Reactions

ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg [RN:R03646]

Enzyme 49 Pfam Domain Function

Arg_tRNA_synt_N (PF03485 )
DALR_1 (PF05746 )
tRNA-synt_1d (PF00750 )

Enzyme 49 Signals

None

Enzyme 49 Transmembrane Regions

None

Enzyme 49 Essentiality

Not Available

Enzyme 49 GenBank ID Protein

62897153

Enzyme 49 UniProtKB/Swiss-Prot ID

P54136

Enzyme 49 UniProtKB/Swiss-Prot Entry Name

SYRC_HUMAN Link Image

Enzyme 49 PDB ID

Not Available

Enzyme 49 Cellular Location

Not Available

Enzyme 49 Gene Sequence

>1983 bp

ATGGACGTACTGGTGTCTGAGTGCTCCGCGCGGCTGCTGCAGCAGGAAGAAGAGATTAAA
TCTCTGACTGCTGAAATTGACCGGTTGAAAAACTGTGGCTGTTTAGGAGCTTCTCCAAAT
TTGGAGCAGTTACAAGAAGAAAATTTAAAATTAAAGTATCGACTGAATATTCTTCGAAAG
AGTCTTCAGGCAGAAAGGAACAAACCAACTAAAAATATGATTAACATTATTAGCCGCCTA
CAAGAGGTCTTTGGTCATGCAATTAAGGCTGCATATCCAGATTTGGAAAATCCTCCTCTG
CTAGTGACACCAAGTCAGCAGGCCAAGTTTGGGGACTATCAGTGTAATAGTGCTATGGGT
ATTTCTCAGATGCTCAAAACCAAGGAACAGAAAGTTAATCCAAGAGAAATTGCTGAAAAC
ATTACCAAACACCTCCCAGACAATGAATGTATTGAAAAAGTTGAAATTGCTGGTCCTGGT
TTTATTAATGTCCACTTAAGAAAGGATTTTGTATCAGAACAATTGACCAGTCTTCTAGTG
AATGGAGTTCAACTACCTGCTCTGGGAGAGAATAAAAAGGTTATAGTTGACTTTTCCTCC
CCTAATATAGCTAAAGAGATGCATGTAGGCCACCTGAGGTCAACTATCATAGGAGAGAGT
ATAAGCCGCCTCTTTGAATTTGCAGGGTATGACGTGCTCAGGTTAAATCATGTAGGAGAC
TGGGGGACCCAGTTTGGCATGCTCATCGCTCACCTGCAAGACAAATTTCCAGATTATCTA
ACAGTTTCACCTCCTATTGGGGATCTTCAGGTCTTTTATAAGGAATCTAAGAAGAGGTTT
GATACTGAGGAGGAATTTAAGAAGCGAGCATATCAGTGTGTAGTTCTGCTCCAGGGTAAA
AACCCAGATATTACAAAAGCTTGGAAGCTTATCTGTGATGTCTCCCGCCAAGAGTTAAAT
AAAATCTATGATGCATTGGACGTCTCTTTAATAGAGAGAGGGGAATCCTTCTATCAAGAT
GGGATGAATGATATTGTAAAGGAATTTGAAGATAGAGGATTTGTGCAGGTGGATGATGGC
AGAAAGATTGTATTTGTCCCAGGGTGTTCCATACCATTAACCATAGTAAAATCAGATGGA
GGTTATACCTATGATACATCTGACCTGGCTGCTATTAAACAAAGACTATTTGAGGAAAAA
GCAGATATGATTATCTATGTTGTGGACAATGGACAATCTGTGCACTTCCAGACAATATTT
GCTGCTGCTCAAATGATTGGTTGGTATGACCCTAAAGTAACTCGAGTCTTCCATGCTGGA
TTTGGTGTGGTGCTAGGGGAAGACAAGAAAAAGTTTAAAACACGTTCGGGTGAAACAGTG
CGCCTCATGGATCTTCTGGGAGAAGGACTAAAACGATCCATGGACAAGTTGAAGGAAAAA
GAAAGAGACAAGGTCTTAGCTGCAGAGGAATTGAATGCTGCTCAGACATCCGTTGCGTAT
GGCTGCATCAAATATGCTGACCTTTCCCATAACCGGTTGAATGACTACATCTTCTCCTTT
GACAAAATGCTAGATGACAGAGGAAATACAGCTGCTTACTTGTTGTATGCCTTCACTAGA
ATCAGGTCTATTGCACGTCTGGCCAATATTGATGAAGAAATGCTCCAAAAAGCTGCTCGA
GAAACCAAGATTCTTTTGGATCATGAGAAGGAATGGAAACTAGGCCGGTGCATTTTACGG
TTCCCTGAGATTCTGCAAAAGATTTTAGATGACTTATTTCTCCACACTCTCTGTGATTAT
ATATATGAGCTGGCAACTGCTTTCACAGAGTTCTATGATAGCTGCTACTGTGTGGAGAAA
GATAGACAGACTGGAAAAATATTGAAGGTGAACATGTGGCGTATGCTGCTATGTGAAGCA
GTAGCTGCTGTCATGGCCAAGGGGTTTGATATCCTGGGAATAAAACCTGTCCAAAGGATG
TAA

Enzyme 49 GenBank Gene ID

AK222797

Enzyme 49 GeneCard ID

RARS

Enzyme 49 GenAtlas ID

RARS

Enzyme 49 HGNC ID

HGNC:9870

Enzyme 49 Chromosome Location

Enzyme 49 Locus

5q35.1

Enzyme 49 SNPs

SNPJam Report Link Image

Enzyme 49 General References

Girjes AA, Hobson K, Chen P, Lavin MF: Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase. Gene. 1995 Oct 27;164(2):347-50. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
Park SG, Jung KH, Lee JS, Jo YJ, Motegi H, Kim S, Shiba K: Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase. J Biol Chem. 1999 Jun 11;274(24):16673-6. [PubMed ]
Ling C, Yao YN, Zheng YG, Wei H, Wang L, Wu XF, Wang ED: The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex. J Biol Chem. 2005 Oct 14;280(41):34755-63. Epub 2005 Jul 29. [PubMed ]
Zheng YG, Wei H, Ling C, Xu MG, Wang ED: Two forms of human cytoplasmic arginyl-tRNA synthetase produced from two translation initiations by a single mRNA. Biochemistry. 2006 Jan 31;45(4):1338-44. [PubMed ]
Bottoni A, Vignali C, Piccin D, Tagliati F, Luchin A, Zatelli MC, Uberti EC: Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines. J Cell Physiol. 2007 Aug;212(2):293-7. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 49 Metabolite References

Not Available

Enzyme 50 [top]

Enzyme 50 ID

5864

Enzyme 50 Name

GMP synthase [glutamine-hydrolyzing]

Enzyme 50 Synonyms

GMP synthetase
Glutamine amidotransferase

Enzyme 50 Gene Name

GMPS

Enzyme 50 Protein Sequence

>GMP synthase [glutamine-hydrolyzing]

MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE

Enzyme 50 Number of Residues

693

Enzyme 50 Molecular Weight

76714.8

Enzyme 50 Theoretical pI

6.86

Enzyme 50 GO Classification

Function
ATP binding GMP synthase (glutamine-hydrolyzing) activity GMP synthase (glutamine-hydrolyzing) activity adenyl nucleotide binding adenyl ribonucleotide binding binding carbon-nitrogen ligase activity, with glutamine as amido-N-donor catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds nucleoside binding purine nucleoside binding
Process
GMP biosynthetic process biosynthetic process cellular amino acid and derivative metabolic process cellular amino acid metabolic process cellular metabolic process cellular nitrogen compound metabolic process glutamine family amino acid metabolic process glutamine metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside phosphate metabolic process nucleotide metabolic process purine nucleoside monophosphate biosynthetic process purine nucleotide biosynthetic process purine nucleotide metabolic process purine ribonucleoside monophosphate biosynthetic process
Component
—

Enzyme 50 General Function

Involved in catalytic activity

Enzyme 50 Specific Function

Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division

Enzyme 50 Pathways

Glutamate Metabolism (map00251 )
Purine Metabolism (map00230 )

Enzyme 50 Reactions

ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate [RN:R01231]

Enzyme 50 Pfam Domain Function

GATase (PF00117 )
GMP_synt_C (PF00958 )
NAD_synthase (PF02540 )

Enzyme 50 Signals

None

Enzyme 50 Transmembrane Regions

None

Enzyme 50 Essentiality

Not Available

Enzyme 50 GenBank ID Protein

Not Available

Enzyme 50 UniProtKB/Swiss-Prot ID

P49915

Enzyme 50 UniProtKB/Swiss-Prot Entry Name

GUAA_HUMAN Link Image

Enzyme 50 PDB ID

Not Available

Enzyme 50 Cellular Location

Not Available

Enzyme 50 Gene Sequence

>2082 bp

ATGGCTCTGTGCAACGGAGACTCCAAGCTGGAGAATGCTGGAGGAGACCTTAAGGATGGC
CACCACCACTATGAAGGAGCTGTTGTCATTCTGGATGCTGGTGCTCAGTACGGGAAAGTC
ATAGACCGAAGAGTGAGGGAACTGTTCGTGCAGTCTGAAATTTTCCCCTTGGAAACACCA
GCATTTGCTATAAAGGAACAAGGATTCCGTGCTATTATCATCTCTGGAGGACCTAATTCT
GTGTATGCTGAAGATGCTCCCTGGTTTGATCCAGCAATATTCACTATTGGCAAGCCTGTT
CTTGGAATTTGCTATGGTATGCAGATGATGAATAAGGTATTTGGAGGTACTGTGCACAAA
AAAAGTGTCAGAGAAGATGGAGTTTTCAACATTAGTGTGGATAATACATGTTCATTATTC
AGGGGCCTTCAGAAGGAAGAAGTTGTTTTGCTTACACATGGAGATAGTGTAGACAAAGTA
GCTGATGGATTCAAGGTTGTGGCACGTTCTGGAAACATAGTAGCAGGCATAGCAAATGAA
TCTAAAAAGTTATATGGAGCACAGTTCCACCCTGAAGTTGGCCTTACAGAAAATGGAAAA
GTAATACTGAAGAATTTCCTTTATGATATAGCTGGATGCAGTGGAACCTTCACCGTGCAG
AACAGAGAACTTGAGTGTATTCGAGAGATCAAAGAGAGAGTAGGCACGTCAAAAGTTTTG
GTTTTACTCAGTGGTGGAGTAGACTCAACAGTTTGTACAGCTTTGCTAAATCGTGCTTTG
AACCAAGAACAAGTCATTGCTGTGCACATTGATAATGGCTTTATGAGAAAACGAGAAAGC
CAGTCTGTTGAAGAGGCCCTCAAAAAGCTTGGAATTCAGGTCAAAGTGATAAATGCTGCT
CATTCTTTCTACAATGGAACAACAACCCTACCAATATCAGATGAAGATAGAACCCCACGG
AAAAGAATTAGCAAAACGTTAAATATGACCACAAGTCCTGAAGAGAAAAGAAAAATCATT
GGGGATACTTTTGTTAAGATTGCCAATGAAGTAATTGGAGAAATGAACTTGAAACCAGAG
GAGGTTTTCCTTGCCCAAGGTACTTTACGGCCTGATCTAATTGAAAGTGCATCCCTTGTT
GCAAGTGGCAAAGCTGAACTCATCAAAACCCATCACAATGACACAGAGCTCATCAGAAAG
TTGAGAGAGGAGGGAAAAGTAATAGAACCTCTGAAAGATTTTCATAAAGATGAAGTGAGA
ATTTTGGGCAGAGAACTTGGACTTCCAGAAGAGTTAGTTTCCAGGCATCCATTTCCAGGT
CCTGGCCTGGCAATCAGAGTAATATGTGCTGAAGAACCTTATATTTGTAAGGACTTTCCT
GAAACCAACAATATTTTGAAAATAGTAGCTGATTTTTCTGCAAGTGTTAAAAAGCCACAT
ACCCTATTACAGAGAGTCAAAGCCTGCACAACAGAAGAGGATCAGGAGAAGCTGATGCAA
ATTACCAGTCTGCATTCACTGAATGCCTTCTTGCTGCCAATTAAAACTGTAGGTGTGCAG
GGTGACTGTCGTTCCTACAGTTACGTGTGTGGAATCTCCAGTAAAGATGAACCTGACTGG
GAATCACTTATTTTTCTGGCTAGGCTTATACCTCGCATGTGTCACAACGTTAACAGAGTT
GTTTATATATTTGGCCCACCAGTTAAAGAACCTCCTACAGATGTTACTCCCACTTTCTTG
ACAACAGGGGTGCTCAGTACTTTACGCCAAGCTGATTTTGAGGCCCATAACATTCTCAGG
GAGTCTGGGTATGCTGGGAAAATCAGCCAGATGCCGGTGATTTTGACACCATTACATTTT
GATCGGGACCCACTTCAAAAGCAGCCTTCATGCCAGAGATCTGTGGTTATTCGAACCTTT
ATTACTAGTGACTTCATGACTGGTATACCTGCAACACCTGGCAATGAGATCCCTGTAGAG
GTGGTATTAAAGATGGTCACTGAGATTAAGAAGATTCCTGGTATTTCTCGAATTATGTAT
GACTTAACATCAAAGCCCCCAGGAACTACTGAGTGGGAGTAA

Enzyme 50 GenBank Gene ID

U10860

Enzyme 50 GeneCard ID

GMPS

Enzyme 50 GenAtlas ID

GMPS

Enzyme 50 HGNC ID

HGNC:4378

Enzyme 50 Chromosome Location

Enzyme 50 Locus

3q24

Enzyme 50 SNPs

SNPJam Report Link Image

Enzyme 50 General References

Hirst M, Haliday E, Nakamura J, Lou L: Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA. J Biol Chem. 1994 Sep 23;269(38):23830-7. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Pegram LD, Megonigal MD, Lange BJ, Nowell PC, Rowley JD, Rappaport EF, Felix CA: t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (GUANOSINE 5' MONOPHOSPHATE SYNTHETASE) gene. Blood. 2000 Dec 15;96(13):4360-2. [PubMed ]
Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 50 Metabolite References

Not Available

Enzyme 51 [top]

Enzyme 51 ID

5865

Enzyme 51 Name

Ubiquitin-conjugating enzyme E2 E3

Enzyme 51 Synonyms

UbcH9
Ubiquitin carrier protein E3
Ubiquitin-conjugating enzyme E2-23 kDa
Ubiquitin-protein ligase E3

Enzyme 51 Gene Name

UBE2E3

Enzyme 51 Protein Sequence

>Ubiquitin-conjugating enzyme E2 E3

MSSDRQRSDDESPSTSSGSSDADQRDPAAPEPEEQEERKPSATQQKKNTKLSSKTTAKLS
TSAKRIQKELAEITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFSSDY
PFKPPKVTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLV
GSIATQYLTNRAEHDRIARQWTKRYAT

Enzyme 51 Number of Residues

207

Enzyme 51 Molecular Weight

22912.3

Enzyme 51 Theoretical pI

7.25

Enzyme 51 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 51 General Function

Involved in acid-amino acid ligase activity

Enzyme 51 Specific Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest

Enzyme 51 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 51 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 51 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 51 Signals

None

Enzyme 51 Transmembrane Regions

None

Enzyme 51 Essentiality

Not Available

Enzyme 51 GenBank ID Protein

Not Available

Enzyme 51 UniProtKB/Swiss-Prot ID

Q969T4

Enzyme 51 UniProtKB/Swiss-Prot Entry Name

UB2E3_HUMAN Link Image

Enzyme 51 PDB ID

1Y6L

Enzyme 51 PDB File

Show

Enzyme 51 3D Structure

Enzyme 51 Cellular Location

Not Available

Enzyme 51 Gene Sequence

>624 bp

ATGTCCAGTGATAGGCAAAGGTCCGATGATGAGAGCCCCAGCACCAGCAGTGGCAGTTCA
GATGCGGACCAGCGAGACCCAGCCGCTCCAGAGCCTGAAGAACAAGAGGAAAGAAAACCT
TCTGCCACCCAGCAGAAGAAAAACACCAAACTCTCTAGCAAAACCACTGCTAAGTTATCC
ACTAGTGCTAAAAGAATTCAGAAGGAGCTAGCTGAAATAACCCTTGATCCTCCTCCTAAT
TGCAGTGCTGGGCCTAAAGGAGATAACATTTATGAATGGAGATCAACTATACTTGGTCCA
CCGGGTTCTGTATATGAAGGTGGTGTGTTTTTTCTGGATATCACATTTTCATCAGATTAT
CCATTTAAGCCACCAAAGGTTACTTTCCGCACCAGAATCTATCACTGCAACATCAACAGT
CAGGGAGTCATCTGTCTGGACATCCTTAAAGACAACTGGAGTCCCGCTTTGACTATTTCA
AAGGTTTTGCTGTCTATTTGTTCCCTTTTGACAGACTGCAACCCTGCGGATCCTCTGGTT
GGAAGCATAGCCACTCAGTATTTGACCAACAGAGCAGAACACGACAGGATAGCCAGACAG
TGGACCAAGAGATACGCAACATAA

Enzyme 51 GenBank Gene ID

AB017644

Enzyme 51 GeneCard ID

UBE2E3

Enzyme 51 GenAtlas ID

UBE2E3

Enzyme 51 HGNC ID

HGNC:12479 Link Image

Enzyme 51 Chromosome Location

Enzyme 51 Locus

2q32.1

Enzyme 51 SNPs

SNPJam Report Link Image

Enzyme 51 General References

Ito K, Kato S, Matsuda Y, Kimura M, Okano Y: cDNA cloning, characterization, and chromosome mapping of UBE2E3 (alias UbcH9), encoding an N-terminally extended human ubiquitin-conjugating enzyme. Cytogenet Cell Genet. 1999;84(1-2):99-104. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Plafker SM, Plafker KS, Weissman AM, Macara IG: Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import. J Cell Biol. 2004 Nov 22;167(4):649-59. Epub 2004 Nov 15. [PubMed ]
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]

Enzyme 51 Metabolite References

Not Available

Enzyme 52 [top]

Enzyme 52 ID

5867

Enzyme 52 Name

Ubiquitin-conjugating enzyme E2 B

Enzyme 52 Synonyms

RAD6 homolog B
HR6B
hHR6B
Ubiquitin carrier protein B
Ubiquitin-conjugating enzyme E2-17 kDa
Ubiquitin-protein ligase B

Enzyme 52 Gene Name

UBE2B

Enzyme 52 Protein Sequence

>Ubiquitin-conjugating enzyme E2 B

MSTPARRRLMRDFKRLQEDPPVGVSGAPSENNIMQWNAVIFGPEGTPFEDGTFKLVIEFS
EEYPNKPPTVRFLSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNS
PANSQAAQLYQENKREYEKRVSAIVEQSWNDS

Enzyme 52 Number of Residues

152

Enzyme 52 Molecular Weight

17312.2

Enzyme 52 Theoretical pI

4.64

Enzyme 52 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 52 General Function

Involved in ATP binding

Enzyme 52 Specific Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'-, as well as 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. May be involved in neurite outgrowth

Enzyme 52 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 52 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 52 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 52 Signals

None

Enzyme 52 Transmembrane Regions

None

Enzyme 52 Essentiality

Not Available

Enzyme 52 GenBank ID Protein

Not Available

Enzyme 52 UniProtKB/Swiss-Prot ID

P63146

Enzyme 52 UniProtKB/Swiss-Prot Entry Name

UBE2B_HUMAN Link Image

Enzyme 52 PDB ID

1JAS

Enzyme 52 PDB File

Show

Enzyme 52 3D Structure

Enzyme 52 Cellular Location

Not Available

Enzyme 52 Gene Sequence

>459 bp

ATGTCGACCCCGGCCCGGAGGAGGCTCATGCGGGATTTCAAGCGGTTACAAGAGGACCCA
CCTGTGGGTGTCAGTGGCGCACCATCTGAAAACAACATCATGCAGTGGAATGCAGTTATA
TTTGGACCAGAAGGGACACCTTTTGAAGATGGTACTTTTAAACTAGTAATAGAATTTTCT
GAAGAATATCCAAATAAACCACCAACTGTTAGGTTTTTATCCAAAATGTTTCATCCAAAT
GTGTATGCTGATGGTAGCATATGTTTAGATATCCTTCAGAATCGATGGAGTCCAACATAT
GATGTATCTTCTATCTTAACATCAATTCAGTCTCTGCTGGATGAACCGAATCCTAACAGT
CCAGCCAATAGCCAGGCAGCACAGCTTTATCAGGAAAACAAACGAGAATATGAGAAAAGA
GTTTCGGCCATTGTTGAACAAAGCTGGAATGATTCATAA

Enzyme 52 GenBank Gene ID

M74525

Enzyme 52 GeneCard ID

UBE2B

Enzyme 52 GenAtlas ID

UBE2B

Enzyme 52 HGNC ID

HGNC:12473 Link Image

Enzyme 52 Chromosome Location

Enzyme 52 Locus

5q31.1

Enzyme 52 SNPs

SNPJam Report Link Image

Enzyme 52 General References

Schneider R, Eckerskorn C, Lottspeich F, Schweiger M: The human ubiquitin carrier protein E2(Mr = 17,000) is homologous to the yeast DNA repair gene RAD6. EMBO J. 1990 May;9(5):1431-5. [PubMed ]
Woffendin C, Chen ZY, Staskus K, Retzel EF, Plagemann PG: Mammalian mRNAs encoding protein closely related to ubiquitin-conjugating enzyme encoded by yeast DNA repair gene RAD6. Biochim Biophys Acta. 1991 Aug 27;1090(1):81-5. [PubMed ]
Koken MH, Reynolds P, Jaspers-Dekker I, Prakash L, Prakash S, Bootsma D, Hoeijmakers JH: Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6. Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):8865-9. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Xin H, Lin W, Sumanasekera W, Zhang Y, Wu X, Wang Z: The human RAD18 gene product interacts with HHR6A and HHR6B. Nucleic Acids Res. 2000 Jul 15;28(14):2847-54. [PubMed ]
Motegi A, Sood R, Moinova H, Markowitz SD, Liu PP, Myung K: Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination. J Cell Biol. 2006 Dec 4;175(5):703-8. Epub 2006 Nov 27. [PubMed ]
Unk I, Hajdu I, Fatyol K, Szakal B, Blastyak A, Bermudez V, Hurwitz J, Prakash L, Prakash S, Haracska L: Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen. Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18107-12. Epub 2006 Nov 15. [PubMed ]
David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
Miura T, Klaus W, Ross A, Guntert P, Senn H: The NMR structure of the class I human ubiquitin-conjugating enzyme 2b. J Biomol NMR. 2002 Jan;22(1):89-92. [PubMed ]

Enzyme 52 Metabolite References

Not Available

Enzyme 53 [top]

Enzyme 53 ID

5868

Enzyme 53 Name

Probable leucyl-tRNA synthetase, mitochondrial

Enzyme 53 Synonyms

Leucine--tRNA ligase
LeuRS

Enzyme 53 Gene Name

LARS2

Enzyme 53 Protein Sequence

>Probable leucyl-tRNA synthetase, mitochondrial

MASVWQRLGFYASLLKRQLNGGPDVIKWERRVIPGCTRSIYSATGKWTKEYTLQTRKDVE
KWWHQRIKEQASKISEADKSKPKFYVLSMFPYPSGKLHMGHVRVYTISDTIARFQKMRGM
QVINPMGWDAFGLPAENAAVERNLHPQSWTQSNIKHMRKQLDRLGLCFSWDREITTCLPD
YYKWTQYLFIKLYEAGLAYQKEALVNWDPVDQTVLANEQVDEHGCSWRSGAKVEQKYLRQ
WFIKTTAYAKAMQDALADLPEWYGIKGMQAHWIGDCVGCHLDFTLKVHGQATGEKLTAYT
ATPEAIYGTSHVAISPSHRLLHGHSSLKEALRMALVPGKDCLTPVMAVNMLTQQEVPVVI
LAKADLEGSLDSKIGIPSTSSEDTILAQTLGLAYSEVIETLPDGTERLSSSAEFTGMTRQ
DAFLALTQKARGKRVGGDVTSDKLKDWLISRQRYWGTPIPIVHCPVCGPTPVPLEDLPVT
LPNIASFTGKGGPPLAMASEWVNCSCPRCKGAAKRETDTMDTFVDSAWYYFRYTDPHNPH
SPFNTAVADYWMPVDLYIGGKEHAVMHLFYARFFSHFCHDQKMVKHREPFHKLLAQGLIK
GQTFRLPSGQYLQREEVDLTGSVPVHAKTKEKLEVTWEKMSKSKHNGVDPEEVVEQYGID
TIRLYILFAAPPEKDILWDVKTDALPGVLRWQQRLWTLTTRFIEARASGKSPQPQLLSNK
EKAEARKLWEYKNSVISQVTTHFTEDFSLNSAISQLMGLSNALSQASQSVILHSPEFEDA
LCALMVMAAPLAPHVTSEIWAGLALVPRKLCAHYTWDASVLLQAWPAVDPEFLQQPEVVQ
MAVLINNKACGKIPVPQQVARDQDKVHEFVLQSELGVRLLQGRSIKKSFLSPRTALINFL
VQD

Enzyme 53 Number of Residues

903

Enzyme 53 Molecular Weight

101975.4

Enzyme 53 Theoretical pI

8.32

Enzyme 53 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity leucine-tRNA ligase activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process leucyl-tRNA aminoacylation macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 53 General Function

Involved in nucleotide binding

Enzyme 53 Specific Function

ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)

Enzyme 53 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )

Enzyme 53 Reactions

ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu [RN:R03657]

Enzyme 53 Pfam Domain Function

Anticodon_1 (PF08264 )
tRNA-synt_1 (PF00133 )

Enzyme 53 Signals

None

Enzyme 53 Transmembrane Regions

None

Enzyme 53 Essentiality

Not Available

Enzyme 53 GenBank ID Protein

19683964

Enzyme 53 UniProtKB/Swiss-Prot ID

Q15031

Enzyme 53 UniProtKB/Swiss-Prot Entry Name

SYLM_HUMAN Link Image

Enzyme 53 PDB ID

Not Available

Enzyme 53 Cellular Location

Not Available

Enzyme 53 Gene Sequence

>2712 bp

ATGGCTTCTGTTTGGCAGAGATTGGGTTTTTATGCCTCTCTTCTGAAAAGACAGCTAAAT
GGTGGGCCAGATGTCATCAAGTGGGAAAGGAGAGTAATTCCCGGATGTACCAGAAGCATC
TACAGTGCCACGGGAAAGTGGACAAAAGAGTATACATTGCAGACAAGAAAGGATGTTGAG
AAATGGTGGCATCAACGAATAAAAGAACAGGCCTCCAAAATTTCAGAAGCTGATAAATCG
AAGCCAAAATTTTACGTGCTTTCCATGTTCCCTTATCCTTCTGGTAAGCTGCACATGGGC
CATGTGCGTGTCTACACCATCAGCGACACCATAGCACGGTTCCAGAAGATGAGAGGGATG
CAGGTCATCAACCCCATGGGATGGGATGCTTTTGGATTGCCTGCTGAAAATGCCGCAGTC
GAGAGGAATCTACATCCACAAAGTTGGACACAAAGTAATATTAAACACATGAGGAAACAG
CTTGATCGTCTGGGCCTGTGTTTCAGCTGGGATAGGGAAATAACTACGTGTTTGCCAGAT
TACTACAAGTGGACTCAGTATCTCTTTATTAAACTGTATGAGGCTGGGCTGGCCTATCAA
AAGGAGGCCCTGGTTAACTGGGACCCAGTGGATCAAACAGTGCTTGCCAATGAGCAGGTG
GATGAACATGGCTGTTCATGGCGTTCTGGAGCAAAGGTGGAACAGAAGTACCTCAGACAA
TGGTTTATTAAGACAACCGCTTATGCAAAGGCCATGCAGGACGCGTTGGCAGACCTTCCA
GAATGGTATGGAATAAAAGGCATGCAAGCCCACTGGATTGGGGACTGTGTGGGCTGCCAC
CTGGACTTCACATTAAAGGTTCATGGGCAAGCCACGGGCGAAAAGCTGACTGCCTATACG
GCCACCCCTGAAGCCATTTATGGCACCTCCCACGTGGCCATCTCGCCCAGCCACAGACTC
CTACATGGGCACAGCTCTCTGAAGGAAGCCTTGAGGATGGCCCTTGTCCCTGGCAAAGAT
TGCCTCACGCCTGTAATGGCTGTGAACATGCTCACCCAGCAGGAGGTCCCTGTCGTTATT
TTGGCCAAAGCTGACTTGGAAGGCTCTCTGGATTCAAAAATAGGAATTCCCAGTACTAGC
TCAGAGGACACCATCTTAGCCCAAACCCTGGGCCTGGCCTACTCTGAAGTCATTGAAACT
TTGCCAGATGGCACAGAGAGACTGAGCAGCTCTGCTGAGTTCACAGGTATGACCCGGCAG
GATGCTTTTCTAGCCCTGACTCAGAAAGCCCGGGGGAAGAGAGTGGGTGGAGACGTGACA
AGTGATAAACTGAAAGACTGGCTGATTTCACGGCAGCGGTACTGGGGCACACCAATCCCC
ATTGTCCACTGCCCAGTCTGTGGCCCCACACCTGTGCCCCTGGAGGACTTGCCTGTGACC
CTGCCCAACATCGCATCTTTCACTGGCAAGGGAGGCCCCCCACTGGCCATGGCTTCAGAG
TGGGTGAACTGCTCCTGCCCAAGGTGCAAGGGAGCAGCCAAGAGAGAGACAGACACGATG
GATACCTTTGTTGATTCTGCTTGGTACTACTTCAGATACACTGACCCTCATAATCCACAC
AGCCCTTTTAACACAGCAGTGGCCGATTACTGGATGCCTGTGGATTTGTACATTGGAGGG
AAAGAACATGCCGTCATGCACTTGTTCTATGCAAGATTCTTTAGTCATTTTTGCCATGAT
CAAAAAATGGTTAAACATAGGGAGCCTTTTCATAAGCTGCTGGCCCAAGGCCTTATCAAG
GGGCAGACATTCCGCCTACCATCTGGACAGTATCTACAGAGAGAGGAAGTGGATCTCACA
GGTTCCGTTCCTGTTCATGCAAAAACGAAAGAGAAGTTAGAGGTGACGTGGGAGAAGATG
AGTAAGTCCAAACACAACGGGGTGGACCCAGAGGAAGTTGTGGAGCAGTATGGGATCGAC
ACGATTCGGCTCTACATCCTTTTTGCTGCCCCTCCTGAGAAGGATATCTTGTGGGATGTG
AAAACTGATGCTCTCCCTGGGGTGCTGAGATGGCAACAACGACTGTGGACCTTGACAACT
CGGTTTATTGAGGCCAGGGCTTCTGGGAAGTCTCCCCAGCCTCAGCTGCTGAGTAACAAG
GAGAAAGCCGAGGCCAGGAAGCTCTGGGAGTACAAGAACTCCGTCATCTCTCAGGTGACC
ACCCATTTCACAGAGGACTTCTCACTGAATTCTGCAATTTCTCAGCTGATGGGACTCAGC
AATGCCCTCTCGCAAGCCTCTCAGAGCGTCATTCTCCACAGCCCCGAGTTTGAGGATGCT
TTGTGTGCCCTGATGGTGATGGCTGCTCCACTGGCCCCTCATGTAACCTCAGAGATCTGG
GCAGGCCTGGCGCTGGTGCCGAGGAAGCTCTGTGCCCACTACACTTGGGATGCCAGTGTG
CTGCTCCAGGCATGGCCTGCTGTGGACCCGGAGTTCCTGCAGCAGCCTGAGGTTGTCCAG
ATGGCAGTTCTGATCAACAATAAAGCTTGTGGCAAAATTCCTGTGCCCCAACAAGTTGCC
CGGGACCAGGACAAAGTCCACGAATTTGTTCTTCAAAGCGAGCTGGGTGTCAGGCTTTTG
CAAGGACGAAGCATCAAGAAGTCCTTCCTTTCCCCGAGAACTGCCCTCATCAACTTCCTG
GTGCAAGATTGA

Enzyme 53 GenBank Gene ID

BC025989

Enzyme 53 GeneCard ID

LARS2

Enzyme 53 GenAtlas ID

LARS2

Enzyme 53 HGNC ID

HGNC:17095 Link Image

Enzyme 53 Chromosome Location

Enzyme 53 Locus

3p21.3

Enzyme 53 SNPs

SNPJam Report Link Image

Enzyme 53 General References

Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 53 Metabolite References

Not Available

Enzyme 54 [top]

Enzyme 54 ID

5870

Enzyme 54 Name

Ubiquitin-conjugating enzyme E2 J2

Enzyme 54 Synonyms

Non-canonical ubiquitin-conjugating enzyme 2
NCUBE-2

Enzyme 54 Gene Name

UBE2J2

Enzyme 54 Protein Sequence

>Ubiquitin-conjugating enzyme E2 J2

MSSTSSKRAPTTATQRLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGY
YHGKLIFPREFPFKPPSIYMITPNGRFKCNTRLCLSITDFHPDTWNPAWSVSTILTGLLS
FMVEKGPTLGSIETSDFTKRQLAVQSLAFNLKDKVFCELFPEVVEEIKQKQKAQDELSSR
PQTLPLPDVVPDGETHLVQNGIQLLNGHAPGAVPNLAGLQQANRHHGLLGGALANLFVIV
GFAAFAYTVKYVLRSIAQE

Enzyme 54 Number of Residues

259

Enzyme 54 Molecular Weight

28898.1

Enzyme 54 Theoretical pI

8.59

Enzyme 54 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 54 General Function

Involved in acid-amino acid ligase activity

Enzyme 54 Specific Function

Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD)

Enzyme 54 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 54 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 54 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 54 Signals

None

Enzyme 54 Transmembrane Regions

227-247

Enzyme 54 Essentiality

Not Available

Enzyme 54 GenBank ID Protein

37577124

Enzyme 54 UniProtKB/Swiss-Prot ID

Q8N2K1

Enzyme 54 UniProtKB/Swiss-Prot Entry Name

UB2J2_HUMAN Link Image

Enzyme 54 PDB ID

Not Available

Enzyme 54 Cellular Location

Not Available

Enzyme 54 Gene Sequence

>780 bp

ATGAGCAGCACCAGCAGTAAGAGGGCTCCGACCACGGCAACCCAGAGGCTGAAGCAGGAC
TACCTTCGCATTAAGAAAGACCCGGTGCCTTACATCTGTGCCGAGCCCCTCCCTTCGAAT
ATTCTCGAGTGGCACTATGTCGTCCGAGGCCCAGAGATGACCCCTTATGAAGGTGGCTAT
TATCATGGAAAACTAATTTTTCCCAGAGAATTTCCTTTCAAACCTCCCAGTATCTATATG
ATCACTCCCAACGGGAGGTTTAAGTGCAACACCAGGCTGTGTCTTTCTATCACGGATTTC
CACCCGGACACGTGGAACCCGGCCTGGTCTGTCTCCACCATCCTGACTGGGCTCCTGAGC
TTCATGGTGGAGAAGGGCCCCACCCTGGGCAGTATAGAGACGTCGGACTTCACGAAAAGA
CAACTGGCAGTGCAGAGTTTAGCATTTAATTTGAAAGATAAAGTCTTTTGTGAATTATTT
CCTGAAGTCGTGGAGGAGATTAAACAAAAACAGAAAGCACAAGACGAACTCAGTAGCAGA
CCCCAGACTCTCCCCTTGCCAGACGTGGTTCCAGACGGGGAGACGCACCTCGTCCAGAAC
GGGATTCAGCTGCTCAACGGGCATGCGCCGGGGGCCGTCCCAAACCTCGCAGGGCTCCAG
CAGGCCAACCGGCACCACGGACTCCTGGGTGGCGCCCTGGCGAACTTGTTTGTGATAGTT
GGGTTTGCAGCCTTTGCTTACACGGTCAAGTACGTGCTGAGGAGCATCGCGCAGGAGTGA

Enzyme 54 GenBank Gene ID

NM_058167.2 Link Image

Enzyme 54 GeneCard ID

UBE2J2

Enzyme 54 GenAtlas ID

UBE2J2

Enzyme 54 HGNC ID

HGNC:19268 Link Image

Enzyme 54 Chromosome Location

Enzyme 54 Locus

1p36.33

Enzyme 54 SNPs

SNPJam Report Link Image

Enzyme 54 General References

Tiwari S, Weissman AM: Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s). J Biol Chem. 2001 May 11;276(19):16193-200. Epub 2001 Feb 2. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 54 Metabolite References

Not Available

Enzyme 55 [top]

Enzyme 55 ID

5871

Enzyme 55 Name

AMP deaminase 2

Enzyme 55 Synonyms

AMP deaminase isoform L

Enzyme 55 Gene Name

AMPD2

Enzyme 55 Protein Sequence

>AMP deaminase 2

MRNRGQGLFRLRSRCFLHQSLPLGAGRRKGLDVAEPGPSRCRSDSPAVAAVVPAMASYPS
GSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMD
GKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLR
AKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDA
AKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPP
ALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVN
VLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIH
ASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHAD
RNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELR
LSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLP
LFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYL
YYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQ
YLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEY
SIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRV
GYRYETLCQELALITQAVQSEMLETIPEEAGITMSPGPQ

Enzyme 55 Number of Residues

879

Enzyme 55 Molecular Weight

100686.9

Enzyme 55 Theoretical pI

6.93

Enzyme 55 GO Classification

Function
AMP deaminase activity catalytic activity deaminase activity hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
Process
cellular aromatic compound metabolic process cellular metabolic process cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside phosphate metabolic process nucleotide metabolic process purine base metabolic process purine nucleoside monophosphate biosynthetic process purine nucleotide biosynthetic process purine nucleotide metabolic process purine ribonucleoside monophosphate biosynthetic process
Component
—

Enzyme 55 General Function

Involved in deaminase activity

Enzyme 55 Specific Function

AMP deaminase plays a critical role in energy metabolism

Enzyme 55 Pathways

Purine Metabolism (map00230 )

Enzyme 55 Reactions

AMP + H2O = IMP + NH3 [RN:R00181]

Enzyme 55 Pfam Domain Function

A_deaminase (PF00962 )

Enzyme 55 Signals

None

Enzyme 55 Transmembrane Regions

None

Enzyme 55 Essentiality

Not Available

Enzyme 55 GenBank ID Protein

21264318

Enzyme 55 UniProtKB/Swiss-Prot ID

Q01433

Enzyme 55 UniProtKB/Swiss-Prot Entry Name

AMPD2_HUMAN Link Image

Enzyme 55 PDB ID

Not Available

Enzyme 55 Cellular Location

Not Available

Enzyme 55 Gene Sequence

>2640 bp

ATGAGAAATCGTGGCCAGGGCCTCTTCCGCCTGCGGAGCCGCTGCTTCCTGCATCAGTCA
CTCCCGCTGGGGGCGGGGCGGAGGAAGGGGTTGGATGTGGCAGAGCCAGGCCCCAGCCGG
TGCCGCTCAGACTCCCCCGCTGTCGCCGCCGTGGTCCCAGCCATGGCATCCTATCCATCT
GGCTCTGGCAAGCCCAAGGCCAAATATCCCTTTAAGAAGCGGGCCAGCCTGCAGGCCTCC
ACTGCAGCTCCAGAGGCTCGGGGTGGTCTGGGGGCCCCTCCGCTGCAGTCTGCCCGATCC
CTGCCGGGCCCCGCCCCCTGCCTCAAGCACTTCCCGCTCGACCTGCGCACGTCTATGGAT
GGCAAATGCAAGGAGATCGCCGAGGAGCTGTTCACCCGCTCACTGGCTGAGAGCGAGCTC
CGTAGTGCCCCGTATGAGTTCCCCGAGGAGAGCCCCATTGAACAGCTGGAGGAGCGGCGG
CAGCGGCTGGAGCGGCAGATCAGCCAGGATGTCAAGCTGGAGCCAGACATCCTGCTTCGG
GCCAAGCAAGATTTCCTGAAGACGGACAGTGACTCGGACCTACAGCTCTACAAGGAACAG
GGTGAGGGGCAGGGTGACCGGAGCCTGCGGGAGCGTGATGTGCTGGAACGGGAGTTTCAG
CGGGTCACCATCTCTGGGGAGGAGAAGTGTGGGGTGCCGTTCACAGACCTGCTGGATGCA
GCCAAGAGTGTGGTGCGGGCGCTCTTCATCCGGGAGAAGTACATGGCCCTGTCCCTGCAG
AGCTTCTGCCCCACCACCCGCCGCTACCTGCAGCAGCTGGCTGAAAAGCCTCTGGAGACC
CGGACCTATGAACAGGGCCCCGACACCCCTGTGTCTGCTGATGCCCCGGTGCACCCCCCT
GCGCTGGAGCAGCACCCGTATGAGCACTGTGAGCCAAGCACCATGCCTGGGGACCTGGGC
TTGGGTCTGCGCATGGTGCGGGGTGTGGTGCACGTCTACACCCGCAGGGAACCCGACGAG
CATTGCTCAGAGGTGGAGCTGCCATACCCTGACCTGCAGGAATTTGTGGCTGACGTCAAT
GTGCTGATGGCCCTGATTATCAATGGCCCCATAAAGTCATTCTGCTACCGCCGGCTGCAG
TACCTGAGCTCCAAGTTCCAGATGCATGTGCTACTCAATGAGATGAAGGAGCTGGCCGCC
CAGAAGAAAGTGCCACACCGAGATTTCTACAACATCCGCAAGGTGGACACCCACATCCAT
GCCTCGTCCTGCATGAACCAGAAGCATCTGCTGCGCTTCATCAAGCGGGCAATGAAGCGG
CACCTGGAGGAGATCGTGCACGTGGAGCAGGGCCGTGAACAGACGCTGCGGGAGGTCTTT
GAGAGCATGAATCTCACGGCCTACGACCTGAGTGTGGACACGCTGGATGTGCATGCGGAC
AGGAACACTTTCCATCGCTTTGACAAGTTTAATGCCAAATACAACCCTATTGGGGAGTCC
GTCCTCCGAGAGATCTTCATCAAGACGGACAACAGGGTATCTGGGAAGTACTTTGCTCAC
ATCATCAAGGAGGTGATGTCAGACCTGGAGGAGAGCAAATACCAGAATGCAGAGCTGCGG
CTCTCCATTTACGGGCGCTCGAGGGATGAGTGGGACAAGCTGGCGCGCTGGGCCGTCATG
CACCGCGTGCACTCCCCCAACGTGCGCTGGCTGGTGCAGGTGCCCCGCCTCTTTGATGTG
TACCGTACCAAGGGCCAGCTGGCCAACTTCCAGGAGATGCTGGAGAACATCTTCCTGCCA
CTGTTCGAGGCCACTGTGCACCCTGCCAGCCACCCGGAACTGCATCTCTTCTTAGAGCAC
GTGGATGGTTTTGACAGCGTGGATGATGAGTCCAAGCCTGAAAACCATGTCTTCAACCTG
GAGAGCCCCCTGCCTGAGGCGTGGGTGGAGGAGGACAACCCACCCTATGCCTACTACCTG
TACTACACCTTTGCCAACATGGCCATGTTGAACCACCTGCGCAGGCAGAGGGGCTTCCAC
ACGTTTGTGCTGAGGCCACACTGTGGGGAGGCTGGGCCCATCCACCACCTGGTGTCAGCC
TTCATGCTGGCTGAGAACATTTCCCACGGGCTCCTTCTGCGCAAGGCCCCCGTCCTGCAG
TACCTGTACTACCTGGCCCAGATCGGCATCGCCATGTCTCCGCTCAGCAACAACAGCCTC
TTCCTCAGCTATCACCGGAATCCGCTACCGGAGTACCTGTCCCGCGGCCTCATGGTCTCC
CTGTCCACTGATGATCCCTTGCAGTTCCACTTCACCAAGGAGCCGCTGATGGAGGAGTAC
AGCATCGCCACCCAGGTGTGGAAGCTCAGCTCCTGCGATATGTGTGAGCTGGCCCGCAAC
AGCGTGCTCATGAGCGGCTTCTCGCACAAGGTAAAGAGCCACTGGCTGGGACCCAACTAT
ACCAAGGAAGGCCCTGAGGGGAATGACATCCGCCGGACCAATGTGCCAGACATCCGCGTG
GGCTACCGCTACGAGACCCTGTGCCAGGAGCTGGCGCTCATCACGCAGGCAGTCCAGAGT
GAGATGCTGGAGACCATTCCAGAGGAGGCGGGTATCACCATGAGCCCAGGGCCTCAATGA

Enzyme 55 GenBank Gene ID

NM_004037.6 Link Image

Enzyme 55 GeneCard ID

AMPD2

Enzyme 55 GenAtlas ID

AMPD2

Enzyme 55 HGNC ID

HGNC:469

Enzyme 55 Chromosome Location

Enzyme 55 Locus

1p13.3

Enzyme 55 SNPs

SNPJam Report Link Image

Enzyme 55 General References

Bausch-Jurken MT, Mahnke-Zizelman DK, Morisaki T, Sabina RL: Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA. J Biol Chem. 1992 Nov 5;267(31):22407-13. [PubMed ]
Van den Bergh F, Sabina RL: Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative transcripts encoding variable N-terminal extensions of isoform L. Biochem J. 1995 Dec 1;312 ( Pt 2):401-10. [PubMed ]
Mahnke-Zizelman DK, van den Bergh F, Bausch-Jurken MT, Eddy R, Sait S, Shows TB, Sabina RL: Cloning, sequence and characterization of the human AMPD2 gene: evidence for transcriptional regulation by two closely spaced promoters. Biochim Biophys Acta. 1996 Aug 14;1308(2):122-32. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 55 Metabolite References

Not Available

Enzyme 56 [top]

Enzyme 56 ID

5872

Enzyme 56 Name

cGMP-inhibited 3',5'-cyclic phosphodiesterase A

Enzyme 56 Synonyms

Cyclic GMP-inhibited phosphodiesterase A
CGI-PDE A

Enzyme 56 Gene Name

PDE3A

Enzyme 56 Protein Sequence

>cGMP-inhibited 3',5'-cyclic phosphodiesterase A

MAVPGDAARVRDKPVHSGVSQAPTAGRDCHHRADPASPRDSGCRGCWGDLVLQPLRSSRK
LSSALCAGSLSFLLALLVRLVRGEVGCDLEQCKEAAAAEEEEAAPGAEGGVFPGPRGGAP
GGGARLSPWLQPSALLFSLLCAFFWMGLYLLRAGVRLPLAVALLAACCGGEALVQIGLGV
GEDHLLSLPAAGVVLSCLAAATWLVLRLRLGVLMIALTSAVRTVSLISLERFKVAWRPYL
AYLAGVLGILLARYVEQILPQSAEAAPREHLGSQLIAGTKEDIPVFKRRRRSSSVVSAEM
SGCSSKSHRRTSLPCIPREQLMGHSEWDHKRGPRGSQSSGTSITVDIAVMGEAHGLITDL
LADPSLPPNVCTSLRAVSNLLSTQLTFQAIHKPRVNPVTSLSENYTCSDSEESSEKDKLA
IPKRLRRSLPPGLLRRVSSTWTTTTSATGLPTLEPAPVRRDRSTSIKLQEAPSSSPDSWN
NPVMMTLTKSRSFTSSYAISAANHVKAKKQSRPGALAKISPLSSPCSSPLQGTPASSLVS
KISAVQFPESADTTAKQSLGSHRALTYTQSAPDLSPQILTPPVICSSCGRPYSQGNPADE
PLERSGVATRTPSRTDDTAQVTSDYETNNNSDSSDIVQNEDETECLREPLRKASACSTYA
PETMMFLDKPILAPEPLVMDNLDSIMEQLNTWNFPIFDLVENIGRKCGRILSQVSYRLFE
DMGLFEAFKIPIREFMNYFHALEIGYRDIPYHNRIHATDVLHAVWYLTTQPIPGLSTVIN
DHGSTSDSDSDSGFTHGHMGYVFSKTYNVTDDKYGCLSGNIPALELMALYVAAAMHDYDH
PGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLFMSRPEYNFLINLDHVEFKHFRFL
VIEAILATDLKKHFDFVAKFNGKVNDDVGIDWTNENDRLLVCQMCIKLADINGPAKCKEL
HLQWTDGIVNEFYEQGDEEASLGLPISPFMDRSAPQLANLQESFISHIVGPLCNSYDSAG
LMPGKWVEDSDESGDTDDPEEEEEEAPAPNEEETCENNESPKKKTFKRRKIYCQITQHLL
QNHKMWKKVIEEEQRLAGIENQSLDQTPQSHSSEQIQAIKEEEEEKGKPRGEEIPTQKPD
Q

Enzyme 56 Number of Residues

1141

Enzyme 56 Molecular Weight

124978.1

Enzyme 56 Theoretical pI

5.87

Enzyme 56 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 56 General Function

Involved in catalytic activity

Enzyme 56 Specific Function

Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes

Enzyme 56 Pathways

Purine Metabolism (map00230 )

Enzyme 56 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 56 Pfam Domain Function

PDEase_I (PF00233 )

Enzyme 56 Signals

None

Enzyme 56 Transmembrane Regions

61-81 130-150 160-180 185-205 210-230 232-252

Enzyme 56 Essentiality

Not Available

Enzyme 56 GenBank ID Protein

38201493

Enzyme 56 UniProtKB/Swiss-Prot ID

Q14432

Enzyme 56 UniProtKB/Swiss-Prot Entry Name

PDE3A_HUMAN Link Image

Enzyme 56 PDB ID

Not Available

Enzyme 56 Cellular Location

Not Available

Enzyme 56 Gene Sequence

>3426 bp

ATGGCAGTGCCCGGCGACGCTGCACGAGTCAGGGACAAGCCCGTCCACAGTGGGGTGAGT
CAAGCCCCCACGGCGGGCCGGGACTGCCACCATCGTGCGGACCCCGCATCGCCGCGGGAC
TCGGGCTGCCGTGGCTGCTGGGGAGACCTGGTGCTGCAGCCGCTCCGGAGCTCTCGGAAA
CTTTCCTCCGCGCTGTGCGCGGGCTCCCTATCCTTTCTGCTGGCGCTGCTGGTGAGGCTG
GTCCGCGGGGAGGTCGGCTGTGACCTGGAGCAGTGTAAGGAGGCGGCGGCGGCGGAGGAG
GAGGAAGCAGCCCCGGGAGCAGAAGGGGGCGTCTTCCCGGGGCCTCGGGGAGGTGCTCCC
GGGGGCGGTGCGCGGCTCAGCCCCTGGCTGCAGCCCTCGGCGCTGCTCTTCAGTCTCCTG
TGTGCCTTCTTCTGGATGGGCTTGTACCTCCTGCGCGCCGGGGTGCGCCTGCCTCTGGCT
GTCGCGCTGCTGGCCGCCTGCTGCGGGGGGGAAGCGCTCGTCCAGATTGGGCTGGGCGTC
GGGGAGGATCACTTACTCTCACTCCCCGCTGCGGGGGTGGTGCTCAGCTGCTTGGCCGCC
GCGACATGGCTGGTGCTGAGGCTGAGGCTGGGCGTCCTCATGATCGCCTTGACTAGCGCG
GTCAGGACCGTGTCCCTCATTTCCTTAGAGAGGTTCAAGGTCGCCTGGAGACCTTACCTG
GCGTACCTGGCCGGCGTGCTGGGGATCCTCTTGGCCAGGTACGTGGAACAAATCTTGCCG
CAGTCCGCGGAGGCGGCTCCAAGGGAGCATTTGGGGTCCCAGCTGATTGCTGGGACCAAG
GAAGATATCCCGGTGTTTAAGAGGAGGAGGCGGTCCAGCTCCGTCGTGTCCGCCGAGATG
TCCGGCTGCAGCAGCAAGTCCCATCGGAGGACCTCCCTGCCCTGTATACCGAGGGAACAG
CTCATGGGGCATTCAGAATGGGACCACAAACGAGGGCCAAGAGGATCACAGTCTTCAGGA
ACCAGTATTACTGTGGACATCGCCGTCATGGGCGAAGCCCACGGCCTCATTACCGACCTC
CTGGCAGACCCTTCTCTTCCACCAAACGTGTGCACATCCTTGAGAGCCGTGAGCAACTTG
CTCAGCACACAGCTCACCTTCCAGGCCATTCACAAGCCCAGAGTGAATCCCGTTACTTCG
CTCAGTGAAAACTATACCTGTTCTGACTCTGAAGAGAGCTCTGAAAAAGACAAGCTTGCT
ATTCCAAAGCGCCTGAGAAGGAGTTTGCCTCCTGGCTTGTTGAGACGAGTTTCTTCCACT
TGGACCACCACCACCTCGGCCACAGGTCTACCCACCTTGGAGCCTGCACCAGTACGGAGA
GACCGCAGCACCAGCATCAAACTGCAGGAAGCACCTTCATCCAGTCCTGATTCTTGGAAT
AATCCAGTGATGATGACCCTCACCAAAAGCAGATCCTTTACTTCATCCTATGCTATTTCT
GCAGCTAACCATGTAAAGGCTAAAAAGCAAAGTCGACCAGGTGCCCTCGCTAAAATTTCA
CCTCTTTCATCGCCCTGCTCCTCACCTCTCCAAGGGACTCCTGCCAGCAGCCTGGTCAGC
AAAATTTCTGCAGTGCAGTTTCCAGAATCTGCTGACACAACTGCCAAACAAAGCCTAGGT
TCTCACAGGGCCTTAACTTACACTCAGAGTGCCCCAGACCTATCCCCTCAAATCCTGACT
CCACCTGTTATATGTAGCAGCTGTGGCAGACCATATTCCCAAGGGAATCCTGCTGATGAG
CCCCTGGAGAGAAGTGGGGTAGCCACTCGGACACCAAGTCGAACAGATGACACTGCTCAA
GTTACCTCTGATTATGAAACCAATAACAACAGTGACAGCAGTGACATTGTACAGAATGAA
GATGAAACAGAGTGCCTGAGAGAGCCTCTGAGGAAAGCATCGGCTTGCAGCACCTATGCT
CCTGAGACCATGATGTTTCTGGACAAACCAATTCTTGCTCCCGAACCTCTTGTCATGGAT
AACCTGGACTCAATTATGGAGCAGCTAAATACTTGGAATTTTCCAATTTTTGATTTAGTG
GAAAATATAGGAAGAAAATGTGGCCGTATTCTTAGTCAGGTATCTTACAGACTTTTTGAA
GACATGGGCCTCTTTGAAGCTTTTAAAATTCCAATTAGGGAATTTATGAATTATTTTCAT
GCTTTGGAGATTGGATATAGGGATATTCCTTATCATAACAGAATCCATGCCACTGATGTT
TTACATGCTGTTTGGTATCTTACTACACAGCCTATTCCAGGCCTCTCAACTGTGATTAAT
GATCATGGTTCAACCAGTGATTCAGATTCTGACAGTGGATTTACACATGGACATATGGGA
TATGTATTCTCAAAAACGTATAATGTGACAGATGATAAATACGGATGTCTGTCTGGGAAT
ATCCCTGCCTTGGAGTTGATGGCGCTGTATGTGGCTGCAGCCATGCACGATTATGATCAT
CCAGGAAGGACTAATGCTTTCCTGGTTGCAACTAGTGCTCCTCAGGCGGTGCTATATAAC
GATCGTTCAGTTTTGGAGAATCATCACGCAGCTGCTGCATGGAATCTTTTCATGTCCCGG
CCAGAGTATAACTTCTTAATTAACCTTGACCATGTGGAATTTAAGCATTTCCGTTTCCTT
GTCATTGAAGCAATTTTGGCCACTGACCTGAAGAAACACTTTGACTTCGTAGCCAAATTT
AATGGCAAGGTAAATGATGATGTTGGAATAGATTGGACCAATGAAAATGATCGTCTACTG
GTTTGTCAAATGTGTATAAAGTTGGCTGATATCAATGGTCCAGCTAAATGTAAAGAACTC
CATCTTCAGTGGACAGATGGTATTGTCAATGAATTTTATGAACAGGGTGATGAAGAGGCC
AGCCTTGGATTACCCATAAGCCCCTTCATGGATCGTTCTGCTCCTCAGCTGGCCAACCTT
CAGGAATCCTTCATCTCTCACATTGTGGGGCCTCTGTGCAACTCCTATGATTCAGCAGGA
CTAATGCCTGGAAAATGGGTGGAAGACAGCGATGAGTCAGGAGATACTGATGACCCAGAA
GAAGAGGAGGAAGAAGCACCAGCACCAAATGAAGAGGAAACCTGTGAAAATAATGAATCT
CCAAAAAAGAAGACTTTCAAAAGGAGAAAAATCTACTGCCAAATAACTCAGCACCTCTTA
CAGAACCACAAGATGTGGAAGAAAGTCATTGAAGAGGAGCAACGGTTGGCAGGCATAGAA
AATCAATCCCTGGACCAGACCCCTCAGTCGCACTCTTCAGAACAGATCCAGGCTATCAAG
GAAGAAGAAGAAGAGAAAGGGAAACCAAGAGGCGAGGAGATACCAACCCAAAAGCCAGAC
CAGTGA

Enzyme 56 GenBank Gene ID

M91667

Enzyme 56 GeneCard ID

PDE3A

Enzyme 56 GenAtlas ID

PDE3A

Enzyme 56 HGNC ID

HGNC:8778

Enzyme 56 Chromosome Location

Enzyme 56 Locus

12p12

Enzyme 56 SNPs

SNPJam Report Link Image

Enzyme 56 General References

Meacci E, Taira M, Moos M Jr, Smith CJ, Movsesian MA, Degerman E, Belfrage P, Manganiello V: Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase. Proc Natl Acad Sci U S A. 1992 May 1;89(9):3721-5. [PubMed ]
Cheung PP, Xu H, McLaughlin MM, Ghazaleh FA, Livi GP, Colman RW: Human platelet cGI-PDE: expression in yeast and localization of the catalytic domain by deletion mutagenesis. Blood. 1996 Aug 15;88(4):1321-9. [PubMed ]
Kuthe A, Eckel H, Stief CG, Uckert S, Forssmann WG, Jonas U, Magert HJ: Molecular biological characterization of phosphodiesterase 3A from human corpus cavernosum. Chem Biol Interact. 1999 May 14;119-120:593-8. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Degerman E, Moos M Jr, Rascon A, Vasta V, Meacci E, Smith CJ, Lindgren S, Andersson KE, Belfrage P, Manganiello V: Single-step affinity purification, partial structure and properties of human platelet cGMP inhibited cAMP phosphodiesterase. Biochim Biophys Acta. 1994 Apr 13;1205(2):189-98. [PubMed ]
Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed ]
Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]

Enzyme 56 Metabolite References

Not Available

Enzyme 57 [top]

Enzyme 57 ID

5873

Enzyme 57 Name

Ubiquitin-conjugating enzyme E2 L3

Enzyme 57 Synonyms

L-UBC
UbcH7
Ubiquitin carrier protein L3
Ubiquitin-conjugating enzyme E2-F1
Ubiquitin-protein ligase L3

Enzyme 57 Gene Name

UBE2L3

Enzyme 57 Protein Sequence

>Ubiquitin-conjugating enzyme E2 L3

MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAE
YPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHP
LRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD

Enzyme 57 Number of Residues

154

Enzyme 57 Molecular Weight

17861.4

Enzyme 57 Theoretical pI

8.79

Enzyme 57 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 57 General Function

Involved in acid-amino acid ligase activity

Enzyme 57 Specific Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis

Enzyme 57 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 57 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 57 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 57 Signals

None

Enzyme 57 Transmembrane Regions

None

Enzyme 57 Essentiality

Not Available

Enzyme 57 GenBank ID Protein

Not Available

Enzyme 57 UniProtKB/Swiss-Prot ID

P68036

Enzyme 57 UniProtKB/Swiss-Prot Entry Name

UB2L3_HUMAN Link Image

Enzyme 57 PDB ID

1FBV

Enzyme 57 PDB File

Show

Enzyme 57 3D Structure

Enzyme 57 Cellular Location

Not Available

Enzyme 57 Gene Sequence

>465 bp

ATGGCGGCCAGCAGGAGGCTGATGAAGGAGCTTGAAGAAATCCGCAAATGTGGGATGAAA
AACTTCCGTAACATCCAGGTTGATGAAGCTAATTTATTGACTTGGCAAGGGCTTATTGTT
CCTGACAACCCTCCATATGATAAGGGAGCCTTCAGAATCGAAATCAACTTTCCAGCAGAG
TACCCATTCAAACCACCGAAGATCACATTTAAAACAAAGATCTATCACCCAAACATCGAC
GAAAAGGGGCAGGTCTGTCTGCCAGTAATTAGTGCCGAAAACTGGAAGCCAGCAACCAAA
ACCGACCAAGTAATCCAGTCCCTCATAGCACTGGTGAATGACCCCCAGCCTGAGCACCCG
CTTCGGGCTGACCTAGCTGAAGAATACTCTAAGGACCGTAAAAAATTCTGTAAGAATGCT
GAAGAGTTTACAAAGAAATATGGGGAAAAGCGACCTGTGGACTAA

Enzyme 57 GenBank Gene ID

S81003

Enzyme 57 GeneCard ID

UBE2L3

Enzyme 57 GenAtlas ID

UBE2L3

Enzyme 57 HGNC ID

HGNC:12488 Link Image

Enzyme 57 Chromosome Location

Enzyme 57 Locus

22q11.21

Enzyme 57 SNPs

SNPJam Report Link Image

Enzyme 57 General References

Robinson PA, Leek JP, Thompson J, Carr IM, Bailey A, Moynihan TP, Coletta PL, Lench NJ, Markham AF: A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3. Mamm Genome. 1995 Oct;6(10):725-31. [PubMed ]
Nuber U, Schwarz S, Kaiser P, Schneider R, Scheffner M: Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. J Biol Chem. 1996 Feb 2;271(5):2795-800. [PubMed ]
Moynihan TP, Cole CG, Dunham I, O'Neil L, Markham AF, Robinson PA: Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3. Genomics. 1998 Jul 1;51(1):124-7. [PubMed ]
Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Blumenfeld N, Gonen H, Mayer A, Smith CE, Siegel NR, Schwartz AL, Ciechanover A: Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-"N-end rule" protein substrates. J Biol Chem. 1994 Apr 1;269(13):9574-81. [PubMed ]
Ardley HC, Moynihan TP, Markham AF, Robinson PA: Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7. Biochim Biophys Acta. 2000 Apr 25;1491(1-3):57-64. [PubMed ]
Shimura H, Hattori N, Kubo S, Mizuno Y, Asakawa S, Minoshima S, Shimizu N, Iwai K, Chiba T, Tanaka K, Suzuki T: Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet. 2000 Jul;25(3):302-5. [PubMed ]
Niwa J, Ishigaki S, Doyu M, Suzuki T, Tanaka K, Sobue G: A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity. Biochem Biophys Res Commun. 2001 Mar 2;281(3):706-13. [PubMed ]
Ardley HC, Tan NG, Rose SA, Markham AF, Robinson PA: Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7. J Biol Chem. 2001 Jun 1;276(22):19640-7. Epub 2001 Mar 13. [PubMed ]
Toby GG, Gherraby W, Coleman TR, Golemis EA: A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels. Mol Cell Biol. 2003 Mar;23(6):2109-22. [PubMed ]
Verma S, Ismail A, Gao X, Fu G, Li X, O'Malley BW, Nawaz Z: The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors. Mol Cell Biol. 2004 Oct;24(19):8716-26. [PubMed ]
Huang J, Xu LG, Liu T, Zhai Z, Shu HB: The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis. FEBS Lett. 2006 Feb 6;580(3):940-7. Epub 2006 Jan 18. [PubMed ]
Garside H, Waters C, Berry A, Rice L, Ardley HC, White A, Robinson PA, Ray D: UbcH7 interacts with the glucocorticoid receptor and mediates receptor autoregulation. J Endocrinol. 2006 Sep;190(3):621-9. [PubMed ]
Fortier JM, Kornbluth J: NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase. J Immunol. 2006 Jun 1;176(11):6454-63. [PubMed ]
Marteijn JA, van der Meer LT, Smit JJ, Noordermeer SM, Wissink W, Jansen P, Swarts HG, Hibbert RG, de Witte T, Sixma TK, Jansen JH, van der Reijden BA: The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains. Leukemia. 2009 Aug;23(8):1480-9. Epub 2009 Apr 2. [PubMed ]
Whitcomb EA, Dudek EJ, Liu Q, Taylor A: Novel control of S phase of the cell cycle by ubiquitin-conjugating enzyme H7. Mol Biol Cell. 2009 Jan;20(1):1-9. Epub 2008 Oct 22. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
Huang L, Kinnucan E, Wang G, Beaudenon S, Howley PM, Huibregtse JM, Pavletich NP: Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science. 1999 Nov 12;286(5443):1321-6. [PubMed ]
Zheng N, Wang P, Jeffrey PD, Pavletich NP: Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell. 2000 Aug 18;102(4):533-9. [PubMed ]

Enzyme 57 Metabolite References

Not Available

Enzyme 58 [top]

Enzyme 58 ID

5874

Enzyme 58 Name

RNA 3'-terminal phosphate cyclase

Enzyme 58 Synonyms

RNA cyclase
RNA-3'-phosphate cyclase
RNA terminal phosphate cyclase domain-containing protein 1
RTC domain-containing protein 1

Enzyme 58 Gene Name

RTCD1

Enzyme 58 Protein Sequence

>RNA 3'-terminal phosphate cyclase

MAGPRVEVDGSIMEGGGQILRVSTALSCLLGLPLRVQKIRAGRSTPGLRPQHLSGLEMIR
DLCDGQLEGAEIGSTEITFTPEKIKGGIHTADTKTAGSVCLLMQVSMPCVLFAASPSELH
LKGGTNAEMAPQIDYTVMVFKPIVEKFGFIFNCDIKTRGYYPKGGGEVIVRMSPVKQLNP
INLTERGCVTKIYGRAFVAGVLPFKVAKDMAAAAVRCIRKEIRDLYVNIQPVQEPKDQAF
GNGNGIIIIAETSTGCLFAGSSLGKRGVNADKVGIEAAEMLLANLRHGGTVDEYLQDQLI
VFMALANGVSRIKTGPVTLHTQTAIHFAEQIAKAKFIVKKSEDEEDAAKDTYIIECQGIG
MTNPNL

Enzyme 58 Number of Residues

366

Enzyme 58 Molecular Weight

39336.4

Enzyme 58 Theoretical pI

7.94

Enzyme 58 GO Classification

Function
RNA-3'-phosphate cyclase activity catalytic activity cyclase activity ligase activity ligase activity, forming phosphoric ester bonds
Process
RNA metabolic process RNA processing cellular macromolecule metabolic process macromolecule metabolic process metabolic process
Component
—

Enzyme 58 General Function

Involved in ligase activity, forming phosphoric ester bonds

Enzyme 58 Specific Function

Catalyzes the conversion of 3'-phosphate to a 2',3'- cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps:(A) adenylation of the enzyme by ATP; (B) the enzyme acts on RNA-N3'P to produce RNA-N3'PP5'A; (C) a non catalytic nucleophilic attack by the adjacent 2'hydroxyl on the phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing

Enzyme 58 Pathways

Not Available

Enzyme 58 Reactions

ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate [RN:R04274]

Enzyme 58 Pfam Domain Function

RTC (PF01137 )
RTC_insert (PF05189 )

Enzyme 58 Signals

None

Enzyme 58 Transmembrane Regions

None

Enzyme 58 Essentiality

Not Available

Enzyme 58 GenBank ID Protein

55665043

Enzyme 58 UniProtKB/Swiss-Prot ID

O00442

Enzyme 58 UniProtKB/Swiss-Prot Entry Name

RTC1_HUMAN Link Image

Enzyme 58 PDB ID

Not Available

Enzyme 58 Cellular Location

Not Available

Enzyme 58 Gene Sequence

>1101 bp

ATGGCGGGGCCGCGGGTGGAGGTCGATGGCAGCATCATGGAAGGGGGCGGCCAGATCCTG
AGAGTCTCTACGGCCTTGAGCTGTCTCCTAGGCCTCCCCTTGCGGGTGCAGAAGATCCGA
GCCGGCCGGAGCACGCCAGGCCTGAGGCCTCAACATTTATCTGGACTGGAAATGATTCGA
GATTTGTGTGATGGGCAACTGGAGGGGGCAGAAATTGGCTCAACAGAAATAACCTTTACA
CCAGAGAAGATCAAAGGTGGAATCCACACAGCAGATACCAAGACAGCAGGGAGTGTGTGC
CTCTTGATGCAGGTCTCAATGCCGTGTGTTCTCTTTGCTGCTTCTCCATCAGAACTTCAT
TTGAAAGGTGGAACTAATGCTGAAATGGCACCACAGATCGATTATACAGTGATGGTCTTC
AAGCCAATTGTTGAAAAATTTGGTTTCATATTTAATTGTGACATTAAAACAAGGGGATAT
TACCCAAAAGGGGGTGGTGAAGTGATTGTTCGAATGTCACCAGTTAAACAATTGAACCCT
ATAAATTTAACTGAGCGTGGCTGTGTGACTAAGATATATGGAAGAGCTTTCGTTGCTGGT
GTTTTGCCATTTAAAGTAGCAAAAGATATGGCAGCGGCAGCAGTTAGATGCATCAGAAAG
GAGATCCGGGATTTGTATGTTAACATCCAGCCTGTTCAAGAACCTAAAGACCAAGCATTT
GGCAATGGAAATGGAATAATAATTATTGCTGAGACCTCCACTGGCTGTTTGTTTGCTGGA
TCATCGCTTGGTAAACGAGGTGTAAATGCAGACAAAGTTGGAATTGAAGCTGCCGAAATG
CTATTAGCAAATCTTAGACATGGTGGTACTGTGGATGAGTATCTGCAAGACCAGCTGATT
GTTTTCATGGCATTAGCCAATGGAGTTTCCAGAATAAAAACAGGACCAGTTACACTCCAT
ACGCAAACCGCGATACATTTTGCTGAACAAATAGCAAAGGCTAAATTTATTGTGAAGAAA
TCAGAAGATGAAGAAGACGCCGCTAAAGATACTTATATTATTGAATGCCAAGGAATTGGG
ATGACAAATCCAAATCTATAG

Enzyme 58 GenBank Gene ID

AL445928

Enzyme 58 GeneCard ID

RTCD1

Enzyme 58 GenAtlas ID

RTCD1

Enzyme 58 HGNC ID

HGNC:17981 Link Image

Enzyme 58 Chromosome Location

Enzyme 58 Locus

1p21.2

Enzyme 58 SNPs

SNPJam Report Link Image

Enzyme 58 General References

Genschik P, Billy E, Swianiewicz M, Filipowicz W: The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea. EMBO J. 1997 May 15;16(10):2955-67. [PubMed ]
Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Filipowicz W, Vicente O: RNA 3'-terminal phosphate cyclase from HeLa cells. Methods Enzymol. 1990;181:499-510. [PubMed ]

Enzyme 58 Metabolite References

Not Available

Enzyme 59 [top]

Enzyme 59 ID

5875

Enzyme 59 Name

Putative adenylate kinase 7

Enzyme 59 Synonyms

Not Available

Enzyme 59 Gene Name

AK7

Enzyme 59 Protein Sequence

>Putative adenylate kinase 7

MAEEEETAALTEKVIRTQRVFINLLDSYSSGNIGKFLSNCVVGASLEEITEEEEEEDENK
SAMLEASSTKVKEGTFQIVGTLSKPDSPRPDFAVETYSAISREDLLMRLLECDVIIYNIT
ESSQQMEEAIWAVSALSEEVSHFEKRKLFILLSTVMTWARSKALDPEDSEVPFTEEDYRR
RKSHPNFLDHINAEKMVLKFGKKARKFAAYVVAAGLQYGAEGGMLHTFFKMAWLGEIPAL
PVFGDGTNVIPTIHVLDLAGVIQNVIDHVPKPHYLVAVDESVHTLEDIVKCISKNTGPGK
IQKIPRENAYLTKDLTQDCLDHLLVNLRMEALFVKENFNIRWAAQTGFVENINTILKEYK
QSRGLMPIKICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLEAIVAPNDVGE
GEEEVEEEEEEENVEDAQELLDGIKESMEQNAGQLDDQYIIRFMKEKLKSMPCRNQGYIL
DGFPKTYDQAKDLFNQEDEEEEDDVRGRMFPFDKLIIPEFVCALDASDEFLKERVINLPE
SIVAGTHYSQDRFLRALSNYRDINIDDETVFNYFDELEIHPIHIDVGKLEDAQNRLAIKQ
LIKEIGEPRNYGLTDEEKAEEERKAAEERLAREAAEEAEREHQEAVEMAEKIARWEEWNK
RLEEVKREERELLEAQSIPLRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNNP
EAQ

Enzyme 59 Number of Residues

723

Enzyme 59 Molecular Weight

82657.7

Enzyme 59 Theoretical pI

4.38

Enzyme 59 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity kinase activity nucleobase, nucleoside, nucleotide kinase activity nucleoside binding purine nucleoside binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
Component
—

Enzyme 59 General Function

Involved in ATP binding

Enzyme 59 Specific Function

Play a role in maintaining ciliary structure and function

Enzyme 59 Pathways

Purine Metabolism (map00230 )

Enzyme 59 Reactions

ATP + AMP = 2 ADP [RN:R00127]

Enzyme 59 Pfam Domain Function

ADK (PF00406 )
Dpy-30 (PF05186 )

Enzyme 59 Signals

None

Enzyme 59 Transmembrane Regions

None

Enzyme 59 Essentiality

Not Available

Enzyme 59 GenBank ID Protein

16553126

Enzyme 59 UniProtKB/Swiss-Prot ID

Q96M32

Enzyme 59 UniProtKB/Swiss-Prot Entry Name

KAD7_HUMAN Link Image

Enzyme 59 PDB ID

Not Available

Enzyme 59 Cellular Location

Not Available

Enzyme 59 Gene Sequence

>2172 bp

ATGGCTGAAGAAGAGGAAACTGCTGCTCTCACGGAGAAGGTTATCCGGACCCAGAGGGTG
TTTATAAACCTGTTGGATTCCTACAGCAGCGGAAACATCGGGAAGTTTCTATCTAACTGT
GTAGTTGGGGCTTCGCTTGAAGAAATTACAGAGGAAGAGGAAGAGGAAGATGAAAATAAG
TCAGCTATGCTGGAAGCTTCCTCAACCAAAGTGAAGGAAGGCACATTCCAGATTGTGGGC
ACGCTGTCCAAGCCTGACAGCCCGCGGCCTGACTTTGCGGTGGAGACGTACTCTGCCATC
TCTCAAGAAGACCTTCTCATGCGCCTGCTGGAGTGTGATGTTATTATTTATAACATCACT
GAGAGCTCACAGCAAATGGAGGAAGCCATCTGGGCAGTCTCTGCACTCAGTGAAGAAGTC
AGCCACTTTGAAAAGCGAAAGCTATTTATTTTACTGTCGACGGTGATGACTTGGGCGCGC
TCCAAAGCCCTGGACCCCGAGGATTCTGAGGTTCCATTCACTGAAGAAGATTATCGAAGA
AGAAAGTCTCATCCTAATTTTCTGGACCACATAAATGCTGAAAAAATGGTTCTCAAATTT
GGAAAAAAGGCCAGAAAATTTGCAGCATACGTAGTTGCTGCTGGACTCCAGTATGGAGCG
GAAGGAGGCATGTTACACACATTTTTTAAGATGGCTTGGTTGGGCGAGATTCCTGCATTA
CCAGTTTTTGGCGATGGAACAAATGTAATTCCAACAATCCATGTTCTTGATCTAGCAGGA
GTGATACAAAACGTCATAGATCACGTGCCAAAGCTTCACTACCTGGTTGCTGTGGATGAG
TCTGTTCATACCCTGGAAGACATAGTCAAGTGTATCAGTAAAAATACTGGCCCTGGGAAA
ATCCAGAAAATACCCAGAGAAAATGCATACCTAACCAAGGACTTAACGCAAGATTGTCTT
GACCATTTACTGGTCAACTTAAGAATGGAAGCGCTCTTTGTGAAGGAGAATTTTAATATT
CGATGGGCTGCCCAAACAGGATTTGTGGAAAATATCAACACTATCCTCAAGGAGTACAAG
CAAAGCAGAGGATTGATGCCAATCAAGATCTGCATTCTTGGTCCCCCTGCTGTGGGAAAA
TCCAGTATTGCTAAAGAATTGGCCAAGTACTACAAACTGCATCACATCCAACTGAAGGAT
GTCATTTCTGAAGCCATAGCAAAACTGGGGGCGATTGTTGCCCCTAACGATGTAGGGGAA
GGAGAAGAAGAAGTCGAAGAGGAAGAGGAGGAGGAGAATGTGGAAGATGCACAGGAGCTC
CTAGATGGCATCAAGGAGAGCATGGAGCAGAATGCAGGTCAACTAGACGATCAATATATA
ATTAGATTTATGAAAGAAAAGCTAAAATCAATGCCTTGCAGGAATCAAGGTTATATTTTG
GATGGATTCCCAAAGACCTATGATCAAGCAAAAGACCTGTTCAATCAGGAAGATGAGGAG
GAGGAAGATGATGTCAGAGGCAGAATGTTTCCCTTTGATAAATTAATTATACCTGAATTC
GTTTGTGCACTGGATGCTTCGGATGAGTTTCTGAAGGAGCGTGTGATAAACCTTCCTGAG
AGCATCGTGGCGGGGACCCACTACAGCCAAGACCGATTCCTCCGGGCTCTGAGCAACTAC
CGGGACATCAATATCGACGATGAGACTGTCTTCAACTATTTTGATGAACTTGAAATTCAC
CCGATACATATTGATGTAGGAAAACTTGAAGATGCTCAGAATAGACTTGCTATCAAACAG
CTCATCAAAGAGATTGGGGAGCCTCGAAATTATGGTTTAACAGACGAAGAAAAGGCAGAA
GAGGAGCGGAAGGCTGCGGAGGAGCGGCTGGCCAGGGAGGCTGCTGAGGAAGCAGAACGC
GAGCACCAGGAGGCCGTGGAGATGGCAGAGAAGATAGCTCGCTGGGAGGAGTGGAATAAA
CGACTGGAGGAAGTGAAAAGAGAAGAAAGAGAATTACTGGAGGCTCAGTCAATTCCCCTG
AGAAACTATTTAATGACCTATGTGATGCCAACTCTTATTCAGGGCCTGAATGAATGTTGC
AACGTCCGACCCGAAGACCCTGTTGATTTTCTGGCAGAATATCTCTTCAAGAACAATCCT
GAAGCACAGTGA

Enzyme 59 GenBank Gene ID

AK057426

Enzyme 59 GeneCard ID

AK7

Enzyme 59 GenAtlas ID

AK7

Enzyme 59 HGNC ID

HGNC:20091 Link Image

Enzyme 59 Chromosome Location

Enzyme 59 Locus

14q32.2

Enzyme 59 SNPs

SNPJam Report Link Image

Enzyme 59 General References

Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed ]

Enzyme 59 Metabolite References

Not Available

Enzyme 60 [top]

Enzyme 60 ID

5876

Enzyme 60 Name

cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A

Enzyme 60 Synonyms

Not Available

Enzyme 60 Gene Name

PDE10A

Enzyme 60 Protein Sequence

>cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A

MRIEERKSQHLTGLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRKNNKSEDESAP
KEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNQLLLYELSSIIKIATKADGFALYFLGEC
NNSLCIFTPPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGDERFPRGTGLE
SGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWASVAIHQVQVC
RGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALFQVDHKNKELY
SDLFDIGEEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADPRFNREVDLYT
GYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHR
IRHSECIYRVTMEKLSYHSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIF
VYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTD
LERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNI
FSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMM
TACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFY
NAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED

Enzyme 60 Number of Residues

779

Enzyme 60 Molecular Weight

88411.7

Enzyme 60 Theoretical pI

6.57

Enzyme 60 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 60 General Function

