|
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 |
|
| Enzyme 1 Reactions |
- a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| 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  |
| 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  |
| Enzyme 1 GeneCard ID |
NT5C1B  |
| Enzyme 1 GenAtlas ID |
NT5C1B  |
| Enzyme 1 HGNC ID |
HGNC:17818  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
2p24.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| 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 |
|
| Enzyme 2 Reactions |
- a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| 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  |
| 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  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p34.3-p33 |
| Enzyme 2 SNPs |
SNPJam Report  |
| 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 |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| 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  |
| 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 |
1 |
| Enzyme 3 Locus |
17q25.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| 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 |
5236 |
| Enzyme 4 Name |
5'(3')-deoxyribonucleotidase, mitochondrial |
| Enzyme 4 Synonyms |
- 5',3'-nucleotidase, mitochondrial
- Deoxy-5'-nucleotidase 2
- dNT-2
|
| Enzyme 4 Gene Name |
NT5M |
| Enzyme 4 Protein Sequence |
>5'(3')-deoxyribonucleotidase, mitochondrial
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
|
| Enzyme 4 Number of Residues |
228 |
| Enzyme 4 Molecular Weight |
25861.5 |
| Enzyme 4 Theoretical pI |
8.12 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in phosphatase activity |
| Enzyme 4 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 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
Not Available |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9NPB1  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
NT5M_HUMAN  |
| Enzyme 4 PDB ID |
1Q92  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>687 bp
ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA
|
| Enzyme 4 GenBank Gene ID |
AF210652  |
| Enzyme 4 GeneCard ID |
NT5M  |
| Enzyme 4 GenAtlas ID |
NT5M  |
| Enzyme 4 HGNC ID |
HGNC:15769  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
17p11.2 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5237 |
| Enzyme 5 Name |
Cytosolic purine 5'-nucleotidase |
| Enzyme 5 Synonyms |
- Cytosolic 5'-nucleotidase II
|
| Enzyme 5 Gene Name |
NT5C2 |
| Enzyme 5 Protein Sequence |
>Cytosolic purine 5'-nucleotidase
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
PQEITHCHDEDDDEEEEEEEE
|
| Enzyme 5 Number of Residues |
561 |
| Enzyme 5 Molecular Weight |
64969.2 |
| Enzyme 5 Theoretical pI |
6.05 |
| Enzyme 5 GO Classification |
Not Available |
| Enzyme 5 General Function |
Involved in 5'-nucleotidase activity |
| Enzyme 5 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 5 Pathways |
|
| Enzyme 5 Reactions |
- a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
Not Available |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P49902  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
5NTC_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 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 5 GenBank Gene ID |
D38524  |
| Enzyme 5 GeneCard ID |
NT5C2  |
| Enzyme 5 GenAtlas ID |
NT5C2  |
| Enzyme 5 HGNC ID |
HGNC:8022  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
10q24.32 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 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 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5313 |
| Enzyme 6 Name |
Ectonucleoside triphosphate diphosphohydrolase 1 |
| Enzyme 6 Synonyms |
- NTPDase 1
- Ecto-ATP diphosphohydrolase 1
- Ecto-ATPDase 1
- Ecto-ATPase 1
- Ecto-apyrase
- Lymphoid cell activation antigen
- CD39 antigen
|
| Enzyme 6 Gene Name |
ENTPD1 |
| Enzyme 6 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
|
| Enzyme 6 Number of Residues |
510 |
| Enzyme 6 Molecular Weight |
57964.1 |
| Enzyme 6 Theoretical pI |
6.29 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in hydrolase activity |
| Enzyme 6 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 6 Pathways |
|
| Enzyme 6 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
45580700  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P49961  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
ENTP1_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 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 6 GenBank Gene ID |
NM_001776.5  |
| Enzyme 6 GeneCard ID |
ENTPD1  |
| Enzyme 6 GenAtlas ID |
ENTPD1  |
| Enzyme 6 HGNC ID |
HGNC:3363  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
10q24 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 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 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5314 |
| Enzyme 7 Name |
Soluble calcium-activated nucleotidase 1 |
| Enzyme 7 Synonyms |
- SCAN-1
- Apyrase homolog
- Putative MAPK-activating protein PM09
- Putative NF-kappa-B-activating protein 107
|
| Enzyme 7 Gene Name |
CANT1 |
| Enzyme 7 Protein Sequence |
>Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
|
| Enzyme 7 Number of Residues |
401 |
| Enzyme 7 Molecular Weight |
44839.2 |
| Enzyme 7 Theoretical pI |
5.98 |
| Enzyme 7 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 7 General Function |
Involved in calcium ion binding |
| Enzyme 7 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 7 Pathways |
|
| Enzyme 7 Reactions |
- a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
229577440  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q8WVQ1  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
CANT1_HUMAN  |
| Enzyme 7 PDB ID |
1S1D  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 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 7 GenBank Gene ID |
NM_001159772.1  |
| Enzyme 7 GeneCard ID |
CANT1  |
| Enzyme 7 GenAtlas ID |
CANT1  |
| Enzyme 7 HGNC ID |
HGNC:19721  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
17q25.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 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 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5318 |
| Enzyme 8 Name |
Ectonucleoside triphosphate diphosphohydrolase 3 |
| Enzyme 8 Synonyms |
- NTPDase 3
- CD39 antigen-like 3
- Ecto-ATP diphosphohydrolase 3
- Ecto-ATPDase 3
- Ecto-ATPase 3
- Ecto-apyrase 3
- HB6
|
| Enzyme 8 Gene Name |
ENTPD3 |
| Enzyme 8 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 3
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
|
| Enzyme 8 Number of Residues |
529 |
| Enzyme 8 Molecular Weight |
59104.8 |
| Enzyme 8 Theoretical pI |
6.40 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in hydrolase activity |
| Enzyme 8 Specific Function |
Has a threefold preference for the hydrolysis of ATP over ADP |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
13817037  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O75355  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
ENTP3_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 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 8 GenBank Gene ID |
AF034840  |
| Enzyme 8 GeneCard ID |
ENTPD3  |
| Enzyme 8 GenAtlas ID |
ENTPD3  |
| Enzyme 8 HGNC ID |
HGNC:3365  |
| Enzyme 8 Chromosome Location |
3 |
| Enzyme 8 Locus |
3p21.3 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5337 |
| Enzyme 9 Name |
Uridine-cytidine kinase 1 |
| Enzyme 9 Synonyms |
- UCK 1
- Cytidine monophosphokinase 1
- Uridine monophosphokinase 1
|
| Enzyme 9 Gene Name |
UCK1 |
| Enzyme 9 Protein Sequence |
>Uridine-cytidine kinase 1
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVRRGRDL
EQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGDICKWHR
GGSNGRSYKRTFSEPGDHPGMLTSGKRSHLESSSRPH
|
| Enzyme 9 Number of Residues |
277 |
| Enzyme 9 Molecular Weight |
31434.5 |
| Enzyme 9 Theoretical pI |
7.33 |
| Enzyme 9 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in ATP binding |
| Enzyme 9 Specific Function |
Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and N(4)-anisoylcytidine |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- ATP + uridine = ADP + UMP [RN:R00964]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
13899253  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q9HA47  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
UCK1_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>834 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGGTGAGCGGCGGCACTGCCAGCGGGAAGTCGACCGTGTGT
GAGAAGATCATGGAGTTGCTGGGACAGAACGAGGTGGAACAGCGGCAGCGGAAGGTGGTC
ATCCTGAGCCAGGACAGGTTCTACAAGGTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTG
AAAGGACAGTACAATTTTGACCATCCAGATGCCTTTGATAATGATTTGATGCACAGGACT
CTGAAGAACATCGTGGAGGGCAAAACGGTGGAGGTGCCGACCTATGATTTTGTGACACAC
TCAAGGTTACCAGAGACCACGGTGGTCTACCCTGCGGACGTGGTTCTGTTTGAGGGCATC
TTGGTGTTCTACAGCCAGGAGATCCGGGACATGTTCCACCTGCGCCTCTTCGTGGACACC
GACTCCGACGTCAGGCTGTCTCGAAGAGTTCTCCGGGACGTGCGCCGAGGGAGGGACCTG
GAGCAGATTCTGACGCAGTACACCACCTTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTG
CCGACAAAGAAGTATGCCGATGTGATCATCCCGCGAGGAGTGGACAATATGGTTGCCATC
AACCTGATCGTGCAGCACATCCAGGACATTCTGAATGGTGACATCTGCAAATGGCACCGA
GGAGGGTCCAATGGGCGGAGCTACAAGCGGACCTTTTCTGAGCCAGGGGACCACCCTGGG
ATGCTGACCTCTGGCAAACGGTCACATTTGGAGTCCAGCAGCAGACCCCACTGA
|
| Enzyme 9 GenBank Gene ID |
NM_031432.2  |
| Enzyme 9 GeneCard ID |
UCK1  |
| Enzyme 9 GenAtlas ID |
UCK1  |
| Enzyme 9 HGNC ID |
HGNC:14859  |
| Enzyme 9 Chromosome Location |
9 |
| Enzyme 9 Locus |
9q34.13 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [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
]
- 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
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5439 |
| Enzyme 10 Name |
CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase |
| Enzyme 10 Synonyms |
- Beta-galactoside alpha-2,3-sialyltransferase 3
- Alpha 2,3-ST 3
- Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase
- N-acetyllactosaminide alpha-2,3-sialyltransferase
- ST3Gal III
- ST3GalIII
- ST3N
- Sialyltransferase 6
|
| Enzyme 10 Gene Name |
ST3GAL3 |
| Enzyme 10 Protein Sequence |
>CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
MGLLVFVRNLLLALCLFLVLGFLYYSAWKLHLLQWEEDSNSVVLSFDSAGQTLGSEYDRL
GFLLNLDSKLPAELATKYANFSEGACKPGYASALMTAIFPRFSKPAPMFLDDSFRKWARI
REFVPPFGIKGQDNLIKAILSVTKEYRLTPALDSLRCRRCIIVGNGGVLANKSLGSRIDD
YDIVVRLNSAPVKGFEKDVGSKTTLRITYPEGAMQRPEQYERDSLFVLAGFKWQDFKWLK
YIVYKERVSASDGFWKSVATRVPKEPPEIRILNPYFIQEAAFTLIGLPFNNGLMGRGNIP
TLGSVAVTMALHGCDEVAVAGFGYDMSTPNAPLHYYETVRMAAIKESWTHNIQREKEFLR
KLVKARVITDLSSGI
|
| Enzyme 10 Number of Residues |
375 |
| Enzyme 10 Molecular Weight |
42170.5 |
| Enzyme 10 Theoretical pI |
9.31 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- sialyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid glycosylation
- protein modification process
|
| Component |
- cell part
- integral to Golgi membrane
- intrinsic to Golgi membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane part
|
|
| Enzyme 10 General Function |
Involved in sialyltransferase activity |
| Enzyme 10 Specific Function |
Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta- 1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- or NeuAc-alpha- 2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3- GalNAc |
| Enzyme 10 Pathways |
- Glycosphingolipid biosynthesis - lactoseries (map00601
)
- Keratan sulfate biosynthesis (map00533
)
|
| Enzyme 10 Reactions |
- CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-D- glucosaminyl-glycoprotein [RN:R04596]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
