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Enzyme 1
[top]
|
| Enzyme 1 ID |
5235 |
| Enzyme 1 Name |
Deoxycytidine kinase |
| Enzyme 1 Synonyms |
- dCK
|
| Enzyme 1 Gene Name |
DCK |
| Enzyme 1 Protein Sequence |
>Deoxycytidine kinase
MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCN
VQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAE
KPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQA
TPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNE
DFKDKYESLVEKVKEFLSTL
|
| Enzyme 1 Number of Residues |
260 |
| Enzyme 1 Molecular Weight |
30518.3 |
| Enzyme 1 Theoretical pI |
4.88 |
| Enzyme 1 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in ATP binding |
| Enzyme 1 Specific Function |
Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- NTP + deoxycytidine = NDP + dCMP [RN:R02321]
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| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P27707  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
DCK_HUMAN |
| Enzyme 1 PDB ID |
1P62 |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>783 bp
ATGGCCACCCCGCCCAAGAGAAGCTGCCCGTCTTTCTCAGCCAGCTCTGAGGGGACCCGC
ATCAAGAAAATCTCCATCGAAGGGAACATCGCTGCAGGGAAGTCAACATTTGTGAATATC
CTTAAACAATTGTGTGAAGATTGGGAAGTGGTTCCTGAACCTGTTGCCAGATGGTGCAAT
GTTCAAAGTACTCAAGATGAATTTGAGGAACTTACAATGTCTCAGAAAAATGGTGGGAAT
GTTCTTCAGATGATGTATGAGAAACCTGAACGATGGTCTTTTACCTTCCAAACATATGCC
TGTCTCAGTCGAATAAGAGCTCAGCTTGCCTCTCTGAATGGCAAGCTCAAAGATGCAGAG
AAACCTGTATTATTTTTTGAACGATCTGTGTATAGTGACAGGTATATTTTTGCATCTAAT
TTGTATGAATCTGAATGCATGAATGAGACAGAGTGGACAATTTATCAAGACTGGCATGAC
TGGATGAATAACCAATTTGGCCAAAGCCTTGAATTGGATGGAATCATTTATCTTCAAGCC
ACTCCAGAGACATGCTTACATAGAATATATTTACGGGGAAGAAATGAAGAGCAAGGCATT
CCTCTTGAATATTTAGAGAAGCTTCATTATAAACATGAAAGCTGGCTCCTGCATAGGACA
CTGAAAACCAACTTCGATTATCTTCAAGAGGTGCCTATCTTAACACTGGATGTTAATGAA
GACTTTAAAGACAAATATGAAAGTCTGGTTGAAAAGGTCAAAGAGTTTTTGAGTACTTTG
TGA
|
| Enzyme 1 GenBank Gene ID |
M60527 |
| Enzyme 1 GeneCard ID |
DCK |
| Enzyme 1 GenAtlas ID |
DCK |
| Enzyme 1 HGNC ID |
HGNC:2704 |
| Enzyme 1 Chromosome Location |
4 |
| Enzyme 1 Locus |
4q13.3-q21.1 |
| Enzyme 1 SNPs |
SNPJam Report |
| Enzyme 1 General References |
- Chottiner EG, Shewach DS, Datta NS, Ashcraft E, Gribbin D, Ginsburg D, Fox IH, Mitchell BS: Cloning and expression of human deoxycytidine kinase cDNA. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1531-5. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Eriksson S, Cederlund E, Bergman T, Jornvall H, Bohman C: Characterization of human deoxycytidine kinase. Correlation with cDNA sequences. FEBS Lett. 1991 Mar 25;280(2):363-6. [PubMed ]
- Johansson M, Brismar S, Karlsson A: Human deoxycytidine kinase is located in the cell nucleus. Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11941-5. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Sabini E, Ort S, Monnerjahn C, Konrad M, Lavie A: Structure of human dCK suggests strategies to improve anticancer and antiviral therapy. Nat Struct Biol. 2003 Jul;10(7):513-9. [PubMed ]