Involved in catalytic activity

Enzyme 60 Specific Function

Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate

Enzyme 60 Pathways

Purine Metabolism (map00230 )

Enzyme 60 Reactions

guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]

Enzyme 60 Pfam Domain Function

GAF (PF01590 )
PDEase_I (PF00233 )

Enzyme 60 Signals

None

Enzyme 60 Transmembrane Regions

None

Enzyme 60 Essentiality

Not Available

Enzyme 60 GenBank ID Protein

Not Available

Enzyme 60 UniProtKB/Swiss-Prot ID

Q9Y233

Enzyme 60 UniProtKB/Swiss-Prot Entry Name

PDE10_HUMAN Link Image

Enzyme 60 PDB ID

Not Available

Enzyme 60 Cellular Location

Not Available

Enzyme 60 Gene Sequence

>2340 bp

ATGAGGATAGAAGAGAGGAAATCCCAACATTTAACAGGTTTGACAGATGAAAAAGTGAAG
GCATATCTTTCTCTTCACCCCCAGGTATTAGATGAATTTGTATCTGAAAGTGTTAGTGCA
GAGACAGTAGAGAAATGGCTGAAGAGGAAGAACAACAAATCAGAAGATGAATCAGCTCCT
AAGGAAGTCAGCAGGTACCAAGATACGAATATGCAGGGAGTTGTATATGAACTAAACAGC
TATATAGAACAACGGTTGGACACAGGAGGAGACAACCAGCTACTCCTCTATGAACTGAGC
AGCATCATTAAAATAGCCACAAAAGCCGATGGATTTGCACTGTATTTCCTTGGAGAGTGC
AATAATAGCCTGTGTATATTCACGCCACCTGGGATAAAGGAAGGAAAACCCCGCCTCATC
CCTGCTGGGCCCATCACTCAGGGCACCACCGTCTCTGCTTATGTGGCCAAGTCCAGGAAA
ACACTGCTAGTAGAAGACATCCTTGGAGATGAACGATTTCCAAGAGGTACTGGACTGGAA
TCAGGGACTCGTATCCAGTCTGTTCTTTGCTTACCAATTGTCACTGCAATTGGTGACTTG
ATTGGTATTCTCGAGCTGTATCGGCACTGGGGCAAAGAAGCCTTCTGTCTTAGTCACCAG
GAGGTTGCAACAGCAAATCTTGCCTGGGCTTCAGTAGCAATACATCAGGTGCAGGTATGC
AGAGGCCTTGCCAAACAGACAGAATTGAATGACTTCCTACTCGACGTATCAAAAACATAT
TTTGATAACATAGTTGCAATAGATTCTCTACTTGAACACATAATGATATATGCAAAAAAC
CTGGTGAATGCCGATCGTTGTGCGCTTTTCCAGGTGGACCATAAGAACAAGGAGTTATAT
TCAGACCTTTTTGATATTGGAGAGGAAAAGGAAGGAAAACCTGTCTTCAAGAAGACCAAA
GAGATAAGATTTTCAATTGAGAAAGGAATTGCTGGCCAAGTAGCAAGAACAGGGGAAGTC
CTGAACATTCCAGATGCCTATGCAGACCCACGCTTTAACAGAGAAGTAGACTTGTACACA
GGCTACACCACGCGGAACATCCTGTGCATGCCCATCGTCAGCCGAGGCAGCGTGATAGGT
GTGGTGCAGATGGTCAACAAAATCAGTGGCAGTGCCTTCTCTAAAACAGATGAAAACAAC
TTCAAAATGTTTGCCGTCTTTTGTGCTTTAGCCTTACACTGTGCTAATATGTATCATAGA
ATTCGCCACTCAGAGTGCATTTACCGGGTAACGATGGAAAAGCTGTCCTACCATAGCATT
TGTACTTCAGAAGAGTGGCAAGGTCTCATGCAATTCACCCTTCCCGTGCGTCTCTGCAAA
GAAATTGAATTATTCCACTTTGACATTGGTCCTTTTGAAAACATGTGGCCTGGAATTTTT
GTCTACATGGTTCATCGGTCCTGTGGGACATCCTGCTTTGAGCTTGAAAAGTTGTGTCGT
TTTATTATGTCTGTGAAGAAGAACTATCGGCGGGTTCCTTATCACAACTGGAAGCATGCG
GTCACTGTAGCACACTGCATGTATGCCATACTTCAGAACAATCACACGCTTTTCACAGAC
CTTGAGCGCAAAGGACTGCTGATTGCGTGTCTGTGTCATGACCTGGACCACAGGGGCTTC
AGTAACAGCTACCTGCAGAAGTTCGACCACCCTCTGGCCGCTCTCTACTCCACTTCCACC
ATGGAGCAGCACCACTTCTCCCAGACTGTGTCCATCCTTCAGTTGGAAGGGCACAATATC
TTCTCCACTCTGAGCTCCAGTGAATATGAGCAGGTGCTTGAGATCATCCGCAAAGCCATC
ATTGCCACAGACCTTGCTTTATACTTTGGAAACAGGAAGCAGTTGGAAGAGATGTACCAG
ACCGGATCACTAAACCTTAATAATCAATCACATAGAGACCGTGTAATTGGTTTGATGATG
ACTGCCTGTGACCTTTGTTCTGTGACAAAACTGTGGCCCGTTACAAAATTGACGGCAAAT
GATATATATGCAGAATTCTGGGCTGAGGGTGATGAAATGAAGAAATTGGGAATACAGCCT
ATTCCTATGATGGACAGAGACAAGAAGGATGAAGTCCCCCAAGGCCAGCTTGGGTTCTAC
AATGCCGTGGCCATTCCCTGCTATACAACCCTTACCCAGATCCTCCCTCCCACGGAGCCT
CTTCTGAAAGCATGCAGGGATAATCTCAGTCAGTGGGAGAAGGTGATTCGAGGGGAGGAG
ACTGCAACCTGGATTTCATCCCCATCCGTGGCTCAGAAGGCAGCTGCATCTGAAGATTGA

Enzyme 60 GenBank Gene ID

AB020593

Enzyme 60 GeneCard ID

PDE10A

Enzyme 60 GenAtlas ID

PDE10A

Enzyme 60 HGNC ID

HGNC:8772

Enzyme 60 Chromosome Location

Enzyme 60 Locus

6q26

Enzyme 60 SNPs

SNPJam Report Link Image

Enzyme 60 General References

Fujishige K, Kotera J, Michibata H, Yuasa K, Takebayashi S, Okumura K, Omori K: Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A). J Biol Chem. 1999 Jun 25;274(26):18438-45. [PubMed ]
Loughney K, Snyder PB, Uher L, Rosman GJ, Ferguson K, Florio VA: Isolation and characterization of PDE10A, a novel human 3', 5'-cyclic nucleotide phosphodiesterase. Gene. 1999 Jun 24;234(1):109-17. [PubMed ]
Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Fujishige K, Kotera J, Yuasa K, Omori K: The human phosphodiesterase PDE10A gene genomic organization and evolutionary relatedness with other PDEs containing GAF domains. Eur J Biochem. 2000 Oct;267(19):5943-51. [PubMed ]
Gross-Langenhoff M, Hofbauer K, Weber J, Schultz A, Schultz JE: cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11. J Biol Chem. 2006 Feb 3;281(5):2841-6. Epub 2005 Dec 5. [PubMed ]
Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
Wang H, Liu Y, Hou J, Zheng M, Robinson H, Ke H: Structural insight into substrate specificity of phosphodiesterase 10. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5782-7. Epub 2007 Mar 26. [PubMed ]
Handa N, Mizohata E, Kishishita S, Toyama M, Morita S, Uchikubo-Kamo T, Akasaka R, Omori K, Kotera J, Terada T, Shirouzu M, Yokoyama S: Crystal structure of the GAF-B domain from human phosphodiesterase 10A complexed with its ligand, cAMP. J Biol Chem. 2008 Jul 11;283(28):19657-64. Epub 2008 May 13. [PubMed ]

Enzyme 60 Metabolite References

Not Available

Enzyme 61 [top]

Enzyme 61 ID

5877

Enzyme 61 Name

Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C

Enzyme 61 Synonyms

Cam-PDE 1C
hCam-3

Enzyme 61 Gene Name

PDE1C

Enzyme 61 Protein Sequence

>Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C

MESPTKEIEEFESNSLKYLQPEQIEKIWLRLRGLRKYKKTSQRLRSLVKQLERGEASVVD
LKKNLEYAATVLESVYIDETRRLLDTEDELSDIQSDAVPSEVRDWLASTFTRQMGMMLRR
SDEKPRFKSIVHAVQAGIFVERMYRRTSNMVGLSYPPAVIEALKDVDKWSFDVFSLNEAS
GDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTV
HYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENH
HLSAAYRLLQDDEEMNILINLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPE
AIEKPKALSLMLHTADISHPAKAWDLHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKS
TMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDETSQTGGTGQRRSSLNSISSSDAKR
SGVKTSGSEGSAPINNSVISVDYKSFKATWTEVVHINRERWRAKVPKEEKAKKEAEEKAR
LAAEEQQKEMEAKSQAEEGASGKAEKKTSGETKNQVNGTRANKSDNPRGKNSKAEKSSGE
QQQNGDFKDGKNKTDKKDHSNIGNDSKKTDGTKQRSHGSPAPSTSSTCRLTLPVIKPPLR
HFKRPAYASSSYAPSVSKKTDEHPARYKMLDQRIKMKKIQNISHNWNRK

Enzyme 61 Number of Residues

709

Enzyme 61 Molecular Weight

80759.7

Enzyme 61 Theoretical pI

9.31

Enzyme 61 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 61 General Function

Involved in catalytic activity

Enzyme 61 Specific Function

Enzyme 61 Pathways

Purine Metabolism (map00230 )

Enzyme 61 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 61 Pfam Domain Function

PDEase_I (PF00233 )
PDEase_I_N (PF08499 )

Enzyme 61 Signals

None

Enzyme 61 Transmembrane Regions

None

Enzyme 61 Essentiality

Not Available

Enzyme 61 GenBank ID Protein

193786355

Enzyme 61 UniProtKB/Swiss-Prot ID

Q14123

Enzyme 61 UniProtKB/Swiss-Prot Entry Name

PDE1C_HUMAN Link Image

Enzyme 61 PDB ID

Not Available

Enzyme 61 Cellular Location

Not Available

Enzyme 61 Gene Sequence

>2130 bp

ATGGAGTCGCCAACCAAGGAGATTGAAGAATTTGAGAGCAACTCTCTGAAATACCTGCAA
CCGGAACAGATCGAGAAAATCTGGCTTCGGCTCCGCGGGCTGAGGAAATATAAGAAAACG
TCCCAGAGATTACGGTCTTTGGTCAAACAATTAGAGAGAGGGGAAGCTTCAGTGGTAGAT
CTTAAGAAGAATTTGGAATATGCAGCCACAGTGCTTGAATCTGTGTATATTGATGAAACA
AGGAGACTCCTGGATACAGAGGATGAGCTCAGTGACATTCAGTCAGATGCTGTGCCTTCT
GAGGTCCGAGACTGGCTGGCCTCCACCTTCACGCGGCAGATGGGGATGATGCTCAGGAGG
AGCGACGAGAAGCCCCGGTTCAAGAGCATCGTTCACGCAGTGCAGGCTGGGATATTTGTG
GAGAGAATGTATAGACGGACATCAAACATGGTTGGACTGAGCTATCCACCAGCTGTTATT
GAGGCATTAAAGGATGTGGACAAGTGGTCCTTTGACGTCTTTTCCCTCAATGAGGCCAGT
GGGGATCATGCACTGAAATTTATTTTCTATGAACTACTCACACGTTATGATCTGATCAGC
CGTTTCAAGATCCCCATTTCTGCACTTGTCTCATTTGTGGAGGCCCTGGAAGTGGGATAC
AGCAAGCACAAAAATCCTTACCATAACTTAATGCACGCTGCCGATGTTACACAGACAGTG
CATTACCTCCTCTATAAGACAGGAGTGGCGAACTGGCTGACGGAGCTGGAGATCTTTGCT
ATAATCTTCTCAGCTGCCATCCATGACTACGAGCATACCGGAACCACCAACAATTTCCAC
ATTCAGACTCGGTCTGATCCAGCTATTCTGTATAATGACAGATCTGTACTGGAGAATCAC
CATTTAAGTGCAGCTTATCGCCTTCTGCAAGATGACGAGGAAATGAATATTTTGATTAAC
CTCTCAAAGGATGACTGGAGGGAGTTTCGAACCTTGGTAATTGAAATGGTGATGGCCACA
GATATGTCTTGTCACTTCCAACAAATCAAAGCAATGAAGACTGCTCTGCAGCAGCCAGAA
GCCATTGAAAAGCCAAAAGCCTTATCCCTTATGCTGCATACAGCAGATATTAGCCATCCA
GCAAAAGCATGGGACCTCCATCATCGCTGGACAATGTCACTCCTGGAGGAGTTCTTCAGA
CAGGGTGACAGAGAAGCAGAGCTGGGGCTGCCTTTTTCTCCTCTGTGTGACCGAAAGTCC
ACTATGGTTGCTCAGTCACAAGTAGGTTTCATTGATTTCATCGTGGAACCCACCTTCACT
GTGCTTACGGACATGACCGAGAAGATTGTGAGTCCATTAATCGATGAAACCTCTCAAACT
GGTGGGACAGGACAGAGGCGTTCGAGTTTGAATAGCATCAGCTCGTCAGATGCCAAGCGA
TCAGGTGTCAAGACCTCTGGTTCAGAGGGAAGTGCCCCGATCAACAATTCTGTCATCTCC
GTTGACTATAAGAGCTTTAAAGCTACTTGGACGGAAGTGGTGCACATCAATCGGGAGAGA
TGGAGGGCCAAGGTACCCAAAGAGGAGAAGGCCAAGAAGGAAGCAGAGGAAAAGGCTCGC
CTGGCCGCAGAGGAGCAGCAAAAGGAAATGGAAGCCAAAAGCCAGGCTGAAGAAGGCGCA
TCCGGCAAAGCTGAGAAAAAGACGTCTGGAGAAACTAAGAATCAAGTCAATGGAACACGG
GCAAACAAAAGTGACAACCCTCGTGGGAAAAATTCCAAAGCCGAGAAGTCATCAGGAGAA
CAGCAACAGAATGGTGACTTCAAAGATGGTAAAAATAAGACAGACAAGAAGGATCACTCT
AACATCGGAAATGATTCAAAGAAAACAGATGGCACAAAACAGCGTTCTCACGGCTCACCA
GCCCCAAGCACCAGCTCCACGTGTCGCCTTACGTTGCCAGTCATCAAGCCTCCTTTGCGT
CATTTTAAACGCCCTGCTTACGCATCTAGCTCCTATGCACCTTCAGTCTCAAAGAAAACT
GATGAGCATCCTGCAAGGTACAAGATGCTGGATCAGAGGATCAAAATGAAAAAGATTCAG
AACATCTCACATAACTGGAACAGAAAATAG

Enzyme 61 GenBank Gene ID

AK056170

Enzyme 61 GeneCard ID

PDE1C

Enzyme 61 GenAtlas ID

PDE1C

Enzyme 61 HGNC ID

HGNC:8776

Enzyme 61 Chromosome Location

Enzyme 61 Locus

7p14.3

Enzyme 61 SNPs

SNPJam Report Link Image

Enzyme 61 General References

Loughney K, Martins TJ, Harris EA, Sadhu K, Hicks JB, Sonnenburg WK, Beavo JA, Ferguson K: Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. J Biol Chem. 1996 Jan 12;271(2):796-806. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]

Enzyme 61 Metabolite References

Not Available

Enzyme 62 [top]

Enzyme 62 ID

5878

Enzyme 62 Name

Tyrosyl-tRNA synthetase, cytoplasmic

Enzyme 62 Synonyms

Tyrosyl--tRNA ligase
TyrRS

Enzyme 62 Gene Name

YARS

Enzyme 62 Protein Sequence

>Tyrosyl-tRNA synthetase, cytoplasmic

MGDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIA
DFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKG
TDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVD
AQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKED
VKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFA
AEVVHPGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEP
EEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLV
VVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDEE
LKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS

Enzyme 62 Number of Residues

528

Enzyme 62 Molecular Weight

59143.0

Enzyme 62 Theoretical pI

7.05

Enzyme 62 GO Classification

Function
ATP binding RNA binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleic acid binding nucleoside binding nucleotide binding purine nucleoside binding tRNA binding tyrosine-tRNA ligase activity
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation tyrosyl-tRNA aminoacylation
Component
cell part cytoplasm intracellular part

Enzyme 62 General Function

Involved in nucleotide binding

Enzyme 62 Specific Function

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction:tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr)

Enzyme 62 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Phenylalanine and Tyrosine Metabolism (map00400 )

Enzyme 62 Reactions

ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr [RN:R02918]

Enzyme 62 Pfam Domain Function

tRNA-synt_1b (PF00579 )
tRNA_bind (PF01588 )

Enzyme 62 Signals

None

Enzyme 62 Transmembrane Regions

None

Enzyme 62 Essentiality

Not Available

Enzyme 62 GenBank ID Protein

193785013

Enzyme 62 UniProtKB/Swiss-Prot ID

P54577

Enzyme 62 UniProtKB/Swiss-Prot Entry Name

SYYC_HUMAN Link Image

Enzyme 62 PDB ID

1Q11

Enzyme 62 PDB File

Show

Enzyme 62 3D Structure

Enzyme 62 Cellular Location

Not Available

Enzyme 62 Gene Sequence

>1587 bp

ATGGGGGACGCTCCCAGCCCTGAAGAGAAACTGCACCTTATCACCCGGAACCTGCAGGAG
GTTCTGGGGGAAGAGAAGCTGAAGGAGATACTGAAGGAGCGGGAACTTAAAATTTACTGG
GGAACGGCAACCACGGGCAAACCACATGTGGCTTACTTTGTGCCCATGTCAAAGATTGCA
GACTTCTTAAAGGCAGGGTGTGAGGTAACAATTCTGTTTGCGGACCTCCACGCATACCTG
GATAACATGAAAGCCCCATGGGAACTTCTAGAACTCCGAGTCAGTTACTATGAGAATGTG
ATCAAAGCAATGCTGGAGAGCATTGGTGTGCCCTTGGAGAAGCTCAAGTTCATCAAAGGC
ACTGATTACCAGCTCAGCAAAGAGTACACACTAGATGTGTACAGACTCTCCTCCGTGGTC
ACACAGCACGATTCCAAGAAGGCTGGAGCTGAGGTGGTAAAGCAGGTGGAGCACCCTTTG
CTGAGTGGCCTCTTATACCCCGGACTGCAGGCTTTGGATGAAGAGTATTTAAAAGTAGAT
GCCCAATTTGGAGGCATTGATCAGAGAAAGATTTTCACCTTTGCAGAGAAGTACCTCCCT
GCACTTGGCTATTCAAAACGGGTCCATCTGATGAATCCTATGGTTCCAGGATTAACAGGC
AGCAAAATGAGCTCTTCAGAAGAGGAGTCCAAGATTGATCTCCTTGATCGGAAGGAGGAT
GTGAAGAAAAAACTGAAGAAGGCCTTCTGTGAGCCAGGAAATGTGGAGAACAATGGGGTT
CTGTCCTTCATCAAGCATGTCCTTTTTCCCCTTAAGTCCGAGTTTGTGATCCTACGAGAT
GAGAAATGGGGTGGAAACAAAACCTACACAGCTTACGTGGACCTGGAAAAGGACTTTGCT
GCTGAGGTTGTACATCCTGGAGACCTGAAGAATTCTGTTGAAGTCGCACTGAACAAGTTG
CTGGATCCAATCCGGGAAAAGTTTAATACCCCTGCCCTGAAAAAACTGGCCAGCGCTGCC
TACCCAGATCCCTCAAAGCAGAAGCCAATGGCCAAAGGCCCTGCCAAGAATTCAGAACCA
GAGGAGGTCATCCCATCCCGGCTGGATATCCGTGTGGGGAAAATCATTACTGTGGAGAAG
CACCCAGATGCAGACAGCCTGTATGTAGAGAAGATTGACGTGGGGGAAGCTGAACCACGG
ACTGTGGTGAGCGGCCTGGTACAGTTCGTGCCCAAGGAGGAACTGCAGGACAGGCTGGTA
GTGGTGCTGTGCAACCTGAAACCCCAGAAGATGAGAGGAGTCGAGTCCCAAGGCATGCTT
CTGTGTGCTTCTATAGAAGGGATAAACCGCCAGGTTGAACCTCTGGACCCTCCGGCAGGC
TCTGCTCCTGGTGAGCACGTGTTTGTGAAGGGCTATGAAAAGGGCCAACCAGATGAGGAG
CTCAAGCCCAAGAAGAAAGTCTTCGAGAAGTTGCAGGCTGACTTCAAAATTTCTGAGGAG
TGCATCGCACAGTGGAAGCAAACCAACTTCATGACCAAGCTGGGCTCCATTTCCTGTAAA
TCGCTGAAAGGGGGGAACATTAGCTAG

Enzyme 62 GenBank Gene ID

AK125213

Enzyme 62 GeneCard ID

YARS

Enzyme 62 GenAtlas ID

YARS

Enzyme 62 HGNC ID

HGNC:12840 Link Image

Enzyme 62 Chromosome Location

Enzyme 62 Locus

1p35.1

Enzyme 62 SNPs

SNPJam Report Link Image

Enzyme 62 General References

Ribas de Pouplana L, Frugier M, Quinn CL, Schimmel P: Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria. Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):166-70. [PubMed ]
Kleeman TA, Wei D, Simpson KL, First EA: Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. J Biol Chem. 1997 May 30;272(22):14420-5. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Yang XL, Skene RJ, McRee DE, Schimmel P: Crystal structure of a human aminoacyl-tRNA synthetase cytokine. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15369-74. Epub 2002 Nov 11. [PubMed ]
Yang XL, Otero FJ, Skene RJ, McRee DE, Schimmel P, Ribas de Pouplana L: Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15376-80. Epub 2003 Dec 11. [PubMed ]
Jordanova A, Irobi J, Thomas FP, Van Dijck P, Meerschaert K, Dewil M, Dierick I, Jacobs A, De Vriendt E, Guergueltcheva V, Rao CV, Tournev I, Gondim FA, D'Hooghe M, Van Gerwen V, Callaerts P, Van Den Bosch L, Timmermans JP, Robberecht W, Gettemans J, Thevelein JM, De Jonghe P, Kremensky I, Timmerman V: Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy. Nat Genet. 2006 Feb;38(2):197-202. Epub 2006 Jan 22. [PubMed ]

Enzyme 62 Metabolite References

Not Available

Enzyme 63 [top]

Enzyme 63 ID

5879

Enzyme 63 Name

DNA ligase 3

Enzyme 63 Synonyms

DNA ligase III
Polydeoxyribonucleotide synthase [ATP] 3

Enzyme 63 Gene Name

LIG3

Enzyme 63 Protein Sequence

>DNA ligase 3

MSLAFKIFFPQTLRALSRKELCLFRKHHWRDVRQFSQWSETDLLHGHPLFLRRKPVLSFQ
GSHLRSRATYLVFLPGLHVGLCSGPCEMAEQRFCVDYAKRGTAGCKKCKEKIVKGVCRIG
KVVPNPFSESGGDMKEWYHIKCMFEKLERARATTKKIEDLTELEGWEELEDNEKEQITQH
IADLSSKAAGTPKKKAVVQAKLTTTGQVTSPVKGASFVTSTNPRKFSGFSAKPNNSGEAP
SSPTPKRSLSSSKCDPRHKDCLLREFRKLCAMVADNPSYNTKTQIIQDFLRKGSAGDGFH
GDVYLTVKLLLPGVIKTVYNLNDKQIVKLFSRIFNCNPDDMARDLEQGDVSETIRVFFEQ
SKSFPPAAKSLLTIQEVDEFLLRLSKLTKEDEQQQALQDIASRCTANDLKCIIRLIKHDL
KMNSGAKHVLDALDPNAYEAFKASRNLQDVVERVLHNAQEVEKEPGQRRALSVQASLMTP
VQPMLAEACKSVEYAMKKCPNGMFSEIKYDGERVQVHKNGDHFSYFSRSLKPVLPHKVAH
FKDYIPQAFPGGHSMILDSEVLLIDNKTGKPLPFGTLGVHKKAAFQDANVCLFVFDCIYF
NDVSLMDRPLCERRKFLHDNMVEIPNRIMFSEMKRVTKALDLADMITRVIQEGLEGLVLK
DVKGTYEPGKRHWLKVKKDYLNEGAMADTADLVVLGAFYGQGSKGGMMSIFLMGCYDPGS
QKWCTVTKCAGGHDDATLARLQNELDMVKISKDPSKIPSWLKVNKIYYPDFIVPDPKKAA
VWEITGAEFSKSEAHTADGISIRFPRCTRIRDDKDWKSATNLPQLKELYQLSKEKADFTV
VAGDEGSSTTGGSSEENKGPSGSAVSRKAPSKPSASTKKAEGKLSNSNSKDGNMQTAKPS
AMKVGEKLATKSSPVKVGEKRKAADETLCQTKVLLDIFTGVRLYLPPSTPDFSRLRRYFV
AFDGDLVQEFDMTSATHVLGSRDKNPAAQQVSPEWIWACIRKRRLVAPC

Enzyme 63 Number of Residues

1009

Enzyme 63 Molecular Weight

112906.0

Enzyme 63 Theoretical pI

9.43

Enzyme 63 GO Classification

Function
ATP binding DNA binding DNA ligase (ATP) activity DNA ligase (ATP) activity DNA ligase (ATP) activity DNA ligase (ATP) activity DNA ligase activity adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity cation binding ion binding ligase activity ligase activity, forming phosphoric ester bonds metal ion binding nucleic acid binding nucleoside binding purine nucleoside binding transition metal ion binding zinc ion binding
Process
DNA ligation DNA ligation involved in DNA repair DNA metabolic process DNA recombination DNA repair DNA replication cellular macromolecule metabolic process macromolecule metabolic process metabolic process
Component
cell part intracellular

Enzyme 63 General Function

Involved in DNA ligase (ATP) activity

Enzyme 63 Specific Function

Interacts with DNA-repair protein XRCC1 and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents

Enzyme 63 Pathways

Not Available

Enzyme 63 Reactions

ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = AMP + diphosphate + (deoxyribonucleotide)n+m [RN:R00381]

Enzyme 63 Pfam Domain Function

DNA_ligase_A_C (PF04679 )
DNA_ligase_A_M (PF01068 )
DNA_ligase_A_N (PF04675 )
zf-PARP (PF00645 )

Enzyme 63 Signals

None

Enzyme 63 Transmembrane Regions

None

Enzyme 63 Essentiality

Not Available

Enzyme 63 GenBank ID Protein

73747829

Enzyme 63 UniProtKB/Swiss-Prot ID

P49916

Enzyme 63 UniProtKB/Swiss-Prot Entry Name

DNLI3_HUMAN Link Image

Enzyme 63 PDB ID

1UW0

Enzyme 63 PDB File

Show

Enzyme 63 3D Structure

Enzyme 63 Cellular Location

Not Available

Enzyme 63 Gene Sequence

>3030 bp

ATGTCTTTGGCTTTCAAGATCTTCTTTCCACAAACCCTCCGTGCACTCAGCCGAAAAGAA
CTGTGCCTATTCCGAAAACATCACTGGCGTGATGTAAGACAATTCAGCCAGTGGTCAGAA
ACAGATCTGCTTCATGGACATCCCCTCTTCCTGAGAAGAAAGCCTGTTCTATCATTCCAG
GGAAGCCATCTAAGATCACGTGCCACCTACCTTGTTTTCTTGCCAGGGTTGCATGTGGGA
CTCTGCAGTGGCCCCTGTGAGATGGCTGAGCAACGGTTCTGTGTGGACTATGCCAAGCGT
GGCACAGCTGGCTGCAAAAAATGCAAGGAAAAGATTGTGAAGGGCGTATGCCGAATTGGC
AAAGTGGTGCCCAATCCCTTCTCAGAGTCTGGGGGTGATATGAAAGAGTGGTACCACATT
AAATGCATGTTTGAGAAACTAGAGCGGGCCCGGGCCACCACAAAAAAAATCGAGGACCTC
ACAGAGCTGGAAGGCTGGGAAGAGCTGGAAGATAATGAGAAGGAACAGATAACCCAGCAC
ATTGCAGATCTGTCTTCTAAGGCAGCAGGTACACCAAAGAAGAAAGCTGTTGTCCAGGCT
AAGTTGACAACCACTGGCCAGGTGACTTCTCCAGTGAAAGGCGCCTCATTTGTCACCAGT
ACCAATCCCCGGAAATTTTCTGGCTTTTCAGCCAAGCCCAACAACTCTGGGGAAGCCCCC
TCGAGCCCCACCCCTAAGAGAAGTCTGTCTTCAAGCAAATGTGACCCCAGGCATAAGGAC
TGTCTGCTACGGGAGTTTCGAAAGTTATGCGCCATGGTGGCCGATAATCCTAGCTACAAC
ACGAAGACCCAGATCATCCAGGACTTCCTTCGGAAAGGCTCAGCAGGAGATGGTTTCCAC
GGTGATGTGTACCTAACAGTGAAGCTGCTGCTGCCAGGAGTCATTAAGACTGTTTACAAC
TTGAACGATAAGCAGATTGTGAAGCTTTTCAGTCGCATTTTTAACTGCAACCCAGATGAT
ATGGCACGGGACCTAGAGCAGGGTGACGTGTCAGAGACAATCAGAGTCTTCTTTGAGCAG
AGCAAGTCTTTCCCCCCAGCTGCCAAGAGCCTCCTTACCATCCAGGAAGTGGATGAGTTC
CTTCTGCGGCTGTCCAAGCTCACCAAGGAGGATGAGCAGCAACAGGCCCTACAGGACATT
GCCTCCAGGTGTACAGCCAATGACCTTAAATGCATCATCAGGTTGATCAAACATGATCTG
AAGATGAACTCAGGTGCAAAACATGTGTTAGACGCCCTTGACCCCAATGCCTATGAAGCC
TTCAAAGCCTCGCGCAACCTGCAGGATGTGGTGGAGCGGGTCCTTCACAACGCGCAGGAG
GTGGAGAAGGAGCCGGGCCAGAGACGAGCTCTGAGCGTCCAGGCCTCGCTGATGACACCT
GTGCAGCCCATGTTGGCGGAGGCCTGCAAGTCCGTTGAGTATGCAATGAAGAAATGTCCC
AATGGCATGTTCTCTGAGATCAAGTACGATGGAGAGCGAGTCCAGGTGCATAAGAATGGA
GACCACTTCAGCTACTTCAGCCGCAGTCTCAAGCCCGTCCTTCCTCACAAGGTGGCCCAC
TTTAAGGACTACATTCCCCAGGCTTTTCCTGGGGGCCACAGCATGATCTTGGATTCTGAA
GTGCTTCTGATTGACAACAAGACAGGCAAACCACTGCCCTTTGGGACTCTGGGAGTACAC
AAGAAAGCAGCCTTCCAGGATGCTAATGTCTGCCTGTTTGTTTTTGATTGTATCTACTTT
AATGATGTCAGCTTGATGGACAGACCTCTGTGTGAGCGGCGGAAGTTTCTTCATGACAAC
ATGGTTGAAATTCCAAACCGGATCATGTTCTCAGAAATGAAGCGAGTCACAAAAGCTTTG
GACTTGGCTGACATGATAACCCGGGTGATCCAGGAGGGATTGGAGGGGCTGGTGCTGAAG
GATGTGAAGGGTACATATGAGCCTGGGAAGCGGCACTGGCTGAAAGTGAAGAAAGACTAT
TTGAACGAGGGGGCCATGGCCGACACAGCTGACCTGGTGGTCCTTGGAGCCTTCTATGGG
CAAGGGAGCAAAGGCGGCATGATGTCAATCTTCCTCATGGGCTGCTACGACCCTGGCAGC
CAGAAGTGGTGCACAGTCACCAAGTGTGCAGGAGGCCATGATGATGCCACGCTTGCCCGC
CTGCAGAATGAACTAGACATGGTGAAGATCAGCAAGGACCCCAGCAAAATACCCAGCTGG
TTGAAGGTCAACAAGATCTACTATCCTGACTTCATCGTCCCAGACCCAAAGAAAGCTGCC
GTGTGGGAGATCACAGGGGCTGAATTCTCCAAATCGGAGGCTCATACAGCTGACGGGATC
TCCATCCGATTCCCTCGCTGCACCCGAATCCGAGATGATAAGGACTGGAAATCTGCCACT
AACCTTCCCCAACTCAAGGAACTGTACCAGTTGTCCAAGGAGAAGGCAGACTTCACTGTA
GTGGCTGGAGATGAGGGGAGCTCCACTACAGGGGGTAGCAGTGAAGAGAATAAGGGTCCC
TCAGGGTCTGCTGTGTCCCGCAAGGCCCCCAGCAAGCCCTCAGCCAGTACCAAGAAAGCA
GAAGGGAAGCTGAGTAACTCCAACAGCAAAGATGGCAACATGCAGACTGCAAAGCCTTCC
GCTATGAAGGTGGGGGAGAAGCTGGCCACAAAGTCTTCTCCAGTGAAAGTAGGGGAGAAG
CGGAAAGCTGCTGATGAGACGCTGTGCCAAACAAAGGTATTGCTGGACATCTTCACTGGG
GTGCGGCTTTACTTGCCACCCTCCACACCAGACTTCAGCCGTCTCAGACGCTACTTTGTG
GCATTCGACGGGGACCTGGTACAGGAATTTGATATGACTTCAGCCACGCACGTGCTGGGT
AGCAGGGACAAGAACCCTGCGGCCCAGCAGGTCTCCCCAGAGTGGATTTGGGCATGTATC
CGGAAACGGAGACTGGTAGCTCCCTGCTAG

Enzyme 63 GenBank Gene ID

NM_013975.3 Link Image

Enzyme 63 GeneCard ID

LIG3

Enzyme 63 GenAtlas ID

LIG3

Enzyme 63 HGNC ID

HGNC:6600

Enzyme 63 Chromosome Location

Enzyme 63 Locus

17q11.2-q12

Enzyme 63 SNPs

SNPJam Report Link Image

Enzyme 63 General References

Wei YF, Robins P, Carter K, Caldecott K, Pappin DJ, Yu GL, Wang RP, Shell BK, Nash RA, Schar P, et al.: Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination. Mol Cell Biol. 1995 Jun;15(6):3206-16. [PubMed ]
Chen J, Tomkinson AE, Ramos W, Mackey ZB, Danehower S, Walter CA, Schultz RA, Besterman JM, Husain I: Mammalian DNA ligase III: molecular cloning, chromosomal localization, and expression in spermatocytes undergoing meiotic recombination. Mol Cell Biol. 1995 Oct;15(10):5412-22. [PubMed ]
Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Thornton KH, Krishnan VV, West MG, Popham J, Ramirez M, Thelen MP, Cosman M: Expression, purification, and biophysical characterization of the BRCT domain of human DNA ligase IIIalpha. Protein Expr Purif. 2001 Apr;21(3):401-11. [PubMed ]
Kulczyk AW, Yang JC, Neuhaus D: Solution structure and DNA binding of the zinc-finger domain from DNA ligase IIIalpha. J Mol Biol. 2004 Aug 13;341(3):723-38. [PubMed ]
Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]

Enzyme 63 Metabolite References

Not Available

Enzyme 64 [top]

Enzyme 64 ID

5880

Enzyme 64 Name

Aspartyl-tRNA synthetase, cytoplasmic

Enzyme 64 Synonyms

Aspartate--tRNA ligase
AspRS
Cell proliferation-inducing gene 40 protein

Enzyme 64 Gene Name

DARS

Enzyme 64 Protein Sequence

>Aspartyl-tRNA synthetase, cytoplasmic

MPSASASRKSQEKPREIMDAAEDYAKERYGISSMIQSQEKPDRVLVRVRDLTIQKADEVV
WVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVV
RKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAEGEEEGRATVNQDTRL
DNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYF
KNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYH
EVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLREAGV
EMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFM
RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLF
LGLHNVRQTSMFPRDPKRLTP

Enzyme 64 Number of Residues

501

Enzyme 64 Molecular Weight

57135.8

Enzyme 64 Theoretical pI

6.52

Enzyme 64 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity aspartate-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleic acid binding nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process aspartyl-tRNA aminoacylation biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 64 General Function

Involved in nucleotide binding

Enzyme 64 Specific Function

Enzyme 64 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )

Enzyme 64 Reactions

ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp [RN:R05577]

Enzyme 64 Pfam Domain Function

tRNA-synt_2 (PF00152 )
tRNA_anti (PF01336 )

Enzyme 64 Signals

None

Enzyme 64 Transmembrane Regions

None

Enzyme 64 Essentiality

Not Available

Enzyme 64 GenBank ID Protein

62896511

Enzyme 64 UniProtKB/Swiss-Prot ID

P14868

Enzyme 64 UniProtKB/Swiss-Prot Entry Name

SYDC_HUMAN Link Image

Enzyme 64 PDB ID

Not Available

Enzyme 64 Cellular Location

Not Available

Enzyme 64 Gene Sequence

>1506 bp

ATGCCCAGCGCCAGCGCCAGCCGCAAGAGTCAGGAGAAGCCGCGGGAGATCATGGACGCG
GCGGAAGATTATGCTAAAGAGAGATATGGAATATCTTCAATGATACAATCACACGAAAAA
CCAGATCGAGTTTTGGTTCGGGTTAGAGACTTGACAATACAAAAAGCTGATGAAGTTGTT
TGGGTACGTGCAAGAGTTCATACAAGCAGAGCTAAAGGGAAACAGTGCTTCTTAGTCCTA
CGTCAGCAGCAGTTTAATGTCCAGGCTCTTGTGGCGGTGGGAGACCATGCAAGCAAGCAG
ATGGTTAAATTTGCTGCCAACATCAACAAAGAGAGCATTGTGGATGTAGAAGGTGTTGTG
AGAAAAGTGAATCAGAAAATTGGAAGCTGTACACAGCAAGACGTTGAGTTACATGTTCAG
AAGATTTATGTGATCAGTTTGGCTGAACCCCGTCTGCCCCTGCAGCTGGATGATGCTGTT
CGGCCTGAGGCAGAAGGAGAAGAGGAAGGAAGAGCTACTGTTAACCAGGATACAAGATTA
GACAACAGAGTCATTGATCTTAGGACATCAACTAGTCAGGCAGTCTTCCGTCTCCAGTCT
GGCATCTGCCATCTCTTCCGAGAAACTTTAATTAACAAAGGTTTTGTGGAAATCCAAACT
CCTAAAATTATTTCAGCTGCCAGTGAAGGAGGAGCCAATGTTTTTACTGTGTCATATTTT
AAAAATAATGCATACCTGGCTCAGTCCCCACAGCTATATAAGCAAATGTGCATTTGTGCT
GATTTTGAGAAGGTTTTCTCTATTGGACCAGTATTCAGAGCGGAAGACTCTAATACCCAT
AGACATCTAACTGAGTTTGTTGGTTTGGACATTGAAATGGCTTTTAATTACCATTACCAC
GAAGTTATGGAAGAAATTGCTGACACCATGGTACAAATATTCAAAGGACTTCAAGAAAGG
TTTCAGACTGAAATTCAAACAGTGAATAAACAGTTCCCATGTGAGCCATTCAAATTTTTG
GAGCCAACTCTAAGACTAGAATATTGTGAAGCATTGGCTATGCTTAGGGAAGCTGGAGTC
GAAATGGGAGATGAAGACGATCTGAGCACACCAAATGAAAAGCTGTTGGGTCATTTGGTA
AAGGAAAAGTATGATACAGATTTTTATATTCTTGATAAATATCCATTGGCTGTAAGACCT
TTCTATACCATGCCTGACCCAAGAAATCCCAAACAGTCCAACTCTTACGATATGTTCATG
AGAGGAGAAGAAATATTGTCAGGAGCTCAAAGAATACATGATCCTCAACTGCTAACAGAG
AGAGCTTTACATCATGGAATTGATTTGGAGAAAATTAAGGCTTACATTGATTCCTTCCGC
TTTGGAGCCCCTCCTCATGCTGGTGGAGGCATTGGATTGGAACGAGTTACTATGCTGTTT
CTGGGATTGCATAATGTTCGTCAGACCTCCATGTTCCCTCGTGATCCCAAACGACTCACT
CCTTAA

Enzyme 64 GenBank Gene ID

AK222476

Enzyme 64 GeneCard ID

DARS

Enzyme 64 GenAtlas ID

DARS

Enzyme 64 HGNC ID

HGNC:2678

Enzyme 64 Chromosome Location

Enzyme 64 Locus

2q21.3

Enzyme 64 SNPs

SNPJam Report Link Image

Enzyme 64 General References

Jacobo-Molina A, Peterson R, Yang DC: cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase. J Biol Chem. 1989 Oct 5;264(28):16608-12. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
Guzzo CM, Yang DC: Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro. Biochem Biophys Res Commun. 2008 Jan 25;365(4):718-23. Epub 2007 Nov 20. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 64 Metabolite References

Not Available

Enzyme 65 [top]

Enzyme 65 ID

5881

Enzyme 65 Name

cAMP-specific 3',5'-cyclic phosphodiesterase 4B

Enzyme 65 Synonyms

DPDE4
PDE32

Enzyme 65 Gene Name

PDE4B

Enzyme 65 Protein Sequence

>cAMP-specific 3',5'-cyclic phosphodiesterase 4B

MKKSRSVMTVMADDNVKDYFECSLSKSYSSSSNTLGIDLWRGRRCCSGNLQLPPLSQRQS
ERARTPEGDGISRPTTLPLTTLPSIAITTVSQECFDVENGPSPGRSPLDPQASSSAGLVL
HATFPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDLIVTPFAQVLASLRSVR
NNFTILTNLHGTSNKRSPAASQPPVSRVNPQEESYQKLAMETLEELDWCLDQLETIQTYR
SVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKK
KQQLMTQISGVKKLMHSSSLNNTSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSH
NRPLTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDVAYHNSLHAADVAQSTHV
LLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHL
AVGFKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTS
SGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEI
SPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSP
SPPLDEQNRDCQGLMEKFQFELTLDEEDSEGPEKEGEGHSYFSSTKTLCVIDPENRDSLG
ETDIDIATEDKSPVDT

Enzyme 65 Number of Residues

736

Enzyme 65 Molecular Weight

83342.7

Enzyme 65 Theoretical pI

4.89

Enzyme 65 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 65 General Function

Involved in catalytic activity

Enzyme 65 Specific Function

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in mediating central nervous system effects of therapeutic agents ranging from antidepressants to antiasthmatic and anti-inflammatory agents

Enzyme 65 Pathways

Purine Metabolism (map00230 )

Enzyme 65 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 65 Pfam Domain Function

PDEase_I (PF00233 )

Enzyme 65 Signals

None

Enzyme 65 Transmembrane Regions

None

Enzyme 65 Essentiality

Not Available

Enzyme 65 GenBank ID Protein

Not Available

Enzyme 65 UniProtKB/Swiss-Prot ID

Q07343

Enzyme 65 UniProtKB/Swiss-Prot Entry Name

PDE4B_HUMAN Link Image

Enzyme 65 PDB ID

1TB5

Enzyme 65 PDB File

Show

Enzyme 65 3D Structure

Enzyme 65 Cellular Location

Not Available

Enzyme 65 Gene Sequence

>2211 bp

ATGAAGAAAAGCAGGAGTGTGATGACGGTGATGGCTGATGATAATGTTAAAGATTATTTT
GAATGTAGCTTGAGTAAATCCTACAGTTCTTCCAGTAACACACTTGGGATCGACCTCTGG
AGAGGGAGAAGGTGTTGCTCAGGAAACTTACAGTTACCACCACTGTCTCAAAGACAGAGT
GAAAGGGCAAGGACTCCTGAGGGAGATGGTATTTCCAGGCCGACCACACTGCCTTTGACA
ACGCTTCCAAGCATTGCTATTACAACTGTAAGCCAGGAGTGCTTTGATGTGGAAAATGGC
CCTTCCCCAGGTCGGAGTCCACTGGATCCCCAGGCCAGCTCTTCCGCTGGGCTGGTACTT
CACGCCACCTTTCCTGGGCACAGCCAGCGCAGAGAGTCATTTCTCTACAGATCAGACAGC
GACTATGACTTGTCACCAAAGGCGATGTCGAGAAACTCTTCTCTTCCAAGCGAGCAACAC
GGCGATGACTTGATTGTAACTCCTTTTGCCCAGGTCCTTGCCAGCTTGCGAAGTGTGAGA
AACAACTTCACTATACTGACAAACCTTCATGGTACATCTAACAAGAGGTCCCCAGCTGCT
AGTCAGCCTCCTGTCTCCAGAGTCAACCCACAAGAAGAATCTTATCAAAAATTAGCAATG
GAAACGCTGGAGGAATTAGACTGGTGTTTAGACCAGCTAGAGACCATACAGACCTACCGG
TCTGTCAGTGAGATGGCTTCTAACAAGTTCAAAAGAATGCTGAACCGGGAGCTGACACAC
CTCTCAGAGATGAGCCGATCAGGGAACCAGGTGTCTGAATACATTTCAAATACTTTCTTA
GACAAGCAGAATGATGTGGAGATCCCATCTCCTACCCAGAAAGACAGGGAGAAAAAGAAA
AAGCAGCAGCTCATGACCCAGATAAGTGGAGTGAAGAAATTAATGCATAGTTCAAGCCTA
AACAATACAAGCATCTCACGCTTTGGAGTCAACACTGAAAATGAAGATCACCTGGCCAAG
GAGCTGGAAGACCTGAACAAATGGGGTCTTAACATCTTTAATGTGGCTGGATATTCTCAC
AATAGACCCCTAACATGCATCATGTATGCTATATTCCAGGAAAGAGACCTCCTAAAGACA
TTCAGAATCTCATCTGACACATTTATAACCTACATGATGACTTTAGAAGACCATTACCAT
TCTGACGTGGCATATCACAACAGCCTGCACGCTGCTGATGTAGCCCAGTCGACCCATGTT
CTCCTTTCTACACCAGCATTAGACGCTGTCTTCACAGATTTGGAGATCCTGGCTGCCATT
TTTGCAGCTGCCATCCATGACGTTGATCATCCTGGAGTCTCCAATCAGTTTCTCATCAAC
ACAAATTCAGAACTTGCTTTGATGTATAATGATGAATCTGTGTTGGAAAATCATCACCTT
GCTGTGGGTTTCAAACTGCTGCAAGAAGAACACTGTGACATCTTCATGAATCTCACCAAG
AAGCAGCGTCAGACACTCAGGAAGATGGTTATTGACATGGTGTTAGCAACTGATATGTCT
AAACATATGAGCCTGCTGGCAGACCTGAAGACAATGGTAGAAACGAAGAAAGTTACAAGT
TCAGGCGTTCTTCTCCTAGACAACTATACCGATCGCATTCAGGTCCTTCGCAACATGGTA
CACTGTGCAGACCTGAGCAACCCCACCAAGTCCTTGGAATTGTATCGGCAATGGACAGAC
CGCATCATGGAGGAATTTTTCCAGCAGGGAGACAAAGAGCGGGAGAGGGGAATGGAAATT
AGCCCAATGTGTGATAAACACACAGCTTCTGTGGAAAAATCCCAGGTTGGTTTCATCGAC
TACATTGTCCATCCATTGTGGGAGACATGGGCAGATTTGGTACAGCCTGATGCTCAGGAC
ATTCTCGATACCTTAGAAGATAACAGGAACTGGTATCAGAGCATGATACCTCAAAGTCCC
TCACCACCACTGGACGAGCAGAACAGGGACTGCCAGGGTCTGATGGAGAAGTTTCAGTTT
GAACTGACTCTCGATGAGGAAGATTCTGAAGGACCTGAGAAGGAGGGAGAGGGACACAGC
TATTTCAGCAGCACAAAGACGCTTTGTGTGATTGATCCAGAAAACAGAGATTCCCTGGGA
GAGACTGACATAGACATTGCAACAGAAGACAAGTCCCCCGTGGATACATAA

Enzyme 65 GenBank Gene ID

L20966

Enzyme 65 GeneCard ID

PDE4B

Enzyme 65 GenAtlas ID

PDE4B

Enzyme 65 HGNC ID

HGNC:8781

Enzyme 65 Chromosome Location

Enzyme 65 Locus

1p31

Enzyme 65 SNPs

SNPJam Report Link Image

Enzyme 65 General References

Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed ]
Huston E, Lumb S, Russell A, Catterall C, Ross AH, Steele MR, Bolger GB, Perry MJ, Owens RJ, Houslay MD: Molecular cloning and transient expression in COS7 cells of a novel human PDE4B cAMP-specific phosphodiesterase, HSPDE4B3. Biochem J. 1997 Dec 1;328 ( Pt 2):549-58. [PubMed ]
McLaughlin MM, Cieslinski LB, Burman M, Torphy TJ, Livi GP: A low-Km, rolipram-sensitive, cAMP-specific phosphodiesterase from human brain. Cloning and expression of cDNA, biochemical characterization of recombinant protein, and tissue distribution of mRNA. J Biol Chem. 1993 Mar 25;268(9):6470-6. [PubMed ]
Xu RX, Hassell AM, Vanderwall D, Lambert MH, Holmes WD, Luther MA, Rocque WJ, Milburn MV, Zhao Y, Ke H, Nolte RT: Atomic structure of PDE4: insights into phosphodiesterase mechanism and specificity. Science. 2000 Jun 9;288(5472):1822-5. [PubMed ]
Xu RX, Rocque WJ, Lambert MH, Vanderwall DE, Luther MA, Nolte RT: Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram. J Mol Biol. 2004 Mar 19;337(2):355-65. [PubMed ]
Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G: A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases. Mol Cell. 2004 Jul 23;15(2):279-86. [PubMed ]
Card GL, England BP, Suzuki Y, Fong D, Powell B, Lee B, Luu C, Tabrizizad M, Gillette S, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: Structural basis for the activity of drugs that inhibit phosphodiesterases. Structure. 2004 Dec;12(12):2233-47. [PubMed ]
Card GL, Blasdel L, England BP, Zhang C, Suzuki Y, Gillette S, Fong D, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design. Nat Biotechnol. 2005 Feb;23(2):201-7. Epub 2005 Jan 30. [PubMed ]
Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed ]
Hamblin JN, Angell TD, Ballantine SP, Cook CM, Cooper AW, Dawson J, Delves CJ, Jones PS, Lindvall M, Lucas FS, Mitchell CJ, Neu MY, Ranshaw LE, Solanke YE, Somers DO, Wiseman JO: Pyrazolopyridines as a novel structural class of potent and selective PDE4 inhibitors. Bioorg Med Chem Lett. 2008 Jul 15;18(14):4237-41. Epub 2008 May 17. [PubMed ]

Enzyme 65 Metabolite References

Not Available

Enzyme 66 [top]

Enzyme 66 ID

5882

Enzyme 66 Name

Ubiquitin-conjugating enzyme E2 D3

Enzyme 66 Synonyms

Ubiquitin carrier protein D3
Ubiquitin-conjugating enzyme E2(17)KB 3
Ubiquitin-conjugating enzyme E2-17 kDa 3
Ubiquitin-protein ligase D3

Enzyme 66 Gene Name

UBE2D3

Enzyme 66 Protein Sequence

>Ubiquitin-conjugating enzyme E2 D3

MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDY
PFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLV
PEIARIYKTDRDKYNRISREWTQKYAM

Enzyme 66 Number of Residues

147

Enzyme 66 Molecular Weight

16687.0

Enzyme 66 Theoretical pI

7.95

Enzyme 66 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 66 General Function

Involved in acid-amino acid ligase activity

Enzyme 66 Specific Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA- linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML- NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction

Enzyme 66 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 66 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 66 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 66 Signals

None

Enzyme 66 Transmembrane Regions

None

Enzyme 66 Essentiality

Not Available

Enzyme 66 GenBank ID Protein

4507777

Enzyme 66 UniProtKB/Swiss-Prot ID

P61077

Enzyme 66 UniProtKB/Swiss-Prot Entry Name

UB2D3_HUMAN Link Image

Enzyme 66 PDB ID

1X23

Enzyme 66 PDB File

Show

Enzyme 66 3D Structure

Enzyme 66 Cellular Location

Not Available

Enzyme 66 Gene Sequence

>444 bp

ATGGCGCTGAAACGGATTAATAAGGAACTTAGTGATTTGGCCCGTGACCCTCCAGCACAA
TGTTCTGCAGGTCCAGTTGGGGATGATATGTTTCATTGGCAAGCCACAATTATGGGACCT
AATGACAGCCCATATCAAGGCGGTGTATTCTTTTTGACAATTCATTTTCCTACAGACTAC
CCCTTCAAACCACCTAAGGTTGCATTTACAACAAGAATTTATCATCCAAATATTAACAGT
AATGGCAGCATTTGTCTCGATATTCTAAGATCACAGTGGTCGCCTGCTTTAACAATTTCT
AAAGTTCTTTTATCCATTTGTTCACTGCTATGTGATCCAAACCCAGATGACCCCCTAGTG
CCAGAGATTGCACGGATCTATAAAACAGACAGAGATAAGTACAACAGAATATCTCGGGAA
TGGACTCAGAAGTATGCCATGTGA

Enzyme 66 GenBank Gene ID

NM_003340.5 Link Image

Enzyme 66 GeneCard ID

UBE2D3

Enzyme 66 GenAtlas ID

UBE2D3

Enzyme 66 HGNC ID

HGNC:12476 Link Image

Enzyme 66 Chromosome Location

Enzyme 66 Locus

4q24

Enzyme 66 SNPs

SNPJam Report Link Image

Enzyme 66 General References

Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM: Identification of a family of closely related human ubiquitin conjugating enzymes. J Biol Chem. 1995 Dec 22;270(51):30408-14. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gonen H, Bercovich B, Orian A, Carrano A, Takizawa C, Yamanaka K, Pagano M, Iwai K, Ciechanover A: Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha. J Biol Chem. 1999 May 21;274(21):14823-30. [PubMed ]
Murata S, Minami Y, Minami M, Chiba T, Tanaka K: CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2001 Dec;2(12):1133-8. Epub 2001 Nov 21. [PubMed ]
Yogosawa S, Miyauchi Y, Honda R, Tanaka H, Yasuda H: Mammalian Numb is a target protein of Mdm2, ubiquitin ligase. Biochem Biophys Res Commun. 2003 Mar 21;302(4):869-72. [PubMed ]
Rajendra R, Malegaonkar D, Pungaliya P, Marshall H, Rasheed Z, Brownell J, Liu LF, Lutzker S, Saleem A, Rubin EH: Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53. J Biol Chem. 2004 Aug 27;279(35):36440-4. Epub 2004 Jul 9. [PubMed ]
Saville MK, Sparks A, Xirodimas DP, Wardrop J, Stevenson LF, Bourdon JC, Woods YL, Lane DP: Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in vivo. J Biol Chem. 2004 Oct 1;279(40):42169-81. Epub 2004 Jul 26. [PubMed ]
Huang J, Huang Q, Zhou X, Shen MM, Yen A, Yu SX, Dong G, Qu K, Huang P, Anderson EM, Daniel-Issakani S, Buller RM, Payan DG, Lu HH: The poxvirus p28 virulence factor is an E3 ubiquitin ligase. J Biol Chem. 2004 Dec 24;279(52):54110-6. Epub 2004 Oct 20. [PubMed ]
Polanowska J, Martin JS, Garcia-Muse T, Petalcorin MI, Boulton SJ: A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA damage sites. EMBO J. 2006 May 17;25(10):2178-88. Epub 2006 Apr 20. [PubMed ]
Ohbayashi N, Okada K, Kawakami S, Togi S, Sato N, Ikeda O, Kamitani S, Muromoto R, Sekine Y, Kawai T, Akira S, Matsuda T: Physical and functional interactions between ZIP kinase and UbcH5. Biochem Biophys Res Commun. 2008 Aug 8;372(4):708-12. Epub 2008 Jun 2. [PubMed ]
Zhang S, Chea J, Meng X, Zhou Y, Lee EY, Lee MY: PCNA is ubiquitinated by RNF8. Cell Cycle. 2008 Nov 1;7(21):3399-404. [PubMed ]
Umebayashi K, Stenmark H, Yoshimori T: Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation. Mol Biol Cell. 2008 Aug;19(8):3454-62. Epub 2008 May 28. [PubMed ]
Saha A, Deshaies RJ: Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol Cell. 2008 Oct 10;32(1):21-31. [PubMed ]
Kubori T, Hyakutake A, Nagai H: Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions. Mol Microbiol. 2008 Mar;67(6):1307-19. Epub 2008 Feb 13. [PubMed ]
David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
Wu K, Kovacev J, Pan ZQ: Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate. Mol Cell. 2010 Mar 26;37(6):784-96. [PubMed ]
Brzovic PS, Lissounov A, Christensen DE, Hoyt DW, Klevit RE: A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination. Mol Cell. 2006 Mar 17;21(6):873-80. [PubMed ]

Enzyme 66 Metabolite References

Not Available

Enzyme 67 [top]

Enzyme 67 ID

5883

Enzyme 67 Name

Asparaginyl-tRNA synthetase, cytoplasmic

Enzyme 67 Synonyms

Asparagine--tRNA ligase
AsnRS

Enzyme 67 Gene Name

NARS

Enzyme 67 Protein Sequence

>Asparaginyl-tRNA synthetase, cytoplasmic

MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISK
SQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGAL
EGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVA
VYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGE
NMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSS
QLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCD
VVDRILKSPAGSIVHELNPNFQPPKRPFKRMNYSDAIVWLKEHDVKKEDGTFYEFGEDIP
EAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIF
DSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP
RFVQRCTP

Enzyme 67 Number of Residues

548

Enzyme 67 Molecular Weight

62942.4

Enzyme 67 Theoretical pI

6.17

Enzyme 67 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity asparagine-tRNA ligase activity aspartate-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleic acid binding nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process asparaginyl-tRNA aminoacylation aspartyl-tRNA aminoacylation biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 67 General Function

Involved in nucleotide binding

Enzyme 67 Specific Function

ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn)

Enzyme 67 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )

Enzyme 67 Reactions

ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn [RN:R03648]

Enzyme 67 Pfam Domain Function

tRNA-synt_2 (PF00152 )
tRNA_anti (PF01336 )

Enzyme 67 Signals

None

Enzyme 67 Transmembrane Regions

None

Enzyme 67 Essentiality

Not Available

Enzyme 67 GenBank ID Protein

2764505

Enzyme 67 UniProtKB/Swiss-Prot ID

O43776

Enzyme 67 UniProtKB/Swiss-Prot Entry Name

SYNC_HUMAN Link Image

Enzyme 67 PDB ID

Not Available

Enzyme 67 Cellular Location

Not Available

Enzyme 67 Gene Sequence

>1647 bp

ATGGTGCTAGCAGAGCTGTACGTCTCTGACCGAGAGGGAAGCGATGCCACGGGAGATGGA
ACCAAGGAGAAACCATTTAAAACAGGTCTAAAGGCTTTGATGACAGTAGGGAAAGAACCA
TTTCCTACCATTTACGTAGATTCACAAAAAGAAAATGAGAGGTGGAATGTTATTTCTAAA
TCACAGTTGAAGAACATTAAAAAGATGTGGCATAGGGAACAAATGAAGAGTGAATCCCGG
GAAAAGAAAGAGGCAGAAGATAGTTTACGAAGAGAAAAGAACCTGGAAGAAGCAAAGAAG
ATTACCATTAAAAATGATCCAAGTCTCCCAGAGCCAAAATGTGTGAAGATTGGTGCGTTA
GAAGGATATAGAGGCCAAAGAGTAAAGGTGTTTGGCTGGGTCCACAGGCTGCGCAGGCAA
GGAAAGAATTTAATGTTTCTGGTGTTGCGAGATGGTACAGGTTATCTTCAGTGTGTCTTG
GCGGATGAGTTGTGTCAGTGCTACAATGGAGTTCTCTTGTCCACGGAGAGCAGTGTTGCA
GTGTATGGAATGCTAAATCTTACCCCAAAGGGCAAGCAGGCTCCAGGTGGCCATGAGCTG
AGTTGTGACTTCTGGGAACTAATTGGGTTGGCCCCTGCTGGAGGAGCTGACAACCTGATC
AATGAGGAGTCTGACGTTGATGTCCAGCTCAACAACAGACACATGATGATCCGAGGAGAA
AACATGTCCAAAATCCTAAAAGCACGATCCATGGTCACCAGGTGCTTTAGAGATCACTTC
TTTGATAGGGGGTACTATGAAGTTACTCCTCCAACATTAGTGCAAACACAAGTAGAAGGT
GGTGCCACACTCTTCAAGCTTGACTATTTTGGGGAAGAGGCATTTTTGACTCAATCCTCT
CAGTTGTACTTGGAGACCTGCCTCCCAGCCCTGGGAGATGTTTTTTGTATTGCTCAGTCA
TACCGGGCAGAGCAGTCCAGAACACGAAGGCACCTGGCTGAGTACACTCACGTGGAAGCT
GAGTGTCCTTTCCTGACTTTTGACGACCTCCTGAACCGGTTGGAGGACTTGGTTTGTGAT
GTGGTAGATCGAATATTGAAGTCACCTGCAGGGAGCATAGTGCATGAGCTCAACCCGAAC
TTTCAGCCCCCCAAACGGCCTTTCAAACGGATGAACTATTCAGATGCTATCGTTTGGCTA
AAAGAACATGATGTAAAGAAAGAAGATGGAACTTTCTATGAATTTGGAGAAGATATCCCA
GAAGCTCCTGAGAGACTGATGACAGACACCATTAATGAACCAATCTTGCTGTGTCGATTT
CCTGTGGAGATCAAGTCCTTCTACATGCAGCGATGTCCTGAGGATTCCCGTCTTACTGAA
TCTGTCGACGTGTTGATGCCCAATGTTGGTGAGATTGTGGGAGGCTCAATGCGTATCTTT
GATAGTGAAGAAATACTGGCAGGTTATAAAAGGGAAGGGATTGACCCCACTCCCTATTAC
TGGTATACGGATCAGAGAAAATACGGTACATGTCCCCATGGAGGATATGGCTTGGGCTTG
GAACGATTCTTAACGTGGATTCTGAATAGGTATCACATCCGAGACGTGTGCTTATACCCT
CGATTTGTCCAGCGTTGCACGCCATAA

Enzyme 67 GenBank Gene ID

AJ000334

Enzyme 67 GeneCard ID

NARS

Enzyme 67 GenAtlas ID

NARS

Enzyme 67 HGNC ID

HGNC:7643

Enzyme 67 Chromosome Location

Enzyme 67 Locus

18q21.31

Enzyme 67 SNPs

SNPJam Report Link Image

Enzyme 67 General References

Beaulande M, Tarbouriech N, Hartlein M: Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen. Nucleic Acids Res. 1998 Jan 15;26(2):521-4. [PubMed ]
Shiba K, Motegi H, Yoshida M, Noda T: Human asparaginyl-tRNA synthetase: molecular cloning and the inference of the evolutionary history of Asx-tRNA synthetase family. Nucleic Acids Res. 1998 Nov 15;26(22):5045-51. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Xu G, Shin SB, Jaffrey SR: Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini. Proc Natl Acad Sci U S A. 2009 Nov 17;106(46):19310-5. Epub 2009 Nov 5. [PubMed ]
Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 67 Metabolite References

Not Available

Enzyme 68 [top]

Enzyme 68 ID

5884

Enzyme 68 Name

cAMP-specific 3',5'-cyclic phosphodiesterase 7B

Enzyme 68 Synonyms

Not Available

Enzyme 68 Gene Name

PDE7B

Enzyme 68 Protein Sequence

>cAMP-specific 3',5'-cyclic phosphodiesterase 7B

MSCLMVERCGEILFENPDQNAKCVCMLGDIRLRGQTGVRAERRGSYPFIDFRLLNSTTYS
GEIGTKKKVKRLLSFQRYFHASRLLRGIIPQAPLHLLDEDYLGQARHMLSKVGMWDFDIF
LFDRLTNGNSLVTLLCHLFNTHGLIHHFKLDMVTLHRFLVMVQEDYHSQNPYHNAVHAAD
VTQAMHCYLKEPKLASFLTPLDIMLGLLAAAAHDVDHPGVNQPFLIKTNHHLANLYQNMS
VLENHHWRSTIGMLRESRLLAHLPKEMTQDIEQQLGSLILATDINRQNEFLTRLKAHLHN
KDLRLEDAQDRHFMLQIALKCADICNPCRIWEMSKQWSERVCEEFYRQGELEQKFELEIS
PLCNQQKDSIPSIQIGFMSYIVEPLFREWAHFTGNSTLSENMLGHLAHNKAQWKSLLPRQ
HRSRGSSGSGPDHDHAGQGTESEEQEGDSP

Enzyme 68 Number of Residues

450

Enzyme 68 Molecular Weight

51834.9

Enzyme 68 Theoretical pI

7.03

Enzyme 68 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 68 General Function

Involved in catalytic activity

Enzyme 68 Specific Function

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain

Enzyme 68 Pathways

Purine Metabolism (map00230 )

Enzyme 68 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 68 Pfam Domain Function

PDEase_I (PF00233 )

Enzyme 68 Signals

None

Enzyme 68 Transmembrane Regions

None

Enzyme 68 Essentiality

Not Available

Enzyme 68 GenBank ID Protein

8439497

Enzyme 68 UniProtKB/Swiss-Prot ID

Q9NP56

Enzyme 68 UniProtKB/Swiss-Prot Entry Name

PDE7B_HUMAN Link Image

Enzyme 68 PDB ID

Not Available

Enzyme 68 Cellular Location

Not Available

Enzyme 68 Gene Sequence

>1353 bp

ATGTCTTGTTTAATGGTTGAGAGGTGTGGCGAAATCTTGTTTGAGAACCCCGATCAGAAT
GCCAAATGTGTTTGCATGCTGGGAGATATACGACTAAGGGGTCAGACGGGGGTTCGTGCT
GAACGCCGTGGCTCCTACCCATTCATTGACTTCCGCCTACTTAACAGTACAACATACTCA
GGGGAGATTGGCACCAAGAAAAAGGTGAAAAGACTATTAAGCTTTCAAAGATACTTCCAT
GCATCAAGGCTGCTTCGTGGAATTATACCACAAGCCCCTCTGCACCTGCTGGATGAAGAC
TACCTTGGACAAGCAAGGCATATGCTCTCCAAAGTGGGAATGTGGGATTTTGACATTTTC
TTGTTTGATCGCTTGACAAATGGAAACAGCCTGGTAACACTGTTGTGCCACCTCTTCAAT
ACCCATGGACTCATTCACCATTTCAAGTTAGATATGGTGACCTTACACCGATTTTTAGTC
ATGGTTCAAGAAGATTACCACAGCCAAAACCCGTATCACAATGCTGTTCACGCAGCCGAC
GTCACCCAGGCCATGCACTGCTACCTGAAAGAGCCAAAGCTTGCCAGCTTCCTCACGCCT
CTGGACATCATGCTTGGACTGCTGGCTGCAGCAGCACACGATGTGGACCACCCAGGGGTG
AACCAGCCATTTTTGATAAAAACTAACCACCATCTTGCAAACCTATATCAGAATATGTCT
GTGCTGGAGAATCATCACTGGCGATCTACAATTGGCATGCTTCGAGAATCAAGGCTTCTT
GCTCATTTGCCAAAGGAAATGACACAGGATATTGAACAGCAGCTGGGCTCCTTGATCTTG
GCAACAGACATCAACAGGCAGAATGAATTTTTGACCAGATTGAAAGCTCACCTCCACAAT
AAAGACTTAAGACTGGAGGATGCACAGGACAGGCACTTTATGCTTCAGATCGCCTTGAAG
TGTGCTGACATTTGCAATCCTTGTAGAATCTGGGAGATGAGCAAGCAGTGGAGTGAAAGG
GTCTGTGAAGAATTCTACAGGCAAGGTGAACTTGAACAGAAATTTGAACTGGAAATCAGT
CCTCTTTGTAATCAACAGAAAGATTCCATCCCTAGTATACAAATTGGTTTCATGAGCTAC
ATCGTGGAGCCGCTCTTCCGGGAATGGGCCCATTTCACGGGTAACAGCACCCTGTCGGAG
AACATGCTGGGCCACCTCGCACACAACAAGGCCCAGTGGAAGAGCCTGTTGCCCAGGCAG
CACAGAAGCAGGGGCAGCAGTGGCAGCGGGCCTGACCACGACCACGCAGGCCAAGGGACT
GAGAGCGAGGAGCAGGAAGGCGACAGCCCCTAG

Enzyme 68 GenBank Gene ID

AB038040

Enzyme 68 GeneCard ID

PDE7B

Enzyme 68 GenAtlas ID

PDE7B

Enzyme 68 HGNC ID

HGNC:8792

Enzyme 68 Chromosome Location

Enzyme 68 Locus

6q23-q24

Enzyme 68 SNPs

SNPJam Report Link Image

Enzyme 68 General References

Sasaki T, Kotera J, Yuasa K, Omori K: Identification of human PDE7B, a cAMP-specific phosphodiesterase. Biochem Biophys Res Commun. 2000 May 19;271(3):575-83. [PubMed ]
Gardner C, Robas N, Cawkill D, Fidock M: Cloning and characterization of the human and mouse PDE7B, a novel cAMP-specific cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 2000 May 27;272(1):186-92. [PubMed ]
Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]

Enzyme 68 Metabolite References

Not Available

Enzyme 69 [top]

Enzyme 69 ID

5885

Enzyme 69 Name

Lysyl-tRNA synthetase

Enzyme 69 Synonyms

Lysine--tRNA ligase
LysRS

Enzyme 69 Gene Name

KARS

Enzyme 69 Protein Sequence

>Lysyl-tRNA synthetase

MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTT
DNGVGPEEESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDH
LTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGD
IIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFV
RQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAP
ELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSG
MVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETR
KILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKE
GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYG
LPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV

Enzyme 69 Number of Residues

597

Enzyme 69 Molecular Weight

68047.5

Enzyme 69 Theoretical pI

6.31

Enzyme 69 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds lysine-tRNA ligase activity nucleic acid binding nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process lysyl-tRNA aminoacylation macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 69 General Function

Involved in nucleotide binding

Enzyme 69 Specific Function

Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction:the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of diadenosine oligophosphate (Ap4A), a signaling molecule involved in the activation of MITF transcriptional activity. Interacts with HIV-1 virus GAG protein, facilitating the selective packaging of tRNA(3)(Lys), the primer for reverse transcription initiation

Enzyme 69 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Lysine Biosynthesis (map00300 )

Enzyme 69 Reactions

ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys [RN:R03658]

Enzyme 69 Pfam Domain Function

tRNA-synt_2 (PF00152 )
tRNA_anti (PF01336 )

Enzyme 69 Signals

None

Enzyme 69 Transmembrane Regions

None

Enzyme 69 Essentiality

Not Available

Enzyme 69 GenBank ID Protein

5031815

Enzyme 69 UniProtKB/Swiss-Prot ID

Q15046

Enzyme 69 UniProtKB/Swiss-Prot Entry Name

SYK_HUMAN

Enzyme 69 PDB ID

Not Available

Enzyme 69 Cellular Location

Not Available

Enzyme 69 Gene Sequence

>1794 bp

ATGGCGGCCGTGCAGGCGGCCGAGGTGAAAGTGGATGGCAGCGAGCCGAAACTGAGCAAG
AATGAGCTGAAGAGACGCCTGAAAGCTGAGAAGAAAGTAGCAGAGAAGGAGGCCAAACAG
AAAGAGCTCAGTGAGAAACAGCTAAGCCAAGCCACTGCTGCTGCCACCAACCACACCACT
GATAATGGTGTGGGTCCTGAGGAAGAGAGCGTGGACCCAAATCAATACTACAAAATCCGC
AGTCAAGCAATTCATCAGCTGAAGGTCAATGGGGAAGACCCATACCCACACAAGTTCCAT
GTAGACATCTCACTCACTGACTTCATCCAAAAATATAGTCACCTGCAGCCTGGGGATCAC
CTGACTGACATCACCTTAAAGGTGGCAGGTAGGATCCATGCCAAAAGAGCTTCTGGGGGA
AAGCTCATCTTCTATGATCTTCGAGGAGAGGGGGTGAAGTTGCAAGTCATGGCCAATTCC
AGAAATTATAAATCAGAAGAAGAATTTATTCATATTAATAACAAACTGCGTCGGGGAGAC
ATAATTGGAGTTCAGGGGAATCCTGGTAAAACCAAGAAGGGTGAGCTGAGCATCATTCCG
TATGAGATCACACTGCTGTCTCCCTGTTTGCATATGTTACCTCATCTTCACTTTGGCCTC
AAAGACAAGGAAACAAGGTATCGCCAGAGATACTTGGACTTGATCCTGAATGACTTTGTG
AGGCAGAAATTTATCATCCGCTCTAAGATCATCACATATATAAGAAGTTTCTTAGATGAG
CTGGGATTCCTAGAGATTGAAACTCCCATGATGAACATCATCCCAGGGGGAGCCGTGGCC
AAGCCTTTCATCACTTATCACAACGAGCTGGACATGAACTTATATATGAGAATTGCTCCA
GAACTCTATCATAAGATGCTTGTGGTTGGTGGCATCGACCGGGTTTATGAAATTGGACGC
CAGTTCCGGAATGAGGGGATTGATTTGACGCACAATCCTGAGTTCACCACCTGTGAGTTC
TACATGGCCTATGCAGACTATCACGATCTCATGGAAATCACGGAGAAGATGGTTTCAGGG
ATGGTGAAGCATATTACAGGCAGTTACAAGGTCACCTACCACCCAGATGGCCCAGAGGGC
CAAGCCTACGATGTTGACTTCACCCCACCCTTCCGGCGAATCAACATGGTAGAAGAGCTT
GAGAAAGCCCTGGGGATGAAGCTGCCAGAAACGAACCTCTTTGAAACTGAAGAAACTCGC
AAAATTCTTGATGATATCTGTGTGGCAAAAGCTGTTGAATGCCCTCCACCTCGGACCACA
GCCAGGCTCCTTGACAAGCTTGTTGGGGAGTTCCTGGAAGTGACTTGCATCAATCCTACA
TTCATCTGTGATCACCCACAGATAATGAGCCCTTTGGCTAAATGGCACCGCTCTAAAGAG
GGTCTGACTGAGCGCTTTGAGCTGTTTGTCATGAAGAAAGAGATATGCAATGCGTATACT
GAGCTGAATGATCCCATGCGGCAGCGGCAGCTTTTTGAAGAACAGGCCAAGGCCAAGGCT
GCAGGTGATGATGAGGCCATGTTCATAGATGAAAACTTCTGTACTGCCCTGGAATATGGG
CTGCCCCCCACAGCTGGCTGGGGCATGGGCATTGATCGAGTCGCCATGTTTCTCACGGAC
TCCAACAACATCAAGGAAGTACTTCTGTTTCCTGCCATGAAACCCGAAGACAAGAAGGAG
AATGTAGCAACCACTGATACACTGGAAAGCACAACAGTTGGCACTTCTGTCTAG

Enzyme 69 GenBank Gene ID

NM_005548.2 Link Image

Enzyme 69 GeneCard ID

KARS

Enzyme 69 GenAtlas ID

KARS

Enzyme 69 HGNC ID

HGNC:6215

Enzyme 69 Chromosome Location

Enzyme 69 Locus

16q23.1

Enzyme 69 SNPs

SNPJam Report Link Image

Enzyme 69 General References

Shiba K, Stello T, Motegi H, Noda T, Musier-Forsyth K, Schimmel P: Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant. J Biol Chem. 1997 Sep 5;272(36):22809-16. [PubMed ]
Tolkunova E, Park H, Xia J, King MP, Davidson E: The human lysyl-tRNA synthetase gene encodes both the cytoplasmic and mitochondrial enzymes by means of an unusual alternative splicing of the primary transcript. J Biol Chem. 2000 Nov 10;275(45):35063-9. [PubMed ]
Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1994;1(5):223-9. [PubMed ]
Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Zamecnik PC, Stephenson ML, Janeway CM, Randerath K: Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase. Biochem Biophys Res Commun. 1966 Jul 6;24(1):91-7. [PubMed ]
Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M: Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. J Mol Biol. 1999 Jan 8;285(1):183-95. [PubMed ]
Tan M, Wei C, Price CM: The telomeric protein Rap1 is conserved in vertebrates and is expressed from a bidirectional promoter positioned between the Rap1 and KARS genes. Gene. 2003 Dec 24;323:1-10. [PubMed ]
Lee YN, Nechushtan H, Figov N, Razin E: The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells. Immunity. 2004 Feb;20(2):145-51. [PubMed ]
Javanbakht H, Halwani R, Cen S, Saadatmand J, Musier-Forsyth K, Gottlinger H, Kleiman L: The interaction between HIV-1 Gag and human lysyl-tRNA synthetase during viral assembly. J Biol Chem. 2003 Jul 25;278(30):27644-51. Epub 2003 May 19. [PubMed ]
Halwani R, Cen S, Javanbakht H, Saadatmand J, Kim S, Shiba K, Kleiman L: Cellular distribution of Lysyl-tRNA synthetase and its interaction with Gag during human immunodeficiency virus type 1 assembly. J Virol. 2004 Jul;78(14):7553-64. [PubMed ]
Park SG, Kim HJ, Min YH, Choi EC, Shin YK, Park BJ, Lee SW, Kim S: Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response. Proc Natl Acad Sci U S A. 2005 May 3;102(18):6356-61. Epub 2005 Apr 25. [PubMed ]
Guzzo CM, Yang DC: Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro. Biochem Biophys Res Commun. 2008 Jan 25;365(4):718-23. Epub 2007 Nov 20. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Guo M, Ignatov M, Musier-Forsyth K, Schimmel P, Yang XL: Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formation. Proc Natl Acad Sci U S A. 2008 Feb 19;105(7):2331-6. Epub 2008 Feb 13. [PubMed ]

Enzyme 69 Metabolite References

Not Available

Enzyme 70 [top]

Enzyme 70 ID

5886

Enzyme 70 Name

Isoleucyl-tRNA synthetase, cytoplasmic

Enzyme 70 Synonyms

Isoleucine--tRNA ligase
IRS
IleRS

Enzyme 70 Gene Name

IARS

Enzyme 70 Protein Sequence

>Isoleucyl-tRNA synthetase, cytoplasmic

MLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHYGHIL
AGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEYNNQC
RAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMP
FSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAVCVNP
EMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYFLKCK
ENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASGCFTT
EVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWFVRVE
NMVDQLLRNNDLCYWVPELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFEEVVC
IGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYAQVHY
PFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLASDGQK
MSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAY
RFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRLYTVV
PRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELM
YQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKT
IPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMV
LGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATGGTAQ
FEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAKSEGT
YLNSVIESHTEFIFTTIKAPLKPYPVSPSDKVLIQEKTQLKGSELEITLTRGSSLPGPAC
AYVNLNICANGSEQGGVLLLENPKGDNRLDLLKLKSVVTSIFGVKNTELAVFHDETEIQN
QTDLLSLSGKTLCVTAGSAPSLINSSSTLLCQYINLQLLNAKPQECLMGTVGTLLLENPL
GQNGLTHQGLLYEAAKVFGLRSRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVLPTTA
DF

Enzyme 70 Number of Residues

1262

Enzyme 70 Molecular Weight

144496.9

Enzyme 70 Theoretical pI

6.03

Enzyme 70 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity isoleucine-tRNA ligase activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process isoleucyl-tRNA aminoacylation macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 70 General Function

Involved in nucleotide binding

Enzyme 70 Specific Function

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)

Enzyme 70 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )

Enzyme 70 Reactions

ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle [RN:R03656]

Enzyme 70 Pfam Domain Function

Anticodon_1 (PF08264 )
tRNA-synt_1 (PF00133 )