5454060  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q11203  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
SIAT6_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1128 bp
ATGGGACTCTTGGTATTTGTGCGCAATCTGCTGCTAGCCCTCTGCCTCTTTCTGGTACTG
GGATTTTTGTATTATTCTGCGTGGAAGCTACACTTACTCCAGTGGGAGGAGGACTCCAAT
TCAGTGGTTCTTTCCTTTGACTCCGCTGGACAAACACTAGGCTCAGAGTATGATCGGTTG
GGCTTCCTCCTGAATCTGGACTCTAAACTGCCTGCTGAATTAGCCACCAAGTACGCAAAC
TTTTCAGAGGGAGCTTGCAAGCCTGGCTATGCTTCAGCCTTGATGACGGCCATCTTCCCC
CGGTTCTCCAAGCCAGCACCCATGTTCCTGGATGACTCCTTTCGCAAGTGGGCTAGAATC
CGGGAGTTCGTGCCGCCTTTTGGGATCAAAGGTCAAGACAATCTGATCAAAGCCATCTTG
TCAGTCACCAAAGAGTACCGCCTGACCCCTGCCTTGGACAGCCTCCGCTGCCGCCGCTGC
ATCATCGTGGGCAATGGAGGCGTTCTTGCCAACAAGTCTCTGGGGTCACGAATTGACGAC
TATGACATTGTGGTGAGACTGAATTCAGCACCAGTGAAAGGCTTTGAGAAGGACGTGGGC
AGCAAAACGACACTGCGCATCACCTACCCCGAGGGCGCCATGCAGCGGCCTGAGCAGTAC
GAGCGCGATTCTCTCTTTGTCCTCGCCGGCTTCAAGTGGCAGGACTTTAAGTGGTTGAAA
TACATCGTCTACAAGGAGAGAGTGAGTGCATCGGATGGCTTCTGGAAATCTGTGGCCACT
CGAGTGCCCAAGGAGCCCCCTGAGATTCGAATCCTCAACCCATATTTCATCCAGGAGGCC
GCCTTCACCCTCATTGGCCTGCCCTTCAACAATGGCCTCATGGGCCGGGGGAACATCCCT
ACCCTTGGCAGTGTGGCAGTGACCATGGCACTACACGGCTGTGACGAGGTGGCAGTCGCA
GGATTTGGCTATGACATGAGCACACCCAACGCACCCCTGCACTACTATGAGACCGTTCGC
ATGGCAGCCATCAAAGAGTCCTGGACGCACAATATCCAGCGAGAGAAAGAGTTTCTGCGG
AAGCTGGTGAAAGCTCGCGTCATCACTGATCTAAGCAGTGGCATCTGA
|
| Enzyme 10 GenBank Gene ID |
NM_006279.2  |
| Enzyme 10 GeneCard ID |
ST3GAL3  |
| Enzyme 10 GenAtlas ID |
ST3GAL3  |
| Enzyme 10 HGNC ID |
HGNC:10866  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
1p34.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Kitagawa H, Paulson JC: Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase. Biochem Biophys Res Commun. 1993 Jul 15;194(1):375-82. [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 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5636 |
| Enzyme 11 Name |
N-acylneuraminate cytidylyltransferase |
| Enzyme 11 Synonyms |
- CMP-N-acetylneuraminic acid synthase
- CMP-NeuNAc synthase
|
| Enzyme 11 Gene Name |
CMAS |
| Enzyme 11 Protein Sequence |
>N-acylneuraminate cytidylyltransferase
MDSVEKGAATSVSNPRGRPSRGRPPKLQRNSRGGQGRGVEKPPHLAALILARGGSKGIPL
KNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSS
TSLDAIIEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRW
SEIQKGVREVTEPLNLNPAKRPRRQDWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEM
RAEHSVDIDVDIDWPIAEQRVLRYGYFGKEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEI
ISYDVKDAIGISLLKKSGIEVRLISERACSKQTLSSLKLDCKMEVSVSDKLAVVDEWRKE
MGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEH
ICLLMEKVNNSCQK
|
| Enzyme 11 Number of Residues |
434 |
| Enzyme 11 Molecular Weight |
48378.8 |
| Enzyme 11 Theoretical pI |
8.02 |
| Enzyme 11 GO Classification |
| Function |
| — |
| Process |
- lipid biosynthetic process
- lipid metabolic process
- lipopolysaccharide biosynthetic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in lipopolysaccharide biosynthetic process |
| Enzyme 11 Specific Function |
Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN) |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate [RN:R02599]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
8515843  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q8NFW8  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
NEUA_HUMAN  |
| Enzyme 11 PDB ID |
1QWJ  |
| Enzyme 11 PDB File |
Show |
| Enzyme 11 3D Structure |
|
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1305 bp
ATGGACTCGGTGGAGAAGGGGGCCGCCACCTCCGTCTCCAACCCGCGGGGGCGACCGTCC
CGGGGCCGGCCGCCGAAGCTGCAGCGCAACTCTCGCGGCGGCCAGGGCCGAGGTGTGGAG
AAGCCCCCGCACCTGGCAGCCCTAATTCTGGCCCGGGGAGGCAGCAAAGGCATCCCCCTG
AAGAACATTAAGCACCTGGCGGGGGTCCCGCTCATTGGCTGGGTCCTGCGTGCGGCCCTG
GATTCAGGGGCCTTCCAGAGTGTATGGGTTTCGACAGACCATGATGAAATTGAGAATGTG
GCCAAACAATTTGGTGCACAAGTTCATCGAAGAAGTTCTGAAGTTTCAAAAGACAGCTCT
ACCTCACTAGATGCCATCATAGAATTTCTTAATTATCATAATGAGGTTGACATTGTAGGA
AATATTCAAGCTACTTCTCCATGTTTACATCCTACTGATCTTCAAAAAGTTGCAGAAATG
ATTCGAGAAGAAGGATATGATTCTGTTTTCTCTGTTGTGAGACGCCATCAGTTTCGATGG
AGTGAAATTCAGAAAGGAGTTCGTGAAGTGACCGAACCTCTGAATTTAAATCCAGCTAAA
CGGCCTCGTCGACAAGACTGGGATGGAGAATTATATGAAAATGGCTCATTTTATTTTGCT
AAAAGACATTTGATAGAGATGGGTTACTTGCAGGGTGGAAAAATGGCATACTACGAAATG
CGAGCTGAACATAGTGTGGATATAGATGTGGATATTGATTGGCCTATTGCAGAGCAAAGA
GTATTAAGATATGGCTATTTTGGCAAAGAGAAGCTTAAGGAAATAAAACTTTTGGTTTGC
AATATTGATGGATGTCTCACCAATGGCCACATTTATGTATCAGGAGACCAAAAAGAAATA
ATATCTTATGATGTAAAAGATGCTATTGGGATAAGTTTATTAAAGAAAAGTGGTATTGAG
GTGAGGCTAATCTCAGAAAGGGCCTGTTCAAAGCAGACGCTGTCTTCTTTAAAACTGGAT
TGCAAAATGGAAGTCAGTGTATCAGACAAGCTAGCAGTTGTAGATGAATGGAGAAAAGAA
ATGGGCCTGTGCTGGAAAGAAGTGGCATATCTTGGAAATGAAGTGTCTGATGAAGAGTGC
TTGAAGAGAGTGGGCCTAAGTGGCGCTCCTGCTGATGCCTGTTCTACTGCCCAGAAGGCT
GTTGGATACATTTGCAAATGTAATGGTGGCCGTGGTGCCATCCGAGAATTTGCAGAGCAC
ATTTGCCTACTAATGGAAAAGGTTAATAATTCATGCCAAAAATAG
|
| Enzyme 11 GenBank Gene ID |
AF271388  |
| Enzyme 11 GeneCard ID |
CMAS  |
| Enzyme 11 GenAtlas ID |
CMAS  |
| Enzyme 11 HGNC ID |
HGNC:18290  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
12p12.1 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Lawrence SM, Huddleston KA, Tomiya N, Nguyen N, Lee YC, Vann WF, Coleman TA, Betenbaugh MJ: Cloning and expression of human sialic acid pathway genes to generate CMP-sialic acids in insect cells. Glycoconj J. 2001 Mar;18(3):205-13. [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
]
- 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 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6049 |
| Enzyme 12 Name |
Phosphatidylcholine:ceramide cholinephosphotransferase 2 |
| Enzyme 12 Synonyms |
- Sphingomyelin synthase 2
|
| Enzyme 12 Gene Name |
SGMS2 |
| Enzyme 12 Protein Sequence |
>Phosphatidylcholine:ceramide cholinephosphotransferase 2
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYI
QIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDY
IDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLP
VPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFI
KEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNL
KVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGED
NEKST
|
| Enzyme 12 Number of Residues |
365 |
| Enzyme 12 Molecular Weight |
42279.8 |
| Enzyme 12 Theoretical pI |
9.00 |
| Enzyme 12 GO Classification |
| Function |
|
| Process |
| — |
| Component |
|
|
| Enzyme 12 General Function |
Involved in catalytic activity |
| Enzyme 12 Specific Function |
Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Required for cell growth |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
- a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol [RN:R08969]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
- 80-100
128-148
159-179
206-226
248-268
275-295
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
Not Available |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q8NHU3  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
SMS2_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1098 bp
ATGGATATCATAGAGACAGCAAAACTTGAAGAACATTTGGAAAATCAACCCAGTGATCCT
ACGAACACTTATGCAAGACCCGCTGAACCTGTTGAAGAAGAAAACAAAAATGGCAATGGT
AAACCCAAGAGCTTATCCAGTGGGCTGCGAAAAGGCACCAAAAAGTACCCGGACTATATC
CAAATTGCTATGCCCACTGAATCAAGGAACAAATTTCCACTAGAGTGGTGGAAAACGGGC
ATTGCCTTCATATATGCAGTTTTCAACCTCGTCTTGACAACCGTCATGATCACAGTTGTA
CATGAGAGGGTCCCTCCCAAGGAGCTTAGCCCTCCACTCCCAGACAAGTTTTTTGATTAC
ATTGATAGGGTGAAATGGGCATTTTCTGTATCAGAAATAAATGGGATTATATTAGTTGGA
TTATGGATCACCCAGTGGCTGTTTCTGAGATACAAGTCAATAGTGGGACGCAGATTCTGT
TTTATTATTGGAACTTTATACCTGTATCGCTGCATTACAATGTATGTTACTACTCTACCT
GTGCCTGGAATGCATTTCCAGTGTGCTCCAAAGCTCAATGGAGACTCTCAGGCAAAAGTT
CAACGGATTCTACGATTGATTTCTGGTGGTGGATTGTCCATAACTGGATCACATATCTTA
TGTGGAGACTTCCTCTTCAGCGGTCACACGGTTACGCTGACACTGACTTATTTGTTCATC
AAAGAATATTCGCCTCGTCACTTCTGGTGGTATCATTTAATCTGCTGGCTGCTGAGTGCT
GCCGGGATCATCTGCATTCTTGTAGCACACGAACACTACACTATCGATGTGATCATTGCT
TATTATATCACAACACGACTGTTTTGGTGGTACCATTCAATGGCCAATGAAAAGAACTTG
AAGGTCTCTTCACAGACTAATTTCTTATCTCGAGCATGGTGGTTCCCCATCTTTTATTTT
TTTGAGAAAAATGTACAAGGCTCAATTCCTTGCTGCTTCTCCTGGCCGCTGTCTTGGCCT
CCTGGCTGCTTCAAATCATCATGCAAAAAGTATTCACGGGTTCAGAAGATTGGTGAAGAC
AATGAGAAATCGACCTGA
|
| Enzyme 12 GenBank Gene ID |
AF452717  |
| Enzyme 12 GeneCard ID |
SGMS2  |
| Enzyme 12 GenAtlas ID |
SGMS2  |
| Enzyme 12 HGNC ID |
HGNC:28395  |
| Enzyme 12 Chromosome Location |
4 |
| Enzyme 12 Locus |
4q25 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 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
]
- 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
]
- Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC: Identification of a family of animal sphingomyelin synthases. EMBO J. 2004 Jan 14;23(1):33-44. Epub 2003 Dec 18. [PubMed
]
- Dong J, Liu J, Lou B, Li Z, Ye X, Wu M, Jiang XC: Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice. J Lipid Res. 2006 Jun;47(6):1307-14. Epub 2006 Feb 28. [PubMed
]
- Tafesse FG, Huitema K, Hermansson M, van der Poel S, van den Dikkenberg J, Uphoff A, Somerharju P, Holthuis JC: Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells. J Biol Chem. 2007 Jun 15;282(24):17537-47. Epub 2007 Apr 22. [PubMed
]
- Tani M, Kuge O: Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes. Biochem Biophys Res Commun. 2009 Apr 10;381(3):328-32. Epub 2009 Feb 20. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6051 |
| Enzyme 13 Name |
Lactosylceramide alpha-2,3-sialyltransferase |
| Enzyme 13 Synonyms |
- CMP-NeuAc:lactosylceramide alpha-2,3-sialyltransferase
- Ganglioside GM3 synthase
- ST3Gal V
- ST3GalV
- Sialyltransferase 9
|
| Enzyme 13 Gene Name |
ST3GAL5 |
| Enzyme 13 Protein Sequence |
>Lactosylceramide alpha-2,3-sialyltransferase
MRTKAAGCAERRPLQPRTEAAAAPAGRAMPSEYTYVKLRSDCSRPSLQWYTRAQSKMRRP
SLLLKDILKCTLLVFGVWILYILKLNYTTEECDMKKMHYVDPDHVKRAQKYAQQVLQKEC
RPKFAKTSMALLFEHRYSVDLLPFVQKAPKDSEAESKYDPPFGFRKFSSKVQTLLELLPE
HDLPEHLKAKTCRRCVVIGSGGILHGLELGHTLNQFDVVIRLNSAPVEGYSEHVGNKTTI
RMTYPEGAPLSDLEYYSNDLFVAVLFKSVDFNWLQAMVKKETLPFWVRLFFWKQVAEKIP
LQPKHFRILNPVIIKETAFDILQYSEPQSRFWGRDKNVPTIGVIAVVLATHLCDEVSLAG
FGYDLNQPRTPLHYFDSQCMAAMNFQTMHNVTTETKFLLKLVKEGVVKDLSGGIDREF
|
| Enzyme 13 Number of Residues |
418 |
| Enzyme 13 Molecular Weight |
47989.4 |
| Enzyme 13 Theoretical pI |
9.32 |
| Enzyme 13 GO Classification |
| Function |
- catalytic activity
- sialyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid glycosylation
- protein modification process
|
| Component |
- cell part
- integral to Golgi membrane
- intrinsic to Golgi membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane part
|
|
| Enzyme 13 General Function |
Involved in sialyltransferase activity |
| Enzyme 13 Specific Function |
Catalyzes the formation of ganglioside GM3 (alpha-N- acetylneuraminyl-2,3-beta-D-galactosyl-1, 4-beta-D- glucosylceramide) |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-beta-D-glucosyl-(11)-ceramide = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D- glucosyl-(11)-ceramide [RN:R03488 R05937]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
109633044  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q9UNP4  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
SIAT9_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1257 bp
ATGCGGACGAAGGCGGCGGGCTGCGCGGAGCGGCGTCCCCTGCAGCCGCGGACCGAGGCA
GCGGCGGCACCTGCCGGCCGAGCAATGCCAAGTGAGTACACCTATGTGAAACTGAGAAGT
GATTGCTCGAGGCCTTCCCTGCAATGGTACACCCGAGCTCAAAGCAAGATGAGAAGGCCC
AGCTTGTTATTAAAAGACATCCTCAAATGTACATTGCTTGTGTTTGGAGTGTGGATCCTT
TATATCCTCAAGTTAAATTATACTACTGAAGAATGTGACATGAAAAAAATGCATTATGTG
GACCCTGACCATGTAAAGAGAGCTCAGAAATATGCTCAGCAAGTCTTGCAGAAGGAATGT
CGTCCCAAGTTTGCCAAGACATCAATGGCGCTGTTATTTGAGCACAGGTATAGCGTGGAC
TTACTCCCTTTTGTGCAGAAGGCCCCCAAAGACAGTGAAGCTGAGTCCAAGTACGATCCT