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| Enzyme 1 Metabolite References |
Not Available |
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Enzyme 2
[top]
|
| Enzyme 2 ID |
5239 |
| Enzyme 2 Name |
ATP-citrate synthase |
| Enzyme 2 Synonyms |
- ATP-citrate (pro-S-)-lyase
- Citrate cleavage enzyme
|
| Enzyme 2 Gene Name |
ACLY |
| Enzyme 2 Protein Sequence |
>ATP-citrate synthase
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPD
QLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFY
VCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEI
LASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPP
PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNE
LANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRA
IRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALG
HRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVP
SPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQK
FYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEG
IPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYV
SRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG
GTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALK
EAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASF
MTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADH
GPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFV
NKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPN
LILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLK
QGLYRHPWDDISYVLPEHMSM
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| Enzyme 2 Number of Residues |
1101 |
| Enzyme 2 Molecular Weight |
120838.3 |
| Enzyme 2 Theoretical pI |
7.34 |
| Enzyme 2 GO Classification |
| Function |
- ATP binding
- ATP citrate synthase activity
- CoA-ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- nucleoside binding
- purine nucleoside binding
- succinate-CoA ligase (ADP-forming) activity
- succinate-CoA ligase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
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| Process |
- carbohydrate metabolic process
- cellular carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 2 General Function |
Involved in ATP citrate synthase activity |
| Enzyme 2 Specific Function |
ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA [RN:R00352]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
13623199 |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P53396 |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ACLY_HUMAN |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>3306 bp
ATGTCGGCCAAGGCAATTTCAGAGCAGACGGGCAAAGAACTCCTTTACAAGTTCATCTGT
ACCACCTCAGCCATCCAGAATCGGTTCAAGTATGCTCGGGTCACTCCTGACACAGACTGG
GCCCGCTTGCTGCAGGACCACCCCTGGCTGCTCAGCCAGAACTTGGTAGTCAAGCCAGAC
CAGCTGATCAAACGTCGTGGAAAACTTGGTCTCGTTGGGGTCAACCTCACTCTGGATGGG
GTCAAGTCCTGGCTGAAGCCACGGCTGGGACAGGAAGCCACAGTTGGCAAGGCCACAGGC
TTCCTCAAGAACTTTCTGATCGAGCCCTTCGTCCCCCACAGTCAGGCTGAGGAGTTCTAT
GTCTGCATCTATGCCACCCGAGAAGGGGACTACGTCCTGTTCCACCACGAGGGGGGTGTG