Enzyme 70 Signals

None

Enzyme 70 Transmembrane Regions

None

Enzyme 70 Essentiality

Not Available

Enzyme 70 GenBank ID Protein

158259489

Enzyme 70 UniProtKB/Swiss-Prot ID

P41252

Enzyme 70 UniProtKB/Swiss-Prot Entry Name

SYIC_HUMAN Link Image

Enzyme 70 PDB ID

Not Available

Enzyme 70 Cellular Location

Not Available

Enzyme 70 Gene Sequence

>3789 bp

ATGCTTCAACAAGTTCCAGAAAACATAAATTTTCCTGCTGAAGAAGAGAAAATCTTGGAG
TTTTGGACTGAATTTAATTGTTTTCAGGAATGCTTAAAGCAATCAAAACATAAACCAAAA
TTTACCTTCTATGATGGTCCTCCTTTTGCAACTGGACTGCCTCACTATGGACATATACTT
GCGGGTACAATTAAAGATATAGTTACAAGATATGCTCACCAGAGTGGGTTTCATGTTGAC
AGAAGATTTGGATGGGATTGCCATGGCTTACCTGTGGAATATGAAATTGATAAGACACTG
GGAATCAGAGGACCAGAGGATGTGGCCAAAATGGGGATTACAGAGTATAACAATCAGTGC
CGAGCAATTGTGATGAGATATTCTGCTGAGTGGAAGTCTACTGTTAGCAGACTTGGCCGA
TGGATTGACTTTGACAATGACTATAAAACTCTGTATCCACAATTCATGGAATCAGTCTGG
TGGGTCTTCAAACAACTCTATGATAAAGGCCTTGTTTATAGAGGTGTGAAAGTCATGCCC
TTCTCTACGGCATGTAACACTCCACTTTCCAACTTCGAGTCACACCAGAATTATAAGGAT
GTTCAAGATCCTTCAGTATTTGTAACTTTCCCTTTGGAAGAAGATGAAACTGTATCTTTA
GTTGCTTGGACAACCACTCCCTGGACTCTACCTAGTAACCTTGCTGTGTGTGTTAATCCA
GAAATGCAATATGTGAAAATTAAAGATGTTGCCAGAGGACGATTACTCATTTTAATGGAA
GCCAGATTGTCAGCCCTCTATAAATTGGAGAGTGACTATGAGATCCTTGAAAGATTTCCT
GGTGCCTATCTTAAAGGCAAGAAGTACAGGCCCCTGTTTGACTATTTCCTGAAGTGTAAA
GAGAATGGCGCTTTCACTGTGCTTGTTGACAACTATGTGAAGGAAGAAGAAGGCACAGGG
GTTGTCCACCAAGCTCCTTACTTCGGTGCTGAGGACTATCGGGTCTGTATGGACTTTAAC
ATTATTCGGAAAGACTCACTCCCTGTTTGCCCTGTGGATGCTTCAGGCTGCTTCACAACG
GAGGTGACAGATTTCGCAGGACAGTATGTGAAGGATGCTGACAAAAGTATCATCAGGACT
TTGAAGGAACAAGGCCGACTTCTGGTTGCCACCACCTTCACTCACAGCTACCCTTTTTGC
TGGAGATCAGACACTCCTCTAATTTACAAAGCAGTGCCCAGCTGGTTTGTGCGAGTGGAG
AACATGGTGGACCAGCTCCTAAGGAACAATGACCTGTGCTACTGGGTCCCAGAGTTGGTA
CGAGAAAAACGATTTGGAAATTGGCTGAAAGATGCACGTGACTGGACAATTTCCAGAAAC
AGATACTGGGGCACCCCCATCCCACTGTGGGTCAGCGATGACTTTGAGGAGGTGGTATGC
ATTGGGTCAGTGGCGGAACTTGAAGAACTGTCAGGAGCAAAGATCTCAGATCTCCACAGA
GAGAGTGTTGACCACCTGACCATTCCTTCACGCTGTGGGAAGGGATCCTTGCACCGCATC
TCTGAAGTGTTTGACTGTTGGTTTGAGAGTGGCAGCATGCCCTATGCTCAGGTTCATTAC
CCGTTTGAAAACAAGAGGGAGTTTGAGGATGCTTTTCCTGCAGATTTCATTGCCGAGGGC
ATCGACCAAACCAGAGGATGGTTTTATACCCTGCTGGTGCTGGCCACGGCCCTCTTTGGA
CAACCGCCTTTCAAGAACGTAATTGTGAATGGGCTTGTCCTGGCAAGTGATGGCCAAAAA
ATGAGCAAACGGAAAAAGAATTATCCAGATCCAGTTTCCATCATCCAGAAGTATGGTGCT
GATGCCCTCAGATTATATCTGATTAACTCCCCTGTGGTGAGAGCAGAAAACCTCCGCTTT
AAAGAAGAGGGTGTGCGGGACGTCCTTAAGGATGTACTGCTCCCATGGTACAATGCCTAT
CGCTTCTTAATCCAGAACGTTCTGAGGCTCCAGAAGGAGGAAGAAATAGAATTTCTCTAC
AATGAGAACACGGTTAGAGAAAGCCCCAACATTACAGACCGGTGGATCCTGTCCTTCATG
CAGTCTCTCATTGGCTTCTTTGAGACTGAAATGGCAGCTTATAGGCTTTATACTGTGGTG
CCTCGCCTGGTCAAGTTTGTAGATATTCTGACCAATTGGTATGTTAGAATGAACCGCAGA
AGATTAAAGGGTGAAAATGGGATGGAGGATTGTGTCATGGCCCTAGAAACCTTGTTTAGT
GTTCTGCTTTCTCTTTGCAGACTTATGGCTCCCTACACACCTTTTCTCACTGAATTGATG
TACCAGAATCTAAAGGTGCTGATTGACCCTGTTTCTGTTCAGGACAAGGACACACTCAGC
ATTCACTACCTCATGCTGCCCCGTGTTCGAGAAGAATTGATTGACAAGAAAACAGAGAGT
GCAGTATCTCAGATGCAGTCTGTGATTGAACTTGGAAGAGTGATCAGAGACCGAAAAACT
ATTCCCATAAAGTATCCTTTGAAAGAAATTGTGGTTATCCATCAAGATCCAGAAGCTCTT
AAAGATATCAAGTCTTTGGAGAAGTATATCATTGAGGAACTCAATGTTCGAAAAGTTACA
CTGTCTACAGATAAAAACAAGTATGGCATTCGGCTAAGGGCAGAACCAGATCACATGGTC
CTGGGGAAGCGTCTGAAGGGAGCCTTTAAGGCAGTGATGACGTCCATCAAGCAGTTGAGC
AGTGAGGAGCTGGAGCAGTTCCAGAAGACTGGGACCATTGTTGTGGAAGGCCATGAATTG
CACGATGAAGACATCCGCCTCATGTACACCTTTGATCAGGCCACAGGTGGGACTGCGCAA
TTTGAAGCACACTCAGATGCTCAGGCTTTGGTCCTCTTAGATGTCACTCCTGACCAGTCA
ATGGTAGATGAAGGAATGGCTCGGGAAGTCATCAATCGCATACAGAAACTTCGCAAAAAG
TGCAATCTGGTTCCAACTGATGAAATCACAGTGTACTATAAAGCAAAGTCTGAAGGAACA
TATCTGAATAGTGTTATTGAAAGCCACACAGAGTTCATATTTACCACCATAAAGGCTCCC
TTGAAACCATATCCAGTTTCTCCATCGGATAAAGTCCTTATTCAAGAAAAAACACAGTTG
AAGGGATCTGAACTGGAAATTACACTCACCAGAGGATCTTCCCTTCCTGGTCCTGCTTGT
GCATATGTCAATCTTAACATTTGTGCAAATGGCAGTGAACAAGGTGGAGTATTGCTCCTG
GAAAATCCAAAAGGTGACAATAGGTTGGACCTTTTAAAGCTGAAGAGTGTTGTCACTAGC
ATTTTTGGTGTGAAAAATACAGAGCTGGCTGTCTTCCATGATGAAACAGAAATACAAAAC
CAAACTGACTTACTGAGTCTTAGTGGAAAAACACTTTGTGTGACTGCAGGATCGGCTCCC
TCTCTGATCAACAGTTCTAGTACTCTTCTTTGTCAGTATATCAACCTACAGCTCCTGAAT
GCAAAGCCACAAGAGTGTTTAATGGGGACAGTGGGCACTCTCCTGCTTGAAAACCCACTT
GGGCAGAATGGGCTCACCCACCAAGGTCTTCTGTATGAAGCAGCCAAGGTGTTTGGCCTT
CGGAGCAGGAAGCTAAAGCTGTTTCTGAATGAGACCCAAACGCAGGAAATTACAGAAGAC
ATCCCCGTGAAGACTTTGAATATGAAGACTGTGTATGTTTCTGTGTTACCAACAACAGCA
GACTTCTAG

Enzyme 70 GenBank Gene ID

AK293014

Enzyme 70 GeneCard ID

IARS

Enzyme 70 GenAtlas ID

IARS

Enzyme 70 HGNC ID

HGNC:5330

Enzyme 70 Chromosome Location

Enzyme 70 Locus

9q21

Enzyme 70 SNPs

SNPJam Report Link Image

Enzyme 70 General References

Shiba K, Suzuki N, Shigesada K, Namba Y, Schimmel P, Noda T: Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit. Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7435-9. [PubMed ]
Nichols RC, Raben N, Boerkoel CF, Plotz PH: Human isoleucyl-tRNA synthetase: sequence of the cDNA, alternative mRNA splicing, and the characteristics of an unusually long C-terminal extension. Gene. 1995 Apr 3;155(2):299-304. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed ]
Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 70 Metabolite References

Not Available

Enzyme 71 [top]

Enzyme 71 ID

5887

Enzyme 71 Name

Bis(5'-adenosyl)-triphosphatase

Enzyme 71 Synonyms

AP3A hydrolase
AP3Aase
Diadenosine 5',5'''-P1,P3-triphosphate hydrolase
Dinucleosidetriphosphatase
Fragile histidine triad protein

Enzyme 71 Gene Name

FHIT

Enzyme 71 Protein Sequence

>Bis(5'-adenosyl)-triphosphatase

MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQ
TTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSIYEELQKH
DKEDFPASWRSEEEMAAEAAALRVYFQ

Enzyme 71 Number of Residues

147

Enzyme 71 Molecular Weight

16858.1

Enzyme 71 Theoretical pI

7.09

Enzyme 71 GO Classification

Function
catalytic activity
Process
—
Component
—

Enzyme 71 General Function

Involved in catalytic activity

Enzyme 71 Specific Function

Cleaves A-5'-PPP-5'A to yield AMP and ADP. Possible tumor suppressor for specific tissues

Enzyme 71 Pathways

Purine Metabolism (map00230 )

Enzyme 71 Reactions

P1,P3-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP [RN:R00187]

Enzyme 71 Pfam Domain Function

HIT (PF01230 )

Enzyme 71 Signals

None

Enzyme 71 Transmembrane Regions

None

Enzyme 71 Essentiality

Not Available

Enzyme 71 GenBank ID Protein

261278358

Enzyme 71 UniProtKB/Swiss-Prot ID

P49789

Enzyme 71 UniProtKB/Swiss-Prot Entry Name

FHIT_HUMAN Link Image

Enzyme 71 PDB ID

1FHI

Enzyme 71 PDB File

Show

Enzyme 71 3D Structure

Enzyme 71 Cellular Location

Not Available

Enzyme 71 Gene Sequence

>444 bp

ATGTCGTTCAGATTTGGCCAACATCTCATCAAGCCCTCTGTAGTGTTTCTCAAAACAGAA
CTGTCCTTCGCTCTTGTGAATAGGAAACCTGTGGTACCAGGACATGTCCTTGTGTGCCCG
CTGCGGCCAGTGGAGCGCTTCCATGACCTGCGTCCTGATGAAGTGGCCGATTTGTTTCAG
ACGACCCAGAGAGTCGGGACAGTGGTGGAAAAACATTTCCATGGGACCTCTCTCACCTTT
TCCATGCAGGATGGCCCCGAAGCCGGACAGACTGTGAAGCACGTTCACGTCCATGTTCTT
CCCAGGAAGGCTGGAGACTTTCACAGGAATGACAGCATCTATGAGGAGCTCCAGAAACAT
GACAAGGAGGACTTTCCTGCCTCTTGGAGATCAGAGGAGGAAATGGCAGCAGAAGCCGCA
GCTCTGCGGGTCTACTTTCAGTGA

Enzyme 71 GenBank Gene ID

NM_001166243.1 Link Image

Enzyme 71 GeneCard ID

FHIT

Enzyme 71 GenAtlas ID

FHIT

Enzyme 71 HGNC ID

HGNC:3701

Enzyme 71 Chromosome Location

Enzyme 71 Locus

3p14.2

Enzyme 71 SNPs

SNPJam Report Link Image

Enzyme 71 General References

Ohta M, Inoue H, Cotticelli MG, Kastury K, Baffa R, Palazzo J, Siprashvili Z, Mori M, McCue P, Druck T, Croce CM, Huebner K: The FHIT gene, spanning the chromosome 3p14.2 fragile site and renal carcinoma-associated t(3;8) breakpoint, is abnormal in digestive tract cancers. Cell. 1996 Feb 23;84(4):587-97. [PubMed ]
Druck T, Hadaczek P, Fu TB, Ohta M, Siprashvili Z, Baffa R, Negrini M, Kastury K, Veronese ML, Rosen D, Rothstein J, McCue P, Cotticelli MG, Inoue H, Croce CM, Huebner K: Structure and expression of the human FHIT gene in normal and tumor cells. Cancer Res. 1997 Feb 1;57(3):504-12. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Barnes LD, Garrison PN, Siprashvili Z, Guranowski A, Robinson AK, Ingram SW, Croce CM, Ohta M, Huebner K: Fhit, a putative tumor suppressor in humans, is a dinucleoside 5',5"'-P1,P3-triphosphate hydrolase. Biochemistry. 1996 Sep 10;35(36):11529-35. [PubMed ]
Huang K, Arabshahi A, Wei Y, Frey PA: The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit. Biochemistry. 2004 Jun 15;43(23):7637-42. [PubMed ]
Pekarsky Y, Garrison PN, Palamarchuk A, Zanesi N, Aqeilan RI, Huebner K, Barnes LD, Croce CM: Fhit is a physiological target of the protein kinase Src. Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3775-9. Epub 2004 Mar 8. [PubMed ]
Lima CD, D'Amico KL, Naday I, Rosenbaum G, Westbrook EM, Hendrickson WA: MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family. Structure. 1997 Jun 15;5(6):763-74. [PubMed ]
Lima CD, Klein MG, Hendrickson WA: Structure-based analysis of catalysis and substrate definition in the HIT protein family. Science. 1997 Oct 10;278(5336):286-90. [PubMed ]
Pace HC, Garrison PN, Robinson AK, Barnes LD, Draganescu A, Rosler A, Blackburn GM, Siprashvili Z, Croce CM, Huebner K, Brenner C: Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit. Proc Natl Acad Sci U S A. 1998 May 12;95(10):5484-9. [PubMed ]

Enzyme 71 Metabolite References

Not Available

Enzyme 72 [top]

Enzyme 72 ID

5888

Enzyme 72 Name

High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A

Enzyme 72 Synonyms

Not Available

Enzyme 72 Gene Name

PDE9A

Enzyme 72 Protein Sequence

>High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A

MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAM
VSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRRE
GAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANH
LAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDV
PTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLF
CVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYN
NTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLI
LATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCL
LEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIML
QPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA

Enzyme 72 Number of Residues

593

Enzyme 72 Molecular Weight

68491.9

Enzyme 72 Theoretical pI

6.10

Enzyme 72 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 72 General Function

Involved in catalytic activity

Enzyme 72 Specific Function

Hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes

Enzyme 72 Pathways

Not Available

Enzyme 72 Reactions

guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]

Enzyme 72 Pfam Domain Function

PDEase_I (PF00233 )

Enzyme 72 Signals

None

Enzyme 72 Transmembrane Regions

None

Enzyme 72 Essentiality

Not Available

Enzyme 72 GenBank ID Protein

Not Available

Enzyme 72 UniProtKB/Swiss-Prot ID

O76083

Enzyme 72 UniProtKB/Swiss-Prot Entry Name

PDE9A_HUMAN Link Image

Enzyme 72 PDB ID

1TBM

Enzyme 72 PDB File

Show

Enzyme 72 3D Structure

Enzyme 72 Cellular Location

Not Available

Enzyme 72 Gene Sequence

>1782 bp

ATGGGATCCGGCTCCTCCAGCTACCGGCCCAAGGCCATCTACCTGGACATCGATGGACGC
ATTCAGAAGGTAATCTTCAGCAAGTACTGCAACTCCAGCGACATCATGGACCTGTTCTGC
ATCGCCACCGGCCTGCCTCGGAACACGACCATCTCCCTGCTGACCACCGACGACGCCATG
GTCTCCATCGACCCCACCATGCCCGCGAATTCAGAACGCACTCCGTACAAAGTGAGACCT
GTGGCCATCAAGCAACTCTCCGCTGGTGTCGAGGACAAGAGAACCACAAGCCGTGGCCAG
TCTGCTGAGAGACCACTGAGGGACAGACGGGTTGTGGGCCTGGAGCAGCCCCGGAGGGAA
GGAGCATTTGAAAGTGGACAGGTAGAGCCCAGGCCCAGAGAGCCCCAGGGCTGCTACCAG
GAAGGCCAGCGCATCCCTCCAGAGAGAGAAGAATTAATCCAGAGCGTGCTGGCGCAGGTT
GCAGAGCAGTTCTCAAGAGCATTCAAAATCAATGAACTGAAAGCTGAAGTTGCAAATCAC
TTGGCTGTCCTAGAGAAACGCGTGGAATTGGAAGGACTAAAAGTGGTGGAGATTGAGAAA
TGCAAGAGTGACATTAAGAAGATGAGGGAGGAGCTGGCGGCCAGAAGCAGCAGGACCAAC
TGCCCCTGTAAGTACAGTTTTTTGGATAACCACAAGAAGTTGACTCCTCGACGCGATGTT
CCCACTTACCCCAAGTACCTGCTCTCTCCAGAGACCATCGAGGCCCTGCGGAAGCCGACC
TTTGACGTCTGGCTTTGGGAGCCCAATGAGATGCTGAGCTGCCTGGAGCACATGTACCAC
GACCTCGGGCTGGTCAGGGACTTCAGCATCAACCCTGTCACCCTCAGGAGGTGGCTGTTC
TGTGTCCACGACAACTACAGAAACAACCCCTTCCACAACTTCCGGCACTGCTTCTGCGTG
GCCCAGATGATGTACAGCATGGTCTGGCTCTGCAGTCTCCAGGAGAAGTTCTCACAAACG
GATATCCTGATCCTAATGACAGCGGCCATCTGCCACGATCTGGACCATCCCGGCTACAAC
AACACGTACCAGATCAATGCCCGCACAGAGCTGGCGGTCCGCTACAATGACATCTCACCG
CTGGAGAACCACCACTGCGCCGTGGCCTTCCAGATCCTCGCCGAGCCTGAGTGCAACATC
TTCTCCAACATCCCACCTGATGGGTTCAAGCAGATCCGACAGGGAATGATCACATTAATC
TTGGCCACTGACATGGCAAGACATGCAGAAATTATGGATTCTTTCAAAGAGAAAATGGAG
AATTTTGACTACAGCAACGAGGAGCACATGACCCTGCTGAAGATGATTTTGATAAAATGC
TGTGATATCTCTAACGAGGTCCGTCCAATGGAAGTCGCAGAGCCTTGGGTGGACTGTTTA
TTAGAGGAATATTTTATGCAGAGCGACCGTGAGAAGTCAGAAGGCCTTCCTGTGGCACCG
TTCATGGACCGAGACAAAGTGACCAAGGCCACAGCCCAGATTGGGTTCATCAAGTTTGTC
CTGATCCCAATGTTTGAAACAGTGACCAAGCTCTTCCCCATGGTTGAGGAGATCATGCTG
CAGCCACTTTGGGAATCCCGAGATCGCTACGAGGAGCTGAAGCGGATAGATGACGCCATG
AAAGAGTTACAGAAGAAGACTGACAGCTTGACGTCTGGGGCCACCGAGAAGTCCAGAGAG
AGAAGCAGAGATGTGAAAAACAGTGAAGGAGACTGTGCCTGA

Enzyme 72 GenBank Gene ID

AF048837

Enzyme 72 GeneCard ID

PDE9A

Enzyme 72 GenAtlas ID

PDE9A

Enzyme 72 HGNC ID

HGNC:8795

Enzyme 72 Chromosome Location

Enzyme 72 Locus

21q22.3

Enzyme 72 SNPs

SNPJam Report Link Image

Enzyme 72 General References

Fisher DA, Smith JF, Pillar JS, St Denis SH, Cheng JB: Isolation and characterization of PDE9A, a novel human cGMP-specific phosphodiesterase. J Biol Chem. 1998 Jun 19;273(25):15559-64. [PubMed ]
Guipponi M, Scott HS, Kudoh J, Kawasaki K, Shibuya K, Shintani A, Asakawa S, Chen H, Lalioti MD, Rossier C, Minoshima S, Shimizu N, Antonarakis SE: Identification and characterization of a novel cyclic nucleotide phosphodiesterase gene (PDE9A) that maps to 21q22.3: alternative splicing of mRNA transcripts, genomic structure and sequence. Hum Genet. 1998 Oct;103(4):386-92. [PubMed ]
Rentero C, Monfort A, Puigdomenech P: Identification and distribution of different mRNA variants produced by differential splicing in the human phosphodiesterase 9A gene. Biochem Biophys Res Commun. 2003 Feb 14;301(3):686-92. [PubMed ]
Wang P, Wu P, Egan RW, Billah MM: Identification and characterization of a new human type 9 cGMP-specific phosphodiesterase splice variant (PDE9A5). Differential tissue distribution and subcellular localization of PDE9A variants. Gene. 2003 Sep 18;314:15-27. [PubMed ]
Rentero C, Puigdomenech P: Specific use of start codons and cellular localization of splice variants of human phosphodiesterase 9A gene. BMC Mol Biol. 2006 Nov 8;7:39. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed ]
Huai Q, Wang H, Zhang W, Colman RW, Robinson H, Ke H: Crystal structure of phosphodiesterase 9 shows orientation variation of inhibitor 3-isobutyl-1-methylxanthine binding. Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9624-9. Epub 2004 Jun 21. [PubMed ]
Liu S, Mansour MN, Dillman KS, Perez JR, Danley DE, Aeed PA, Simons SP, Lemotte PK, Menniti FS: Structural basis for the catalytic mechanism of human phosphodiesterase 9. Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13309-14. Epub 2008 Aug 29. [PubMed ]

Enzyme 72 Metabolite References

Not Available

Enzyme 73 [top]

Enzyme 73 ID

5889

Enzyme 73 Name

cGMP-dependent 3',5'-cyclic phosphodiesterase

Enzyme 73 Synonyms

Cyclic GMP-stimulated phosphodiesterase
CGS-PDE
cGSPDE

Enzyme 73 Gene Name

PDE2A

Enzyme 73 Protein Sequence

>cGMP-dependent 3',5'-cyclic phosphodiesterase

MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQDALLSLGSVIDI
SGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCN
GLGFSDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAV
EKHTLVALRRVQVLQQRGPREAPRAVQNPPEGTAEDQKGGAAYTDRDRKILQLCGELYDL
DASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTGCLGQVV
EDKKSIQLKDLTSEDVQQLQSMLGCELQAMLCVPVISRATDQVVALACAFNKLEGDLFTD
EDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITE
ARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPD
AYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAF
SIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNF
ASFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMH
AFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYS
SEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDL
QKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAM
GNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSH
KFTIRGLPSNNSLDFLDEEYEVPDLDGTRAPINGCCSLDAE

Enzyme 73 Number of Residues

941

Enzyme 73 Molecular Weight

105715.8

Enzyme 73 Theoretical pI

5.08

Enzyme 73 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 73 General Function

Involved in catalytic activity

Enzyme 73 Specific Function

Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes

Enzyme 73 Pathways

Purine Metabolism (map00230 )

Enzyme 73 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 73 Pfam Domain Function

GAF (PF01590 )
PDEase_I (PF00233 )

Enzyme 73 Signals

None

Enzyme 73 Transmembrane Regions

None

Enzyme 73 Essentiality

Not Available

Enzyme 73 GenBank ID Protein

2108052

Enzyme 73 UniProtKB/Swiss-Prot ID

O00408

Enzyme 73 UniProtKB/Swiss-Prot Entry Name

PDE2A_HUMAN Link Image

Enzyme 73 PDB ID

1MC0

Enzyme 73 PDB File

Show

Enzyme 73 3D Structure

Enzyme 73 Cellular Location

Not Available

Enzyme 73 Gene Sequence

>2826 bp

ATGGGGCAGGCATGCGGCCACTCCATCCTCTGCAGGAGCCAGCAGTACCCGGCAGCGCGA
CCGGCTGAGCCGCGGGGCCAGCAGGTCTTCCTCAAGCCGGACGAGCCGCCGCCGCCGCCG
CAGCCATGCGCCGACAGCCTGCAGGACGCCTTGCTGAGTCTGGGCTCTGTCATCGACATT
TCAGGCCTGCAACGTGCTGTCAAGGAGGCCCTGTCAGCTGTGCTCCCCCGAGTGGAAACT
GTCTACACCTACCTACTGGATGGTGAGTCCCAGCTGGTGTGTGAGGACCCCCCACATGAG
CTGCCCCAGGAGGGGAAAGTCCGGGAGGCTATCATCTCCCAGAAGCGGCTGGGCTGCAAT
GGGCTGGGCTTCTCAGACCTGCCAGGGAAGCCCTTGGCCAGGCTGGTGGCTCCACTGGCT
CCTGATACCCAAGTGCTGGTCATGCCGCTAGCGGACAAGGAGGCTGGGGCCGTGGCAGCT
GTCATCTTGGTGCACTGTGGCCAGCTGAGTGATAATGAGGAATGGAGCCTGCAGGCGGTG
GAGAAGCATACCCTGGTCGCCCTGCGGAGGGTGCAGGTCCTGCAGCAGCGCGGGCCCAGG
GAGGCTCCCCGAGCCGTCCAGAACCCCCCGGAGGGGACGGCGGAAGACCAGAAGGGCGGG
GCGGCGTACACCGACCGCGACCGCAAGATCCTCCAACTGTGCGGGGAACTCTACGACCTG
GATGCCTCTTCCCTGCAGCTCAAAGTGCTCCAATACCTGCAGCAGGAGACCCGGGCATCC
CGCTGCTGCCTCCTGCTGGTGTCGGAGGACAATCTCCAGCTTTCTTGCAAGGTCATCGGA
GACAAAGTGCTCGGGGAAGAGGTCAGCTTTCCCTTGACAGGATGCCTGGGCCAGGTGGTG
GAAGACAAGAAGTCCATCCAGCTGAAGGACCTCACCTCCGAGGATGTACAACAGCTGCAG
AGCATGTTGGGCTGTGAGCTGCAGGCCATGCTCTGTGTCCCTGTCATCAGCCGGGCCACT
GACCAGGTGGTGGCCTTGGCCTGCGCCTTCAACAAGCTAGAAGGAGACTTGTTCACCGAC
GAGGACGAGCATGTGATCCAGCACTGCTTCCACTACACCAGCACCGTGCTCACCAGCACC
CTGGCCTTCCAGAAGGAACAGAAACTCAAGTGTGAGTGCCAGGCTCTTCTCCAAGTGGCA
AAGAACCTCTTCACCCACCTGGATGACGTCTCTGTCCTGCTCCAGGAGATCATCACGGAG
GCCAGAAACCTCAGCAACGCAGAGATCTGCTCTGTGTTCCTGCTGGATCAGAATGAGCTG
GTGGCCAAGGTGTTCGACGGGGGCGTGGTGGATGATGAGAGCTATGAGATCCGCATCCCG
GCCGATCAGGGCATCGCGGGACACGTGGCGACCACGGGCCAGATCCTGAACATCCCTGAC
GCATATGCCCATCCGCTTTTCTACCGCGGCGTGGACGACAGCACCGGCTTCCGCACGCGC
AACATCCTCTGCTTCCCCATCAAGAACGAGAACCAGGAGGTCATCGGTGTGGCCGAGCTG
GTGAACAAGATCAATGGGCCATGGTTCAGCAAGTTCGACGAGGACCTGGCGACGGCCTTC
TCCATCTACTGCGGCATCAGCATCGCCCATTCTCTCCTATACAAAAAAGTGAATGAGGCT
CAGTATCGCAGCCACCTGGCCAATGAGATGATGATGTACCACATGAAGGTCTCCGACGAT
GAGTATACCAAACTTCTCCATGATGGGATCCAGCCTGTGGCTGCCATTGACTCCAATTTT
GCAAGTTTCACCTATACCCCTCGTTCCCTGCCCGAGGATGACACGTCCATGGCCATCCTG
AGCATGCTGCAGGACATGAATTTCATCAACAACTACAAAATTGACTGCCCGACCCTGGCC
CGGTTCTGTTTGATGGTGAAGAAGGGCTACCGGGATCCCCCCTACCACAACTGGATGCAC
GCCTTTTCTGTCTCCCACTTCTGCTACCTGCTCTACAAGAACCTGGAGCTCACCAACTAC
CTCGAGGACATCGAGATCTTTGCCTTGTTTATTTCCTGCATGTGTCATGACCTGGACCAC
AGAGGCACAAACAACTCTTTCCAGGTGGCCTCGAAATCTGTGCTGGCTGCGCTCTACAGC
TCTGAGGGCTCCGTCATGGAGAGGCACCACTTTGCTCAGGCCATCGCCATCCTCAACACC
CACGGCTGCAACATCTTTGATCATTTCTCCCGGAAGGACTATCAGCGCATGCTGGATCTG
ATGCGGGACATCATCTTGGCCACAGACCTGGCCCACCATCTCCGCATCTTCAAGGACCTC
CAGAAGATGGCTGAGGTGGGCTACGACCGAAACAACAAGCAGCACCACAGACTTCTCCTC
TGCCTCCTCATGACCTCCTGTGACCTCTCTGACCAGACCAAGGGCTGGAAGACTACGAGA
AAGATCGCGGAGCTGATCTACAAAGAATTCTTCTCCCAGGGAGACCTGGAGAAGGCCATG
GGCAACAGGCCGATGGAGATGATGGACCGGGAGAAGGCCTATATCCCTGAGCTGCAAATC
AGCTTCATGGAGCACATTGCAATGCCCATCTACAAGCTGTTGCAGGACCTGTTCCCCAAA
GCGGCAGAGCTGTACGAGCGCGTGGCCTCCAACCGTGAGCACTGGACCAAGGTGTCCCAC
AAGTTCACCATCCGCGGCCTCCCAAGTAACAACTCGCTGGACTTCCTGGATGAGGAGTAC
GAGGTGCCTGATCTGGATGGCACTAGGGCCCCCATCAATGGCTGCTGCAGCCTTGATGCT
GAGTGA

Enzyme 73 GenBank Gene ID

U67733

Enzyme 73 GeneCard ID

PDE2A

Enzyme 73 GenAtlas ID

PDE2A

Enzyme 73 HGNC ID

HGNC:8777

Enzyme 73 Chromosome Location

Enzyme 73 Locus

11q13.4

Enzyme 73 SNPs

SNPJam Report Link Image

Enzyme 73 General References

Rosman GJ, Martins TJ, Sonnenburg WK, Beavo JA, Ferguson K, Loughney K: Isolation and characterization of human cDNAs encoding a cGMP-stimulated 3',5'-cyclic nucleotide phosphodiesterase. Gene. 1997 May 20;191(1):89-95. [PubMed ]
Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
Iffland A, Kohls D, Low S, Luan J, Zhang Y, Kothe M, Cao Q, Kamath AV, Ding YH, Ellenberger T: Structural determinants for inhibitor specificity and selectivity in PDE2A using the wheat germ in vitro translation system. Biochemistry. 2005 Jun 14;44(23):8312-25. [PubMed ]
Pandit J, Forman MD, Fennell KF, Dillman KS, Menniti FS: Mechanism for the allosteric regulation of phosphodiesterase 2A deduced from the X-ray structure of a near full-length construct. Proc Natl Acad Sci U S A. 2009 Oct 27;106(43):18225-30. Epub 2009 Oct 14. [PubMed ]

Enzyme 73 Metabolite References

Not Available

Enzyme 74 [top]

Enzyme 74 ID

5890

Enzyme 74 Name

Ubiquitin-like modifier-activating enzyme 1

Enzyme 74 Synonyms

Protein A1S9
Ubiquitin-activating enzyme E1

Enzyme 74 Gene Name

UBA1

Enzyme 74 Protein Sequence

>Ubiquitin-like modifier-activating enzyme 1

MSSSPLSKKRRVSGPDPKPGSNCSPAQSVLSEVPSVPTNGMAKNGSEADIDEGLYSRQLY
VLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLRE
EDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCH
NRGIKLVVADTRGLFGQLFCDFGEEMILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARH
GFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKK
ISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVA
LAQAVNARALPAVQQNNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPI
MQWLYFDALECLPEDKEVLTEDKCLQRQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIG
CELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMN
PHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGT
LGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPA
ENVNQYLTDPKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSN
NIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTG
SQDRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSRLEELKATLPSPDKLP
GFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAA
VVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYNQEWTLWDRFEV
QGLQPNGEEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVS
RVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRYTIR

Enzyme 74 Number of Residues

1058

Enzyme 74 Molecular Weight

117848.1

Enzyme 74 Theoretical pI

5.50

Enzyme 74 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity nucleoside binding purine nucleoside binding small protein activating enzyme activity
Process
macromolecule metabolic process macromolecule modification metabolic process protein modification process
Component
—

Enzyme 74 General Function

Involved in catalytic activity

Enzyme 74 Specific Function

Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin- E1 thioester and free AMP

Enzyme 74 Pathways

Not Available

Enzyme 74 Reactions

Not Available

Enzyme 74 Pfam Domain Function

ThiF (PF00899 )
UBA_e1_C (PF09358 )
UBA_e1_thiolCys (PF10585 )
UBACT (PF02134 )

Enzyme 74 Signals

None

Enzyme 74 Transmembrane Regions

None

Enzyme 74 Essentiality

Not Available

Enzyme 74 GenBank ID Protein

35830

Enzyme 74 UniProtKB/Swiss-Prot ID

P22314

Enzyme 74 UniProtKB/Swiss-Prot Entry Name

UBA1_HUMAN Link Image

Enzyme 74 PDB ID

1Z7L

Enzyme 74 PDB File

Show

Enzyme 74 3D Structure

Enzyme 74 Cellular Location

Not Available

Enzyme 74 Gene Sequence

>3177 bp

ATGTCCAGCTCGCCGCTGTCCAAGAAACGTCGCGTGTCCGGGCCTGATCCAAAGCCGGGT
TCTAACTGCTCCCCTGCCCAGTCCGTGTTGTCCGAAGTGCCCTCGGTGCCAACCAACGGA
ATGGCCAAGAACGGCAGTGAAGCAGACATAGACGAGGGCCTTTACTCCCGGCAGCTGTAT
GTGTTGGGCCATGAGGCAATGAAGCGGCTCCAGACATCCAGTGTCCTGGTATCAGGCCTG
CGGGGCCTGGGCGTGGAGATCGCTAAGAACATCATCCTTGGTGGGGTCAAGGCTGTTACC
CTACATGACCAGGGCACTGCCCAGTGGGCTGATCTTTCCTCCCAGTTCTACCTGCGGGAG
GAGGACATCGGTAAAAACCGGGCCGAGGTATCACAGCCCCGCCTCGCTGAGCTCAACAGC
TATGTGCCTGTCACTGCCTACACTGGACCCCTCGTTGAGGACTTCCTTAGTGGTTTCCAG
GTGGTGGTGCTCACCAACACCCCCCTGGAGGACCAGCTGCGAGTGGGTGAGTTCTGTCAC
AACCGTGGCATCAAGCTGGTGGTGGCAGGCACGCGGGGCCTGTTTGGGCAGCTCTTCTGT
GACTTTGGAGAGGAAATGATCCTCACAGATTCCAATGGGGAGCAGCCACTCAGTGCTATG
GTTTCTATGGTTACCAAGGACAACCCCGGTGTGGTTACCTGCCTGGATGAGGCCCGACAC
GGGTTTGAGAGCGGGGACTTTGTCTCCTTTTCAGAAGTACAGGGCATGGTTGAACTCAAC
GGAAATCAGCCCATGGAGATCAAAGTCCTGGGTCCTTATACCTTTAGCATCTGTGACACC
TCCAACTTCTCCGACTACATCCGTGGAGGCATCGTCAGTCAGGTCAAAGTACCTAAGAAG
ATTAGCTTTAAATCCTTGGTGGCCTCACTGGCAGAACCTGACTTTGTGGTGACGGACTTC
GCCAAGTTTTCTCGCCCTGCCCAGCTGCACATTGGCTTCCAGGCCCTGCACCAGTTCTGT
GCTCAGCATGGCCGGCCACCTCGGCCCCGCAATGAGGAGGATGCAGCAGAACTGGTAGCC
TTAGCACAGGCTGTGAATGCTCGAGCCCTGCCAGCAGTGCAGCAAAATAACCTGGACGAG
GACCTCATCCGGAAGCTGGCATATGTGGCTGCTGGGGATCTGGCACCCATAAACGCCTTC
ATTGGGGGCCTGGCTGCCCAGGAAGTCATGAAGGCCTGCTCCGGGAAGTTCATGCCCATC
ATGCAGTGGCTATACTTTGATGCCCTTGAGTGTCTCCCTCAGGACAAAGAGGTCCTCACA
GAGGACAAGTGCCTCCAGCGCCAGAACCGTTATGACGGGCAAGTGGCTGTGTTTGGCTCA
GACCTGCAAGAGAAGCTGGGCAAGCAGAAGTATTTCCTGGTGGGTGCGGGGGCCATTGGC
TGTGAGCTGCTCAAGAACTTTGCCATGATTGGGCTGGGCTGCGGGGAGGGTGGAGAAATC
ATCGTTACAGACATGGACACCATTGAGAAGTCAAATCTGAATCGACAGTTTCTTTTCCGG
CCCTGGGATGTCACGAAGTTAAAGTCTGACACGGCTGCTGCAGCTGTGCGCCAAATGAAT
CCACATATCCGGGTGACAAGCCACCAGAACCGTGTGGGTCCTGACACGGAGCGCATCTAT
GATGACGATTTTTTCCAAAACCTAGATGGCGTGGCCAATGCCCTGGACAACGTGGATGCC
CGCATGTACATGGACCGCCGCTGTGTCTACTACCGGAAGCCACTGCTGGAGTCAGGCACA
CTGGGCACCAAAGGCAATGTGCAGGTGGTGATCCCCTTCCTGACAGAGTCGTACAGTTCC
AGCCAGGACCCACCTGAGAAGTCCATCCCCATCTGTACCCTGAAGAACTTCCCTAATGCC
ATCGAGCACACCCTGCAGTGGGCTCGGGATGAGTTTGAAGGCCTCTTCAAGCAGCCAGCA
GAAAATGTCAACCAGTACCTCACAGACCCCAAGTTTGTGGAGCGAACACTGCGGCTGGCA
GGCACTCAGCCCTTGGAGGTGCTGGAGGCTGTGCAGCGCAGCCTGGTGCTGCAGCGACCA
CAGACCTGGGCTGACTGCGTGACCTGGGCCTGCCACCACTGGCACACCCAGTACTCGAAC
AACATCCGGCAGCTGCTGCACAACTTCCCTCCTGACCAGCTCACAAGCTCAGGAGCGCCG
TTCTGGTCTGGGCCCAAACGCTGTCCACACCCGCTCACCTTTGATGTCAACAATCCCCTG
CATCTGGACTATGTGATGGCTGCTGCCAACCTGTTTGCCCAGACCTACGGGCTGACAGGC
TCTCAGGACCGAGCTGCTGTGGCCACATTCCTGCAGTCTGTGCAGGTCCCCGAATTCACC
CCCAAGTCTGGCGTCAAGATCCATGTTTCTGACCAGGAGCTGCAGAGCGCCAATGCCTCT
GTTGATGACAGTCGTCTAGAGGAGCTCAAAGCCACTCTGCCCAGCCCAGACAAGCTCCCT
GGATTCAAGATGTACCCCATTGACTTTGAGAAGGATGATGACAGCAACTTTCATATGGAT
TTCATCGTGGCTGCATCCAACCTCCGGGCAGAAAACTATGACATTCCTTCTGCAGACCGG
CACAAGAGCAAGCTGATTGCAGGGAAGATCATCCCAGCCATTGCCACGACCACAGCAGCC
GTGGTTGGCCTTGTGTGTCTGGAGCTGTACAAGGTTGTGCAGGGGCACCGACAGCTTGAC
TCCTACAAGAATGGTTTCCTCAACTTGGCCCTGCCTTTCTTTGGTTTCTCTGAACCCCTT
GCCGCACCACGTCACCAGTACTATAACCAAGAGTGGACATTGTGGGATCGCTTTGAGGTA
CAAGGGCTGCAGCCTAATGGTGAGGAGATGACCCTCAAACAGTTCCTCGACTATTTTAAG
ACAGAGCACAAATTAGAGATCACCATGCTGTCCCAGGGCGTGTCCATGCTCTATTCCTTC
TTCATGCCAGCTGCCAAGCTCAAGGAACGGTTGGATCAGCCGATGACAGAGATTGTGAGC
CGTGTGTCGAAGCGAAAGCTGGGCCGCCACGTGCGGGCGCTGGTGCTTGAGCTGTGCTGT
AACGACGAGAGCGGCGAGGATGTCGAGGTTCCCTATGTCCGATACACCATCCGCTGA

Enzyme 74 GenBank Gene ID

X56976

Enzyme 74 GeneCard ID

UBA1

Enzyme 74 GenAtlas ID

UBA1

Enzyme 74 HGNC ID

HGNC:12469 Link Image

Enzyme 74 Chromosome Location

Not Available

Enzyme 74 Locus

Not Available

Enzyme 74 SNPs

SNPJam Report Link Image

Enzyme 74 General References

Ayusawa D, Kaneda S, Itoh Y, Yasuda H, Murakami Y, Sugasawa K, Hanaoka F, Seno T: Complementation by a cloned human ubiquitin-activating enzyme E1 of the S-phase-arrested mouse FM3A cell mutant with thermolabile E1. Cell Struct Funct. 1992 Apr;17(2):113-22. [PubMed ]
Handley PM, Mueckler M, Siegel NR, Ciechanover A, Schwartz AL: Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):258-62. [PubMed ]
Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7456. [PubMed ]
Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Zacksenhaus E, Sheinin R: Molecular cloning, primary structure and expression of the human X linked A1S9 gene cDNA which complements the ts A1S9 mouse L cell defect in DNA replication. EMBO J. 1990 Sep;9(9):2923-9. [PubMed ]
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
Allen E, Ding J, Wang W, Pramanik S, Chou J, Yau V, Yang Y: Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival. Nature. 2005 Nov 10;438(7065):224-8. Epub 2005 Oct 16. [PubMed ]
Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Ramser J, Ahearn ME, Lenski C, Yariz KO, Hellebrand H, von Rhein M, Clark RD, Schmutzler RK, Lichtner P, Hoffman EP, Meindl A, Baumbach-Reardon L: Rare missense and synonymous variants in UBE1 are associated with X-linked infantile spinal muscular atrophy. Am J Hum Genet. 2008 Jan;82(1):188-93. [PubMed ]

Enzyme 74 Metabolite References

Not Available

Enzyme 75 [top]

Enzyme 75 ID

5891

Enzyme 75 Name

Tyrosyl-tRNA synthetase, mitochondrial

Enzyme 75 Synonyms

Tyrosine--tRNA ligase
TyrRS

Enzyme 75 Gene Name

YARS2

Enzyme 75 Protein Sequence

>Tyrosyl-tRNA synthetase, mitochondrial

MAAPILRSFSWGRWSGTLNLSVLLPLGLRKAHSGAQGLLAAQKARGLFKDFFPETGTKIE
LPELFDRGTASFPQTIYCGFDPTADSLHVGHLLALLGLFHLQRAGHNVIALVGGATARLG
DPSGRTKEREALETERVRANARALRLGLEALAANHQQLFTDGRSWGSFTVLDNSAWYQKQ
HLVDFLAAVGGHFRMGTLLSRQSVQLRLKSPEGMSLAEFFYQVLQAYDFYYLFQRYGCRV
QLGGSDQLGNIMSGYEFINKLTGEDVFGITVPLITSTTGAKLGKSAGNAVWLNRDKTSPF
ELYQFFVRQPDDSVERYLKLFTFLPLPEIDHIMQLHVKEPERRGPQKRLAAEVTKLVHGR
EGLDSAKRCTQALYHSSIDALEVMSDQELKELFKEAPFSEFFLDPGTSVLDTCRKANAIP
DGPRGYRMITEGGVSINHQQVTNPESVLIVGQHILKNGLSLLKIGKRNFYIIKWLQL

Enzyme 75 Number of Residues

477

Enzyme 75 Molecular Weight

53198.6

Enzyme 75 Theoretical pI

9.34

Enzyme 75 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding tyrosine-tRNA ligase activity
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation tyrosyl-tRNA aminoacylation
Component
cell part cytoplasm intracellular part

Enzyme 75 General Function

Involved in nucleotide binding

Enzyme 75 Specific Function

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction:tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr)

Enzyme 75 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Phenylalanine and Tyrosine Metabolism (map00400 )

Enzyme 75 Reactions

ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr [RN:R02918]

Enzyme 75 Pfam Domain Function

tRNA-synt_1b (PF00579 )

Enzyme 75 Signals

None

Enzyme 75 Transmembrane Regions

None

Enzyme 75 Essentiality

Not Available

Enzyme 75 GenBank ID Protein

94681057

Enzyme 75 UniProtKB/Swiss-Prot ID

Q9Y2Z4

Enzyme 75 UniProtKB/Swiss-Prot Entry Name

SYYM_HUMAN Link Image

Enzyme 75 PDB ID

Not Available

Enzyme 75 Cellular Location

Not Available

Enzyme 75 Gene Sequence

>1434 bp

ATGGCGGCGCCCATCTTGCGGTCCTTTTCCTGGGGCCGGTGGTCTGGTACCCTAAATCTC
TCAGTATTGTTGCCCTTGGGGCTGCGTAAGGCCCACTCGGGCGCTCAGGGGTTACTGGCA
GCGCAGAAGGCTCGAGGTCTGTTCAAGGACTTCTTCCCGGAGACGGGGACGAAAATAGAG
CTCCCAGAGCTCTTCGACCGTGGCACGGCGAGTTTTCCCCAAACCATTTACTGTGGCTTC
GACCCCACGGCAGACTCGCTTCATGTGGGTCATCTACTTGCGCTGCTGGGCCTGTTTCAT
TTGCAGCGAGCGGGCCACAACGTGATCGCGCTGGTGGGAGGCGCCACGGCGCGCCTGGGA
GACCCGAGCGGCCGTACCAAGGAACGCGAGGCGCTGGAGACAGAGCGCGTGCGAGCCAAC
GCGCGAGCTCTGCGCCTAGGGCTTGAGGCCCTGGCGGCTAATCACCAGCAGCTTTTCACT
GATGGGCGCTCCTGGGGCAGCTTCACTGTGCTGGACAACTCGGCCTGGTACCAGAAGCAG
CACCTGGTGGACTTCCTGGCGGCAGTGGGGGGTCACTTCCGCATGGGGACGCTGCTGAGC
CGGCAGAGCGTGCAGCTGCGGCTCAAGAGCCCCGAGGGCATGAGCTTGGCCGAGTTCTTT
TACCAGGTGCTCCAGGCCTATGACTTCTATTACCTCTTCCAGCGTTATGGATGCAGGGTC
CAGCTGGGCGGATCTGATCAACTAGGCAACATCATGTCCGGATATGAGTTCATCAACAAG
TTGACTGGAGAAGATGTATTTGGAATCACCGTTCCTCTAATTACAAGTACAACTGGAGCA
AAGCTGGGAAAGTCTGCTGGCAACGCTGTTTGGCTAAACAGAGATAAGACATCTCCATTT
GAATTGTATCAATTCTTTGTCAGGCAACCGGACGATTCAGTGGAAAGGTACCTGAAGCTG
TTCACTTTCCTGCCCCTTCCAGAGATTGATCATATCATGCAGCTGCATGTCAAAGAGCCA
GAAAGGCGGGGTCCTCAGAAACGACTGGCAGCAGAAGTAACAAAGCTTGTTCATGGACGA
GAAGGATTGGATTCTGCTAAAAGGTGTACACAAGCCCTTTATCACAGTAGCATAGATGCA
CTGGAGGTCATGTCTGATCAGGAGTTAAAAGAGTTGTTTAAAGAAGCTCCATTTTCTGAA
TTTTTTCTCGATCCTGGAACAAGTGTCCTAGATACTTGCCGCAAAGCAAATGCCATTCCA
GATGGTCCCCGAGGGTATCGAATGATAACAGAAGGCGGAGTCAGCATAAATCACCAACAA
GTAACAAATCCTGAGAGTGTTTTAATTGTTGGACAACATATTCTCAAGAATGGACTTTCC
TTACTTAAAATAGGAAAAAGAAATTTCTACATTATAAAATGGCTTCAGTTGTGA

Enzyme 75 GenBank Gene ID

NM_001040436.1 Link Image

Enzyme 75 GeneCard ID

YARS2

Enzyme 75 GenAtlas ID

YARS2

Enzyme 75 HGNC ID

HGNC:24249 Link Image

Enzyme 75 Chromosome Location

Enzyme 75 Locus

12p11.21

Enzyme 75 SNPs

SNPJam Report Link Image

Enzyme 75 General References

Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M: Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. [PubMed ]
Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 75 Metabolite References

Not Available

Enzyme 76 [top]

Enzyme 76 ID

5892

Enzyme 76 Name

Ubiquitin-conjugating enzyme E2 E1

Enzyme 76 Synonyms

UbcH6
Ubiquitin carrier protein E1
Ubiquitin-protein ligase E1

Enzyme 76 Gene Name

UBE2E1

Enzyme 76 Protein Sequence

>Ubiquitin-conjugating enzyme E2 E1

MSDDDSRASTSSSSSSSSNQQTEKETNTPKKKESKVSMSKNSKLLSTSAKRIQKELADIT
LDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFTPEYPFKPPKVTFRTRIY
HCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQYMTNRAEH
DRMARQWTKRYAT

Enzyme 76 Number of Residues

193

Enzyme 76 Molecular Weight

21403.9

Enzyme 76 Theoretical pI

8.71

Enzyme 76 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 76 General Function

Involved in acid-amino acid ligase activity

Enzyme 76 Specific Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination

Enzyme 76 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 76 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 76 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 76 Signals

None

Enzyme 76 Transmembrane Regions

None

Enzyme 76 Essentiality

Not Available

Enzyme 76 GenBank ID Protein

189054583

Enzyme 76 UniProtKB/Swiss-Prot ID

P51965

Enzyme 76 UniProtKB/Swiss-Prot Entry Name

UB2E1_HUMAN Link Image

Enzyme 76 PDB ID

1Y6L

Enzyme 76 PDB File

Show

Enzyme 76 3D Structure

Enzyme 76 Cellular Location

Not Available

Enzyme 76 Gene Sequence

>582 bp

ATGTCGGATGACGATTCGAGGGCCAGCACCAGCTCCTCCTCATCTTCGTCTTCCAACCAG
CAAACCGAGAAAGAAACAAACACCCCCAAGAAGAAGGAGAGTAAAGTCAGCATGAGCAAA
AACTCCAAACTCCTCTCCACCAGCGCCAAGAGAATTCAGAAGGAGCTGGCGGACATCACT
TTAGACCCTCCACCTAATTGCAGTGCTGGTCCCAAAGGCGATAACATCTATGAATGGAGA
TCAACCATTCTAGGGCCTCCAGGATCCGTGTATGAGGGTGGTGTATTCTTTCTCGATATC
ACTTTTACACCAGAATATCCCTTCAAGCCTCCAAAGGTTACATTTCGGACAAGAATCTAT
CATTGTAATATTAACAGTCAAGGTGTTATTTGCTTGGACATATTGAAAGATAATTGGAGT
CCAGCACTAACCATTTCTAAAGTCCTCCTTTCTATCTGCTCACTTCTTACAGACTGTAAT
CCTGCCGACCCCTTGGTGGGAAGTATTGCCACTCAGTATATGACCAACAGAGCAGAACAT
GACAGAATGGCCAGACAGTGGACCAAGAGATACGCTACATAA

Enzyme 76 GenBank Gene ID

AK314854

Enzyme 76 GeneCard ID

UBE2E1

Enzyme 76 GenAtlas ID

UBE2E1

Enzyme 76 HGNC ID

HGNC:12477 Link Image

Enzyme 76 Chromosome Location

Enzyme 76 Locus

3p24.2

Enzyme 76 SNPs

SNPJam Report Link Image

Enzyme 76 General References

Nuber U, Schwarz S, Kaiser P, Schneider R, Scheffner M: Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. J Biol Chem. 1996 Feb 2;271(5):2795-800. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Takeuchi T, Iwahara S, Saeki Y, Sasajima H, Yokosawa H: Link between the ubiquitin conjugation system and the ISG15 conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme. J Biochem. 2005 Dec;138(6):711-9. [PubMed ]
Espinosa A, Oke V, Elfving A, Nyberg F, Covacu R, Wahren-Herlenius M: The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but enters the nucleus upon cellular exposure to nitric oxide. Exp Cell Res. 2008 Dec 10;314(20):3605-13. Epub 2008 Sep 25. [PubMed ]
Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]

Enzyme 76 Metabolite References

Not Available

Enzyme 77 [top]

Enzyme 77 ID

5893

Enzyme 77 Name

Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]

Enzyme 77 Synonyms

Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
Ap4A hydrolase
Ap4Aase
Diadenosine tetraphosphatase
Nucleoside diphosphate-linked moiety X motif 2
Nudix motif 2

Enzyme 77 Gene Name

NUDT2

Enzyme 77 Protein Sequence

>Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]

MALRACGLIIFRRCLIPKVDNNAIEFLLLQASDGIHHWTPPKGHVEPGEDDLETALRETQ
EEAGIEAGQLTIIEGFKRELNYVARNKPKTVIYWLAEVKDYDVEIRLSHEHQAYRWLGLE
EACQLAQFKEMKAALQEGHQFLCSIEA

Enzyme 77 Number of Residues

147

Enzyme 77 Molecular Weight

16829.1

Enzyme 77 Theoretical pI

5.06

Enzyme 77 GO Classification

Function
bis(5'-nucleosyl)-tetraphosphatase activity catalytic activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides nucleotide diphosphatase activity pyrophosphatase activity
Process
—
Component
—

Enzyme 77 General Function

Involved in hydrolase activity

Enzyme 77 Specific Function

Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis

Enzyme 77 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 77 Reactions

P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP [RN:R01232]

Enzyme 77 Pfam Domain Function

NUDIX (PF00293 )

Enzyme 77 Signals

None

Enzyme 77 Transmembrane Regions

None

Enzyme 77 Essentiality

Not Available

Enzyme 77 GenBank ID Protein

55958893

Enzyme 77 UniProtKB/Swiss-Prot ID

P50583

Enzyme 77 UniProtKB/Swiss-Prot Entry Name

AP4A_HUMAN Link Image

Enzyme 77 PDB ID

1XSC

Enzyme 77 PDB File

Show

Enzyme 77 3D Structure

Enzyme 77 Cellular Location

Not Available

Enzyme 77 Gene Sequence

>444 bp

ATGGCCTTGAGAGCATGTGGCTTGATCATCTTCCGAAGATGCCTCATTCCCAAAGTGGAC
AACAATGCAATTGAGTTTTTACTGCTGCAGGCATCAGATGGCATTCATCACTGGACTCCT
CCCAAAGGCCATGTGGAACCAGGAGAGGATGACTTGGAAACAGCCCTGAGGGAGACCCAA
GAGGAAGCAGGCATAGAAGCAGGCCAGCTGACCATTATTGAGGGGTTCAAAAGGGAACTC
AATTATGTGGCCAGGAACAAGCCTAAAACAGTCATTTACTGGCTGGCGGAGGTGAAGGAC
TATGACGTGGAGATCCGCCTCTCCCATGAGCACCAAGCCTACCGCTGGCTGGGGCTGGAG
GAGGCCTGCCAGTTGGCTCAGTTCAAGGAGATGAAGGCAGCGCTCCAAGAAGGACACCAG
TTTCTTTGCTCCATAGAGGCCTGA

Enzyme 77 GenBank Gene ID

AL356494

Enzyme 77 GeneCard ID

NUDT2

Enzyme 77 GenAtlas ID

NUDT2

Enzyme 77 HGNC ID

HGNC:8049

Enzyme 77 Chromosome Location

Enzyme 77 Locus

9p13

Enzyme 77 SNPs

SNPJam Report Link Image

Enzyme 77 General References

Thorne NM, Hankin S, Wilkinson MC, Nunez C, Barraclough R, McLennan AG: Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases. Biochem J. 1995 Nov 1;311 ( Pt 3):717-21. [PubMed ]
Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Swarbrick JD, Buyya S, Gunawardana D, Gayler KR, McLennan AG, Gooley PR: Structure and substrate-binding mechanism of human Ap4A hydrolase. J Biol Chem. 2005 Mar 4;280(9):8471-81. Epub 2004 Dec 13. [PubMed ]

Enzyme 77 Metabolite References

Not Available

Enzyme 78 [top]

Enzyme 78 ID

5894

Enzyme 78 Name

Long-chain-fatty-acid--CoA ligase 6

Enzyme 78 Synonyms

Long-chain acyl-CoA synthetase 6
LACS 6

Enzyme 78 Gene Name

ACSL6

Enzyme 78 Protein Sequence

>Long-chain-fatty-acid--CoA ligase 6

MQTQEILRILRLPELGDLGQFFRSLSATTLVSMGALAAILAYWFTHRPKALQPPCNLLMQ
SEEVEDSGGARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPKQPYQW
LSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDT
LGPGAIRYIINTADISTVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKERGQK
CGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF
LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCP
TIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKI
QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV
GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGD
IGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGI
VVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHS
DMFSVQNGLLTPTLKAKRPELREYFKKQIEELYSISM

Enzyme 78 Number of Residues

697

Enzyme 78 Molecular Weight

77751.3

Enzyme 78 Theoretical pI

7.46

Enzyme 78 GO Classification

Function
catalytic activity
Process
metabolic process
Component
—

Enzyme 78 General Function

Involved in catalytic activity

Enzyme 78 Specific Function

Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid

Enzyme 78 Pathways

Fatty Acid Metabolism (map00071 )

Enzyme 78 Reactions

ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]

Enzyme 78 Pfam Domain Function

AMP-binding (PF00501 )

Enzyme 78 Signals

None

Enzyme 78 Transmembrane Regions

25-45

Enzyme 78 Essentiality

Not Available

Enzyme 78 GenBank ID Protein

5702202

Enzyme 78 UniProtKB/Swiss-Prot ID

Q9UKU0

Enzyme 78 UniProtKB/Swiss-Prot Entry Name

ACSL6_HUMAN Link Image

Enzyme 78 PDB ID

Not Available

Enzyme 78 Cellular Location

Not Available

Enzyme 78 Gene Sequence

>2094 bp

ATGCAGACACAGGAGATCCTGAGGATACTGCGACTGCCTGAGCTAGGTGACTTGGAACAG
TTTTTCCGCAGCCTCTCGGCCACCACCCTCGTGAGTATGGGTGCCCTGGCTGCCATCCTT
GCCTACTGGTTCACTCAGCGGCCAAAGGCCTTGCAGCCGCCATGCAACCTCCTGATGCAG
TCAGAAGAAGTAGAGGACAGTGGCGGGGCACGGCGATCTGTGATTGGGTCTGGCCCTCAG
CTACTTACCCACTACTATGATGATGCCCGGACCATGTACCAGGTGTTCCGCCGTGGGCTT
AGCATCTCAGGGAATGGGCCCTGTCTTGGTTTCAGGAAGCCTAAGCAGCCTTACCAGTGG
CTGTCCTACCAGGAGGTGGCCGACAGGGCTGAATTTCTGGGGTCCGGACTTCTCCAGCAC
AATTGTAAAGCATGCACTGATCAGTTTATTGGTGTTTTTGCACAAAATCGGCCAGAGTGG
ATCATTGTGGAGCTGGCCTGCTACACATATTCCATGGTGGTGGTCCCGCTCTATGACACC
CTGGGCCCTGGGGCTATCCGCTACATCATCAATACAGCGGACATCAGCACCGTGATTGTG
GACAAACCTCAGAAGGCTGTGCTTCTGCTAGAGCATGTGGAGAGGAAGGAGACTCCAGGC
CTCAAGCTGATCATCCTCATGGACCCATTCGAAGAAGCCCTGAAAGAGAGAGGGCAGAAG
TGCGGGGTGGTCATTAAGTCCATGCAGGCCGTGGAGGACTGTGGCCAAGAGAATCACCAG
GCTCCTGTGCCCCCGCAGCCTGATGACCTCTCCATTGTGTGTTTCACAAGCGGCACGACA
GGGAACCCAAAAGGTGCGATGCTCACCCATGGGAACGTGGTGGCTGATTTCTCAGGCTTT
CTGAAAGTGACAGAGAGTCAGTGGGCTCCCACTTGTGCGGATGTGCACATTTCCTATTTG
CCTTTAGCACACATGTTTGAGCGAATGGTGCAGTCTGTCGTCTATTGCCACGGAGGGCGT
GTTGGCTTCTTCCAGGGAGATATCCGCCTTCTCTCAGATGACATGAAGGCTCTATGCCCC
ACCATCTTCCCTGTGGTCCCACGACTGCTGAACCGGATGTACGACAAGATCTTCAGCCAG
GCAAACACACCATTAAAGCGCTGGCTCCTGGAGTTTGCAGCAAAGCGTAAGCAAGCCGAG
GTCCGGAGTGGAATCATCAGGAATGATAGTATCTGGGATGAACTCTTCTTTAATAAGATT
CAGGCCAGTCTTGGTGGGTGTGTGCGGATGATTGTTACTGGAGCAGCCCCAGCATCACCA
ACAGTTCTGGGATTTCTCCGGGCAGCTCTAGGGTGCCAGGTTTATGAAGGTTATGGCCAA
ACTGAGTGCACAGCTGGATGTACCTTCACCACTCCTGGCGACTGGACCTCAGGGCACGTA
GGGGCGCCACTTCCCTGCAATCATATCAAGCTCGTTGATGTTGAGGAACTGAACTACTGG
GCCTGCAAAGGAGAGGGAGAGATATGTGTGAGAGGACCAAATGTGTTCAAAGGCTACTTG
AAAGATCCAGACAGGACGAAGGAGGCCCTGGACAGCGATGGCTGGCTTCACACTGGAGAC
ATCGGAAAATGGCTGCCGGCAGGAACTCTTAAAATTATTGATCGGAAAAAGCATATATTT
AAACTTGCTCAGGGAGAATATGTTGCACCCGAGAAGATTGAGAACATCTACATCCGGAGC
CAACCTGTGGCGCAAATCTATGTCCATGGGGACAGCTTAAAGGCCTTTTTGGTAGGCATT
GTTGTGCCTGACCCTGAAGTTATGCCCTCCTGGGCCCAGAAGAGAGGAATTGAAGGAACA
TATGCAGATCTCTGCACAAATAAGGATCTGAAGAAAGCCATTTTGGAAGATATGGTGAGG
TTAGGAAAAGAAAGTGGACTCCATTCTTTTGAGCAGGTTAAAGCCATTCACATCCATTCT
GACATGTTCTCAGTTCAAAATGGCTTGCTGACCCCAACACTAAAAGCTAAGAGACCTGAG
CTGAGAGAGTACTTCAAAAAACAAATAGAAGAGCTTTACTCAATCCCCATGTGA

Enzyme 78 GenBank Gene ID

AF129166

Enzyme 78 GeneCard ID

ACSL6

Enzyme 78 GenAtlas ID

ACSL6

Enzyme 78 HGNC ID

HGNC:16496 Link Image

Enzyme 78 Chromosome Location

Enzyme 78 Locus

5q31

Enzyme 78 SNPs

SNPJam Report Link Image

Enzyme 78 General References

Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed ]
Yagasaki F, Jinnai I, Yoshida S, Yokoyama Y, Matsuda A, Kusumoto S, Kobayashi H, Terasaki H, Ohyashiki K, Asou N, Murohashi I, Bessho M, Hirashima K: Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and acute myelogenous leukemia with t(5;12)(q31;p13). Genes Chromosomes Cancer. 1999 Nov;26(3):192-202. [PubMed ]
Soupene E, Kuypers FA: Multiple erythroid isoforms of human long-chain acyl-CoA synthetases are produced by switch of the fatty acid gate domains. BMC Mol Biol. 2006 Jul 11;7:21. [PubMed ]
Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed ]
Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 78 Metabolite References

Not Available

Enzyme 79 [top]

Enzyme 79 ID

5895

Enzyme 79 Name

Methionyl-tRNA synthetase, cytoplasmic

Enzyme 79 Synonyms

Methionine--tRNA ligase
MetRS

Enzyme 79 Gene Name

MARS

Enzyme 79 Protein Sequence

>Methionyl-tRNA synthetase, cytoplasmic

MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLF
STSAICRYFFLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRA
LTHIDHSLSRQNCPFLAGETESLADIVLWGALYPLLQDPAYLPEELSALHSWFQTLSTQE
PCQRAAETVLKQQGVLALRPYLQKQPQPSPAEGRAVTNEPEEEELATLSEEEIAMAVTAW
EKGLESLPPLRPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRL
RQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYRWFNISFDIFGRTTTP
QQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDK
CGKLINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQF
ITRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWW
KNPEQVDLYQFMAKDNVPFHSLVFPCSALGAEDNYTLVSHLIATEYLNYEDGKFSKSRGV
GVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMF
VSKFFGGYVPEMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQ
VNEPWKRIKGSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSI
LLTNFLCTLPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPAVVETVTTAKPQ
QIQALMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKPPEAPKGKKKK

Enzyme 79 Number of Residues

900

Enzyme 79 Molecular Weight

101114.9

Enzyme 79 Theoretical pI

6.05

Enzyme 79 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds methionine-tRNA ligase activity nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process methionyl-tRNA aminoacylation ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 79 General Function

Involved in nucleotide binding

Enzyme 79 Specific Function

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)

Enzyme 79 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Methionine Metabolism (map00271 )
Selenoamino Acid Metabolism (map00450 )

Enzyme 79 Reactions

ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet [RN:R03659]

Enzyme 79 Pfam Domain Function

tRNA-synt_1g (PF09334 )
WHEP-TRS (PF00458 )

Enzyme 79 Signals

None

Enzyme 79 Transmembrane Regions

None

Enzyme 79 Essentiality

Not Available

Enzyme 79 GenBank ID Protein

1702932

Enzyme 79 UniProtKB/Swiss-Prot ID

P56192

Enzyme 79 UniProtKB/Swiss-Prot Entry Name

SYMC_HUMAN Link Image

Enzyme 79 PDB ID

Not Available

Enzyme 79 Cellular Location

Not Available

Enzyme 79 Gene Sequence

>2703 bp

ATGAGACTGTTCGTGAGTGATGGCGTCCCGGGTTGCTTGCCGGTGCTGGCCGCCGCCGGG
AGAGCCCGGGGCAGAGCAGAGGTGCTGATCAGCACTGTAGGCCCGGAAGATTGTGTGGTC
CCGTTCCTGACCCGGCCTAAGGTCCCTGTCTTGCAGGTGGATAGCGGCAACTACCTCTTC
TCCACTAGTGCAATCTGCCGATATTTTTTTTTGTTATCTGGCTGGGAGCAAGATGACCTC
ACTAACCAGTGGCTGGAATGGGAAGCGACAGAGCTGCAGCCAGCTTTGTCTGCTCCCCTG
TACTATTTAGTGGTCCAAGGCAAGAAGGGGGAAGATGTTCTTGGTTCAGTGCGGAGAGCC
CTGACTCACATTGACCACAGCTTGAGTCGTCAGAACTGTCCTTTCCTGGCTGGGGAGACA
GAATCTCTAGCCGACATTGTTTTGTGGGGAGCCCAATACCCATTACTGCAAGATCCCGCC
TACCTCCCTGAGGAGCTGAGTGCCCTGCACAGCTGGTTCCAGACACTGAGTACCCAGGAA
CCATGTCAGCGAGCTGCAGAGACTGTACTGAAACAGCAAGGTGTCCTGGCTCTCCGGCCT
TACCTCCAAAAGCAGCCCCAGCCCAGCCCCGCTGAGGGAAGGGCTGTCACCAATGAGCCT
GAGGAGGAGGAGCTGGCTACCCTATCTGAGGAGGAGATTGCTATGGCTGTTACTGCTTGG
GAGAAGGGCCTAGAAAGTTTGCCCCCGCTGCGGCCCCAGCAGAATCCAGTGTTGCCTGTG
GCTGGAGAAAGGAATGTGCTCATCACCAGTGCCCTCCCTTACGTCAACAATGTCCCCCAC
CTTGGGAACATCATTGGTTGTGTGCTCAGTGCCGATGTCTTTGCCAGGTACTCTCGCCTC
CGCCAGTGGAACACCCTCTATCTGTGTGGGACAGATGAGTATGGTACAGCAACAGAGACC
AAGGCTCTGGAGGAGGGACTAACCCCCCAGGAGATCTGCGACAAGTACCACATCATCCAT
GCTGACATCTACCGCTGGTTTAACATTTCGTTTGATATTTTTGGTCGCACCACCACTCCA
CAGCAGACCAAAATCACCCAGGACATTTTCCAGCAGTTGCTGAAACGAGGTTTTGTGCTG
CAAGATACTGTGGAGCAACTGCGATGTGAGCACTGTGCTCGCTTCCTGGCTGACCGCTTC
GTGGAGGGCGTGTGTCCCTTCTGTGGCTATGAGGAGGCTCGGGGTGACCAGTGTGACAAG
TGTGGCAAGCTCATCAATGCTGTCGAGCTTAAGAAGCCTCAGTGTAAAGTCTGCCGATCA
TGCCCTGTGGTGCAGTCGAGCCAGCACCTGTTTCTGGACCTGCCTAAGCTGGAGAAGCGA
CTGGAGGAGTGGTTGGGGAGGACATTGCCTGGCAGTGACTGGACACCCAATGCCCAGTTT
ATCACCCGTTCTTGGCTTCGGGATGGCCTCAAGCCACGCTGCATAACCCGAGACCTCAAA
TGGGGAACCCCTGTACCCTTAGAAGGTTTTGAAGACAAGGTATTCTATGTCTGGTTTGAT
GCCACTATTGGCTATCTGTCCATCACAGCCAACTACACAGACCAGTGGGAGAGATGGTGG
AAGAACCCAGAGCAAGTGGACCTGTATCAGTTCATGGCCAAAGACAATGTTCCTTTCCAT
AGCTTAGTCTTTCCTTGCTCAGCCCTAGGAGCTGAGGATAACTATACCTTGGTCAGCCAC
CTCATTGCTACAGAGTACCTGAACTATGAGGATGGGAAATTCTCTAAGAGCCGCGGTGTG
GGAGTGTTTGGGGACATGGCCCAGGACACGGGGATCCCTGCTGACATCTGGCGCTTCTAT
CTGCTGTACATTCGGCCTGAGGGCCAGGACAGTGCTTTCTCCTGGACGGACCTGCTGCTG
AAGAATAATTCTGAGCTGCTTAACAACCTGGGCAACTTCATCAACAGAGCTGGGATGTTT
GTGTCTAAGTTCTTTGGGGGCTATGTGCCTGAGATGGTGCTCACCCCTGATGATCAGCGC
CTGCTGGGCCATGTCACCCTGGAGCTCCAGCACTATCACCAGCTACTTGAGAAGGTTCGG
ATCCGGGATGCCTTGCGCAGTATCCTCACCATATCTCGACATGGCAACCAATATATTCAG
GTGAATGAGCCCTGGAAGCGGATTAAAGGCAGTGAGGCTGACAGGCAACGGGCAGGAACA
GTGACTGGCTTGGCAGTGAATATAGCTGCCTTGCTCTCTGTCATGCTTCAGCCTTACATG
CCCACGGTTAGTGCCACAATCCAGGCCCAGCTGCAGCTCCCACCTCCAGCCTGCAGTATC
CTGCTGACAAACTTCCTGTGTACCTTACCAGCAGGACACCAGATTGGCACAGTCAGTCCC
TTGTTCCAAAAATTGGAAAATGACCAGATTGAAAGTTTAAGGCAGCGCTTTGGAGGGGGC
CAGGCAAAAACGTCCCCGAAGCCAGCAGTTGTAGAGACTGTTACAACAGCCAAGCCACAG
CAGATACAAGCGCTGATGGATGAAGTGACAAAACAAGGAAACATTGTCCGAGAACTGAAA
GCACAAAAGGCAGACAAGAACGAGGTTGCTGCGGAGGTGGCGAAACTCTTGGATCTAAAG
AAACAGTTGGCTGTAGCTGAGGGGAAACCCCCTGAAGCCCCTAAAGGCAAGAAGAAAAAG
TAA

Enzyme 79 GenBank Gene ID

X94754

Enzyme 79 GeneCard ID

MARS

Enzyme 79 GenAtlas ID

MARS

Enzyme 79 HGNC ID

HGNC:6898

Enzyme 79 Chromosome Location

Enzyme 79 Locus

12q13.2

Enzyme 79 SNPs

SNPJam Report Link Image

Enzyme 79 General References

Lage H, Dietel M: Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase. Gene. 1996 Oct 31;178(1-2):187-9. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 79 Metabolite References

Not Available

Enzyme 80 [top]

Enzyme 80 ID

5897

Enzyme 80 Name

Alanyl-tRNA synthetase, cytoplasmic

Enzyme 80 Synonyms

Alanine--tRNA ligase
AlaRS
Renal carcinoma antigen NY-REN-42

Enzyme 80 Gene Name

AARS

Enzyme 80 Protein Sequence

>Alanyl-tRNA synthetase, cytoplasmic

MDSTLTASEIRQRFIDFFKRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTIDPS
HPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALE
LLTQEFGIPIERLYVTYFGGDEAAGLEADLECKQIWQNLGLDDTKILPGNMKDNFWEMGD
TGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNREADGILKPLPKKSIDT
GMGLERLVSVLQNKMSNYDTDLFVPYFEAIQKGTGARPYTGKVGAEDADGIDMAYRVLAD
HARTITVALADGGRPDNTGRGYVLRRILRRAVRYAHEKLNASRGFFATLVDVVVQSLGDA
FPELKKDPDMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDSKTIPGDTAWLLYDTYGF
PVDLTGLIAEEKGLVVDMDGFEEERKLAQLKSQGKGAGGEDLIMLDIYAIEELRARGLEV
TDDSPKYNYHLDSSGSYVFENTVATVMALRREKMFVEEVSTGQECGVVLDKTCFYAEQGG
QIYDEGYLVKVDDSSEDKTEFTVKNAQVRGGYVLHIGTIYGDLKVGDQVWLFIDEPRRRP
IMSNHTATHILNFALRSVLGEADQKGSLVAPDRLRFDFTAKGAMSTQQIKKAEEIANEMI
EAAKAVYTQDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPSGPAGSLTSV
EFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKAESLKKCLSVMEAK
VKAQTAPNKDVQREIADLGEALATAVIPQWQKDELRETLKSLKKVMDDLDRASKADVQKR
VLEKTKQFIDSNPNQPLVILEMESGASAKALNEALKLFKMHSPQTSAMLFTVDNEAGKIT
CLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDVSAQATGKNVGCLQEALQLATSFAQ
LRLGDVKN

Enzyme 80 Number of Residues

968

Enzyme 80 Molecular Weight

106809.5

Enzyme 80 Theoretical pI

5.18

Enzyme 80 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding alanine-tRNA ligase activity aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleic acid binding nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process alanyl-tRNA aminoacylation biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 80 General Function

Involved in nucleotide binding

Enzyme 80 Specific Function

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction:alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain

Enzyme 80 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )

Enzyme 80 Reactions

ATP + L-alanine + tRNAAla = AMP + diphosphate + L-alanyl-tRNAAla [RN:R03038]

Enzyme 80 Pfam Domain Function

DHHA1 (PF02272 )
tRNA-synt_2c (PF01411 )
tRNA_SAD (PF07973 )

Enzyme 80 Signals

None

Enzyme 80 Transmembrane Regions

None

Enzyme 80 Essentiality

Not Available

Enzyme 80 GenBank ID Protein

109148542

Enzyme 80 UniProtKB/Swiss-Prot ID

P49588

Enzyme 80 UniProtKB/Swiss-Prot Entry Name

SYAC_HUMAN Link Image

Enzyme 80 PDB ID

Not Available

Enzyme 80 Cellular Location

Not Available

Enzyme 80 Gene Sequence

>2907 bp

ATGGACTCTACTCTAACAGCAAGTGAAATCCGGCAGCGATTTATAGATTTCTTCAAGAGG
AACGAGCATACGTATGTTCACTCGTCTGCCACCATCCCATTGGATGACCCCACTTTGCTC
TTTGCCAATGCAGGCATGAACCAGTTTAAACCCATTTTCCTGAACACAATTGACCCATCT
CACCCCATGGCAAAGCTGAGCAGAGCTGCCAATACCCAGAAGTGCATCCGGGCTGGGGGC
AAACATAATGACCTGGACGATGTGGGCAAGGATGTCTATCATCACACCTTCTTCGAGATG
CTGGGCTCTTGGTCTTTTGGAGATTACTTTAAGGAATTGGCATGTAAGATGGCTCTGGAA
CTCCTCACCCAAGAGTTTGGCATTCCCATTGAAAGACTTTATGTTACTTACTTTGGCGGG
GATGAAGCAGCTGGCTTAGAAGCAGATCTGGAATGCAAACAGATCTGGCAAAATTTGGGG
CTGGATGACACCAAAATCCTCCCAGGCAACATGAAGGATAACTTCTGGGAGATGGGTGAC
ACGGGCCCCTGTGGTCCTTGCAGTGAGATCCACTACGACCGGATTGGTGGTCGGGACGCC
GCACATCTTGTCAACCAGGACGACCCTAATGTGCTGGAGATCTGGAACCTTGTGTTCATC
CAGTATAACAGGGAAGCTGATGGCATTCTGAAACCTCTTCCCAAGAAAAGCATTGACACA
GGGATGGGCCTGGAACGACTGGTATCTGTGCTGCAGAATAAGATGTCCAACTATGACACT
GACCTTTTTGTCCCTTACTTTGAAGCCATTCAGAAGGGCACAGGTGCCCGACCATACACT
GGGAAAGTTGGTGCTGAGGATGCCGATGGGATTGACATGGCCTACCGGGTGCTGGCTGAC
CACGCTCGGACCATCACTGTGGCACTGGCTGATGGTGGCCGGCCTGACAACACAGGGCGT
GGATATGTGTTGAGACGGATTCTCCGCCGAGCTGTCCGATACGCCCATGAAAAGCTCAAT
GCCAGCAGGGGCTTCTTTGCTACGTTAGTGGATGTTGTCGTCCAGTCCCTGGGAGATGCA
TTTCCTGAGCTGAAGAAGGACCCAGACATGGTGAAGGACATCATTAATGAAGAAGAGGTG
CAGTTTCTCAAGACTCTCAGCAGAGGGCGTCGCATCCTGGACAGGAAAATTCAGAGCCTG
GGAGACAGCAAGACCATTCCCGGAGACACTGCTTGGCTCCTCTATGACACCTATGGGTTT
CCAGTGGATCTGACTGGACTGATTGCTGAAGAGAAGGGCCTGGTGGTAGACATGGATGGC
TTTGAAGAGGAGAGGAAACTGGCCCAGCTGAAATCACAGGGCAAGGGAGCTGGTGGGGAA
GACCTCATTATGCTGGACATTTACGCTATCGAAGAGCTCCGGGCACGGGGTCTGGAGGTC
ACAGATGATTCCCCAAAGTACAATTACCATTTGGACTCCAGTGGTAGCTATGTATTTGAG
AACACAGTGGCTACGGTGATGGCTCTGCGCAGGGAGAAGATGTTCGTGGAAGAGGTGTCC
ACAGGCCAGGAGTGTGGAGTGGTGCTGGACAAGACCTGTTTCTATGCTGAGCAAGGAGGC
CAGATCTATGACGAAGGCTACCTGGTGAAGGTGGATGACAGCAGTGAAGATAAAACAGAG
TTTACAGTGAAGAATGCTCAGGTCCGAGGAGGGTATGTGCTACACATTGGAACCATCTAC
GGTGACCTGAAAGTGGGGGATCAGGTCTGGCTGTTTATTGATGAGCCCCGACGAAGACCC
ATCATGAGCAACCACACAGCTACGCACATTCTGAACTTCGCCCTGCGCTCAGTGCTTGGG
GAAGCTGACCAGAAAGGCTCATTGGTTGCTCCTGACCGCCTCAGATTTGACTTTACTGCC
AAGGGAGCCATGTCCACCCAACAGATCAAGAAGGCTGAAGAGATTGCTAATGAGATGATT
GAGGCAGCCAAGGCCGTCTATACCCAGGATTGCCCCCTGGCAGCAGCGAAAGCCATCCAG
GGCCTACGGGCTGTGTTTGATGAGACCTATCCTGACCCTGTGCGAGTCGTCTCCATTGGG
GTCCCGGTGTCCGAGTTGCTGGATGACCCCTCTGGGCCTGCTGGCTCCCTGACTTCTGTT
GAGTTCTGTGGGGGAACGCACCTGCGGAACTCGAGTCATGCAGGAGCTTTTGTGATCGTG
ACGGAAGAAGCCATTGCCAAGGGTATCCGGAGGATTGTGGCTGTCACAGGTGCCGAGGCC
CAGAAGGCCCTCAGGAAAGCAGAGAGCTTGAAGAAATGTCTCTCTGTCATGGAAGCCAAA
GTGAAGGCTCAGACTGCTCCAAACAAGGATGTGCAGAGGGAGATCGCTGACCTTGGAGAG
GCCCTGGCCACTGCAGTCATCCCCCAGTGGCAGAAGGATGAATTGCGGGAGACTCTCAAA
TCCCTAAAGAAGGTCATGGATGACTTGGACCGAGCCAGCAAAGCCGATGTCCAGAAACGA
GTGTTAGAGAAGACGAAGCAGTTCATCGACAGCAACCCCAACCAGCCTCTTGTCATCCTG
GAGATGGAGAGCGGCGCCTCAGCCAAGGCCCTGAATGAAGCCTTGAAGCTCTTCAAGATG
CACTCCCCTCAGACTTCTGCCATGCTCTTCACGGTGGACAATGAGGCTGGCAAGATCACG
TGCCTGTGTCAAGTTCCCCAGAATGCAGCCAATCGGGGCTTAAAAGCCAGCGAGTGGGTG
CAGCAGGTGTCAGGCTTGATGGACGGTAAAGGTGGTGGCAAGGATGTGTCTGCACAGGCC
ACAGGCAAGAACGTTGGCTGCCTGCAGGAGGCGCTGCAGCTGGCCACTTCCTTCGCCCAG
CTGCGCCTCGGGGATGTAAAGAACTGA