CCTTTTGGGTTCCGGAAGTTCTCCAGTAAAGTCCAGACCCTCTTGGAACTCTTGCCAGAG
CACGACCTCCCTGAACACTTGAAAGCCAAGACCTGTCGGCGCTGTGTGGTTATTGGAAGC
GGAGGAATACTGCACGGATTAGAACTGGGCCACACCCTGAACCAGTTCGATGTTGTGATA
AGGTTAAACAGTGCACCAGTTGAGGGATATTCAGAACATGTTGGAAATAAAACTACTATA
AGGATGACTTATCCAGAGGGCGCACCACTGTCTGACCTTGAATATTATTCCAATGACTTA
TTTGTTGCTGTTTTATTTAAGAGTGTTGATTTCAACTGGCTTCAAGCAATGGTAAAAAAG
GAAACCCTGCCATTCTGGGTACGACTCTTCTTTTGGAAGCAGGTGGCAGAAAAAATCCCA
CTGCAGCCAAAACATTTCAGGATTTTGAATCCAGTTATCATCAAAGAGACTGCCTTTGAC
ATCCTTCAGTACTCAGAGCCTCAGTCAAGGTTCTGGGGCCGAGATAAGAACGTCCCCACA
ATCGGTGTCATTGCCGTTGTCTTAGCCACACATCTGTGCGATGAAGTCAGTTTGGCGGGT
TTTGGATATGACCTCAATCAACCCAGAACACCTTTGCACTACTTCGACAGTCAATGCATG
GCTGCTATGAACTTTCAGACCATGCATAATGTGACAACGGAAACCAAGTTCCTCTTAAAG
CTGGTCAAAGAGGGAGTGGTGAAAGATCTCAGTGGAGGCATTGATCGTGAATTTTGA
|
| Enzyme 13 GenBank Gene ID |
NM_003896.3  |
| Enzyme 13 GeneCard ID |
ST3GAL5  |
| Enzyme 13 GenAtlas ID |
ST3GAL5  |
| Enzyme 13 HGNC ID |
HGNC:10872  |
| Enzyme 13 Chromosome Location |
2 |
| Enzyme 13 Locus |
2p11.2 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Ishii A, Ohta M, Watanabe Y, Matsuda K, Ishiyama K, Sakoe K, Nakamura M, Inokuchi J, Sanai Y, Saito M: Expression cloning and functional characterization of human cDNA for ganglioside GM3 synthase. J Biol Chem. 1998 Nov 27;273(48):31652-5. [PubMed
]
- Berselli P, Zava S, Sottocornola E, Milani S, Berra B, Colombo I: Human GM3 synthase: a new mRNA variant encodes an NH2-terminal extended form of the protein. Biochim Biophys Acta. 2006 Jul;1759(7):348-58. Epub 2006 Jul 21. [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
]
- 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
]
- Simpson MA, Cross H, Proukakis C, Priestman DA, Neville DC, Reinkensmeier G, Wang H, Wiznitzer M, Gurtz K, Verganelaki A, Pryde A, Patton MA, Dwek RA, Butters TD, Platt FM, Crosby AH: Infantile-onset symptomatic epilepsy syndrome caused by a homozygous loss-of-function mutation of GM3 synthase. Nat Genet. 2004 Nov;36(11):1225-9. Epub 2004 Oct 24. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6052 |
| Enzyme 14 Name |
Type 2 lactosamine alpha-2,3-sialyltransferase |
| Enzyme 14 Synonyms |
- CMP-NeuAc:beta-galactoside alpha-2,3-sialyltransferase VI
- ST3Gal VI
- ST3GalVI
- Sialyltransferase 10
|
| Enzyme 14 Gene Name |
ST3GAL6 |
| Enzyme 14 Protein Sequence |
>Type 2 lactosamine alpha-2,3-sialyltransferase
MRGYLVAIFLSAVFLYYVLHCILWGTNVYWVAPVEMKRRNKIQPCLSKPAFASLLRFHQF
HPFLCAADFRKIASLYGSDKFDLPYGMRTSAEYFRLALSKLQSCDLFDEFDNIPCKKCVV
VGNGGVLKNKTLGEKIDSYDVIIRMNNGPVLGHEEEVGRRTTFRLFYPESVFSDPIHNDP
NTTVILTAFKPHDLRWLLELLMGDKINTNGFWKKPALNLIYKPYQIRILDPFIIRTAAYE
LLHFPKVFPKNQKPKHPTTGIIAITLAFYICHEVHLAGFKYNFSDLKSPLHYYGNATMSL
MNKNAYHNVTAEQLFLKDIIEKNLVINLTQD
|
| Enzyme 14 Number of Residues |
331 |
| Enzyme 14 Molecular Weight |
38213.3 |
| Enzyme 14 Theoretical pI |
9.30 |
| Enzyme 14 GO Classification |
| Function |
- catalytic activity
- sialyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid glycosylation
- protein modification process
|
| Component |
- cell part
- integral to Golgi membrane
- intrinsic to Golgi membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane part
|
|
| Enzyme 14 General Function |
Involved in sialyltransferase activity |
| Enzyme 14 Specific Function |
Involved in the synthesis of sialyl-paragloboside, a precursor of sialyl-Lewis X determinant. Has a alpha-2,3- sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on glycoproteins and glycolipids. Has a restricted substrate specificity, it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and neolactotetraosylceramide and neolactohexaosylceramide, but not lactotetraosylceramide, lactosylceramide or asialo-GM1 |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
Not Available |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q9Y274  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
SIA10_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>996 bp
ATGAGAGGGTATCTTGTGGCCATATTCCTGAGTGCTGTCTTCCTCTATTATGTACTGCAT
TGCATATTATGGGGAACGAATGTCTATTGGGTGGCACCTGTGGAAATGAAACGGAGAAAT
AAGATCCAGCCTTGTTTATCAAAGCCAGCTTTTGCCTCTCTGCTGAGGTTTCATCAGTTT
CACCCTTTTCTGTGTGCGGCTGATTTTAGAAAGATTGCTTCCTTGTATGGTAGCGATAAG
TTTGATTTGCCCTATGGGATGAGAACATCAGCGGAATATTTTCGACTTGCTCTTTCAAAA
CTGCAGAGTTGTGATCTCTTTGATGAGTTTGACAACATACCCTGTAAAAAGTGTGTGGTG
GTTGGTAATGGAGGAGTTTTGAAGAATAAGACATTAGGAGAAAAAATCGACTCCTATGAT
GTAATAATAAGAATGAATAATGGTCCTGTTTTAGGACATGAAGAAGAAGTTGGGAGAAGG
ACAACCTTCCGACTTTTTTATCCAGAATCTGTTTTTTCAGATCCTATTCACAATGACCCT
AATACGACAGTGATTCTCACTGCTTTTAAGCCACATGATTTAAGGTGGCTGTTGGAATTG
TTGATGGGTGACAAAATAAACACTAATGGTTTTTGGAAGAAACCAGCCTTAAACCTGATT
TATAAACCTTATCAAATCCGAATATTAGATCCTTTCATTATCAGAACAGCAGCTTATGAA
CTGCTTCATTTTCCAAAAGTGTTTCCCAAAAATCAGAAACCTAAACACCCAACAACAGGA
ATTATTGCCATCACATTGGCGTTTTACATATGTCACGAAGTTCACCTAGCTGGTTTTAAA
TACAACTTTTCTGACCTCAAGAGTCCTTTGCACTACTATGGGAATGCCACCATGTCTTTG
ATGAATAAGAACGCGTATCACAATGTGACTGCAGAGCAGCTCTTTTTGAAGGACATTATA
GAAAAAAACCTCGTAATCAACTTGACTCAAGATTGA
|
| Enzyme 14 GenBank Gene ID |
AB022918  |
| Enzyme 14 GeneCard ID |
ST3GAL6  |
| Enzyme 14 GenAtlas ID |
ST3GAL6  |
| Enzyme 14 HGNC ID |
HGNC:18080  |
| Enzyme 14 Chromosome Location |
3 |
| Enzyme 14 Locus |
3q12.1 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Okajima T, Fukumoto S, Miyazaki H, Ishida H, Kiso M, Furukawa K, Urano T, Furukawa K: Molecular cloning of a novel alpha2,3-sialyltransferase (ST3Gal VI) that sialylates type II lactosamine structures on glycoproteins and glycolipids. J Biol Chem. 1999 Apr 23;274(17):11479-86. [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
]
- 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 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6054 |
| Enzyme 15 Name |
Phosphatidylcholine:ceramide cholinephosphotransferase 1 |
| Enzyme 15 Synonyms |
- Medulla oblongata-derived protein
- Protein Mob
- Sphingomyelin synthase 1
- Transmembrane protein 23
|
| Enzyme 15 Gene Name |
SGMS1 |
| Enzyme 15 Protein Sequence |
>Phosphatidylcholine:ceramide cholinephosphotransferase 1
MLSASTMKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLCRVSS
DNGQRLLDMIETLKMEHHLEAHKNGHANGHLNIGVDIPTPDGSFSIKIKPNGMPNGYRKE
MIKIPMPELERSQYPMEWGKTFLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFF
DHFNRVQWAFSICEINGMILVGLWLIQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTT
LPVPGMHFNCSPKLFGDWEAQLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYL
FIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQ
VLKEASQMNLLARVWWYRPFQYFEKNVQGIVPRSYHWPFPWPVVHLSRQVKYSRLVNDT
|
| Enzyme 15 Number of Residues |
419 |
| Enzyme 15 Molecular Weight |
49207.3 |
| Enzyme 15 Theoretical pI |
8.51 |
| Enzyme 15 GO Classification |
| Function |
|
| Process |
| — |
| Component |
|
|
| Enzyme 15 General Function |
Involved in catalytic activity |
| Enzyme 15 Specific Function |
Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Suppresses BAX-mediated apoptosis and also prevents cell death in response to stimuli such as hydrogen peroxide, osmotic stress, elevated temperature and exogenously supplied sphingolipids. May protect against cell death by reversing the stress-inducible increase in levels of proapoptotic ceramide. Required for cell growth |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
- a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol [RN:R08969]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
- 142-162
190-210
221-241
282-302
310-330
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
29789379  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q86VZ5  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
SMS1_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1242 bp
ATGAAGGAAGTGGTTTATTGGTCACCCAAGAAGGTGGCAGACTGGCTGCTGGAGAATGCT
ATGCCAGAATACTGTGAGCCTCTGGAGCATTTCACAGGCCAGGACTTGATCAACCTAACC
CAAGAGGATTTCAAAAAACCCCCCTTGTGCCGAGTCTCCTCTGACAATGGGCAGCGGCTC
CTGGACATGATAGAAACCCTGAAAATGGAGCACCATTTGGAAGCACACAAGAACGGCCAT
GCCAATGGGCACCTCAACATTGGCGTAGACATCCCCACCCCCGACGGCAGCTTCAGCATC
AAGATTAAACCCAACGGGATGCCAAATGGGTATAGGAAAGAGATGATAAAGATCCCCATG
CCAGAACTGGAGCGCTCTCAGTACCCCATGGAGTGGGGCAAGACTTTTCTGGCCTTTCTT
TATGCACTTTCCTGTTTCGTTCTCACCACAGTGATGATCTCGGTCGTCCACGAACGAGTA
CCTCCTAAGGAGGTGCAGCCTCCACTACCGGACACATTTTTTGACCATTTTAACCGGGTG
CAGTGGGCCTTTTCTATTTGTGAAATTAATGGCATGATCCTTGTAGGACTCTGGTTAATT
CAGTGGCTGCTCTTAAAATACAAGTCTATTATTAGCAGAAGATTTTTCTGCATAGTTGGC
ACGCTGTACCTGTATCGGTGTATTACAATGTATGTAACTACACTCCCAGTACCTGGTATG
CATTTCAACTGTTCTCCGAAGCTTTTCGGAGACTGGGAAGCCCAACTGCGAAGAATAATG
AAGCTCATTGCTGGAGGTGGCTTGTCTATCACTGGCTCTCACAACATGTGTGGGGACTAT
CTGTACAGCGGCCACACGGTCATGCTAACACTTACCTACTTATTTATCAAAGAGTATTCC
CCTCGGCGACTCTGGTGGTATCACTGGATTTGCTGGCTTCTCAGCGTAGTTGGAATCTTC
TGTATTCTCTTAGCGCATGACCACTACACTGTGGACGTGGTGGTGGCATATTACATCACC
ACGAGACTCTTCTGGTGGTATCACACTATGGCCAATCAGCAAGTGCTAAAGGAAGCTTCC
CAGATGAACCTCCTGGCCAGGGTGTGGTGGTACAGGCCATTTCAGTACTTTGAAAAGAAT
GTCCAAGGAATTGTACCTCGATCTTACCATTGGCCTTTCCCCTGGCCAGTAGTCCACCTC
AGTAGGCAAGTTAAATACAGCCGGCTGGTGAATGACACATAA
|
| Enzyme 15 GenBank Gene ID |
Not Available |
| Enzyme 15 GeneCard ID |
SGMS1  |
| Enzyme 15 GenAtlas ID |
SGMS1  |
| Enzyme 15 HGNC ID |
HGNC:29799  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
10q11.2 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Yamaoka S, Miyaji M, Kitano T, Umehara H, Okazaki T: Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells. J Biol Chem. 2004 Apr 30;279(18):18688-93. Epub 2004 Feb 19. [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
]
- Vladychenskaya IP, Dergunova LV, Dmitrieva VG, Limborska SA: Human gene MOB: structure specification and aspects of transcriptional activity. Gene. 2004 Sep 1;338(2):257-65. [PubMed
]
- Vladychenskaya IP, Dergunova LV, Limborska SA: In vitro and in silico analysis of the predicted human MOB gene encoding a phylogenetically conserved transmembrane protein. Biomol Eng. 2002 Feb;18(6):263-8. [PubMed
]
- Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC: Identification of a family of animal sphingomyelin synthases. EMBO J. 2004 Jan 14;23(1):33-44. Epub 2003 Dec 18. [PubMed
]
- Dong J, Liu J, Lou B, Li Z, Ye X, Wu M, Jiang XC: Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice. J Lipid Res. 2006 Jun;47(6):1307-14. Epub 2006 Feb 28. [PubMed
]
- Tafesse FG, Huitema K, Hermansson M, van der Poel S, van den Dikkenberg J, Uphoff A, Somerharju P, Holthuis JC: Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells. J Biol Chem. 2007 Jun 15;282(24):17537-47. Epub 2007 Apr 22. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
7696 |
| Enzyme 16 Name |
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 |
| Enzyme 16 Synonyms |
- Alpha 2,3-ST 1
- Beta-galactoside alpha-2,3-sialyltransferase 1
- Gal-NAc6S
- Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase
- SIATFL
- ST3Gal I
- ST3GalI
- ST3GalA.1
- ST3O
- Sialyltransferase 4A
- SIAT4-A
|
| Enzyme 16 Gene Name |
ST3GAL1 |
| Enzyme 16 Protein Sequence |
>CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
MVTLRKRTLKVLTFLVLFIFLTSFFLNYSHTMVATTWFPKQMVLELSENLKRLIKHRPCT
CTHCIGQRKLSAWFDERFNQTMQPLLTAQNALLEDDTYRWWLRLQREKKPNNLNDTIKEL
FRVVPGNVDPMLEKRSVGCRRCAVVGNSGNLRESSYGPEIDSHDFVLRMNKAPTAGFEAD
VGTKTTHHLVYPESFRELGDNVSMILVPFKTIDLEWVVSAITTGTISHTYIPVPAKIRVK
QDKILIYHPAFIKYVFDNWLQGHGRYPSTGILSVIFSMHVCDEVDLYGFGADSKGNWHHY
WENNPSAGAFRKTGVHDADFESNVTATLASINKIRIFKGR
|
| Enzyme 16 Number of Residues |
340 |
| Enzyme 16 Molecular Weight |
39074.7 |
| Enzyme 16 Theoretical pI |
9.45 |
| Enzyme 16 GO Classification |
| Function |
- catalytic activity
- sialyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid glycosylation
- protein modification process
|
| Component |
- cell part
- integral to Golgi membrane
- intrinsic to Golgi membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane part