Enzyme 80 GenBank Gene ID

NM_001605.2 Link Image

Enzyme 80 GeneCard ID

AARS

Enzyme 80 GenAtlas ID

AARS

Enzyme 80 HGNC ID

HGNC:20

Enzyme 80 Chromosome Location

Enzyme 80 Locus

16q22

Enzyme 80 SNPs

SNPJam Report Link Image

Enzyme 80 General References

Shiba K, Ripmaster T, Suzuki N, Nichols R, Plotz P, Noda T, Schimmel P: Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition. Biochemistry. 1995 Aug 22;34(33):10340-9. [PubMed ]
Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed ]
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, Schimmel P: The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science. 2009 Aug 7;325(5941):744-7. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Latour P, Thauvin-Robinet C, Baudelet-Mery C, Soichot P, Cusin V, Faivre L, Locatelli MC, Mayencon M, Sarcey A, Broussolle E, Camu W, David A, Rousson R: A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease. Am J Hum Genet. 2010 Jan;86(1):77-82. Epub 2009 Dec 31. [PubMed ]

Enzyme 80 Metabolite References

Not Available

Enzyme 81 [top]

Enzyme 81 ID

5898

Enzyme 81 Name

Tryptophanyl-tRNA synthetase, mitochondrial

Enzyme 81 Synonyms

(Mt)TrpRS
Tryptophan--tRNA ligase
TrpRS

Enzyme 81 Gene Name

WARS2

Enzyme 81 Protein Sequence

>Tryptophanyl-tRNA synthetase, mitochondrial

MALHSMRKARERWSFIRALHKGSAAAPALQKDSKKRVFSGIQPTGILHLGNYLGAIESWV
RLQDEYDSVLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQQSQVSEH
TQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGE
DQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDKLATVRI
TDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVRRSAGMNTA
RYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGFL

Enzyme 81 Number of Residues

360

Enzyme 81 Molecular Weight

40146.3

Enzyme 81 Theoretical pI

9.82

Enzyme 81 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding tryptophan-tRNA ligase activity
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation tryptophanyl-tRNA aminoacylation
Component
cell part cytoplasm intracellular part

Enzyme 81 General Function

Involved in nucleotide binding

Enzyme 81 Specific Function

ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)

Enzyme 81 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Tryptophan Metabolism (map00380 )

Enzyme 81 Reactions

ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp [RN:R03664]

Enzyme 81 Pfam Domain Function

tRNA-synt_1b (PF00579 )

Enzyme 81 Signals

None

Enzyme 81 Transmembrane Regions

None

Enzyme 81 Essentiality

Not Available

Enzyme 81 GenBank ID Protein

6572289

Enzyme 81 UniProtKB/Swiss-Prot ID

Q9UGM6

Enzyme 81 UniProtKB/Swiss-Prot Entry Name

SYWM_HUMAN Link Image

Enzyme 81 PDB ID

Not Available

Enzyme 81 Cellular Location

Not Available

Enzyme 81 Gene Sequence

>1083 bp

ATGGCGCTGCACTCAATGCGGAAAGCGCGTGAGCGCTGGAGCTTCATCCGGGCACTTCAT
AAGGGATCCGCAGCTGCTCCCGCTCTCCAGAAAGACAGCAAGAAGCGAGTATTTTCCGGC
ATTCAACCTACAGGAATCCTCCACCTGGGCAATTACCTGGGAGCCATTGAGAGCTGGGTG
AGGTTACAGGATGAATATGACTCTGTATTATACAGCATTGTTGACCTCCACTCCATTACT
GTCCCCCAAGACCCAGCTGTCCTTCGGCAGAGCATCCTGGACATGACTGCTGTTCTTCTT
GCCTGTGGCATAAACCCGGAAAAAAGCATCCTTTTCCAACAATCTCAGGTGTCTGAACAC
ACACAATTAAGTTGGATCCTTTCCTGCATGGTCAGACTACCTCGATTACAACATTTACAT
CAGTGGAAGGCAAAGACTACCAAGCAGAAGCACGATGGCACGGTGGGCCTGCTCACATAC
CCAGTACTCCAGGCAGCCGACATTCTGTTGTACAAGTCCACACACGTTCCTGTTGGGGAG
GATCAAGTCCAGCACATGGAACTAGTTCAGGATCTAGCACAAGGTTTCAACAAGAAGTAT
GGGGAGTTCTTTCCAGTGCCCGAGTCCATTCTCACATCCATGAAGAAGGTAAAATCCCTA
CGTGATCCTTCTGCCAAAATGTCGAAATCAGACCCTGACAAACTGGCCACCGTCCGAATA
ACAGACAGCCCAGAGGAGATAGTGCAGAAATTCCGCAAGGCTGTGACAGACTTCACCTCG
GAGGTCACCTATGACCCGGCTGGCCGCGCTGGCGTGTCCAACATAGTGGCGGTGCATGCC
GCGGTGACGGGGCTCTCCGTGGAGGAAGTGGTGCGCCGCAGCGCGGGCATGAACACTGCT
CGCTACAAGCTGGCCGTGGCAGATGCTGTGATTGAGAAGTTTGCCCCAATTAAGCGTGAA
ATTGAAAAACTGAAGCTGGACAAGGACCATTTAGAGAAGGTTTTACAAATTGGATCAGCA
AAAGCCAAAGAATTAGCATACACTGTGTGCCAGGAGGTGAAGAAATTGGTGGGTTTTCTA
TAG

Enzyme 81 GenBank Gene ID

AJ242739

Enzyme 81 GeneCard ID

WARS2

Enzyme 81 GenAtlas ID

WARS2

Enzyme 81 HGNC ID

HGNC:12730 Link Image

Enzyme 81 Chromosome Location

Enzyme 81 Locus

1p12

Enzyme 81 SNPs

SNPJam Report Link Image

Enzyme 81 General References

Jorgensen R, Sogaard TM, Rossing AB, Martensen PM, Justesen J: Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase. J Biol Chem. 2000 Jun 2;275(22):16820-6. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 81 Metabolite References

Not Available

Enzyme 82 [top]

Enzyme 82 ID

5899

Enzyme 82 Name

ADP-sugar pyrophosphatase

Enzyme 82 Synonyms

Nucleoside diphosphate-linked moiety X motif 5
Nudix motif 5
YSA1H

Enzyme 82 Gene Name

NUDT5

Enzyme 82 Protein Sequence

>ADP-sugar pyrophosphatase

MESQEPTESSQNGKQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTTRKEQTAD
GVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFPAGLIDDGETPEAAALRELEEETGYK
GDIAECSPAVCMDPGLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPKNDLLQ
RLDALVAEEHLTVDARVYSYALALKHANAKPFEVPFLKF

Enzyme 82 Number of Residues

219

Enzyme 82 Molecular Weight

24327.4

Enzyme 82 Theoretical pI

4.59

Enzyme 82 GO Classification

Function
catalytic activity hydrolase activity
Process
—
Component
—

Enzyme 82 General Function

Involved in hydrolase activity

Enzyme 82 Specific Function

Hydrolyzes with similar activities ADP-ribose, ADP- mannose, and ADP-glucose. Can also hydrolyze other nucleotide sugars with low activity

Enzyme 82 Pathways

Purine Metabolism (map00230 )

Enzyme 82 Reactions

ADP-ribose + H2O = AMP + D-ribose 5-phosphate [RN:R01054]

Enzyme 82 Pfam Domain Function

NUDIX (PF00293 )

Enzyme 82 Signals

None

Enzyme 82 Transmembrane Regions

None

Enzyme 82 Essentiality

Not Available

Enzyme 82 GenBank ID Protein

6288769

Enzyme 82 UniProtKB/Swiss-Prot ID

Q9UKK9

Enzyme 82 UniProtKB/Swiss-Prot Entry Name

NUDT5_HUMAN Link Image

Enzyme 82 PDB ID

Not Available

Enzyme 82 Cellular Location

Not Available

Enzyme 82 Gene Sequence

>660 bp

ATGGAGAGCCAAGAACCAACGGAATCTTCTCAGAATGGCAAACAGTATATCATTTCAGAG
GAGTTAATTTCAGAAGGAAAATGGGTCAAGCTTGAAAAAACAACGTACATGGATCCTACT
GGTAAAACTAGAACTTGGGAATCAGTGAAACGTACAACCAGGAAAGAGCAGACTGCGGAT
GGTGTCGCGGTCATCCCCGTGCTGCAGAGAACACTTCACTATGAGTGTATCGTTCTGGTG
AAACAGTTCCGACCACCAATGGGGGGCTACTGCATAGAGTTCCCTGCAGGTCTCATAGAT
GATGGTGAAACCCCAGAAGCAGCTGCTCTCCGGGAGCTTGAAGAAGAAACTGGCTACAAA
GGGGACATTGCCGAATGTTCTCCAGCGGTCTGTATGGACCCAGGCTTGTCAAACTGTACT
ATACACATCGTGACAGTCACCATTAACGGAGATGATGCCGAAAACGCAAGGCCGAAGCCA
AAGCCAGGGGATGGAGAGTTTGTGGAAGTCATTTCTTTACCCAAGAATGACCTGCTGCAG
AGACTTGATGCTCTGGTAGCTGAAGAACATCTCACAGTGGACGCCAGGGTCTATTCCTAC
GCTCTAGCGCTGAAACATGCAAATGCAAAGCCATTTGAAGTGCCCTTCTTGAAATTTTAA

Enzyme 82 GenBank Gene ID

AF155832

Enzyme 82 GeneCard ID

NUDT5

Enzyme 82 GenAtlas ID

NUDT5

Enzyme 82 HGNC ID

HGNC:8052

Enzyme 82 Chromosome Location

Enzyme 82 Locus

10p14

Enzyme 82 SNPs

SNPJam Report Link Image

Enzyme 82 General References

Gasmi L, Cartwright JL, McLennan AG: Cloning, expression and characterization of YSA1H, a human adenosine 5'-diphosphosugar pyrophosphatase possessing a MutT motif. Biochem J. 1999 Dec 1;344 Pt 2:331-7. [PubMed ]
Yang H, Slupska MM, Wei YF, Tai JH, Luther WM, Xia YR, Shih DM, Chiang JH, Baikalov C, Fitz-Gibbon S, Phan IT, Conrad A, Miller JH: Cloning and characterization of a new member of the Nudix hydrolases from human and mouse. J Biol Chem. 2000 Mar 24;275(12):8844-53. [PubMed ]
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Zha M, Zhong C, Peng Y, Hu H, Ding J: Crystal structures of human NUDT5 reveal insights into the structural basis of the substrate specificity. J Mol Biol. 2006 Dec 15;364(5):1021-33. Epub 2006 Oct 3. [PubMed ]
Zha M, Guo Q, Zhang Y, Yu B, Ou Y, Zhong C, Ding J: Molecular mechanism of ADP-ribose hydrolysis by human NUDT5 from structural and kinetic studies. J Mol Biol. 2008 Jun 6;379(3):568-78. Epub 2008 Apr 8. [PubMed ]

Enzyme 82 Metabolite References

Not Available

Enzyme 83 [top]

Enzyme 83 ID

5900

Enzyme 83 Name

Ribose-phosphate pyrophosphokinase 1

Enzyme 83 Synonyms

PPRibP
Phosphoribosyl pyrophosphate synthase I
PRS-I

Enzyme 83 Gene Name

PRPS1

Enzyme 83 Protein Sequence

>Ribose-phosphate pyrophosphokinase 1

MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGC
GEINDNLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENISEWRNCTIVSPDAGGAKRVTS
IADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAI
RRTHNGESVSYLFSHVPL

Enzyme 83 Number of Residues

318

Enzyme 83 Molecular Weight

34833.9

Enzyme 83 Theoretical pI

6.98

Enzyme 83 GO Classification

Function
binding catalytic activity cation binding diphosphotransferase activity ion binding magnesium ion binding metal ion binding ribose phosphate diphosphokinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
biosynthetic process cellular biosynthetic process cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside metabolic process nucleoside monophosphate biosynthetic process nucleoside monophosphate metabolic process nucleoside phosphate metabolic process nucleotide biosynthetic process nucleotide metabolic process ribonucleoside monophosphate biosynthetic process
Component
—

Enzyme 83 General Function

Involved in magnesium ion binding

Enzyme 83 Specific Function

Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis

Enzyme 83 Pathways

Pentose Pathway (map00030 )
Purine Metabolism (map00230 )

Enzyme 83 Reactions

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate [RN:R01049]

Enzyme 83 Pfam Domain Function

Pribosyltran (PF00156 )

Enzyme 83 Signals

None

Enzyme 83 Transmembrane Regions

None

Enzyme 83 Essentiality

Not Available

Enzyme 83 GenBank ID Protein

57208781

Enzyme 83 UniProtKB/Swiss-Prot ID

P60891

Enzyme 83 UniProtKB/Swiss-Prot Entry Name

PRPS1_HUMAN Link Image

Enzyme 83 PDB ID

Not Available

Enzyme 83 Cellular Location

Not Available

Enzyme 83 Gene Sequence

>957 bp

ATGCCGAATATCAAAATCTTCAGCGGCAGCTCCCACCAGGACTTATCTCAGAAAATTGCT
GACCGCCTGGGCCTGGAGCTAGGCAAGGTGGTGACTAAGAAATTCAGCAACCAGGAGACC
TGTGTGGAAATTGGTGAAAGTGTACGTGGAGAGGATGTCTACATTGTTCAGAGTGGTTGT
GGCGAAATCAATGACAATTTAATGGAGCTTTTGATCATGATTAATGCCTGCAAGATTGCT
TCAGCCAGCCGGGTTACTGCAGTCATCCCATGCTTCCCTTATGCCCGGCAGGATAAGAAA
GATAAGAGCCGGGCGCCAATCTCAGCCAAGCTTGTTGCAAATATGCTATCTGTAGCAGGT
GCAGATCATATTATCACCATGGACCTACATGCTTCTCAAATTCAGGGCTTTTTTGATATC
CCAGTAGACAATTTGTATGCAGAGCCGGCTGTCCTAAAGTGGATAAGGGAGAATATCTCT
GAGTGGAGGAACTGCACTATTGTCTCACCTGATGCTGGTGGAGCTAAGAGAGTGACCTCC
ATTGCAGACAGGCTGAATGTGGACTTTGCCTTGATTCACAAAGAACGGAAGAAGGCCAAT
GAAGTGGACCGCATGGTGCTTGTGGGAGATGTGAAGGATCGGGTGGCCATCCTTGTGGAT
GACATGGCTGACACTTGTGGCACAATCTGCCATGCAGCTGACAAACTTCTCTCAGCTGGC
GCCACCAGAGTTTATGCCATCTTGACTCATGGAATCTTCTCCGGTCCTGCTATTTCTCGC
ATCAACAACGCATGCTTTGAGGCAGTAGTAGTCACCAATACCATACCTCAGGAGGACAAG
ATGAAGCATTGCTCCAAAATACAGGTGATTGACATCTCTATGATCCTTGCAGAAGCCATC
AGGAGAACTCACAATGGAGAATCCGTTTCTTACCTATTCAGCCATGTCCCTTTATAA

Enzyme 83 GenBank Gene ID

AL137787

Enzyme 83 GeneCard ID

PRPS1

Enzyme 83 GenAtlas ID

PRPS1

Enzyme 83 HGNC ID

HGNC:9462

Enzyme 83 Chromosome Location

Not Available

Enzyme 83 Locus

Not Available

Enzyme 83 SNPs

SNPJam Report Link Image

Enzyme 83 General References

Roessler BJ, Bell G, Heidler S, Seino S, Becker M, Palella TD: Cloning of two distinct copies of human phosphoribosylpyrophosphate synthetase cDNA. Nucleic Acids Res. 1990 Jan 11;18(1):193. [PubMed ]
Sonoda T, Taira M, Ishijima S, Ishizuka T, Iizasa T, Tatibana M: Complete nucleotide sequence of human phosphoribosyl pyrophosphate synthetase subunit I (PRS I) cDNA and a comparison with human and rat PRPS gene families. J Biochem (Tokyo). 1991 Feb;109(2):361-4. [PubMed ]
Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Ishizuka T, Iizasa T, Taira M, Ishijima S, Sonoda T, Shimada H, Nagatake N, Tatibana M: Promoter regions of the human X-linked housekeeping genes PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and II isoforms. Biochim Biophys Acta. 1992 Mar 24;1130(2):139-48. [PubMed ]
Li S, Lu Y, Peng B, Ding J: Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site. Biochem J. 2007 Jan 1;401(1):39-47. [PubMed ]
Becker MA, Smith PR, Taylor W, Mustafi R, Switzer RL: The genetic and functional basis of purine nucleotide feedback-resistant phosphoribosylpyrophosphate synthetase superactivity. J Clin Invest. 1995 Nov;96(5):2133-41. [PubMed ]
Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
de Brouwer AP, Williams KL, Duley JA, van Kuilenburg AB, Nabuurs SB, Egmont-Petersen M, Lugtenberg D, Zoetekouw L, Banning MJ, Roeffen M, Hamel BC, Weaving L, Ouvrier RA, Donald JA, Wevers RA, Christodoulou J, van Bokhoven H: Arts syndrome is caused by loss-of-function mutations in PRPS1. Am J Hum Genet. 2007 Sep;81(3):507-18. Epub 2007 Aug 3. [PubMed ]
Kim HJ, Sohn KM, Shy ME, Krajewski KM, Hwang M, Park JH, Jang SY, Won HH, Choi BO, Hong SH, Kim BJ, Suh YL, Ki CS, Lee SY, Kim SH, Kim JW: Mutations in PRPS1, which encodes the phosphoribosyl pyrophosphate synthetase enzyme critical for nucleotide biosynthesis, cause hereditary peripheral neuropathy with hearing loss and optic neuropathy (cmtx5). Am J Hum Genet. 2007 Sep;81(3):552-8. Epub 2007 Jun 29. [PubMed ]
Liu X, Han D, Li J, Han B, Ouyang X, Cheng J, Li X, Jin Z, Wang Y, Bitner-Glindzicz M, Kong X, Xu H, Kantardzhieva A, Eavey RD, Seidman CE, Seidman JG, Du LL, Chen ZY, Dai P, Teng M, Yan D, Yuan H: Loss-of-function mutations in the PRPS1 gene cause a type of nonsyndromic X-linked sensorineural deafness, DFN2. Am J Hum Genet. 2010 Jan;86(1):65-71. [PubMed ]

Enzyme 83 Metabolite References

Not Available

Enzyme 84 [top]

Enzyme 84 ID

5901

Enzyme 84 Name

Seryl-tRNA synthetase, mitochondrial

Enzyme 84 Synonyms

SerRSmt
Serine--tRNA ligase
SerRS
Seryl-tRNA(Ser/Sec) synthetase

Enzyme 84 Gene Name

SARS2

Enzyme 84 Protein Sequence

>Seryl-tRNA synthetase, mitochondrial

MAASMARRLWPLLTRRGFRPRGGCISNDSPRRSFTTEKRNRNLLYEYAREGYSALPQLDI
ERFCACPEEAAHALELRKGELRSADLPAIISTWQELRQLQEQIRSLEEEKAAVTEAVRAL
LANQDSGEVQQDPKYQGLRARGREIRKELVHLYPREAQLEEQFYLQALKLPNQTHPDVPV
GDESQARVLHMVGDKPVFSFQPRGHLEIGEKLDIIRQKRLSHVSGHRSYYLRGAGALLQH
GLVNFTFNKLLRRGFTPMTVPDLLRGAVFEGCGMTPNANPSQIYNIDPARFKDLNLAGTA
EVGLAGYFMDHTVAFRDLPVRMVCSSTCYRAETNTGQEPRGLYRVHHFTKVEMFGVTGPG
LEQSSQLLEEFLSLQMEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRFGEVT
SASNCTDFQSRRLHIMFQTEAGELQFAHTVNATACAVPRLLIALLESNQQKDGSVLVPPA
LQSYLGTDRITAPTHVPLQYIGPNQPRKPGLPGQPAVS

Enzyme 84 Number of Residues

518

Enzyme 84 Molecular Weight

58282.1

Enzyme 84 Theoretical pI

8.22

Enzyme 84 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding serine-tRNA ligase activity
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process seryl-tRNA aminoacylation tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 84 General Function

Involved in nucleotide binding

Enzyme 84 Specific Function

Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)

Enzyme 84 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Glycine, Serine and Threonine Metabolism (map00260 )

Enzyme 84 Reactions

ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer [RN:R03662]

Enzyme 84 Pfam Domain Function

tRNA-synt_2b (PF00587 )

Enzyme 84 Signals

None

Enzyme 84 Transmembrane Regions

None

Enzyme 84 Essentiality

Not Available

Enzyme 84 GenBank ID Protein

9188535

Enzyme 84 UniProtKB/Swiss-Prot ID

Q9NP81

Enzyme 84 UniProtKB/Swiss-Prot Entry Name

SYSM_HUMAN Link Image

Enzyme 84 PDB ID

Not Available

Enzyme 84 Cellular Location

Not Available

Enzyme 84 Gene Sequence

>1557 bp

ATGGCTGCGTCCATGGCGCGGCGCTTGTGGCCTTTGCTGACTCGTCGGGGGTTCCGGCCC
CGGGGAGGCTGCATCTCCAACGATAGTCCAAGGAGAAGTTTCACTACAGAGAAACGAAAC
CGGAACCTCCTGTACGAGTATGCGCGCGAGGGCTACAGCGCACTCCCTCAGCTGGACATA
GAGCGGTTCTGCGCATGCCCAGAAGAGGCCGCACACGCCCTGGAGCTCCGCAAGGGGGAG
CTGCGCTCGGCGGACCTGCCCGCGATCATCTCGACATGGCAGGAGCTGAGGCAGCTGCAG
GAGCAGATCCGGAGCCTGGAGGAAGAGAAGGCAGCTGTGACTGAGGCAGTGCGGGCCCTG
CTGGCAAACCAGGACAGTGGTGAAGTGCAGCAGGACCCCAAGTACCAGGGTCTGCGGGCA
CGTGGCCGGGAGATCCGGAAGGAGCTTGTTCACCTGTACCCCAGGGAGGCCCAGCTTGAG
GAGCAGTTCTACCTGCAGGCGCTGAAGCTGCCCAACCAGACCCACCCAGACGTGCCCGTC
GGGGATGAGAGCCAGGCTCGAGTGCTCCACATGGTCGGAGACAAGCCAGTTTTCTCCTTC
CAACCTCGGGGCCACCTGGAAATTGGCGAGAAACTCGACATCATCCGTCAGAAGCGCCTG
TCCCACGTGTCTGGCCACCGGTCCTATTACCTGCGCGGGGCTGGAGCCCTCCTGCAGCAC
GGCCTGGTCAACTTCACATTCAACAAGCTTCTCCGCCGGGGCTTCACCCCCATGACGGTG
CCAGACCTTCTCCGCGGAGCAGTGTTTGAAGGCTGTGGGATGACACCAAATGCCAACCCA
TCCCAAATTTACAACATCGACCCTGCCCGCTTCAAAGATCTCAACCTGGCTGGAACAGCG
GAGGTGGGGCTTGCAGGCTACTTCATGGACCACACCGTGGCCTTCAGGGACCTGCCAGTC
AGGATGGTTTGCTCCAGCACCTGCTACCGGGCAGAGACAAACACGGGACAGGAACCCCGG
GGGCTGTATCGAGTACACCACTTCACCAAGGTGGAGATGTTTGGGGTGACAGGCCCTGGG
CTGGAGCAGAGCTCACAGCTGCTGGAGGAGTTCCTGTCCCTTCAGATGGAGATCTTGACA
GAGCTGGGCTTGCACTTCCGGGTCCTGGATATGCCCACCCAAGAACTGGGCCTCCCCGCC
TACCGCAAGTTTGACATTGAGGCCTGGATGCCAGGCCGAGGCCGCTTTGGAGAGGTCACC
AGTGCTTCCAACTGCACAGACTTCCAGAGCCGCCGCCTCCACATCATGTTCCAGACCGAG
GCTGGGGAGCTGCAGTTTGCCCACACGGTGAACGCCACCGCCTGTGCTGTCCCCCGCCTT
CTCATCGCGCTCCTGGAGAGTAACCAGCAGAAGGACGGCTCAGTGCTCGTGCCCCCTGCC
CTCCAGTCCTACCTCGGCACTGATCGGATCACAGCCCCTACCCACGTGCCTCTCCAGTAC
ATCGGCCCCAACCAGCCCCGGAAGCCTGGGCTGCCTGGCCAGCCTGCTGTAAGCTAA

Enzyme 84 GenBank Gene ID

AB029948

Enzyme 84 GeneCard ID

SARS2

Enzyme 84 GenAtlas ID

SARS2

Enzyme 84 HGNC ID

HGNC:17697 Link Image

Enzyme 84 Chromosome Location

Enzyme 84 Locus

19q13.2

Enzyme 84 SNPs

SNPJam Report Link Image

Enzyme 84 General References

Yokogawa T, Shimada N, Takeuchi N, Benkowski L, Suzuki T, Omori A, Ueda T, Nishikawa K, Spremulli LL, Watanabe K: Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase. J Biol Chem. 2000 Jun 30;275(26):19913-20. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 84 Metabolite References

Not Available

Enzyme 85 [top]

Enzyme 85 ID

5902

Enzyme 85 Name

High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B

Enzyme 85 Synonyms

HsPDE8B
Cell proliferation-inducing gene 22 protein

Enzyme 85 Gene Name

PDE8B

Enzyme 85 Protein Sequence

>High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B

MGCAPSIHVSQSGVIYCRDSDESSSPRQTTSVSQGPAAPLPGLFVQTDAADAIPPSRASG
PPSVARVRRARTELGSGSSAGSAAPAATTSRGRRRHCCSSAEAETQTCYTSVKQVSSAEV
RIGPMRLTQDPIQVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEII
VIDHRQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASVLPLLHAGFNRRFME
NSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFER
MMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVK
ITPVIGQGGKIRHFVSLKKLCCTTDNNKQIHKIHRDSGDNSQTEPHSFRYKNRRKESIDV
KSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLE
ILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHQSHSHLAMPITI
NDVPPCISQLLDNEESWDFNIFELEAITHKRPLVYLGLKVFSRFGVCEFLNCSETTLRAW
FQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHP
GRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAI
IDMVLATEMTKHFEHVNKFVNSINKPMAAEIEGSDCECNPAGKNFPENQILIKRMMIKCA
DVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYF
ITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKSLRLPSDS

Enzyme 85 Number of Residues

885

Enzyme 85 Molecular Weight

98977.9

Enzyme 85 Theoretical pI

6.81

Enzyme 85 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds molecular transducer activity phosphoric diester hydrolase activity phosphoric ester hydrolase activity signal transducer activity two-component response regulator activity
Process
biological regulation regulation of biological process regulation of cellular process regulation of gene expression regulation of macromolecule metabolic process regulation of metabolic process regulation of transcription regulation of transcription, DNA-dependent signal transduction signal transmission signaling process two-component signal transduction system (phosphorelay)
Component
—

Enzyme 85 General Function

Involved in catalytic activity

Enzyme 85 Specific Function

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland

Enzyme 85 Pathways

Purine Metabolism (map00230 )

Enzyme 85 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 85 Pfam Domain Function

PAS (PF00989 )
PDE8 (PF08629 )
PDEase_I (PF00233 )
Response_reg (PF00072 )

Enzyme 85 Signals

None

Enzyme 85 Transmembrane Regions

None

Enzyme 85 Essentiality

Not Available

Enzyme 85 GenBank ID Protein

27372873

Enzyme 85 UniProtKB/Swiss-Prot ID

O95263

Enzyme 85 UniProtKB/Swiss-Prot Entry Name

PDE8B_HUMAN Link Image

Enzyme 85 PDB ID

Not Available

Enzyme 85 Cellular Location

Not Available

Enzyme 85 Gene Sequence

>2658 bp

ATGGGCTGCGCCCCCAGCATCCATGTCTCGCAGAGCGGCGTGATCTACTGCCGGGACTCG
GACGAGTCCAGCTCGCCCCGCCAGACCACCAGCGTGTCGCAGGGCCCGGCGGCACCCCTG
CCCGGCCTCTTCGTCCAGACCGACGCCGCCGACGCCATCCCCCCGAGCCGCGCGTCGGGA
CCCCCCAGCGTAGCCCGCGTCCGCAGGGCCCGCACCGAGCTGGGCAGCGGTAGCAGCGCG
GGTTCCGCAGCCCCCGCCGCGACCACCAGCAGGGGCCGGAGGCGCCACTGCTGCAGCAGC
GCCGAGGCCGAGACTCAGACCTGCTACACCAGCGTGAAGCAGGTGTCTTCTGCGGAGGTG
CGCATCGGGCCCATGAGACTGACGCAGGACCCTATTCAGGTTTTGCTGATCTTTGCAAAG
GAAGATAGTCAGAGCGATGGCTTCTGGTGGGCCTGCGACAGAGCTGGTTATAGATGCAAT
ATTGCTCGGACTCCAGAGTCAGCCCTTGAATGCTTTCTTGATAAGCATCATGAAATTATT
GTAATTGATCATAGACAAACTCAGAACTTCGATGCAGAAGCAGTGTGCAGGTCGATCCGG
GCCACAAATCCCTCCGAGCACACGGTGATCCTCGCAGTGGTTTCGCGAGTATCGGATGAC
CATGAAGAGGCGTCAGTCCTTCCTCTTCTCCACGCAGGCTTCAACAGGAGATTTATGGAG
AATAGCAGCATAATTGCTTGCTATAATGAACTGATTCAAATAGAACATGGGGAAGTTCGC
TCCCAGTTCAAATTACGGGCCTGTAATTCAGTGTTTACAGCATTAGATCACTGTCATGAA
GCCATAGAAATAACAAGCGATGACCACGTGATTCAGTATGTCAACCCAGCCTTCGAAAGG
ATGATGGGCTACCACAAAGGTGAGCTCCTGGGAAAAGAACTCGCTGATCTGCCCAAAAGC
GATAAGAACCGGGCAGACCTTCTCGACACCATCAATACATGCATCAAGAAGGGAAAGGAG
TGGCAGGGGGTTTACTATGCCAGACGGAAATCCGGGGACAGCATCCAACAGCACGTGAAG
ATCACCCCAGTGATTGGCCAAGGAGGGAAAATTAGGCATTTTGTCTCGCTCAAGAAACTG
TGTTGTACCACTGACAATAATAAGCAGATTCACAAGATTCATCGTGATTCAGGAGACAAT
TCTCAGACAGAGCCTCATTCATTCAGATATAAGAACAGGAGGAAAGAGTCCATTGACGTG
AAATCGATATCATCTCGAGGCAGTGATGCACCAAGCCTGCAGAATCGTCGCTATCCGTCC
ATGGCGAGGATCCACTCCATGACCATCGAGGCTCCCATCACAAAGGTTATAAATATAATC
AATGCAGCCCAAGAAAACAGCCCAGTCACAGTAGCGGAAGCCTTGGACAGAGTTCTAGAG
ATTTTACGGACCACAGAACTGTACTCCCCTCAGCTGGGTACCAAAGATGAAGATCCCCAC
ACCAGTGATCTTGTTGGAGGCCTGATGACTGACGGCTTGAGAAGACTGTCAGGAAACGAG
TATGTGTTTACTAAGAATGTGCACCAGAGTCACAGTCACCTTGCAATGCCAATAACCATC
AATGATGTTCCCCCTTGTATCTCTCAATTACTTGATAATGAGGAGAGTTGGGACTTCAAC
ATCTTTGAATTGGAAGCCATTACGCATAAAAGGCCATTGGTTTATCTGGGCTTAAAGGTC
TTCTCTCGGTTTGGAGTATGTGAGTTTTTAAACTGTTCTGAAACCACTCTTCGGGCCTGG
TTCCAAGTGATCGAAGCCAACTACCACTCTTCCAATGCCTACCACAACTCCACCCATGCT
GCCGACGTCCTGCACGCCACCGCTTTCTTTCTTGGAAAGGAAAGAGTAAAGGGAAGCCTC
GATCAGTTGGATGAGGTGGCAGCCCTCATTGCTGCCACAGTCCATGACGTGGATCACCCG
GGAAGGACCAACTCTTTCCTCTGCAATGCAGGCAGTGAGCTTGCTGTGCTCTACAATGAC
ACTGCTGTTCTGGAGAGTCACCACACCGCCCTGGCCTTCCAGCTCACGGTCAAGGACACC
AAATGCAACATTTTCAAGAATATTGACAGGAACCATTATCGAACGCTGCGCCAGGCTATT
ATTGACATGGTTTTGGCAACAGAGATGACAAAACACTTTGAACATGTGAATAAGTTTGTG
AACAGCATCAACAAGCCAATGGCAGCTGAGATTGAAGGCAGCGACTGTGAATGCAACCCT
GCTGGGAAGAACTTCCCTGAAAACCAAATCCTGATCAAACGCATGATGATTAAGTGTGCT
GACGTGGCCAACCCATGCCGCCCCTTGGACCTGTGCATTGAATGGGCTGGGAGGATCTCT
GAGGAGTATTTTGCACAGACTGATGAAGAGAAGAGACAGGGACTACCTGTGGTGATGCCA
GTGTTTGACCGGAATACCTGTAGCATCCCCAAGTCTCAGATCTCTTTCATTGACTACTTC
ATAACAGACATGTTTGATGCTTGGGATGCCTTTGCACATCTGCCAGCCCTGATGCAACAT
TTGGCTGACAACTACAAACACTGGAAGACACTAGATGACCTAAAGTGCAAAAGTTTGAGG
CTTCCATCTGACAGCTAA

Enzyme 85 GenBank Gene ID

AB085824

Enzyme 85 GeneCard ID

PDE8B

Enzyme 85 GenAtlas ID

PDE8B

Enzyme 85 HGNC ID

HGNC:8794

Enzyme 85 Chromosome Location

Enzyme 85 Locus

5q13.3

Enzyme 85 SNPs

SNPJam Report Link Image

Enzyme 85 General References

Hayashi M, Shimada Y, Nishimura Y, Hama T, Tanaka T: Genomic organization, chromosomal localization, and alternative splicing of the human phosphodiesterase 8B gene. Biochem Biophys Res Commun. 2002 Oct 11;297(5):1253-8. [PubMed ]
Gamanuma M, Yuasa K, Sasaki T, Sakurai N, Kotera J, Omori K: Comparison of enzymatic characterization and gene organization of cyclic nucleotide phosphodiesterase 8 family in humans. Cell Signal. 2003 Jun;15(6):565-74. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Hayashi M, Matsushima K, Ohashi H, Tsunoda H, Murase S, Kawarada Y, Tanaka T: Molecular cloning and characterization of human PDE8B, a novel thyroid-specific isozyme of 3',5'-cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 1998 Sep 29;250(3):751-6. [PubMed ]
Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]

Enzyme 85 Metabolite References

Not Available

Enzyme 86 [top]

Enzyme 86 ID

5903

Enzyme 86 Name

cAMP-specific 3',5'-cyclic phosphodiesterase 4C

Enzyme 86 Synonyms

DPDE1
PDE21

Enzyme 86 Gene Name

PDE4C

Enzyme 86 Protein Sequence

>cAMP-specific 3',5'-cyclic phosphodiesterase 4C

MENLGVGEGAEACSRLSRSRGRHSMTRAPKHLWRQPRRPIRIQQRFYSDPDKSAGCRERD
LSPRPELRKSRLSWPVSSCRRFDLENGLSCGRRALDPQSSPGLGRIMQAPVPHSQRRESF
LYRSDSDYELSPKAMSRNSSVASDLHGEDMIVTPFAQVLASLRTVRSNVAALARQQCLGA
AKQGPVGNPSSSNQLPPAEDTGQKLALETLDELDWCLDQLETLQTRHSVGEMASNKFKRI
LNRELTHLSETSRSGNQVSEYISRTFLDQQTEVELPKVTAEEAPQPMSRISGLHGLCHSA
SLSSATVPRFGVQTDQEEQLAKELEDTNKWGLDVFKVAELSGNRPLTAIIFSIFQERDLL
KTFQIPADTLATYLLMLEGHYHANVAYHNSLHAADVAQSTHVLLATPALEAVFTDLEILA
ALFASAIHDVDHPGVSNQFLINTNSELALMYNDASVLENHHLAVGFKLLQAENCDIFQNL
SAKQRLSLRRMVIDMVLATDMSKHMNLLADLKTMVETKKVTSLGVLLLDNYSDRIQVLQN
LVHCADLSNPTKPLPLYRQWTDRIMAEFFQQGDRERESGLDISPMCDKHTASVEKSQVGF
IDYIAHPLWETWADLVHPDAQDLLDTLEDNREWYQSKIPRSPSDLTNPERDGPDRFQFEL
TLEEAEEEDEEEEEEGEETALAKEALELPDTELLSPEAGPDPGDLPLDNQRT

Enzyme 86 Number of Residues

712

Enzyme 86 Molecular Weight

79900.8

Enzyme 86 Theoretical pI

4.84

Enzyme 86 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 86 General Function

Involved in catalytic activity

Enzyme 86 Specific Function

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes

Enzyme 86 Pathways

Purine Metabolism (map00230 )

Enzyme 86 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 86 Pfam Domain Function

PDEase_I (PF00233 )

Enzyme 86 Signals

None

Enzyme 86 Transmembrane Regions

None

Enzyme 86 Essentiality

Not Available

Enzyme 86 GenBank ID Protein

115529445

Enzyme 86 UniProtKB/Swiss-Prot ID

Q08493

Enzyme 86 UniProtKB/Swiss-Prot Entry Name

PDE4C_HUMAN Link Image

Enzyme 86 PDB ID

Not Available

Enzyme 86 Cellular Location

Not Available

Enzyme 86 Gene Sequence

>2139 bp

ATGGAGAACCTGGGGGTCGGCGAAGGGGCAGAGGCTTGCAGCAGGTTGAGTCGCTCTCGC
GGCCGCCACAGCATGACCAGAGCCCCGAAGCACCTGTGGCGGCAACCCCGGCGCCCCATC
CGCATCCAACAGCGCTTCTATTCGGATCCGGACAAGTCCGCGGGCTGCCGCGAGAGGGAC
CTGAGCCCGCGGCCGGAGCTCAGGAAGTCGCGGCTCTCCTGGCCCGTTTCCTCCTGCAGG
CGCTTTGACCTGGAAAATGGGCTCTCGTGTGGGAGGAGGGCCCTGGACCCTCAGTCCAGC
CCTGGCCTGGGCCGGATTATGCAGGCTCCAGTCCCGCACAGCCAGCGGCGCGAGTCCTTC
CTGTACCGCTCAGATAGCGACTATGAACTCTCGCCCAAGGCCATGTCTCGGAACTCCTCT
GTGGCCAGCGACCTACATGGAGAGGACATGATTGTGACGCCCTTTGCCCAGGTCCTGGCC
AGTCTGCGGACCGTTCGGAGCAACGTGGCGGCCCTTGCCCGCCAGCAATGCCTAGGAGCA
GCCAAGCAGGGACCCGTCGGAAACCCTTCATCCAGCAATCAGCTCCCTCCTGCAGAGGAC
ACGGGGCAGAAGCTGGCATTGGAGACGCTAGACGAGCTGGACTGGTGCCTGGATCAGTTG
GAGACGCTGCAGACCCGGCACTCGGTGGGGGAGATGGCCTCCAACAAGTTCAAGCGGATC
CTGAACCGGGAGTTGACCCACCTGTCCGAAACCAGCCGCTCCGGGAACCAGGTGTCCGAG
TACATCTCCCGGACCTTCCTGGACCAGCAGACCGAGGTGGAGCTGCCCAAGGTGACCGCT
GAGGAGGCCCCACAGCCCATGTCCCGGATCAGTGGCCTACATGGGCTCTGCCACAGTGCC
AGCCTCTCCTCAGCCACTGTCCCACGCTTTGGGGTCCAGACTGACCAGGAGGAGCAACTG
GCCAAGGAGCTAGAAGACACCAACAAGTGGGGACTTGATGTGTTCAAGGTGGCGGAGCTA
AGTGGGAACCGGCCCCTCACAGCTATCATATTCAGCATTTTTCAGGAGCGGGACCTGCTG
AAGACATTCCAGATCCCAGCAGACACACTGGCCACCTACCTGCTGATGCTGGAAGGTCAC
TACCACGCCAATGTGGCCTACCACAACAGCCTACATGCCGCCGACGTGGCCCAGTCCACG
CATGTGCTGCTGGCTACGCCCGCCCTCGAGGCTGTGTTCACAGACTTGGAAATCCTGGCT
GCCCTCTTTGCAAGCGCCATCCACGACGTGGACCATCCTGGGGTCTCCAACCAGTTTCTG
ATTAACACCAACTCAGAGCTGGCGCTTATGTACAACGACGCCTCGGTGCTGGAGAACCAT
CACCTGGCTGTGGGCTTCAAGCTGCTGCAGGCAGAGAACTGCGATATCTTCCAGAACCTC
AGCGCCAAGCAGCGACTGAGTCTGCGCAGGATGGTCATTGACATGGTGCTGGCCACAGAC
ATGTCCAAACACATGAACCTCCTGGCCGACCTCAAGACCATGGTGGAGACCAAGAAGGTG
ACAAGCCTCGGTGTCCTCCTCCTGGACAACTATTCCGACCGAATCCAGGTCTTGCAGAAC
CTGGTGCACTGTGCTGATCTGAGCAACCCCACCAAGCCGCTGCCCCTGTACCGCCAGTGG
ACGGACCGCATCATGGCCGAGTTCTTCCAGCAGGGAGACCGCGAGCGTGAGTCGGGCCTG
GACATCAGTCCCATGTGTGACAAGCATACGGCCTCAGTGGAGAAGTCCCAGGTGGGTTTC
ATTGACTACATTGCTCACCCACTGTGGGAGACTTGGGCTGACCTGGTCCACCCAGATGCA
CAGGACCTGCTGGACACGCTGGAGGACAATCGAGAGTGGTACCAGAGCAAGATCCCCCGA
AGTCCCTCAGACCTCACCAACCCCGAGCGGGACGGGCCTGACAGATTCCAGTTTGAACTG
ACTCTGGAGGAGGCAGAGGAAGAGGATGAGGAGGAAGAAGAGGAGGGGGAAGAGACAGCT
TTAGCCAAAGAGGCCTTGGAGTTGCCTGACACTGAACTCCTGTCCCCTGAAGCCGGCCCA
GACCCTGGGGACTTACCCCTCGACAACCAGAGGACTTAG

Enzyme 86 GenBank Gene ID

NM_000923.3 Link Image

Enzyme 86 GeneCard ID

PDE4C

Enzyme 86 GenAtlas ID

PDE4C

Enzyme 86 HGNC ID

HGNC:8782

Enzyme 86 Chromosome Location

Enzyme 86 Locus

19p13.11

Enzyme 86 SNPs

SNPJam Report Link Image

Enzyme 86 General References

Engels P, Sullivan M, Muller T, Lubbert H: Molecular cloning and functional expression in yeast of a human cAMP-specific phosphodiesterase subtype (PDE IV-C). FEBS Lett. 1995 Jan 30;358(3):305-10. [PubMed ]
Sullivan M, Olsen AS, Houslay MD: Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND. Cell Signal. 1999 Oct;11(10):735-42. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed ]
Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed ]
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed ]

Enzyme 86 Metabolite References

Not Available

Enzyme 87 [top]

Enzyme 87 ID

5904

Enzyme 87 Name

Ribose-phosphate pyrophosphokinase 2

Enzyme 87 Synonyms

PPRibP
Phosphoribosyl pyrophosphate synthase II
PRS-II

Enzyme 87 Gene Name

PRPS2

Enzyme 87 Protein Sequence

>Ribose-phosphate pyrophosphokinase 2

MPNIVLFSGSSHQDLSQRVADRLGLELGKVVTKKFSNQETSVEIGESVRGEDVYIIQSGC
GEINDNLMELLIMINACKIASSSRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPAVLQWIRENIAEWKNCIIVSPDAGGAKRVTS
IADRLNVEFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATKVYAILTHGIFSGPAISRINNAAFEAVVVTNTIPQEDKMKHCTKIQVIDISMILAEAI
RRTHNGESVSYLFSHVPL

Enzyme 87 Number of Residues

318

Enzyme 87 Molecular Weight

34768.8

Enzyme 87 Theoretical pI

6.60

Enzyme 87 GO Classification

Function
binding catalytic activity cation binding diphosphotransferase activity ion binding magnesium ion binding metal ion binding ribose phosphate diphosphokinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
biosynthetic process cellular biosynthetic process cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside metabolic process nucleoside monophosphate biosynthetic process nucleoside monophosphate metabolic process nucleoside phosphate metabolic process nucleotide biosynthetic process nucleotide metabolic process ribonucleoside monophosphate biosynthetic process
Component
—

Enzyme 87 General Function

Involved in magnesium ion binding

Enzyme 87 Specific Function

Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis

Enzyme 87 Pathways

Pentose Pathway (map00030 )
Purine Metabolism (map00230 )

Enzyme 87 Reactions

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate [RN:R01049]

Enzyme 87 Pfam Domain Function

Pribosyltran (PF00156 )

Enzyme 87 Signals

None

Enzyme 87 Transmembrane Regions

None

Enzyme 87 Essentiality

Not Available

Enzyme 87 GenBank ID Protein

4506129

Enzyme 87 UniProtKB/Swiss-Prot ID

P11908

Enzyme 87 UniProtKB/Swiss-Prot Entry Name

PRPS2_HUMAN Link Image

Enzyme 87 PDB ID

Not Available

Enzyme 87 Cellular Location

Not Available

Enzyme 87 Gene Sequence

>957 bp

ATGCCCAACATCGTGCTGTTCAGCGGCAGCTCGCATCAGGACCTGTCCCAGCGCGTGGCC
GACCGCCTGGGCCTGGAGCTGGGCAAGGTGGTCACGAAGAAGTTCAGCAACCAGGAGACC
AGCGTGGAGATTGGTGAAAGCGTGAGAGGGGAAGATGTCTACATCATCCAGAGCGGCTGC
GGGGAAATTAACGACAACCTGATGGAACTCCTCATCATGATCAATGCCTGCAAGATTGCG
TCATCATCCAGAGTAACTGCCGTGATCCCGTGTTTCCCATACGCCCGACAAGATAAAAAG
GACAAGAGTCGTGCCCCAATTTCTGCAAAACTTGTGGCCAATATGCTGTCGGTGGCTGGG
GCGGATCACATCATCACCATGGACCTGCATGCTTCTCAGATACAGGGATTCTTTGATATT
CCTGTGGATAATTTGTATGCGGAGCCCGCAGTCCTGCAGTGGATTCGGGAAAACATTGCC
GAGTGGAAGAACTGTATCATTGTTTCACCTGACGCAGGGGGAGCCAAAAGGGTTACATCA
ATTGCAGACAGGTTGAATGTGGAATTTGCTTTGATCCACAAAGAGAGGAAGAAGGCGAAT
GAAGTGGACCGGATGGTCCTGGTGGGCGACGTGAAGGACCGTGTGGCCATCCTCGTGGAT
GACATGGCTGACACTTGCGGCACCATCTGCCATGCTGCGGACAAGCTGCTGTCAGCTGGA
GCCACCAAAGTGTATGCTATCCTTACCCATGGGATCTTCTCTGGACCAGCTATTTCCAGA
ATAAATAATGCCGCCTTTGAGGCTGTTGTCGTCACAAACACAATTCCGCAAGAGGACAAA
ATGAAACACTGCACCAAGATTCAGGTCATTGACATTTCCATGATCTTGGCCGAAGCAATC
CGAAGGACACACAATGGGGAATCCGTGTCCTACCTGTTCAGCCATGTCCCGCTATAA

Enzyme 87 GenBank Gene ID

NM_002765.4 Link Image

Enzyme 87 GeneCard ID

PRPS2

Enzyme 87 GenAtlas ID

PRPS2

Enzyme 87 HGNC ID

HGNC:9465

Enzyme 87 Chromosome Location

Not Available

Enzyme 87 Locus

Not Available

Enzyme 87 SNPs

SNPJam Report Link Image

Enzyme 87 General References

Iizasa T, Taira M, Shimada H, Ishijima S, Tatibana M: Molecular cloning and sequencing of human cDNA for phosphoribosyl pyrophosphate synthetase subunit II. FEBS Lett. 1989 Feb 13;244(1):47-50. [PubMed ]
Iizasa T, Taira M, Shimada H, Tatibana M: Deduced amino acid sequence from human phosphoribosylpyrophosphate synthetase subunit II cDNA. Adv Exp Med Biol. 1989;253A:519-23. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Ishizuka T, Iizasa T, Taira M, Ishijima S, Sonoda T, Shimada H, Nagatake N, Tatibana M: Promoter regions of the human X-linked housekeeping genes PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and II isoforms. Biochim Biophys Acta. 1992 Mar 24;1130(2):139-48. [PubMed ]

Enzyme 87 Metabolite References

Not Available

Enzyme 88 [top]

Enzyme 88 ID

5907

Enzyme 88 Name

SUMO-conjugating enzyme UBC9

Enzyme 88 Synonyms

SUMO-protein ligase
Ubiquitin carrier protein 9
Ubiquitin carrier protein I
Ubiquitin-conjugating enzyme E2 I
Ubiquitin-protein ligase I
p18

Enzyme 88 Gene Name

UBE2I

Enzyme 88 Protein Sequence

>SUMO-conjugating enzyme UBC9

MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKL
RMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELL
NEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS

Enzyme 88 Number of Residues

158

Enzyme 88 Molecular Weight

18006.7

Enzyme 88 Theoretical pI

8.90

Enzyme 88 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 88 General Function

Involved in acid-amino acid ligase activity

Enzyme 88 Specific Function

Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation

Enzyme 88 Pathways

Not Available

Enzyme 88 Reactions

Not Available

Enzyme 88 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 88 Signals

None

Enzyme 88 Transmembrane Regions

None

Enzyme 88 Essentiality

Not Available

Enzyme 88 GenBank ID Protein

4507785

Enzyme 88 UniProtKB/Swiss-Prot ID

P63279

Enzyme 88 UniProtKB/Swiss-Prot Entry Name

UBC9_HUMAN Link Image

Enzyme 88 PDB ID

1KPS

Enzyme 88 PDB File

Show

Enzyme 88 3D Structure

Enzyme 88 Cellular Location

Not Available

Enzyme 88 Gene Sequence

>477 bp

ATGTCGGGGATCGCCCTCAGCAGACTCGCCCAGGAGAGGAAAGCATGGAGGAAAGACCAC
CCATTTGGTTTCGTGGCTGTCCCAACAAAAAATCCCGATGGCACGATGAACCTCATGAAC
TGGGAGTGCGCCATTCCAGGAAAGAAAGGGACTCCGTGGGAAGGAGGCTTGTTTAAACTA
CGGATGCTTTTCAAAGATGATTATCCATCTTCGCCACCAAAATGTAAATTCGAACCACCA
TTATTTCACCCGAATGTGTACCCTTCGGGGACAGTGTGCCTGTCCATCTTAGAGGAGGAC
AAGGACTGGAGGCCAGCCATCACAATCAAACAGATCCTATTAGGAATACAGGAACTTCTA
AATGAACCAAATATCCAAGACCCAGCTCAAGCAGAGGCCTACACGATTTACTGCCAAAAC
AGAGTGGAGTACGAGAAAAGGGTCCGAGCACAAGCCAAGAAGTTTGCGCCCTCATAA

Enzyme 88 GenBank Gene ID

NM_003345.3 Link Image

Enzyme 88 GeneCard ID

UBE2I

Enzyme 88 GenAtlas ID

UBE2I

Enzyme 88 HGNC ID

HGNC:12485 Link Image

Enzyme 88 Chromosome Location

Enzyme 88 Locus

16p13.3

Enzyme 88 SNPs

SNPJam Report Link Image

Enzyme 88 General References

Yasugi T, Howley PM: Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9. Nucleic Acids Res. 1996 Jun 1;24(11):2005-10. [PubMed ]
Tachibana M, Iwata N, Watanabe A, Nobukuni Y, Ploplis B, Kajigaya S: Assignment of the gene for a ubiquitin-conjugating enzyme (UBE2I) to human chromosome band 16p13.3 by in situ hybridization. Cytogenet Cell Genet. 1996;75(4):222-3. [PubMed ]
Watanabe TK, Fujiwara T, Kawai A, Shimizu F, Takami S, Hirano H, Okuno S, Ozaki K, Takeda S, Shimada Y, Nagata M, Takaichi A, Takahashi E, Nakamura Y, Shin S: Cloning, expression, and mapping of UBE2I, a novel gene encoding a human homologue of yeast ubiquitin-conjugating enzymes which are critical for regulating the cell cycle. Cytogenet Cell Genet. 1996;72(1):86-9. [PubMed ]
Masson M, Menissier-de Murcia J, Mattei MG, de Murcia G, Niedergang CP: Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin conjugating enzyme: hUbc9. Gene. 1997 May 6;190(2):287-96. [PubMed ]
Kovalenko OV, Plug AW, Haaf T, Gonda DK, Ashley T, Ward DC, Radding CM, Golub EI: Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes. Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):2958-63. [PubMed ]
Jiang W, Koltin Y: Two-hybrid interaction of a human UBC9 homolog with centromere proteins of Saccharomyces cerevisiae. Mol Gen Genet. 1996 May 23;251(2):153-60. [PubMed ]
Wang ZY, Qiu QQ, Seufert W, Taguchi T, Testa JR, Whitmore SA, Callen DF, Welsh D, Shenk T, Deuel TF: Molecular cloning of the cDNA and chromosome localization of the gene for human ubiquitin-conjugating enzyme 9. J Biol Chem. 1996 Oct 4;271(40):24811-6. [PubMed ]
Hahn SL, Wasylyk B, Criqui-Filipe P: Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme. Oncogene. 1997 Sep 18;15(12):1489-95. [PubMed ]
Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed ]
Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Hateboer G, Hijmans EM, Nooij JB, Schlenker S, Jentsch S, Bernards R: mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect. J Biol Chem. 1996 Oct 18;271(42):25906-11. [PubMed ]
Hu G, Zhang S, Vidal M, Baer JL, Xu T, Fearon ER: Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway. Genes Dev. 1997 Oct 15;11(20):2701-14. [PubMed ]
Poukka H, Aarnisalo P, Karvonen U, Palvimo JJ, Janne OA: Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription. J Biol Chem. 1999 Jul 2;274(27):19441-6. [PubMed ]
Tatham MH, Jaffray E, Vaughan OA, Desterro JM, Botting CH, Naismith JH, Hay RT: Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J Biol Chem. 2001 Sep 21;276(38):35368-74. Epub 2001 Jul 12. [PubMed ]
Eloranta JJ, Hurst HC: Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo. J Biol Chem. 2002 Aug 23;277(34):30798-804. Epub 2002 Jun 18. [PubMed ]
Tatham MH, Chen Y, Hay RT: Role of two residues proximal to the active site of Ubc9 in substrate recognition by the Ubc9.SUMO-1 thiolester complex. Biochemistry. 2003 Mar 25;42(11):3168-79. [PubMed ]
Tatham MH, Kim S, Yu B, Jaffray E, Song J, Zheng J, Rodriguez MS, Hay RT, Chen Y: Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation. Biochemistry. 2003 Aug 26;42(33):9959-69. [PubMed ]
Pichler A, Knipscheer P, Saitoh H, Sixma TK, Melchior F: The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type. Nat Struct Mol Biol. 2004 Oct;11(10):984-91. Epub 2004 Sep 19. [PubMed ]
Tatham MH, Kim S, Jaffray E, Song J, Chen Y, Hay RT: Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. Nat Struct Mol Biol. 2005 Jan;12(1):67-74. Epub 2004 Dec 19. [PubMed ]
Li T, Santockyte R, Shen RF, Tekle E, Wang G, Yang DC, Chock PB: A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers. Arch Biochem Biophys. 2006 Sep 1;453(1):70-4. Epub 2006 Mar 20. [PubMed ]
Pan X, Li H, Zhang P, Jin B, Man J, Tian L, Su G, Zhao J, Li W, Liu H, Gong W, Zhou T, Zhang X: Ubc9 interacts with SOX4 and represses its transcriptional activity. Biochem Biophys Res Commun. 2006 Jun 9;344(3):727-34. Epub 2006 Apr 17. [PubMed ]
Tomoiu A, Gravel A, Tanguay RM, Flamand L: Functional interaction between human herpesvirus 6 immediate-early 2 protein and ubiquitin-conjugating enzyme 9 in the absence of sumoylation. J Virol. 2006 Oct;80(20):10218-28. [PubMed ]
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Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed ]
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Enzyme 88 Metabolite References

Not Available

Enzyme 89 [top]

Enzyme 89 ID

5908

Enzyme 89 Name

cAMP-specific 3',5'-cyclic phosphodiesterase 4D

Enzyme 89 Synonyms

DPDE3
PDE43

Enzyme 89 Gene Name

PDE4D

Enzyme 89 Protein Sequence

>cAMP-specific 3',5'-cyclic phosphodiesterase 4D

MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPP
PPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRA
MDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQA
NFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNF
AALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSV
SEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRP
MSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPL
TVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLST
PALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGF
KLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVL
LLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMC
DKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAP
DDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPL
DEQVEEEAVGEEEESQPEACVIDDRSPDT

Enzyme 89 Number of Residues

809

Enzyme 89 Molecular Weight

91114.1

Enzyme 89 Theoretical pI

5.25

Enzyme 89 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 89 General Function

Involved in catalytic activity

Enzyme 89 Specific Function

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes

Enzyme 89 Pathways

Purine Metabolism (map00230 )

Enzyme 89 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 89 Pfam Domain Function

PDEase_I (PF00233 )

Enzyme 89 Signals

None

Enzyme 89 Transmembrane Regions

None

Enzyme 89 Essentiality

Not Available

Enzyme 89 GenBank ID Protein

157277988

Enzyme 89 UniProtKB/Swiss-Prot ID

Q08499

Enzyme 89 UniProtKB/Swiss-Prot Entry Name

PDE4D_HUMAN Link Image

Enzyme 89 PDB ID

1PTW

Enzyme 89 PDB File

Show

Enzyme 89 3D Structure

Enzyme 89 Cellular Location

Not Available

Enzyme 89 Gene Sequence

>2430 bp

ATGGAGGCAGAGGGCAGCAGCGCGCCGGCCCGGGCGGGCAGCGGAGAGGGCAGCGACAGC
GCCGGCGGGGCCACGCTCAAAGCCCCCAAGCATCTCTGGAGGCACGAGCAGCACCACCAG
TACCCGCTCCGGCAGCCCCAGTTCCGCCTCCTGCATCCCCATCACCACCTGCCCCCGCCG
CCGCCACCCTCGCCCCAGCCCCAGCCCCAGTGTCCGCTACAGCCGCCGCCGCCGCCCCCC
CTGCCGCCGCCCCCGCCGCCGCCCGGGGCTGCCCGCGGCCGCTACGCCTCGAGCGGGGCC
ACCGGCCGCGTCCGGCATCGCGGCTACTCGGACACCGAGCGCTACCTGTACTGTCGCGCC
ATGGACCGCACCTCCTACGCGGTGGAGACCGGCCACCGGCCCGGCCTGAAGAAATCCAGG
ATGTCCTGGCCCTCCTCGTTCCAGGGACTCAGGCGTTTTGATGTGGACAATGGCACATCT
GCGGGACGGAGTCCCTTGGATCCCATGACCAGCCCAGGATCCGGGCTAATTCTCCAAGCA
AATTTTGTCCACAGTCAACGACGGGAGTCCTTCCTGTATCGATCCGACAGCGATTATGAC
CTCTCTCCAAAGTCTATGTCCCGGAACTCCTCCATTGCCAGTGATATACACGGAGATGAC
TTGATTGTGACTCCATTTGCTCAGGTCTTGGCCAGTCTGCGAACTGTACGAAACAACTTT
GCTGCATTAACTAATTTGCAAGATCGAGCACCTAGCAAAAGATCACCCATGTGCAACCAA
CCATCCATCAACAAAGCCACCATAACAGAGGAGGCCTACCAGAAACTGGCCAGCGAGACC
CTGGAGGAGCTGGACTGGTGTCTGGACCAGCTAGAGACCCTACAGACCAGGCACTCCGTC
AGTGAGATGGCCTCCAACAAGTTTAAAAGGATGCTTAATCGGGAGCTCACCCATCTCTCT
GAAATGAGTCGGTCTGGAAATCAAGTGTCAGAGTTTATATCAAACACATTCTTAGATAAG
CAACATGAAGTGGAAATTCCTTCTCCAACTCAGAAGGAAAAGGAGAAAAAGAAAAGACCA
ATGTCTCAGATCAGTGGAGTCAAGAAATTGATGCACAGCTCTAGTCTGACTAATTCAAGT
ATCCCAAGGTTTGGAGTTAAAACTGAACAAGAAGATGTCCTTGCCAAGGAACTAGAAGAT
GTGAACAAATGGGGTCTTCATGTTTTCAGAATAGCAGAGTTGTCTGGTAACCGGCCCTTG
ACTGTTATCATGCACACCATTTTTCAGGAACGGGATTTATTAAAAACATTTAAAATTCCA
GTAGATACTTTAATTACATATCTTATGACTCTCGAAGACCATTACCATGCTGATGTGGCC
TATCACAACAATATCCATGCTGCAGATGTTGTCCAGTCTACTCATGTGCTATTATCTACA
CCTGCTTTGGAGGCTGTGTTTACAGATTTGGAGATTCTTGCAGCAATTTTTGCCAGTGCA
ATACATGATGTAGATCATCCTGGTGTGTCCAATCAATTTCTGATCAATACAAACTCTGAA
CTTGCCTTGATGTACAATGATTCCTCAGTCTTAGAGAACCATCATTTGGCTGTGGGCTTT
AAATTGCTTCAGGAAGAAAACTGTGACATTTTCCAGAATTTGACCAAAAAACAAAGACAA
TCTTTAAGGAAAATGGTCATTGACATCGTACTTGCAACAGATATGTCAAAACACATGAAT
CTACTGGCTGATTTGAAGACTATGGTTGAAACTAAGAAAGTGACAAGCTCTGGAGTTCTT
CTTCTTGATAATTATTCCGATAGGATTCAGGTTCTTCAGAATATGGTGCACTGTGCAGAT
CTGAGCAACCCAACAAAGCCTCTCCAGCTGTACCGCCAGTGGACGGACCGGATAATGGAG
GAGTTCTTCCGCCAAGGAGACCGAGAGAGGGAACGTGGCATGGAGATAAGCCCCATGTGT
GACAAGCACAATGCTTCCGTGGAAAAATCACAGGTGGGCTTCATAGACTATATTGTTCAT
CCCCTCTGGGAGACATGGGCAGACCTCGTCCACCCTGACGCCCAGGATATTTTGGACACT
TTGGAGGACAATCGTGAATGGTACCAGAGCACAATCCCTCAGAGCCCCTCTCCTGCACCT
GATGACCCAGAGGAGGGCCGGCAGGGTCAAACTGAGAAATTCCAGTTTGAACTAACTTTA
GAGGAAGATGGTGAGTCAGACACGGAAAAGGACAGTGGCAGTCAAGTGGAAGAAGACACT
AGCTGCAGTGACTCCAAGACTCTTTGTACTCAAGACTCAGAGTCTACTGAAATTCCCCTT
GATGAACAGGTTGAAGAGGAGGCAGTAGGGGAAGAAGAGGAAAGCCAGCCTGAAGCCTGT
GTCATAGATGATCGTTCTCCTGACACGTAA

Enzyme 89 GenBank Gene ID

NM_001104631.1 Link Image

Enzyme 89 GeneCard ID

PDE4D

Enzyme 89 GenAtlas ID

PDE4D

Enzyme 89 HGNC ID

HGNC:8783

Enzyme 89 Chromosome Location

Enzyme 89 Locus

5q12

Enzyme 89 SNPs

SNPJam Report Link Image

Enzyme 89 General References

Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed ]
Nemoz G, Zhang R, Sette C, Conti M: Identification of cyclic AMP-phosphodiesterase variants from the PDE4D gene expressed in human peripheral mononuclear cells. FEBS Lett. 1996 Apr 8;384(1):97-102. [PubMed ]
Baecker PA, Obernolte R, Bach C, Yee C, Shelton ER: Isolation of a cDNA encoding a human rolipram-sensitive cyclic AMP phosphodiesterase (PDE IVD). Gene. 1994 Jan 28;138(1-2):253-6. [PubMed ]
Bolger GB, Erdogan S, Jones RE, Loughney K, Scotland G, Hoffmann R, Wilkinson I, Farrell C, Houslay MD: Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene. Biochem J. 1997 Dec 1;328 ( Pt 2):539-48. [PubMed ]
Miro X, Casacuberta JM, Gutierrez-Lopez MD, de Landazuri MO, Puigdomenech P: Phosphodiesterases 4D and 7A splice variants in the response of HUVEC cells to TNF-alpha(1). Biochem Biophys Res Commun. 2000 Aug 2;274(2):415-21. [PubMed ]
Wang D, Deng C, Bugaj-Gaweda B, Kwan M, Gunwaldsen C, Leonard C, Xin X, Hu Y, Unterbeck A, De Vivo M: Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7. Cell Signal. 2003 Sep;15(9):883-91. [PubMed ]
Gretarsdottir S, Thorleifsson G, Reynisdottir ST, Manolescu A, Jonsdottir S, Jonsdottir T, Gudmundsdottir T, Bjarnadottir SM, Einarsson OB, Gudjonsdottir HM, Hawkins M, Gudmundsson G, Gudmundsdottir H, Andrason H, Gudmundsdottir AS, Sigurdardottir M, Chou TT, Nahmias J, Goss S, Sveinbjornsdottir S, Valdimarsson EM, Jakobsson F, Agnarsson U, Gudnason V, Thorgeirsson G, Fingerle J, Gurney M, Gudbjartsson D, Frigge ML, Kong A, Stefansson K, Gulcher JR: The gene encoding phosphodiesterase 4D confers risk of ischemic stroke. Nat Genet. 2003 Oct;35(2):131-8. Epub 2003 Sep 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Bolger GB, McCahill A, Yarwood SJ, Steele MR, Warwicker J, Houslay MD: Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5. BMC Biochem. 2002 Aug 23;3:24. [PubMed ]
Bolger GB, McCahill A, Huston E, Cheung YF, McSorley T, Baillie GS, Houslay MD: The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins. J Biol Chem. 2003 Dec 5;278(49):49230-8. Epub 2003 Sep 18. [PubMed ]
Richter W, Conti M: The oligomerization state determines regulatory properties and inhibitor sensitivity of type 4 cAMP-specific phosphodiesterases. J Biol Chem. 2004 Jul 16;279(29):30338-48. Epub 2004 May 6. [PubMed ]
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
Rosand J, Bayley N, Rost N, de Bakker PI: Many hypotheses but no replication for the association between PDE4D and stroke. Nat Genet. 2006 Oct;38(10):1091-2; author reply 1092-3. [PubMed ]
Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed ]
Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Lee ME, Markowitz J, Lee JO, Lee H: Crystal structure of phosphodiesterase 4D and inhibitor complex(1). FEBS Lett. 2002 Oct 23;530(1-3):53-8. [PubMed ]
Huai Q, Colicelli J, Ke H: The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterase catalysis. Biochemistry. 2003 Nov 18;42(45):13220-6. [PubMed ]
Huai Q, Wang H, Sun Y, Kim HY, Liu Y, Ke H: Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity. Structure. 2003 Jul;11(7):865-73. [PubMed ]
Huai Q, Liu Y, Francis SH, Corbin JD, Ke H: Crystal structures of phosphodiesterases 4 and 5 in complex with inhibitor 3-isobutyl-1-methylxanthine suggest a conformation determinant of inhibitor selectivity. J Biol Chem. 2004 Mar 26;279(13):13095-101. Epub 2003 Dec 10. [PubMed ]
Xu RX, Rocque WJ, Lambert MH, Vanderwall DE, Luther MA, Nolte RT: Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram. J Mol Biol. 2004 Mar 19;337(2):355-65. [PubMed ]
Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G: A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases. Mol Cell. 2004 Jul 23;15(2):279-86. [PubMed ]
Card GL, England BP, Suzuki Y, Fong D, Powell B, Lee B, Luu C, Tabrizizad M, Gillette S, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: Structural basis for the activity of drugs that inhibit phosphodiesterases. Structure. 2004 Dec;12(12):2233-47. [PubMed ]
Card GL, Blasdel L, England BP, Zhang C, Suzuki Y, Gillette S, Fong D, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design. Nat Biotechnol. 2005 Feb;23(2):201-7. Epub 2005 Jan 30. [PubMed ]
Huai Q, Sun Y, Wang H, Macdonald D, Aspiotis R, Robinson H, Huang Z, Ke H: Enantiomer discrimination illustrated by the high resolution crystal structures of type 4 phosphodiesterase. J Med Chem. 2006 Mar 23;49(6):1867-73. [PubMed ]
Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed ]
Smith KJ, Baillie GS, Hyde EI, Li X, Houslay TM, McCahill A, Dunlop AJ, Bolger GB, Klussmann E, Adams DR, Houslay MD: 1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1. Cell Signal. 2007 Dec;19(12):2612-24. Epub 2007 Sep 1. [PubMed ]
Wang H, Robinson H, Ke H: The molecular basis for different recognition of substrates by phosphodiesterase families 4 and 10. J Mol Biol. 2007 Aug 10;371(2):302-7. Epub 2007 May 26. [PubMed ]

Enzyme 89 Metabolite References

Not Available

Enzyme 90 [top]

Enzyme 90 ID

5909

Enzyme 90 Name

Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma

Enzyme 90 Synonyms

GMP-PDE gamma

Enzyme 90 Gene Name

PDE6G

Enzyme 90 Protein Sequence

>Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma

MNLEPPKAEFRSATRVAGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGL
GTDITVICPWEAFNHLELHELAQYGII

Enzyme 90 Number of Residues

Enzyme 90 Molecular Weight

9643.1

Enzyme 90 Theoretical pI

10.16

Enzyme 90 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity GMP binding binding cGMP binding catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds nucleoside binding phosphoric diester hydrolase activity phosphoric ester hydrolase activity purine nucleoside binding
Process
multicellular organismal process neurological system process sensory perception sensory perception of light stimulus system process visual perception
Component
—

Enzyme 90 General Function

Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity

Enzyme 90 Specific Function

Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones

Enzyme 90 Pathways

Purine Metabolism (map00230 )

Enzyme 90 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 90 Pfam Domain Function

PDE6_gamma (PF04868 )

Enzyme 90 Signals

None

Enzyme 90 Transmembrane Regions

None

Enzyme 90 Essentiality

Not Available

Enzyme 90 GenBank ID Protein

Not Available

Enzyme 90 UniProtKB/Swiss-Prot ID

P18545

Enzyme 90 UniProtKB/Swiss-Prot Entry Name

CNRG_HUMAN Link Image

Enzyme 90 PDB ID

1FQJ

Enzyme 90 PDB File

Show

Enzyme 90 3D Structure

Enzyme 90 Cellular Location

Not Available

Enzyme 90 Gene Sequence

>264 bp

ATGAACCTGGAACCGCCCAAGGCTGAGTTCCGGTCAGCCACCAGGGTGGCCGGGGGACCT
GTCACCCCCAGGAAAGGGCCCCCTAAATTTAAGCAGCGACAGACCAGGCAGTTCAAGAGC
AAGCCCCCAAAGAAAGGCGTTCAAGGGTTTGGGGACGACATCCCTGGAATGGAAGGCCTG
GGAACAGACATCACAGTCATCTGCCCTTGGGAGGCCTTCAACCACCTGGAGCTGCACGAG
CTGGCCCAATATGGCATCATCTAG

Enzyme 90 GenBank Gene ID

M36476

Enzyme 90 GeneCard ID

PDE6G

Enzyme 90 GenAtlas ID

PDE6G

Enzyme 90 HGNC ID

HGNC:8789

Enzyme 90 Chromosome Location

Enzyme 90 Locus

17q25

Enzyme 90 SNPs

SNPJam Report Link Image

Enzyme 90 General References

Tuteja N, Danciger M, Klisak I, Tuteja R, Inana G, Mohandas T, Sparkes RS, Farber DB: Isolation and characterization of cDNA encoding the gamma-subunit of cGMP phosphodiesterase in human retina. Gene. 1990 Apr 16;88(2):227-32. [PubMed ]
Piriev NI, Purishko VA, Khramtsov NV, Lipkin VM: [The organization of the gamma-subunit gene of human photoreceptor cyclic GMP phosphodiesterase] Dokl Akad Nauk SSSR. 1990;315(1):229-31. [PubMed ]
Hahn LB, Berson EL, Dryja TP: Evaluation of the gene encoding the gamma subunit of rod phosphodiesterase in retinitis pigmentosa. Invest Ophthalmol Vis Sci. 1994 Mar;35(3):1077-82. [PubMed ]
Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 90 Metabolite References

Not Available

Enzyme 91 [top]

Enzyme 91 ID

5912

Enzyme 91 Name

Adenosine kinase

Enzyme 91 Synonyms

AK
Adenosine 5'-phosphotransferase

Enzyme 91 Gene Name

ADK

Enzyme 91 Protein Sequence

>Adenosine kinase

MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAED
KHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKA
AEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKAR
VCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGN
ETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFA
VLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPD
FH

Enzyme 91 Number of Residues

362

Enzyme 91 Molecular Weight

40545.1

Enzyme 91 Theoretical pI

6.67

Enzyme 91 GO Classification

Function
adenosine kinase activity catalytic activity kinase activity nucleobase, nucleoside, nucleotide kinase activity nucleoside kinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
biosynthetic process cellular biosynthetic process heterocycle biosynthetic process metabolic process purine ribonucleoside salvage purine salvage
Component
—

Enzyme 91 General Function

Involved in adenosine kinase activity

Enzyme 91 Specific Function

ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides

Enzyme 91 Pathways

Purine Metabolism (map00230 )

Enzyme 91 Reactions

ATP + adenosine = ADP + AMP [RN:R00185]

Enzyme 91 Pfam Domain Function

PfkB (PF00294 )

Enzyme 91 Signals

None

Enzyme 91 Transmembrane Regions

None

Enzyme 91 Essentiality

Not Available

Enzyme 91 GenBank ID Protein

32484975

Enzyme 91 UniProtKB/Swiss-Prot ID

P55263

Enzyme 91 UniProtKB/Swiss-Prot Entry Name

ADK_HUMAN

Enzyme 91 PDB ID

1BX4

Enzyme 91 PDB File

Show

Enzyme 91 3D Structure

Enzyme 91 Cellular Location

Not Available

Enzyme 91 Gene Sequence

>1089 bp

ATGGCAGCTGCTGAGGAGGAGCCGAAGCCCAAAAAGCTGAAGGTGGAGGCGCCGCAAGCG
CTGAGAGAAAATATTCTCTTTGGAATGGGAAATCCTCTGCTTGACATCTCTGCTGTAGTG
GACAAAGATTTCCTTGATAAGTATTCTCTGAAACCAAATGACCAAATCTTGGCTGAAGAC
AAACACAAGGAACTGTTTGATGAACTTGTGAAAAAATTCAAAGTCGAATATCATGCTGGT
GGCTCTACCCAGAATTCAATTAAAGTGGCTCAGTGGATGATTCAACAGCCACACAAAGCA
GCAACATTTTTTGGATGCATTGGGATAGATAAATTTGGGGAGATCCTGAAGAGAAAAGCT
GCTGAAGCCCATGTGGATGCTCATTACTACGAGCAGAATGAGCAGCCAACAGGAACTTGT
GCTGCATGCATCACTGGTGACAACAGGTCCCTCATAGCTAATCTTGCTGCTGCCAATTGT
TATAAAAAGGAAAAACATCTTGATCTGGAGAAAAACTGGATGTTGGTAGAAAAAGCAAGA
GTTTGTTATATAGCAGGCTTTTTTCTTACAGTTTCCCCAGAGTCAGTATTAAAGGTGGCT
CACCATGCTTCTGAAAACAACAGGATTTTCACTTTGAATCTATCTGCACCGTTTATTAGC
CAGTTCTACAAGGAATCATTGATGAAAGTTATGCCTTATGTTGATATACTTTTTGGAAAT
GAGACAGAAGCTGCCACTTTTGCTAGAGAGCAAGGCTTTGAGACTAAAGACATTAAAGAG
ATAGCCAAAAAGACACAAGCCCTGCCAAAGATGAACTCAAAGAGGCAGCGAATCGTGATC
TTCACCCAAGGGAGAGATGACACTATAATGGCTACAGAAAGTGAAGTCACTGCTTTTGCT
GTCTTGGATCAAGACCAGAAAGAAATTATTGATACCAATGGAGCTGGAGATGCATTTGTT
GGAGGTTTTCTGTCTCAACTGGTCTCTGACAAGCCTCTGACTGAATGTATCCGTGCTGGC
CACTATGCAGCAAGCATCATAATTAGACGGACTGGCTGCACCTTTCCTGAGAAGCCAGAC
TTCCACTGA

Enzyme 91 GenBank Gene ID

NM_006721

Enzyme 91 GeneCard ID

ADK

Enzyme 91 GenAtlas ID

ADK

Enzyme 91 HGNC ID

HGNC:257

Enzyme 91 Chromosome Location

Enzyme 91 Locus

10q22|10q11-q24

Enzyme 91 SNPs

SNPJam Report Link Image

Enzyme 91 General References

Spychala J, Datta NS, Takabayashi K, Datta M, Fox IH, Gribbin T, Mitchell BS: Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and fructokinases. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1232-7. [PubMed ]
Singh B, Hao W, Wu Z, Eigl B, Gupta RS: Cloning and characterization of cDNA for adenosine kinase from mammalian (Chinese hamster, mouse, human and rat) species. High frequency mutants of Chinese hamster ovary cells involve structural alterations in the gene. Eur J Biochem. 1996 Oct 15;241(2):564-71. [PubMed ]
McNally T, Helfrich RJ, Cowart M, Dorwin SA, Meuth JL, Idler KB, Klute KA, Simmer RL, Kowaluk EA, Halbert DN: Cloning and expression of the adenosine kinase gene from rat and human tissues. Biochem Biophys Res Commun. 1997 Feb 24;231(3):645-50. [PubMed ]
Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Mathews II, Erion MD, Ealick SE: Structure of human adenosine kinase at 1.5 A resolution. Biochemistry. 1998 Nov 10;37(45):15607-20. [PubMed ]
Maguire PB, Wynne KJ, Harney DF, O'Donoghue NM, Stephens G, Fitzgerald DJ: Identification of the phosphotyrosine proteome from thrombin activated platelets. Proteomics. 2002 Jun;2(6):642-8. [PubMed ]

Enzyme 91 Metabolite References

Not Available

Enzyme 92 [top]

Enzyme 92 ID

5913

Enzyme 92 Name

Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta

Enzyme 92 Synonyms

GMP-PDE delta
Protein p17

Enzyme 92 Gene Name

PDE6D

Enzyme 92 Protein Sequence

>Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta

MSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVS
RELNFSSTEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPA
SVLTGNVIIETKFFDDDLLVSTSRVRLFYV

Enzyme 92 Number of Residues

150

Enzyme 92 Molecular Weight

17419.9

Enzyme 92 Theoretical pI

5.35

Enzyme 92 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity binding catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity protein binding
Process
multicellular organismal process neurological system process sensory perception sensory perception of light stimulus system process visual perception
Component
—

Enzyme 92 General Function

Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity

Enzyme 92 Specific Function

Not Available

Enzyme 92 Pathways

Purine Metabolism (map00230 )

Enzyme 92 Reactions

Not Available

Enzyme 92 Pfam Domain Function

GMP_PDE_delta (PF05351 )

Enzyme 92 Signals

None

Enzyme 92 Transmembrane Regions

None

Enzyme 92 Essentiality

Not Available

Enzyme 92 GenBank ID Protein

2655094

Enzyme 92 UniProtKB/Swiss-Prot ID

O43924

Enzyme 92 UniProtKB/Swiss-Prot Entry Name

PDE6D_HUMAN Link Image

Enzyme 92 PDB ID

1KSG

Enzyme 92 PDB File

Show

Enzyme 92 3D Structure

Enzyme 92 Cellular Location

Not Available

Enzyme 92 Gene Sequence

>453 bp

ATGTCAGCCAAGGACGAGCGGGCCAGGGAGATCCTGAGGGGCTTCAAACTAAATTGGATG
AACCTTCGGGATGCTGAGACAGGGAAGATACTCTGGCAAGGAACAGAAGACCTGTCTGTC
CCTGGTGTGGAGCATGAAGCCCGTGTTCCCAAGAAAATCCTCAAGTGCAAGGCAGTGTCT
CGAGAACTTAATTTTTCTTCGACAGAACAAATGGAAAAATTCCGCCTGGAACAAAAAGTT
TACTTCAAAGGGCAATGCCTAGAAGAATGGTTCTTCGAGTTTGGCTTTGTGATCCCTAAC
TCCACAAATACCTGGCAGTCCTTGATAGAGGCAGCACCCGAGTCCCAGATGATGCCAGCA
AGCGTCTTAACTGGGAACGTTATCATAGAAACAAAGTTTTTTGACGACGATCTTCTTGTA
AGCACATCCAGAGTGAGACTTTTCTATGTTTGA

Enzyme 92 GenBank Gene ID

AF022912

Enzyme 92 GeneCard ID

PDE6D

Enzyme 92 GenAtlas ID

PDE6D

Enzyme 92 HGNC ID

HGNC:8788

Enzyme 92 Chromosome Location

Enzyme 92 Locus

2q35-q36

Enzyme 92 SNPs

SNPJam Report Link Image

Enzyme 92 General References

Li N, Florio SK, Pettenati MJ, Rao PN, Beavo JA, Baehr W: Characterization of human and mouse rod cGMP phosphodiesterase delta subunit (PDE6D) and chromosomal localization of the human gene. Genomics. 1998 Apr 1;49(1):76-82. [PubMed ]
Ershova G, Derre J, Chetelin S, Nancy V, Berger R, Kaplan J, Munnich A, de Gunzburg J: cDNA sequence, genomic organization and mapping of PDE6D, the human gene encoding the delta subunit of the cGMP phosphodiesterase of retinal rod cells to chromosome 2q36. Cytogenet Cell Genet. 1997;79(1-2):139-41. [PubMed ]
Lorenz B, Migliaccio C, Lichtner P, Meyer C, Strom TM, D'Urso M, Becker J, Ciccodicola A, Meitinger T: Cloning and gene structure of the rod cGMP phosphodiesterase delta subunit gene (PDED) in man and mouse. Eur J Hum Genet. 1998 May-Jun;6(3):283-90. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Linari M, Hanzal-Bayer M, Becker J: The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner. FEBS Lett. 1999 Sep 10;458(1):55-9. [PubMed ]
Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC: The complex of Arl2-GTP and PDE delta: from structure to function. EMBO J. 2002 May 1;21(9):2095-106. [PubMed ]

Enzyme 92 Metabolite References

Not Available

Enzyme 93 [top]

Enzyme 93 ID

5914

Enzyme 93 Name

Probable histidyl-tRNA synthetase, mitochondrial

Enzyme 93 Synonyms

Histidine--tRNA ligase
HisRS
Histidine--tRNA ligase-like

Enzyme 93 Gene Name

HARS2

Enzyme 93 Protein Sequence

>Probable histidyl-tRNA synthetase, mitochondrial

MPLLGLLPRRAWASLLSQLLRPPCASCTGAVRCQSQVAEAVLTSQLKAHQEKPNFIIKTP
KGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKD
QGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTIVQGRYREFCQCDFDIA
GQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSID
KLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPRLSQNKQALEGL
GDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQAGEEPLNVGSVAA
GGRYDGLVGMFDPKGHKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTETQVFVATPQKN
FLQERLKLIAELWDSGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIR
SVASREEVAIKRENFVAEIQKRLSES

Enzyme 93 Number of Residues

506

Enzyme 93 Molecular Weight

56887.9

Enzyme 93 Theoretical pI

8.35

Enzyme 93 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity histidine-tRNA ligase activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process histidyl-tRNA aminoacylation macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 93 General Function

Involved in nucleotide binding

Enzyme 93 Specific Function

ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His)

Enzyme 93 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Histidine Metabolism (map00340 )

Enzyme 93 Reactions

ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis [RN:R03655]

Enzyme 93 Pfam Domain Function

HGTP_anticodon (PF03129 )
tRNA-synt_2b (PF00587 )

Enzyme 93 Signals

None

Enzyme 93 Transmembrane Regions

None

Enzyme 93 Essentiality

Not Available

Enzyme 93 GenBank ID Protein

Not Available

Enzyme 93 UniProtKB/Swiss-Prot ID

P49590

Enzyme 93 UniProtKB/Swiss-Prot Entry Name

SYHM_HUMAN Link Image

Enzyme 93 PDB ID

Not Available

Enzyme 93 Cellular Location

Not Available

Enzyme 93 Gene Sequence

>1521 bp

ATGCCCCTGCTCGGACTTCTTCCCAGGAGGGCCTGGGCTTCGCTGCTCAGCCAGCTCCTG
CGACCGCCCTGCGCTTCGTGCACCGGGGCGGTCCGTTGCCAAAGCCAGGTTGCAGAGGCA
GTGTTAACATCCCAACTGAAAGCACATCAAGAGAAACCAAATTTTATTATCAAGACCCCA
AAGGGTACCAGGGATCTTAGTCCTCAGCATATGGTTGTGAGGGAGAAAATTCTTGATTTG
GTTATCAGCTGCTTTAAACGTCATGGAGCAAAGGGGATGGACACCCCAGCATTTGAGCTG
AAGGAAACCCTGACTGAGAAGTATGGAGAGGACTCTGGGCTCATGTATGATCTGAAGGAT
CAAGGTGGAGAGCTGTTGTCCCTCCGCTATGACCTTACTGTTCCCTTTGCTCGTTATCTG
GCCATGAATAAGGTGAAGAAGATGAAACGTTATCATGTTGGAAAGGTGTGGCGGCGAGAG
AGCCCAACCATAGTCCAAGGCCGTTATAGGGAGTTCTGCCAGTGTGATTTTGACATTGCT
GGTCAGTTTGACCCTATGATCCCCGATGCAGAGTGTTTGAAGATCATGTGTGAAATCCTA
AGTGGATTGCAGTTGGGAGACTTTCTCATTAAGGTAAATGACCGGCGGATTGTGGATGGG
ATGTTTGCTGTCTGTGGTGTTCCTGAAAGCAAGTTCCGTGCCATCTGCTCCTCCATAGAT
AAACTAGACAAGATGGCTTGGAAAGATGTGAGACATGAGATGGTGGTGAAGAAAGGCCTG
GCTCCTGAGGTGGCTGATCGAATTGGGGACTATGTCCAGTGTCATGGTGGGGTATCCCTA
GTAGAGCAAATGTTTCAGGATCCCAGACTATCCCAGAACAAGCAGGCCCTGGAGGGCCTG
GGAGACCTAAAGCTGCTATTTGAATACCTGACTTTATTTGGAATTGCTGATAAGATCTCC
TTTGACCTCAGCCTGGCTCGGGGCCTAGACTACTATACAGGAGTGATCTATGAAGCAGTG
CTGCTGCAGACCCCAACTCAGGCTGGGGAGGAGCCCCTGAATGTGGGCAGTGTGGCTGCT
GGTGGGCGCTATGATGGGCTGGTGGGCATGTTTGACCCCAAGGGCCACAAGGTGCCATGT
GTGGGACTCAGCATTGGGGTTGAGCGAATCTTCTACATTGTGGAGCAGAGGATGAAGACC
AAAGGTGAGAAGGTGCGGACTACAGAGACTCAAGTGTTTGTGGCCACACCACAGAAGAAC
TTTCTCCAAGAACGGTTGAAGCTTATTGCAGAGCTTTGGGATTCTGGAATCAAGGCAGAG
ATGCTATACAAGAACAACCCCAAACTATTAACCCAGCTGCACTATTGTGAGAGCACAGGC
ATTCCACTGGTGGTCATTATTGGTGAGCAAGAACTGAAAGAAGGGGTCATCAAGATCCGT
TCAGTGGCCAGCAGAGAGGAGGTGGCCATTAAACGGGAAAATTTTGTGGCTGAAATTCAG
AAGCGACTGTCTGAGTCTTGA

Enzyme 93 GenBank Gene ID

U18937

Enzyme 93 GeneCard ID

HARS2

Enzyme 93 GenAtlas ID

HARS2

Enzyme 93 HGNC ID

HGNC:4817

Enzyme 93 Chromosome Location

Enzyme 93 Locus

5q31.3

Enzyme 93 SNPs

SNPJam Report Link Image

Enzyme 93 General References

O'Hanlon TP, Raben N, Miller FW: A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS. Biochem Biophys Res Commun. 1995 May 16;210(2):556-66. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 93 Metabolite References

Not Available

Enzyme 94 [top]

Enzyme 94 ID

5915

Enzyme 94 Name

Ubiquitin-conjugating enzyme E2 J1

Enzyme 94 Synonyms

Non-canonical ubiquitin-conjugating enzyme 1
NCUBE-1
Yeast ubiquitin-conjugating enzyme UBC6 homolog E
HsUBC6e

Enzyme 94 Gene Name

UBE2J1

Enzyme 94 Protein Sequence

>Ubiquitin-conjugating enzyme E2 J1

METRYNLKSPAVKRLMKEAAELKDPTDHYHAQPLEDNLFEWHFTVRGPPDSDFDGGVYHG
RIVLPPEYPMKPPSIILLTANGRFEVGKKICLSISGHHPETWQPSWSIRTALLAIIGFMP
TKGEGAIGSLDYTPEERRALAKKSQDFCCEGCGSAMKDVLLPLKSGSDSSQADQEAKELA
RQISFKAEVNSSGKTISESDLNHSFSLTDLQDDIPTTFQGATASTSYGLQNSSAASFHQP
TQPVAKNTSMSPRQRRAQQQSQRRLSTSPDVIQGHQPRDNHTDHGGSAVLIVILTLALAA
LIFRRIYLANEYIFDFEL

Enzyme 94 Number of Residues

318

Enzyme 94 Molecular Weight

35198.3

Enzyme 94 Theoretical pI

6.74

Enzyme 94 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 94 General Function

Involved in acid-amino acid ligase activity

Enzyme 94 Specific Function

Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum

Enzyme 94 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 94 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 94 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 94 Signals

None

Enzyme 94 Transmembrane Regions

283-303

Enzyme 94 Essentiality

Not Available

Enzyme 94 GenBank ID Protein

37577122

Enzyme 94 UniProtKB/Swiss-Prot ID

Q9Y385

Enzyme 94 UniProtKB/Swiss-Prot Entry Name

UB2J1_HUMAN Link Image

Enzyme 94 PDB ID

Not Available

Enzyme 94 Cellular Location

Not Available

Enzyme 94 Gene Sequence

>957 bp

ATGGAGACCCGCTACAACCTGAAGAGTCCGGCTGTTAAACGTTTAATGAAAGAAGCGGCA
GAATTGAAAGATCCAACAGATCATTACCATGCGCAGCCTTTAGAGGATAACCTTTTTGAA
TGGCACTTCACGGTTAGAGGGCCCCCAGACTCCGATTTTGATGGAGGAGTTTATCACGGG
CGGATAGTACTGCCACCAGAGTATCCCATGAAACCACCAAGCATTATTCTCCTAACGGCT
AATGGTCGATTTGAAGTGGGCAAGAAAATCTGTTTGAGCATCTCAGGCCATCATCCTGAA
ACTTGGCAGCCTTCGTGGAGTATAAGGACAGCATTATTAGCCATCATTGGGTTTATGCCA
ACAAAAGGAGAGGGAGCCATAGGTTCTCTAGATTACACTCCTGAGGAAAGAAGAGCACTT
GCCAAAAAATCACAAGATTTCTGTTGTGAAGGATGTGGCTCTGCCATGAAGGATGTCCTG
TTGCCTTTAAAATCTGGAAGCGATTCAAGCCAAGCTGACCAAGAAGCCAAAGAACTGGCT
AGGCAAATAAGCTTTAAGGCAGAAGTCAATTCATCTGGAAAGACTATCTCTGAGTCAGAC
TTAAACCACTCTTTTTCACTAACTGATTTACAAGATGATATACCTACAACATTCCAGGGT
GCTACGGCCAGTACATCGTACGGACTCCAGAATTCCTCAGCAGCATCCTTTCATCAACCT
ACCCAACCTGTAGCTAAGAATACCTCCATGAGCCCTCGACAGCGCCGGGCCCAGCAGCAG
AGTCAGAGAAGGTTGTCTACTTCACCAGATGTAATCCAGGGCCACCAGCCAAGAGACAAC
CACACTGATCATGGTGGGTCAGCTGTACTGATTGTCATCCTGACTTTGGCATTGGCAGCT
CTTATATTCCGACGAATATATCTGGCAAACGAATACATATTTGACTTTGAGTTATAA

Enzyme 94 GenBank Gene ID

NM_016021.2 Link Image

Enzyme 94 GeneCard ID

UBE2J1

Enzyme 94 GenAtlas ID

UBE2J1

Enzyme 94 HGNC ID

HGNC:17598 Link Image

Enzyme 94 Chromosome Location

Enzyme 94 Locus

6q15

Enzyme 94 SNPs

SNPJam Report Link Image

Enzyme 94 General References

Lester D, Farquharson C, Russell G, Houston B: Identification of a family of noncanonical ubiquitin-conjugating enzymes structurally related to yeast UBC6. Biochem Biophys Res Commun. 2000 Mar 16;269(2):474-80. [PubMed ]
Lenk U, Yu H, Walter J, Gelman MS, Hartmann E, Kopito RR, Sommer T: A role for mammalian Ubc6 homologues in ER-associated protein degradation. J Cell Sci. 2002 Jul 15;115(Pt 14):3007-14. [PubMed ]
Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed ]
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]

Enzyme 94 Metabolite References

Not Available

Enzyme 95 [top]

Enzyme 95 ID

5916

Enzyme 95 Name

Long-chain-fatty-acid--CoA ligase 5

Enzyme 95 Synonyms

Long-chain acyl-CoA synthetase 5
LACS 5

Enzyme 95 Gene Name

ACSL5

Enzyme 95 Protein Sequence

>Long-chain-fatty-acid--CoA ligase 5

MLFIFNFLFSPLPTPALICILTFGAAIFLWLITRPQPVLPLLDLNNQSVGIEGGARKGVS
QKNNDLTSCCFSDAKTMYEVFQRGLAVSDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGS
CLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVHIVNKADI
AMVICDTPQKALVLIGNVEKGFTPSLKVIILMDPFDDDLKQRGEKSGIEILSLYDAENLG
KEHFRKPVPPSPEDLSVICFTSGTTGDPKGAMITHQNIVSNAAAFLKCVEHAYEPTPDDV
AISYLPLAHMFERIVQAVVYSCGARVGFFQGDIRLLADDMKTLKPTLFPAVPRLLNRIYD
KVQNEAKTPLKKFLLKLAVSSKFKELQKGIIRHDSFWDKLIFAKIQDSLGGRVRVIVTGA
APMSTSVMTFFRAAMGCQVYEAYGQTECTGGCTFTLPGDWTSGHVGVPLACNYVKLEDVA
DMNYFTVNNEGEVCIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDR
KKNIFKLAQGEYIAPEKIENIYNRSQPVLQIFVHGESLRSSLVGVVVPDTDVLPSFAAKL
GVKGSFEELCQNQVVREAILEDLQKIGKESGLKTFEQVKAIFLHPEPFSIENGLLTPTLK
AKRGELSKYFRTQIDSLYEHIQD

Enzyme 95 Number of Residues

683

Enzyme 95 Molecular Weight

75990.1

Enzyme 95 Theoretical pI

6.91

Enzyme 95 GO Classification

Function
catalytic activity
Process
metabolic process
Component
—

Enzyme 95 General Function

Involved in catalytic activity

Enzyme 95 Specific Function

Acyl-CoA synthetases (ACSL) activate long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids. It was suggested that it may also stimulate fatty acid oxidation. At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL. May have a role in the survival of glioma cells

Enzyme 95 Pathways

Fatty Acid Metabolism (map00071 )

Enzyme 95 Reactions

ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]

Enzyme 95 Pfam Domain Function

AMP-binding (PF00501 )

Enzyme 95 Signals

None

Enzyme 95 Transmembrane Regions

12-32

Enzyme 95 Essentiality

Not Available

Enzyme 95 GenBank ID Protein

6174680

Enzyme 95 UniProtKB/Swiss-Prot ID

Q9ULC5

Enzyme 95 UniProtKB/Swiss-Prot Entry Name

ACSL5_HUMAN Link Image

Enzyme 95 PDB ID

Not Available

Enzyme 95 Cellular Location

Not Available

Enzyme 95 Gene Sequence

>2052 bp

ATGCTTTTTATCTTTAACTTTTTGTTTTCCCCACTTCCGACCCCGGCGTTGATCTGCATC
CTGACATTTGGAGCTGCCATCTTCTTGTGGCTGATCACCAGACCTCAACCCGTCTTACCT
CTTCTTGACCTGAACAATCAGTCTGTGGGAATTGAGGGAGGAGCACGGAAGGGGGTTTCC
CAGAAGAACAATGACCTAACAAGTTGCTGCTTCTCAGATGCCAAGACTATGTATGAGGTT
TTCCAAAGAGGACTCGCTGTGTCTGACAATGGGCCCTGCTTGGGATATAGAAAACCAAAC
CAGCCCTACAGATGGCTATCTTACAAACAGGTGTCTGATAGAGCAGAGTACCTGGGTTCC
TGTCTCTTGCATAAAGGTTATAAATCATCACCAGACCAGTTTGTCGGCATCTTTGCTCAG
AATAGGCCAGAGTGGATCATCTCCGAATTGGCTTGTTACACGTACTCTATGGTAGCTGTA
CCTCTGTATGACACCTTGGGACCAGAAGCCATCGTACATATTGTCAACAAGGCTGATATC
GCCATGGTGATCTGTGACACACCCCAAAAGGCATTGGTGCTGATAGGGAATGTAGAGAAA
GGCTTCACCCCGAGCCTGAAGGTGATCATCCTTATGGACCCCTTTGATGATGACCTGAAG
CAAAGAGGGGAGAAGAGTGGAATTGAGATCTTATCCCTATATGATGCTGAGAACCTAGGC
AAAGAGCACTTCAGAAAACCTGTGCCTCCTAGCCCAGAAGACCTGAGCGTCATCTGCTTC
ACCAGTGGGACCACAGGTGACCCCAAAGGAGCCATGATAACCCATCAAAATATTGTTTCA
AATGCTGCTGCCTTTCTCAAATGTGTGGAGCATGCTTATGAGCCCACTCCTGATGATGTG
GCCATATCCTACCTCCCTCTGGCTCATATGTTTGAGAGGATTGTACAGGCTGTTGTGTAC
AGCTGTGGAGCCAGAGTTGGATTCTTCCAAGGGGATATTCGGTTGCTGGCTGACGACATG
AAGACTTTGAAGCCCACATTGTTTCCCGCGGTGCCTCGACTCCTTAACAGGATCTACGAT
AAGGTACAAAATGAGGCCAAGACACCCTTGAAGAAGTTCTTGTTGAAGCTGGCTGTTTCC
AGTAAATTCAAAGAGCTTCAAAAGGGTATCATCAGGCATGATAGTTTCTGGGACAAGCTC
ATCTTTGCAAAGATCCAGGACAGCCTGGGCGGAAGGGTTCGTGTAATTGTCACTGGAGCT
GCCCCCATGTCCACTTCAGTCATGACATTCTTCCGGGCAGCAATGGGATGTCAGGTGTAT
GAAGCTTATGGTCAAACAGAATGCACAGGTGGCTGTACATTTACATTACCTGGGGACTGG
ACATCAGGTCACGTTGGGGTGCCCCTGGCTTGCAATTACGTGAAGCTGGAAGATGTGGCT
GACATGAACTACTTTACAGTGAATAATGAAGGAGAGGTCTGCATCAAGGGTACAAACGTG
TTCAAAGGATACCTGAAGGACCCTGAGAAGACACAGGAAGCCCTGGACAGTGATGGCTGG
CTTCACACAGGAGACATTGGTCGCTGGCTCCCGAATGGAACTCTGAAGATCATCGACCGT
AAAAAGAACATTTTCAAGCTGGCCCAAGGAGAATACATTGCACCAGAGAAGATAGAAAAT
ATCTACAACAGGAGTCAACCAGTGTTACAAATTTTTGTACACGGGGAGAGCTTACGGTCA
TCCTTAGTAGGAGTGGTGGTTCCTGACACAGATGTACTTCCCTCATTTGCAGCCAAGCTT
GGGGTGAAGGGCTCCTTTGAGGAACTGTGCCAAAACCAAGTTGTAAGGGAAGCCATTTTA
GAAGACTTGCAGAAAATTGGGAAAGAAAGTGGCCTTAAAACTTTTGAACAGGTCAAAGCC
ATTTTTCTTCATCCAGAGCCATTTTCCATTGAAAATGGGCTCTTGACACCAACATTGAAA
GCAAAGCGAGGAGAGCTTTCCAAATACTTTCGGACCCAAATTGACAGCCTGTATGAGCAC
ATCCAGGATTAG

Enzyme 95 GenBank Gene ID

AB033899

Enzyme 95 GeneCard ID

ACSL5

Enzyme 95 GenAtlas ID

ACSL5

Enzyme 95 HGNC ID

HGNC:16526 Link Image

Enzyme 95 Chromosome Location

Enzyme 95 Locus

10q25.1-q25.2

Enzyme 95 SNPs

SNPJam Report Link Image

Enzyme 95 General References

Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gassler N, Roth W, Funke B, Schneider A, Herzog F, Tischendorf JJ, Grund K, Penzel R, Bravo IG, Mariadason J, Ehemann V, Sykora J, Haas TL, Walczak H, Ganten T, Zentgraf H, Erb P, Alonso A, Autschbach F, Schirmacher P, Knuchel R, Kopitz J: Regulation of enterocyte apoptosis by acyl-CoA synthetase 5 splicing. Gastroenterology. 2007 Aug;133(2):587-98. Epub 2007 Jun 8. [PubMed ]
Mashima T, Sato S, Okabe S, Miyata S, Matsuura M, Sugimoto Y, Tsuruo T, Seimiya H: Acyl-CoA synthetase as a cancer survival factor: its inhibition enhances the efficacy of etoposide. Cancer Sci. 2009 Aug;100(8):1556-62. Epub 2009 May 13. [PubMed ]
Mashima T, Sato S, Sugimoto Y, Tsuruo T, Seimiya H: Promotion of glioma cell survival by acyl-CoA synthetase 5 under extracellular acidosis conditions. Oncogene. 2009 Jan 8;28(1):9-19. Epub 2008 Sep 22. [PubMed ]
Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]

Enzyme 95 Metabolite References

Not Available

Enzyme 96 [top]

Enzyme 96 ID

5917

Enzyme 96 Name

Histidyl-tRNA synthetase, cytoplasmic

Enzyme 96 Synonyms

Histidine--tRNA ligase
HisRS

Enzyme 96 Gene Name

HARS

Enzyme 96 Protein Sequence

>Histidyl-tRNA synthetase, cytoplasmic

MAERAALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPK
GTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQ
GGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFDIAG
NFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDK
LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDPKLSQNKQALEGLG
DLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQAGEEPLGVGSVAAG
GRYDGLVGMFDPKGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKL
LEERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRS
VTSREEVDVRREDLVEEIKRRTGQPLCIC

Enzyme 96 Number of Residues

509

Enzyme 96 Molecular Weight

57410.0

Enzyme 96 Theoretical pI

5.56

Enzyme 96 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity histidine-tRNA ligase activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process histidyl-tRNA aminoacylation macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 96 General Function

Involved in nucleotide binding

Enzyme 96 Specific Function

ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His)

Enzyme 96 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Histidine Metabolism (map00340 )

Enzyme 96 Reactions

ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis [RN:R03655]

Enzyme 96 Pfam Domain Function

HGTP_anticodon (PF03129 )
tRNA-synt_2b (PF00587 )
WHEP-TRS (PF00458 )

Enzyme 96 Signals

None

Enzyme 96 Transmembrane Regions

None

Enzyme 96 Essentiality

Not Available

Enzyme 96 GenBank ID Protein

32460

Enzyme 96 UniProtKB/Swiss-Prot ID

P12081

Enzyme 96 UniProtKB/Swiss-Prot Entry Name

SYHC_HUMAN Link Image

Enzyme 96 PDB ID

Not Available

Enzyme 96 Cellular Location

Not Available

Enzyme 96 Gene Sequence

>1530 bp

ATGGCAGAGCGTGCGGCGCTGGAGGAGCTGGTGAAACTTCAGGGAGAGCGCGTGCGAGGC
CTCAAGCAGCAGAAGGCCAGCGCCGAGCTGATCGAGGAGGAGGTGGCGAAACTCCTGAAA
CTGAAGGCACAGCTGGGTCCTGATGAAAGCAAACAGAAATTTGTGCTCAAAACCCCCAAG
GGCACAAGAGACTATAGTCCCCGGCAGATGGCAGTTCGCGAGAAGGTGTTTGACGTAATC
ATCCGTTGCTTCAAGCGCCACGGTGCAGAAGTCATTGATACACCTGTATTTGAACTAAAG
GAAACACTGATGGGAAAGTATGGGGAAGACTCCAAGCTTATCTATGACCTGAAGGACCAG
GGCGGGGAGCTCCTGTCCCTTCGCTATGACCTCACTGTTCCTTTTGCTCGGTATTTGGCA
ATGAATAAACTGACCAACATTAAACGCTACCACATAGCAAAGGTATATCGGCGGGATAAC
CCAGCCATGACCCGTGGCCGATACCGGGAATTCTACCAGTGTGATTTTGACATTGCTGGG
AACTTTGATCCCATGATCCCTGATGCAGAGTGCCTGAAGATCATGTGCGAGATCCTGAGT
TCACTTCAGATAGGCGACTTCCTGGTCAAGGTAAACGATCGACGCATTCTAGATGGGATG
TTTGCTATCTGTGGTGTTTCTGACAGCAAGTTCCGTACCATCTGCTCCTCAGTAGACAAG
CTGGACAAGGTGTCCTGGGAAGAGGTGAAGAATGAGATGGTGGGAGAGAAGGGCCTTGCA
CCTGAGGTGGCTGACCGCATTGGGGACTATGTCCAGCAACATGGTGGGGTATCCCTGGTG
GAACAGCTGCTCCAGGATCCTAAACTATCCCAAAACAAGCAGGCCTTGGAGGGCCTGGGA
GACCTGAAGTTGCTCTTTGAGTACCTGACCCTATTTGGCATTGATGACAAAATCTCCTTT
GACCTGAGCCTTGCTCGAGGGCTGGATTACTACACTGGGGTGATCTATGAGGCAGTGCTG
CTACAGACCCCAGCCCAGGCAGGGGAAGAGCCCCTGGGTGTGGGCAGTGTGGCTGCTGGA
GGACGCTATGATGGGCTAGTGGGCATGTTCGACCCCAAAGGGCGCAAGGTGCCATGTGTG
GGGCTCAGCATTGGGGTGGAGCGGATTTTCTCCATCGTGGAACAGAGACTAGAGGCTTTG
GAGGAGAAGATACGGACCACGGAGACACAGGTGCTTGTGGCATCTGCACAGAAGAAGCTG
CTAGAGGAAAGACTAAAGCTTGTCTCAGAACTGTGGGATGCTGGGATCAAGGCTGAGCTG
CTGTACAAGAAGAACCCAAAGCTACTGAACCAGTTACAGTACTGTGAGGAGGCAGGCATC
CCACTGGTGGCTATCATCGGCGAGCAGGAACTCAAGGATGGGGTCATCAAGCTCCGTTCA
GTGACGAGCAGGGAAGAGGTGGATGTCCGAAGAGAAGACCTTGTGGAGGAAATCAAAAGG
AGAACAGGCCAGCCCCTCTGCATCTGCTGA

Enzyme 96 GenBank Gene ID

Z11518

Enzyme 96 GeneCard ID

HARS

Enzyme 96 GenAtlas ID

HARS

Enzyme 96 HGNC ID

HGNC:4816

Enzyme 96 Chromosome Location

Enzyme 96 Locus

5q31.3

Enzyme 96 SNPs

SNPJam Report Link Image

Enzyme 96 General References

Raben N, Borriello F, Amin J, Horwitz R, Fraser D, Plotz P: Human histidyl-tRNA synthetase: recognition of amino acid signature regions in class 2a aminoacyl-tRNA synthetases. Nucleic Acids Res. 1992 Mar 11;20(5):1075-81. [PubMed ]
Tsui FW, Siminovitch L: Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase. Nucleic Acids Res. 1987 Apr 24;15(8):3349-67. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Tsui HW, Mok S, de Souza L, Martin A, Tsui FW: Transcriptional analyses of the gene region that encodes human histidyl-tRNA synthetase: identification of a novel bidirectional regulatory element. Gene. 1993 Sep 15;131(2):201-8. [PubMed ]
O'Hanlon TP, Raben N, Miller FW: A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS. Biochem Biophys Res Commun. 1995 May 16;210(2):556-66. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 96 Metabolite References

Not Available

Enzyme 97 [top]

Enzyme 97 ID

5918

Enzyme 97 Name

Seryl-tRNA synthetase, cytoplasmic

Enzyme 97 Synonyms

Serine--tRNA ligase
SerRS
Seryl-tRNA(Ser/Sec) synthetase

Enzyme 97 Gene Name

SARS

Enzyme 97 Protein Sequence

>Seryl-tRNA synthetase, cytoplasmic

MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLC
SKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAE
RIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGF
EGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQL
SQFDEELYKVIGKGSEKSDDNSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTC
FRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYH
IVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKMMDKV
EFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMPPGLQELIPFVKPAPIEQEP
SKKQKKQHEGSKKKAAARDVTLENRLQNMEVTDA

Enzyme 97 Number of Residues

514

Enzyme 97 Molecular Weight

58776.8

Enzyme 97 Theoretical pI

6.38

Enzyme 97 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding serine-tRNA ligase activity
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process seryl-tRNA aminoacylation tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 97 General Function

Involved in nucleotide binding

Enzyme 97 Specific Function

Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)

Enzyme 97 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Glycine, Serine and Threonine Metabolism (map00260 )

Enzyme 97 Reactions

ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer [RN:R03662]

Enzyme 97 Pfam Domain Function

Seryl_tRNA_N (PF02403 )
tRNA-synt_2b (PF00587 )

Enzyme 97 Signals

None

Enzyme 97 Transmembrane Regions

None

Enzyme 97 Essentiality

Not Available

Enzyme 97 GenBank ID Protein

1050527

Enzyme 97 UniProtKB/Swiss-Prot ID

P49591

Enzyme 97 UniProtKB/Swiss-Prot Entry Name

SYSC_HUMAN Link Image

Enzyme 97 PDB ID

Not Available

Enzyme 97 Cellular Location

Not Available

Enzyme 97 Gene Sequence

>1545 bp

ATGGTGCTGGATCTGGATTTGTTTCGGGTGGATAAAGGAGGGGACCCAGCCCTCATCCGA
GAGACGCAGGAGAAGCGCTTCAAGGACCCGGGACTAGTGGACCAGCTGGTGAAGGCAGAC
AGCGAGTGGCGACGATGTAGATTTCGGGCAGACAACTTGAGCAAGCTGAAGAACCTATGC
AGCAAGACAATCGGAGAGAAAATGAAGAAAAAAGAGCCAGTGGGAGATGATGAGTCTGTC
CCAGAGAATGTGCTGAGTTTCGATGACCTTACTGCAGACGCTTTAGCTAACCTGAAAGTC
TCACAAATCAAAAAAGTCCGACTCCTCATTGATGAAGCCATCCTGAAGTGTGACGCGGAG
CGGATAAAGTTGGAAGCAGAGCGGTTTGAGAACCTCCGAGAGATTGGGAACCTTCTGCAC
CCTTCTGTACCCATCAGTAACGATGAGGATGTGGACAACAAAGTAGAGAGGATTTGGGGC
GATTGTACAGTCAGGAAGAAGTACTCTCATGTGGACCTGGTGGTGATGGTAGATGGCTTT
GAAGGCGAAAAGGGGGCCGTGGTGGCTGGGAGTCGAGGGTACTTCTTGAAGGGGGTCCTG
GTGTTCCTGGAACAGGCTCTCATCCAGTATGCCCTTCGCACCTTGGGAAGTCGGGGCTAC
ATTCCCATTTATACCCCCTTTTTCATGAGGAAGGAGGTCATGCAGGAGGTGGCACAGCTC
AGCCAGTTTGATGAAGAACTTTATAAGGTGATTGGCAAAGGCAGTGAAAAGTCTGATGAC
AACTCCTATGATGAGAAGTACCTGATTGCCACCTCAGAGCAGCCCATTGCTGCCCTGCAC
CGGGATGAGTGGCTCCGGCCGGAGGACCTGCCCATCAAGTATGCTGGCCTGTCTACCTGC
TTCCGTCAGGAGGTGGGCTCCCATGGCCGTGACACCCGTGGCATCTTCCGAGTCCATCAG
TTTGAGAAGATTGAACAGTTTGTGTACTCATCACCCCATGACAACAAGTCATGGGAGATG
TTTGAAGAGATGATTACCACCGCAGAGGAGTTCTACCAGTCCCTGGGGATTCCTTACCAC
ATTGTGAATATTGTCTCAGGTTCTTTGAATCATGCTGCCAGTAAGAAGCTTGACCTGGAG
GCCTGGTTTCCGGGCTCAGGAGCCTTCCGTGAGTTGGTCTCCTGTTCTAATTGCACGGAT
TACCAGGCTCGCCGGCTTCGAATCCGATATGGGCAAACCAAGAAGATGATGGACAAGGTG
GAGTTTGTCCATATGCTCAATGCTACCATGTGCGCCACTACCCGTACCATCTGCGCCATC
CTGGAGAACTACCAGACAGAGAAGGGCATCACTGTGCCTGAGAAATTGAAGGAGTTCATG
CCGCCAGGACTGCAAGAACTGATCCCCTTTGTGAAGCCTGCGCCCATTGAGCAGGAGCCA
TCAAAGAAGCAGAAGAAGCAACATGAGGGCAGCAAAAAGAAAGCAGCAGCAAGAGACGTC
ACCCTAGAAAACAGGCTGCAGAACATGGAGGTCACCGATGCTTGA

Enzyme 97 GenBank Gene ID

X91257

Enzyme 97 GeneCard ID

SARS

Enzyme 97 GenAtlas ID

SARS

Enzyme 97 HGNC ID

HGNC:10537 Link Image

Enzyme 97 Chromosome Location

Enzyme 97 Locus

1p13.3

Enzyme 97 SNPs

SNPJam Report Link Image

Enzyme 97 General References

Vincent C, Tarbouriech N, Hartlein M: Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase. Eur J Biochem. 1997 Nov 15;250(1):77-84. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 97 Metabolite References

Not Available

Enzyme 98 [top]

Enzyme 98 ID

5919

Enzyme 98 Name

Long-chain-fatty-acid--CoA ligase 3

Enzyme 98 Synonyms

Long-chain acyl-CoA synthetase 3
LACS 3

Enzyme 98 Gene Name

ACSL3

Enzyme 98 Protein Sequence

>Long-chain-fatty-acid--CoA ligase 3

MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPV
NSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPN
GKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACF
MYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGK
PPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMIS
HSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQ
SSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQI
SKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTES
AGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYY
KNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAA
LKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLK
VLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK

Enzyme 98 Number of Residues

720

Enzyme 98 Molecular Weight

80419.4

Enzyme 98 Theoretical pI

8.51

Enzyme 98 GO Classification

Function
catalytic activity
Process
metabolic process
Component
—

Enzyme 98 General Function

Involved in catalytic activity

Enzyme 98 Specific Function

Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 mediates hepatic lipogenesis. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates. Has mainly an anabolic role in energy metabolism. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins)

Enzyme 98 Pathways

Fatty Acid Metabolism (map00071 )

Enzyme 98 Reactions

ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]

Enzyme 98 Pfam Domain Function

AMP-binding (PF00501 )

Enzyme 98 Signals

None

Enzyme 98 Transmembrane Regions

21-41

Enzyme 98 Essentiality

Not Available

Enzyme 98 GenBank ID Protein

17026088

Enzyme 98 UniProtKB/Swiss-Prot ID

O95573

Enzyme 98 UniProtKB/Swiss-Prot Entry Name

ACSL3_HUMAN Link Image

Enzyme 98 PDB ID

Not Available

Enzyme 98 Cellular Location

Not Available

Enzyme 98 Gene Sequence

>2163 bp

ATGAATAACCACGTGTCTTCAAAACCATCTACCATGAAGCTAAAACATACCATCAACCCT
ATTCTTTTATATTTTATACATTTTCTAATATCACTTTATACTATTTTAACATACATTCCG
TTTTATTTTTTCTCCGAGTCAAGACAAGAAAAATCAAACCGAATTAAAGCAAAGCCTGTA
AATTCAAAACCTGATTCTGCATACAGATCTGTTAATAGTTTGGATGGTTTGGCTTCAGTA
TTATACCCTGGATGTGATACTTTAGATAAAGTTTTTACATATGCAAAAAACAAATTTAAG
AACAAAAGACTCTTGGGAACACGTGAAGTTTTAAATGAGGAAGATGAAGTACAACCAAAT
GGAAAAATTTTTAAAAAGGTTATTCTTGGACAGTATAATTGGCTTTCCTATGAAGATGTC
TTTGTTCGAGCCTTTAATTTTGGAAATGGATTACAGATGTTGGGTCAGAAACCAAAGACC
AACATCGCCATCTTCTGTGAGACCAGGGCCGAGTGGATGATAGCTGCACAGGCGTGTTTT
ATGTATAATTTTCAGCTTGTTACATTATATGCCACTCTAGGAGGTCCAGCCATTGTTCAT
GCATTAAATGAAACAGAGGTGACCAACATCATTACTAGTAAAGAACTCTTACAAACAAAG
TTGAAGGATATAGTTTCTTTGGTCCCACGCCTGCGGCACATCATCACTGTTGATGGAAAG
CCACCGACCTGGTCCGACTTCCCCAAGGGCATCATTGTGCATACCATGGCTGCAGTGGAG
GCCCTGGGAGCCAAGGCCAGCATGGAAAACCAACCTCATAGCAAACCATTGCCCTCAGAT
ATTGCAGTAATCATGTACACAAGTGGATCCACAGGACTTCCAAAGGGAGTCATGATCTCA
CATAGTAACATTATTGCTGGTATAACTGGGATGGCAGAAAGGATTCCAGAACTAGGAGAG
GAAGATGTCTACATTGGATATTTGCCTCTGGCCCATGTTCTAGAATTAAGTGCTGAGCTT
GTCTGTCTTTCTCACGGATGCCGCATTGGTTACTCTTCACCACAGACTTTAGCAGATCAG
TCTTCAAAAATTAAAAAAGGAAGCAAAGGGGATACATCCATGTTGAAACCAACACTGATG
GCAGCAGTTCCGGAAATCATGGATCGGATCTACAAAAATGTCATGAATAAAGTCAGTGAA
ATGAGTAGTTTTCAACGTAATCTGTTTATTCTGGCCTATAATTACAAAATGGAACAGATT
TCAAAAGGACGTAATACTCCACTGTGCGACAGCTTTGTTTTCCGGAAAGTTCGAAGCTTG
CTAGGGGGAAATATTCGTCTCCTGTTGTGTGGTGGCGCTCCACTTTCTGCAACCACGCAG
CGATTCATGAACATCTGTTTCTGCTGTCCTGTTGGTCAGGGATACGGGCTCACTGAATCT
GCTGGGGCTGGAACAATTTCCGAAGTGTGGGACTACAATACTGGCAGAGTGGGAGCACCA
TTAGTTTGCTGTGAAATCAAATTAAAAAACTGGGAGGAAGGTGGATACTTTAATACTGAT
AAGCCACACCCCAGGGGTGAAATTCTTATTGGGGGCCAAAGTGTGACAATGGGGTACTAC
AAAAATGAAGCAAAAACAAAAGCTGATTTCTCTGAAGATGAAAATGGACAAAGGTGGCTC
TGTACTGGGGATATTGGAGAGTTTGAACCCGATGGATGCTTAAAGATTATTGATCGTAAA
AAGGACCTTGTAAAACTACAGGCAGGGGAATATGTTTCTCTTGGGAAAGTAGAGGCAGCT
TTGAAGAATCTTCCACTAGTAGATAACATTTGTGCATATGCAAACAGTTATCATTCTTAT
GTCATTGGATTTGTTGTGCCAAATCAAAAGGAACTAACTGAACTAGCTCGAAAGAAAGGA
CTTAAAGGGACTTGGGAGGAGCTGTGTAACAGTTGTGAAATGGAAAATGAGGTACTTAAA
GTGCTTTCCGAAGCTGCTATTTCAGCAAGTCTGGAAAAGTTTGAAATTCCAGTAAAAATT
CGTTTGAGTCCTGAACCGTGGACCCCTGAAACTGGTCTGGTGACAGATGCCTTCAAGCTG
AAACGCAAAGAGCTTAAAACACATTACCAGGCGGACATTGAGCGAATGTATGGAAGAAAA
TAA

Enzyme 98 GenBank Gene ID

AB061436

Enzyme 98 GeneCard ID

ACSL3

Enzyme 98 GenAtlas ID

ACSL3

Enzyme 98 HGNC ID

HGNC:3570

Enzyme 98 Chromosome Location

Enzyme 98 Locus

2q34-q35

Enzyme 98 SNPs

SNPJam Report Link Image

Enzyme 98 General References

Minekura H, Fujino T, Kang MJ, Fujita T, Endo Y, Yamamoto TT: Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35. Genomics. 1997 May 15;42(1):180-1. [PubMed ]
Minekura H, Kang MJ, Inagaki Y, Suzuki H, Sato H, Fujino T, Yamamoto TT: Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene. Gene. 2001 Oct 31;278(1-2):185-92. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
Yao H, Ye J: Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine synthesis is required for assembly of very low density lipoproteins in human hepatoma Huh7 cells. J Biol Chem. 2008 Jan 11;283(2):849-54. Epub 2007 Nov 14. [PubMed ]
Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]

Enzyme 98 Metabolite References

Not Available

Enzyme 99 [top]

Enzyme 99 ID

5921

Enzyme 99 Name

Ubiquitin-conjugating enzyme E2 C

Enzyme 99 Synonyms

UbcH10
Ubiquitin carrier protein C
Ubiquitin-protein ligase C

Enzyme 99 Gene Name

UBE2C

Enzyme 99 Protein Sequence

>Ubiquitin-conjugating enzyme E2 C

MASQNRDPAATSVAAARKGAEPSGGAARGPVGKRLQQELMTLMMSGDKGISAFPESDNLF
KWVGTIHGAAGTVYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNICLDILKE
KWSALYDVRTILLSIQSLLGEPNIDSPLNTHAAELWKNPTAFKKYLQETYSKQVTSQEP

Enzyme 99 Number of Residues

179

Enzyme 99 Molecular Weight

19652.1

Enzyme 99 Theoretical pI

7.50

Enzyme 99 GO Classification

Function
ATP binding acid-amino acid ligase activity adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds nucleoside binding purine nucleoside binding small conjugating protein ligase activity ubiquitin-protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification by small protein conjugation protein modification by small protein conjugation or removal protein modification process protein ubiquitination regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 99 General Function

Involved in ubiquitin-protein ligase activity

Enzyme 99 Specific Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit

Enzyme 99 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 99 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 99 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 99 Signals

None

Enzyme 99 Transmembrane Regions

None

Enzyme 99 Essentiality

Not Available

Enzyme 99 GenBank ID Protein

5902146

Enzyme 99 UniProtKB/Swiss-Prot ID

O00762

Enzyme 99 UniProtKB/Swiss-Prot Entry Name

UBE2C_HUMAN Link Image

Enzyme 99 PDB ID

1I7K

Enzyme 99 PDB File

Show

Enzyme 99 3D Structure

Enzyme 99 Cellular Location

Not Available

Enzyme 99 Gene Sequence

>540 bp

ATGGCTTCCCAAAACCGCGACCCAGCCGCCACTAGCGTCGCCGCCGCCCGTAAAGGAGCT
GAGCCGAGCGGGGGCGCCGCCCGGGGTCCGGTGGGCAAAAGGCTACAGCAGGAGCTGATG
ACCCTCATGATGTCTGGCGATAAAGGGATTTCTGCCTTCCCTGAATCAGACAACCTTTTC
AAATGGGTAGGGACCATCCATGGAGCAGCTGGAACAGTATATGAAGACCTGAGGTATAAG
CTCTCGCTAGAGTTCCCCAGTGGCTACCCTTACAATGCGCCCACAGTGAAGTTCCTCACG
CCCTGCTATCACCCCAACGTGGACACCCAGGGTAACATATGCCTGGACATCCTGAAGGAA
AAGTGGTCTGCCCTGTATGATGTCAGGACCATTCTGCTCTCCATCCAGAGCCTTCTAGGA
GAACCCAACATTGATAGTCCCTTGAACACACATGCTGCCGAGCTCTGGAAAAACCCCACA
GCTTTTAAGAAGTACCTGCAAGAAACCTACTCAAAGCAGGTCACCAGCCAGGAGCCCTGA

Enzyme 99 GenBank Gene ID

NM_007019.2 Link Image

Enzyme 99 GeneCard ID

UBE2C

Enzyme 99 GenAtlas ID

UBE2C

Enzyme 99 HGNC ID

HGNC:15937 Link Image

Enzyme 99 Chromosome Location

Enzyme 99 Locus

20q13.12

Enzyme 99 SNPs

SNPJam Report Link Image

Enzyme 99 General References

Townsley FM, Aristarkhov A, Beck S, Hershko A, Ruderman JV: Dominant-negative cyclin-selective ubiquitin carrier protein E2-C/UbcH10 blocks cells in metaphase. Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2362-7. [PubMed ]
Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Rape M, Kirschner MW: Autonomous regulation of the anaphase-promoting complex couples mitosis to S-phase entry. Nature. 2004 Dec 2;432(7017):588-95. Epub 2004 Nov 21. [PubMed ]
Jin L, Williamson A, Banerjee S, Philipp I, Rape M: Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex. Cell. 2008 May 16;133(4):653-65. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Garnett MJ, Mansfeld J, Godwin C, Matsusaka T, Wu J, Russell P, Pines J, Venkitaraman AR: UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic exit. Nat Cell Biol. 2009 Nov;11(11):1363-9. Epub 2009 Oct 11. [PubMed ]
Williamson A, Wickliffe KE, Mellone BG, Song L, Karpen GH, Rape M: Identification of a physiological E2 module for the human anaphase-promoting complex. Proc Natl Acad Sci U S A. 2009 Oct 27;106(43):18213-8. Epub 2009 Oct 12. [PubMed ]
David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
Lin Y, Hwang WC, Basavappa R: Structural and functional analysis of the human mitotic-specific ubiquitin-conjugating enzyme, UbcH10. J Biol Chem. 2002 Jun 14;277(24):21913-21. Epub 2002 Apr 1. [PubMed ]

Enzyme 99 Metabolite References

Not Available

Enzyme 100 [top]

Enzyme 100 ID

5922

Enzyme 100 Name

cAMP-specific 3',5'-cyclic phosphodiesterase 4A

Enzyme 100 Synonyms

DPDE2
PDE46

Enzyme 100 Gene Name

PDE4A

Enzyme 100 Protein Sequence

>cAMP-specific 3',5'-cyclic phosphodiesterase 4A

MEPPTVPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERAERERQ
PHRPIERADAMDTSDRPGLRTTRMSWPSSFHGTGTGSGGAGGGSSRRFEAENGPTPSPGR
SPLDSQASPGLVLHAGAATSQRRESFLYRSDSDYDMSPKTMSRNSSVTSEAHAEDLIVTP
FAQVLASLRSVRSNFSLLTNVPVPSNKRSPLGGPTPVCKATLSEETCQQLARETLEELDW
CLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISTTFLDKQNEVEI
PSPTMKEREKQQAPRPRPSQPPPPPVPHLQPMSQITGLKKLMHSNSLNNSNIPRFGVKTD
QEELLAQELENLNKWGLNIFCVSDYAGGRSLTCIMYMIFQERDLLKKFRIPVDTMVTYML
TLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGV
SNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEDNCDIFQNLSKRQRQSLRKMVIDM
VLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLE
LYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADL
VHPDAQEILDTLEDNRDWYYSAIRQSPSPPPEEESRGPGHPPLPDKFQFELTLEEEEEEE
ISMAQIPCTAQEALTAQGLSGVEEALDATIAWEASPAQESLEVMAQEASLEAELEAVYLT
QQAQSTGSAPVAPDEFSSREEFVVAVSHSSPSALALQSPLLPAWRTLSVSEHAPGLPGLP
STAAEVEAQREHQAAKRACSACAGTFGEDTSALPAPGGGGSGGDPT

Enzyme 100 Number of Residues

886

Enzyme 100 Molecular Weight

98142.2

Enzyme 100 Theoretical pI

4.87

Enzyme 100 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 100 General Function

Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity

Enzyme 100 Specific Function

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes

Enzyme 100 Pathways

Purine Metabolism (map00230 )

Enzyme 100 Reactions

nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]

Enzyme 100 Pfam Domain Function

PDEase_I (PF00233 )

Enzyme 100 Signals

None

Enzyme 100 Transmembrane Regions

None

Enzyme 100 Essentiality

Not Available

Enzyme 100 GenBank ID Protein

Not Available

Enzyme 100 UniProtKB/Swiss-Prot ID

P27815

Enzyme 100 UniProtKB/Swiss-Prot Entry Name

PDE4A_HUMAN Link Image

Enzyme 100 PDB ID

Not Available

Enzyme 100 Cellular Location

Not Available

Enzyme 100 Gene Sequence

>2661 bp

ATGGAACCCCCGACCGTCCCCTCGGAAAGGAGCCTGTCTCTGTCACTGCCCGGGCCCCGG
GAGGGCCAGGCCACCCTGAAGCCTCCCCCGCAGCACCTGTGGCGGCAGCCTCGGACCCCC
ATCCGTATCCAGCAGCGCGGCTACTCCGACAGCGCGGAGCGCGCCGAGCGGGAGCGGCAG
CCGCACCGGCCCATAGAGCGCGCCGATGCCATGGACACCAGCGACCGGCCCGGCCTGCGC
ACGACCCGCATGTCCTGGCCCTCGTCCTTCCATGGCACTGGCACCGGCAGCGGCGGCGCG
GGCGGAGGCAGCAGCAGGCGCTTCGAGGCAGAGAATGGGCCGACACCATCTCCTGGCCGC
AGCCCCCTGGACTCGCAGGCGAGCCCAGGACTCGTGCTGCACGCCGGGGCGGCCACCAGC
CAGCGCCGGGAGTCCTTCCTGTACCGCTCAGACAGCGACTATGACATGTCACCCAAGACC
ATGTCCCGGAACTCATCGGTCACCAGCGAGGCGCACGCTGAAGACCTCATCGTAACACCA
TTTGCTCAGGTGCTGGCCAGCCTCCGGAGCGTCCGTAGCAACTTCTCACTCCTGACCAAT
GTGCCCGTTCCCAGTAACAAGCGGTCCCCGCTGGGCGGCCCCACCCCTGTCTGCAAGGCC
ACGCTGTCAGAAGAAACGTGTCAGCAGTTGGCCCGGGAGACTCTGGAGGAGCTGGACTGG
TGTCTGGAGCAGCTGGAGACCATGCAGACCTATCGCTCTGTCAGCGAGATGGCCTCGCAC
AAGTTCAAAAGGATGTTGAACCGTGAGCTCACACACCTGTCAGAAATGAGCAGGTCCGGA
AACCAGGTCTCAGAGTACATTTCCACAACATTCCTGGACAAACAGAATGAAGTGGAGATC
CCATCACCCACGATGAAGGAACGAGAAAAACAGCAAGCGCCGCGACCAAGACCCTCCCAG
CCGCCCCCGCCCCCTGTACCACACTTACAGCCCATGTCCCAAATCACAGGGTTGAAAAAG
TTGATGCATAGTAACAGCCTGAACAACTCTAACATTCCCCGATTTGGGGTGAAGACCGAT
CAAGAAGAGCTCCTGGCCCAAGAACTGGAGAACCTGAACAAGTGGGGCCTGAACATCTTT
TGCGTGTCGGATTACGCTGGAGGCCGCTCACTCACCTGCATCATGTACATGATATTCCAG
GAGCGGGACCTGCTGAAGAAATTCCGCATCCCGGTGGACACGATGGTGACATACATGCTG
ACGCTGGAGGATCACTACCACGCTGACGTGGCCTACCATAACAGCCTGCACGCAGCTGAC
GTGCTGCAGTCCACCCACGTACTGCTGGCCACGCCTGCACTAGATGCAGTGTTCACGGAC
CTGGAGATTCTCGCCGCCCTCTTCGCGGCTGCCATCCACGATGTGGATCACCCTGGGGTC
TCCAACCAGTTCCTCATCAACACCAATTCGGAGCTGGCGCTCATGTACAACGATGAGTCG
GTGCTCGAGAATCACCACCTGGCCGTGGGCTTCAAGCTGCTGCAGGAGGACAACTGCGAC
ATCTTCCAGAACCTCAGCAAGCGCCAGCGGCAGAGCCTACGCAAGATGGTCATCGACATG
GTGCTGGCCACGGACATGTCCAAGCACATGACCCTCCTGGCTGACCTGAAGACCATGGTG
GAGACCAAGAAAGTGACCAGCTCAGGGGTCCTCCTGCTAGATAACTACTCCGACCGCATC
CAGGTCCTCCGGAACATGGTGCACTGTGCCGACCTCAGCAACCCCACCAAGCCGCTGGAG
CTGTACCGCCAGTGGACAGACCGCATCATGGCCGAGTTCTTCCAGCAGGGTGACCGAGAG
CGCGAGCGTGGCATGGAAATCAGCCCCATGTGTGACAAGCACACTGCCTCCGTGGAGAAG
TCTCAGGTGGGTTTTATTGACTACATTGTGCACCCATTGTGGGAGACCTGGGCGGACCTT
GTCCACCCAGATGCCCAGGAGATCTTGGACACTTTGGAGGACAACCGGGACTGGTACTAC
AGCGCCATCCGGCAGAGCCCATCTCCGCCACCCGAGGAGGAGTCAAGGGGGCCAGGCCAC
CCACCCCTGCCTGACAAGTTCCAGTTTGAGCTGACGCTGGAGGAGGAAGAGGAGGAAGAA
ATATCAATGGCCCAGATACCGTGCACAGCCCAAGAGGCATTGACTGCGCAGGGATTGTCA
GGAGTCGAGGAAGCTCTGGATGCAACCATAGCCTGGGAGGCATCCCCGGCCCAGGAGTCG
TTGGAAGTTATGGCACAGGAAGCATCCCTGGAGGCCGAGCTGGAGGCAGTGTATTTGACA
CAGCAGGCACAGTCCACAGGCAGTGCACCTGTGGCTCCGGATGAGTTCTCGTCCCGGGAG
GAATTCGTGGTTGCTGTAAGCCACAGCAGCCCCTCTGCCCTGGCTCTTCAAAGCCCCCTT
CTCCCTGCTTGGAGGACCCTGTCTGTTTCAGAGCATGCCCCGGGCCTCCCGGGCCTCCCC
TCCACGGCGGCCGAGGTGGAGGCCCAACGAGAGCACCAGGCTGCCAAGAGGGCTTGCAGT
GCCTGCGCAGGGACATTTGGGGAGGACACATCCGCACTCCCAGCTCCTGGTGGCGGGGGG
TCAGGTGGAGACCCTACCTGA

Enzyme 100 GenBank Gene ID

L20965

Enzyme 100 GeneCard ID

PDE4A

Enzyme 100 GenAtlas ID

PDE4A

Enzyme 100 HGNC ID

HGNC:8780

Enzyme 100 Chromosome Location

Enzyme 100 Locus

19p13.2

Enzyme 100 SNPs

SNPJam Report Link Image

Enzyme 100 General References

Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed ]
Sullivan M, Egerton M, Shakur Y, Marquardsen A, Houslay MD: Molecular cloning and expression, in both COS-1 cells and S. cerevisiae, of a human cytosolic type-IVA, cyclic AMP specific phosphodiesterase (hPDE-IVA-h6.1). Cell Signal. 1994 Sep;6(7):793-812. [PubMed ]
Horton YM, Sullivan M, Houslay MD: Molecular cloning of a novel splice variant of human type IVA (PDE-IVA) cyclic AMP phosphodiesterase and localization of the gene to the p13.2-q12 region of human chromosome 19 [corrected] Biochem J. 1995 Jun 1;308 ( Pt 2):683-91. [PubMed ]
Sullivan M, Rena G, Begg F, Gordon L, Olsen AS, Houslay MD: Identification and characterization of the human homologue of the short PDE4A cAMP-specific phosphodiesterase RD1 (PDE4A1) by analysis of the human HSPDE4A gene locus located at chromosome 19p13.2. Biochem J. 1998 Aug 1;333 ( Pt 3):693-703. [PubMed ]
Rena G, Begg F, Ross A, MacKenzie C, McPhee I, Campbell L, Huston E, Sullivan M, Houslay MD: Molecular cloning, genomic positioning, promoter identification, and characterization of the novel cyclic amp-specific phosphodiesterase PDE4A10. Mol Pharmacol. 2001 May;59(5):996-1011. [PubMed ]
Wallace DA, Johnston LA, Huston E, MacMaster D, Houslay TM, Cheung YF, Campbell L, Millen JE, Smith RA, Gall I, Knowles RG, Sullivan M, Houslay MD: Identification and characterization of PDE4A11, a novel, widely expressed long isoform encoded by the human PDE4A cAMP phosphodiesterase gene. Mol Pharmacol. 2005 Jun;67(6):1920-34. Epub 2005 Feb 28. [PubMed ]
Mackenzie KF, Topping EC, Bugaj-Gaweda B, Deng C, Cheung YF, Olsen AE, Stockard CR, High Mitchell L, Baillie GS, Grizzle WE, De Vivo M, Houslay MD, Wang D, Bolger GB: Human PDE4A8, a novel brain-expressed PDE4 cAMP-specific phosphodiesterase that has undergone rapid evolutionary change. Biochem J. 2008 Apr 15;411(2):361-9. [PubMed ]
Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Livi GP, Kmetz P, McHale MM, Cieslinski LB, Sathe GM, Taylor DP, Davis RL, Torphy TJ, Balcarek JM: Cloning and expression of cDNA for a human low-Km, rolipram-sensitive cyclic AMP phosphodiesterase. Mol Cell Biol. 1990 Jun;10(6):2678-86. [PubMed ]
Lario PI, Bobechko B, Bateman K, Kelly J, Vrielink A, Huang Z: Purification and characterization of the human PDE4A catalytic domain (PDE4A330-723) expressed in Sf9 cells. Arch Biochem Biophys. 2001 Oct 1;394(1):54-60. [PubMed ]
Hillman RT, Green RE, Brenner SE: An unappreciated role for RNA surveillance. Genome Biol. 2004;5(2):R8. Epub 2004 Feb 2. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed ]

Enzyme 100 Metabolite References

Not Available

Enzyme 101 [top]

Enzyme 101 ID

5923

Enzyme 101 Name

Valyl-tRNA synthetase

Enzyme 101 Synonyms

Protein G7a
Valine--tRNA ligase
ValRS

Enzyme 101 Gene Name

VARS

Enzyme 101 Protein Sequence

>Valyl-tRNA synthetase

MSTLYVSPHPDAFPSLRALIAARYGEAGEGPGWGGAHPRICLQPPPTSRTPFPPPRLPAL
EQGPGGLWVWGATAVAQLLWPAGLGGPGGSRAAVLVQQWVSYADTELIPAACGATLPALG
LRSSAQDPQAVLGALGRALSPLEEWLRLHTYLAGEAPTLADLAAVTALLLPFRYVLDPPA
RRIWNNVTRWFVTCVRQPEFRAVLGEVVLYSGARPLSHQPGPEAPALPKTAAQLKKEAKK
REKLEKFQQKQKIQQQQPPPGEKKPKPEKREKRDPGVITYDLPTPPGEKKDVSGPMPDSY
SPRYVEAAWYPWWEQQGFFKPEYGRPNVSAANPRGVFMMCIPPPNVTGSLHLGHALTNAI
QDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWREQGLSRHQLGREAFLQEVWKWK
EEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCT
LNSAISDIEVDKKELTGRTLLSVPGYKEKVEFGVLVSFAYKVQGSDSDEEVVVATTRIET
MLGDVAVAVHPKDTRYQHLKGKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQND
YEVGQRHGLEAISIMDSRGALINVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVV
PLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHAWMDNIREWC
ISRQLWWGHRIPAYFVTVSDPAVPPGEDPDGRYWVSGRNEAEAREKAAKEFGVSPDKISL
QQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKL
TGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIYGISLQGLHNQLLNSNLDPSEVE
KAKEGQKADFPAGIPECGTDALRFGLCAYMSQGRDINLDVNRILGYRHFCNKLWNATKFA
LRGLGKGFVPSPTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSFWLY
ELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRMP
QAPPSLCVTPYPEPSECSWKDPEAEAALELALSITRAVRSLRADYNLTRIRPDCFLEVAD
EATGALASAVSGYVQALASAGVVAVLALGAPAPQGCAVALASDRCSIHLQLQGLVDPARE
LGKLQAKRVEAQRQAQRLRERRAASGYPVKVPLEVQEADEAKLQQTEAELRKVDEAIALF
QKML

Enzyme 101 Number of Residues

1264

Enzyme 101 Molecular Weight

140474.8

Enzyme 101 Theoretical pI

7.63

Enzyme 101 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding valine-tRNA ligase activity
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation valyl-tRNA aminoacylation
Component
cell part cytoplasm intracellular part

Enzyme 101 General Function

Involved in nucleotide binding

Enzyme 101 Specific Function

ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)

Enzyme 101 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )

Enzyme 101 Reactions

ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal [RN:R03665]

Enzyme 101 Pfam Domain Function

Anticodon_1 (PF08264 )
GST_C (PF00043 )
GST_N (PF02798 )
tRNA-synt_1 (PF00133 )

Enzyme 101 Signals

None

Enzyme 101 Transmembrane Regions

None

Enzyme 101 Essentiality

Not Available

Enzyme 101 GenBank ID Protein

4529896

Enzyme 101 UniProtKB/Swiss-Prot ID

P26640

Enzyme 101 UniProtKB/Swiss-Prot Entry Name

SYVC_HUMAN Link Image

Enzyme 101 PDB ID

Not Available

Enzyme 101 Cellular Location

Not Available

Enzyme 101 Gene Sequence

>3795 bp

ATGTCCACCCTCTACGTCTCCCCTCACCCAGATGCCTTCCCCAGCCTCCGAGCCCTCATA
GCCGCTCGCTATGGGGAGGCTGGGGAGGGTCCCGGATGGGGAGGAGCCCACCCCCGCATC
TGTCTCCAGCCACCCCCGACTAGCAGGACTCCCTTTCCCCCACCCCGCCTGCCGGCCCTG
GAGCAGGGGCCCGGTGGGCTCTGGGTGTGGGGGGCCACGGCTGTGGCCCAGCTGCTGTGG
CCAGCAGGCCTGGGGGGCCCAGGGGGCAGCCGGGCGGCTGTCCTTGTCCAACAGTGGGTC
AGTTACGCCGACACGGAGTTAATACCAGCTGCCTGTGGAGCAACGCTGCCGGCCCTGGGA
CTCCGAAGCTCGGCCCAGGACCCCCAGGCTGTGCTGGGGGCCCTGGGCAGGGCCCTGAGC
CCCTTGGAGGAGTGGCTTCGGCTGCACACCTACTTGGCCGGGGAGGCCCCCACTCTGGCT
GACCTGGCGGCTGTCACAGCCTTGCTGCTGCCTTTCCGATACGTCCTAGACCCACCTGCC
CGCCGGATCTGGAATAATGTGACTCGCTGGTTTGTCACGTGTGTCCGGCAGCCAGAATTC
CGAGCCGTGCTAGGAGAAGTGGTTCTATACTCAGGAGCCAGGCCTCTCTCTCATCAGCCA
GGCCCCGAGGCTCCTGCCCTCCCAAAGACAGCTGCTCAGCTCAAGAAAGAGGCAAAGAAA
CGGGAGAAGCTAGAGAAATTCCAACAGAAGCAGAAGATCCAACAGCAGCAGCCACCTCCA
GGGGAGAAGAAACCAAAACCAGAGAAGAGGGAGAAACGGGATCCTGGGGTCATTACCTAT
GACCTCCCAACCCCACCCGGGGAAAAGAAAGATGTCAGTGGCCCCATGCCCGACTCCTAC
AGCCCTCGGTATGTGGAGGCTGCCTGGTACCCTTGGTGGGAGCAGCAGGGCTTCTTCAAG
CCAGAGTATGGGCGTCCTAATGTGTCAGCAGCAAATCCCCGAGGTGTCTTCATGATGTGC
ATCCCACCCCCCAATGTGACAGGCTCCCTGCACCTGGGCCATGCACTCACCAACGCCATC
CAGGACTCCCTGACTCGATGGCACCGCATGCGTGGGGAGACCACCCTGTGGAACCCTGGC
TGTGACCATGCAGGTATTGCCACCCAGGTGGTGGTGGAGAAGAAGCTATGGCGTGAGCAG
GGACTGAGCCGGCACCAGCTGGGCCGCGAGGCCTTTCTACAGGAAGTCTGGAAGTGGAAG
GAGGAGAAAGGTGACCGGATTTACCACCAGTTGAAGAAGCTTGGCAGCTCCTTGGACTGG
GATCGAGCCTGTTTCACCATGGACCCTAAACTCTCAGCAGCTGTGACAGAGGCCTTTGTC
CGGCTTCACGAGGAAGGCATCATCTATCGCAGTACCCGCCTTGTTAACTGGTCCTGCACC
CTCAACTCCGCCATCTCTGACATTGAGGTGGATAAGAAGGAGCTGACAGGTCGCACCCTG
CTCTCCGTGCCTGGCTACAAGGAGAAGGTGGAGTTCGGGGTCCTCGTGTCCTTTGCCTAT
AAGGTCCAAGGCTCAGATAGCGACGAGGAGGTGGTGGTGGCAACAACTCGGATCGAGACA
ATGCTGGGAGATGTGGCTGTAGCTGTGCACCCCAAAGATACCAGATACCAGCACCTGAAG
GGGAAGAACGTGATCCACCCATTCCTGTCTCGGAGCCTTCCCATTGTCTTCGATGAATTT
GTGGACATGGACTTTGGCACAGGTGCTGTGAAGATCACCCCCGCACATGACCAAAATGAC
TATGAAGTTGGGCAGCGGCACGGGCTGGAGGCCATCAGCATCATGGACTCCCGGGGGGCC
CTCATCAATGTGCCTCCGCCTTTCCTGGGCCTGCCCAGGTTTGAGGCCAGGAAAGCGGTG
CTGGTGGCGCTGAAGGAGCGGGGACTGTTCCGTGGCATTGAGGACAACCCCATGGTGGTG
CCACTTTGCAACCGGTCGAAGGACGTGGTAGAGCCTCTGCTGCGGCCGCAGTGGTACGTT
CGCTGCGGGGAGATGGCCCAGGCTGCCAGCGCCGCTGTGACTCGGGGTGACCTCCGCATC
CTGCCTGAGGCCCATCAGCGCACATGGCATGCCTGGATGGACAACATCCGGGAGTGGTGC
ATTTCCAGGCAGCTGTGGTGGGGCCATCGCATCCCAGCCTACTTTGTCACTGTCAGTGAC
CCAGCGGTGCCCCCTGGGGAGGACCCTGATGGGCGGTACTGGGTGAGTGGACGCAATGAG
GCGGAGGCCCGGGAGAAGGCAGCCAAGGAGTTCGGAGTGTCCCCTGACAAGATCAGTCTC
CAGCAAGATGAGGATGTATTGGATACCTGGTTCTCCTCTGGCCTCTTCCCCTTATCCATT
TTGGGCTGGCCCAACCAGTCAGAAGACCTGAGTGTGTTCTACCCCGGGACACTGCTGGAG
ACCGGTCATGACATCCTCTTCTTCTGGGTGGCCCGGATGGTCATGCTGGGCCTGAAGCTC
ACGGGCAGGCTGCCCTTTAGAGAGGTCTACCTCCATGCCATCGTGCGAGATGCTCACGGC
CGGAAGATGAGCAAGTCTCTAGGCAATGTCATCGATCCCCTGGATGTCATCTATGGAATC
TCCCTGCAGGGCCTCCACAACCAGCTGCTGAACAGCAACCTGGATCCCAGCGAGGTGGAG
AAGGCCAAAGAAGGGCAGAAAGCTGACTTCCCAGCGGGGATTCCTGAATGTGGCACCGAT
GCTCTCCGGTTTGGATTATGTGCCTACATGTCCCAGGGTCGTGACATCAACCTGGATGTG
AACCGGATACTGGGTTACCGCCACTTCTGCAACAAGCTCTGGAATGCCACCAAGTTTGCC
CTTCGTGGCCTTGGGAAGGGTTTTGTGCCCTCACCCACCTCCCAGCCCGGAGGCCATGAG
AGCCTGGTGGACCGCTGGATCCGCAGCCGCCTGACAGAGGCTGTGAGGCTCAGCAATCAA
GGCTTCCAGGCCTACGACTTCCCGGCCGTCACCACTGCCCAGTACAGCTTCTGGCTCTAT
GAGCTCTGTGATGTCTACTTGGAGTGCCTGAAACCTGTACTGAATGGGGTGGACCAGGTG
GCAGCTGAGTGTGCCCGCCAGACCCTGTACACTTGCCTGGACGTTGGCCTGCGGCTGCTC
TCACCCTTCATGCCCTTCGTGACGGAGGAGCTGTTCCAGAGGCTGCCCCGGAGGATGCCG
CAAGCTCCCCCTAGCCTCTGTGTTACCCCCTACCCGGAGCCCTCAGAGTGCTCCTGGAAG
GACCCCGAGGCAGAAGCCGCCCTTGAGCTGGCGCTAAGCATCACGCGAGCCGTGCGCTCC
CTGCGGGCCGACTACAACCTCACCCGGATCCGGCCTGACTGTTTCCTGGAAGTGGCGGAT
GAGGCCACGGGCGCCCTGGCATCGGCGGTGTCGGGCTACGTGCAGGCCCTGGCCAGCGCA
GGTGTGGTGGCTGTTCTGGCCCTGGGGGCTCCCGCCCCCCAGGGTTGCGCTGTGGCTCTG
GCTTCTGATCGCTGCTCCATCCACCTGCAGCTTCAGGGGCTGGTGGACCCTGCACGGGAG
CTGGGCAAGCTGCAAGCCAAGCGAGTTGAGGCCCAGCGGCAGGCCCAGCGTCTGCGGGAA
CGCCGTGCTGCCTCGGGCTATCCTGTCAAGGTGCCGCTCGAAGTCCAGGAGGCAGATGAA
GCCAAGCTCCAACAGACAGAAGCAGAGCTCAGGAAGGTGGATGAGGCCATCGCCCTATTC
CAGAAGATGCTGTGA

Enzyme 101 GenBank Gene ID

AF134726

Enzyme 101 GeneCard ID

VARS

Enzyme 101 GenAtlas ID

VARS

Enzyme 101 HGNC ID

HGNC:12651 Link Image

Enzyme 101 Chromosome Location

Enzyme 101 Locus

6p21.3

Enzyme 101 SNPs

SNPJam Report Link Image

Enzyme 101 General References

Hsieh SL, Campbell RD: Evidence that gene G7a in the human major histocompatibility complex encodes valyl-tRNA synthetase. Biochem J. 1991 Sep 15;278 ( Pt 3):809-16. [PubMed ]
Xie T, Rowen L, Aguado B, Ahearn ME, Madan A, Qin S, Campbell RD, Hood L: Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. Genome Res. 2003 Dec;13(12):2621-36. [PubMed ]
Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Vilalta A, Donovan D, Wood L, Vogeli G, Yang DC: Cloning, sequencing and expression of a cDNA encoding mammalian valyl-tRNA synthetase. Gene. 1993 Jan 30;123(2):181-6. [PubMed ]
Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 101 Metabolite References

Not Available

Enzyme 102 [top]

Enzyme 102 ID

5924

Enzyme 102 Name

Adenylate kinase isoenzyme 5

Enzyme 102 Synonyms

AK 5
ATP-AMP transphosphorylase 5

Enzyme 102 Gene Name

AK5

Enzyme 102 Protein Sequence

>Adenylate kinase isoenzyme 5

MNTNDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKELGGCDKVKWDTFV
SQEKKTLPPLNGGQSRRSFLRNVMPENSNFPYRRYDRLPPIHQFSIESDTDLSETAELIE
EYEVFDPTRPRPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKW
SLIAKIITTGELAPQETTITEIKQKLMQIPDEEGIVIDGFPRDVAQALSFEDQICTPDLV
VFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDA
DRDEDEVFYDISMAVDNKLFPNKEAAAGSSDLDPSMILDTGEIIDTGSDYEDQGDDQLNV
FGEDTMGGFMEDLRKCKIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESE
RSKLIRDIMERGDLVPSGIVLELLKEAMVASLGDTRGFLIDGYPREVKQGEEFGRRIGDP
QLVICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHK
INAEGTPEDVFLQLCTAIDSIF

Enzyme 102 Number of Residues

562

Enzyme 102 Molecular Weight

63332.4

Enzyme 102 Theoretical pI

4.69

Enzyme 102 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding adenylate kinase activity binding catalytic activity kinase activity nucleobase, nucleoside, nucleotide kinase activity nucleoside binding phosphotransferase activity, phosphate group as acceptor purine nucleoside binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
ATP metabolic process cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside phosphate metabolic process nucleotide metabolic process purine nucleoside triphosphate metabolic process purine nucleotide metabolic process purine ribonucleoside triphosphate metabolic process
Component
cell part cytoplasm intracellular part

Enzyme 102 General Function

Involved in ATP binding

Enzyme 102 Specific Function

Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP

Enzyme 102 Pathways

Purine Metabolism (map00230 )

Enzyme 102 Reactions

ATP + AMP = 2 ADP [RN:R00127]

Enzyme 102 Pfam Domain Function

ADK (PF00406 )
Dpy-30 (PF05186 )

Enzyme 102 Signals

None

Enzyme 102 Transmembrane Regions

None

Enzyme 102 Essentiality

Not Available

Enzyme 102 GenBank ID Protein

28144897

Enzyme 102 UniProtKB/Swiss-Prot ID

Q9Y6K8

Enzyme 102 UniProtKB/Swiss-Prot Entry Name

KAD5_HUMAN Link Image

Enzyme 102 PDB ID

Not Available

Enzyme 102 Cellular Location

Not Available

Enzyme 102 Gene Sequence

>1689 bp

ATGAACACCAACGATGCCAAGGAGTATCTGGCCCGGAGGGAAATCCCTCAGCTTTTTGAG
AGCCTTTTGAATGGACTGATGTGTTCTAAGCCCGAAGATCCAGTAGAATACTTGGAAAGT
TGTTTACAAAAAGTAAAGGAACTGGGTGGCTGTGACAAGGTGAAATGGGATACATTTGTA
AGCCAGGAAAAGAAGACCTTACCTCCACTAAATGGAGGACAGTCACGGAGATCCTTTCTA
AGAAATGTAATGCCTGAAAACTCAAACTTTCCATATCGGCGGTATGACCGGCTCCCTCCA
ATCCATCAATTCTCCATAGAAAGTGACACGGATCTCTCTGAGACTGCAGAGTTGATTGAG
GAGTATGAGGTTTTTGATCCTACCAGACCTCGACCAAAAATCATTCTTGTTATAGGTGGT
CCAGGAAGTGGAAAGGGTACTCAGAGTTTGAAAATTGCAGAACGATATGGATTCCAATAC
ATTTCTGTGGGAGAATTATTAAGAAAGAAGATCCACAGTACCAGCAGCAATAGGAAATGG
AGTCTTATTGCCAAGATAATTACAACTGGAGAATTGGCCCCACAGGAAACAACAATTACA
GAGATAAAACAAAAATTGATGCAAATACCTGATGAAGAGGGCATTGTTATTGATGGATTT
CCAAGAGATGTTGCCCAGGCTCTATCTTTTGAGGACCAAATCTGTACCCCCGATTTGGTG
GTATTCCTGGCTTGTGCTAATCAGAGACTCAAAGAAAGATTACTGAAGCGTGCAGAACAG
CAGGGCCGACCAGACGACAATGTAAAAGCTACCCAAAGGAGACTAATGAACTTCAAGCAG
AATGCTGCTCCATTGGTTAAATACTTCCAGGAAAAGGGGCTCATCATGACATTTGATGCC
GACCGCGATGAGGATGAGGTGTTCTATGACATCAGCATGGCAGTTGACAACAAGTTATTT
CCAAACAAAGAGGCTGCAGCAGGTTCAAGTGACCTTGATCCTTCGATGATATTGGACACT
GGAGAGATCATTGATACAGGATCTGATTATGAAGATCAGGGTGATGACCAGTTAAATGTA
TTTGGAGAGGACACTATGGGAGGTTTCATGGAAGATTTGAGAAAGTGTAAAATTATTTTC
ATAATTGGTGGTCCTGGCTCTGGCAAAGGCACACAGTGTGAAAAGCTGGTGGAAAAATAT
GGATTTACACATCTCTCAACTGGCGAGCTCCTGCGTGAGGAACTGGCATCAGAATCTGAA
AGAAGCAAATTGATCAGAGACATTATGGAACGTGGAGACCTGGTGCCCTCAGGCATCGTT
TTGGAGCTCCTGAAGGAGGCCATGGTGGCCAGCCTCGGGGACACCAGGGGCTTCCTGATT
GACGGCTATCCTCGGGAGGTGAAGCAAGGGGAAGAGTTCGGACGCAGGATTGGAGACCCA
CAGTTGGTGATCTGTATGGACTGCTCGGCAGACACCATGACCAACCGCCTTCTCCAAAGG
AGCCGGAGCAGCCTGCCTGTGGACGACACCACCAAGACCATCGCCAAGCGCCTAGAAGCC
TACTACCGAGCGTCCATCCCCGTGATCGCCTACTACGAGACAAAAACACAGCTACACAAG
ATAAATGCAGAGGGAACACCAGAGGACGTTTTTCTTCAACTCTGCACAGCTATTGACTCT
ATTTTCTGA