|
|
| Enzyme 16 General Function |
Involved in beta-galactoside alpha-2,3-sialyltransferas |
| Enzyme 16 Specific Function |
It may be responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found on sugar chains O- linked to Thr or Ser and also as a terminal sequence on certain gangliosides. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- CMP-N-acetylneuraminate + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl- alpha-D-galactosaminyl-R [RN:R04590 R05913]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
3169564  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q11201  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
SIA4A_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1023 bp
ATGGTGACCCTGCGGAAGAGGACCCTGAAAGTGCTCACCTTCCTCGTGCTCTTCATCTTC
CTCACCTCCTTCTTCCTGAACTACTCCCACACCATGGTGGCCACCACCTGGTTCCCCAAG
CAGATGGTCCTGGAGCTCTCCGAGAACCTGAAGAGACTGATCAAGCACAGGCCTTGCACC
TGCACCCACTGCATCGGGCAGCGCAAGCTCTCGGCCTGGTTCGATGAGAGGTTCAACCAG
ACCATGCAGCCGCTCGTGACCGCCCAGAACGCGCTCTTGGAGGACGACACCTACCGATGG
TGGCTGAGGCTCCAGCGGGAGAAGAAGCCCAATAACTTGAATGACACCATCAAGGAGCTG
TTCAGAGTGGTGCCTGGGAATGTGGACCCTATGCTGGAGAAGAGGTCGGTGGGCTGCCGG
CGCTGCGCTGTGGTGGGCAACTCGGGCAACCTGAGGGAGTCTTCTTATGGGCCTGAGATA
GACAGTCACGACTTTGTCCTCAGGATGAACAAGGCGCCCACGGCAGGGTTTGAAGCTGAT
GTTGGGACCAAGACCACCCACCATCTGGTGTACCCTGAGAGCTTCCGGGAGCTGGGAGAT
AATGTCAGCATGATCCTGGTGCCCTTCAAGACCATCGACTTGGAGTGGGTGGTGAGGGCC
ATCACCACGGGCACCATTTCCCACACCTACATCCCGGTTCCTGCAAAGATCAGAGTGAAA
CAGGATAAGATCCTGATCTACCACCCAGCCTTCATCAAGTATGTCTTTGACAACTGGCTG
CAAGGGCACGGGCGATACCCATCTACCGGCATCCTCTCAGTCATCTTCTCAATGCATGTC
TGCGATGAGGTGGACTTGTACGGCTTCGGGGCAGACAGCAAAGGGAACTGGCACCACTAC
TGGGAGAACAACCCATCCGCGGGGGCTTTTCGCAAGACGGGGGTGCACGATGCAGACTTT
GAGTCTAACGTGACGGCCACCTTGGCCTCCATCAATAAAATCCGGATCTTCAAGGGGAGA
TGA
|
| Enzyme 16 GenBank Gene ID |
AF059321  |
| Enzyme 16 GeneCard ID |
ST3GAL1  |
| Enzyme 16 GenAtlas ID |
Not Available |
| Enzyme 16 HGNC ID |
Not Available |
| Enzyme 16 Chromosome Location |
8 |
| Enzyme 16 Locus |
8q24.22 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Kitagawa H, Paulson JC: Differential expression of five sialyltransferase genes in human tissues. J Biol Chem. 1994 Jul 8;269(27):17872-8. [PubMed
]
- Chang ML, Eddy RL, Shows TB, Lau JT: Three genes that encode human beta-galactoside alpha 2,3-sialyltransferases. Structural analysis and chromosomal mapping studies. Glycobiology. 1995 May;5(3):319-25. [PubMed
]
- Shang J, Qiu R, Wang J, Liu J, Zhou R, Ding H, Yang S, Zhang S, Jin C: Molecular cloning and expression of Galbeta1,3GalNAc alpha2, 3-sialyltransferase from human fetal liver. Eur J Biochem. 1999 Oct;265(2):580-8. [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
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
8075 |
| Enzyme 17 Name |
Uridine-cytidine kinase 2 |
| Enzyme 17 Synonyms |
- UCK 2
- Cytidine monophosphokinase 2
- Testis-specific protein TSA903
- Uridine monophosphokinase 2
|
| Enzyme 17 Gene Name |
UCK2 |
| Enzyme 17 Protein Sequence |
>Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
|
| Enzyme 17 Number of Residues |
261 |
| Enzyme 17 Molecular Weight |
29298.9 |
| Enzyme 17 Theoretical pI |
6.68 |
| Enzyme 17 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 17 General Function |
Involved in ATP binding |
| Enzyme 17 Specific Function |
Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and N(4)-anisoylcytidine |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- ATP + uridine = ADP + UMP [RN:R00964]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
18699734  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q9BZX2  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
UCK2_HUMAN  |
| Enzyme 17 PDB ID |
1XRJ  |
| Enzyme 17 PDB File |
Show |
| Enzyme 17 3D Structure |
|
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>786 bp
ATGGCCGGGGACAGCGAGCAGACCCTGCAGAACCACCAGCAGCCCAACGGCGGCGAGCCC
TTCCTTATAGGCGTCAGCGGGGGAACAGCTAGCGGCAAGTCTTCCGTGTGTGCTAAGATC
GTGCAGCTCCTGGGGCAGAATGAGGTGGACTATCGCCAGAAGCAGGTGGTCATCCTGAGC
CAGGATAGCTTCTACCGTGTCCTTACCTCGGAGCAGAAGGCCAAAGCCCTGAAGGGCCAG
TTCAACTTTGACCACCCGGATGCCTTTGACAATGAACTCATTCTCAAAACACTCAAAGAA
ATCACTGAAGGGAAAACAGTCCAGATCCCCGTGTATGACTTTGTCTCCCATTCCCGGAAG
GAGGAGACAGTTACTGTCTATCCCGCAGACGTGGTGCTCTTTGAAGGGATCCTGGCCTTC
TACTCCCAGGAGGTACGAGACCTGTTCCAGATGAAGCTTTTTGTGGATACAGATGCGGAC
ACCCGGCTCTCACGCAGAGTATTAAGGGACATCAGCGAGAGAGGCAGGGATCTTGAGCAG
ATTTTATCTCAGTACATTACGTTCGTCAAGCCTGCCTTTGAGGAATTCTGCTTGCCAACA
AAGAAGTATGCTGATGTGATCATCCCTAGAGGTGCAGATAATCTGGTGGCCATCAACCTC
ATCGTGCAGCACATCCAGGACATCCTGAATGGAGGGCCCTCCAAACGGCAGACCAATGGC
TGTCTCAACGGCTACACCCCTTCACGCAAGAGGCAGGCATCGGAGTCCAGCAGCAGGCCG
CATTGA
|
| Enzyme 17 GenBank Gene ID |
NM_012474.3  |
| Enzyme 17 GeneCard ID |
UCK2  |
| Enzyme 17 GenAtlas ID |
UCK2  |
| Enzyme 17 HGNC ID |
HGNC:12562  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
1q23 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Ozaki K, Kuroki T, Hayashi S, Nakamura Y: Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method. Genomics. 1996 Sep 1;36(2):316-9. [PubMed
]
- Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [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
]
- Koizumi K, Shimamoto Y, Azuma A, Wataya Y, Matsuda A, Sasaki T, Fukushima M: Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells. Int J Mol Med. 2001 Sep;8(3):273-8. [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
]
- Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F: Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase. Structure. 2004 May;12(5):751-64. [PubMed
]
- Appleby TC, Larson G, Cheney IW, Walker H, Wu JZ, Zhong W, Hong Z, Yao N: Structure of human uridine-cytidine kinase 2 determined by SIRAS using a rotating-anode X-ray generator and a single samarium derivative. Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):278-84. Epub 2005 Feb 24. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
8362 |
| Enzyme 18 Name |
Cholinephosphotransferase 1 |
| Enzyme 18 Synonyms |
- hCPT1
- AAPT1-like protein
- Diacylglycerol cholinephosphotransferase 1
|
| Enzyme 18 Gene Name |
CHPT1 |
| Enzyme 18 Protein Sequence |
>Cholinephosphotransferase 1
MAAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLW
MAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARR
TNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYV
SGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSC
SNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILM
FGCVFAKVSQKLVVAHMTKSELYLQDTVFLGPGLLFLDQYFNNFIDEYVVLWMAMVISSF
DMVIYFSALCLQISRHLHLNIFKTACHQAPEQVQVLSSKSHQNNMD
|
| Enzyme 18 Number of Residues |
406 |
| Enzyme 18 Molecular Weight |
45096.5 |
| Enzyme 18 Theoretical pI |
6.92 |
| Enzyme 18 GO Classification |
| Function |
- catalytic activity
- phosphotransferase activity, for other substituted phosphate groups
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
|
|
| Enzyme 18 General Function |
Involved in phosphotransferase activity, for other substituted phosphate groups |
| Enzyme 18 Specific Function |
Catalyzes phosphatidylcholine biosynthesis from CDP- choline. It thereby plays a central role in the formation and maintenance of vesicular membranes |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
- CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine [RN:R01321]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
- 66-86
93-113
153-173
193-213
226-248
261-281
295-315
349-369
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
50726996  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q8WUD6  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
CHPT1_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1221 bp
ATGGCGGCAGGCGCCGGGGCCGGGTCCGCGCCGCGCTGGCTGAGGGCGCTGAGCGAGCCG
CTGAGCGCGGCGCAGCTGCGGCGACTGGAGGAGCACCGCTACAGCGCGGCGGGCGTCTCG
CTGCTCGAGCCGCCGCTGCAGCTCTACTGGACCTGGCTGCTCCAGTGGATCCCGCTCTGG
ATGGCCCCCAACTCCATCACCCTGCTGGGGCTCGCCGTCAACGTGGTCACCACGCTCGTG
CTCATCTCCTACTGTCCCACGGCCACCGAAGAGGCACCATACTGGACATACCTTTTATGT
GCACTGGGACTTTTTATTTACCAGTCACTGGATGCTATTGATGGGAAACAAGCCAGAAGA
ACAAACTCTTGTTCCCCTTTAGGGGAGCTCTTTGACCATGGCTGTGACTCTCTTTCCACA
GTATTTATGGCAGTGGGAGCTTCAATTGCCGCTCGCTTAGGAACTTATCCTGACTGGTTT
TTTTTCTGCTCTTTTATTGGGATGTTTGTGTTTTATTGCGCTCATTGGCAGACTTATGTT
TCAGGCATGTTGAGATTTGGAAAAGTGGATGTAACTGAAATTCAGATAGCTTTAGTGATT
GTCTTTGTGTTGTCTGCATTTGGAGGAGCAACAATGTGGGACTATACGATTCCTATTCTA
GAAATAAAATTGAAGATCCTTCCAGTTCTTGGATTTCTAGGTGGAGTAATATTTTCCTGT
TCAAATTATTTCCATGTTATCCTCCATGGTGGTGTTGGCAAGAATGGATCCACTATAGCA
GGCACCAGTGTCTTGTCACCTGGACTCCACATAGGACTAATTATTATACTGGCAATAATG
ATCTATAAAAAGTCAGCAACTGATGTGTTTGAAAAGCATCCTTGTCTTTATATCCTAATG
TTTGGATGTGTCTTTGCTAAAGTCTCACAAAAATTAGTGGTAGCTCACATGACCAAAAGT
GAACTATATCTTCAAGACACTGTCTTTTTGGGGCCAGGTCTTTTGTTTTTAGACCAGTAC
TTTAATAACTTTATAGACGAATATGTTGTTCTATGGATGGCAATGGTGATTTCTTCATTT
GATATGGTGATATACTTTAGTGCTTTGTGCCTGCAAATTTCAAGACACCTTCATCTAAAT
ATATTCAAGACTGCATGTCATCAAGCACCTGAACAGGTTCAAGTTCTTTCTTCAAAGAGT
CATCAGAATAACATGGATTGA
|
| Enzyme 18 GenBank Gene ID |
NM_020244.2  |
| Enzyme 18 GeneCard ID |
CHPT1  |
| Enzyme 18 GenAtlas ID |
CHPT1  |
| Enzyme 18 HGNC ID |
HGNC:17852  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
12q |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Henneberry AL, Wistow G, McMaster CR: Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J Biol Chem. 2000 Sep 22;275(38):29808-15. [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
]
- Sinha Roy S, Mukherjee S, Kabir S, Rajaratnam V, Smith M, Das SK: Inhibition of cholinephosphotransferase activity in lung injury induced by 2-chloroethyl ethyl sulfide, a mustard analog. J Biochem Mol Toxicol. 2005;19(5):289-97. [PubMed
]
- Ghosh A, Akech J, Mukherjee S, Das SK: Differential expression of cholinephosphotransferase in normal and cancerous human mammary epithelial cells. Biochem Biophys Res Commun. 2002 Oct 4;297(4):1043-8. [PubMed
]
- Henneberry AL, Wright MM, McMaster CR: The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity. Mol Biol Cell. 2002 Sep;13(9):3148-61. [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
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
8529 |
| Enzyme 19 Name |
Phosphopantothenoylcysteine synthetase |
| Enzyme 19 Synonyms |
Not Available |
| Enzyme 19 Gene Name |
PPCS |
| Enzyme 19 Protein Sequence |
>Phosphopantothenoylcysteine synthetase
MFYLAAAVSDFYVPVSEMPEHKIQSSGGPLQITMKMVPKLLSPLVKDWAPKAFIISFKLE
TDPAIVINRARKALEIYQHQVVVANILESRQSFVFIVTKDSETKLLLSEEEIEKGVEIEE
KIVDNLQSRHTAFIGDRN
|
| Enzyme 19 Number of Residues |
138 |
| Enzyme 19 Molecular Weight |
15645.0 |
| Enzyme 19 Theoretical pI |
5.71 |
| Enzyme 19 GO Classification |
Not Available |
| Enzyme 19 General Function |
Coenzyme transport and metabolism |
| Enzyme 19 Specific Function |
Not Available |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
Not Available |
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
55665120  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q5VVM0  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
Q5VVM0_HUMAN  |
| Enzyme 19 PDB ID |
1P9O  |
| Enzyme 19 PDB File |
Show |
| Enzyme 19 3D Structure |
|
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>417 bp
ATGTTTTACCTGGCTGCGGCTGTGTCAGATTTCTATGTTCCTGTCTCTGAAATGCCTGAA
CACAAGATCCAGTCATCTGGGGGCCCACTGCAGATAACAATGAAGATGGTGCCAAAACTG
CTTTCTCCTTTGGTTAAAGATTGGGCTCCCAAAGCATTTATAATTTCCTTTAAGTTGGAG
ACTGACCCCGCCATTGTAATTAATCGAGCTCGGAAGGCTTTGGAAATTTATCAGCATCAA
GTGGTGGTGGCTAATATCCTTGAGTCACGACAGTCCTTTGTGTTTATTGTAACCAAAGAC
TCGGAAACCAAGTTATTGCTATCAGAGGAAGAAATAGAAAAAGGCGTAGAGATAGAAGAG
AAGATAGTGGATAATCTTCAGTCTCGACACACAGCTTTTATAGGTGACAGAAACTGA
|
| Enzyme 19 GenBank Gene ID |
AL445669  |
| Enzyme 19 GeneCard ID |
PPCS  |
| Enzyme 19 GenAtlas ID |
PPCS  |
| Enzyme 19 HGNC ID |
HGNC:25686  |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
1p34.2 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
Not Available |
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
8660 |
| Enzyme 20 Name |
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4 |
| Enzyme 20 Synonyms |
- Alpha 2,3-ST 4
- Beta-galactoside alpha-2,3-sialyltransferase 4
- Alpha 2,3-sialyltransferase IV
- Gal-NAc6S
- Gal-beta-1,4-GalNAc-alpha-2,3-sialyltransferase
- SAT-3
- ST-4
- ST3Gal IV
- ST3GalIV
- ST3GalA.2
- STZ
- Sialyltransferase 4C
- SIAT4-C
|
| Enzyme 20 Gene Name |
ST3GAL4 |
| Enzyme 20 Protein Sequence |
>CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
MVSKSRWKLLAMLALVLVVMVWYSISREDRYIELFYFPIPEKKEPCLQGEAESKASKLFG
NYSRDQPIFLRLEDYFWVKTPSAYELPYGTKGSEDLLLRVLAITSSSIPKNIQSLRCRRC
VVVGNGHRLRNSSLGDAINKYDVVIRLNNAPVAGYEGDVGSKTTMRLFYPESAHFDPKVE
NNPDTLLVLVAFKAMDFHWIETILSDKKRVRKGFWKQPPLIWDVNPKQIRILNPFFMEIA
ADKLLSLPMQQPRKIKQKPTTGLLAITLALHLCDLVHIAGFGYPDAYNKKQTIHYYEQIT
LKSMAGSGHNVSQEALAIKRMLEMGAIKNLTSF
|
| Enzyme 20 Number of Residues |
333 |
| Enzyme 20 Molecular Weight |
38045.1 |
| Enzyme 20 Theoretical pI |
9.88 |
| Enzyme 20 GO Classification |
| Function |
- catalytic activity
- sialyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid glycosylation
- protein modification process
|
| Component |
- cell part
- integral to Golgi membrane
- intrinsic to Golgi membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane part
|
|
| Enzyme 20 General Function |
Involved in sialyltransferase activity |
| Enzyme 20 Specific Function |
It may catalyze the formation of the NeuAc-alpha-2,3- Gal-beta-1,3-GalNAc- or NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. It may be involved in the biosynthesis of the sialyl Lewis X determinant. Also acts on the corresponding 1,3- galactosyl derivative |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
14714972  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q11206  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
SIA4C_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1002 bp
ATGGTCAGCAAGTCCCGCTGGAAGCTCCTGGCCATGTTGGCTCTGGTCCTGGTCGTCATG
GTGTGGTATTCCATCTCCCGGGAAGACAGGTACATCGAGCTTTTTTATTTTCCCATCCCA
GAGAAGAAGGAGCCGTGCCTCCAGGGTGAGGCAGAGAGCAAGGCCTCTAAGCTCTTTGGC
AACTACTCCCGGGATCAGCCCATCTTCCTGCGGCTTGAGGATTATTTCTGGGTCAAGACG
CCATCTGCTTACGAGCTGCCCTATGGGACCAAGGGGAGTGAGGATCTGCTCCTCCGGGTG
CTAGCCATCACCAGCTCCTCCATCCCCAAGAACATCCAGAGCCTCAGGTGCCGCCGCTGT
GTGGTCGTGGGGAACGGGCACCGGCTGCGGAACAGCTCACTGGGAGATGCCATCAACAAG
TACGATGTGGTCATCAGATTGAACAATGCCCCAGTGGCTGGCTATGAGGGTGACGTGGGC
TCCAAGACCACCATGCGTCTCTTCTACCCTGAATCTGCCCACTTCGACCCCAAAGTAGAA
AACAACCCAGACACACTCCTCGTCCTGGTAGCTTTCAAGGCAATGGACTTCCACTGGATT
GAGACCATCCTGAGTGATAAGAAGCGGGTGCGAAAGGGTTTCTGGAAACAGCCTCCCCTC
ATCTGGGATGTCAATCCTAAACAGATTCGGATTCTCAACCCCTTCTTCATGGAGATTGCA
GCTGACAAACTGCTGAGCCTGCCAATGCAACAGCCACGGAAGATTAAGCAGAAGCCCACC
ACGGGCCTGTTGGCCATCACGCTGGCCCTCCACCTCTGTGACTTGGTGCACATTGCCGGC
TTTGGCTACCCAGACGCCTACAACAAGAAGCAGACCATTCACTACTATGAGCAGATCACG
CTCAAGTCCATGGCGGGGTCAGGCCATAATGTCTCCCAAGAGGCCCTGGCCATTAAGCGG
ATGCTGGAGATGGGAGCTATCAAGAACCTCACGTCCTTCTGA
|
| Enzyme 20 GenBank Gene ID |
BC010645  |
| Enzyme 20 GeneCard ID |
ST3GAL4  |
| Enzyme 20 GenAtlas ID |
ST3GAL4  |
| Enzyme 20 HGNC ID |
HGNC:10864  |
| Enzyme 20 Chromosome Location |
1 |
| Enzyme 20 Locus |
11q24.2 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Kitagawa H, Mattei MG, Paulson JC: Genomic organization and chromosomal mapping of the Gal beta 1,3GalNAc/Gal beta 1,4GlcNAc alpha 2,3-sialyltransferase. J Biol Chem. 1996 Jan 12;271(2):931-8. [PubMed
]
- Kitagawa H, Paulson JC: Cloning of a novel alpha 2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups. J Biol Chem. 1994 Jan 14;269(2):1394-401. [PubMed
]
- Sasaki K, Watanabe E, Kawashima K, Sekine S, Dohi T, Oshima M, Hanai N, Nishi T, Hasegawa M: Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-sialyltransferase using lectin resistance selection. J Biol Chem. 1993 Oct 25;268(30):22782-7. [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
]
- 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
]
- Basu SS, Basu M, Li Z, Basu S: Characterization of two glycolipid: alpha 2-3sialyltransferases, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), from human colon carcinoma (Colo 205) cell line. Biochemistry. 1996 Apr 23;35(16):5166-74. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
8749 |
| Enzyme 21 Name |
Cytosolic 5'-nucleotidase 3 |
| Enzyme 21 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 21 Gene Name |
NT5C3 |
| Enzyme 21 Protein Sequence |
>Cytosolic 5'-nucleotidase 3
MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSV
RIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDEC
RKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVM
LKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLK
GFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYL
NDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
|
| Enzyme 21 Number of Residues |
336 |
| Enzyme 21 Molecular Weight |
37947.8 |
| Enzyme 21 Theoretical pI |
7.15 |
| Enzyme 21 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 21 General Function |
Involved in magnesium ion binding |
| Enzyme 21 Specific Function |
Can act both as nucleotidase and as phosphotransferase |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
|
| Enzyme 21 Pfam Domain Function |
Not Available |
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
70608082  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9H0P0  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
5NT3_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1011 bp
ATGAGGGCCCCGTCCATGGACCGCGCGGCCGTGGCGAGGGTGGGCGCGGTAGCGAGCGCC
AGCGTGTGCGCCCTGGTGGCGGGGGTGGTGCTGGCTCAGTACATATTCACCTTGAAGAGG
AAGACGGGGCGGAAGACCAAGATCATCGAGATGATGCCAGAATTCCAGAAAAGTTCAGTT
CGAATCAAGAACCCTACAAGAGTAGAAGAAATTATCTGTGGTCTTATCAAAGGAGGAGCT
GCCAAACTTCAGATAATAACGGACTTTGATATGACACTCAGTAGATTTTCATATAAAGGG
AAAAGATGCCCAACATGTCATAATATCATTGACAACTGTAAGCTGGTTACAGATGAATGT
AGAAAAAAGTTATTGCAACTAAAGGAAAAATATTACGCTATTGAAGTTGATCCTGTTCTT
ACTGTAGAAGAGAAGTACCCTTATATGGTGGAATGGTATACTAAATCACATGGTTTGCTT
GTTCAGCAAGCTTTACCAAAAGCTAAACTTAAAGAAATTGTGGCAGAATCTGACGTTATG
CTCAAAGAAGGATATGAGAATTTCTTTGATAAGCTCCAACAACATAGCATCCCCGTGTTC
ATATTTTCGGCTGGAATCGGCGATGTACTAGAGGAAGTTATTCGTCAAGCTGGTGTTTAT
CATCCCAATGTCAAAGTTGTGTCCAATTTTATGGATTTTGATGAAACTGGGGTGCTCAAA
GGATTTAAAGGAGAACTAATTCATGTATTTAACAAACATGATGGTGCCTTGAGGAATACA
GAATATTTCAATCAACTAAAAGACAATAGTAACATAATTCTTCTGGGAGACTCCCAAGGA
GACTTAAGAATGGCAGATGGAGTGGCCAATGTTGAGCACATTCTGAAAATTGGATATCTA
AATGATAGAGTGGATGAGCTTTTAGAAAAGTACATGGACTCTTATGATATTGTTTTAGTA
CAAGATGAATCATTAGAAGTAGCCAACTCTATTTTACAGAAGATTCTATAA
|
| Enzyme 21 GenBank Gene ID |
NM_001002010.1  |
| Enzyme 21 GeneCard ID |
NT5C3  |
| Enzyme 21 GenAtlas ID |
NT5C3  |
| Enzyme 21 HGNC ID |
HGNC:17820  |
| Enzyme 21 Chromosome Location |
7 |
| Enzyme 21 Locus |
7p14.3 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 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 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
13097 |
| Enzyme 22 Name |
UMP-CMP kinase 2, mitochondrial |
| Enzyme 22 Synonyms |
Not Available |
| Enzyme 22 Gene Name |
CMPK2 |
| Enzyme 22 Protein Sequence |
>UMP-CMP kinase 2, mitochondrial
MAFARRLLRGPLSGPLLGRRGVCAGAMAPPRRFVLELPDCTLAHFALGADAPGDADAPDP
RLAALLGPPERSYSLCVPVTPDAGCGARVRAARLHQRLLHQLRRGPFQRCQLLRLLCYCP
GGQAGGAQQGFLLRDPLDDPDTRQALLELLGACQEAPRPHLGEFEADPRGQLWQRLWEVQ
DGRRLQVGCAQVVPVPEPPLHPVVPDLPSSVVFPDREAARAVLEECTSFIPEARAVLDLV
DQCPKQIQKGKFQVVAIEGLDATGKTTVTQSVADSLKAVLLKSPPSCIGQWRKIFDDEPT
IIRRAFYSLGNYIVASEIAKESAKSPVIVDRYWHSTATYAIATEVSGGLQHLPPAHHPVY
QWPEDLLKPDLILLLTVSPEERLQRLQGRGMEKTREEAELEANSVFRQKVEMSYQRMENP
GCHVVDASPSREKVLQTVLSLIQNSFSEP
|
| Enzyme 22 Number of Residues |
449 |
| Enzyme 22 Molecular Weight |
49447.3 |
| Enzyme 22 Theoretical pI |
7.00 |
| Enzyme 22 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- thymidylate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular nitrogen compound metabolic process
- dTDP biosynthetic 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
- pyrimidine deoxyribonucleoside diphosphate biosynthetic process
- pyrimidine nucleoside diphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
|
| Component |
| — |
|
| Enzyme 22 General Function |
Involved in thymidylate kinase activity |
| Enzyme 22 Specific Function |
May participate in dUTP and dCTP synthesis in mitochondria. Is able to phosphorylate dUMP, dCMP, CMP, UMP and monophosphates of the pyrimidine nucleoside analogs ddC, dFdC, araC, BVDU and FdUrd with ATP as phosphate donor. Efficacy is highest for dUMP followed by dCMP; CMP and UMP are poor substrates. May be involved in mtDNA depletion caused by long term treatment with ddC or other pyrimidine analogs |
| Enzyme 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
- ATP + (d)CMP = ADP + (d)CDP [RN:R00512 R01665]
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
117606370  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q5EBM0  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
CMPK2_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1350 bp
ATGGCCTTCGCCCGCCGGCTCCTGCGCGGGCCACTGTCGGGGCCGCTGCTCGGGCGGCGC
GGGGTCTGCGCTGGGGCCATGGCTCCGCCGCGCCGCTTCGTCCTGGAGCTTCCCGACTGC
ACCCTGGCTCACTTCGCCCTAGGCGCCGACGCCCCCGGCGACGCAGACGCCCCCGACCCC
CGCCTGGCGGCGCTGCTGGGGCCCCCGGAGCGCAGCTACTCGCTGTGCGTGCCCGTGACC
CCGGACGCCGGCTGCGGGGCCCGGGTCCGGGCGGCGCGGCTGCACCAGCGCCTGCTGCAC
CAGCTGCGCCGCGGCCCCTTCCAGCGGTGCCAGCTGCTCAGGCTGCTCTGCTACTGCCCG
GGCGGCCAGGCCGGCGGCGCACAGCAAGGCTTCCTGCTGCGCGACCCCCTGGATGACCCT
GACACCCGGCAAGCGCTGCTCGAGCTGCTGGGCGCCTGTCAGGAGGCACCACGCCCGCAC
TTGGGCGAGTTCGAGGCCGACCCGCGCGGCCAGCTGTGGCAGCGCCTCTGGGAGGTGCAA
GACGGCAGGCGGCTGCAGGTGGGCTGCGCACAGGTCGTGCCCGTCCCGGAGCCCCCGCTG
CACCCGGTGGTGCCAGACTTGCCCAGTTCCGTGGTCTTCCCGGACCGGGAAGCCGCCCGG
GCCGTTTTGGAGGAGTGTACCTCCTTTATTCCTGAAGCCCGGGCAGTGCTTGACCTGGTC
GACCAGTGCCCAAAACAGATCCAGAAAGGAAAGTTCCAGGTTGTTGCCATCGAAGGACTG
GATGCCACGGGTAAAACCACGGTGACCCAGTCAGTGGCAGATTCACTTAAGGCTGTCCTC
TTAAAGTCACCACCCTCTTGCATTGGCCAGTGGAGGAAGATCTTTGATGATGAACCAACT
ATCATTAGAAGAGCTTTTTACTCTTTGGGCAATTATATTGTGGCCTCCGAAATAGCTAAA
GAATCTGCCAAATCTCCTGTGATTGTAGACAGGTACTGGCACAGCACGGCCACCTATGCC
ATAGCCACTGAGGTGAGTGGGGGTCTCCAGCACCTGCCCCCAGCCCATCACCCTGTGTAC
CAGTGGCCAGAGGACCTGCTCAAACCTGACCTTATCCTGCTGCTCACTGTGAGTCCTGAG
GAGAGGTTGCAGAGGCTGCAGGGCCGGGGCATGGAGAAGACCAGGGAAGAAGCAGAACTT
GAGGCCAACAGTGTGTTTCGTCAAAAGGTAGAAATGTCCTACCAGCGGATGGAGAATCCT
GGCTGCCATGTGGTTGATGCCAGCCCCTCCAGAGAAAAGGTCCTGCAGACGGTATTAAGC
CTAATCCAGAATAGTTTTAGTGAACCGTAG
|
| Enzyme 22 GenBank Gene ID |
NM_207315.2  |
| Enzyme 22 GeneCard ID |
CMPK2  |
| Enzyme 22 GenAtlas ID |
CMPK2  |
| Enzyme 22 HGNC ID |
HGNC:27015  |
| Enzyme 22 Chromosome Location |
2 |
| Enzyme 22 Locus |
2p25.2 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Xu Y, Johansson M, Karlsson A: Human UMP-CMP kinase 2, a novel nucleoside monophosphate kinase localized in mitochondria. J Biol Chem. 2008 Jan 18;283(3):1563-71. Epub 2007 Nov 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
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
13098 |
| Enzyme 23 Name |
Uridine-cytidine kinase-like 1 |
| Enzyme 23 Synonyms |
Not Available |
| Enzyme 23 Gene Name |
UCKL1 |
| Enzyme 23 Protein Sequence |
>Uridine-cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
|
| Enzyme 23 Number of Residues |
548 |
| Enzyme 23 Molecular Weight |
61140.4 |
| Enzyme 23 Theoretical pI |
7.40 |
| Enzyme 23 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 23 General Function |
Involved in ATP binding |
| Enzyme 23 Specific Function |
May contribute to UTP accumulation needed for blast transformation and proliferation |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- ATP + uridine = ADP + UMP [RN:R00964]