Enzyme 102 GenBank Gene ID

NM_174858.1 Link Image

Enzyme 102 GeneCard ID

AK5

Enzyme 102 GenAtlas ID

AK5

Enzyme 102 HGNC ID

HGNC:365

Enzyme 102 Chromosome Location

Enzyme 102 Locus

1p31

Enzyme 102 SNPs

SNPJam Report Link Image

Enzyme 102 General References

Van Rompay AR, Johansson M, Karlsson A: Identification of a novel human adenylate kinase. cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein. Eur J Biochem. 1999 Apr;261(2):509-17. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 102 Metabolite References

Not Available

Enzyme 103 [top]

Enzyme 103 ID

5925

Enzyme 103 Name

Selenide, water dikinase 1

Enzyme 103 Synonyms

Selenium donor protein 1
Selenophosphate synthase 1

Enzyme 103 Gene Name

SEPHS1

Enzyme 103 Protein Sequence

>Selenide, water dikinase 1

MSTRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAV
MPRLGIGMDTCVIPLRHGGLSLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECD
NMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVC
QPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
MMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMA
AVSKACGNMFGLMHGTCPETSGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKG
NRTARIIDKPRIIEVAPQVATQNVNPTPGATS

Enzyme 103 Number of Residues

392

Enzyme 103 Molecular Weight

42910.3

Enzyme 103 Theoretical pI

5.84

Enzyme 103 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity kinase activity nucleoside binding purine nucleoside binding selenide, water dikinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
—
Component
—

Enzyme 103 General Function

Involved in catalytic activity

Enzyme 103 Specific Function

Synthesizes selenophosphate from selenide and ATP

Enzyme 103 Pathways

Selenoamino Acid Metabolism (map00450 )

Enzyme 103 Reactions

ATP + selenide + H2O = AMP + selenophosphate + phosphate [RN:R03595]

Enzyme 103 Pfam Domain Function

AIRS (PF00586 )
AIRS_C (PF02769 )

Enzyme 103 Signals

None

Enzyme 103 Transmembrane Regions

None

Enzyme 103 Essentiality

Not Available

Enzyme 103 GenBank ID Protein

55957750

Enzyme 103 UniProtKB/Swiss-Prot ID

P49903

Enzyme 103 UniProtKB/Swiss-Prot Entry Name

SPS1_HUMAN Link Image

Enzyme 103 PDB ID

Not Available

Enzyme 103 Cellular Location

Not Available

Enzyme 103 Gene Sequence

>1179 bp

ATGTCTACGCGGGAGTCCTTTAACCCGGAAAGTTACGAATTGGACAAAAGCTTCCGGCTA
ACCAGATTCACTGAACTGAAGGGCACAGGCTGCAAAGTGCCCCAAGATGTCCTGCAAAAA
TTGCTGGAATCTTTACAGGAGAACCACTTCCAAGAAGATGAGCAGTTTCTGGGAGCCGTT
ATGCCAAGGCTTGGCATTGGAATGGATACTTGTGTCATTCCTTTGAGGCACGGTGGGCTT
TCCTTGGTTCAAACCACAGATTACATTTACCCGATCGTAGACGACCCTTACATGATGGGC
AGGATAGCGTGTGCCAATGTCCTCAGTGACCTCTATGCAATGGGGGTCACGGAATGTGAC
AATATGCTGATGCTCCTTGGAGTCAGTAATAAAATGACCGACAGGGAAAGGGATAAAGTG
ATGCCTCTGATTATCCAAGGTTTTAAAGACGCAGCTGAGGAAGCAGGAACATCTGTAACA
GGCGGCCAAACAGTACTAAACCCCTGGATTGTCCTGGGAGGAGTGGCTACCACTGTCTGC
CAACCCAATGAATTTATCATGCCAGACAATGCAGTGCCAGGGGACGTGCTGGTGCTGACA
AAACCCCTGGGGACACAGGTGGCAGTGGCTGTGCACCAGTGGCTGGATATCCCTGAGAAA
TGGAATAAGATTAAACTAGTGGTCACCCAAGAAGATGTAGAGCTGGCCTACCAGGAGGCG
ATGATGAACATGGCGAGGCTCAACAGGACAGCTGCAGGACTCATGCACACGTTCAATGCC
CACGCCGCCACTGACATCACGGGCTTCGGGATTTTGGGCCATGCGCAGAACCTGGCCAAG
CAGCAGAGGAACGAGGTGTCGTTTGTAATTCACAACCTCCCGGTGCTGGCCAAGATGGCT
GCGGTGAGCAAGGCCTGCGGAAACATGTTCGGCCTCATGCACGGGACCTGCCCGGAGACT
TCAGGCGGCCTTCTGATCTGTTTACCACGTGAGCAAGCAGCTCGGTTCTGTGCAGAGATA
AAGTCCCCCAAATATGGTGAAGGCCACCAAGCATGGATTATTGGGATTGTAGAGAAGGGC
AACCGCACAGCCAGAATCATAGACAAACCCCGGATCATCGAGGTCGCACCACAAGTGGCC
ACTCAAAATGTGAATCCCACACCCGGGGCCACCTCTTAA

Enzyme 103 GenBank Gene ID

AL138764

Enzyme 103 GeneCard ID

SEPHS1

Enzyme 103 GenAtlas ID

SEPHS1

Enzyme 103 HGNC ID

HGNC:19685 Link Image

Enzyme 103 Chromosome Location

Enzyme 103 Locus

10p14

Enzyme 103 SNPs

SNPJam Report Link Image

Enzyme 103 General References

Low SC, Harney JW, Berry MJ: Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis. J Biol Chem. 1995 Sep 15;270(37):21659-64. [PubMed ]
Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Wang KT, Wang J, Li LF, Su XD: Crystal structures of catalytic intermediates of human selenophosphate synthetase 1. J Mol Biol. 2009 Jul 24;390(4):747-59. Epub 2009 May 25. [PubMed ]

Enzyme 103 Metabolite References

Not Available

Enzyme 104 [top]

Enzyme 104 ID

5926

Enzyme 104 Name

Ubiquitin-conjugating enzyme E2 N

Enzyme 104 Synonyms

Bendless-like ubiquitin-conjugating enzyme
Ubc13
Ubiquitin carrier protein N
Ubiquitin-protein ligase N

Enzyme 104 Gene Name

UBE2N

Enzyme 104 Protein Sequence

>Ubiquitin-conjugating enzyme E2 N

MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPE
EYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDP
LANDVAEQWKTNEAQAIETARAWTRLYAMNNI

Enzyme 104 Number of Residues

152

Enzyme 104 Molecular Weight

17137.6

Enzyme 104 Theoretical pI

6.53

Enzyme 104 GO Classification

Function
acid-amino acid ligase activity catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds small conjugating protein ligase activity
Process
biological regulation macromolecule metabolic process macromolecule modification metabolic process post-translational protein modification protein modification process regulation of biological process regulation of macromolecule metabolic process regulation of metabolic process regulation of protein metabolic process
Component
—

Enzyme 104 General Function

Involved in acid-amino acid ligase activity

Enzyme 104 Specific Function

The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD

Enzyme 104 Pathways

Ubiquitin mediated proteolysis (map04120 )

Enzyme 104 Reactions

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]

Enzyme 104 Pfam Domain Function

UQ_con (PF00179 )

Enzyme 104 Signals

None

Enzyme 104 Transmembrane Regions

None

Enzyme 104 Essentiality

Not Available

Enzyme 104 GenBank ID Protein

12653255

Enzyme 104 UniProtKB/Swiss-Prot ID

P61088

Enzyme 104 UniProtKB/Swiss-Prot Entry Name

UBE2N_HUMAN Link Image

Enzyme 104 PDB ID

1J7D

Enzyme 104 PDB File

Show

Enzyme 104 3D Structure

Enzyme 104 Cellular Location

Not Available

Enzyme 104 Gene Sequence

>459 bp

ATGGCCGGGCTGCCCCGCAGGATCATCAAGGAAACCCAGCGTTTGCTGGCAGAACCAGTT
CCTGGCATCAAAGCCGAACCAGATGAGAGCAACGCCCGTTATTTTCATGTGGTCATTGCT
GGCCCTCAGGATTCCCCCTTTGAGGGAGGGACTTTTAAACTTGAACTATTCCTTCCAGAA
GAATACCCAATGGCAGCCCCTAAAGTACGTTTCATGACCAAAATTTATCATCCTAATGTA
GACAAGTTGGGAAGAATATGTTTAGATATTTTGAAAGATAAGTGGTCCCCAGCACTGCAG
ATCCGCACAGTTCTGCTATCGATCCAGGCCTTGTTAAGTGCTCCCAATCCAGATGATCCA
TTAGCAAATGATGTAGCGGAGCAGTGGAAGACCAACGAAGCCCAAGCCATAGAAACAGCT
AGAGCATGGACTAGGCTATATGCCATGAATAATATTTAA

Enzyme 104 GenBank Gene ID

BC000396

Enzyme 104 GeneCard ID

UBE2N

Enzyme 104 GenAtlas ID

UBE2N

Enzyme 104 HGNC ID

HGNC:12492 Link Image

Enzyme 104 Chromosome Location

Enzyme 104 Locus

12q22

Enzyme 104 SNPs

SNPJam Report Link Image

Enzyme 104 General References

Yamaguchi T, Kim NS, Sekine S, Seino H, Osaka F, Yamao F, Kato S: Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product. J Biochem (Tokyo). 1996 Sep;120(3):494-97. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Zou W, Papov V, Malakhova O, Kim KI, Dao C, Li J, Zhang DE: ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin. Biochem Biophys Res Commun. 2005 Oct 14;336(1):61-8. [PubMed ]
Hofmann RM, Pickart CM: Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell. 1999 Mar 5;96(5):645-53. [PubMed ]
Bothos J, Summers MK, Venere M, Scolnick DM, Halazonetis TD: The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains. Oncogene. 2003 Oct 16;22(46):7101-7. [PubMed ]
Takeuchi T, Yokosawa H: ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating activity. Biochem Biophys Res Commun. 2005 Oct 14;336(1):9-13. [PubMed ]
Motegi A, Sood R, Moinova H, Markowitz SD, Liu PP, Myung K: Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination. J Cell Biol. 2006 Dec 4;175(5):703-8. Epub 2006 Nov 27. [PubMed ]
Plans V, Scheper J, Soler M, Loukili N, Okano Y, Thomson TM: The RING finger protein RNF8 recruits UBC13 for lysine 63-based self polyubiquitylation. J Cell Biochem. 2006 Feb 15;97(3):572-82. [PubMed ]
Unk I, Hajdu I, Fatyol K, Szakal B, Blastyak A, Bermudez V, Hurwitz J, Prakash L, Prakash S, Haracska L: Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen. Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18107-12. Epub 2006 Nov 15. [PubMed ]
Lamothe B, Besse A, Campos AD, Webster WK, Wu H, Darnay BG: Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation. J Biol Chem. 2007 Feb 9;282(6):4102-12. Epub 2006 Nov 29. [PubMed ]
Unk I, Hajdu I, Fatyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska L: Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination. Proc Natl Acad Sci U S A. 2008 Mar 11;105(10):3768-73. Epub 2008 Mar 3. [PubMed ]
Motegi A, Liaw HJ, Lee KY, Roest HP, Maas A, Wu X, Moinova H, Markowitz SD, Ding H, Hoeijmakers JH, Myung K: Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks. Proc Natl Acad Sci U S A. 2008 Aug 26;105(34):12411-6. Epub 2008 Aug 21. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Stewart GS, Panier S, Townsend K, Al-Hakim AK, Kolas NK, Miller ES, Nakada S, Ylanko J, Olivarius S, Mendez M, Oldreive C, Wildenhain J, Tagliaferro A, Pelletier L, Taubenheim N, Durandy A, Byrd PJ, Stankovic T, Taylor AM, Durocher D: The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell. 2009 Feb 6;136(3):420-34. [PubMed ]
Tcherpakov M, Delaunay A, Toth J, Kadoya T, Petroski MD, Ronai ZA: Regulation of endoplasmic reticulum-associated degradation by RNF5-dependent ubiquitination of JNK-associated membrane protein (JAMP). J Biol Chem. 2009 May 1;284(18):12099-109. Epub 2009 Mar 6. [PubMed ]
Marteijn JA, van der Meer LT, Smit JJ, Noordermeer SM, Wissink W, Jansen P, Swarts HG, Hibbert RG, de Witte T, Sixma TK, Jansen JH, van der Reijden BA: The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains. Leukemia. 2009 Aug;23(8):1480-9. Epub 2009 Apr 2. [PubMed ]
Scheper J, Oliva B, Villa-Freixa J, Thomson TM: Analysis of electrostatic contributions to the selectivity of interactions between RING-finger domains and ubiquitin-conjugating enzymes. Proteins. 2009 Jan;74(1):92-103. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
Moraes TF, Edwards RA, McKenna S, Pastushok L, Xiao W, Glover JN, Ellison MJ: Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13. Nat Struct Biol. 2001 Aug;8(8):669-73. [PubMed ]

Enzyme 104 Metabolite References

Not Available

Enzyme 105 [top]

Enzyme 105 ID

5927

Enzyme 105 Name

cGMP-specific 3',5'-cyclic phosphodiesterase

Enzyme 105 Synonyms

cGMP-binding cGMP-specific phosphodiesterase
CGB-PDE

Enzyme 105 Gene Name

PDE5A

Enzyme 105 Protein Sequence

>cGMP-specific 3',5'-cyclic phosphodiesterase

MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAE
RVHTIPVCKEGIRGHTESCSCPLQQSPRADNSVPGTPTRKISASEFDRPLRPIVVKDSEG
TVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLI
SADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPL
NIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDE
KDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIIS
FMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTME
PLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGK
VKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETREL
QSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWIL
SVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGV
NNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAI
LATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAE
LVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCF
PLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN

Enzyme 105 Number of Residues

875

Enzyme 105 Molecular Weight

100012.2

Enzyme 105 Theoretical pI

6.00

Enzyme 105 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 105 General Function

Involved in catalytic activity

Enzyme 105 Specific Function

Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'- GMP

Enzyme 105 Pathways

Not Available

Enzyme 105 Reactions

guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]

Enzyme 105 Pfam Domain Function

GAF (PF01590 )
PDEase_I (PF00233 )

Enzyme 105 Signals

None

Enzyme 105 Transmembrane Regions

None

Enzyme 105 Essentiality

Not Available

Enzyme 105 GenBank ID Protein

Not Available

Enzyme 105 UniProtKB/Swiss-Prot ID

O76074

Enzyme 105 UniProtKB/Swiss-Prot Entry Name

PDE5A_HUMAN Link Image

Enzyme 105 PDB ID

1T9R

Enzyme 105 PDB File

Show

Enzyme 105 3D Structure

Enzyme 105 Cellular Location

Not Available

Enzyme 105 Gene Sequence

>2628 bp

ATGGAGCGGGCCGGCCCCAGCTTCGGGCAGCAGCGACAGCAGCAGCAGCCCCAGCAGCAG
AAGCAGCAGCAGAGGGATCAGGACTCGGTCGAAGCATGGCTGGACGATCACTGGGACTTT
ACCTTCTCATACTTTGTTAGAAAAGCCACCAGAGAAATGGTCAATGCATGGTTTGCTGAG
AGAGTTCACACCATCCCTGTGTGCAAGGAAGGTATCAGAGGCCACACCGAATCTTGCTCT
TGTCCCTTGCAGCAGAGTCCTCGTGCAGATAACAGTGTCCCTGGAACACCAACCAGGAAA
ATCTCTGCCTCTGAATTTGACCGGCCTCTTAGACCCATTGTTGTCAAGGATTCTGAGGGA
ACTGTGAGCTTCCTCTCTGACTCAGAAAAGAAGGAACAGATGCCTCTAACCCCTCCAAGG
TTTGATCATGATGAAGGGGACCAGTGCTCAAGACTCTTGGAATTAGTGAAGGATATTTCT
AGTCATTTGGATGTCACAGCCTTATGTCACAAAATTTTCTTGCATATCCATGGACTGATA
TCTGCTGACCGCTATTCCCTGTTCCTTGTCTGTGAAGACAGCTCCAATGACAAGTTTCTT
ATCAGCCGCCTCTTTGATGTTGCTGAAGGTTCAACACTGGAAGAAGTTTCAAATAACTGT
ATCCGCTTAGAATGGAACAAAGGCATTGTGGGACATGTGGCAGCGCTTGGTGAGCCCTTG
AACATCAAAGATGCATATGAGGATCCTCGGTTCAATGCAGAAGTTGACCAAATTACAGGC
TACAAGACACAAAGCATTCTTTGTATGCCAATTAAGAATCATAGGGAAGAGGTTGTTGGT
GTAGCCCAGGCCATCAACAAGAAATCAGGAAACGGTGGGACATTTACTGAAAAAGATGAA
AAGGACTTTGCTGCTTATTTGGCATTTTGTGGTATTGTTCTTCATAATGCTCAGCTCTAT
GAGACTTCACTGCTGGAGAACAAGAGAAATCAGGTGCTGCTTGACCTTGCTAGTTTAATT
TTTGAAGAACAACAATCATTAGAAGTAATTTTGAAGAAAATAGCTGCCACTATTATCTCT
TTCATGCAAGTGCAGAAATGCACCATTTTCATAGTGGATGAAGATTGCTCCGATTCTTTT
TCTAGTGTGTTTCACATGGAGTGTGAGGAATTAGAAAAATCATCTGATACATTAACAAGG
GAACATGATGCAAACAAAATCAATTACATGTATGCTCAGTATGTCAAAAATACTATGGAA
CCACTTAATATCCCAGATGTCAGTAAGGATAAAAGATTTCCCTGGACAACTGAAAATACA
GGAAATGTAAACCAGCAGTGCATTAGAAGTTTGCTTTGTACACCTATAAAAAATGGAAAG
AAGAATAAAGTTATAGGGGTTTGCCAACTTGTTAATAAGATGGAGGAGAATACTGGCAAG
GTTAAGCCTTTCAACCGAAATGACGAACAGTTTCTGGAAGCTTTTGTCATCTTTTGTGGC
TTGGGGATCCAGAACACGCAGATGTATGAAGCAGTGGAGAGAGCCATGGCCAAGCAAATG
GTCACATTGGAGGTTCTGTCGTATCATGCTTCAGCAGCAGAGGAAGAAACAAGAGAGCTA
CAGTCGTTAGCGGCTGCTGTGGTGCCATCTGCCCAGACCCTTAAAATTACTGACTTTAGC
TTCAGTGACTTTGAGCTGTCTGATCTGGAAACAGCACTGTGTACAATTCGGATGTTTACT
GACCTCAACCTTGTGCAGAACTTCCAGATGAAACATGAGGTTCTTTGCAGATGGATTTTA
AGTGTTAAGAAGAATTATCGGAAGAATGTTGCCTATCATAATTGGAGACATGCCTTTAAT
ACAGCTCAGTGCATGTTTGCTGCTCTAAAAGCAGGCAAAATTCAGAACAAGCTGACTGAC
CTGGAGATACTTGCATTGCTGATTGCTGCACTAAGCCACGATTTGGATCACCGTGGTGTG
AATAACTCTTACATACAGCGAAGTGAACATCCACTTGCCCAGCTTTACTGCCATTCAATC
ATGGAACACCATCATTTTGACCAGTGCCTGATGATTCTTAATAGTCCAGGCAATCAGATT
CTCAGTGGCCTCTCCATTGAAGAATATAAGACCACGTTGAAAATAATCAAGCAAGCTATT
TTAGCTACAGACCTAGCACTGTACATTAAGAGGCGAGGAGAATTTTTTGAACTTATAAGA
AAAAATCAATTCAATTTGGAAGATCCTCATCAAAAGGAGTTGTTTTTGGCAATGCTGATG
ACAGCTTGTGATCTTTCTGCAATTACAAAACCCTGGCCTATTCAACAACGGATAGCAGAA
CTTGTAGCAACTGAATTTTTTGATCAAGGAGACAGAGAGAGAAAAGAACTCAACATAGAA
CCCACTGATCTAATGAACAGGGAGAAGAAAAACAAAATCCCAAGTATGCAAGTTGGGTTC
ATAGATGCCATCTGCTTGCAACTGTATGAGGCCCTGACCCACGTGTCAGAGGACTGTTTC
CCTTTGCTAGATGGCTGCAGAAAGAACAGGCAGAAATGGCAGGCCCTTGCAGAACAGCAG
GAGAAGATGCTGATTAATGGGGAAAGCGGCCAGGCCAAGCGGAACTGA

Enzyme 105 GenBank Gene ID

AF043731

Enzyme 105 GeneCard ID

PDE5A

Enzyme 105 GenAtlas ID

PDE5A

Enzyme 105 HGNC ID

HGNC:8784

Enzyme 105 Chromosome Location

Enzyme 105 Locus

4q27

Enzyme 105 SNPs

SNPJam Report Link Image

Enzyme 105 General References

Loughney K, Hill TR, Florio VA, Uher L, Rosman GJ, Wolda SL, Jones BA, Howard ML, McAllister-Lucas LM, Sonnenburg WK, Francis SH, Corbin JD, Beavo JA, Ferguson K: Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase. Gene. 1998 Aug 17;216(1):139-47. [PubMed ]
Yanaka N, Kotera J, Ohtsuka A, Akatsuka H, Imai Y, Michibata H, Fujishige K, Kawai E, Takebayashi S, Okumura K, Omori K: Expression, structure and chromosomal localization of the human cGMP-binding cGMP-specific phosphodiesterase PDE5A gene. Eur J Biochem. 1998 Jul 15;255(2):391-9. [PubMed ]
Stacey P, Rulten S, Dapling A, Phillips SC: Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase (PDE5). Biochem Biophys Res Commun. 1998 Jun 18;247(2):249-54. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Zhou L, Thompson WJ, Potter DE: Multiple cyclic nucleotide phosphodiesterases in human trabecular meshwork cells. Invest Ophthalmol Vis Sci. 1999 Jul;40(8):1745-52. [PubMed ]
Sung BJ, Hwang KY, Jeon YH, Lee JI, Heo YS, Kim JH, Moon J, Yoon JM, Hyun YL, Kim E, Eum SJ, Park SY, Lee JO, Lee TG, Ro S, Cho JM: Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules. Nature. 2003 Sep 4;425(6953):98-102. [PubMed ]

Enzyme 105 Metabolite References

Not Available

Enzyme 106 [top]

Enzyme 106 ID

5928

Enzyme 106 Name

Argininosuccinate synthase

Enzyme 106 Synonyms

Citrulline--aspartate ligase

Enzyme 106 Gene Name

ASS1

Enzyme 106 Protein Sequence

>Argininosuccinate synthase

MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVF
IEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATG
KGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWS
MDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKD
GTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAF
TMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVLKGQVYI
LGRESPLSLYNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVTAK

Enzyme 106 Number of Residues

412

Enzyme 106 Molecular Weight

46530.1

Enzyme 106 Theoretical pI

8.18

Enzyme 106 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding argininosuccinate synthase activity binding catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds nucleoside binding purine nucleoside binding
Process
arginine biosynthetic process arginine metabolic process cellular amino acid and derivative metabolic process cellular amino acid metabolic process cellular metabolic process glutamine family amino acid metabolic process metabolic process
Component
—

Enzyme 106 General Function

Involved in argininosuccinate synthase activity

Enzyme 106 Specific Function

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate

Enzyme 106 Pathways

Arginine and Proline Metabolism (map00330 )

Enzyme 106 Reactions

ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate [RN:R01954]

Enzyme 106 Pfam Domain Function

Arginosuc_synth (PF00764 )

Enzyme 106 Signals

None

Enzyme 106 Transmembrane Regions

None

Enzyme 106 Essentiality

Not Available

Enzyme 106 GenBank ID Protein

28872

Enzyme 106 UniProtKB/Swiss-Prot ID

P00966

Enzyme 106 UniProtKB/Swiss-Prot Entry Name

ASSY_HUMAN Link Image

Enzyme 106 PDB ID

Not Available

Enzyme 106 Cellular Location

Not Available

Enzyme 106 Gene Sequence

>1239 bp

ATGTCCAGCAAAGGCTCCGTGGTTCTGGCCTACAGTGGCGGCCTGGACACCTCGTGCATC
CTCGTGTGGCTGAAGGAACAAGGCTATGACGTCATTGCCTATCTGGCCAACATTGGCCAG
AAGGAAGACTTCGAGGAAGCCAGGAAGAAGGCACTGAAGCTTGGGGCCAAAAAGGTGTTC
ATTGAGGATGTCAGCAGGGAGTTTGTGGAGGAGTTCATCTGGCCGGCCATCCAGTCCAGC
GCACTGTATGAGGACCGCTACCTCCTGGGCACCTCTCTTGCCAGGCCCTGCATCGCCCGC
AAACAAGTGGAAATCGCCCAGCGGGAGGGGGCCAAGTATGTGTCCCACGGCGCCACAGGA
AAGGGGAACGATCAGGTCCGGTTTGAGCTCAGCTGCTACTCACTGGCCCCCCAGATAAAG
GTCATTGCTCCCTGGAGGATGCCTGAATTCTACAACCGGTTCAAGGGCCGCAATGACCTG
ATGGAGTACGCAAAGCAACACGGGATTCCCATCCCGGTCACTCCCAAGAACCCGTGGAGC
ATGGATGAGAACCTCATGCACATCAGCTACGAGGCTGGAATCCTGGAGAACCCCAAGAAC
CAAGCGCCTCCAGGTCTCTACACGAAGACCCAGGACCCAGCCAAAGCCCCCAACACCCCT
GACATTCTCGAGATCGAGTTCAAAAAAGGGGTCCCTGTGAAGGTGACCAACGTCAAGGAT
GGCACCACCCACCAGACCTCCTTGGAGCTCTTCATGTACCTGAACGAAGTCGCGGGCAAG
CATGGCGTGGGCCGTATTGACATCGTGGAGAACCGCTTCATTGGAATGAAGTCCCGAGGT
ATCTACGAGACCCCAGCAGGCACCATCCTTTACCATGCTCATTTAGACATCGAGGCCTTC
ACCATGGACCGGGAAGTGCGCAAAATCAAACAAGGCCTGGGCTTGAAATTTGCTGAGCTG
GTGTATACCGGTTTACGGCCTAGCCCTGAGTGTGAATTTGTCCGCCACTGCATCGCCAAG
TCCCAGGAGCGAGTGGAAGGGAAAGTGCAGGTGTCCGTCCTCAAGGGCCAGGTGTACATC
CTCGGCCGGGAGTCCCCACTGTCTCTCTACAATGAGGAGCTGGTGAGCATGAACGTGCAG
GGTGATTATGAGCCAACTGATGCCACCGGGTTCATCAACATCAATTCCCTCAGGCTGAAG
GAATATCATCGTCTCCAGAGCAAGGTCACTGCCAAATAG

Enzyme 106 GenBank Gene ID

X01630

Enzyme 106 GeneCard ID

ASS1

Enzyme 106 GenAtlas ID

ASS1

Enzyme 106 HGNC ID

HGNC:758

Enzyme 106 Chromosome Location

Enzyme 106 Locus

9q34.1

Enzyme 106 SNPs

SNPJam Report Link Image

Enzyme 106 General References

Bock HG, Su TS, O'Brien WE, Beaudet AL: Sequence for human argininosuccinate synthetase cDNA. Nucleic Acids Res. 1983 Sep 24;11(18):6505-12. [PubMed ]
Freytag SO, Bock HG, Beaudet AL, O'Brien WE: Molecular structures of human argininosuccinate synthetase pseudogenes. Evolutionary and mechanistic implications. J Biol Chem. 1984 Mar 10;259(5):3160-6. [PubMed ]
Haberle J, Pauli S, Linnebank M, Kleijer WJ, Bakker HD, Wanders RJ, Harms E, Koch HG: Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia. Hum Genet. 2002 Apr;110(4):327-33. Epub 2002 Mar 1. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Jinno Y, Nomiyama H, Matuo S, Shimada K, Matsuda I, Saheki T: Structure of the 5' end region of the human argininosuccinate synthetase gene. J Inherit Metab Dis. 1985;8(3):157-9. [PubMed ]
Isashiki Y, Noda T, Kobayashi K, Sase M, Saheki T, Titani K: Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase. Protein Seq Data Anal. 1989 Jul;2(4):283-7. [PubMed ]
Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed ]
Zheng X, Dai X, Zhao Y, Chen Q, Lu F, Yao D, Yu Q, Liu X, Zhang C, Gu X, Luo M: Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein. Proc Natl Acad Sci U S A. 2007 May 22;104(21):8809-14. Epub 2007 May 11. [PubMed ]
Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Engel K, Hohne W, Haberle J: Mutations and polymorphisms in the human argininosuccinate synthetase (ASS1) gene. Hum Mutat. 2009 Mar;30(3):300-7. [PubMed ]
Kobayashi K, Jackson MJ, Tick DB, O'Brien WE, Beaudet AL: Heterogeneity of mutations in argininosuccinate synthetase causing human citrullinemia. J Biol Chem. 1990 Jul 5;265(19):11361-7. [PubMed ]
Kobayashi K, Rosenbloom C, Beaudet AL, O'Brien WE: Additional mutations in argininosuccinate synthetase causing citrullinemia. Mol Biol Med. 1991 Feb;8(1):95-100. [PubMed ]
Kobayashi K, Shaheen N, Terazono H, Saheki T: Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia. Am J Hum Genet. 1994 Dec;55(6):1103-12. [PubMed ]
Shaheen N, Kobayashi K, Terazono H, Fukushige T, Horiuchi M, Saheki T: Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells. Enzyme Protein. 1994-1995;48(5-6):251-64. [PubMed ]
Vilaseca MA, Kobayashi K, Briones P, Lambruschini N, Campistol J, Tabata A, Alomar A, Rodes M, Lluch M, Saheki T: Phenotype and genotype heterogeneity in Mediterranean citrullinemia. Mol Genet Metab. 2001 Nov;74(3):396-8. [PubMed ]
Gao HZ, Kobayashi K, Tabata A, Tsuge H, Iijima M, Yasuda T, Kalkanoglu HS, Dursun A, Tokatli A, Coskun T, Trefz FK, Skladal D, Mandel H, Seidel J, Kodama S, Shirane S, Ichida T, Makino S, Yoshino M, Kang JH, Mizuguchi M, Barshop BA, Fuchinoue S, Seneca S, Zeesman S, Knerr I, Rodes M, Wasant P, Yoshida I, De Meirleir L, Abdul Jalil M, Begum L, Horiuchi M, Katunuma N, Nakagawa S, Saheki T: Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients. Hum Mutat. 2003 Jul;22(1):24-34. [PubMed ]
Haberle J, Pauli S, Schmidt E, Schulze-Eilfing B, Berning C, Koch HG: Mild citrullinemia in Caucasians is an allelic variant of argininosuccinate synthetase deficiency (citrullinemia type 1). Mol Genet Metab. 2003 Nov;80(3):302-6. [PubMed ]
Kleijer WJ, Garritsen VH, van der Sterre ML, Berning C, Haberle J, Huijmans JG: Prenatal diagnosis of citrullinemia and argininosuccinic aciduria: evidence for a transmission ratio distortion in citrullinemia. Prenat Diagn. 2006 Mar;26(3):242-7. [PubMed ]

Enzyme 106 Metabolite References

Not Available

Enzyme 107 [top]

Enzyme 107 ID

5929

Enzyme 107 Name

AMP deaminase 1

Enzyme 107 Synonyms

AMP deaminase isoform M
Myoadenylate deaminase

Enzyme 107 Gene Name

AMPD1

Enzyme 107 Protein Sequence

>AMP deaminase 1

MPLFKLPAEEKQIDDAMRNFAEKVFASEVKDEGGRQEISPFDVDEICPISHHEMQAHIFH
LETLSTSTEARRKKRFQGRKTVNLSIPLSETSSTKLSHIDEYISSSPTYQTVPDFQRVQI
TGDYASGVTVEDFEIVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEAWVANESF
YPVFTPPVKKGEDPFRTDNLPENLGYHLKMKDGVVYVYPNEAAVSKDEPKPLPYPNLDTF
LDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKV
DTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSL
DVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQ
HAEPRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLE
NIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKHSGHMFSSKSPKPQEWTLEKNPS
YTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKK
SPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEP
LMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNV
AQIRMAYRYETWCYELNLIAEGLKSTE

Enzyme 107 Number of Residues

747

Enzyme 107 Molecular Weight

86489.2

Enzyme 107 Theoretical pI

6.89

Enzyme 107 GO Classification

Function
AMP deaminase activity catalytic activity deaminase activity hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
Process
cellular aromatic compound metabolic process cellular metabolic process cellular nitrogen compound metabolic process metabolic process nitrogen compound metabolic process nucleobase metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside phosphate metabolic process nucleotide metabolic process purine base metabolic process purine nucleoside monophosphate biosynthetic process purine nucleotide biosynthetic process purine nucleotide metabolic process purine ribonucleoside monophosphate biosynthetic process
Component
—

Enzyme 107 General Function

Involved in deaminase activity

Enzyme 107 Specific Function

AMP deaminase plays a critical role in energy metabolism

Enzyme 107 Pathways

Purine Metabolism (map00230 )

Enzyme 107 Reactions

AMP + H2O = IMP + NH3 [RN:R00181]

Enzyme 107 Pfam Domain Function

A_deaminase (PF00962 )

Enzyme 107 Signals

None

Enzyme 107 Transmembrane Regions

None

Enzyme 107 Essentiality

Not Available

Enzyme 107 GenBank ID Protein

178544

Enzyme 107 UniProtKB/Swiss-Prot ID

P23109

Enzyme 107 UniProtKB/Swiss-Prot Entry Name

AMPD1_HUMAN Link Image

Enzyme 107 PDB ID

Not Available

Enzyme 107 Cellular Location

Not Available

Enzyme 107 Gene Sequence

>2244 bp

ATGCCTCTGTTCAAACTCCCAGCTGAAGAGAAACAAATTGATGATGCAATGCGCAACTTT
GCTGAAAAAGTGTTTGCCTCTGAAGTCAAAGATGAAGGAGGTCGTCAGGAGATTTCCCCC
TTTGATGTGGATGAGATCTGTCCGATTTCTCATCATGAGATGCAAGCACACATATTCCAT
CTGGAGACTCTGTCCACCTCCACAGAAGCCAGGAGAAAAAAGCGTTTCCAAGGACGGAAG
ACTGTTAATTTGTCCATTCCACTAAGTGAAACATCTTCCACCAAACTGTCCCACATTGAT
GAATACATTTCCTCATCTCCAACCTACCAGACCGTGCCTGATTTTCAGAGAGTGCAGATT
ACTGGTGACTATGCCTCTGGGGTTACAGTTGAAGATTTTGAAATTGTTTGCAAAGGTCTG
TATCGGGCACTATGCATACGTGAGAAATACATGCAGAAGTCGTTTCAGAGGTTCCCTAAA
ACCCCTTCCAAATACTTGCGGAACATTGATGGTGAGGCTTGGGTAGCAAATGAGAGCTTC
TATCCAGTCTTTACTCCTCCTGTGAAGAAGGGAGAGGACCCCTTCCGAACAGACAACCTT
CCTGAAAACCTGGGCTATCACCTCAAAATGAAGGACGGTGTAGTTTACGTCTATCCTAAT
GAAGCAGCAGTCAGCAAAGATGAGCCTAAGCCACTTCCTTACCCAAATCTGGACACCTTC
TTAGACGATATGAATTTTTTACTTGCTTTAATTGCTCAAGGACCTGTTAAGACCTATACC
CACCGGCGCCTGAAGTTCCTCTCCTCCAAGTTCCAGGTCCATCAGATGCTTAACGAGATG
GACGAGTTAAAGGAGCTGAAAAACAACCCCCACCGAGATTTTTATAACTGCAGGAAGGTG
GACACCCATATCCATGCAGCCGCTTGCATGAACCAGAAACATCTGCTGCGTTTTATTAAG
AAATCTTACCAAATTGATGCTGACAGAGTGGTCTATAGCACCAAAGAGAAGAATCTGACC
CTAAAGGAACTTTTTGCTAAATTAAAAATGCATCCTTATGACCTGACTGTTGATTCTCTG
GATGTTCATGCTGGACGCCAGACCTTCCAGCGTTTTGATAAGTTCAATGACAAATATAAT
CCTGTAGGAGCAAGTGAGCTACGGGACCTCTACTTGAAGACAGACAATTACATTAATGGG
GAATATTTTGCCACTATCATCAAGGAGGTAGGTGCGGACCTGGTGGAGGCCAAGTACCAG
CATGCTGAGCCCCGCCTGTCCATCTATGGCCGCAGTCCTGATGAGTGGAGCAAACTCTCC
TCCTGGTTCGTCTGCAATCGCATCCACTGCCCCAACATGACATGGATGATCCAGGTTCCC
AGGATCTATGATGTGTTCCGTTCCAAGAATTTCCTTCCACATTTTGGAAAAATGCTGGAG
AATATTTTCATGCCAGTGTTTGAGGCCACCATCAACCCCCAGGCTGACCCAGAACTCAGT
GTCTTCCTCAAGCATATCACTGGCTTTGACAGTGTGGATGATGAGTCCAAACACAGTGGC
CACATGTTCTCCTCCAAGAGTCCCAAGCCCCAGGAGTGGACATTGGAAAAGAATCCATCT
TACACTTACTATGCCTACTACATGTATGCAAACATCATGGTGCTCAACAGCCTGAGAAAG
GAACGAGGCATGAATACGTTTCTGTTCCGACCTCACTGTGGAGAAGCTGGAGCCCTCACC
CATCTCATGACAGCATTCATGATAGCAGATGATATCTCTCATGGCCTAAATTTAAAAAAG
AGTCCCGTGCTACAGTACTTGTTTTTCTTAGCCCAAATTCCCATCGCCATGTCACCACTA
AGTAACAATAGCCTATTTCTAGAGTATGCCAAAAATCCTTTTTTGGATTTCCTTCAGAAA
GGGCTAATGATCTCACTGTCTACAGATGACCCAATGCAATTCCACTTTACCAAGGAGCCC
CTAATGGAAGAATATGCTATTGCTGCACAAGTCTTCAAGCTGAGCACCTGTGATATGTGC
GAAGTGGCAAGGAACAGTGTCTTGCAGTGTGGAATTTCTCATGAGGAGAAAGTAAAGTTT
CTGGGCGACAATTACCTTGAGGAAGGCCCTGCTGGAAATGATATCCGGAGGACAAATGTA
GCCCAAATCCGCATGGCCTATCGCTATGAAACCTGGTGTTATGAACTCAATTTAATTGCT
GAGGGTCTTAAATCAACAGAATAA

Enzyme 107 GenBank Gene ID

M60092

Enzyme 107 GeneCard ID

AMPD1

Enzyme 107 GenAtlas ID

AMPD1

Enzyme 107 HGNC ID

HGNC:468

Enzyme 107 Chromosome Location

Enzyme 107 Locus

1p13

Enzyme 107 SNPs

SNPJam Report Link Image

Enzyme 107 General References

Sabina RL, Morisaki T, Clarke P, Eddy R, Shows TB, Morton CC, Holmes EW: Characterization of the human and rat myoadenylate deaminase genes. J Biol Chem. 1990 Jun 5;265(16):9423-33. [PubMed ]
Sabina RL, Fishbein WN, Pezeshkpour G, Clarke PR, Holmes EW: Molecular analysis of the myoadenylate deaminase deficiencies. Neurology. 1992 Jan;42(1):170-9. [PubMed ]
Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
Morisaki T, Gross M, Morisaki H, Pongratz D, Zollner N, Holmes EW: Molecular basis of AMP deaminase deficiency in skeletal muscle. Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6457-61. [PubMed ]
Morisaki H, Higuchi I, Abe M, Osame M, Morisaki T: First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient. Hum Mutat. 2000 Dec;16(6):467-72. [PubMed ]
Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]

Enzyme 107 Metabolite References

Not Available

Enzyme 108 [top]

Enzyme 108 ID

5930

Enzyme 108 Name

Selenide, water dikinase 2

Enzyme 108 Synonyms

Selenium donor protein 2
Selenophosphate synthase 2

Enzyme 108 Gene Name

SEPHS2

Enzyme 108 Protein Sequence

>Selenide, water dikinase 2

MAEASATGACGEAMAAAEGSSGPAGLTLGRSFSNYRPFEPQALGLSPSWRLTGFSGMKGU
GCKVPQEALLKLLAGLTRPDVRPPLGRGLVGGQEEASQEAGLPAGAGPSPTFPALGIGMD
SCVIPLRHGGLSLVQTTDFFYPLVEDPYMMGRIACANVLSDLYAMGITECDNMLMLLSVS
QSMSEEEREKVTPLMVKGFRDAAEEGGTAVTGGQTVVNPWIIIGGVATVVCQPNEFIMPD
SAVVGDVLVLTKPLGTQVAVNAHQWLDNPERWNKVKMVVSREEVELAYQEAMFNMATLNR
TAAGLMHTFNAHAATDITGFGILGHSQNLAKQQRNEVSFVIHNLPIIAKMAAVSKASGRF
GLLQGTSAETSGGLLICLPREQAARFCSEIKSSKYGEGHQAWIVGIVEKGNRTARIIDKP
RVIEVLPRGATAAVLAPDSSNASSEPSS

Enzyme 108 Number of Residues

448

Enzyme 108 Molecular Weight

47304.7

Enzyme 108 Theoretical pI

5.69

Enzyme 108 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity kinase activity nucleoside binding purine nucleoside binding selenide, water dikinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
—
Component
—

Enzyme 108 General Function

Involved in catalytic activity

Enzyme 108 Specific Function

Synthesizes selenophosphate from selenide and ATP

Enzyme 108 Pathways

Selenoamino Acid Metabolism (map00450 )

Enzyme 108 Reactions

ATP + selenide + H2O = AMP + selenophosphate + phosphate [RN:R03595]

Enzyme 108 Pfam Domain Function

AIRS (PF00586 )
AIRS_C (PF02769 )

Enzyme 108 Signals

None

Enzyme 108 Transmembrane Regions

None

Enzyme 108 Essentiality

Not Available

Enzyme 108 GenBank ID Protein

Not Available

Enzyme 108 UniProtKB/Swiss-Prot ID

Q99611

Enzyme 108 UniProtKB/Swiss-Prot Entry Name

SPS2_HUMAN Link Image

Enzyme 108 PDB ID

Not Available

Enzyme 108 Cellular Location

Not Available

Enzyme 108 Gene Sequence

>1347 bp

ATGGCGGAAGCCTCGGCGACGGGCGCCTGCGGAGAGGCGATGGCAGCGGCGGAAGGCTCC
TCGGGCCCGGCGGGCTTGACTCTGGGCCGGAGCTTCTCGAACTACCGGCCCTTCGAGCCC
CAGGCGTTGGGCCTCAGCCCGAGCTGGCGGCTGACGGGCTTCTCCGGCATGAAGGGCTGA
GGCTGCAAGGTCCCGCAGGAGGCGCTGCTCAAACTCCTGGCGGGACTGACGCGGCCGGAC
GTGCGGCCCCCGCTGGGCCGGGGCCTGGTGGGTGGCCAGGAAGAGGCGTCCCAGGAAGCC
GGCCTGCCGGCAGGAGCGGGCCCCAGCCCCACCTTTCCAGCCCTGGGCATCGGGATGGAC
TCCTGCGTCATCCCCCTGAGGCACGGGGGCCTGTCACTGGTGCAGACCACGGACTTCTTT
TACCCCTTGGTAGAAGATCCCTACATGATGGGGCGCATAGCTTGTGCCAACGTGCTGAGT
GACCTCTACGCCATGGGGATTACTGAGTGTGACAACATGTTGATGTTACTCAGCGTCAGC
CAGAGTATGAGTGAGGAGGAACGCGAAAAGGTAACGCCACTCATGGTCAAAGGCTTTCGG
GATGCGGCTGAGGAAGGAGGGACGGCAGTGACCGGTGGGCAAACGGTGGTCAACCCTTGG
ATTATAATCGGTGGAGTTGCCACTGTAGTATGCCAACCAAATGAGTTCATAATGCCGGAC
AGCGCCGTCGTTGGGGACGTGCTGGTGTTAACCAAACCGTTAGGAACCCAGGTTGCTGTC
AATGCCCACCAATGGCTGGATAATCCTGAAAGATGGAATAAAGTAAAGATGGTGGTCTCC
AGAGAAGAGGTGGAGCTGGCCTATCAGGAAGCCATGTTCAATATGGCTACCCTCAACAGA
ACTGCTGCAGGTTTAATGCACACATTTAATGCCCATGCGGCCACAGATATCACAGGCTTT
GGCATTCTAGGACACTCCCAGAACCTTGCAAAACAACAAAGAAATGAAGTGTCCTTTGTT
ATTCATAATCTGCCAATAATTGCCAAGATGGCTGCCGTCAGCAAGGCCAGTGGACGGTTT
GGGCTTCTTCAAGGAACCTCAGCTGAAACCTCTGGGGGATTACTGATTTGTCTGCCAAGA
GAACAGGCGGCTCGCTTTTGTTCTGAAATCAAATCCTCCAAGTACGGAGAGGGTCACCAA
GCGTGGATCGTTGGCATTGTGGAAAAGGGAAACCGAACGGCCCGGATCATTGACAAGCCG
CGAGTTATTGAAGTCCTGCCTCGTGGGGCCACAGCTGCTGTTCTTGCTCCTGACAGTTCA
AATGCCTCCTCTGAGCCTAGCTCGTGA

Enzyme 108 GenBank Gene ID

U43286

Enzyme 108 GeneCard ID

SEPHS2

Enzyme 108 GenAtlas ID

SEPHS2

Enzyme 108 HGNC ID

HGNC:19686 Link Image

Enzyme 108 Chromosome Location

Enzyme 108 Locus

16p11.2

Enzyme 108 SNPs

SNPJam Report Link Image

Enzyme 108 General References

Guimaraes MJ, Bazan JF, Zlotnik A, Wiles MV, Grimaldi JC, Lee F, McClanahan T: A new approach to the study of haematopoietic development in the yolk sac and embryoid bodies. Development. 1995 Oct;121(10):3335-46. [PubMed ]
Guimaraes MJ, Peterson D, Vicari A, Cocks BG, Copeland NG, Gilbert DJ, Jenkins NA, Ferrick DA, Kastelein RA, Bazan JF, Zlotnik A: Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism? Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15086-91. [PubMed ]
Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]

Enzyme 108 Metabolite References

Not Available

Enzyme 109 [top]

Enzyme 109 ID

5932

Enzyme 109 Name

DNA ligase 1

Enzyme 109 Synonyms

DNA ligase I
Polydeoxyribonucleotide synthase [ATP] 1

Enzyme 109 Gene Name

LIG1

Enzyme 109 Protein Sequence

>DNA ligase 1

MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKEWNGVVSESDSPVKRPGRKA
ARVLGSEGEEEDEALSPAKGQKPALDCSQVSPPRPATSPENNASLSDTSPMDSSPSGIPK
RRTARKQLPKRTIQEVLEEQSEDEDREAKRKKEEEEEETPKESLTEAEVATEKEGEDGDQ
PTTPPKPLKTSKAETPTESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVK
KEVKEEEPGAPGKEGAAEGPLDPSGYNPAKNNYHPVEDACWKPGQKVPYLAVARTFEKIE
EVSARLRMVETLSNLLRSVVALSPPDLLPVLYLSLNHLGPPQQGLELGVGDGVLLKAVAQ
ATGRQLESVRAEAAEKGDVGLVAENSRSTQRLMLPPPPLTASGVFSKFRDIARLTGSAST
AKKIDIIKGLFVACRHSEARFIARSLSGRLRLGLAEQSVLAALSQAVSLTPPGQEFPPAM
VDAGKGKTAEARKTWLEEQGMILKQTFCEVPDLDRIIPVLLEHGLERLPEHCKLSPGIPL
KPMLAHPTRGISEVLKRFEEAAFTCEYKYDGQRAQIHALEGGEVKIFSRNQEDNTGKYPD
IISRIPKIKLPSVTSFILDTEAVAWDREKKQIQPFQVLTTRKRKEVDASEIQVQVCLYAF
DLIYLNGESLVREPLSRRRQLLRENFVETEGEFVFATSLDTKDIEQIAEFLEQSVKDSCE
GLMVKTLDVDATYEIAKRSHNWLKLKKDYLDGVGDTLDLVVIGAYLGRGKRAGRYGGFLL
ASYDEDSEELQAICKLGTGFSDEELEEHHQSLKALVLPSPRPYVRIDGAVIPDHWLDPSA
VWEVKCADLSLSPIYPAARGLVDSDKGISLRFPRFIRVREDKQPEQATTSAQVACLYRKQ
SQIQNQQGEDSGSDPEDTY

Enzyme 109 Number of Residues

919

Enzyme 109 Molecular Weight

101735.1

Enzyme 109 Theoretical pI

5.30

Enzyme 109 GO Classification

Function
ATP binding DNA binding DNA ligase (ATP) activity DNA ligase (ATP) activity DNA ligase (ATP) activity DNA ligase (ATP) activity DNA ligase activity adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity ligase activity ligase activity, forming phosphoric ester bonds nucleic acid binding nucleoside binding purine nucleoside binding
Process
DNA ligation DNA ligation involved in DNA repair DNA metabolic process DNA recombination DNA repair DNA replication cellular macromolecule metabolic process macromolecule metabolic process metabolic process
Component
—

Enzyme 109 General Function

Involved in DNA ligase (ATP) activity

Enzyme 109 Specific Function

DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair

Enzyme 109 Pathways

Not Available

Enzyme 109 Reactions

ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = AMP + diphosphate + (deoxyribonucleotide)n+m [RN:R00381]

Enzyme 109 Pfam Domain Function

DNA_ligase_A_C (PF04679 )
DNA_ligase_A_M (PF01068 )
DNA_ligase_A_N (PF04675 )

Enzyme 109 Signals

None

Enzyme 109 Transmembrane Regions

None

Enzyme 109 Essentiality

Not Available

Enzyme 109 GenBank ID Protein

187143

Enzyme 109 UniProtKB/Swiss-Prot ID

P18858

Enzyme 109 UniProtKB/Swiss-Prot Entry Name

DNLI1_HUMAN Link Image

Enzyme 109 PDB ID

1X9N

Enzyme 109 PDB File

Show

Enzyme 109 3D Structure

Enzyme 109 Cellular Location

Not Available

Enzyme 109 Gene Sequence

>2760 bp

ATGCAGCGAAGTATCATGTCATTTTTCCACCCCAAGAAAGAGGGTAAAGCAAAGAAGCCT
GAGAAGGAGGCATCCAATAGCAGCAGAGAGACGGAGCCCCCTCCAAAGGCGGCACTGAAG
GAGTGGAATGGAGTGGTGTCCGAGAGTGACTCTCCGGTGAAGAGGCCAGGGAGGAAGGCG
GCCCGGGTCCTGGGCAGCGAAGGGGAAGAGGAGGATGAAGCCCTTAGCCCTGCTAAAGGC
CAGAAGCCTGCCCTGGACTGCTCACAGGTCTCCCCGCCCCGTCCTGCCACATCTCCTGAG
AACAATGCTTCCCTCTCTGACACCTCTCCCATGGACAGTTCCCCATCAGGGATTCCGAAG
CGTCGCACAGCTCGGAAGCAGCTCCCGAAACGGACCATTCAGGAAGTCCTGGAAGAGCAG
AGTGAGGACGAGGACAGAGAAGCCAAGAGGAAGAAGGAGGAGGAAGAAGAGGAGACCCCG
AAAGAAAGCCTCACAGAGGCTGAAGTGGCAACAGAGAAGGAAGGAGAAGACGGGGACCAG
CCCACCACGCCTCCCAAGCCCCTAAAGACCTCCAAAGCAGAGACCCCGACGGAAAGCGTT
TCAGAGCCTGAGGTGGCCACGAAGCAGGAACTGCAGGAGGAGGAAGAGCAGACCAAGCCT
CCCCGCAGAGCTCCCAAGACGCTCAGCAGCTTCTTCACCCCCCGGAAGCCAGCAGTCAAA
AAAGAAGTGAAGGAAGAGGAGCCAGGGGCTCCAGGAAAGGAGGGAGCTGCTGAGGGACCC
CTGGATCCATCTGGTTACAATCCTGCCAAGAACAACTATCATCCCGTGGAAGATGCCTGC
TGGAAACCGGGCCAGAAGGTTCCTTACCTGGCTGTGGCCCGGACGTTTGAGAAGATCGAG
GAGGTGTCTGCTCGGCTCCGGATGGTGGAGACGCTGAGCAACTTGCTGCGCTCCGTGGTG
GCCCTGTCGCCTCCAGACCTCCTCCCTGTCCTCTACCTCAGCCTCAACCACCTTGGGCCA
CCCCAGCAGGGCCTGGAGCTTGGCGTGGGTGATGGTGTCCTTCTCAAGGCAGTGGCCCAG
GCCACAGGTCGGCAGCTGGAGTCCGTCCGGGCTGAGGCAGCCGAGAAAGGCGACGTGGGG
CTGGTGGCCGAGAACAGCCGCAGCACCCAGAGGCTCATGCTGCCACCACCTCCGCTCACT
GCCTCCGGGGTCTTCAGCAAGTTCCGCGACATCGCCAGGCTCACTGGCAGTGCTTCCACA
GCCAAGAAGATAGACATCATCAAAGGCCTCTTTGTGGCCTGCCGCCACTCAGAAGCCCGG
TTCATCGCTAGGTCCCTGAGCGGACGGCTGCGCCTTGGGCTGGCAGAGCAGTCGGTGCTG
GCTGCCCTCTCCCAGGCAGTGAGCCTCACGCCCCCGGGCCAAGAATTCCCACCAGCCATG
GTGGATGCTGGGAAGGGCAAGACAGCAGAGGCCAGAAAGACGTGGCTGGAGGAGCAAGGC
ATGATCCTGAAGCAGACGTTCTGCGAGGTTCCCGACCTGGACCGAATTATCCCCGTGCTG
CTGGAGCACGGCCTGGAACGTCTCCCGGAGCACTGCAAGCTGAGCCCAGGGATTCCCCTG
AAACCAATGTTGGCCCATCCCACCCGGGGCATCAGCGAGGTCCTGAAACGCTTTGAGGAG
GCAGCTTTCACCTGCGAATACAAATATGACGGGCAGAGGGCACAGATCCACGCCCTGGAA
GGCGGGGAGGTGAAGATCTTCAGCAGGAATCAGGAAGACAACACTGGGAAGTACCCGGAC
ATCATCAGCCGCATCCCCAAGATTAAACTCCCATCGGTCACATCCTTCATCCTGGACACC
GAAGCCGTGGCTTGGGACCGGGAAAAGAAGCAGATCCAGCCATTCCAAGTGCTCACCACC
CGCAAACGCAAGGAGGTGGATGCGTCTGAGATCCAGGTGCAGGTGTGTTTGTACGCCTTC
GACCTCATCTACCTCAATGGAGAGTCCCTGGTACGTGAGCCCCTTTCCCGGCGCCGGCAG
CTGCTCCGGGAGAACTTTGTGGAGACAGAGGGCGAGTTTGTCTTCGCCACCTCCCTGGAC
ACCAAGGACATCGAGCAGATCGCCGAGTTCCTGGAGCAGTCAGTGAAAGACTCCTGCGAG
GGGCTGATGGTGAAGACCCTGGATGTTGATGCCACCTACGAGATCGCCAAGAGATCGCAC
AACTGGCTCAAGCTGAAGAAGGACTACCTTGATGGCGTGGGTGACACCCTGGACCTGGTG
GTGATCGGCGCCTACCTGGGCCGGGGGAAGCGGGCCGGCCGGTACGGGGGCTTCCTGCTG
GCCTCCTACGACGAGGACAGTGAGGAGCTGCAGGCCATATGCAAGCTTGGAACTGGCTTC
AGTGATGAGGAGCTGGAGGAGCATCACCAGAGCCTCAAGGCGCTGGTGCTGCCCAGCCCA
CGCCCTTACGTGCGGATAGATGGCGCTGTGATTCCCGACCACTGGCTGGACCCCAGCGCT
GTGTGGGAGGTGAAGTGCGCTGACCTCTCCCTCTCTCCCATCTACCCTGCTGCGCGGGGC
CTGGTGGATAGTGACAAGGGCATCTCCCTTCGCTTCCCTCGGTTTATTCGAGTCCGTGAA
GACAAGCAGCCGGAGCAGGCCACCACCAGTGCTCAGGTGGCCTGTTTGTACCGGAAGCAA
AGTCAGATTCAGAACCAACAAGGCGAGGACTCAGGCTCTGACCCTGAAGATACCTACTAA

Enzyme 109 GenBank Gene ID

M36067

Enzyme 109 GeneCard ID

LIG1

Enzyme 109 GenAtlas ID

LIG1

Enzyme 109 HGNC ID

HGNC:6598

Enzyme 109 Chromosome Location

Enzyme 109 Locus

19q13.2-q13.3

Enzyme 109 SNPs

SNPJam Report Link Image

Enzyme 109 General References

Barnes DE, Johnston LH, Kodama K, Tomkinson AE, Lasko DD, Lindahl T: Human DNA ligase I cDNA: cloning and functional expression in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6679-83. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Petrini JH, Huwiler KG, Weaver DT: A wild-type DNA ligase I gene is expressed in Bloom's syndrome cells. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7615-9. [PubMed ]
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed ]
Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Tan F, Lu L, Cai Y, Wang J, Xie Y, Wang L, Gong Y, Xu BE, Wu J, Luo Y, Qiang B, Yuan J, Sun X, Peng X: Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells. Proteomics. 2008 Jul;8(14):2885-96. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
Pascal JM, O'Brien PJ, Tomkinson AE, Ellenberger T: Human DNA ligase I completely encircles and partially unwinds nicked DNA. Nature. 2004 Nov 25;432(7016):473-8. [PubMed ]
Barnes DE, Tomkinson AE, Lehmann AR, Webster AD, Lindahl T: Mutations in the DNA ligase I gene of an individual with immunodeficiencies and cellular hypersensitivity to DNA-damaging agents. Cell. 1992 May 1;69(3):495-503. [PubMed ]
Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]

Enzyme 109 Metabolite References

Not Available

Enzyme 110 [top]

Enzyme 110 ID

5984

Enzyme 110 Name

Adenylate cyclase type 1

Enzyme 110 Synonyms

ATP pyrophosphate-lyase 1
Adenylate cyclase type I
Adenylyl cyclase 1
Ca(2+)/calmodulin-activated adenylyl cyclase

Enzyme 110 Gene Name

ADCY1

Enzyme 110 Protein Sequence

>Adenylate cyclase type 1

MAGAPRGGGGGGGGAGEPGGAERAAGTSRRRGLRACDEEFACPELEALFRGYTLRLEQAA
TLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQ
QVGQLALLFSLTFALLCCPFALGGPARGSAGAAGGPATAEQGVWQLLLVTFVSYALLPVR
SLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFVGVNMYGVFVRILTERSQR
KAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHD
NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGL
TQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWS
NDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGYGHERNSFLKTHNIETFFIVPSH
RRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALR
TASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQK
YHQLQDEYFTSAVVLTLILAALFGLVYLLIFPQSVVVLLLLVFCICFLVACVLYLHITRV
QCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWAWSSKPNSSLVVLSSGGQRTALP
TLPCESTHHALLCCLVGTLPLAIFFRVSSLPKMILLSGLTTSYILVLELSGYTRTGGGAV
SGRSYEPIVAILLFSCALALHARQVDIRLRLDYLWAAQAEEEREDMEKVKLDNRRILFNL
LPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEI
IADFDELMEKDFYKDIEKIKTIGSTYMAAVGLAPTSGTKAKKSISSHLSTLADFAIEMFD
VLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQV
TEEVHRLLRRCPYHFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQIRSLGLDRKMCPFGRA
GLQGRRPPVCPMPGVSVRAGLPPHSPGQYLPSAAAGKEA

Enzyme 110 Number of Residues

1119

Enzyme 110 Molecular Weight

123438.8

Enzyme 110 Theoretical pI

8.49

Enzyme 110 GO Classification

Function
catalytic activity lyase activity phosphorus-oxygen lyase activity
Process
cellular nitrogen compound metabolic process cyclic nucleotide biosynthetic process intracellular signaling pathway metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside monophosphate biosynthetic process nucleoside monophosphate metabolic process nucleoside phosphate metabolic process nucleotide metabolic process signaling signaling pathway
Component
—

Enzyme 110 General Function

Involved in phosphorus-oxygen lyase activity

Enzyme 110 Specific Function

This is a calmodulin-sensitive adenylyl cyclase. May be involved in regulatory processes in the central nervous system. It may play a role in memory acquisition and learning

Enzyme 110 Pathways

Purine Metabolism (map00230 )

Enzyme 110 Reactions

ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]

Enzyme 110 Pfam Domain Function

Guanylate_cyc (PF00211 )

Enzyme 110 Signals

None

Enzyme 110 Transmembrane Regions

64-84 88-108 125-145 158-178 183-203 214-234 611-631 635-655 674-694 725-745 753-773 775-794

Enzyme 110 Essentiality

Not Available

Enzyme 110 GenBank ID Protein

31083193

Enzyme 110 UniProtKB/Swiss-Prot ID

Q08828

Enzyme 110 UniProtKB/Swiss-Prot Entry Name

ADCY1_HUMAN Link Image

Enzyme 110 PDB ID

Not Available

Enzyme 110 Cellular Location

Not Available

Enzyme 110 Gene Sequence

>3360 bp

ATGGCGGGGGCGCCGCGCGGCGGAGGCGGCGGCGGAGGCGGCGCGGGCGAGCCCGGGGGC
GCCGAGCGGGCGGCCGGGACAAGCCGCCGGCGCGGGCTCCGGGCGTGCGACGAGGAGTTC
GCTTGCCCAGAGCTGGAGGCGCTGTTCCGCGGCTACACGCTGCGGCTGGAGCAGGCGGCC
ACGCTGAAGGCGCTGGCCGTTCTCAGCCTGCTGGCGGGCGCGCTGGCGCTGGCCGAGCTG
CTGGGCGCGCCGGGGCCCGCGCCCGGCCTGGCCAAGGGCTCACACCCGGTGCACTGCGTC
CTCTTCCTGGCGCTGCTCGTGGTAACCAACGTCCGGTCCCTGCAGGTGCCCCAGCTGCAG
CAGGTCGGCCAGCTGGCGCTGCTCTTCAGCCTCACCTTCGCGCTGCTCTGCTGTCCTTTC
GCGCTGGGCGGCCCCGCCCGGGGTTCCGCCGGGGCCGCTGGGGGGCCAGCGACCGCCGAA
CAAGGGGTTTGGCAGCTCCTTTTGGTCACCTTCGTGTCCTATGCCTTGCTGCCCGTGCGC
AGCCTGCTGGCCATAGGCTTTGGGCTCGTGGTGGCTGCGTCGCACTTGCTGGTCACAGCC
ACCTTGGTCCCCGCCAAGCGCCCACGTCTCTGGAGGACGCTCGGTGCCAATGCCTTGCTC
TTCGTCGGTGTGAACATGTATGGGGTCTTTGTGCGGATTCTGACTGAGCGTTCACAGAGG
AAGGCGTTCCTGCAGGCCCGGAGCTGCATTGAGGACCGACTGAGGCTGGAGGATGAGAAC
GAGAAGCAGGAGCGGCTCCTCATGAGCCTCCTGCCCCGGAACGTTGCCATGGAGATGAAG
GAGGACTTCCTGAAGCCCCCTGAGAGGATTTTCCACAAGATTTACATCCAGAGGCACGAC
AATGTGAGCATCCTGTTTGCTGACATCGTGGGTTTCACGGGCTTGGCATCCCAGTGCACA
GCCCAGGAGCTGGTGAAACTCCTCAATGAGCTCTTCGGCAAGTTCGATGAATTAGCCACG
GAGAACCACTGTCGCCGCATCAAGATTCTCGGGGACTGCTACTACTGCGTGTCGGGCCTC
ACCCAGCCCAAGACTGACCATGCCCACTGCTGTGTGGAGATGGGACTCGACATGATTGAT
ACCATCACATCTGTGGCTGAAGCCACCGAGGTGGATCTGAACATGCGTGTGGGTCTGCAC
ACGGGCAGGGTCCTCTGTGGTGTCCTGGGCTTGCGCAAGTGGCAGTACGACGTGTGGTCC
AATGATGTGACCTTGGCCAATGTCATGGAAGCCGCTGGCCTGCCAGGGAAGGTTCATATC
ACAAAGACGACCCTAGCGTGCTTGAATGGGGACTACGAGGTAGAACCGGGTTACGGACAT
GAGAGGAACAGTTTCTTGAAAACTCATAACATCGAAACCTTTTTTATTGTGCCATCCCAT
CGCCGAAAGATATTTCCAGGCCTGATTCTCTCAGATATAAAACCGGCCAAAAGGATGAAG
TTCAAGACTGTCTGCTACCTGCTGGTGCAGCTCATGCACTGCCGGAAAATGTTCAAGGCC
GAGATCCCCTTCTCCAATGTCATGACCTGCGAGGACGATGACAAGCGGAGGGCATTAAGA
ACAGCCTCGGAAAAACTCAGAAACCGCTCATCTTTTTCTACCAACGTTGTCTACACCACC
CCGGGCACTCGCGTCAACAGGTACATCAGCCGCCTCTTAGAAGCCCGCCAGACAGAGCTG
GAGATGGCAGACCTGAACTTCTTTACCCTGAAGTACAAACATGTCGAACGGGAGCAAAAG
TACCACCAGCTTCAGGACGAGTATTTCACCAGCGCCGTTGTCCTCACCCTCATCCTGGCT
GCCTTATTTGGCCTTGTCTACCTTCTAATATTCCCACAGAGTGTGGTCGTCCTGCTCCTG
CTAGTATTCTGCATCTGCTTCCTGGTGGCCTGTGTCCTGTACCTGCACATCACCCGGGTC
CAGTGTTTTCCAGGGTGCCTGACGATTCAGATTCGCACTGTCCTGTGTATTTTCATAGTG
GTCTTAATCTACTCAGTAGCCCAAGGTTGTGTGGTGGGCTGCCTGCCTTGGGCCTGGAGC
TCCAAGCCCAACAGTTCCCTGGTGGTCCTTTCGTCTGGGGGCCAGCGCACAGCCCTGCCC
ACCCTGCCCTGCGAGTCTACACACCATGCCCTGCTCTGCTGCCTGGTGGGCACCCTCCCG
CTAGCCATATTTTTCCGGGTGTCCTCCTTGCCAAAAATGATCCTGCTCTCCGGGCTCACC
ACGTCCTACATCCTCGTTCTGGAGCTCAGCGGATACACCAGGACTGGGGGTGGTGCCGTC
TCCGGGCGCAGCTACGAGCCGATTGTGGCCATCCTGCTCTTCTCCTGTGCGCTGGCCCTG
CATGCCAGGCAGGTGGACATCAGGCTGAGGCTGGACTACCTCTGGGCCGCACAGGCAGAG
GAGGAGCGAGAGGACATGGAGAAGGTGAAGCTGGACAACAGGCGCATCCTCTTCAACCTC
CTGCCGGCCCACGTCGCCCAGCACTTCCTCATGTCCAACCCTCGGAACATGGACCTCTAC
TACCAGTCCTACTCCCAGGTGGGCGTCATGTTTGCCTCCATCCCCAACTTCAATGACTTC
TACATCGAGCTGGACGGCAACAACATGGGGGTGGAGTGTCTGCGGCTTCTCAACGAGATC
ATCGCCGACTTTGACGAGCTCATGGAAAAAGACTTTTACAAGGACATAGAGAAGATCAAG
ACCATCGGGAGCACCTACATGGCCGCTGTGGGGCTAGCGCCCACCTCGGGGACCAAGGCT
AAGAAGTCCATCTCCTCCCACCTGAGCACGCTGGCGGACTTTGCCATTGAGATGTTTGAC
GTTCTGGATGAAATCAACTACCAGTCTTACAACGACTTTGTCCTCCGAGTTGGCATCAAT
GTTGGCCCTGTGGTGGCTGGAGTGATTGGCGCTCGCAGGCCCCAGTACGACATCTGGGGA
AACACAGTCAACGTGGCCAGTCGGATGGATAGCACAGGGGTCCAGGGCAGAATCCAGGTG
ACTGAGGAAGTCCACCGGCTGCTGAGAAGGTGCCCCTACCACTTTGTGTGCCGAGGCAAA
GTCAGTGTCAAGGGCAAAGGCGAGATGTTGACATACTTTCTAGAAGGCAGGACTGATGGA
AACGGCTCCCAAATCAGGTCCCTGGGCTTGGATCGGAAAATGTGTCCATTTGGGAGAGCT
GGCCTTCAGGGCAGACGTCCCCCCGTGTGCCCCATGCCTGGCGTCTCAGTCAGGGCTGGG
CTCCCTCCACACTCCCCAGGCCAGTACCTGCCCTCTGCAGCAGCTGGGAAGGAGGCTTAG

Enzyme 110 GenBank Gene ID

NM_021116.2 Link Image

Enzyme 110 GeneCard ID

ADCY1

Enzyme 110 GenAtlas ID

ADCY1

Enzyme 110 HGNC ID

HGNC:232

Enzyme 110 Chromosome Location

Enzyme 110 Locus

7p13-p12

Enzyme 110 SNPs

SNPJam Report Link Image

Enzyme 110 General References

Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
Villacres EC, Xia Z, Bookbinder LH, Edelhoff S, Disteche CM, Storm DR: Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase. Genomics. 1993 May;16(2):473-8. [PubMed ]

Enzyme 110 Metabolite References

Not Available

Enzyme 111 [top]

Enzyme 111 ID

6983

Enzyme 111 Name

Histidine triad nucleotide-binding protein 1

Enzyme 111 Synonyms

Adenosine 5'-monophosphoramidase
Protein kinase C inhibitor 1
Protein kinase C-interacting protein 1
PKCI-1

Enzyme 111 Gene Name

HINT1

Enzyme 111 Protein Sequence

>Histidine triad nucleotide-binding protein 1

MADEIAKAQVARPGGDTIFGKIIRKEIPAKIIFEDDRCLAFHDISPQAPTHFLVIPKKHI
SQISVAEDDDESLLGHLMIVGKKCAADLGLNKGYRMVVNEGSDGGQSVYHVHLHVLGGRQ
MHWPPG

Enzyme 111 Number of Residues

126

Enzyme 111 Molecular Weight

13801.8

Enzyme 111 Theoretical pI

6.96

Enzyme 111 GO Classification

Function
catalytic activity
Process
—
Component
—

Enzyme 111 General Function

Involved in catalytic activity

Enzyme 111 Specific Function

Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha- acetyl lysine methyl ester and AMP-NH2

Enzyme 111 Pathways

Not Available

Enzyme 111 Reactions

Not Available

Enzyme 111 Pfam Domain Function

HIT (PF01230 )

Enzyme 111 Signals

None

Enzyme 111 Transmembrane Regions

None

Enzyme 111 Essentiality

Not Available

Enzyme 111 GenBank ID Protein

10439439

Enzyme 111 UniProtKB/Swiss-Prot ID

P49773

Enzyme 111 UniProtKB/Swiss-Prot Entry Name

HINT1_HUMAN Link Image

Enzyme 111 PDB ID

1KPF

Enzyme 111 PDB File

Show

Enzyme 111 3D Structure

Enzyme 111 Cellular Location

Not Available

Enzyme 111 Gene Sequence

>381 bp

ATGGCAGATGAGATTGCCAAGGCTCAGGTCGCTCGGCCTGGTGGCGACACGATCTTTGGG
AAGATCATCCGCGAGGAAATACCAGCCAAAATCATTTTTGAGGATGACCGGTGCCTTGCT
TTCCATGACATTTCCCCTCAAGCACCAACACATTTTCTGGTGATACCCAAGAAACATATA
TCCCAGATTTCTGTGGCAGAAGATGATGATGAAAGTCTTCTTGGACACTTAATGATTGTT
GGCAAGAAATGTGCTGCTGATCTGGGCCTGAATAAGGGTTATCGAATGGTGGTGAATGAA
GGTTCAGATGGTGGACAGTCTGTCTATCACGTTCATCTCCATGTTCTTGGAGGTCGGCAA
ATGCATTGGCCTCCTGGTTAA

Enzyme 111 GenBank Gene ID

AK026557

Enzyme 111 GeneCard ID

HINT1

Enzyme 111 GenAtlas ID

HINT1

Enzyme 111 HGNC ID

HGNC:4912

Enzyme 111 Chromosome Location

Enzyme 111 Locus

5q31.2

Enzyme 111 SNPs

SNPJam Report Link Image

Enzyme 111 General References

Brzoska PM, Chen H, Levin NA, Kuo WL, Collins C, Fu KK, Gray JW, Christman MF: Cloning, mapping, and in vivo localization of a human member of the PKCI-1 protein family (PRKCNH1). Genomics. 1996 Aug 15;36(1):151-6. [PubMed ]
Brzoska PM, Chen H, Zhu Y, Levin NA, Disatnik MH, Mochly-Rosen D, Murnane JP, Christman MF: The product of the ataxia-telangiectasia group D complementing gene, ATDC, interacts with a protein kinase C substrate and inhibitor. Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7824-8. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Lima CD, Klein MG, Weinstein IB, Hendrickson WA: Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins. Proc Natl Acad Sci U S A. 1996 May 28;93(11):5357-62. [PubMed ]
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
Lima CD, Klein MG, Hendrickson WA: Structure-based analysis of catalysis and substrate definition in the HIT protein family. Science. 1997 Oct 10;278(5336):286-90. [PubMed ]

Enzyme 111 Metabolite References

Not Available

Enzyme 112 [top]

Enzyme 112 ID

7615

Enzyme 112 Name

Cyclic AMP-responsive element-binding protein 1

Enzyme 112 Synonyms

CREB-1
cAMP-responsive element-binding protein 1

Enzyme 112 Gene Name

CREB1

Enzyme 112 Protein Sequence

>Cyclic AMP-responsive element-binding protein 1

MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPN
GQTVQVHGVIQAAQPSVIQSPQVQTVQSSCKDLKRLFSGTQISTIAESEDSQESVDSVTD
SQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSG
QYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQV
VVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAAREC
RRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD

Enzyme 112 Number of Residues

341

Enzyme 112 Molecular Weight

36687.9

Enzyme 112 Theoretical pI

5.24

Enzyme 112 GO Classification

Function
DNA binding binding nucleic acid binding protein binding protein dimerization activity sequence-specific DNA binding sequence-specific DNA binding transcription factor activity
Process
biological regulation regulation of biological process regulation of gene expression regulation of macromolecule metabolic process regulation of metabolic process regulation of transcription regulation of transcription, DNA-dependent
Component
intracellular membrane-bounded organelle membrane-bounded organelle nucleus organelle

Enzyme 112 General Function

Involved in sequence-specific DNA binding transcription factor activity

Enzyme 112 Specific Function

This protein binds the cAMP response element (CRE), a sequence present in many viral and cellular promoters. CREB stimulates transcription on binding to the CRE. Transcription activation is enhanced by the TORC coactivators which act independently of Ser-133 phosphorylation. Implicated in synchronization of circadian rhythmicity

Enzyme 112 Pathways

Not Available

Enzyme 112 Reactions

Not Available

Enzyme 112 Pfam Domain Function

bZIP_1 (PF00170 )
pKID (PF02173 )

Enzyme 112 Signals

None

Enzyme 112 Transmembrane Regions

None

Enzyme 112 Essentiality

Not Available

Enzyme 112 GenBank ID Protein

287638

Enzyme 112 UniProtKB/Swiss-Prot ID

P16220

Enzyme 112 UniProtKB/Swiss-Prot Entry Name

CREB1_HUMAN Link Image

Enzyme 112 PDB ID

Not Available

Enzyme 112 Cellular Location

Not Available

Enzyme 112 Gene Sequence

>1026 bp

ATGACCATGGAATCTGGAGCCGAGAACCAGCAGAGTGGAGATGCAGCTGTAACAGAAGCT
GAAAACCAACAAATGACAGTTCAAGCCCAGCCACAGATTGCCACATTAGCCCAGGTATCT
ATGCCAGCAGCTCATGCAACATCATCTGCTCCCACCGTAACTCTAGTACAGCTGCCCAAT
GGGCAGACAGTTCAAGTCCATGGAGTCATTCAGGCGGCCCAGCCATCAGTTATTCAGTCT
CCACAAGTCCAAACAGTTCAGTCTTCCTGTAAGGACTTAAAAAGACTTTTCTCCGGAACA
CAGATTTCAACTATTGCAGAAAGTGAAGATTCACAGGAGTCAGTGGATAGTGTAACTGAT
TCCCAAAAGCGAAGGGAAATTCTTTCAAGGAGGCCTTCCTACAGGAAAATTTTGAATGAC
TTATCTTCTGATGCACCAGGAGTGCCAAGGATTGAAGAAGAGAAGTCTGAAGAGGAGACT
TCAGCACCTGCCATCACCACTGTAACGGTGCCAACTCCAATTTACCAAACTAGCAGTGGA
CAGTATATTGCCATTACCCAGGGAGGAGCAATACAGCTGGCTAACAATGGTACCGATGGG
GTACAGGGCCTGCAAACATTAACCATGACCAATGCAGCAGCCACTCAGCCGGGTACTACC
ATTCTACAGTATGCACAGACCACTGATGGACAGCAGATCTTAGTGCCCAGCAACCAAGTT
GTTGTTCAAGCTGCCTCTGGAGACGTACAAACATACCAGATTCGCACAGCACCCACTAGC
ACTATTGCCCCTGGAGTTGTTATGGCATCCTCCCCAGCACTTCCTACACAGCCTGCTGAA
GAAGCAGCACGAAAGAGAGAGGTCCGTCTAATGAAGAACAGGGAAGCAGCTCGAGAGTGT
CGTAGAAAGAAGAAAGAATATGTGAAATGTTTAGAAAACAGAGTGGCAGTGCTTGAAAAT
CAAAACAAGACATTGATTGAGGAGCTAAAAGCACTTAAGGACCTTTACTGCCACAAATCA
GATTAA