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
57863312  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q9NWZ5  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
UCKL1_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>1647 bp
ATGGCTGCGCCCCCGGCCCGCGCGGACGCTGATCCTTCGCCCACGTCGCCACCTACGGCC
CGAGACACACCAGGCCGGCAGGCTGAGAAAAGCGAGACCGCGTGCGAGGACCGCAGCAAT
GCAGAGTCCCTGGACAGGCTCCTGCCACCTGTGGGCACTGGGCGCTCTCCCCGGAAGCGG
ACCACCAGCCAGTGCAAGTCAGAGCCTCCCCTGCTGCGTACAAGCAAGCGTACCATCTAC
ACCGCCGGGCGGCCGCCCTGGTACAATGAACACGGCACGCAATCCAAAGAGGCCTTCGCC
ATCGGCTTGGGAGGCGGCAGTGCCTCTGGGAAGACCACTGTGGCCAGAATGATCATCGAG
GCCCTGGATGTGCCCTGGGTGGTCTTGCTGTCCATGGACTCCTTCTACAAGGTGCTGACT
GAGCAGCAGCAGGAACAGGCCGCACACAACAACTTCAACTTCGACCACCCAGATGCCTTT
GACTTCGACCTCATCATTTCCACCCTCAAGAAGCTGAAGCAGGGGAAGAGTGTCAAGGTG
CCCATTTATGACTTCACCACGCACAGCCGGAAGAAGGACTGGAAAACACTGTATGGTGCA
AACGTCATCATCTTTGAGGGCATCATGGCCTTTGCTGACAAGACACTGTTGGAGCTCCTG
GACATGAAGATCTTTGTGGACACAGACTCCGACATCCGCCTGGTACGGCGGCTGCGCCGG
GACATCAGTGAGCGCGGCCGGGACATCGAGGGTGTCATCAAGCAGTACAACAAGTTTGTC
AAGCCCTCCTTCGACCAGTACATCCAGCCCACCATGCGCCTGGCAGACATCGTGGTCCCC
AGAGGGAGCGGCAACACGGTGGCCATCGACCTGATTGTGCAGCACGTGCACAGCCAGCTG
GAGGAGCGTGAACTCAGCGTCAGGGCTGCGCTGGCCTCGGCACACCAGTGCCACCCGCTG
CCCCGGACGCTGAGCGTCCTGAAGAGCACGCCGCAGGTACGGGGCATGCACACCATCATC
AGGGACAAGGAGACCAGTCGCGACGAGTTCATCTTCTACTCCAAGAGACTGATGCGGCTG
CTCATCGAGCACGCGCTCTCCTTCCTGCCCTTTCAGGACTGCGTCGTACAGACCCCGCAG
GGGCAGGACTATGCGGGCAAGTGCTATGCGGGGAAGCAGATCACCGGTGTGTCCATTCTG
CGCGCCGGTGAAACCATGGAGCCCGCGCTGCGCGCTGTGTGCAAAGACGTGCGCATCGGC
ACCATCCTCATCCAGACCAACCAGCTTACCGGGGAGCCCGAGCTCCACTACCTGAGGCTG
CCCAAGGACATCAGCGATGACCACGTGATCCTCATGGACTGCACCGTGTCCACGGGCGCG
GCGGCCATGATGGCAGTGCGCGTGCTCCTGGACCACGACGTGCCTGAGGACAAGATCTTT
TTGCTGTCGCTGCTCATGGCAGAGATGGGCGTGCACTCAGTGGCCTATGCATTTCCGCGA
GTGAGAATCATCACCACGGCGGTGGACAAGCGGGTCAATGACCTTTTCCGCATCATCCCA
GGCATTGGGAACTTTGGCGACCGCTACTTTGGGACAGACGCGGTCCCCGATGGCAGTGAC
GAGGAGGAAGTGGCCTACACGGGTTAG
|
| Enzyme 23 GenBank Gene ID |
NM_017859.3  |
| Enzyme 23 GeneCard ID |
UCKL1  |
| Enzyme 23 GenAtlas ID |
UCKL1  |
| Enzyme 23 HGNC ID |
HGNC:15938  |
| Enzyme 23 Chromosome Location |
2 |
| Enzyme 23 Locus |
20q13.33 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Kashuba E, Kashuba V, Sandalova T, Klein G, Szekely L: Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase. BMC Cell Biol. 2002 Aug 29;3:23. Epub 2002 Aug 29. [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, 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
]
- 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
]
- 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
]
- 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
]
- 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 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
13379 |
| Enzyme 24 Name |
Ectonucleoside triphosphate diphosphohydrolase 8 |
| Enzyme 24 Synonyms |
- E-NTPDase 8
- NTPDase 8
- NTPDase8
|
| Enzyme 24 Gene Name |
ENTPD8 |
| Enzyme 24 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
|
| Enzyme 24 Number of Residues |
495 |
| Enzyme 24 Molecular Weight |
53903.1 |
| Enzyme 24 Theoretical pI |
4.96 |
| Enzyme 24 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in hydrolase activity |
| Enzyme 24 Specific Function |
Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolyzis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
110431368  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q5MY95  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
ENTP8_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>1488 bp
ATGGGGCTGTCCCGGAAGGAGCAGGTCTTCTTGGCCCTGCTGGGGGCCTCGGGGGTCTCA
GGCCTCACGGCACTCATTCTCCTCCTGGTGGAGGCCACCAGCGTGCTCCTGCCCACAGAC
ATCAAGTTTGGGATCGTGTTTGATGCGGGCTCCTCCCACACGTCCCTCTTCCTGTATCAG
TGGCTGGCGAACAAGGAGAATGGCACGGGTGTGGTCAGCCAGGCCCTGGCCTGCCAGGTG
GAAGGGCCTGGAATCTCCTCCTACACTTCTAATGCTGCACAGGCTGGTGAGAGCCTGCAG
GGCTGCTTGGAGGAGGCGCTGGTGCTGATCCCAGAGGCCCAGCATCGGAAAACACCCACG
TTCCTGGGGGCCACGGCTGGCATGAGGTTGCTCAGCCGGAAGAACAGCTCTCAGGCCAGG
GACATCTTTGCAGCAGTCACCCAGGTCCTGGGCCGGTCTCCCGTGGACTTTTGGGGTGCC
GAGCTCCTGGCCGGGCAGGCCGAAGGTGCCTTTGGTTGGATCACTGTCAACTACGGCTTG
GGGACGCTGGTCAAGTACTCCTTCACTGGAGAATGGATCCAGCCTCCGGAGGAGATGCTG
GTGGGTGCCCTGGACATGGGAGGGGCCTCCACCCAGATCACGTTCGTGCCTGGGGGCCCC
ATCTTGGACAAGAGCACCCAGGCCGATTTTCGCCTCTACGGCTCCGACTACAGCGTCTAC
ACTCACAGCTACCTGTGCTTTGGACGGGACCAGATGCTGAGCAGGCTCCTCGTGGGGCTG
GTACAGAGCCGCCCGGCTGCCCTGCTCCGTCACCCGTGCTACCTCAGCGGCTACCAGACC
ACACTGGCCCTGGGCCCGCTGTATGAGTCACCCTGTGTCCACGCCACGCCCCCGCTGAGC
CTCCCCCAGAACCTCACAGTTGAAGGGACAGGCAACCCTGGAGCCTGCGTCTCAGCCATC
CGGGAACTTTTCAACTTCTCCAGCTGCCAGGGCCAGGAGGACTGCGCCTTTGACGGGGTC
TACCAGCCCCCGCTGCGGGGCCAGTTCTATGCCTTCTCCAACTTCTACTACACCTTCCAC
TTCCTGAACCTCACCTCCAGGCAGCCCCTGAGCACGGTCAACGCCACCATCTGGGAGTTT
TGCCAGAGGCCCTGGAAACTGGTGGAGGCCAGCTACCCTGGGCAGGACCGCTGGCTGCGG
GACTACTGTGCCTCAGGCCTGTACATCCTCACCCTCCTGCACGAGGGCTACGGGTTCAGC
GAGGAGACCTGGCCCAGCCTCGAGTTCCGAAAGCAGGCGGGCGGTGTGGACATTGGCTGG
ACACTGGGCTACATGCTGAACCTGACCGGGATGATCCCGGCCGATGCGCCGGCTCAGTGG
CGGGCAGAGAGCTACGGCGTCTGGGTGGCCAAAGTGGTGTTCATGGTGCTGGCCCTGGTG
GCGGTGGTGGGGGCTGCCTTGGTCCAGCTCTTCTGGTTGCAGGACTAG
|
| Enzyme 24 GenBank Gene ID |
NM_001033113.1  |
| Enzyme 24 GeneCard ID |
ENTPD8  |
| Enzyme 24 GenAtlas ID |
ENTPD8  |
| Enzyme 24 HGNC ID |
HGNC:24860  |
| Enzyme 24 Chromosome Location |
9 |
| Enzyme 24 Locus |
9q34.3 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Knowles AF, Li C: Molecular cloning and characterization of expressed human ecto-nucleoside triphosphate diphosphohydrolase 8 (E-NTPDase 8) and its soluble extracellular domain. Biochemistry. 2006 Jun 13;45(23):7323-33. [PubMed
]
- Fausther M, Lecka J, Kukulski F, Levesque SA, Pelletier J, Zimmermann H, Dranoff JA, Sevigny J: Cloning, purification, and identification of the liver canalicular ecto-ATPase as NTPDase8. Am J Physiol Gastrointest Liver Physiol. 2007 Mar;292(3):G785-95. Epub 2006 Nov 9. [PubMed
]
- 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
]
- 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
]
- Levesque SA, Lavoie EG, Lecka J, Bigonnesse F, Sevigny J: Specificity of the ecto-ATPase inhibitor ARL 67156 on human and mouse ectonucleotidases. Br J Pharmacol. 2007 Sep;152(1):141-50. Epub 2007 Jul 2. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
15061 |
| Enzyme 25 Name |
cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA |
| Enzyme 25 Synonyms |
Not Available |
| Enzyme 25 Gene Name |
Not Available |
| Enzyme 25 Protein Sequence |
>cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
SQEITHCHDEDDDEEEEEEEE
|
| Enzyme 25 Number of Residues |
561 |
| Enzyme 25 Molecular Weight |
64959.2 |
| Enzyme 25 Theoretical pI |
6.05 |
| Enzyme 25 GO Classification |
Not Available |
| Enzyme 25 General Function |
Not Available |
| Enzyme 25 Specific Function |
Not Available |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
158256766  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
A8K6K2  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
A8K6K2_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1686 bp
ATGTCAACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
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
TCCCAGGAAATTACACACTGCCATGATGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
|
| Enzyme 25 GenBank Gene ID |
AK291667  |
| Enzyme 25 GeneCard ID |
Not Available |
| Enzyme 25 GenAtlas ID |
Not Available |
| Enzyme 25 HGNC ID |
HGNC:8022  |
| Enzyme 25 Chromosome Location |
Not Available |
| Enzyme 25 Locus |
Not Available |
| Enzyme 25 SNPs |
Not Available |
| Enzyme 25 General References |
Not Available |
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
15200 |
| Enzyme 26 Name |
Uridine kinase |
| Enzyme 26 Synonyms |
Not Available |
| Enzyme 26 Gene Name |
UCK1 |
| Enzyme 26 Protein Sequence |
>Uridine kinase
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
|
| Enzyme 26 Number of Residues |
201 |
| Enzyme 26 Molecular Weight |
22760.4 |
| Enzyme 26 Theoretical pI |
6.23 |
| Enzyme 26 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 26 General Function |
Involved in ATP binding |
| Enzyme 26 Specific Function |
ATP + cytidine = ADP + CMP |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
- ATP + uridine = ADP + UMP [RN:R00964]
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
57162374  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q5JT13  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
Q5JT13_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>606 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGGTGAGCGGCGGCACTGCCAGCGGGAAGTCGACCGTGTGT
GAGAAGATCATGGAGTTGCTGGGACAGAACGAGGTGGAACAGCGGCAGCGGAAGGTGGTC
ATCCTGAGCCAGGACAGGTTCTACAAGGTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTG
AAAGGACAGTACAATTTTGACCATCCAGATGCCTTTGATAATGATTTGATGCACAGGACT
CTGAAGAACATCGTGGAGGGCAAAACGGTGGAGGTGCCGACCTATGATTTTGTGACACAC
TCAAGGTTACCAGAGACCACGGTGGTCTACCCTGCGGACGTGGTTCTGTTTGAGGGCATC
TTGGTGTTCTACAGCCAGGAGATCCGGGACATGTTCCACCTGCGCCTCTTCGTGGACACC
GACTCCGACGTCAGGCTGTCTCGAAGAGACAAAGAAGTATGCCGATGTGATCATCCCGCG
AGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGACATTCTGAA
TGGTGA
|
| Enzyme 26 GenBank Gene ID |
AL358781  |
| Enzyme 26 GeneCard ID |
UCK1  |
| Enzyme 26 GenAtlas ID |
UCK1  |
| Enzyme 26 HGNC ID |
HGNC:14859  |
| Enzyme 26 Chromosome Location |
9 |
| Enzyme 26 Locus |
9q34.13 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
Not Available |
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
15201 |
| Enzyme 27 Name |
cDNA FLJ77291, highly similar to Homo sapiens ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1), transcript variant 2, mRNA (ST6 beta-galactosamide alpha-2,6-sialyltranferase 1, isoform CRA_d) |
| Enzyme 27 Synonyms |
Not Available |
| Enzyme 27 Gene Name |
ST6GAL1 |
| Enzyme 27 Protein Sequence |
>cDNA FLJ77291, highly similar to Homo sapiens ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1), transcript variant 2, mRNA (ST6 beta-galactosamide alpha-2,6-sialyltranferase 1, isoform CRA_d)
MIHTNLKKKFSCCVLVFLLFAVICVWKEKKKGSYYDSFKLQTKEFQVLKSLGKLAMGSDS
QSVSSSSTQDPHRGRQTLGSLRGLAKAKPEASFQVWNKDSSSKNLIPRLQKIWKNYLSMN
KYKVSYKGPGPGIKFSAEALRCHLRDHVNVSMVEVTDFPFNTSEWEGYLPKESIRTKAGP
WGRCAVVSSAGSLKSSQLGREIDDHDAVLRFNGAPTANFQQDVGTKTTIRLMNSQLVTTE
KRFLKDSLYNEGILIVWDPSVYHSDIPKWYQNPDYNFFNNYKTYRKLHPNQPFYILKPQM
PWELWDILQEISPEEIQPNPPSSGMLGIIIMMTLCDQVDIYEFLPSKRKTDVCYYYQKFF
DSACTMGAYHPLLYEKNLVKHLNQGTDEDIYLLGKATLPGFRTIHC
|
| Enzyme 27 Number of Residues |
406 |
| Enzyme 27 Molecular Weight |
46605 |
| Enzyme 27 Theoretical pI |
9.35 |
| Enzyme 27 GO Classification |
Not Available |
| Enzyme 27 General Function |
Not Available |
| Enzyme 27 Specific Function |
Not Available |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
Not Available |
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
158259219  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
A8KA14  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
A8KA14_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1221 bp
ATGATTCACACCAACCTGAAGAAAAAGTTCAGCTGCTGCGTCCTGGTCTTTCTTCTGTTT
GCAGTCATCTGTGTGTGGAAGGAAAAGAAGAAAGGGAGTTACTATGATTCCTTTAAATTG
CAAACCAAGGAATTCCAGGTGTTAAAGAGTCTGGGGAAATTGGCCATGGGGTCTGATTCC
CAGTCTGTATCCTCAAGCAGCACCCAGGACCCCCACAGGGGCCGCCAGACCCTCGGCAGT
CTCAGAGGCCTAGCCAAGGCCAAACCAGAGGCCTCCTTCCAGGTGTGGAACAAGGACAGC
TCTTCCAAAAACCTTATCCCTAGGCTGCAAAAGATCTGGAAGAATTACCTAAGCATGAAC
AAGTACAAAGTGTCCTACAAGGGGCCAGGACCAGGCATCAAGTTCAGTGCAGAGGCCCTG
CGCTGCCACCTCCGGGACCATGTGAATGTATCCATGGTAGAGGTCACAGATTTTCCCTTC
AATACCTCTGAATGGGAGGGTTATCTGCCCAAGGAGAGCATTAGGACCAAGGCTGGGCCT
TGGGGCAGGTGTGCTGTTGTGTCGTCAGCGGGATCTCTGAAGTCCTCCCAACTAGGCAGA
GAAATCGATGATCATGACGCAGTCCTGAGGTTTAATGGGGCACCCACAGCCAACTTCCAA
CAAGATGTGGGCACAAAAACTACCATTCGCCTGATGAACTCTCAGTTGGTTACCACAGAG
AAGCGCTTCCTCAAAGACAGTTTGTACAATGAAGGAATCCTAATTGTATGGGACCCATCT
GTATACCACTCAGATATCCCAAAGTGGTACCAGAATCCGGATTATAATTTCTTTAACAAC
TACAAGACTTATCGTAAGCTGCACCCCAATCAGCCCTTTTACATCCTCAAGCCCCAGATG
CCTTGGGAGCTATGGGACATTCTTCAAGAAATCTCCCCAGAAGAGATTCAGCCAAACCCC
CCATCCTCTGGGATGCTTGGTATCATCATCATGATGACGCTGTGTGACCAGGTGGATATT
TATGAGTTCCTCCCATCCAAGCGCAAGACTGACGTGTGCTACTACTACCAGAAGTTCTTC
GATAGTGCCTGCACGATGGGTGCCTACCACCCGCTGCTCTATGAGAAGAATTTGGTGAAG
CATCTCAACCAGGGCACAGATGAGGACATCTACCTGCTTGGAAAAGCCACACTGCCTGGC
TTCCGGACCATTCACTGCTAA
|
| Enzyme 27 GenBank Gene ID |
AK292879  |
| Enzyme 27 GeneCard ID |
A8KA14  |
| Enzyme 27 GenAtlas ID |
Not Available |
| Enzyme 27 HGNC ID |
Not Available |
| Enzyme 27 Chromosome Location |
Not Available |
| Enzyme 27 Locus |
Not Available |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
Not Available |
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
15202 |
| Enzyme 28 Name |
ST6 neuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide alpha- 2,6-sialyltransferase 4 (ST6 (Alpha-N-acetyl-neuraminyl-2,3-beta- galactosyl-1, 3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, isoform CRA_a) |
| Enzyme 28 Synonyms |
Not Available |
| Enzyme 28 Gene Name |
ST6GALNAC4 |
| Enzyme 28 Protein Sequence |
>ST6 neuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide alpha- 2,6-sialyltransferase 4 (ST6 (Alpha-N-acetyl-neuraminyl-2,3-beta- galactosyl-1, 3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, isoform CRA_a)
MKAPGRLVLIILCSVVFSAVYILLCCWAGLPLCLATCLDHHFPTGSRPTVPGPLHFSGYS
SVPDGKPLVREPCRSCAVVSSSGQMLGSGLGAEIDSAECVFRMNQAPTVGFEADVGQRST
LRVVSHTSVPLLLRNYSHYFQKARDTLYMVWGQGRHMDRVLGGRTYRTLLQLTRMYPGLQ
VYTFTERMMAYCDQIFQDETGKNRRQSGSFLSTGWFTMILALELCEEIVVYGMVSDSYCR
EKSHPSVPYHYFEKGRLDECQMYLAHEQAPRSAHRFITEKAVFSRWAKKRPIVFAHPSWR
TE
|
| Enzyme 28 Number of Residues |
302 |
| Enzyme 28 Molecular Weight |
34201 |
| Enzyme 28 Theoretical pI |
8.65 |
| Enzyme 28 GO Classification |
| Function |
- catalytic activity
- sialyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid glycosylation
- protein modification
|
| Component |
- cell
- integral to Golgi membrane
- intrinsic to Golgi membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane
|
|
| Enzyme 28 General Function |
Not Available |
| Enzyme 28 Specific Function |
Not Available |
| Enzyme 28 Pathways |
Not Available |
| Enzyme 28 Reactions |
Not Available |
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
55958253  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q5T9D0  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
Q5T9D0_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>909 bp
ATGAAGGCTCCGGGTCGGCTCGTGCTCATCATCCTGTGCTCCGTGGTCTTCTCTGCCGTC
TACATCCTCCTGTGCTGCTGGGCCGGCCTGCCCCTCTGCCTGGCCACCTGCCTGGACCAC
CACTTCCCCACAGGCTCCAGGCCCACTGTGCCGGGACCCCTGCACTTCAGTGGATATAGC
AGTGTGCCAGATGGGAAGCCGCTGGTCCGCGAGCCCTGCCGCAGCTGTGCCGTGGTGTCC
AGCTCCGGCCAAATGCTGGGCTCAGGCCTGGGTGCTGAGATCGACAGTGCCGAGTGCGTG
TTCCGCATGAACCAGGCGCCCACCGTGGGCTTTGAGGCGGATGTGGGCCAGCGCAGCACC
CTGCGTGTCGTCTCACACACAAGCGTGCCGCTGCTGCTGCGCAACTATTCACACTACTTC
CAGAAGGCCCGAGACACGCTCTACATGGTGTGGGGCCAGGGCAGGCACATGGACCGGGTG
CTCGGCGGCCGCACCTACCGCACGCTGCTGCAGCTCACCAGGATGTACCCCGGCCTGCAG
GTGTACACCTTCACGGAGCGCATGATGGCCTACTGCGACCAGATCTTCCAGGACGAGACG
GGCAAGAACCGGAGGCAGTCGGGCTCCTTCCTCAGCACCGGCTGGTTCACCATGATCCTC
GCGCTGGAGCTGTGTGAGGAGATCGTGGTCTATGGGATGGTCAGCGACAGCTACTGCAGG
GAGAAGAGCCACCCCTCAGTGCCTTACCACTACTTTGAGAAGGGCCGGCTAGATGAGTGT
CAGATGTACCTGGCACACGAGCAGGCGCCCCGAAGCGCCCACCGCTTCATCACTGAGAAG
GCGGTCTTCTCCCGCTGGGCCAAGAAGAGGCCCATCGTGTTCGCCCATCCGTCCTGGAGG
ACTGAGTAG
|
| Enzyme 28 GenBank Gene ID |
AL157935  |
| Enzyme 28 GeneCard ID |
Q5T9D0  |
| Enzyme 28 GenAtlas ID |
ST6GALNAC4  |
| Enzyme 28 HGNC ID |
HGNC:17846  |
| Enzyme 28 Chromosome Location |
Not Available |
| Enzyme 28 Locus |
Not Available |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
Not Available |
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
15203 |
| Enzyme 29 Name |
cDNA FLJ77944, highly similar to H.sapiens GD3 synthase mRNA (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1, isoform CRA_a) |
| Enzyme 29 Synonyms |
Not Available |
| Enzyme 29 Gene Name |
ST8SIA1 |
| Enzyme 29 Protein Sequence |
>cDNA FLJ77944, highly similar to H.sapiens GD3 synthase mRNA (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1, isoform CRA_a)
MSPCGRARRQTSRGAMAVLAWKFPRTRLPMGASALCVVVLCWLYIFPVYRLPNEKEIVQG
VLQQGTAWRRNQTAARAFRKQMEDCCDPAHLFAMTKMNSPMGKSMWYDGEFLYSFTIDNS
TYSLFPQATPFQLPLKKCAVVGNGGILKKSGCGRQIDEANFVMRCNLPPLSSEYTKDVGS
KSQLVTANPSIIRQRFQNLLWSRKTFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLS
DVGANQTVLFANPNFLRSIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVAIYGFWPFSV
NMHEQPISHHYYDNVLPFSGFHAMPEEFLQLWYLHKIGALRMQLDPCEDTSLQPTS
|
| Enzyme 29 Number of Residues |
356 |
| Enzyme 29 Molecular Weight |
40519 |
| Enzyme 29 Theoretical pI |
9.61 |
| Enzyme 29 GO Classification |
Not Available |
| Enzyme 29 General Function |
Not Available |
| Enzyme 29 Specific Function |
Not Available |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
Not Available |
| Enzyme 29 Pfam Domain Function |
Not Available |
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
158255318  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
A8K4H6  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
A8K4H6_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>1071 bp
ATGAGCCCCTGCGGGCGGGCCCGGCGACAAACGTCCAGAGGGGCCATGGCTGTACTGGCG
TGGAAGTTCCCGCGGACCCGGCTGCCCATGGGAGCCAGTGCCCTCTGTGTCGTGGTCCTC
TGTTGGCTCTACATCTTCCCCGTCTACCGGCTGCCCAACGAGAAAGAGATCGTGCAGGGG
GTGCTGCAACAGGGCACGGCGTGGAGGAGGAACCAGACCGCGGCCAGAGCGTTCAGGAAA
CAAATGGAAGACTGCTGCGACCCTGCTCATCTCTTTGCTATGACTAAAATGAATTCCCCT
ATGGGGAAGAGCATGTGGTATGACGGGGAGTTTTTATACTCATTCACCATTGACAATTCA
ACTTACTCTCTCTTCCCACAGGCAACCCCATTCCAGCTGCCATTGAAGAAATGCGCGGTG
GTGGGAAATGGTGGGATTCTGAAGAAGAGTGGCTGTGGCCGTCAAATAGATGAAGCAAAT
TTTGTCATGCGATGCAATCTCCCTCCTTTGTCAAGTGAATACACTAAGGATGTTGGATCC
AAAAGTCAGTTAGTGACAGCTAATCCCAGCATAATTCGGCAAAGGTTTCAGAACCTTCTG
TGGTCCAGAAAGACATTTGTGGACAACATGAAAATCTATAACCACAGTTACATCTACATG
CCTGCCTTTTCTATGAAGACAGGAACAGAGCCATCTTTGAGGGTTTATTATACACTGTCA
GATGTTGGTGCCAATCAAACAGTGCTGTTTGCCAACCCCAACTTTCTGCGTAGCATTGGA
AAGTTCTGGAAAAGTAGAGGAATCCATGCCAAGCGCCTGTCCACAGGACTTTTTCTGGTG
AGCGCAGCTCTGGGTCTCTGTGAAGAGGTGGCCATCTATGGCTTCTGGCCCTTCTCTGTG
AATATGCATGAGCAGCCCATCAGCCACCACTACTATGACAACGTCTTACCCTTTTCTGGC
TTCCATGCCATGCCCGAGGAATTTCTCCAACTCTGGTATCTTCATAAAATCGGTGCACTG
AGAATGCAGCTGGACCCATGTGAAGATACCTCACTCCAGCCCACTTCCTAG
|
| Enzyme 29 GenBank Gene ID |
AK290941  |
| Enzyme 29 GeneCard ID |
A8K4H6  |
| Enzyme 29 GenAtlas ID |
Not Available |
| Enzyme 29 HGNC ID |
Not Available |
| Enzyme 29 Chromosome Location |
12 |
| Enzyme 29 Locus |
12p12.1-p11.2 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
Not Available |
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
15204 |
| Enzyme 30 Name |
CDP-diacylglycerol--inositol 3-phosphatidyltransferase (Phosphatidylinositol synthase), isoform CRA_a |
| Enzyme 30 Synonyms |
- SubName: cDNA FLJ40372 fis, clone TESTI2034940, highly similar to CDP-diacylglycerol--inositol3-phosphatidyltransferase (EC 2.7.8.11)
- SubName: cDNA FLJ77674, highly similar to Homo sapiens CDP-diacylglycerol--inositol 3-phosphatidyltransferase (phosphatidylinositol synthase) (CDIPT), transcript variant 1, mRNA
|
| Enzyme 30 Gene Name |
CDIPT |
| Enzyme 30 Protein Sequence |
>CDP-diacylglycerol--inositol 3-phosphatidyltransferase (Phosphatidylinositol synthase), isoform CRA_a
MPDENIFLFVPNLIGYARIVFAIISFYFMPCCPLTASSFYLLSGLLDAFDGHAARALNQG
TRFGAMLDMLTDRCSTMCLLVNLALLYPGATLFFQISMSLDVASHWLHLHSSVVRGSESH
KMIDLSGNPVLRIYYTSRPALFTLCAGNELFYCLLYLFHFSEGPLVGSVGLFRMGLWVTA
PIALLKSLISVIHLITAARNMAALDAADRAKKK
|
| Enzyme 30 Number of Residues |
213 |
| Enzyme 30 Molecular Weight |
23538.5 |
| Enzyme 30 Theoretical pI |
8.13 |
| Enzyme 30 GO Classification |
| Function |
- catalytic activity
- phosphotransferase activity, for other substituted phosphate groups
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
|
|
| Enzyme 30 General Function |
Involved in phosphotransferase activity, for other substituted phosphate groups |
| Enzyme 30 Specific Function |
Not Available |
| Enzyme 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
Not Available |
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
193783603  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
A8K3L7  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
A8K3L7_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>642 bp
ATGCCAGACGAAAATATCTTCCTGTTCGTGCCCAACCTCATCGGTTATGCCCGGATTGTC
TTCGCCATCATTTCTTTCTACTTCATGCCCTGCTGCCCCCTCACGGCCTCCTCCTTCTAC
CTGCTCAGCGGCCTGCTGGACGCTTTCGATGGACACGCTGCTCGCGCTCTTAATCAAGGA
ACCCGGTTTGGGGCCATGCTGGACATGCTGACGGACCGCTGCTCCACCATGTGCCTGTTG
GTCAACCTGGCCCTGCTGTACCCTGGAGCCACGCTGTTCTTCCAAATCAGCATGAGTTTG
GATGTGGCCAGTCACTGGCTGCACCTCCACAGTTCTGTGGTCCGAGGCAGTGAGAGTCAC
AAGATGATCGACTTGTCCGGGAATCCGGTGCTTCGGATCTACTACACCTCGAGGCCTGCT
CTGTTCACCTTGTGTGCTGGGAATGAGCTCTTCTACTGCCTCCTCTACCTGTTCCATTTC
TCTGAGGGACCTTTAGTTGGCTCTGTGGGACTGTTCCGGATGGGCCTCTGGGTCACTGCC
CCCATCGCCTTGCTGAAGTCGCTCATCAGCGTCATCCACCTGATCACGGCCGCCCGCAAC
ATGGCTGCCCTGGACGCAGCAGACCGCGCCAAGAAGAAGTGA
|
| Enzyme 30 GenBank Gene ID |
AK097691  |
| Enzyme 30 GeneCard ID |
CDIPT  |
| Enzyme 30 GenAtlas ID |
CDIPT  |
| Enzyme 30 HGNC ID |
HGNC:1769  |
| Enzyme 30 Chromosome Location |
1 |
| Enzyme 30 Locus |
16p11.2 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 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
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
16422 |
| Enzyme 31 Name |
cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA |
| Enzyme 31 Synonyms |
Not Available |
| Enzyme 31 Gene Name |
Not Available |
| Enzyme 31 Protein Sequence |
>cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
MCPRAARAPATLLLALGAVLWPAAGAWELTILHTNDVHSRLEQTSEDSSKCVNASRCMGG
VARLFTKVQQIRRAEPNVLLLDAGDQYQGTIWFTVYRGAEVAHFMNALRYDAMALGNHEF
DNGVEGLIEPLLKEAKFPILSANIKAKGPLASQISGLYLPYKVLPVGDEVVGIVGYTSKE
TPFLSNPGTNLVFEDEITALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDVVV
GGHSNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKVPVVQAYAFGKYLGYLKIEFDERGNV
ISSHGNPILLNSSIPEDPSIKADINKWRIKLDNYSTQELGKTIVYLDGSSQSCRFRECNM
GNLICDAMINNNLRHTDEMFWNHVSMCILNGGGIRSPIDERNNGTITWENLAAVLPFGGT
FDLVQLKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDLSRKPGDRVVKLDVLCTKCR
VPSYDPLKMDEVYKVILPNFLANGGDGFQMIKDELLRHDSGDQDINVVSTYISKMKVIYP
AVEGRIKFSTGSHCHGSFSLIFLSLWAVIFVLYQ
|
| Enzyme 31 Number of Residues |
574 |
| Enzyme 31 Molecular Weight |
63395.3 |
| Enzyme 31 Theoretical pI |
7.04 |
| Enzyme 31 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- nucleotide binding
|
| 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 catabolic process
- nucleotide metabolic process
|
| Component |
| — |
|
| Enzyme 31 General Function |
Involved in hydrolase activity |
| Enzyme 31 Specific Function |
Not Available |
| Enzyme 31 Pathways |
Not Available |
| Enzyme 31 Reactions |
Not Available |
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
189054446  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
B2RBH2  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
B2RBH2_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>1725 bp
ATGTGTCCCCGAGCCGCGCGGGCGCCCGCGACGCTACTCCTCGCCCTGGGCGCGGTGCTG
TGGCCTGCGGCTGGCGCCTGGGAGCTTACGATTTTGCACACCAACGACGTGCACAGCCGG
CTGGAGCAGACCAGCGAGGACTCCAGCAAGTGCGTCAACGCCAGCCGCTGCATGGGTGGC
GTGGCTCGGCTCTTCACCAAGGTTCAGCAGATCCGCCGCGCCGAACCCAACGTGCTGCTG
CTGGACGCCGGCGACCAGTACCAGGGCACTATCTGGTTCACCGTGTACAGGGGCGCCGAG
GTGGCGCACTTCATGAACGCCCTGCGCTACGATGCCATGGCACTGGGAAATCATGAATTT