Enzyme 112 GenBank Gene ID

X55545

Enzyme 112 GeneCard ID

CREB1

Enzyme 112 GenAtlas ID

CREB1

Enzyme 112 HGNC ID

HGNC:2345

Enzyme 112 Chromosome Location

Enzyme 112 Locus

2q34

Enzyme 112 SNPs

SNPJam Report Link Image

Enzyme 112 General References

Berkowitz LA, Gilman MZ: Two distinct forms of active transcription factor CREB (cAMP response element binding protein). Proc Natl Acad Sci U S A. 1990 Jul;87(14):5258-62. [PubMed ]
Yoshimura T, Fujisawa J, Yoshida M: Multiple cDNA clones encoding nuclear proteins that bind to the tax-dependent enhancer of HTLV-1: all contain a leucine zipper structure and basic amino acid domain. EMBO J. 1990 Aug;9(8):2537-42. [PubMed ]
Waeber G, Meyer TE, Hoeffler JP, Habener JF: Diversification of cyclic AMP-responsive enhancer binding proteins-generated by alternative exon splicing. Trans Assoc Am Physicians. 1990;103:28-37. [PubMed ]
Hoeffler JP, Meyer TE, Yun Y, Jameson JL, Habener JF: Cyclic AMP-responsive DNA-binding protein: structure based on a cloned placental cDNA. Science. 1988 Dec 9;242(4884):1430-3. [PubMed ]
Short ML, Manohar CF, Furtado MR, Ghadge GD, Wolinsky SM, Thimmapaya B, Jungmann RA: Nucleotide and derived amino-acid sequences of the CRE-binding proteins from rat C6 glioma and HeLa cells. Nucleic Acids Res. 1991 Aug 11;19(15):4290. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Meyer TE, Waeber G, Lin J, Beckmann W, Habener JF: The promoter of the gene encoding 3',5'-cyclic adenosine monophosphate (cAMP) response element binding protein contains cAMP response elements: evidence for positive autoregulation of gene transcription. Endocrinology. 1993 Feb;132(2):770-80. [PubMed ]
Maguire HF, Hoeffler JP, Siddiqui A: HBV X protein alters the DNA binding specificity of CREB and ATF-2 by protein-protein interactions. Science. 1991 May 10;252(5007):842-4. [PubMed ]
Zhao LJ, Giam CZ: Human T-cell lymphotropic virus type I (HTLV-I) transcriptional activator, Tax, enhances CREB binding to HTLV-I 21-base-pair repeats by protein-protein interaction. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):7070-4. [PubMed ]
Lee HJ, Mignacca RC, Sakamoto KM: Transcriptional activation of egr-1 by granulocyte-macrophage colony-stimulating factor but not interleukin 3 requires phosphorylation of cAMP response element-binding protein (CREB) on serine 133. J Biol Chem. 1995 Jul 7;270(27):15979-83. [PubMed ]
Conkright MD, Canettieri G, Screaton R, Guzman E, Miraglia L, Hogenesch JB, Montminy M: TORCs: transducers of regulated CREB activity. Mol Cell. 2003 Aug;12(2):413-23. [PubMed ]
Iourgenko V, Zhang W, Mickanin C, Daly I, Jiang C, Hexham JM, Orth AP, Miraglia L, Meltzer J, Garza D, Chirn GW, McWhinnie E, Cohen D, Skelton J, Terry R, Yu Y, Bodian D, Buxton FP, Zhu J, Song C, Labow MA: Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells. Proc Natl Acad Sci U S A. 2003 Oct 14;100(21):12147-52. Epub 2003 Sep 23. [PubMed ]
Screaton RA, Conkright MD, Katoh Y, Best JL, Canettieri G, Jeffries S, Guzman E, Niessen S, Yates JR 3rd, Takemori H, Okamoto M, Montminy M: The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector. Cell. 2004 Oct 1;119(1):61-74. [PubMed ]
Kang J, Shi Y, Xiang B, Qu B, Su W, Zhu M, Zhang M, Bao G, Wang F, Zhang X, Yang R, Fan F, Chen X, Pei G, Ma L: A nuclear function of beta-arrestin1 in GPCR signaling: regulation of histone acetylation and gene transcription. Cell. 2005 Dec 2;123(5):833-47. [PubMed ]
Vercauteren K, Pasko RA, Gleyzer N, Marino VM, Scarpulla RC: PGC-1-related coactivator: immediate early expression and characterization of a CREB/NRF-1 binding domain associated with cytochrome c promoter occupancy and respiratory growth. Mol Cell Biol. 2006 Oct;26(20):7409-19. Epub 2006 Aug 14. [PubMed ]
Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed ]
Antonescu CR, Dal Cin P, Nafa K, Teot LA, Surti U, Fletcher CD, Ladanyi M: EWSR1-CREB1 is the predominant gene fusion in angiomatoid fibrous histiocytoma. Genes Chromosomes Cancer. 2007 Dec;46(12):1051-60. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]

Enzyme 112 Metabolite References

Not Available

Enzyme 113 [top]

Enzyme 113 ID

7767

Enzyme 113 Name

E3 ubiquitin-protein ligase NEDD4-like

Enzyme 113 Synonyms

NEDD4.2
Nedd4-2

Enzyme 113 Gene Name

NEDD4L

Enzyme 113 Protein Sequence

>E3 ubiquitin-protein ligase NEDD4-like

MATGLGEPVYGLSEDEGESRILRVKVVSGIDLAKKDIFGASDPYVKLSLYVADENRELAL
VQTKTIKKTLNPKWNEEFYFRVNPSNHRLLFEVFDENRLTRDDFLGQVDVPLSHLPTEDP
TMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSDQRDDMEHGWEVVDSN
DSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRTTQWHRPSLMDVSSESDNNIRQI
NQEAAHRRFRSRRHISEDLEPEPSEGGDVPEPWETISEEVNIAGDSLGLALPPPPASPGS
RTSPQELSEELSRRLQITPDSNGEQFSSLIQREPSSRLRSCSVTDAVAEQGHLPPPSAPA
GRARSSTVTGGEEPTPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQL
AEDGASGSATNSNNHLIEPQIRRPRSLSSPTVTLSAPLEGAKDSPVRRAVKDTLSNPQSP
QPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKT
SLNPNDLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPAITGPAVPYSREFKQK
YDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDY
GGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLA
VFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEE
NFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLI
KIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQ
FVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREK
LLMAVENAQGFEGVD

Enzyme 113 Number of Residues

975

Enzyme 113 Molecular Weight

111930.9

Enzyme 113 Theoretical pI

5.60

Enzyme 113 GO Classification

Function
acid-amino acid ligase activity binding catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds protein binding
Process
macromolecule metabolic process macromolecule modification metabolic process protein modification process
Component
cell part intracellular

Enzyme 113 General Function

Involved in acid-amino acid ligase activity

Enzyme 113 Specific Function

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Inhibits TGF-beta signaling by triggering SMAD2 and TGFR1 ubiquitination and proteasome-dependent degradation. Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, Nav1.2, Nav1.3, Nav1.5, Nav1.7, Nav1.8, Kv1.3, EAAT1 or CLC5. Promotes ubiquitination and degradation of SGK

Enzyme 113 Pathways

Not Available

Enzyme 113 Reactions

Not Available

Enzyme 113 Pfam Domain Function

C2 (PF00168 )
HECT (PF00632 )
WW (PF00397 )

Enzyme 113 Signals

None

Enzyme 113 Transmembrane Regions

None

Enzyme 113 Essentiality

Not Available

Enzyme 113 GenBank ID Protein

222352086

Enzyme 113 UniProtKB/Swiss-Prot ID

Q96PU5

Enzyme 113 UniProtKB/Swiss-Prot Entry Name

NED4L_HUMAN Link Image

Enzyme 113 PDB ID

Not Available

Enzyme 113 Cellular Location

Not Available

Enzyme 113 Gene Sequence

>2928 bp

ATGGCGACCGGGCTCGGGGAGCCGGTCTATGGACTTTCCGAAGACGAGGGAGAGTCCCGT
ATTCTCAGAGTAAAAGTTGTTTCTGGAATTGATCTCGCCAAAAAGGACATCTTTGGAGCC
AGTGATCCGTATGTGAAACTTTCATTGTACGTAGCGGATGAGAATAGAGAACTTGCTTTG
GTCCAGACAAAAACAATTAAAAAGACACTGAACCCAAAATGGAATGAAGAATTTTATTTC
AGGGTAAACCCATCTAATCACAGACTCCTATTTGAAGTATTTGACGAAAATAGACTGACA
CGAGACGACTTCCTGGGCCAGGTGGACGTGCCCCTTAGTCACCTTCCGACAGAAGATCCA
ACCATGGAGCGACCCTATACATTTAAGGACTTTCTCCTCAGACCAAGAAGTCATAAGTCT
CGAGTTAAGGGATTTTTGCGATTGAAAATGGCCTATATGCCAAAAAATGGAGGTCAAGAT
GAAGAAAACAGTGACCAGAGGGATGACATGGAGCATGGATGGGAAGTTGTTGACTCAAAT
GACTCGGCTTCTCAGCACCAAGAGGAACTTCCTCCTCCTCCTCTGCCTCCCGGGTGGGAA
GAAAAAGTGGACAATTTAGGCCGAACTTACTATGTCAACCACAACAACCGGACCACTCAG
TGGCACAGACCAAGCCTGATGGACGTGTCCTCGGAGTCGGACAATAACATCAGACAGATC
AACCAGGAGGCAGCACACCGGCGCTTCCGCTCCCGCAGGCACATCAGCGAAGACTTGGAG
CCCGAGCCCTCGGAGGGCGGGGATGTCCCCGAGCCTTGGGAGACCATTTCAGAGGAAGTG
AATATCGCTGGAGACTCTCTCGGTCTGGCTCTGCCCCCACCACCGGCCTCCCCAGGATCT
CGGACCAGCCCTCAGGAGCTGTCAGAGGAACTAAGCAGAAGGCTTCAGATCACTCCAGAC
TCCAATGGGGAACAGTTCAGCTCTTTGATTCAAAGAGAACCCTCCTCAAGGTTGAGGTCA
TGCAGTGTCACCGACGCAGTTGCAGAACAGGGCCATCTACCACCGCCCAGTGCCCCAGCT
GGGAGAGCGCGTTCATCAACTGTCACGGGTGGTGAGGAACCAACGCCATCAGTGGCCTAT
GTACATACCACGCCGGGTCTGCCTTCAGGCTGGGAAGAAAGAAAAGATGCTAAGGGGCGC
ACATACTATGTCAATCATAACAATCGAACCACAACTTGGACTCGACCTATCATGCAGCTT
GCAGAAGATGGTGCGTCCGGATCAGCCACAAACAGTAACAACCATCTAATCGAGCCTCAG
ATCCGCCGGCCTCGTAGCCTCAGCTCGCCAACAGTAACTTTATCTGCCCCGCTGGAGGGT
GCCAAGGACTCACCCGTACGTCGGGCTGTGAAAGACACCCTTTCCAACCCACAGTCCCCA
CAGCCATCACCTTACAACTCCCCCAAACCACAACACAAAGTCACACAGAGCTTCTTGCCA
CCCGGCTGGGAAATGAGGATAGCGCCAAACGGCCGGCCCTTCTTCATTGATCATAACACA
AAGACTACAACCTGGGAAGATCCACGTTTGAAATTTCCAGTACATATGCGGTCAAAGACA
TCTTTAAACCCCAATGACCTTGGCCCCCTTCCTCCTGGCTGGGAAGAAAGAATTCACTTG
GATGGCCGAACGTTTTATATTGATCATAATAGCAAAATTACTCAGTGGGAAGACCCAAGA
CTGCAGAACCCAGCTATTACTGGTCCGGCTGTCCCTTACTCCAGAGAATTTAAGCAGAAA
TATGACTACTTCAGGAAGAAATTAAAGAAACCTGCTGATATCCCCAATAGGTTTGAAATG
AAACTTCACAGAAATAACATATTTGAAGAGTCCTATCGGAGAATTATGTCCGTGAAAAGA
CCAGATGTCCTAAAAGCTAGACTGTGGATTGAGTTTGAATCAGAGAAAGGTCTTGACTAT
GGGGGTGTGGCCAGAGAATGGTTCTTCTTACTGTCCAAAGAGATGTTCAACCCCTACTAC
GGCCTCTTTGAGTACTCTGCCACGGACAACTACACCCTTCAGATCAACCCTAATTCAGGC
CTCTGTAATGAGGATCATTTGTCCTACTTCACTTTTATTGGAAGAGTTGCTGGTCTGGCC
GTATTTCATGGGAAGCTCTTAGATGGTTTCTTCATTAGACCATTTTACAAGATGATGTTG
GGAAAGCAGATAACCCTGAATGACATGGAATCTGTGGATAGTGAATATTACAACTCTTTG
AAATGGATCCTGGAGAATGACCCTACTGAGCTGGACCTCATGTTCTGCATAGACGAAGAA
AACTTTGGACAGACATATCAAGTGGATTTGAAGCCCAATGGGTCAGAAATAATGGTCACA
AATGAAAACAAAAGGGAATATATCGACTTAGTCATCCAGTGGAGATTTGTGAACAGGGTC
CAGAAGCAGATGAACGCCTTCTTGGAGGGATTCACAGAACTACTTCCTATTGATTTGATT
AAAATTTTTGATGAAAATGAGCTGGAGTTGCTCATGTGCGGCCTCGGTGATGTGGATGTG
AATGACTGGAGACAGCATTCTATTTACAAGAACGGCTACTGCCCAAACCACCCCGTCATT
CAGTGGTTCTGGAAGGCTGTGCTACTCATGGACGCCGAAAAGCGTATCCGGTTACTGCAG
TTTGTCACAGGGACATCGCGAGTACCTATGAATGGATTTGCCGAACTTTATGGTTCCAAT
GGTCCTCAGCTGTTTACAATAGAGCAATGGGGCAGTCCTGAGAAACTGCCCAGAGCTCAC
ACATGCTTTAATCGCCTTGACTTACCTCCATATGAAACCTTTGAAGATTTACGAGAGAAA
CTTCTCATGGCCGTGGAAAATGCTCAAGGATTTGAAGGGGTGGATTAA

Enzyme 113 GenBank Gene ID

NM_001144967.1 Link Image

Enzyme 113 GeneCard ID

NEDD4L

Enzyme 113 GenAtlas ID

NEDD4L

Enzyme 113 HGNC ID

HGNC:7728

Enzyme 113 Chromosome Location

Enzyme 113 Locus

18q21

Enzyme 113 SNPs

SNPJam Report Link Image

Enzyme 113 General References

Chen H, Ross CA, Wang N, Huo Y, MacKinnon DF, Potash JB, Simpson SG, McMahon FJ, DePaulo Jr JR, McInnis MG: NEDD4L on human chromosome 18q21 has multiple forms of transcripts and is a homologue of the mouse Nedd4-2 gene. Eur J Hum Genet. 2001 Dec;9(12):922-30. [PubMed ]
Malbert-Colas L, Nicolas G, Galand C, Lecomte MC, Dhermy D: Identification of new partners of the epithelial sodium channel alpha subunit. C R Biol. 2003 Jul;326(7):615-24. [PubMed ]
Qi H, Grenier J, Fournier A, Labrie C: Androgens differentially regulate the expression of NEDD4L transcripts in LNCaP human prostate cancer cells. Mol Cell Endocrinol. 2003 Nov 28;210(1-2):51-62. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [PubMed ]
Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
Ichimura T, Yamamura H, Sasamoto K, Tominaga Y, Taoka M, Kakiuchi K, Shinkawa T, Takahashi N, Shimada S, Isobe T: 14-3-3 proteins modulate the expression of epithelial Na+ channels by phosphorylation-dependent interaction with Nedd4-2 ubiquitin ligase. J Biol Chem. 2005 Apr 1;280(13):13187-94. Epub 2005 Jan 26. [PubMed ]
Winberg G, Matskova L, Chen F, Plant P, Rotin D, Gish G, Ingham R, Ernberg I, Pawson T: Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases. Mol Cell Biol. 2000 Nov;20(22):8526-35. [PubMed ]
Snyder PM, Olson DR, Thomas BC: Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel. J Biol Chem. 2002 Jan 4;277(1):5-8. Epub 2001 Nov 5. [PubMed ]
Harvey KF, Shearwin-Whyatt LM, Fotia A, Parton RG, Kumar S: N4WBP5, a potential target for ubiquitination by the Nedd4 family of proteins, is a novel Golgi-associated protein. J Biol Chem. 2002 Mar 15;277(11):9307-17. Epub 2001 Dec 17. [PubMed ]
Boehmer C, Henke G, Schniepp R, Palmada M, Rothstein JD, Broer S, Lang F: Regulation of the glutamate transporter EAAT1 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid-inducible kinase isoforms SGK1/3 and protein kinase B. J Neurochem. 2003 Sep;86(5):1181-8. [PubMed ]
van Bemmelen MX, Rougier JS, Gavillet B, Apotheloz F, Daidie D, Tateyama M, Rivolta I, Thomas MA, Kass RS, Staub O, Abriel H: Cardiac voltage-gated sodium channel Nav1.5 is regulated by Nedd4-2 mediated ubiquitination. Circ Res. 2004 Aug 6;95(3):284-91. Epub 2004 Jun 24. [PubMed ]
Hryciw DH, Ekberg J, Lee A, Lensink IL, Kumar S, Guggino WB, Cook DI, Pollock CA, Poronnik P: Nedd4-2 functionally interacts with ClC-5: involvement in constitutive albumin endocytosis in proximal tubule cells. J Biol Chem. 2004 Dec 31;279(53):54996-5007. Epub 2004 Oct 15. [PubMed ]
Snyder PM, Olson DR, Kabra R, Zhou R, Steines JC: cAMP and serum and glucocorticoid-inducible kinase (SGK) regulate the epithelial Na(+) channel through convergent phosphorylation of Nedd4-2. J Biol Chem. 2004 Oct 29;279(44):45753-8. Epub 2004 Aug 24. [PubMed ]
Henke G, Maier G, Wallisch S, Boehmer C, Lang F: Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1. J Cell Physiol. 2004 May;199(2):194-9. [PubMed ]
Rougier JS, van Bemmelen MX, Bruce MC, Jespersen T, Gavillet B, Apotheloz F, Cordonier S, Staub O, Rotin D, Abriel H: Molecular determinants of voltage-gated sodium channel regulation by the Nedd4/Nedd4-like proteins. Am J Physiol Cell Physiol. 2005 Mar;288(3):C692-701. Epub 2004 Nov 17. [PubMed ]
Kuratomi G, Komuro A, Goto K, Shinozaki M, Miyazawa K, Miyazono K, Imamura T: NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-beta (transforming growth factor-beta) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta type I receptor. Biochem J. 2005 Mar 15;386(Pt 3):461-70. [PubMed ]
Zhou R, Snyder PM: Nedd4-2 phosphorylation induces serum and glucocorticoid-regulated kinase (SGK) ubiquitination and degradation. J Biol Chem. 2005 Feb 11;280(6):4518-23. Epub 2004 Dec 2. [PubMed ]
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
Putz U, Howitt J, Lackovic J, Foot N, Kumar S, Silke J, Tan SS: Nedd4 family-interacting protein 1 (Ndfip1) is required for the exosomal secretion of Nedd4 family proteins. J Biol Chem. 2008 Nov 21;283(47):32621-7. Epub 2008 Sep 25. [PubMed ]
Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
Mund T, Pelham HR: Control of the activity of WW-HECT domain E3 ubiquitin ligases by NDFIP proteins. EMBO Rep. 2009 May;10(5):501-7. Epub 2009 Apr 3. [PubMed ]
Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
Fouladkou F, Alikhani-Koopaei R, Vogt B, Flores SY, Malbert-Colas L, Lecomte MC, Loffing J, Frey FJ, Frey BM, Staub O: A naturally occurring human Nedd4-2 variant displays impaired ENaC regulation in Xenopus laevis oocytes. Am J Physiol Renal Physiol. 2004 Sep;287(3):F550-61. Epub 2004 May 12. [PubMed ]

Enzyme 113 Metabolite References

Not Available

Enzyme 114 [top]

Enzyme 114 ID

7926

Enzyme 114 Name

E3 ubiquitin-protein ligase Mdm2

Enzyme 114 Synonyms

Double minute 2 protein
Hdm2
Oncoprotein Mdm2
p53-binding protein Mdm2

Enzyme 114 Gene Name

MDM2

Enzyme 114 Protein Sequence

>E3 ubiquitin-protein ligase Mdm2

MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQY
IMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGT
SVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQ
RKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDS
VSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLA
DYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVP
DCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQ
DKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQ
PIQMIVLTYFP

Enzyme 114 Number of Residues

491

Enzyme 114 Molecular Weight

55232.4

Enzyme 114 Theoretical pI

4.32

Enzyme 114 GO Classification

Function
binding cation binding ion binding metal ion binding protein binding transition metal ion binding zinc ion binding
Process
—
Component
cell part intracellular

Enzyme 114 General Function

Involved in negative regulation of apoptosis

Enzyme 114 Specific Function

E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degration by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as an ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of TP53/p53. Promotes proteasome-dependent ubiquitin- independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation

Enzyme 114 Pathways

Not Available

Enzyme 114 Reactions

Not Available

Enzyme 114 Pfam Domain Function

SWIB (PF02201 )
zf-RanBP (PF00641 )

Enzyme 114 Signals

None

Enzyme 114 Transmembrane Regions

None

Enzyme 114 Essentiality

Not Available

Enzyme 114 GenBank ID Protein

Not Available

Enzyme 114 UniProtKB/Swiss-Prot ID

Q00987

Enzyme 114 UniProtKB/Swiss-Prot Entry Name

MDM2_HUMAN Link Image

Enzyme 114 PDB ID

1T4F

Enzyme 114 PDB File

Show

Enzyme 114 3D Structure

Enzyme 114 Cellular Location

Not Available

Enzyme 114 Gene Sequence

>1476 bp

ATGTGCAATACCAACATGTCTGTACCTACTGATGGTGCTGTAACCACCTCACAGATTCCA
GCTTCGGAACAAGAGACCCTGGTTAGACCAAAGCCATTGCTTTTGAAGTTATTAAAGTCT
GTTGGTGCACAAAAAGACACTTATACTATGAAAGAGGTTCTTTTTTATCTTGGCCAGTAT
ATTATGACTAAACGATTATATGATGAGAAGCAACAACATATTGTATATTGTTCAAATGAT
CTTCTAGGAGATTTGTTTGGCGTGCCAAGCTTCTCTGTGAAAGAGCACAGGAAAATATAT
ACCATGATCTACAGGAACTTGGTAGTAGTCAATCAGCAGGAATCATCGGACTCAGGTACA
TCTGTGAGTGAGAACAGGTGTCACCTTGAAGGTGGGAGTGATCAAAAGGACCTTGTACAA
GAGCTTCAGGAAGAGAAACCTTCATCTTCACATTTGGTTTCTAGACCATCTACCTCATCT
AGAAGGAGAGCAATTAGTGAGACAGAAGAAAATTCAGATGAATTATCTGGTGAACGACAA
AGAAAACGCCACAAATCTGATAGTATTTCCCTTTCCTTTGATGAAAGCCTGGCTCTGTGT
GTAATAAGGGAGATATGTTGTGAAAGAAGCAGTAGCAGTGAATCTACAGGGACGCCATCG
AATCCGGATCTTGATGCTGGTGTAAGTGAACATTCAGGTGATTGGTTGGATCAGGATTCA
GTTTCAGATCAGTTTAGTGTAGAATTTGAAGTTGAATCTCTCGACTCAGAAGATTATAGC
CTTAGTGAAGAAGGACAAGAACTCTCAGATGAAGATGATGAGGTATATCAAGTTACTGTG
TATCAGGCAGGGGAGAGTGATACAGATTCATTTGAAGAAGATCCTGAAATTTCCTTAGCT
GACTATTGGAAATGCACTTCATGCAATGAAATGAATCCCCCCCTTCCATCACATTGCAAC
AGATGTTGGGCCCTTCGTGAGAATTGGCTTCCTGAAGATAAAGGGAAAGATAAAGGGGAA
ATCTCTGAGAAAGCCAAACTGGAAAACTCAACACAAGCTGAAGAGGGCTTTGATGTTCCT
GATTGTAAAAAAACTATAGTGAATGATTCCAGAGAGTCATGTGTTGAGGAAAATGATGAT
AAAATTACACAAGCTTCACAATCACAAGAAAGTGAAGACTATTCTCAGCCATCAACTTCT
AGTAGCATTATTTATAGCAGCCAAGAAGATGTGAAAGAGTTTGAAAGGGAAGAAACCCAA
GACAAAGAAGAGAGTGTGGAATCTAGTTTGCCCCTTAATGCCATTGAACCTTGTGTGATT
TGTCAAGGTCGACCTAAAAATGGTTGCATTGTCCATGGCAAAACAGGACATCTTATGGCC
TGCTTTACATGTGCAAAGAAGCTAAAGAAAAGGAATAAGCCCTGCCCAGTATGTAGACAA
CCAATTCAAATGATTGTGCTAACTTATTTCCCCTAG

Enzyme 114 GenBank Gene ID

M92424

Enzyme 114 GeneCard ID

MDM2

Enzyme 114 GenAtlas ID

MDM2

Enzyme 114 HGNC ID

HGNC:6973

Enzyme 114 Chromosome Location

Enzyme 114 Locus

12q14.3-q15

Enzyme 114 SNPs

SNPJam Report Link Image

Enzyme 114 General References

Oliner JD, Kinzler KW, Meltzer PS, George DL, Vogelstein B: Amplification of a gene encoding a p53-associated protein in human sarcomas. Nature. 1992 Jul 2;358(6381):80-3. [PubMed ]
Sigalas I, Calvert AH, Anderson JJ, Neal DE, Lunec J: Alternatively spliced mdm2 transcripts with loss of p53 binding domain sequences: transforming ability and frequent detection in human cancer. Nat Med. 1996 Aug;2(8):912-7. [PubMed ]
Veldhoen N, Metcalfe S, Milner J: A novel exon within the mdm2 gene modulates translation initiation in vitro and disrupts the p53-binding domain of mdm2 protein. Oncogene. 1999 Nov 25;18(50):7026-33. [PubMed ]
Tamborini E, Della Torre G, Lavarino C, Azzarelli A, Carpinelli P, Pierotti MA, Pilotti S: Analysis of the molecular species generated by MDM2 gene amplification in liposarcomas. Int J Cancer. 2001 Jun 15;92(6):790-6. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Zauberman A, Flusberg D, Haupt Y, Barak Y, Oren M: A functional p53-responsive intronic promoter is contained within the human mdm2 gene. Nucleic Acids Res. 1995 Jul 25;23(14):2584-92. [PubMed ]
Landers JE, Cassel SL, George DL: Translational enhancement of mdm2 oncogene expression in human tumor cells containing a stabilized wild-type p53 protein. Cancer Res. 1997 Aug 15;57(16):3562-8. [PubMed ]
Liang H, Atkins H, Abdel-Fattah R, Jones SN, Lunec J: Genomic organisation of the human MDM2 oncogene and relationship to its alternatively spliced mRNAs. Gene. 2004 Sep 1;338(2):217-23. [PubMed ]
Taubert H, Kappler M, Meye A, Bartel F, Schlott T, Lautenschlager C, Bache M, Schmidt H, Wurl P: A MboII polymorphism in exon 11 of the human MDM2 gene occuring in normal blood donors and in soft tissue sarcoma patients: an indication for an increased cancer susceptibility? Mutat Res. 2000 Nov 30;456(1-2):39-44. [PubMed ]
Olson DC, Marechal V, Momand J, Chen J, Romocki C, Levine AJ: Identification and characterization of multiple mdm-2 proteins and mdm-2-p53 protein complexes. Oncogene. 1993 Sep;8(9):2353-60. [PubMed ]
Honda R, Tanaka H, Yasuda H: Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 1997 Dec 22;420(1):25-7. [PubMed ]
Sharp DA, Kratowicz SA, Sank MJ, George DL: Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. J Biol Chem. 1999 Dec 31;274(53):38189-96. [PubMed ]
Khosravi R, Maya R, Gottlieb T, Oren M, Shiloh Y, Shkedy D: Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage. Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14973-7. [PubMed ]
Fang S, Jensen JP, Ludwig RL, Vousden KH, Weissman AM: Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J Biol Chem. 2000 Mar 24;275(12):8945-51. [PubMed ]
Lohrum MA, Ashcroft M, Kubbutat MH, Vousden KH: Identification of a cryptic nucleolar-localization signal in MDM2. Nat Cell Biol. 2000 Mar;2(3):179-81. [PubMed ]
Honda R, Yasuda H: Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase. Oncogene. 2000 Mar 9;19(11):1473-6. [PubMed ]
Bres V, Kiernan RE, Linares LK, Chable-Bessia C, Plechakova O, Treand C, Emiliani S, Peloponese JM, Jeang KT, Coux O, Scheffner M, Benkirane M: A non-proteolytic role for ubiquitin in Tat-mediated transactivation of the HIV-1 promoter. Nat Cell Biol. 2003 Aug;5(8):754-61. [PubMed ]
Li M, Brooks CL, Kon N, Gu W: A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol Cell. 2004 Mar 26;13(6):879-86. [PubMed ]
Girnita L, Shenoy SK, Sehat B, Vasilcanu R, Girnita A, Lefkowitz RJ, Larsson O: {beta}-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase. J Biol Chem. 2005 Jul 1;280(26):24412-9. Epub 2005 May 3. [PubMed ]
Chang NS, Doherty J, Ensign A, Schultz L, Hsu LJ, Hong Q: WOX1 is essential for tumor necrosis factor-, UV light-, staurosporine-, and p53-mediated cell death, and its tyrosine 33-phosphorylated form binds and stabilizes serine 46-phosphorylated p53. J Biol Chem. 2005 Dec 30;280(52):43100-8. Epub 2005 Oct 11. [PubMed ]
Sdek P, Ying H, Chang DL, Qiu W, Zheng H, Touitou R, Allday MJ, Xiao ZX: MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein. Mol Cell. 2005 Dec 9;20(5):699-708. [PubMed ]
Brady M, Vlatkovic N, Boyd MT: Regulation of p53 and MDM2 activity by MTBP. Mol Cell Biol. 2005 Jan;25(2):545-53. [PubMed ]
Ding Y, Lee JF, Lu H, Lee MH, Yan DH: Interferon-inducible protein IFIXalpha1 functions as a negative regulator of HDM2. Mol Cell Biol. 2006 Mar;26(5):1979-96. [PubMed ]
Tang J, Qu LK, Zhang J, Wang W, Michaelson JS, Degenhardt YY, El-Deiry WS, Yang X: Critical role for Daxx in regulating Mdm2. Nat Cell Biol. 2006 Aug;8(8):855-62. Epub 2006 Jul 16. [PubMed ]
Kamrul HM, Wadhwa R, Kaul SC: CARF binds to three members (ARF, p53, and HDM2) of the p53 tumor-suppressor pathway. Ann N Y Acad Sci. 2007 Apr;1100:312-5. [PubMed ]
Stevenson LF, Sparks A, Allende-Vega N, Xirodimas DP, Lane DP, Saville MK: The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2. EMBO J. 2007 Feb 21;26(4):976-86. Epub 2007 Feb 8. [PubMed ]
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Song MS, Song SJ, Kim SY, Oh HJ, Lim DS: The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex. EMBO J. 2008 Jul 9;27(13):1863-74. Epub 2008 Jun 19. [PubMed ]
Zweitzig DR, Shcherbik N, Haines DS: Retraction for D. R. Zweitzig, N. Shcherbik, and D. S. Haines: AAA ATPase P97 and adaptor UBXD1 suppress MDM2 ubiquitination and degradation and promote constitutive P53 turnover. Mol Biol Cell. 2008 Nov;19(11):5029. Epub 2008 Sep 3. [PubMed ]
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Enzyme 114 Metabolite References

Not Available

Enzyme 115 [top]

Enzyme 115 ID

8529

Enzyme 115 Name

Phosphopantothenoylcysteine synthetase

Enzyme 115 Synonyms

Not Available

Enzyme 115 Gene Name

PPCS

Enzyme 115 Protein Sequence

>Phosphopantothenoylcysteine synthetase

MFYLAAAVSDFYVPVSEMPEHKIQSSGGPLQITMKMVPKLLSPLVKDWAPKAFIISFKLE
TDPAIVINRARKALEIYQHQVVVANILESRQSFVFIVTKDSETKLLLSEEEIEKGVEIEE
KIVDNLQSRHTAFIGDRN

Enzyme 115 Number of Residues

138

Enzyme 115 Molecular Weight

15645.0

Enzyme 115 Theoretical pI

5.71

Enzyme 115 GO Classification

Not Available

Enzyme 115 General Function

Coenzyme transport and metabolism

Enzyme 115 Specific Function

Not Available

Enzyme 115 Pathways

Not Available

Enzyme 115 Reactions

Not Available

Enzyme 115 Pfam Domain Function

DFP (PF04127 )

Enzyme 115 Signals

None

Enzyme 115 Transmembrane Regions

None

Enzyme 115 Essentiality

Not Available

Enzyme 115 GenBank ID Protein

55665120

Enzyme 115 UniProtKB/Swiss-Prot ID

Q5VVM0

Enzyme 115 UniProtKB/Swiss-Prot Entry Name

Q5VVM0_HUMAN Link Image

Enzyme 115 PDB ID

1P9O

Enzyme 115 PDB File

Show

Enzyme 115 3D Structure

Enzyme 115 Cellular Location

Not Available

Enzyme 115 Gene Sequence

>417 bp

ATGTTTTACCTGGCTGCGGCTGTGTCAGATTTCTATGTTCCTGTCTCTGAAATGCCTGAA
CACAAGATCCAGTCATCTGGGGGCCCACTGCAGATAACAATGAAGATGGTGCCAAAACTG
CTTTCTCCTTTGGTTAAAGATTGGGCTCCCAAAGCATTTATAATTTCCTTTAAGTTGGAG
ACTGACCCCGCCATTGTAATTAATCGAGCTCGGAAGGCTTTGGAAATTTATCAGCATCAA
GTGGTGGTGGCTAATATCCTTGAGTCACGACAGTCCTTTGTGTTTATTGTAACCAAAGAC
TCGGAAACCAAGTTATTGCTATCAGAGGAAGAAATAGAAAAAGGCGTAGAGATAGAAGAG
AAGATAGTGGATAATCTTCAGTCTCGACACACAGCTTTTATAGGTGACAGAAACTGA

Enzyme 115 GenBank Gene ID

AL445669

Enzyme 115 GeneCard ID

PPCS

Enzyme 115 GenAtlas ID

PPCS

Enzyme 115 HGNC ID

HGNC:25686 Link Image

Enzyme 115 Chromosome Location

Enzyme 115 Locus

1p34.2

Enzyme 115 SNPs

SNPJam Report Link Image

Enzyme 115 General References

Not Available

Enzyme 115 Metabolite References

Not Available

Enzyme 116 [top]

Enzyme 116 ID

8587

Enzyme 116 Name

Bile acyl-CoA synthetase

Enzyme 116 Synonyms

BACS
Bile acid-CoA ligase
BA-CoA ligase
BAL
Cholate--CoA ligase
Fatty acid transport protein 5
FATP-5
Fatty-acid-coenzyme A ligase, very long-chain 3
Solute carrier family 27 member 5
Very long-chain acyl-CoA synthetase homolog 2
VLCS-H2
VLCSH2
Very long-chain acyl-CoA synthetase-related protein
VLACS-related
VLACSR

Enzyme 116 Gene Name

SLC27A5

Enzyme 116 Protein Sequence

>Bile acyl-CoA synthetase

MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWV
PHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAF
ERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVL
ASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILP
KLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTG
LPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP
KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQ
QRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDN
QGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMD
REGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQ
LAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVD
PLFVLDNRAQSFRPLTAEMYQAVCEGTWRL

Enzyme 116 Number of Residues

690

Enzyme 116 Molecular Weight

75384.4

Enzyme 116 Theoretical pI

7.70

Enzyme 116 GO Classification

Function
catalytic activity
Process
metabolic process
Component
—

Enzyme 116 General Function

Involved in catalytic activity

Enzyme 116 Specific Function

Acyl-CoA synthetase involved in bile acid metabolism. Proposed to catalyze the first step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi by activating them to their CoA thioesters. Seems to activate secondary bile acids entering the liver from the enterohepatic circulation. In vitro, also activates 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol

Enzyme 116 Pathways

Bile Acid Biosynthesis (map00120 )

Enzyme 116 Reactions

(1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA [RN:R02794]
(2) ATP + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA [RN:R04580]

Enzyme 116 Pfam Domain Function

AMP-binding (PF00501 )

Enzyme 116 Signals

None

Enzyme 116 Transmembrane Regions

31-51 56-76

Enzyme 116 Essentiality

Not Available

Enzyme 116 GenBank ID Protein

4768277

Enzyme 116 UniProtKB/Swiss-Prot ID

Q9Y2P5

Enzyme 116 UniProtKB/Swiss-Prot Entry Name

S27A5_HUMAN Link Image

Enzyme 116 PDB ID

Not Available

Enzyme 116 Cellular Location

Not Available

Enzyme 116 Gene Sequence

>2073 bp

ATGGGTGTCAGGCAACAGTTGGCCTTGCTGCTGCTGCTGCTGCTCCTGCTCTGGGGCCTG
GGGCAGCCAGTGTGGCCAGTCGCTGTGGCCTTGACCCTGCGCTGGCTCCTGGGGGATCCC
ACATGTTGCGTGCTACTTGGGCTGGCCATGTTAGCACGGCCCTGGCTCGGCCCCTGGGTG
CCCCATGGGCTGAGCCTGGCAGCTGCGGCCCTGGCACTAACCCTCCTGCCAGCACGGCTG
CCCCCAGGACTACGCTGGCTGCCGGCTGATGTGATCTTCTTGGCCAAGATCCTCCACCTG
GGCCTGAAGATCAGGGGATGCTTGAGCCGGCAGCCGCCTGACACCTTTGTAGATGCCTTC
GAGCGGCGAGCACGAGCGCAGCCTGGCAGGGCACTCTTGGTGTGGACGGGGCCTGGGGCC
GGCTCAGTCACCTTTGGTGAGCTGGATGCCCGGGCCTGCCAGGCGGCATGGGCCCTGAAG
GCTGAGCTGGGTGACCCTGCGAGCCTGTGTGCCGGGGAGCCTACTGCCCTCCTTGTGCTG
GCTTCCCAGGCCGTTCCAGCCCTGTGTATGTGGCTGGGGCTGGCCAAGCTGGGCTGCCCA
ACAGCCTGGATCAACCCGCATGGCCGGGGGATGCCCCTGGCGCACTCTGTGCTGAGCTCT
GGGGCCCGGGTGCTGGTGGTGGACCCAGACCTCCGGGAGAGCCTGGAGGAGATCCTTCCC
AAGCTGCAGGCTGAGAACATCCGCTGCTTCTACCTCAGCCATACCTCCCCTACACCAGGG
GTGGGGGCTCTGGGGGCTGCCCTGGATGCAGCGCCCTCCCACCCAGTGCCTGCTGACCTG
CGTGCTGGGATCACATGGAGAAGCCCTGCCCTCTTCATCTATACCTCGGGGACCACTGGC
CTCCCGAAGCCAGCCATCCTCACGCATGAGCGGGTACTGCAGATGAGCAAGATGCTGTCC
TTATCTGGGGCCACAGCTGATGATGTGGTTTACACGGTCCTGCCTCTGTACCACGTGATG
GGACTTGTCGTTGGGATCCTCGGCTGCTTAGATCTCGGAGCCACCTGTGTTCTGGCCCCC
AAGTTCTCTACTTCCTGCTTCTGGGATGACTGTCGGCAGCATGGCGTGACAGTGATCCTG
TATGTGGGCGAGCTCCTGCGGTACTTGTGTAACATTCCCCAGCAACCAGAGGACCGGACA
CATACAGTCCGCCTGGCAATGGGCAATGGACTACGGGCTGATGTGTGGGAGACCTTCCAG
CAGCGCTTCGGTCCTATTCGGATCTGGGAAGTCTACGGCTCCACAGAAGGCAACATGGGC
TTAGTCAACTATGTGGGGCGCTGCGGGGCCCTGGGCAAGATGAGCTGCCTCCTCCGAATG
CTGTCCCCCTTTGAGCTGGTGCAGTTCGACATGGAGGCGGCGGAGCCTGTGAGGGACAAT
CAGGGCTTCTGCATCCCTGTAGGGCTAGGGGAGCCGGGGCTGCTGCTGACCAAGGTGGTA
AGCCAGCAACCCTTCGTGGGCTACCGCGGCCCCCGAGAGCTGTCGGAACGGAAGCTGGTG
CGCAACGTGCGGCAATCGGGCGACGTTTACTACAACACCGGGGACGTACTGGCCATGGAC
CGCGAAGGCTTCCTCTACTTCCGCGACCGCCTCGGGGACACCTTCCGATGGAAGGGCGAG
AACGTGTCCACGCACGAGGTGGAGGGCGTGTTGTCGCAGGTGGACTTCTTGCAACAGGTT
AACGTGTATGGCGTGTGCGTGCCAGGTTGTGAGGGTAAGGTGGGCATGGCTGCTGTGCAG
CTAGCCCCCGGCCAGACTTTCGACGGGGAGAAGTTGTACCAGCACGTTCGCGCTTGGCTC
CCTGCCTACGCTACCCCCCATTTCATCCGCATCCAGGACGCCATGGAGGTCACCAGCACG
TTCAAACTGATGAAGACCCGGTTGGTGCGTGAGGGCTTCAATGTGGGGATCGTGGTTGAC
CCTCTGTTTGTACTGGACAACCGGGCCCAGTCCTTCCGGCCCCTGACGGCAGAAATGTAC
CAGGCTGTGTGTGAGGGAACCTGGAGGCTCTGA

Enzyme 116 GenBank Gene ID

AF064255

Enzyme 116 GeneCard ID

SLC27A5

Enzyme 116 GenAtlas ID

SLC27A5

Enzyme 116 HGNC ID

HGNC:10999 Link Image

Enzyme 116 Chromosome Location

Enzyme 116 Locus

19q13.43

Enzyme 116 SNPs

SNPJam Report Link Image

Enzyme 116 General References

Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA: Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein. Mol Genet Metab. 1999 Sep;68(1):32-42. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Steinberg SJ, Mihalik SJ, Kim DG, Cuebas DA, Watkins PA: The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase. J Biol Chem. 2000 May 26;275(21):15605-8. [PubMed ]
Mihalik SJ, Steinberg SJ, Pei Z, Park J, Kim DG, Heinzer AK, Dacremont G, Wanders RJ, Cuebas DA, Smith KD, Watkins PA: Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling. J Biol Chem. 2002 Jul 5;277(27):24771-9. Epub 2002 Apr 29. [PubMed ]

Enzyme 116 Metabolite References

Not Available

Enzyme 117 [top]

Enzyme 117 ID

8749

Enzyme 117 Name

Cytosolic 5'-nucleotidase 3

Enzyme 117 Synonyms

Cytosolic 5'-nucleotidase III
cN-III
Pyrimidine 5'-nucleotidase 1
P5'N-1
P5N-1
PN-I
Uridine 5'-monophosphate hydrolase 1
p36

Enzyme 117 Gene Name

NT5C3

Enzyme 117 Protein Sequence

>Cytosolic 5'-nucleotidase 3

MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSV
RIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDEC
RKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVM
LKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLK
GFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYL
NDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL

Enzyme 117 Number of Residues

336

Enzyme 117 Molecular Weight

37947.8

Enzyme 117 Theoretical pI

7.15

Enzyme 117 GO Classification

Function
5'-nucleotidase activity binding catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding magnesium ion binding metal ion binding nucleotidase activity phosphatase activity phosphoric ester hydrolase activity
Process
—
Component
cell part cytoplasm intracellular part

Enzyme 117 General Function

Involved in magnesium ion binding

Enzyme 117 Specific Function

Can act both as nucleotidase and as phosphotransferase

Enzyme 117 Pathways

Nicotinate and Nicotinamide Metabolism (map00760 )
Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 117 Reactions

a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]

Enzyme 117 Pfam Domain Function

Not Available

Enzyme 117 Signals

None

Enzyme 117 Transmembrane Regions

None

Enzyme 117 Essentiality

Not Available

Enzyme 117 GenBank ID Protein

70608082

Enzyme 117 UniProtKB/Swiss-Prot ID

Q9H0P0

Enzyme 117 UniProtKB/Swiss-Prot Entry Name

5NT3_HUMAN Link Image

Enzyme 117 PDB ID

Not Available

Enzyme 117 Cellular Location

Not Available

Enzyme 117 Gene Sequence

>1011 bp

ATGAGGGCCCCGTCCATGGACCGCGCGGCCGTGGCGAGGGTGGGCGCGGTAGCGAGCGCC
AGCGTGTGCGCCCTGGTGGCGGGGGTGGTGCTGGCTCAGTACATATTCACCTTGAAGAGG
AAGACGGGGCGGAAGACCAAGATCATCGAGATGATGCCAGAATTCCAGAAAAGTTCAGTT
CGAATCAAGAACCCTACAAGAGTAGAAGAAATTATCTGTGGTCTTATCAAAGGAGGAGCT
GCCAAACTTCAGATAATAACGGACTTTGATATGACACTCAGTAGATTTTCATATAAAGGG
AAAAGATGCCCAACATGTCATAATATCATTGACAACTGTAAGCTGGTTACAGATGAATGT
AGAAAAAAGTTATTGCAACTAAAGGAAAAATATTACGCTATTGAAGTTGATCCTGTTCTT
ACTGTAGAAGAGAAGTACCCTTATATGGTGGAATGGTATACTAAATCACATGGTTTGCTT
GTTCAGCAAGCTTTACCAAAAGCTAAACTTAAAGAAATTGTGGCAGAATCTGACGTTATG
CTCAAAGAAGGATATGAGAATTTCTTTGATAAGCTCCAACAACATAGCATCCCCGTGTTC
ATATTTTCGGCTGGAATCGGCGATGTACTAGAGGAAGTTATTCGTCAAGCTGGTGTTTAT
CATCCCAATGTCAAAGTTGTGTCCAATTTTATGGATTTTGATGAAACTGGGGTGCTCAAA
GGATTTAAAGGAGAACTAATTCATGTATTTAACAAACATGATGGTGCCTTGAGGAATACA
GAATATTTCAATCAACTAAAAGACAATAGTAACATAATTCTTCTGGGAGACTCCCAAGGA
GACTTAAGAATGGCAGATGGAGTGGCCAATGTTGAGCACATTCTGAAAATTGGATATCTA
AATGATAGAGTGGATGAGCTTTTAGAAAAGTACATGGACTCTTATGATATTGTTTTAGTA
CAAGATGAATCATTAGAAGTAGCCAACTCTATTTTACAGAAGATTCTATAA

Enzyme 117 GenBank Gene ID

NM_001002010.1 Link Image

Enzyme 117 GeneCard ID

NT5C3

Enzyme 117 GenAtlas ID

NT5C3

Enzyme 117 HGNC ID

HGNC:17820 Link Image

Enzyme 117 Chromosome Location

Enzyme 117 Locus

7p14.3

Enzyme 117 SNPs

SNPJam Report Link Image

Enzyme 117 General References

Amici A, Emanuelli M, Raffaelli N, Ruggieri S, Saccucci F, Magni G: Human erythrocyte pyrimidine 5-nucleotidase, PN-I, is identical to p36, a protein associated to lupus inclusion formation in response to alpha-interferon. Blood. 2000 Aug 15;96(4):1596-8. [PubMed ]
Marinaki AM, Escuredo E, Duley JA, Simmonds HA, Amici A, Naponelli V, Magni G, Seip M, Ben-Bassat I, Harley EH, Thein SL, Rees DC: Genetic basis of hemolytic anemia caused by pyrimidine 5' nucleotidase deficiency. Blood. 2001 Jun 1;97(11):3327-32. [PubMed ]
Kanno H, Takizawa T, Miwa S, Fujii H: Molecular basis of Japanese variants of pyrimidine 5'-nucleotidase deficiency. Br J Haematol. 2004 Jul;126(2):265-71. [PubMed ]
Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]
Rich SA, Bose M, Tempst P, Rudofsky UH: Purification, microsequencing, and immunolocalization of p36, a new interferon-alpha-induced protein that is associated with human lupus inclusions. J Biol Chem. 1996 Jan 12;271(2):1118-26. [PubMed ]
Amici A, Ciccioli K, Naponelli V, Raffaelli N, Magni G: Evidence for essential catalytic determinants for human erythrocyte pyrimidine 5'-nucleotidase. Cell Mol Life Sci. 2005 Jul;62(14):1613-20. [PubMed ]
Wallden K, Stenmark P, Nyman T, Flodin S, Graslund S, Loppnau P, Bianchi V, Nordlund P: Crystal structure of human cytosolic 5'-nucleotidase II: insights into allosteric regulation and substrate recognition. J Biol Chem. 2007 Jun 15;282(24):17828-36. Epub 2007 Apr 3. [PubMed ]
Bianchi P, Fermo E, Alfinito F, Vercellati C, Baserga M, Ferraro F, Guzzo I, Rotoli B, Zanella A: Molecular characterization of six unrelated Italian patients affected by pyrimidine 5'-nucleotidase deficiency. Br J Haematol. 2003 Sep;122(5):847-51. [PubMed ]

Enzyme 117 Metabolite References

Not Available

Enzyme 118 [top]

Enzyme 118 ID

8813

Enzyme 118 Name

Glutamine-dependent NAD(+) synthetase

Enzyme 118 Synonyms

NAD(+) synthase [glutamine-hydrolyzing]
NAD(+) synthetase

Enzyme 118 Gene Name

NADSYN1

Enzyme 118 Protein Sequence

>Glutamine-dependent NAD(+) synthetase

MGRKVTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYES
DTLLHSFQVLAALVESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANE
GNYRELRWFTPWSRSRHTEEYFLPRMIQDLTKQETVPFGDAVLVTWDTCIGSEICEELWT
PHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIYLLANQKGCDGDRL
YYDGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPR
VKVDFALSCHEDLLAPISEPIEWKYHSPEEEISLGPACWLWDFLRRSQQAGFLLPLSGGV
DSAATACLIYSMCCQVCEAVRSGNEEVLADVRTIVNQISYTPQDPRDLCGRILTTCYMAS
KNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPLFAAHGGSSRENLA
LQNVQARIRMVLAYLFAQLSLWSRGVHGGLLVLGSANVDESLLGYLTKYDCSSADINPIG
GISKTDLRAFVQFCIQRFQLPALQSILLAPATAELEPLADGQVSQTDEEDMGMTYAELSV
YGKLRKVAKMGPYSMFCKLLGMWRHICTPRQVADKVKRFFSKYSMNRHKMTTLTPAYHAE
NYSPEDNRFDLRPFLYNTSWPWQFRCIENQVLQLERAEPQSLDGVD

Enzyme 118 Number of Residues

706

Enzyme 118 Molecular Weight

79283.9

Enzyme 118 Theoretical pI

6.40

Enzyme 118 GO Classification

Function
ATP binding NAD+ synthase (glutamine-hydrolyzing) activity NAD+ synthase (glutamine-hydrolyzing) activity adenyl nucleotide binding adenyl ribonucleotide binding binding carbon-nitrogen ligase activity, with glutamine as amido-N-donor catalytic activity hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds ligase activity ligase activity, forming carbon-nitrogen bonds nucleoside binding purine nucleoside binding
Process
NAD biosynthetic process cellular metabolic process coenzyme biosynthetic process coenzyme metabolic process cofactor metabolic process metabolic process nicotinamide nucleotide biosynthetic process nitrogen compound metabolic process pyridine nucleotide biosynthetic process
Component
—

Enzyme 118 General Function

Involved in NAD+ synthase (glutamine-hydrolyzing) activity

Enzyme 118 Specific Function

ATP + deamido-NAD(+) + L-glutamine + H(2)O = AMP + diphosphate + NAD(+) + L-glutamate

Enzyme 118 Pathways

Glutamate Metabolism (map00251 )
Nicotinate and Nicotinamide Metabolism (map00760 )

Enzyme 118 Reactions

ATP + deamido-NAD+ + L-glutamine + H2O = AMP + diphosphate + NAD+ + L-glutamate [RN:R00257]

Enzyme 118 Pfam Domain Function

CN_hydrolase (PF00795 )
NAD_synthase (PF02540 )

Enzyme 118 Signals

None

Enzyme 118 Transmembrane Regions

None

Enzyme 118 Essentiality

Not Available

Enzyme 118 GenBank ID Protein

28849201

Enzyme 118 UniProtKB/Swiss-Prot ID

Q6IA69

Enzyme 118 UniProtKB/Swiss-Prot Entry Name

NADE_HUMAN Link Image

Enzyme 118 PDB ID

Not Available

Enzyme 118 Cellular Location

Not Available

Enzyme 118 Gene Sequence

>2121 bp

ATGGGCCGGAAGGTGACCGTGGCCACCTGCGCACTCAACCAGTGGGCCCTGGACTTCGAG
GGCAATTTGCAAAGAATTTTAAAGAGTATTGAAATTGCCAAAAACAGAGGAGCAAGATAC
AGGCTTGGACCAGAGCTGGAAATATGCGGCTACGGATGTTGGGATCATTATTACGAGTCG
GACACCCTCTTGCACTCGTTTCAAGTCCTAGCGGCCCTTGTGGAGTCTCCCGTCACTCAG
GACATCATCTGCGACGTGGGGATGCCTGTAATGCACCGAAACGTCCGCTACAACTGCAGA
GTGGTATTCCTCAACAGGAAGATCCTGCTCATCAGACCCAAGATGGCCTTGGCCAATGAA
GGCAACTACCGCGAGCTGCGCTGGTTCACCCCGTGGTCGAGGAGTCGGCACACAGAGGAG
TACTTTCTGCCTCGGATGATACAGGACCTGACAAAGCAGGAAACCGTACCCTTCGGAGAT
GCGGTGCTGGTGACATGGGACACCTGCATTGGAAGTGAGATCTGTGAGGAGCTCTGGACA
CCCCACAGCCCGCACATCGACATGGGCCTGGATGGCGTGGAGATCATCACCAACGCCTCG
GGCAGCCACCACGTGCTGCGCAAAGCCAACACCAGGGTGGATCTCGTGACTATGGTCACC
AGCAAGAACGGTGGGATTTACTTGCTGGCCAACCAGAAGGGTTGCGACGGGGACCGCCTG
TACTACGACGGCTGTGCCATGATCGCCATGAACGGAAGCGTCTTTGCTCAAGGATCCCAG
TTTTCTCTGGATGACGTGGAAGTCCTGACGGCCACGCTGGATCTGGAGGACGTCCGGAGC
TACAGGGCGGAGATTTCATCTCGAAACCTGGCGGCCAGCAGGGCGAGCCCCTACCCCAGA
GTGAAGGTGGACTTTGCCCTCTCGTGCCACGAGGACTTGCTGGCACCCATCTCTGAGCCC
ATCGAGTGGAAATACCACAGCCCTGAGGAGGAGATAAGCCTTGGACCTGCCTGCTGGCTC
TGGGATTTTTTAAGACGAAGTCAACAGGCAGGGTTTTTGCTGCCCTTGAGTGGCGGGGTG
GACAGCGCAGCCACCGCCTGCCTCATCTACTCCATGTGCTGCCAGGTCTGCGAGGCCGTG
AGGAGTGGAAATGAGGAAGTGCTGGCTGATGTCCGCACCATCGTGAACCAGATCAGCTAC
ACCCCCCAGGATCCCCGAGACCTCTGTGGACGCATACTGACCACCTGCTACATGGCCAGC
AAGAACTCCTCCCAGGAGACGTGCACCCGGGCCAGAGAGTTGGCCCAGCAGATTGGAAGC
CACCACATCAGTCTCAACATCGATCCAGCCGTGAAGGCCGTCATGGGCATCTTCAGCCTG
GTGACGGGGAAGAGCCCTCTGTTTGCAGCTCATGGAGGAAGCAGCAGGGAAAACCTGGCG
CTGCAAAATGTGCAGGCTCGAATACGGATGGTCCTCGCCTATCTGTTTGCTCAGTTGAGC
CTCTGGTCTCGGGGTGTCCACGGTGGGCTCCTCGTGCTGGGATCCGCCAACGTGGATGAG
AGTCTCCTGGGCTACCTGACCAAGTACGACTGCTCCAGTGCGGACATCAACCCCATAGGC
GGGATCAGCAAGACGGACCTCAGGGCCTTCGTCCAGTTCTGCATCCAGCGCTTCCAGCTT
CCTGCCCTGCAGAGCATCCTGTTGGCGCCGGCCACCGCAGAGCTGGAGCCCTTGGCTGAT
GGACAGGTGTCCCAGACCGACGAGGAAGATATGGGGATGACATATGCGGAGCTCTCGGTC
TATGGGAAACTCAGGAAGGTGGCCAAGATGGGGCCCTACAGCATGTTCTGCAAACTCCTC
GGCATGCGGAGACACATCTGCACCCCGAGACAGGTCGCTGACAAAGTGAAGCGGTTTTTC
TCCAAGTACTCCATGAACAGACACAAGATGACCACGCTCACACCCGCGTACCACGCCGAG
AACTACAGCCCTGAGGACAACAGGTTTGATCTGCGACCATTTCTGTACAACACAAGCTGG
CCTTGGCAGTTTCGGTGCATAGAAAATCAGGTGCTACAGCTCGAGAGGGCAGAGCCACAG
TCCCTGGACGGCGTGGACTGA

Enzyme 118 GenBank Gene ID

AB091316

Enzyme 118 GeneCard ID

NADSYN1

Enzyme 118 GenAtlas ID

NADSYN1

Enzyme 118 HGNC ID

HGNC:29832 Link Image

Enzyme 118 Chromosome Location

Enzyme 118 Locus

11q13.4

Enzyme 118 SNPs

SNPJam Report Link Image

Enzyme 118 General References

Hara N, Yamada K, Terashima M, Osago H, Shimoyama M, Tsuchiya M: Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency. J Biol Chem. 2003 Mar 28;278(13):10914-21. Epub 2003 Jan 23. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 118 Metabolite References

Not Available

Enzyme 119 [top]

Enzyme 119 ID

9698

Enzyme 119 Name

Acetoacetyl-CoA synthetase

Enzyme 119 Synonyms

Acyl-CoA synthetase family member 1
Protein sur-5 homolog

Enzyme 119 Gene Name

AACS

Enzyme 119 Protein Sequence

>Acetoacetyl-CoA synthetase

MSKEERPGREEILECQVMWEPDSKKNTQMDRFRAAVGAACGLALESYDDLYHWSVESYSD
FWAEFWKFSGIVFSRVYDEVVDTSKGIADVPEWFKGSRLNYAENLLRHKENDRVALYIAR
EGKEEIVKVTFEELRQEVALFAAAMRKMGVKKGDRVVGYLPNSEHAVEAMLAAASIGAIW
SSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVYNGKEHNHMEKLQQVVKGLPDLKKVVVIP
YVSSRENIDLSKIPNSVFLDDFLATGTSEQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCM
VHSAGGTLIQHLKEHLLHGNMTSSDILLCYTTVGWMMWNWMVSLLATGAAMVLYDGSPLV
PTPNVLWDLVDRIGITVLVTGAKWLSVLEEKAMKPVETHSLQMLHTILSTGSPLKAQSYE
YVYRCIKSSILLGSISGGTDIISCFMGHNFSLPVYKGEIQARNLGMAVEAWNEEGKAVWG
ESGELVCTKPIPCQPTHFWNDENGNKYRKAYFSKFPGIWAHGDYCRINPKTGGIVMLGRS
DGTLNPNGVRFGSSEIYNIVESFEEVEDSLCVPQYNKYREERVILFLKMASGHAFQPDLV
KRIRDAIRMGLSARHVPSLILETKGIPYTLNGKKVEVAVKQIIAGKAVEQGGAFSNPETL
DLYRDIPELQGF

Enzyme 119 Number of Residues

672

Enzyme 119 Molecular Weight

75143.6

Enzyme 119 Theoretical pI

6.18

Enzyme 119 GO Classification

Function
acetoacetate-CoA ligase activity acid-thiol ligase activity catalytic activity ligase activity ligase activity, forming carbon-sulfur bonds
Process
lipid metabolic process metabolic process primary metabolic process
Component
—

Enzyme 119 General Function

Involved in acetoacetate-CoA ligase activity

Enzyme 119 Specific Function

Activates acetoacetate to acetoacetyl-CoA. May be involved in utilizing ketone body for the fatty acid-synthesis during adipose tissue development

Enzyme 119 Pathways

Butyrate Metabolism (map00650 )

Enzyme 119 Reactions

ATP + acetoacetate + CoA = AMP + diphosphate + acetoacetyl-CoA [RN:R01357]

Enzyme 119 Pfam Domain Function

AMP-binding (PF00501 )

Enzyme 119 Signals

None

Enzyme 119 Transmembrane Regions

None

Enzyme 119 Essentiality

Not Available

Enzyme 119 GenBank ID Protein

48290356

Enzyme 119 UniProtKB/Swiss-Prot ID

Q86V21

Enzyme 119 UniProtKB/Swiss-Prot Entry Name

AACS_HUMAN Link Image

Enzyme 119 PDB ID

Not Available

Enzyme 119 Cellular Location

Not Available

Enzyme 119 Gene Sequence

>2019 bp

ATGTCCAAGGAGGAGCGCCCCGGTCGGGAGGAGATCCTGGAGTGCCAGGTGATGTGGGAG
CCTGACAGTAAGAAGAACACGCAGATGGACCGCTTCCGGGCGGCTGTGGGCGCCGCCTGC
GGCCTGGCGCTGGAGAGTTATGATGACTTGTACCATTGGTCCGTTGAGTCATATTCAGAC
TTCTGGGCAGAGTTCTGGAAATTCAGTGGAATTGTCTTCTCACGTGTGTATGATGAGGTT
GTGGACACATCGAAAGGAATCGCAGATGTCCCCGAGTGGTTCAAAGGCAGTCGGCTCAAC
TATGCAGAAAACCTCCTGCGGCACAAAGAGAATGACAGAGTTGCCCTTTACATTGCAAGG
GAAGGCAAAGAGGAAATTGTGAAGGTGACTTTTGAAGAGCTGAGGCAAGAAGTGGCTTTG
TTTGCAGCAGCAATGAGGAAAATGGGTGTGAAGAAAGGAGATCGGGTTGTTGGTTATTTA
CCCAACAGTGAGCACGCTGTCGAGGCGATGCTGGCTGCGGCAAGCATTGGTGCCATCTGG
AGCTCCACGTCCCCGGACTTCGGTGTGAATGGTGTGCTGGACCGGTTTTCTCAAATTCAG
CCAAAGCTCATCTTCTCTGTGGAGGCTGTTGTCTATAATGGCAAAGAGCACAACCACATG
GAAAAGCTGCAGCAGGTGGTTAAAGGCCTACCAGACTTGAAGAAAGTGGTGGTGATTCCT
TATGTGTCCTCCAGAGAGAACATAGACCTTTCAAAGATTCCAAACAGTGTGTTTCTGGAT
GACTTTCTTGCCACCGGCACCAGTGAGCAGGCCCCGCAGCTGGAGTTCGAGCAGCTGCCC
TTCAGCCACCCACTGTTCATCATGTTCTCATCGGGCACCACGGGCGCACCCAAGTGCATG
GTGCATTCCGCTGGGGGCACCCTCATCCAGCATCTGAAGGAGCACCTGCTGCACGGCAAC
ATGACCAGCAGTGACATCCTCCTGTGCTACACCACGGTCGGCTGGATGATGTGGAACTGG
ATGGTGTCCCTTCTGGCCACAGGAGCGGCCATGGTCTTGTACGATGGCTCCCCCCTGGTG
CCCACGCCCAATGTGCTCTGGGACCTGGTTGACAGGATAGGCATCACTGTCCTGGTAACT
GGGGCCAAGTGGCTGTCAGTGCTGGAAGAGAAGGCCATGAAGCCGGTGGAAACCCACAGT
CTCCAGATGCTCCACACGATCCTGTCCACTGGCTCCCCACTGAAAGCCCAGAGCTACGAG
TATGTCTACAGGTGCATCAAGAGCAGCATCCTCCTGGGCTCCATCTCAGGAGGCACCGAC
ATCATCTCCTGCTTCATGGGCCACAATTTTTCTCTTCCTGTGTATAAAGGGGAGATTCAG
GCCCGGAACCTGGGCATGGCCGTGGAAGCGTGGAACGAGGAAGGAAAGGCGGTCTGGGGA
GAGAGCGGCGAGCTGGTGTGTACTAAGCCGATCCCTTGCCAGCCCACACACTTCTGGAAC
GATGAGAACGGCAACAAGTACAGGAAGGCGTATTTCTCCAAATTCCCAGGTATCTGGGCT
CATGGCGACTACTGCAGAATCAACCCCAAGACCGGGGGCATCGTCATGCTTGGCCGGAGT
GACGGCACCCTCAACCCCAACGGGGTGCGGTTCGGCAGCTCGGAAATCTATAACATTGTG
GAATCCTTCGAGGAGGTGGAGGACAGCCTGTGTGTCCCCCAGTATAACAAGTACAGGGAG
GAGAGGGTGATCCTCTTCCTGAAGATGGCCTCCGGGCACGCCTTCCAGCCTGACTTGGTT
AAGAGGATCCGTGACGCCATCCGCATGGGCTTGTCTGCGCGACACGTGCCCAGCCTCATC
CTGGAAACCAAGGGCATCCCGTATACGCTCAACGGCAAGAAAGTGGAAGTTGCCGTCAAA
CAGATCATCGCTGGAAAAGCCGTGGAGCAAGGAGGTGCTTTCTCGAACCCCGAGACCCTG
GATCTGTACCGGGACATCCCTGAGCTGCAGGGCTTCTGA

Enzyme 119 GenBank Gene ID

AB054121

Enzyme 119 GeneCard ID

AACS

Enzyme 119 GenAtlas ID

AACS

Enzyme 119 HGNC ID

HGNC:21298 Link Image

Enzyme 119 Chromosome Location

Enzyme 119 Locus

12q24.31

Enzyme 119 SNPs

SNPJam Report Link Image

Enzyme 119 General References

Ohgami M, Takahashi N, Yamasaki M, Fukui T: Expression of acetoacetyl-CoA synthetase, a novel cytosolic ketone body-utilizing enzyme, in human brain. Biochem Pharmacol. 2003 Mar 15;65(6):989-94. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Gu T, Orita S, Han M: Caenorhabditis elegans SUR-5, a novel but conserved protein, negatively regulates LET-60 Ras activity during vulval induction. Mol Cell Biol. 1998 Aug;18(8):4556-64. [PubMed ]
Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
Watkins PA, Maiguel D, Jia Z, Pevsner J: Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. J Lipid Res. 2007 Dec;48(12):2736-50. Epub 2007 Aug 30. [PubMed ]

Enzyme 119 Metabolite References

Not Available

Enzyme 120 [top]

Enzyme 120 ID

9777

Enzyme 120 Name

Acyl-coenzyme A synthetase ACSM1, mitochondrial

Enzyme 120 Synonyms

Acyl-CoA synthetase medium-chain family member 1
Butyrate--CoA ligase 1
Butyryl-coenzyme A synthetase 1
Lipoate-activating enzyme
Middle-chain acyl-CoA synthetase 1

Enzyme 120 Gene Name

ACSM1

Enzyme 120 Protein Sequence

>Acyl-coenzyme A synthetase ACSM1, mitochondrial

MQWLMRFRTLWGIHKSFHNIHPAPSQLRCRSLSEFGAPRWNDYEVPEEFNFASYVLDYWA
QKEKEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPR
VPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCP
SLKTKLLVSDHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSH
GLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTK
VIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTG
LLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRI
KPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG
PAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSV
TAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM

Enzyme 120 Number of Residues

577

Enzyme 120 Molecular Weight

65272.7

Enzyme 120 Theoretical pI

8.40

Enzyme 120 GO Classification

Function
catalytic activity
Process
metabolic process
Component
—

Enzyme 120 General Function

Involved in catalytic activity

Enzyme 120 Specific Function

Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro). Functions as GTP-dependent lipoate- activating enzyme that generates the substrate for lipoyltransferase

Enzyme 120 Pathways

Butyrate Metabolism (map00650 )

Enzyme 120 Reactions

ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]

Enzyme 120 Pfam Domain Function

AMP-binding (PF00501 )

Enzyme 120 Signals

None

Enzyme 120 Transmembrane Regions

None

Enzyme 120 Essentiality

Not Available

Enzyme 120 GenBank ID Protein

15487302

Enzyme 120 UniProtKB/Swiss-Prot ID

Q08AH1

Enzyme 120 UniProtKB/Swiss-Prot Entry Name

ACSM1_HUMAN Link Image

Enzyme 120 PDB ID

Not Available

Enzyme 120 Cellular Location

Not Available

Enzyme 120 Gene Sequence

>1734 bp

ATGCAGTGGCTAATGAGGTTCCGGACCCTCTGGGGCATCCACAAATCCTTCCACAACATC
CACCCTGCCCCTTCACAGCTGCGCTGCCGGTCTTTATCAGAATTTGGAGCCCCAAGATGG
AATGACTATGAAGTACCGGAGGAATTTAACTTTGCAAGTTATGTACTGGACTACTGGGCT
CAAAAGGAGAAGGAGGGCAAGAGAGGTCCAAATCCAGCTTTTTGGTGGGTGAATGGCCAA
GGGGATGAAGTAAAGTGGAGCTTCAGAGAGATGGGAGACCTAACCCGCCGTGTAGCCAAC
GTCTTCACACAGACCTGTGGCCTACAACAGGGAGACCATCTGGCCTTGATGCTGCCTCGA
GTTCCTGAGTGGTGGCTGGTGGCTGTGGGCTGCATGCGAACAGGGATCATCTTCATTCCT
GCGACCATCCTGTTGAAGGCCAAAGACATTCTCTATCGACTACAGTTGTCTAAAGCCAAG
GGCATTGTGACCATAGATGCCCTTGCCTCAGAGGTGGACTCCATAGCTTCTCAGTGCCCC
TCTCTGAAAACCAAGCTCCTGGTGTCTGATCACAGCCGTGAAGGGTGGCTGGACTTCCGA
TCGCTGGTTAAATCAGCATCCCCAGAACACACCTGTGTTAAGTCAAAGACCTTGGACCCA
ATGGTCATCTTCTTCACCAGTGGGACCACAGGCTTCCCCAAGATGGCAAAACACTCCCAT
GGGTTGGCCTTACAACCCTCCTTCCCAGGAAGTAGGAAATTACGGAGCCTGAAGACATCT
GATGTCTCCTGGTGCCTGTCGGACTCAGGATGGATTGTGGCTACCATTTGGACCCTGGTA
GAACCATGGACAGCGGGTTGTACAGTCTTTATCCACCATCTGCCACAGTTTGACACCAAG
GTCATCATACAGACATTGTTGAAATACCCCATTAACCACTTTTGGGGGGTATCATCTATA
TATCGAATGATTCTGCAGCAGGATTTCACCAGCATCAGGTTCCCTGCCCTGGAGCACTGC
TATACTGGCGGGGAGGTCGTGTTGCCCAAGGATCAGGAGGAGTGGAAAAGACGGACGGGC
CTTCTGCTCTACGAGAACTATGGGCAGTCGGAAACGGGACTAATTTGTGCCACCTACTGG
GGAATGAAGATCAAGCCGGGTTTCATGGGGAAGGCCACTCCACCCTATGACGTCCAGGTC
ATTGATGACAAGGGCAGCATCCTGCCACCTAACACAGAAGGAAACATTGGCATCAGAATC
AAACCTGTCAGGCCTGTGAGCCTCTTCATGTGCTATGAGGGTGACCCAGAGAAGACAGCT
AAAGTGGAATGTGGGGACTTCTACAACACTGGGGACAGAGGAAAGATGGATGAAGAGGGC
TACATTTGTTTCCTGGGGAGGAGTGATGACATCATTAATGCCTCTGGGTATCGCATCGGG
CCTGCAGAGGTTGAAAGCGCTTTGGTGGAGCACCCAGCGGTGGCGGAGTCAGCCGTGGTG
GGCAGCCCAGACCCGATTCGAGGGGAGGTGGTGAAGGCCTTTATTGTCCTGACCCCACAG
TTCCTGTCCCATGACAAGGATCAGCTGACCAAGGAACTGCAGCAGCATGTCAAGTCAGTG
ACAGCCCCATACAAGTACCCAAGGAACGTGGAGTTTGTCTCAGAGCTGCCAAAAACCATC
ACTGGCAAGATTGAACGGAAGGAACTTCGGAAAAAGGAGACTGGTCAGATGTAA

Enzyme 120 GenBank Gene ID

AB059429

Enzyme 120 GeneCard ID

ACSM1

Enzyme 120 GenAtlas ID

ACSM1

Enzyme 120 HGNC ID

HGNC:18049 Link Image

Enzyme 120 Chromosome Location

Enzyme 120 Locus

16p12.3

Enzyme 120 SNPs

SNPJam Report Link Image

Enzyme 120 General References

Fujino T, Takei YA, Sone H, Ioka RX, Kamataki A, Magoori K, Takahashi S, Sakai J, Yamamoto TT: Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product. J Biol Chem. 2001 Sep 21;276(38):35961-6. Epub 2001 Jul 24. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 120 Metabolite References

Not Available

Enzyme 121 [top]

Enzyme 121 ID

9969

Enzyme 121 Name

Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A

Enzyme 121 Synonyms

cAMP and cGMP phosphodiesterase 11A

Enzyme 121 Gene Name

PDE11A

Enzyme 121 Protein Sequence

>Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A

MAASRLDFGEVETFLDRHPELFEDYLMRKGKQEMVEKWLQRHSQGQGALGPRPSLAGTSS
LAHSTCRGGSSVGGGTGPNGSAHSQPLPGGGDCGGVPLSPSWAGGSRGDGNLQRRASQKE
LRKSFARSKAIHVNRTYDEQVTSRAQEPLSSVRRRALLRKASSLPPTTAHILSALLESRV
NLPRYPPTAIDYKCHLKKHNERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSL
FLVEGAAAGKKTLVSKFFDVHAGTPLLPCSSTENSNEVQVPWGKGIIGYVGEHGETVNIP
DAYQDRRFNDEIDKLTGYKTKSLLCMPIRSSDGEIIGVAQAINKIPEGAPFTEDDEKVMQ
MYLPFCGIAISNAQLFAASRKEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKC
ERCSVLLLEDIESPVVKFTKSFELMSPKCSADAENSFKESMEKSSYSDWLINNSIAELVA
STGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNSNHQIIGVAQVLNRLDGKPFD
DADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQSVALDVLSYHATCSKAEVDKFKAANI
PLVSELAIDDIHFDDFSLDVDAMITAALRMFMELGMVQKFKIDYETLCRWLLTVRKNYRM
VLYHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSG
SALAQLYGTSATLEHHHFNHAVMILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLY
FERRTEFFELVSKGEYDWNIKNHRDIFRSMLMTACDLGAVTKPWEISRQVAELVTSEFFE
QGDRERLELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNVKLKPMLDSVAT
NRSKWEELHQKRLLASTASSSPASVMVAKEDRN

Enzyme 121 Number of Residues

933

Enzyme 121 Molecular Weight

104750.6

Enzyme 121 Theoretical pI

6.57

Enzyme 121 GO Classification

Function
3',5'-cyclic-nucleotide phosphodiesterase activity catalytic activity cyclic-nucleotide phosphodiesterase activity hydrolase activity hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity phosphoric ester hydrolase activity
Process
biological regulation regulation of biological process regulation of cellular process signal transduction
Component
—

Enzyme 121 General Function

Involved in catalytic activity

Enzyme 121 Specific Function

Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'- GMP, respectively

Enzyme 121 Pathways

Progesterone-mediated oocyte maturation (map04914 )
Purine Metabolism (map00230 )

Enzyme 121 Reactions

guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]

Enzyme 121 Pfam Domain Function

GAF (PF01590 )
PDEase_I (PF00233 )

Enzyme 121 Signals

None

Enzyme 121 Transmembrane Regions

None

Enzyme 121 Essentiality

Not Available

Enzyme 121 GenBank ID Protein

116536085

Enzyme 121 UniProtKB/Swiss-Prot ID

Q9HCR9

Enzyme 121 UniProtKB/Swiss-Prot Entry Name

PDE11_HUMAN Link Image

Enzyme 121 PDB ID

Not Available

Enzyme 121 Cellular Location

Not Available

Enzyme 121 Gene Sequence

>2802 bp

ATGGCAGCCTCCCGCCTGGACTTTGGGGAGGTGGAAACTTTCCTGGACAGGCACCCAGAG
TTGTTTGAAGATTACTTGATGCGGAAGGGGAAGCAGGAGATGGTTGAAAAGTGGCTGCAG
AGGCACAGTCAGGGTCAGGGGGCTTTAGGTCCAAGGCCCTCTTTGGCTGGTACCAGCAGC
TTGGCTCACAGCACCTGCAGAGGTGGCAGCAGCGTTGGTGGTGGCACTGGACCAAATGGC
TCTGCCCACAGCCAGCCCCTTCCCGGTGGCGGGGACTGTGGTGGGGTTCCCTTGAGTCCC
AGCTGGGCCGGTGGCAGCAGGGGCGATGGGAACCTGCAGCGGAGAGCTTCTCAGAAAGAG
CTAAGGAAGAGTTTTGCCCGCTCCAAGGCCATCCACGTGAACAGGACCTACGATGAACAG
GTGACCTCCCGGGCTCAGGAACCCCTGAGTAGTGTACGACGGAGGGCACTTCTCCGGAAG
GCAAGCTCCCTGCCCCCCACCACAGCCCATATTCTCAGTGCGCTGCTGGAATCGAGAGTG
AATCTGCCTCGGTATCCCCCTACAGCCATCGACTACAAGTGCCATCTGAAAAAGCATAAT
GAGCGTCAGTTCTTTCTGGAATTGGTCAAAGATATCTCCAATGACCTTGACCTCACCAGC
CTGAGCTACAAGATTCTCATCTTTGTCTGCCTTATGGTGGATGCTGACCGCTGCTCTCTT
TTCCTGGTGGAAGGGGCAGCTGCTGGCAAGAAGACCTTGGTCTCCAAATTCTTTGATGTG
CATGCAGGAACACCTCTGCTGCCTTGCAGCAGCACAGAGAACTCAAATGAGGTGCAGGTC
CCCTGGGGCAAAGGTATCATTGGCTATGTCGGGGAGCATGGAGAAACGGTCAACATTCCT
GATGCCTACCAGGATCGACGATTCAATGATGAAATCGACAAGCTAACTGGATACAAGACA
AAATCATTATTGTGCATGCCTATCCGAAGCAGTGATGGTGAGATTATTGGTGTGGCCCAA
GCGATAAATAAGATTCCTGAAGGAGCTCCATTTACTGAAGATGATGAAAAAGTTATGCAG
ATGTATCTTCCATTTTGTGGAATCGCCATATCTAACGCTCAGCTCTTTGCTGCCTCAAGG
AAAGAATATGAAAGAAGCAGAGCTTTGCTAGAGGTGGTTAATGACCTCTTTGAAGAACAG
ACTGACCTGGAGAAAATTGTCAAGAAAATAATGCATCGGGCCCAAACTCTGCTGAAATGT
GAACGCTGTTCTGTTTTACTCCTAGAGGACATCGAATCACCAGTGGTGAAATTTACCAAA
TCCTTTGAATTGATGTCCCCAAAGTGCAGTGCTGATGCTGAGAACAGTTTCAAAGAAAGC
ATGGAGAAATCATCATACTCCGACTGGCTAATAAATAACAGCATTGCTGAGCTGGTTGCT
TCAACAGGCCTTCCAGTGAACATCAGTGATGCCTACCAGGATCCGCGCTTTGATGCAGAG
GCAGACCAGATATCTGGTTTTCACATAAGATCTGTTCTTTGTGTCCCTATTTGGAATAGC
AACCACCAAATAATTGGAGTGGCTCAAGTGTTAAACAGACTTGATGGGAAACCTTTTGAT
GATGCAGATCAACGACTTTTTGAGGCTTTTGTCATCTTTTGTGGACTTGGCATCAACAAC
ACAATTATGTATGATCAAGTGAAGAAGTCCTGGGCCAAGCAGTCTGTGGCTCTTGATGTG
CTATCATACCATGCAACATGTTCAAAAGCTGAAGTTGACAAGTTTAAGGCAGCCAACATC
CCTCTGGTGTCAGAACTTGCCATCGATGACATTCATTTTGATGACTTTTCTCTCGACGTT
GATGCCATGATCACAGCTGCTCTCCGGATGTTCATGGAGCTGGGGATGGTACAGAAATTT
AAAATTGACTATGAGACACTGTGTAGGTGGCTTTTGACAGTGAGGAAAAACTATCGGATG
GTTCTATACCACAACTGGAGACATGCCTTCAACGTGTGTCAGCTGATGTTCGCGATGTTA
ACCACTGCTGGGTTTCAAGACATTCTGACCGAGGTGGAAATTTTAGCGGTGATTGTGGGA
TGCCTGTGTCATGACCTCGACCACAGGGGAACCAACAATGCCTTCCAAGCTAAGAGTGGC
TCTGCCCTGGCCCAACTCTATGGAACCTCTGCTACCTTGGAGCATCACCATTTCAACCAC
GCCGTGATGATCCTTCAAAGTGAGGGTCACAATATCTTTGCTAACCTGTCCTCCAAGGAA
TATAGTGACCTTATGCAGCTTTTGAAGCAGTCAATATTGGCAACAGACCTCACGCTGTAC
TTTGAGAGGAGAACTGAATTCTTTGAACTTGTCAGTAAAGGAGAATACGATTGGAACATC
AAAAACCATCGTGATATATTTCGATCAATGTTAATGACAGCCTGTGACCTTGGAGCCGTG
ACCAAACCGTGGGAGATCTCCAGACAGGTGGCAGAACTTGTAACCAGTGAGTTCTTCGAA
CAAGGAGATCGGGAGAGATTAGAGCTCAAACTCACTCCTTCAGCAATTTTTGATCGGAAC
CGGAAGGATGAACTGCCTCGGTTGCAACTGGAGTGGATTGATAGCATCTGCATGCCTTTG
TATCAGGCACTGGTGAAGGTCAACGTGAAACTGAAGCCGATGCTAGATTCAGTAGCTACA
AACAGAAGTAAGTGGGAAGAGCTACACCAAAAACGACTGCTGGCCTCAACTGCCTCATCC
TCCCCTGCCAGTGTTATGGTAGCCAAGGAAGACAGGAACTAA