GATAATGGTGTGGAAGGACTGATCGAGCCACTCCTCAAAGAGGCCAAATTTCCAATTCTG
AGTGCAAACATTAAAGCAAAGGGGCCACTAGCATCTCAAATATCAGGACTTTATTTGCCA
TATAAAGTTCTTCCTGTTGGTGATGAAGTTGTGGGAATCGTTGGATACACTTCCAAAGAA
ACCCCTTTTCTCTCAAATCCAGGGACAAATTTAGTGTTTGAAGATGAAATCACTGCATTA
CAACCTGAAGTAGATAAGTTAAAAACTCTAAATGTGAACAAAATTATTGCACTGGGACAT
TCGGGTTTTGAAATGGATAAACTCATCGCTCAGAAAGTGAGGGGTGTGGACGTCGTGGTG
GGAGGACACTCCAACACATTTCTTTACACAGGCAATCCACCTTCCAAAGAGGTGCCTGCT
GGGAAGTACCCATTCATAGTCACTTCTGATGATGGGCGGAAGGTTCCTGTAGTCCAGGCC
TATGCTTTTGGCAAATACCTAGGCTATCTGAAGATCGAGTTTGATGAAAGAGGAAACGTC
ATCTCTTCCCATGGAAATCCCATTCTTCTAAACAGCAGCATTCCTGAAGATCCAAGCATA
AAAGCAGACATTAACAAATGGAGGATAAAATTGGATAATTATTCTACCCAGGAATTAGGG
AAAACAATTGTCTATCTGGATGGCTCCTCTCAATCATGCCGCTTTAGAGAATGCAACATG
GGCAACCTGATTTGTGATGCAATGATTAACAACAACCTGAGACACACGGATGAAATGTTC
TGGAACCACGTATCCATGTGCATTTTAAATGGAGGTGGTATCCGGTCGCCCATTGATGAA
CGCAACAATGGCACAATTACCTGGGAGAACCTGGCTGCTGTATTGCCCTTTGGAGGCACA
TTTGACCTAGTCCAGTTAAAAGGTTCCACCCTGAAGAAGGCCTTTGAGCATAGCGTGCAC
CGCTACGGCCAGTCCACTGGAGAGTTCCTGCAGGTGGGCGGAATCCATGTGGTGTATGAT
CTTTCCCGAAAACCTGGAGACAGAGTAGTCAAATTAGATGTTCTTTGCACCAAGTGTCGA
GTGCCCAGTTATGACCCTCTCAAAATGGACGAGGTATATAAGGTGATCCTCCCAAACTTC
CTGGCCAATGGTGGAGATGGGTTCCAGATGATAAAAGATGAATTATTAAGACATGACTCT
GGTGACCAAGATATCAACGTGGTTTCTACATATATCTCCAAAATGAAAGTAATTTATCCA
GCAGTTGAAGGTCGGATCAAGTTTTCCACAGGAAGTCACTGCCATGGAAGCTTTTCTTTA
ATATTTCTTTCACTTTGGGCAGTGATCTTTGTTTTATACCAATAG
|
| Enzyme 31 GenBank Gene ID |
AK314661  |
| Enzyme 31 GeneCard ID |
Not Available |
| Enzyme 31 GenAtlas ID |
Not Available |
| Enzyme 31 HGNC ID |
HGNC:8021  |
| Enzyme 31 Chromosome Location |
Not Available |
| Enzyme 31 Locus |
Not Available |
| Enzyme 31 SNPs |
Not Available |
| Enzyme 31 General References |
Not Available |
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
16437 |
| Enzyme 32 Name |
cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b) |
| Enzyme 32 Synonyms |
Not Available |
| Enzyme 32 Gene Name |
ENTPD3 |
| Enzyme 32 Protein Sequence |
>cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
|
| Enzyme 32 Number of Residues |
529 |
| Enzyme 32 Molecular Weight |
59106 |
| Enzyme 32 Theoretical pI |
6.40 |
| Enzyme 32 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 32 General Function |
Not Available |
| Enzyme 32 Specific Function |
Not Available |
| Enzyme 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
Not Available |
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
Not Available |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
B2R8D0  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
B2R8D0_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
Not Available |
| Enzyme 32 GenBank Gene ID |
AK313322  |
| Enzyme 32 GeneCard ID |
B2R8D0  |
| Enzyme 32 GenAtlas ID |
Not Available |
| Enzyme 32 HGNC ID |
Not Available |
| Enzyme 32 Chromosome Location |
Not Available |
| Enzyme 32 Locus |
Not Available |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
Not Available |
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
16481 |
| Enzyme 33 Name |
cDNA FLJ45393 fis, clone BRHIP3027105, highly similar to CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3- sialyltransferase (EC 2.4.99.-) |
| Enzyme 33 Synonyms |
Not Available |
| Enzyme 33 Gene Name |
Not Available |
| Enzyme 33 Protein Sequence |
>cDNA FLJ45393 fis, clone BRHIP3027105, highly similar to CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3- sialyltransferase (EC 2.4.99.-)
MKCSLRVWFLSVAFLLVFIMSLLFTYSHHSMATLPYLDSGALDGTHRVKLVPGYAGLQRL
SKERLSGKSCACRRCMGDAGASDWFDSHFDGNISPVWTRENMDLPPDVQRWWMMLQPQFK
SHNTNEVLEKLFQIVPGENPYRFRDPHQCRRCAVVGNSGNLRGSGYGQDVDGHNFIMRMN
QAPTVGFEQDVGSRTTHHFMYPESAKNLPANVSFVLVPFKVQDLLWIASALSTGQIRFTY
APVKSFLRVDKEKVQIYNPAFFKYIHDRWTEHHGRYPSTGMLVLFFALHVCDEVNVYGFG
ADSRGNWHHYWENNRYAGEFRKTGVHDADFEAHIIDMLAKASKIEVYRGN
|
| Enzyme 33 Number of Residues |
350 |
| Enzyme 33 Molecular Weight |
40187.5 |
| Enzyme 33 Theoretical pI |
8.47 |
| Enzyme 33 GO Classification |
| Function |
- catalytic activity
- sialyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid glycosylation
- protein modification process
|
| Component |
- cell part
- integral to Golgi membrane
- intrinsic to Golgi membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane part
|
|
| Enzyme 33 General Function |
Involved in sialyltransferase activity |
| Enzyme 33 Specific Function |
Not Available |
| Enzyme 33 Pathways |
Not Available |
| Enzyme 33 Reactions |
Not Available |
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
193785328  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
B3KXG9  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
B3KXG9_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>1053 bp
ATGAAGTGCTCCCTGCGGGTGTGGTTCCTCTCCGTGGCCTTCCTGCTGGTGTTCATCATG
TCCCTGCTCTTCACCTACTCGCACCACAGCATGGCCACGCTCCCCTACCTGGACTCAGGG
GCCCTGGATGGGACGCACCGGGTGAAGCTGGTGCCCGGCTATGCCGGCCTGCAGCGCCTC
AGCAAGGAGAGGCTCTCGGGCAAGAGCTGTGCCTGTCGCCGCTGCATGGGCGATGCCGGT
GCCTCCGACTGGTTTGACAGCCACTTTGACGGTAACATTTCCCCCGTCTGGACCCGAGAG
AACATGGATCTTCCACCGGACGTCCAGAGGTGGTGGATGATGCTGCAGCCCCAGTTCAAG
TCACACAACACCAATGAGGTGCTGGAGAAGCTGTTCCAGATAGTGCCTGGCGAGAACCCC
TACCGCTTCCGGGACCCCCACCAGTGCCGGCGCTGTGCCGTGGTGGGGAACTCGGGCAAC
CTGCGGGGCTCTGGCTATGGGCAGGACGTGGACGGGCACAACTTCATCATGAGGATGAAT
CAGGCGCCAACCGTGGGCTTTGAGCAGGATGTTGGCAGCCGAACCACCCACCATTTCATG
TACCCTGAGAGTGCCAAGAACCTGCCCGCCAACGTCAGCTTCGTGCTGGTGCCCTTCAAG
GTCCAGGACCTTCTGTGGATCGCCAGCGCCTTGTCCACGGGGCAGATCCGATTCACCTAC
GCCCCAGTGAAGTCCTTCCTTCGAGTGGATAAAGAAAAGGTCCAGATCTACAACCCAGCC
TTCTTCAAGTATATCCACGACAGGTGGACAGAGCATCACGGGCGGTACCCTTCCACGGGG
ATGCTGGTGCTTTTCTTTGCCCTGCATGTGTGTGATGAGGTGAACGTGTACGGGTTCGGG
GCCGACAGCCGGGGCAACTGGCACCACTACTGGGAGAACAACCGGTACGCGGGCGAGTTC
CGGAAGACTGGCGTGCACGACGCGGACTTCGAGGCCCACATCATCGACATGCTGGCCAAG
GCCAGCAAGATCGAAGTCTACCGGGGCAACTGA
|
| Enzyme 33 GenBank Gene ID |
AK127322  |
| Enzyme 33 GeneCard ID |
Not Available |
| Enzyme 33 GenAtlas ID |
Not Available |
| Enzyme 33 HGNC ID |
HGNC:10863  |
| Enzyme 33 Chromosome Location |
Not Available |
| Enzyme 33 Locus |
Not Available |
| Enzyme 33 SNPs |
Not Available |
| Enzyme 33 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
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
16482 |
| Enzyme 34 Name |
ST3 beta-galactoside alpha-2,3-sialyltransferase 6, isoform CRA_a |
| Enzyme 34 Synonyms |
- SubName: cDNA, FLJ96071, Homo sapiens alpha2,3-sialyltransferase (ST3GALVI), mRNA
|
| Enzyme 34 Gene Name |
ST3GAL6 |
| Enzyme 34 Protein Sequence |
>ST3 beta-galactoside alpha-2,3-sialyltransferase 6, isoform CRA_a
MRGYLVAIFLSAVFLYYVLHCILWGTNVYWVAPVEMKRRNKIQPCLSKPAFASLLRFHQF
HPFLCAADFRKIASLYGSDKFDLPYGMRTSAEYFRLALSKLQSCDLFDEFDNIPCKKCVV
VGNGGVLKNKTLGEKIDSYDVIIRMNNGPVLGHEEEVGRRTTFRLFYPESVFSDPIHNDP
NTTVILTAFKPHDLRWLLELLMGDKINTNGFWKKPALNLIYKPYQIRILDPFIIRTAAYE
LLHFPKVFPKNQKPKHPTTGIIAITLAFYICHEVHLAGFKYNFSDLKSPLHYYGNATMSL
MNKNAYHNVTAEQLFLKDIIEKNLVINLTQD
|
| Enzyme 34 Number of Residues |
331 |
| Enzyme 34 Molecular Weight |
38214 |
| Enzyme 34 Theoretical pI |
9.30 |
| Enzyme 34 GO Classification |
| Function |
- catalytic activity
- sialyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid glycosylation
- protein modification
|
| Component |
- cell
- integral to Golgi membrane
- intrinsic to Golgi membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane
|
|
| Enzyme 34 General Function |
Not Available |
| Enzyme 34 Specific Function |
Not Available |
| Enzyme 34 Pathways |
Not Available |
| Enzyme 34 Reactions |
Not Available |
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
Not Available |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
B2RCH2  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
B2RCH2_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
Not Available |
| Enzyme 34 GenBank Gene ID |
AK315111  |
| Enzyme 34 GeneCard ID |
B2RCH2  |
| Enzyme 34 GenAtlas ID |
Not Available |
| Enzyme 34 HGNC ID |
Not Available |
| Enzyme 34 Chromosome Location |
Not Available |
| Enzyme 34 Locus |
Not Available |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
Not Available |
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
16483 |
| Enzyme 35 Name |
cDNA FLJ90730 fis, clone PLACE1010011, highly similar to Homo sapiens choline phosphotransferase 1 (CHPT1), mRNA (Choline phosphotransferase 1, isoform CRA_c) |
| Enzyme 35 Synonyms |
Not Available |
| Enzyme 35 Gene Name |
CHPT1 |
| Enzyme 35 Protein Sequence |
>cDNA FLJ90730 fis, clone PLACE1010011, highly similar to Homo sapiens choline phosphotransferase 1 (CHPT1), mRNA (Choline phosphotransferase 1, isoform CRA_c)
MAAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLW
MAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARR
TNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYV
SGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSC
SNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILM
FGCVFAKVSQKLVVAHMTKSELYLQDTVFLGPGLLFLDQYFNNFIDEYVVLWMAMVISSF
DMVIYFSALCLQISRHLHLNIFKTACHQAPEQVQVLSSKSHQNNMD
|
| Enzyme 35 Number of Residues |
406 |
| Enzyme 35 Molecular Weight |
45097 |
| Enzyme 35 Theoretical pI |
6.92 |
| Enzyme 35 GO Classification |
| Function |
| — |
| Process |
- cellular lipid metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- phospholipid biosynthesis
- phospholipid metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 35 General Function |
Lipid transport and metabolism |
| Enzyme 35 Specific Function |
Not Available |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
Not Available |
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
Not Available |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
B3KQM2  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
B3KQM2_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
Not Available |
| Enzyme 35 GenBank Gene ID |
AK075211  |
| Enzyme 35 GeneCard ID |
B3KQM2  |
| Enzyme 35 GenAtlas ID |
Not Available |
| Enzyme 35 HGNC ID |
Not Available |
| Enzyme 35 Chromosome Location |
12 |
| Enzyme 35 Locus |
12q |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
Not Available |
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
16484 |
| Enzyme 36 Name |
cDNA, FLJ94713 (Putative uncharacterized protein MGC26963) |
| Enzyme 36 Synonyms |
Not Available |
| Enzyme 36 Gene Name |
MGC26963 |
| Enzyme 36 Protein Sequence |
>cDNA, FLJ94713 (Putative uncharacterized protein MGC26963)
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYI
QIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDY
IDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLP
VPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFI
KEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNL
KVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGED
NEKST
|
| Enzyme 36 Number of Residues |
365 |
| Enzyme 36 Molecular Weight |
42281 |
| Enzyme 36 Theoretical pI |
9.00 |
| Enzyme 36 GO Classification |
Not Available |
| Enzyme 36 General Function |
Not Available |
| Enzyme 36 Specific Function |
Not Available |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
Not Available |
| Enzyme 36 Pfam Domain Function |
Not Available |
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
Not Available |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
B2RA61  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
B2RA61_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
Not Available |
| Enzyme 36 GenBank Gene ID |
AK314049  |
| Enzyme 36 GeneCard ID |
B2RA61  |
| Enzyme 36 GenAtlas ID |
Not Available |
| Enzyme 36 HGNC ID |
Not Available |
| Enzyme 36 Chromosome Location |
Not Available |
| Enzyme 36 Locus |
Not Available |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
Not Available |
| Enzyme 36 Metabolite References |
Not Available |