Enzyme 121 GenBank Gene ID

NM_016953.3 Link Image

Enzyme 121 GeneCard ID

PDE11A

Enzyme 121 GenAtlas ID

PDE11A

Enzyme 121 HGNC ID

HGNC:8773

Enzyme 121 Chromosome Location

Enzyme 121 Locus

2q31.2

Enzyme 121 SNPs

SNPJam Report Link Image

Enzyme 121 General References

Yuasa K, Kotera J, Fujishige K, Michibata H, Sasaki T, Omori K: Isolation and characterization of two novel phosphodiesterase PDE11A variants showing unique structure and tissue-specific expression. J Biol Chem. 2000 Oct 6;275(40):31469-79. [PubMed ]
Fawcett L, Baxendale R, Stacey P, McGrouther C, Harrow I, Soderling S, Hetman J, Beavo JA, Phillips SC: Molecular cloning and characterization of a distinct human phosphodiesterase gene family: PDE11A. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3702-7. [PubMed ]
Hetman JM, Robas N, Baxendale R, Fidock M, Phillips SC, Soderling SH, Beavo JA: Cloning and characterization of two splice variants of human phosphodiesterase 11A. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12891-5. [PubMed ]
Yuasa K, Kanoh Y, Okumura K, Omori K: Genomic organization of the human phosphodiesterase PDE11A gene. Evolutionary relatedness with other PDEs containing GAF domains. Eur J Biochem. 2001 Jan;268(1):168-78. [PubMed ]
Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Loughney K, Taylor J, Florio VA: 3',5'-cyclic nucleotide phosphodiesterase 11A: localization in human tissues. Int J Impot Res. 2005 Jul-Aug;17(4):320-5. [PubMed ]
Francis SH: Phosphodiesterase 11 (PDE11): is it a player in human testicular function? Int J Impot Res. 2005 Sep-Oct;17(5):467-8. [PubMed ]
Gross-Langenhoff M, Hofbauer K, Weber J, Schultz A, Schultz JE: cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11. J Biol Chem. 2006 Feb 3;281(5):2841-6. Epub 2005 Dec 5. [PubMed ]
Horvath A, Boikos S, Giatzakis C, Robinson-White A, Groussin L, Griffin KJ, Stein E, Levine E, Delimpasi G, Hsiao HP, Keil M, Heyerdahl S, Matyakhina L, Libe R, Fratticci A, Kirschner LS, Cramer K, Gaillard RC, Bertagna X, Carney JA, Bertherat J, Bossis I, Stratakis CA: A genome-wide scan identifies mutations in the gene encoding phosphodiesterase 11A4 (PDE11A) in individuals with adrenocortical hyperplasia. Nat Genet. 2006 Jul;38(7):794-800. Epub 2006 Jun 11. [PubMed ]

Enzyme 121 Metabolite References

Not Available

Enzyme 122 [top]

Enzyme 122 ID

12980

Enzyme 122 Name

cDNA FLJ77907, highly similar to Homo sapiens aspartyl-tRNA synthetase, mRNA

Enzyme 122 Synonyms

Aspartyl-tRNA synthetase, isoform CRA_a

Enzyme 122 Gene Name

DARS

Enzyme 122 Protein Sequence

>cDNA FLJ77907, highly similar to Homo sapiens aspartyl-tRNA synthetase, mRNA

MPSASASRKSQEKPREIMDAAEDYAKERYGISSMIQSQEKPDRVLVRVRDLTIQKADEVV
WVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVV
RKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAEGEEEGRATVNQDTRL
DNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYF
KNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYH
EVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLREAGV
EMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFM
RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLF
LGLHNVRQTSMFPRDPKRLTP

Enzyme 122 Number of Residues

501

Enzyme 122 Molecular Weight

57137

Enzyme 122 Theoretical pI

6.52

Enzyme 122 GO Classification

Not Available

Enzyme 122 General Function

Translation, ribosomal structure and biogenesis

Enzyme 122 Specific Function

Not Available

Enzyme 122 Pathways

Not Available

Enzyme 122 Reactions

Not Available

Enzyme 122 Pfam Domain Function

Not Available

Enzyme 122 Signals

None

Enzyme 122 Transmembrane Regions

None

Enzyme 122 Essentiality

Not Available

Enzyme 122 GenBank ID Protein

158254646

Enzyme 122 UniProtKB/Swiss-Prot ID

A8K3J2

Enzyme 122 UniProtKB/Swiss-Prot Entry Name

A8K3J2_HUMAN Link Image

Enzyme 122 PDB ID

Not Available

Enzyme 122 Cellular Location

Not Available

Enzyme 122 Gene Sequence

Not Available

Enzyme 122 GenBank Gene ID

AK290607

Enzyme 122 GeneCard ID

A8K3J2

Enzyme 122 GenAtlas ID

Not Available

Enzyme 122 HGNC ID

Not Available

Enzyme 122 Chromosome Location

Not Available

Enzyme 122 Locus

Not Available

Enzyme 122 SNPs

SNPJam Report Link Image

Enzyme 122 General References

Not Available

Enzyme 122 Metabolite References

Not Available

Enzyme 123 [top]

Enzyme 123 ID

12994

Enzyme 123 Name

Probable arginyl-tRNA synthetase, mitochondrial

Enzyme 123 Synonyms

Arginine--tRNA ligase
ArgRS
Arginyl-tRNA synthetase-like

Enzyme 123 Gene Name

RARS2

Enzyme 123 Protein Sequence

>Probable arginyl-tRNA synthetase, mitochondrial

MACGFRRAIACQLSRVLNLPPENLITSISAVPISQKEEVADFQLSVDSLLEKDNDHSRPD
IQVQAKRLAEKLRCDTVVSEISTGQRTVNFKINRELLTKTVLQQVIEDGSKYGLKSELFS
GLPQKKIVVEFSSPNVAKKFHVGHLRSTIIGNFIANLKEALGHQVIRINYLGDWGMQFGL
LGTGFQLFGYEEKLQSNPLQHLFEVYVQVNKEAADDKSVAKAAQEFFQRLELGDVQALSL
WQKFRDLSIEEYIRVYKRLGVYFDEYSGESFYREKSQEVLKLLESKGLLLKTIKGTAVVD
LSGNGDPSSICTVMRSDGTSLYATRDLAAAIDRMDKYNFDTMIYVTDKGQKKHFQQVFQM
LKIMGYDWAERCQHVPFGVVQGMKTRRGDVTFLEDVLNEIQLRMLQNMASIKTTKELKNP
QETAERVGLAALIIQDFKGLLLSDYKFSWDRVFQSRGDTGVFLQYTHARLHSLEETFGCG
YLNDFNTACLQEPQSVSILQHLLRFDEVLYKSSQDFQPRHIVSYLLTLSHLAAVAHKTLQ
IKDSPPEVAGARLHLFKAVRSVLANGMKLLGITPVCRM

Enzyme 123 Number of Residues

578

Enzyme 123 Molecular Weight

65504.9

Enzyme 123 Theoretical pI

8.36

Enzyme 123 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity arginine-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process arginyl-tRNA aminoacylation biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 123 General Function

Involved in nucleotide binding

Enzyme 123 Specific Function

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)

Enzyme 123 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Arginine and Proline Metabolism (map00330 )

Enzyme 123 Reactions

ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg [RN:R03646]

Enzyme 123 Pfam Domain Function

DALR_1 (PF05746 )
tRNA-synt_1d (PF00750 )

Enzyme 123 Signals

None

Enzyme 123 Transmembrane Regions

None

Enzyme 123 Essentiality

Not Available

Enzyme 123 GenBank ID Protein

10435519

Enzyme 123 UniProtKB/Swiss-Prot ID

Q5T160

Enzyme 123 UniProtKB/Swiss-Prot Entry Name

SYRM_HUMAN Link Image

Enzyme 123 PDB ID

Not Available

Enzyme 123 Cellular Location

Not Available

Enzyme 123 Gene Sequence

>1737 bp

ATGGCGTGCGGCTTTCGCCGCGCTATTGCTTGCCAGCTTTCCAGAGTGTTGAATCTTCCA
CCAGAAAACTTGATCACATCAATATCTGCAGTTCCAATTTCCCAAAAAGAAGAAGTAGCT
GATTTTCAGCTTTCTGTGGATCCTTTATTGGAAAAAGACAATGACCATTCAAGACCAGAT
ATTCAAGTTCAAGCCAAGAGACTAGCAGAGAAGCTAAGATGTGATACAGTGGTGAGTGAA
ATCAGTACTGGTCAAAGGACTGTAAATTTCAAAATAAACAGAGAGCTCTTAACAAAGACA
GTGCTACAACAAGTAATTGAAGATGGCTCAAAATATGGATTAAAAAGTGAACTTTTCTCT
GGACTTCCCCAGAAGAAGATTGTGGTTGAATTCAGTTCACCTAATGTTGCCAAAAAATTT
CATGTTGGACATTTGCGTTCTACCGTCATAGGAAATTTTATAGCAAATCTCAAAGAAGCT
TTAGGACATCAAGTAATAAGAATAAATTACCTTGGCGATTGGGGCATGCAGTTTGGTCTT
CTGGGAACTGGCTTCCAGCTGTTTGGCTATGAGGAAAAACTGCAGTCCAATCCTCTACAG
CATCTCTTTGAAGTTTATGTACAAGTTAATAAAGAAGCAGCGGATGATAAAAGTGTAGCA
AAAGCAGCACAGGAGTTCTTCCAACGATTGGAACTGGGCGATGTGCAAGCACTTTCACTG
TGGCAAAAATTTCGGGACTTGAGCATTGAAGAGTACATTCGGGTTTACAAGCGTCTGGGA
GTATATTTTGATGAATATTCAGGAGAATCATTTTATCGTGAAAAATCTCAAGAGGTCTTA
AAGTTGCTGGAGAGTAAAGGACTCCTACTGAAAACAATAAAAGGAACGGCTGTAGTAGAT
CTCTCTGGGAATGGCGACCCCTCCTCAATTTGTACTGTAATGCGAAGTGATGGGACTTCT
CTCTATGCAACCAGAGATCTTGCAGCTGCTGTAGATCGAATGGACAAGTATAATTTTGAT
ACAATGATATATGTGACAGATAAAGGACAAAAAAAGCATTTTCAGCAAGTATTCCAAATG
CTGAAGATCATGGGATATGACTGGGCAGAAAGGTGCCAGCACGTGCCCTTTGGAGTAGTA
CAGGGAATGAAGACTCGAAGAGGAGATGTCACTTTCCTGGAAGATGTTTTAAATGAGATT
CAATTAAGGATGCTACAGAACATGGCTTCAATTAAGACAACTAAAGAACTCAAGAACCCA
CAAGAGACTGCAGAGAGGGTCGGGCTCGCAGCACTCATTATTCAGGACTTCAAAGGTTTA
CTCTTATCTGACTACAAGTTCAGCTGGGATCGTGTTTTCCAGAGTCGCGGGGACACAGGA
GTCTTCCTACAGTACACACACGCCCGCCTCCACAGTTTGGAAGAGACTTTTGGATGTGGG
TACCTGAATGACTTCAACACTGCTTGTTTACAAGAGCCACAGTCTGTTTCAATTCTTCAG
CATCTTCTCAGGTTCGACGAGGTGCTTTATAAATCATCTCAGGACTTTCAACCCAGGCAT
ATCGTCAGTTACCTTCTAACTTTAAGTCATCTTGCAGCTGTGGCACACAAAACACTACAA
ATAAAAGATAGTCCTCCTGAAGTGGCTGGGGCCAGACTTCATCTTTTCAAAGCTGTCCGT
TCTGTCCTAGCCAATGGAATGAAACTTCTTGGAATAACACCTGTATGTAGGATGTAA

Enzyme 123 GenBank Gene ID

AK023550

Enzyme 123 GeneCard ID

RARS2

Enzyme 123 GenAtlas ID

RARS2

Enzyme 123 HGNC ID

HGNC:21406 Link Image

Enzyme 123 Chromosome Location

Enzyme 123 Locus

6q16.1

Enzyme 123 SNPs

SNPJam Report Link Image

Enzyme 123 General References

Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M: Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. [PubMed ]
Edvardson S, Shaag A, Kolesnikova O, Gomori JM, Tarassov I, Einbinder T, Saada A, Elpeleg O: Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase gene is associated with pontocerebellar hypoplasia. Am J Hum Genet. 2007 Oct;81(4):857-62. Epub 2007 Aug 24. [PubMed ]

Enzyme 123 Metabolite References

Not Available

Enzyme 124 [top]

Enzyme 124 ID

13018

Enzyme 124 Name

Probable cysteinyl-tRNA synthetase, mitochondrial

Enzyme 124 Synonyms

Cysteine--tRNA ligase
CysRS

Enzyme 124 Gene Name

CARS2

Enzyme 124 Protein Sequence

>Probable cysteinyl-tRNA synthetase, mitochondrial

MLRTTRGPGLGPPLLQAALGLGRAGWHWPAGRAASGGRGRAWLQPTGRETGVQVYNSLTG
RKEPLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILTKVFGCSIVMVMGITD
VDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGII
ARGNAYSTAKGNVYFDLKSRGDKYGKLVGVVPGPVGEPADSDKRHASDFALWKAAKPQEV
FWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWG
NYFLHSGHLHAKGKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAM
LQAQQLLLGLGSFLEDARAYMKGQLACGSVREAMLWERLSSTKRAVKAALADDFDTPRVV
DAILGLAHHGNGQLRASLKEPEGPRSPAVFGAIISYFEQFFETVGISLANQQYVSGDGSE
ATLHGVVDELVRFRQKVRQFALAMPEATGDARRQQLLERQPLLEACDTLRRGLTAHGINI
KDRSSTTSTWELLDQRTKDQKSAG

Enzyme 124 Number of Residues

564

Enzyme 124 Molecular Weight

62223.3

Enzyme 124 Theoretical pI

8.46

Enzyme 124 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity cysteine-tRNA ligase activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process cysteinyl-tRNA aminoacylation macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 124 General Function

Involved in nucleotide binding

Enzyme 124 Specific Function

ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)

Enzyme 124 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Cysteine Metabolism (map00272 )

Enzyme 124 Reactions

ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys [RN:R03650]

Enzyme 124 Pfam Domain Function

tRNA-synt_1e (PF01406 )

Enzyme 124 Signals

None

Enzyme 124 Transmembrane Regions

None

Enzyme 124 Essentiality

Not Available

Enzyme 124 GenBank ID Protein

Not Available

Enzyme 124 UniProtKB/Swiss-Prot ID

Q9HA77

Enzyme 124 UniProtKB/Swiss-Prot Entry Name

SYCM_HUMAN Link Image

Enzyme 124 PDB ID

Not Available

Enzyme 124 Cellular Location

Not Available

Enzyme 124 Gene Sequence

>1695 bp

ATGTTGAGGACTACGCGCGGCCCAGGCCTGGGCCCCCCGCTGCTCCAGGCCGCGCTGGGC
CTTGGGCGGGCTGGGTGGCACTGGCCTGCGGGCCGGGCGGCGAGCGGGGGGCGCGGGCGG
GCCTGGCTGCAGCCCACGGGCCGGGAGACGGGTGTGCAGGTGTACAACAGCCTCACCGGG
AGGAAGGAACCCCTAATCGTGGCGCACGCCGAAGCCGCCTCCTGGTATAGCTGTGGACCA
ACTGTATATGATCATGCGCACCTTGGCCATGCTTGCTCATATGTTAGATTTGATATCATT
CGAAGGATCCTAACCAAGGTTTTTGGATGCAGCATAGTCATGGTGATGGGTATTACAGAT
GTAGATGATAAAATCATCAAAAGAGCCAATGAGATGAATATTTCCCCCGCTTCCCTCGCC
AGTCTTTATGAGGAAGACTTCAAGCAGGACATGGCAGCCCTGAAGGTTCTCCCACCCACG
GTGTACCTGAGGGTAACCGAAAATATTCCTCAGATAATTTCTTTCATTGAAGGAATCATT
GCTCGTGGGAACGCTTATTCAACGGCAAAAGGCAATGTCTACTTCGATCTGAAGTCTAGA
GGAGACAAGTATGGCAAATTGGTCGGCGTGGTCCCTGGTCCAGTCGGAGAGCCAGCGGAC
TCTGACAAGCGTCATGCCAGTGACTTCGCCCTGTGGAAGGCGGCCAAACCCCAGGAGGTG
TTCTGGGCCTCTCCCTGGGGACCCGGGAGGCCGGGCTGGCACATCGAGTGCTCTGCCATC
GCTAGTATGGTATTTGGAAGTCAACTGGATATCCATTCAGGTGGGATAGATTTAGCTTTT
CCACATCATGAGAACGAAATTGCACAGTGCGAAGTCTTTCATCAGTGCGAGCAGTGGGGA
AATTATTTTCTGCATTCTGGGCATTTGCACGCCAAAGGCAAAGAAGAAAAAATGTCCAAA
TCATTAAAGAACTACATTACTATTAAGGACTTTCTGAAGACCTTTTCCCCCGATGTCTTC
CGGTTCTTCTGCCTGCGGAGCAGCTACCGCTCAGCCATCGACTACAGTGACAGCGCCATG
CTCCAAGCTCAGCAGCTGCTCCTGGGGCTGGGCTCTTTCCTGGAGGACGCACGTGCCTAC
ATGAAGGGGCAGCTGGCCTGCGGCTCCGTCAGGGAAGCGATGCTGTGGGAGAGGCTCTCC
AGCACCAAGAGGGCCGTGAAGGCGGCCTTGGCAGATGATTTTGACACACCCAGGGTGGTT
GATGCCATCCTGGGCCTTGCACACCACGGGAATGGACAGCTCAGGGCGTCCCTGAAGGAA
CCTGAAGGGCCGAGAAGTCCTGCTGTGTTTGGTGCCATCATCTCTTACTTTGAACAGTTT
TTTGAAACTGTTGGAATTTCTCTGGCAAATCAACAGTACGTTTCAGGAGACGGCAGCGAG
GCTACCTTGCATGGTGTGGTGGACGAGCTGGTGCGGTTCCGGCAGAAGGTCCGGCAGTTT
GCGCTGGCCATGCCCGAGGCCACGGGGGACGCCCGGCGGCAGCAGCTCCTAGAAAGGCAG
CCCCTGCTGGAAGCATGCGACACCCTGCGCCGGGGCCTGACTGCCCACGGCATCAACATC
AAGGACAGAAGCAGTACAACATCCACGTGGGAACTGCTGGATCAAAGGACAAAAGACCAA
AAATCAGCGGGCTGA

Enzyme 124 GenBank Gene ID

AK022180

Enzyme 124 GeneCard ID

CARS2

Enzyme 124 GenAtlas ID

CARS2

Enzyme 124 HGNC ID

HGNC:25695 Link Image

Enzyme 124 Chromosome Location

Enzyme 124 Locus

13q34

Enzyme 124 SNPs

SNPJam Report Link Image

Enzyme 124 General References

Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M: Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 124 Metabolite References

Not Available

Enzyme 125 [top]

Enzyme 125 ID

13039

Enzyme 125 Name

Guanine monphosphate synthetase, isoform CRA_b

Enzyme 125 Synonyms

SubName: cDNA FLJ75406, highly similar to Homo sapiens guanine monphosphate synthetase (GMPS), mRNA
SubName: cDNA, FLJ79481, highly similar to GMP synthase (glutamine-hydrolyzing) (EC6.3.5.2)

Enzyme 125 Gene Name

GMPS

Enzyme 125 Protein Sequence

>Guanine monphosphate synthetase, isoform CRA_b

MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE

Enzyme 125 Number of Residues

693

Enzyme 125 Molecular Weight

76714.8

Enzyme 125 Theoretical pI

6.86

Enzyme 125 GO Classification

Function
ATP binding GMP synthase (glutamine-hydrolyzing) activity GMP synthase (glutamine-hydrolyzing) activity adenyl nucleotide binding adenyl ribonucleotide binding binding carbon-nitrogen ligase activity, with glutamine as amido-N-donor catalytic activity ligase activity ligase activity, forming carbon-nitrogen bonds nucleoside binding purine nucleoside binding
Process
GMP biosynthetic process biosynthetic process cellular amino acid and derivative metabolic process cellular amino acid metabolic process cellular metabolic process cellular nitrogen compound metabolic process glutamine family amino acid metabolic process glutamine metabolic process metabolic process nitrogen compound metabolic process nucleobase, nucleoside and nucleotide metabolic process nucleobase, nucleoside, nucleotide and nucleic acid metabolic process nucleoside phosphate metabolic process nucleotide metabolic process purine nucleoside monophosphate biosynthetic process purine nucleotide biosynthetic process purine nucleotide metabolic process purine ribonucleoside monophosphate biosynthetic process
Component
—

Enzyme 125 General Function

Involved in catalytic activity

Enzyme 125 Specific Function

Not Available

Enzyme 125 Pathways

Not Available

Enzyme 125 Reactions

Not Available

Enzyme 125 Pfam Domain Function

GATase (PF00117 )
GMP_synt_C (PF00958 )
NAD_synthase (PF02540 )

Enzyme 125 Signals

None

Enzyme 125 Transmembrane Regions

None

Enzyme 125 Essentiality

Not Available

Enzyme 125 GenBank ID Protein

158256440

Enzyme 125 UniProtKB/Swiss-Prot ID

A8K639

Enzyme 125 UniProtKB/Swiss-Prot Entry Name

A8K639_HUMAN Link Image

Enzyme 125 PDB ID

Not Available

Enzyme 125 Cellular Location

Not Available

Enzyme 125 Gene Sequence

>2082 bp

ATGGCTCTGTGCAACGGAGACTCCAAGCTGGAGAATGCTGGAGGAGACCTTAAGGATGGC
CACCACCACTATGAAGGAGCTGTTGTCATTCTGGATGCTGGTGCTCAGTACGGGAAAGTC
ATAGACCGAAGAGTGAGGGAACTGTTCGTGCAGTCTGAAATTTTCCCCTTGGAAACACCA
GCATTTGCTATAAAGGAACAAGGATTCCGTGCTATTATCATCTCTGGAGGACCTAATTCT
GTGTATGCTGAAGATGCTCCCTGGTTTGATCCAGCAATATTCACTATTGGCAAGCCTGTT
CTTGGAATTTGCTATGGTATGCAGATGATGAATAAGGTATTTGGAGGTACTGTGCACAAA
AAAAGTGTCAGAGAAGATGGAGTTTTCAACATTAGTGTGGATAATACATGTTCATTATTC
AGGGGCCTTCAGAAGGAAGAAGTTGTTTTGCTTACACATGGAGATAGTGTAGACAAAGTA
GCTGATGGATTCAAGGTTGTGGCACGTTCTGGAAACATAGTAGCAGGCATAGCAAATGAA
TCTAAAAAGTTATATGGAGCACAGTTCCACCCTGAAGTTGGCCTTACAGAAAATGGAAAA
GTAATACTGAAGAATTTCCTTTATGATATAGCTGGATGCAGTGGAACCTTCACCGTGCAG
AACAGAGAACTTGAGTGTATTCGAGAGATCAAAGAGAGAGTAGGCACGTCAAAAGTTTTG
GTTTTACTCAGTGGTGGAGTAGACTCAACAGTTTGTACAGCTTTGCTAAATCGTGCTTTG
AACCAAGAACAAGTCATTGCTGTGCACATTGATAATGGCTTTATGAGAAAACGAGAAAGC
CAGTCTGTTGAAGAGGCCCTCAAAAAGCTTGGAATTCAGGTCAAAGTGATAAATGCTGCT
CATTCTTTCTACAATGGAACAACAACCCTACCAATATCAGATGAAGATAGAACCCCACGG
AAAAGAATTAGCAAAACGTTAAATATGACCACAAGTCCTGAAGAGAAAAGAAAAATCATT
GGGGATACTTTTGTTAAGATTGCCAATGAAGTAATTGGAGAAATGAACTTGAAACCAGAG
GAGGTTTTCCTTGCCCAAGGTACTTTACGGCCTGATCTAATTGAAAGTGCATCCCTTGTT
GCAAGTGGCAAAGCTGAACTCATCAAAACCCATCACAATGACACAGAGCTCATCAGAAAG
TTGAGAGAGGAGGGAAAAGTAATAGAACCTCTGAAAGATTTTCATAAAGATGAAGTGAGA
ATTTTGGGCAGAGAACTTGGACTTCCAGAAGAGTTAGTTTCCAGGCATCCATTTCCAGGT
CCTGGCCTGGCAATCAGAGTAATATGTGCTGAAGAACCTTATATTTGTAAGGACTTTCCT
GAAACCAACAATATTTTGAAAATAGTAGCTGATTTTTCTGCAAGTGTTAAAAAGCCACAT
ACCCTATTACAGAGAGTCAAAGCCTGCACAACAGAAGAGGATCAGGAGAAGCTGATGCAA
ATTACCAGTCTGCATTCACTGAATGCCTTCTTGCTGCCAATTAAAACTGTAGGTGTGCAG
GGTGACTGTCGTTCCTACAGTTACGTGTGTGGAATCTCCAGTAAAGATGAACCTGACTGG
GAATCACTTATTTTTCTGGCTAGGCTTATACCTCGCATGTGTCACAACGTTAACAGAGTT
GTTTATATATTTGGCCCACCAGTTAAAGAACCTCCTACAGATGTTACTCCCACTTTCTTG
ACAACAGGGGTGCTCAGTACTTTACGCCAAGCTGATTTTGAGGCCCATAACATTCTCAGG
GAGTCTGGGTATGCTGGGAAAATCAGCCAGATGCCGGTGATTTTGACACCATTACATTTT
GATCGGGACCCACTTCAAAAGCAGCCTTCATGCCAGAGATCTGTGGTTATTCGAACCTTT
ATTACTAGTGACTTCATGACTGGTATACCTGCAACACCTGGCAATGAGATCCCTGTAGAG
GTGGTATTAAAGATGGTCACTGAGATTAAGAAGATTCCTGGTATTTCTCGAATTATGTAT
GACTTAACATCAAAGCCCCCAGGAACTACTGAGTGGGAGTAA

Enzyme 125 GenBank Gene ID

AK291504

Enzyme 125 GeneCard ID

GMPS

Enzyme 125 GenAtlas ID

GMPS

Enzyme 125 HGNC ID

HGNC:4378

Enzyme 125 Chromosome Location

Enzyme 125 Locus

3q24

Enzyme 125 SNPs

SNPJam Report Link Image

Enzyme 125 General References

Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed ]

Enzyme 125 Metabolite References

Not Available

Enzyme 126 [top]

Enzyme 126 ID

13041

Enzyme 126 Name

Probable glutamyl-tRNA synthetase, mitochondrial

Enzyme 126 Synonyms

Glutamate--tRNA ligase
GluRS

Enzyme 126 Gene Name

EARS2

Enzyme 126 Protein Sequence

>Probable glutamyl-tRNA synthetase, mitochondrial

MAALLRRLLQRERPSAASGRPVGRREANLGTDAGVAVRVRFAPSPTGFLHLGGLRTALYN
YIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPYQQSQR
LELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLA
KDPKPAIRFRLEQVVPAFQDLVYGWNRHEVASVEGDPVIMKSDGFPTYHLACVVDDHHMG
ISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLSKRQGDVFLEHFAAD
GFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQ
RLVSNESQRRQLVGKLQVLVEEAFGCQLQNRDVLNPVYVERILLLRQGHICRLQDLVSPV
YSYLWTRPAVGRAQLDAISEKVDVIAKRVLGLLERSSMSLTQDMLNGELKKLSEGLEGTK
YSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQKVVSS

Enzyme 126 Number of Residues

523

Enzyme 126 Molecular Weight

58688.1

Enzyme 126 Theoretical pI

8.98

Enzyme 126 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity glutamate-tRNA ligase activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process glutamyl-tRNA aminoacylation macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation
Component
cell part cytoplasm intracellular part

Enzyme 126 General Function

Involved in nucleotide binding

Enzyme 126 Specific Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction:glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu)

Enzyme 126 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Glutamate Metabolism (map00251 )
Porphyrin Metabolism (map00860 )

Enzyme 126 Reactions

ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu [RN:R05578]

Enzyme 126 Pfam Domain Function

tRNA-synt_1c (PF00749 )

Enzyme 126 Signals

None

Enzyme 126 Transmembrane Regions

None

Enzyme 126 Essentiality

Not Available

Enzyme 126 GenBank ID Protein

134288884

Enzyme 126 UniProtKB/Swiss-Prot ID

Q5JPH6

Enzyme 126 UniProtKB/Swiss-Prot Entry Name

SYEM_HUMAN Link Image

Enzyme 126 PDB ID

Not Available

Enzyme 126 Cellular Location

Not Available

Enzyme 126 Gene Sequence

>1572 bp

ATGGCGGCGCTCCTGAGGAGACTGCTGCAGCGCGAGAGGCCTTCGGCGGCCTCTGGCCGC
CCCGTAGGACGGCGCGAGGCCAACCTGGGCACTGATGCCGGGGTTGCGGTGCGAGTGCGG
TTCGCTCCCAGCCCCACAGGCTTCTTGCACCTGGGTGGCCTCCGCACTGCCTTGTACAAC
TACATCTTTGCTAAGAAGTACCAGGGGAGCTTCATCCTGAGGCTAGAGGACACAGATCAG
ACTCGCGTTGTGCCTGGGGCAGCGGAGAATATTGAGGACATGCTGGAGTGGGCAGGCATC
CCGCCTGATGAGAGCCCCCGCCGGGGCGGTCCTGCTGGGCCCTACCAGCAATCTCAGCGG
TTGGAGCTGTATGCCCAGGCCACAGAAGCGCTGCTGAAGACCGGAGCTGCTTACCCCTGT
TTCTGCTCACCCCAGCGGCTGGAGCTCCTGAAGAAGGAGGCCTTGCGGAACCACCAGACG
CCCCGGTATGACAATCGGTGCAGGAACATGAGCCAGGAGCAGGTGGCCCAGAAGCTGGCC
AAGGACCCCAAGCCTGCGATCCGCTTCCGCCTGGAGCAGGTGGTGCCAGCCTTCCAGGAC
CTGGTCTATGGCTGGAATAGGCATGAAGTGGCCAGCGTGGAGGGAGACCCAGTCATCATG
AAGAGCGACGGCTTCCCCACATACCACCTGGCCTGCGTGGTGGACGACCACCACATGGGC
ATCAGCCACGTGCTGCGAGGCTCTGAGTGGCTCGTCTCCACTGCCAAGCACCTGCTCCTC
TACCAGGCCCTGGGCTGGCAGCCACCCCACTTCGCCCACCTGCCCCTGCTCCTCAACAGG
GATGGCAGCAAGCTCTCCAAGAGGCAAGGGGACGTTTTCCTGGAGCACTTTGCTGCTGAT
GGCTTCCTGCCCGATTCCTTGTTGGACATCATCACCAACTGTGGCTCAGGTTTTGCAGAG
AACCAAATGGGCAGGACCCTGCCGGAGCTGATCACACAGTTCAACCTGACACAGGTCACC
TGTCACTCAGCCCTGCTGGACCTGGAGAAGCTCCCAGAATTCAACAGACTGCACCTCCAG
CGGCTGGTGAGCAATGAGAGCCAGAGGCGCCAGCTGGTGGGGAAGCTGCAGGTCCTTGTG
GAGGAGGCCTTTGGTTGCCAGCTGCAAAACAGGGATGTCCTCAACCCAGTCTACGTGGAG
AGGATCCTCCTGCTGAGACAGGGTCACATTTGCCGCCTGCAGGACTTGGTGTCCCCAGTA
TACTCTTACCTGTGGACTCGCCCTGCAGTAGGTCGAGCACAGCTGGACGCCATCTCGGAG
AAGGTGGATGTGATTGCCAAGCGTGTGCTGGGGCTTCTAGAAAGATCTAGTATGAGCTTA
ACTCAGGATATGCTGAATGGAGAACTGAAGAAGCTATCAGAAGGTCTGGAAGGCACCAAG
TACAGTAATGTGATGAAACTCCTTCGGATGGCCCTCAGTGGACAGCAGCAAGGACCTCCT
GTAGCTGAGATGATGTTGGCCTTGGGACCAAAGGAAGTACGGGAACGGATCCAGAAGGTG
GTTTCCAGCTAG

Enzyme 126 GenBank Gene ID

NM_001083614.1 Link Image

Enzyme 126 GeneCard ID

EARS2

Enzyme 126 GenAtlas ID

EARS2

Enzyme 126 HGNC ID

HGNC:29419 Link Image

Enzyme 126 Chromosome Location

Enzyme 126 Locus

16p12.2

Enzyme 126 SNPs

SNPJam Report Link Image

Enzyme 126 General References

Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed ]
Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M: Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. [PubMed ]
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]

Enzyme 126 Metabolite References

Not Available

Enzyme 127 [top]

Enzyme 127 ID

13056

Enzyme 127 Name

cDNA FLJ75173, highly similar to Homo sapiens threonyl-tRNA synthetase, mRNA

Enzyme 127 Synonyms

Threonyl-tRNA synthetase, isoform CRA_b

Enzyme 127 Gene Name

TARS

Enzyme 127 Protein Sequence

>cDNA FLJ75173, highly similar to Homo sapiens threonyl-tRNA synthetase, mRNA

MFEEKASSPSGKMGGEEKPIGAGEEKQKEGGKKKNKEGSGDGGRAELNPWPEYIYTRLEM
YNILKAEHDSILAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIA
KVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIE
NGFYYDMYLEEGGVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRIL
NEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGI
SFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFI
RSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMF
DHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL
DFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFY
GPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERM
IAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGCTLNK
KIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRSKQAE
EEF

Enzyme 127 Number of Residues

723

Enzyme 127 Molecular Weight

83436

Enzyme 127 Theoretical pI

6.64

Enzyme 127 GO Classification

Not Available

Enzyme 127 General Function

Translation, ribosomal structure and biogenesis

Enzyme 127 Specific Function

Not Available

Enzyme 127 Pathways

Not Available

Enzyme 127 Reactions

Not Available

Enzyme 127 Pfam Domain Function

Not Available

Enzyme 127 Signals

None

Enzyme 127 Transmembrane Regions

None

Enzyme 127 Essentiality

Not Available

Enzyme 127 GenBank ID Protein

158258124

Enzyme 127 UniProtKB/Swiss-Prot ID

A8K8I1

Enzyme 127 UniProtKB/Swiss-Prot Entry Name

A8K8I1_HUMAN Link Image

Enzyme 127 PDB ID

Not Available

Enzyme 127 Cellular Location

Not Available

Enzyme 127 Gene Sequence

Not Available

Enzyme 127 GenBank Gene ID

AK292346

Enzyme 127 GeneCard ID

A8K8I1

Enzyme 127 GenAtlas ID

Not Available

Enzyme 127 HGNC ID

Not Available

Enzyme 127 Chromosome Location

Not Available

Enzyme 127 Locus

Not Available

Enzyme 127 SNPs

SNPJam Report Link Image

Enzyme 127 General References

Not Available

Enzyme 127 Metabolite References

Not Available

Enzyme 128 [top]

Enzyme 128 ID

13066

Enzyme 128 Name

Acyl-CoA synthetase family member 4

Enzyme 128 Synonyms

Protein NRPS998

Enzyme 128 Gene Name

AASDH

Enzyme 128 Protein Sequence

>Acyl-CoA synthetase family member 4

MTLQELVHKAASCYMDRVAVCFDECNNQLPVYYTYKTVVNAASELSNFLLLHCDFQGIRE
IGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKKQINKFK
SFHETLLNYDTFTVEHNDLVLFRLHWKNTEVNLMLNDGKEKYEKEKIKSISSEHVNEEKA
EEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL
TFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLRRFGSQL
IKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPE
KTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGSGQVFLGGRNRVCFLDDEVTVPL
GTMRATGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE
KLILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNY
INLKSENKLSGKEDLWEKLQYLWKSTLNLPEDLLRVPDESLFLNSGGDSLKSIRLLSEIE
KLVGTSVPGLLEIILSSSILEIYNHILQTVVPDEDVTFRKSCATKRKLSDINQEEASGTS
LHQKAIMTFTCHNEINAFVVLSRGSQILSLNSTRFLTKLGHCSSACPSDSVSQTNIQNLK
GLNSPVLIGKSKDPSCVAKVSEEGKPAIGTQKMELHVRWRSDTGKCVDASPLVVIPTFDK
SSTTVYIGSHSHRMKAVDFYSGKVKWEQILGDRIESSACVSKCGNFIVVGCYNGLVYVLK
SNSGEKYWMFTTEDAVKSSATMDPTTGLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFS
SPCLNLIPHHLYFATLGGLLLAVNPATGNVIWKHSCGKPLFSSPQCCSQYICIGCVDGNL
LCFTHFGEQVWQFSTSGPIFSSPCTSPSEQKIFFGSHDCFIYCCNMKGHLQWKFETTSRV
YATPFAFHNYNGSNEMLLAAASTDGKVWILESQSGQLQSVYELPGEVFSSPVVLESMLII
GCRDNYVYCLDLLGGNQK

Enzyme 128 Number of Residues

1098

Enzyme 128 Molecular Weight

122596.1

Enzyme 128 Theoretical pI

7.26

Enzyme 128 GO Classification

Function
acyl carrier activity binding catalytic activity cofactor binding substrate-specific transporter activity transporter activity
Process
metabolic process
Component
—

Enzyme 128 General Function

Involved in acyl carrier activity

Enzyme 128 Specific Function

Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA

Enzyme 128 Pathways

Not Available

Enzyme 128 Reactions

Not Available

Enzyme 128 Pfam Domain Function

AMP-binding (PF00501 )
PP-binding (PF00550 )

Enzyme 128 Signals

None

Enzyme 128 Transmembrane Regions

None

Enzyme 128 Essentiality

Not Available

Enzyme 128 GenBank ID Protein

45580730

Enzyme 128 UniProtKB/Swiss-Prot ID

Q4L235

Enzyme 128 UniProtKB/Swiss-Prot Entry Name

ACSF4_HUMAN Link Image

Enzyme 128 PDB ID

Not Available

Enzyme 128 Cellular Location

Not Available

Enzyme 128 Gene Sequence

>3297 bp

ATGACTCTTCAGGAATTGGTGCATAAGGCTGCCTCCTGTTATATGGACAGAGTAGCTGTA
TGTTTTGATGAATGCAACAACCAGCTTCCAGTTTACTACACCTACAAGACTGTGGTTAAT
GCTGCTTCTGAATTATCAAATTTTCTGCTGTTACACTGTGACTTTCAAGGAATTCGGGAA
ATTGGTCTCTACTGCCAACCTGGGATAGACTTACCCTCTTGGATTTTAGGAATTCTCCAA
GTCCCGGCTGCTTATGTACCTATCGAGCCAGATTCACCACCGTCATTATCAACTCATTTT
ATGAAAAAATGTAATCTAAAGTATATCCTTGTTGAAAAAAAACAAATTAATAAATTTAAA
TCTTTTCATGAAACATTATTGAACTATGATACATTTACAGTGGAACATAATGACCTAGTG
CTCTTCAGACTTCACTGGAAAAATACTGAGGTGAACTTGATGCTAAATGATGGAAAAGAG
AAATATGAAAAAGAAAAAATAAAAAGCATAAGTTCTGAGCATGTCAATGAAGAAAAAGCA
GAAGAACACATGGATCTGAGGCTAAAGCATTGCTTAGCCTATGTTCTACATACATCAGGG
ACTACAGGGATACCGAAGATTGTCAGAGTGCCTCATAAGTGTATAGTACCAAATATCCAG
CATTTTCGGGTACTTTTTGACATCACACAAGAAGATGTTTTGTTTCTGGCTTCACCTCTG
ACCTTCGATCCTTCTGTTGTGGAAATATTTCTTGCTCTATCAAGTGGTGCCTCTCTGCTT
ATTGTACCAACTTCCGTCAAGTTGCTCCCATCAAAATTAGCCAGCGTTCTCTTTTCCCAT
CATAGAGTGACTGTTTTGCAGGCAACACCAACATTGCTTAGAAGATTTGGATCTCAGCTT
ATCAAGTCAACTGTTTTGTCAGCCACTACTTCTCTTCGAGTATTAGCCCTTGGTGGTGAA
GCGTTTCCATCATTGACAGTTCTCAGAAGCTGGAGAGGAGAAGGCAATAAAACACAAATA
TTTAATGTTTATGGTATCACAGAGGTATCAAGTTGGGCGACCATTTATAGGATTCCAGAG
AAGACTCTTAACTCTACTCTCAAATGTGAATTGCCTGTACAACTGGGATTTCCACTTCTT
GGAACAGTAGTTGAAGTCAGAGATACTAATGGCTTCACAATTCAGGAAGGCAGTGGCCAA
GTATTTTTAGGTGGCAGAAACAGAGTGTGTTTTCTTGATGATGAAGTGACAGTACCACTT
GGCACAATGCGAGCTACAGGAGACTTTGTGACTGTGAAAGATGGAGAGATTTTTTTTTTG
GGACGAAAAGACAGTCAGATCAAACGTCATGGCAAACGTCTTAACATTGAACTTGTGCAA
CAGGTTGCTGAAGAGCTTCAGCAAGTGGAGTCTTGTGCAGTTACATGGTATAATCAGGAA
AAATTAATTCTCTTCATGGTGTCTAAAGATGCTTCAGTAAAAGAATACATCTTTAAAGAA
CTGCAGAAATATCTTCCAAGTCATGCAGTCCCGGATGAGCTTGTATTGATCGACTCTCTA
CCATTTACATCCCACGGCAAAATTGATGTTTCTGAGTTAAACAAGATATATTTAAACTAC
ATAAACTTGAAGTCTGAGAATAAGCTCAGTGGGAAAGAGGACCTTTGGGAAAAATTACAG
TATTTGTGGAAGTCTACTCTGAATCTCCCAGAAGATCTTTTGAGGGTTCCTGATGAGTCA
CTCTTCTTAAATAGTGGTGGAGATTCCTTAAAGTCCATCCGGCTCCTCAGTGAGATTGAA
AAACTTGTTGGTACATCAGTACCTGGGCTTCTGGAAATTATTCTCAGCAGTTCCATTTTA
GAGATTTATAATCACATCCTTCAAACAGTGGTTCCAGATGAAGATGTGACATTCAGGAAG
AGTTGTGCCACAAAAAGGAAACTCAGCGACATTAATCAAGAGGAAGCCAGTGGAACATCT
TTACATCAGAAAGCCATCATGACTTTCACTTGCCACAATGAGATTAATGCTTTTGTTGTA
CTGAGCAGAGGGAGTCAAATTTTGTCTCTGAATTCCACTAGGTTTTTAACAAAGTTAGGA
CATTGCTCTTCAGCCTGTCCTTCTGACTCAGTTTCACAGACCAACATTCAAAATTTGAAA
GGCTTAAATTCTCCAGTTCTTATTGGGAAGTCAAAAGATCCATCCTGTGTTGCAAAAGTT
TCTGAAGAGGGGAAACCTGCGATAGGGACTCAGAAAATGGAGTTACATGTGAGGTGGAGG
TCAGACACAGGCAAATGTGTAGATGCTTCACCGCTGGTTGTAATACCCACTTTTGATAAG
TCATCTACAACTGTGTACATTGGTTCCCATTCTCATAGAATGAAGGCAGTTGACTTTTAC
TCTGGGAAGGTAAAATGGGAACAGATTTTGGGAGATCGAATTGAATCCTCAGCATGTGTA
TCTAAGTGTGGAAACTTTATTGTGGTGGGCTGTTATAATGGATTAGTTTATGTTCTGAAA
AGTAATAGTGGAGAAAAATACTGGATGTTTACTACTGAAGATGCTGTCAAAAGCTCGGCA
ACCATGGATCCAACCACAGGACTCATTTACATTGGATCTCATGACCAGCACGCATATGCT
TTAGATATTTATAGAAAGAAGTGTGTTTGGAAGTCAAAATGTGGAGGAACTGTCTTTTCC
TCTCCGTGTTTGAACCTGATTCCACATCATTTGTATTTTGCTACATTGGGAGGACTTTTA
CTGGCTGTAAATCCTGCTACTGGGAACGTTATTTGGAAACATTCCTGTGGAAAACCACTC
TTCTCTTCCCCACAATGTTGCTCACAGTATATTTGTATTGGCTGTGTAGATGGGAATTTA
CTCTGCTTTACTCACTTTGGAGAACAGGTTTGGCAGTTCTCTACCAGTGGACCAATCTTT
TCATCCCCGTGTACCTCACCATCAGAGCAAAAAATATTTTTTGGTTCCCATGATTGCTTT
ATCTACTGTTGTAACATGAAAGGTCACCTGCAGTGGAAATTTGAAACTACTTCAAGGGTC
TATGCAACACCGTTTGCTTTCCATAACTACAATGGCAGCAATGAAATGTTGCTGGCAGCA
GCATCTACTGATGGGAAAGTGTGGATCTTGGAATCTCAGAGTGGACAATTGCAAAGTGTT
TATGAACTTCCTGGAGAAGTCTTCTCTTCTCCTGTGGTCCTGGAATCAATGCTCATTATT
GGGTGTAGAGATAATTATGTTTATTGTCTGGATTTATTGGGTGGCAATCAAAAATAA

Enzyme 128 GenBank Gene ID

NM_181806.2 Link Image

Enzyme 128 GeneCard ID

AASDH

Enzyme 128 GenAtlas ID

AASDH

Enzyme 128 HGNC ID

HGNC:23993 Link Image

Enzyme 128 Chromosome Location

Enzyme 128 Locus

4q12

Enzyme 128 SNPs

SNPJam Report Link Image

Enzyme 128 General References

Wang L, Jil C, Xu Y, Xu J, Dai J, Wu Q, Wu M, Zou X, Sun L, Gu S, Xie Y, Mao Y: Cloning and characterization of a novel human homolog* of mouse U26, a putative PQQ-dependent AAS dehydrogenase. Mol Biol Rep. 2005 Mar;32(1):47-53. [PubMed ]
Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]

Enzyme 128 Metabolite References

Not Available

Enzyme 129 [top]

Enzyme 129 ID

13073

Enzyme 129 Name

Peroxisomal NADH pyrophosphatase NUDT12

Enzyme 129 Synonyms

Nucleoside diphosphate-linked moiety X motif 12
Nudix motif 12

Enzyme 129 Gene Name

NUDT12

Enzyme 129 Protein Sequence

>Peroxisomal NADH pyrophosphatase NUDT12

MSSVKRSLKQEIVTQFHCSAAEGDIAKLTGILSHSPSLLNETSENGWTALMYAARNGHPE
IVQFLLEKGCDRSIVNKSRQTALDIAVFWGYKHIANLLATAKGGKKPWFLTNEVEECENY
FSKTLLDRKSEKRNNSDWLLAKESHPATVFILFSDLNPLVTLGGNKESFQQPEVRLCQLN
YTDIKDYLAQPEKITLIFLGVELEIKDKLLNYAGEVPREEEDGLVAWFALGIDPIAAEEF
KQRHENCYFLHPPMPALLQLKEKEAGVVAQARSVLAWHSRYKFCPTCGNATKIEEGGYKR
LCLKEDCPSLNGVHNTSYPRVDPVVIMQVIHPDGTKCLLGRQKRFPPGMFTCLAGFIEPG
ETIEDAVRREVEEESGVKVGHVQYVACQPWPMPSSLMIGCLALAVSTEIKVDKNEIEDAR
WFTREQVLDVLTKGKQQAFFVPPSRAIAHQLIKHWIRINPNL

Enzyme 129 Number of Residues

462

Enzyme 129 Molecular Weight

52075.5

Enzyme 129 Theoretical pI

6.82

Enzyme 129 GO Classification

Function
binding catalytic activity cation binding hydrolase activity ion binding metal ion binding
Process
—
Component
—

Enzyme 129 General Function

Involved in hydrolase activity

Enzyme 129 Specific Function

Hydrolyzes NAD(P)H to NMNH and AMP (2',5'-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle

Enzyme 129 Pathways

Nicotinate and Nicotinamide Metabolism (map00760 )

Enzyme 129 Reactions

NAD+ + H2O = AMP + NMN [RN:R00103]

Enzyme 129 Pfam Domain Function

Ank (PF00023 )
NUDIX (PF00293 )
NUDIX-like (PF09296 )
zf-NADH-PPase (PF09297 )

Enzyme 129 Signals

None

Enzyme 129 Transmembrane Regions

None

Enzyme 129 Essentiality

Not Available

Enzyme 129 GenBank ID Protein

193783663

Enzyme 129 UniProtKB/Swiss-Prot ID

Q9BQG2

Enzyme 129 UniProtKB/Swiss-Prot Entry Name

NUD12_HUMAN Link Image

Enzyme 129 PDB ID

Not Available

Enzyme 129 Cellular Location

Not Available

Enzyme 129 Gene Sequence

>1389 bp

ATGTCTTCTGTAAAAAGAAGTCTGAAGCAAGAAATAGTTACTCAGTTTCACTGTTCAGCT
GCTGAAGGAGATATTGCCAAGTTAACAGGAATACTCAGTCATTCTCCATCTCTTCTCAAT
GAAACTTCTGAAAATGGCTGGACTGCTTTAATGTATGCGGCAAGGAATGGGCACCCAGAG
ATAGTCCAATTTCTGCTTGAGAAAGGGTGTGACAGATCAATTGTCAATAAATCAAGGCAG
ACTGCACTGGATATTGCTGTATTTTGGGGTTATAAGCATATAGCTAATTTACTAGCTACT
GCTAAAGGTGGGAAGAAGCCTTGGTTCCTAACGAATGAAGTGGAAGAATGTGAAAATTAT
TTTAGCAAAACACTACTGGACCGGAAAAGTGAAAAGAGGAATAATTCTGACTGGCTGCTA
GCTAAAGAAAGCCATCCAGCCACAGTTTTTATTCTTTTCTCAGATTTAAATCCCTTGGTT
ACTCTAGGTGGCAATAAAGAAAGTTTCCAACAGCCAGAAGTTAGGCTTTGTCAGCTGAAC
TACACAGATATAAAGGATTATTTGGCCCAGCCTGAGAAGATCACCTTGATTTTTCTTGGA
GTAGAACTTGAAATAAAAGACAAACTACTTAATTATGCTGGTGAAGTCCCGAGAGAGGAG
GAAGATGGATTGGTTGCCTGGTTTGCTCTAGGTATAGATCCTATTGCTGCTGAAGAATTC
AAGCAAAGACATGAAAATTGTTACTTTCTTCATCCTCCTATGCCAGCCCTTCTGCAATTG
AAAGAAAAAGAAGCTGGGGTTGTAGCTCAAGCAAGATCTGTTCTTGCCTGGCACAGTCGA
TACAAGTTTTGCCCAACCTGTGGAAATGCAACTAAAATTGAAGAAGGTGGCTATAAGAGA
CTATGTTTAAAAGAAGACTGTCCTAGTCTCAATGGCGTCCATAATACCTCATACCCAAGA
GTTGATCCAGTAGTAATCATGCAAGTTATTCATCCAGATGGGACCAAATGCCTTTTAGGC
AGGCAGAAAAGATTTCCCCCAGGCATGTTTACTTGCCTTGCTGGATTTATTGAGCCTGGA
GAGACAATAGAAGATGCTGTTAGGAGAGAAGTAGAAGAGGAAAGTGGAGTCAAAGTTGGC
CATGTTCAGTATGTTGCTTGTCAACCATGGCCAATGCCTTCCTCCTTAATGATTGGTTGC
TTAGCTCTAGCAGTGTCTACAGAAATTAAAGTTGACAAGAATGAAATAGAGGATGCCCGC
TGGTTCACTAGAGAACAGGTCCTGGATGTTCTGACCAAAGGGAAGCAGCAGGCATTCTTT
GTGCCACCAAGCCGAGCTATTGCACATCAATTAATCAAACACTGGATTAGAATAAATCCT
AATCTCTAA

Enzyme 129 GenBank Gene ID

AK098066

Enzyme 129 GeneCard ID

NUDT12

Enzyme 129 GenAtlas ID

NUDT12

Enzyme 129 HGNC ID

HGNC:18826 Link Image

Enzyme 129 Chromosome Location

Enzyme 129 Locus

5q21.2

Enzyme 129 SNPs

SNPJam Report Link Image

Enzyme 129 General References

Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
Abdelraheim SR, Spiller DG, McLennan AG: Mammalian NADH diphosphatases of the Nudix family: cloning and characterization of the human peroxisomal NUDT12 protein. Biochem J. 2003 Sep 1;374(Pt 2):329-35. [PubMed ]

Enzyme 129 Metabolite References

Not Available

Enzyme 130 [top]

Enzyme 130 ID

13088

Enzyme 130 Name

ACSS2 protein

Enzyme 130 Synonyms

Not Available

Enzyme 130 Gene Name

ACSS2

Enzyme 130 Protein Sequence

>ACSS2 protein

PMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLK
ELADEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQISWNQGIDL
WWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDF
HAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFY
TAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQ
TETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMR
TVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA
LVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDY
IQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDMSTVADPSVISHLFSHRCLTIQ

Enzyme 130 Number of Residues

534

Enzyme 130 Molecular Weight

59346.4

Enzyme 130 Theoretical pI

5.68

Enzyme 130 GO Classification

Function
AMP binding CoA-ligase activity acetate-CoA ligase activity adenyl nucleotide binding adenyl ribonucleotide binding binding catalytic activity ligase activity ligase activity, forming carbon-sulfur bonds nucleoside binding purine nucleoside binding
Process
metabolic process
Component
—

Enzyme 130 General Function

Involved in acetate-CoA ligase activity

Enzyme 130 Specific Function

Not Available

Enzyme 130 Pathways

Not Available

Enzyme 130 Reactions

Not Available

Enzyme 130 Pfam Domain Function

AMP-binding (PF00501 )

Enzyme 130 Signals

None

Enzyme 130 Transmembrane Regions

None

Enzyme 130 Essentiality

Not Available

Enzyme 130 GenBank ID Protein

40226463

Enzyme 130 UniProtKB/Swiss-Prot ID

Q96FY7

Enzyme 130 UniProtKB/Swiss-Prot Entry Name

Q96FY7_HUMAN Link Image

Enzyme 130 PDB ID

Not Available

Enzyme 130 Cellular Location

Not Available

Enzyme 130 Gene Sequence

>1606 bp

GCCTATGATCCCAGAGCTTGTGGTGGCCATGCTGGCATGTGCCCGCATTGGGGCTTTGCA
CTCCATTGTGTTTGCAGGCTTCTCTTCAGAGTCTCTATGTGAACGGATCTTGGATTCCAG
CTGCAGTCTTCTCATCACTACAGATGCCTTCTACAGGGGGGAAAAGCTTGTGAACCTGAA
GGAGCTGGCTGACGAGGCCCTGCAGAAGTGTCAGGAGAAGGGTTTCCCAGTAAGATGCTG
CATTGTGGTCAAGCACCTGGGGCGGGCAGAGCTCGGCATGGGTGACTCCACCAGCCAGTC
CCCCCCAATTAAGAGGTCATGCCCAGATGTGCAGATCTCATGGAACCAAGGGATTGACTT
GTGGTGGCATGAGCTCATGCAAGAGGCAGGGGATGAGTGTGAGCCCGAGTGGTGTGATGC
CGAGGACCCACTCTTCATCCTGTACACCAGTGGCTCCACAGGCAAACCCAAGGGTGTGGT
TCACACAGTTGGGGGCTACATGCTCTATGTAGCCACAACCTTCAAGTATGTGTTTGACTT
CCATGCAGAGGATGTGTTCTGGTGCACGGCAGACATTGGTTGGATCACTGGTCATTCCTA
CGTCACCTATGGGCCACTGGCCAATGGTGCCACCAGTGTTTTGTTTGAGGGGATTCCCAC
ATATCCGGACGTGAACCGCCTGTGGAGCATTGTGGACAAATACAAGGTGACCAAGTTCTA
CACAGCACCCACAGCCATCCGTCTGCTCATGAAGTTTGGAGATGAGCCTGTCACCAAGCA
TAGCCGGGCATCCTTGCAGGTGTTAGGCACAGTGGGTGAACCCATCAACCCTGAGGCCTG
GCTATGGTACCACCGGGTGGTAGGTGCCCAGCGCTGCCCCATCGTGGACACCTTCTGGCA
AACAGAGACAGGTGGCCACATGTTGACTCCCCTTCCTGGTGCCACACCCATGAAACCCGG
TTCTGCTACTTTCCCATTCTTTGGTGTAGCTCCTGCAATCCTGAATGAGTCCGGGGAAGA
GTTGGAAGGTGAAGCTGAAGGTTATCTGGTGTTCAAGCAGCCCTGGCCAGGGATCATGCG
CACAGTCTATGGGAACCACGAACGCTTTGAGACAACCTACTTTAAGAAGTTTCCTGGATA
CTATGTTACAGGAGATGGCTGCCAGCGGGACCAGGATGGCTATTACTGGATCACTGGCAG
GATTGATGACATGCTCAATGTATCTGGACACCTGCTGAGTACAGCAGAGGTGGAGTCAGC
ACTTGTGGAACATGAGGCTGTTGCAGAGGCAGCTGTGGTGGGCCACCCTCATCCTGTGAA
GGGTGAATGCCTCTACTGCTTTGTCACCTTGTGTGATGGCCACACCTTCAGCCCCAAGCT
CACCGAGGAGCTCAAGAAGCAGATTAGAGAAAAGATTGGCCCCATTGCCACACCAGACTA
CATCCAGAATGCACCTGGCTTGCCTAAAACCCGCTCAGGGAAAATCATGAGGCGAGTGCT
TCGGAAGATTGCTCAGAATGACCATGACCTCGGGGACATGTCTACTGTGGCTGACCCATC
TGTCATCAGTCACCTCTTCAGCCACCGCTGCCTGACCATCCAGTGA

Enzyme 130 GenBank Gene ID

BC010141

Enzyme 130 GeneCard ID

ACSS2

Enzyme 130 GenAtlas ID

ACSS2

Enzyme 130 HGNC ID

HGNC:15814 Link Image

Enzyme 130 Chromosome Location

Enzyme 130 Locus

20q11.22

Enzyme 130 SNPs

SNPJam Report Link Image

Enzyme 130 General References

Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]

Enzyme 130 Metabolite References

Not Available

Enzyme 131 [top]

Enzyme 131 ID

13090

Enzyme 131 Name

cDNA FLJ76398, highly similar to Homo sapiens nudix

Enzyme 131 Synonyms

nucleoside diphosphate linked moiety X-type motif 5
NUDT5, mRNA
Nudix
Nucleoside diphosphate linked moiety X-type motif 5, isoform CRA_c

Enzyme 131 Gene Name

NUDT5

Enzyme 131 Protein Sequence

>cDNA FLJ76398, highly similar to Homo sapiens nudix

MESQEPTESSQNGKQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTTRKEQTAD
GVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFPAGLIDDGETPEAAALRELEEETGYK
GDIAECSPAVCMDPGLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPKNDLLQ
RLDALVAEEHLTVDARVYSYALALKHANAKPFEVPFLKF

Enzyme 131 Number of Residues

219

Enzyme 131 Molecular Weight

24328

Enzyme 131 Theoretical pI

4.59

Enzyme 131 GO Classification

Not Available

Enzyme 131 General Function

Replication, recombination and repair

Enzyme 131 Specific Function

Not Available

Enzyme 131 Pathways

Not Available

Enzyme 131 Reactions

Not Available

Enzyme 131 Pfam Domain Function

Not Available

Enzyme 131 Signals

None

Enzyme 131 Transmembrane Regions

None

Enzyme 131 Essentiality

Not Available

Enzyme 131 GenBank ID Protein

158255698

Enzyme 131 UniProtKB/Swiss-Prot ID

A8K516

Enzyme 131 UniProtKB/Swiss-Prot Entry Name

A8K516_HUMAN Link Image

Enzyme 131 PDB ID

Not Available

Enzyme 131 Cellular Location

Not Available

Enzyme 131 Gene Sequence

Not Available

Enzyme 131 GenBank Gene ID

AK291131

Enzyme 131 GeneCard ID

A8K516

Enzyme 131 GenAtlas ID

Not Available

Enzyme 131 HGNC ID

Not Available

Enzyme 131 Chromosome Location

Not Available

Enzyme 131 Locus

Not Available

Enzyme 131 SNPs

SNPJam Report Link Image

Enzyme 131 General References

Not Available

Enzyme 131 Metabolite References

Not Available

Enzyme 132 [top]

Enzyme 132 ID

13112

Enzyme 132 Name

cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase

Enzyme 132 Synonyms

PIP gene
3'(2', 5'-bisphosphate nucleotidase 1, isoform CRA_a

Enzyme 132 Gene Name

BPNT1

Enzyme 132 Protein Sequence

>cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase

MASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICS
SLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLD
GTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGF
QLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFAS
PGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPE
SIKNALVP

Enzyme 132 Number of Residues

308

Enzyme 132 Molecular Weight

33393

Enzyme 132 Theoretical pI

5.41

Enzyme 132 GO Classification

Not Available

Enzyme 132 General Function

Carbohydrate transport and metabolism

Enzyme 132 Specific Function

Not Available

Enzyme 132 Pathways

Not Available

Enzyme 132 Reactions

Not Available

Enzyme 132 Pfam Domain Function

Not Available

Enzyme 132 Signals

None

Enzyme 132 Transmembrane Regions

None

Enzyme 132 Essentiality

Not Available

Enzyme 132 GenBank ID Protein

158257318

Enzyme 132 UniProtKB/Swiss-Prot ID

A8K7C8

Enzyme 132 UniProtKB/Swiss-Prot Entry Name

A8K7C8_HUMAN Link Image

Enzyme 132 PDB ID

1JP4

Enzyme 132 PDB File

Show

Enzyme 132 3D Structure

Enzyme 132 Cellular Location

Not Available

Enzyme 132 Gene Sequence

Not Available

Enzyme 132 GenBank Gene ID

AK291943

Enzyme 132 GeneCard ID

A8K7C8

Enzyme 132 GenAtlas ID

Not Available

Enzyme 132 HGNC ID

Not Available

Enzyme 132 Chromosome Location

Not Available

Enzyme 132 Locus

Not Available

Enzyme 132 SNPs

SNPJam Report Link Image

Enzyme 132 General References

Not Available

Enzyme 132 Metabolite References

Not Available

Enzyme 133 [top]

Enzyme 133 ID

13126

Enzyme 133 Name

cDNA FLJ77250, highly similar to Homo sapiens isoleucine-tRNA synthetase

Enzyme 133 Synonyms

IARS, transcript variant short, mRNA
Isoleucine-tRNA synthetase, isoform CRA_e

Enzyme 133 Gene Name

IARS

Enzyme 133 Protein Sequence

>cDNA FLJ77250, highly similar to Homo sapiens isoleucine-tRNA synthetase

MLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHYGHIL
AGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEYNNQC
RAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMP
FSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAVCVNP
EMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYFLKCK
ENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASGCFTT
EVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWFVRVE
NMVDQLLRNNDLCYWVPELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFEEVVC
IGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYAQVHY
PFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLASDGQK
MSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAY
RFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRLYTVV
PRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELM
YQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKT
IPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMV
LGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATGGTAQ
FEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAKSEGT
YLNSVIESHTEFIFTTIKAPLKPYPVSPSDKVLIQEKTQLKGSELEITLTRGSSLPGPAC
AYVNLNICANGSEQGGVLLLENPKGDNRLDLLKLKSVVTSIFGVKNTELAVFHDETEIQN
QTDLLSLSGKTLCVTAGSAPSLINSSSTLLCQYINLQLLNAKPQECLMGTVGTLLLENPL
GQNGLTHQGLLYEAAKVFGLRSRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVLPTTA
DF

Enzyme 133 Number of Residues

1262

Enzyme 133 Molecular Weight

144500

Enzyme 133 Theoretical pI

6.03

Enzyme 133 GO Classification

Not Available

Enzyme 133 General Function

Translation, ribosomal structure and biogenesis

Enzyme 133 Specific Function

Not Available

Enzyme 133 Pathways

Not Available

Enzyme 133 Reactions

Not Available

Enzyme 133 Pfam Domain Function

Not Available

Enzyme 133 Signals

None

Enzyme 133 Transmembrane Regions

None

Enzyme 133 Essentiality

Not Available

Enzyme 133 GenBank ID Protein

158259489

Enzyme 133 UniProtKB/Swiss-Prot ID

A8KAE9

Enzyme 133 UniProtKB/Swiss-Prot Entry Name

A8KAE9_HUMAN Link Image

Enzyme 133 PDB ID

Not Available

Enzyme 133 Cellular Location

Not Available

Enzyme 133 Gene Sequence

Not Available

Enzyme 133 GenBank Gene ID

AK293014

Enzyme 133 GeneCard ID

A8KAE9

Enzyme 133 GenAtlas ID

Not Available

Enzyme 133 HGNC ID

Not Available

Enzyme 133 Chromosome Location

Not Available

Enzyme 133 Locus

Not Available

Enzyme 133 SNPs

SNPJam Report Link Image

Enzyme 133 General References

Not Available

Enzyme 133 Metabolite References

Not Available

Enzyme 134 [top]

Enzyme 134 ID

13127

Enzyme 134 Name

Valyl-tRNA synthetase, mitochondrial

Enzyme 134 Synonyms

Valine--tRNA ligase
ValRS
Valyl-tRNA synthetase-like

Enzyme 134 Gene Name

VARS2

Enzyme 134 Protein Sequence

>Valyl-tRNA synthetase, mitochondrial

MPHLPLASFRPPFWGLRHSRGLPRFHSVSTQSEPHGSPISRRNREAKQKRLREKQATLEA
EIAGESKSPAESIKAWRPKELVLYEIPTKPGEKKDVSGPLPPAYSPRYVEAAWYPWWVRE
GFFKPEYQARLPQATGETFSMCIPPPNVTGSLHIGHALTVAIQDALVRWHRMRGDQVLWV
PGSDHAGIATQAVVEKQLWKERGVRRHELSREAFLREVWQWKEAKGGEICEQLRALGASL
DWDRECFTMDVGSSVAVTEAFVRLYKAGLLYRNHQLVNWSCALRSAISDIEVENRPLPGH
TQLRLPGCPTPVSFGLLFSVAFPVDGEPDAEVVVGTTRPETLPGDVAVAVHPDDSRYTHL
HGRQLRHPLMGQPLPLITDYAVQPHVGTGAVKVTPAHSPADAEMGARHGLSPLNVIAEDG
TMTSLCGDWLQGLHRFVAREKIMSVLSEWGLFRGLQNHPMVLPICSRSGDVIEYLLKNQW
FVRCQEMGARAAKAVESGALELSPSFHQKNWQHWFSHIGDWCVSRQLWWGHQIPAYLVVE
DHAQGEEDCWVVGRSEAEAREVAAELTGRPGAELTLERDPDVLDTWFSSALFPFSALGWP
QETPDLARFYPLSLLETGSDLLLFWVGRMVMLGTQLTGQLPFSKVLLHPMVRDRQGRKMS
KSLGNVLDPRDIISGVEMQVLQEKLRSGNLDPAELAIVAAAQKKDFPHGIPECGTDALRF
TLCSHGVQAGDLHLSVSEVQSCRHFCNKIWNALRFILNALGEKFVPQPAEELSPSSPMDA
WILSRLALAAQECERGFLTRELSLVTHALHHFWLHNLCDVYLEAVKPVLWHSPRPLGPPQ
VLFSCADLGLRLLAPLMPFLAEELWQRLPPRPGCPPAPSISVAPYPSACSLEHWRQPELE
RRFSRVQEVVQVLRALRATYQLTKARPRVLLQSSEPGDQGLFEAFLEPLGTLGYCGAVGL
LPPGAAAPSGWAQAPLSDTAQVYMELQGLVDPQIQLPLLAARRYKLQKQLDSLTARTPSE
GEAGTQRQQKLSSLQLELSKLDKAASHLRQLMDEPPAPGSPEL

Enzyme 134 Number of Residues

1063

Enzyme 134 Molecular Weight

118488.8

Enzyme 134 Theoretical pI

7.02

Enzyme 134 GO Classification

Function
ATP binding adenyl nucleotide binding adenyl ribonucleotide binding aminoacyl-tRNA ligase activity binding catalytic activity ligase activity ligase activity, forming aminoacyl-tRNA and related compounds ligase activity, forming carbon-oxygen bonds nucleoside binding nucleotide binding purine nucleoside binding valine-tRNA ligase activity
Process
RNA metabolic process biosynthetic process cellular macromolecule biosynthetic process cellular macromolecule metabolic process macromolecule biosynthetic process macromolecule metabolic process metabolic process ncRNA metabolic process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolic process translation valyl-tRNA aminoacylation
Component
cell part cytoplasm intracellular part

Enzyme 134 General Function

Involved in nucleotide binding

Enzyme 134 Specific Function

ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)

Enzyme 134 Pathways

Not Available

Enzyme 134 Reactions

ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal [RN:R03665]

Enzyme 134 Pfam Domain Function

Anticodon_1 (PF08264 )
tRNA-synt_1 (PF00133 )

Enzyme 134 Signals

None

Enzyme 134 Transmembrane Regions

None

Enzyme 134 Essentiality

Not Available

Enzyme 134 GenBank ID Protein

268370293

Enzyme 134 UniProtKB/Swiss-Prot ID

Q5ST30

Enzyme 134 UniProtKB/Swiss-Prot Entry Name

SYVM_HUMAN Link Image

Enzyme 134 PDB ID

Not Available

Enzyme 134 Cellular Location

Not Available

Enzyme 134 Gene Sequence

>3192 bp

ATGCCTCATTTGCCTCTCGCCTCTTTTCGACCACCATTTTGGGGGCTGAGGCACTCACGG
GGCCTCCCCAGGTTTCACTCCGTTTCTACACAGTCGGAGCCCCATGGATCTCCCATCTCC
CGGAGGAACCGTGAAGCCAAACAGAAGCGCCTGCGAGAGAAGCAGGCGACTCTGGAGGCT
GAGATAGCAGGGGAGAGCAAGTCACCTGCAGAATCCATTAAGGCCTGGAGGCCTAAGGAG
TTAGTATTGTATGAAATCCCTACGAAACCCGGTGAAAAGAAAGATGTCTCTGGGCCCCTG
CCTCCTGCATACAGCCCCCGATATGTTGAGGCTGCCTGGTACCCGTGGTGGGTACGAGAG
GGCTTCTTCAAACCAGAATATCAGGCCCGGCTGCCCCAAGCTACAGGGGAGACCTTTTCC
ATGTGTATCCCACCTCCCAATGTCACTGGCTCCCTGCACATTGGCCACGCACTCACGGTG
GCCATACAGGATGCCCTCGTGCGCTGGCACCGGATGCGTGGGGATCAAGTGCTGTGGGTC
CCTGGTTCAGATCATGCAGGAATTGCTACACAAGCTGTGGTGGAGAAACAACTGTGGAAG
GAACGGGGAGTGAGGAGACATGAGCTGAGCCGGGAGGCCTTCCTTAGGGAGGTGTGGCAG
TGGAAGGAGGCGAAAGGTGGAGAGATCTGTGAGCAGCTGCGAGCTCTGGGTGCCTCCCTG
GACTGGGATCGAGAGTGTTTTACCATGGATGTTGGCTCCTCAGTGGCTGTGACTGAAGCT
TTTGTGCGGCTCTACAAGGCGGGGTTGCTGTACCGGAACCATCAGCTTGTCAACTGGTCA
TGTGCTTTAAGATCAGCCATCTCGGACATTGAGGTGGAGAACCGGCCCCTGCCTGGCCAC
ACACAGCTTCGACTGCCTGGCTGCCCCACCCCCGTGTCTTTTGGCCTCCTATTTTCTGTT
GCCTTCCCCGTGGATGGAGAGCCTGATGCAGAGGTTGTGGTAGGAACCACAAGGCCAGAG
ACGCTGCCTGGAGATGTGGCTGTGGCCGTTCATCCAGACGACTCGCGATACACACATCTA
CACGGGCGACAGCTTCGTCACCCCTTGATGGGGCAGCCTCTTCCCCTCATCACAGACTAT
GCTGTTCAGCCACATGTGGGCACGGGGGCAGTGAAGGTGACTCCAGCTCACAGTCCTGCC
GATGCTGAGATGGGGGCCCGACATGGCTTGAGCCCCTTGAATGTCATTGCGGAGGATGGG
ACCATGACCTCCCTCTGCGGGGACTGGCTGCAGGGTCTTCACCGGTTTGTGGCCCGGGAA
AAGATAATGTCTGTGCTGAGTGAATGGGGCCTGTTCCGGGGCCTCCAGAACCACCCCATG
GTACTGCCCATCTGCAGCCGTTCTGGGGATGTGATAGAATACCTGCTGAAGAACCAGTGG
TTTGTCCGCTGCCAGGAAATGGGGGCCCGAGCTGCCAAGGCTGTGGAGTCGGGGGCCCTG
GAGCTCAGTCCCTCCTTCCACCAGAAGAACTGGCAGCACTGGTTTTCCCATATTGGGGAC
TGGTGTGTCTCCCGGCAGCTGTGGTGGGGCCATCAGATTCCAGCCTACCTGGTTGTAGAG
GACCATGCGCAGGGAGAAGAGGACTGTTGGGTGGTTGGGCGGTCAGAGGCTGAGGCCAGA
GAGGTAGCAGCGGAACTGACAGGGAGGCCAGGGGCAGAGCTGACCCTGGAGAGGGATCCT
GATGTCCTAGACACATGGTTTTCTTCTGCCCTGTTCCCCTTTTCTGCCCTGGGCTGGCCC
CAAGAGACCCCAGACCTTGCTCGTTTCTACCCCCTGTCACTTTTGGAAACGGGCAGCGAC
CTTCTGCTGTTCTGGGTGGGCCGCATGGTCATGTTGGGGACCCAGCTCACAGGGCAGCTG
CCCTTCAGCAAGGTGCTTCTTCATCCCATGGTTCGGGACAGGCAGGGCCGGAAGATGAGC
AAGTCCCTGGGGAATGTGCTGGACCCAAGAGACATCATCAGTGGGGTGGAGATGCAGGTG
CTGCAGGAAAAGCTGAGAAGCGGAAATTTGGACCCTGCAGAGCTGGCCATTGTGGCTGCA
GCACAGAAAAAGGACTTTCCTCACGGGATCCCTGAGTGTGGGACAGATGCCCTGAGATTC
ACACTCTGCTCCCATGGAGTTCAGGCGGGCGACTTGCACCTGTCAGTCTCTGAGGTCCAG
AGCTGCCGACATTTCTGCAACAAGATCTGGAATGCTCTTCGCTTTATCCTCAATGCTTTA
GGGGAGAAATTTGTGCCACAGCCTGCTGAGGAGCTGTCTCCCTCCTCCCCGATGGATGCC
TGGATCCTGAGCCGCCTTGCCCTGGCTGCCCAGGAGTGTGAGCGGGGCTTCCTCACCCGA
GAGCTCTCGCTCGTCACTCATGCCCTGCACCACTTCTGGCTTCACAACCTCTGTGACGTC
TACCTGGAGGCTGTGAAGCCCGTGCTGTGGCACTCGCCCCGCCCCCTGGGGCCCCCTCAG
GTCCTGTTCTCCTGCGCTGACCTCGGCCTCCGCCTCCTGGCCCCACTGATGCCCTTCCTG
GCTGAAGAGCTCTGGCAGAGGCTGCCCCCCAGGCCTGGTTGCCCCCCTGCCCCCAGCATC
TCGGTTGCCCCCTACCCCAGCGCCTGCAGCTTGGAGCACTGGCGCCAGCCAGAGCTGGAG
CGGCGCTTCTCCCGGGTCCAAGAGGTCGTGCAGGTGCTAAGGGCTCTCCGAGCCACGTAC
CAGCTCACCAAAGCCCGGCCCCGAGTGCTGCTGCAGAGCTCAGAGCCTGGGGACCAGGGC
CTCTTCGAGGCCTTCTTGGAGCCCCTGGGCACCCTGGGCTACTGTGGGGCTGTGGGCCTG
TTACCCCCAGGCGCAGCAGCTCCCTCCGGCTGGGCCCAGGCTCCACTCAGTGACACGGCT
CAAGTCTACATGGAGCTGCAGGGCCTGGTGGACCCGCAGATCCAGCTACCTCTGTTAGCC
GCCCGAAGGTACAAGTTGCAGAAGCAGCTTGACAGCCTCACAGCCAGGACCCCATCAGAA
GGGGAGGCAGGGACTCAGAGGCAACAAAAGCTTTCTTCCCTCCAGCTGGAATTGTCAAAA
CTGGACAAGGCAGCCTCTCACCTCCGGCAGCTGATGGATGAGCCTCCAGCCCCAGGGAGC
CCGGAGCTCTAA

Enzyme 134 GenBank Gene ID

NM_020442.4 Link Image

Enzyme 134 GeneCard ID

VARS2

Enzyme 134 GenAtlas ID

VARS2

Enzyme 134 HGNC ID

HGNC:21642 Link Image

Enzyme 134 Chromosome Location

Enzyme 134 Locus

6p21.33

Enzyme 134 SNPs

SNPJam Report Link Image

Enzyme 134 General References

Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins. DNA Res. 2001 Aug 31;8(4):179-87. [PubMed ]
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spr

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Human Metabolome Database Version 2.5

Showing metabocard for Adenosine monophosphate (HMDB00045)