GACGTGGGTGATGTGGACGCCAAGGCCCAGAAGCTGCTTGTTGGCGTGGATGAGAAACTG
AATCCTGAGGACATCAAAAAACACCTGTTGGTCCACGCCCCTGAAGACAAGAAAGAAATT
CTGGCCAGTTTTATCTCCGGCCTCTTCAATTTCTACGAGGACTTGTACTTCACCTACCTC
GAGATCAATCCCCTTGTAGTGACCAAAGATGGAGTCTATGTCCTTGACTTGGCGGCCAAG
GTGGACGCCACTGCCGACTACATCTGCAAAGTGAAGTGGGGTGACATCGAGTTCCCTCCC
CCCTTCGGGCGGGAGGCATATCCAGAGGAAGCCTACATTGCAGACCTCGATGCCAAAAGT
GGGGCAAGCCTGAAGCTGACCTTGCTGAACCCCAAAGGGAGGATCTGGACCATGGTGGCC
GGGGGTGGCGCCTCTGTCGTGTACAGCGATACCATCTGTGATCTAGGGGGTGTCAACGAG
CTGGCAAACTATGGGGAGTACTCAGGCGCCCCCAGCGAGCAGCAGACCTATGACTATGCC
AAGACTATCCTCTCCCTCATGACCCGAGAGAAGCACCCAGATGGCAAGATCCTCATCATT
GGAGGCAGCATCGCAAACTTCACCAACGTGGCTGCCACGTTCAAGGGCATCGTGAGAGCA
ATTCGAGATTACCAGGGCCCCCTGAAGGAGCACGAAGTCACAATCTTTGTCCGAAGAGGT
GGCCCCAACTATCAGGAGGGCTTACGGGTGATGGGAGAAGTCGGGAAGACCACTGGGATC
CCCATCCATGTCTTTGGCACAGAGACTCACATGACGGCCATTGTGGGCATGGCCCTGGGC
CACCGGCCCATCCCCAACCAGCCACCCACAGCGGCCCACACTGCAAACTTCCTCCTCAAC
GCCAGCGGGAGCACATCGACGCCAGCCCCCAGCAGGACAGCATCTTTTTCTGAGTCCAGG
GCCGATGAGGTGGCGCCTGCAAAGAAGGCCAAGCCTGCCATGCCACAAGATTCAGTCCCA
AGTCCAAGATCCCTGCAAGGAAAGAGCACCACCCTCTTCAGCCGCCACACCAAGGCCATT
GTGTGGGGCATGCAGACCCGGGCCGTGCAAGGCATGCTGGACTTTGACTATGTCTGCTCC
CGAGACGAGCCCTCAGTGGCTGCCATGGTCTACCCTTTCACTGGGGACCACAAGCAGAAG
TTTTACTGGGGGCACAAAGAGATCCTGATCCCTGTCTTCAAGAACATGGCTGATGCCATG
AGGAAGCATCCGGAGGTAGATGTGCTCATCAACTTTGCCTCTCTCCGCTCTGCCTATGAC
AGCACCATGGAGACCATGAACTATGCCCAGATCCGGACCATCGCCATCATAGCTGAAGGC
ATCCCTGAGGCCCTCACGAGAAAGCTGATCAAGAAGGCGGACCAGAAGGGAGTGACCATC
ATCGGACCTGCCACTGTTGGAGGCATCAAGCCTGGGTGCTTTAAGATTGGCAACACAGGT
GGGATGCTGGACAACATCCTGGCCTCCAAACTGTACCGCCCAGGCAGCGTGGCCTATGTC
TCACGTTCCGGAGGCATGTCCAACGAGCTCAACAATATCATCTCTCGGACCACGGATGGC
GTCTATGAGGGCGTGGCCATTGGTGGGGACAGGTACCCGGGCTCCACATTCATGGATCAT
GTGTTACGCTATCAGGACACTCCAGGAGTCAAAATGATTGTGGTTCTTGGAGAGATTGGG
GGCACTGAGGAATATAAGATTTGCCGGGGCATCAAGGAGGGCCGCCTCACTAAGCCCATC
GTCTGCTGGTGCATCGGGACGTGTGCCACCATGTTCTCCTCTGAGGTCCAGTTTGGCCAT
GCTGGAGCTTGTGCCAACCAGGCTTCTGAAACTGCAGTAGCCAAGAACCAGGCTTTGAAG
GAAGCAGGAGTGTTTGTGCCCCGGAGCTTTGATGAGCTTGGAGAGATCATCCAGTCTGTA
TACGAAGATCTCGTGGCCAATGGAGTCATTGTACCTGCCCAGGAGGTGCCGCCCCCAACC
GTGCCCATGGACTACTCCTGGGCCAGGGAGCTTGGTTTGATCCGCAAACCTGCCTCGTTC
ATGACCAGCATCTGCGATGAGCGAGGACAGGAGCTCATCTACGCGGGCATGCCCATCACT
GAGGTCTTCAAGGAAGAGATGGGCATTGGCGGGGTCCTCGGCCTCCTCTGGTTCCAGAAA
AGGTTGCCTAAGTACTCTTGCCAGTTCATTGAGATGTGTCTGATGGTGACAGCTGATCAC
GGGCCAGCCGTCTCTGGAGCCCACAACACCATCATTTGTGCGCGAGCTGGGAAAGACCTG
GTCTCCAGCCTCACCTCGGGGCTGCTCACCATCGGGGATCGGTTTGGGGGTGCCTTGGAT
GCAGCAGCCAAGATGTTCAGTAAAGCCTTTGACAGTGGCATTATCCCCATGGAGTTTGTG
AACAAGATGAAGAAGGAAGGGAAGCTGATCATGGGCATTGGTCACCGAGTGAAGTCGATA
AACAACCCAGACATGCGAGTGCAGATCCTCAAAGATTACGTCAGGCAGCACTTCCCTGCC
ACTCCTCTGCTCGATTATGCACTGGAAGTAGAGAAGATTACCACCTCGAAGAAGCCAAAT
CTTATCCTGAATGTAGATGGTCTCATCGGAGTCGCATTTGTAGACATGCTTAGAAACTGT
GGGTCCTTTACTCGGGAGGAAGCTGATGAATATATTGACATTGGAGCCCTCAATGGCATC
TTTGTGCTGGGAAGGAGTATGGGGTTCATTGGACACTATCTTGATCAGAAGAGGCTGAAG
CAGGGGCTGTATCGTCATCCGTGGGATGATATTTCATATGTTCTTCCGGAACACATGAGC
ATGTAA
|
| Enzyme 2 GenBank Gene ID |
BC006195 |
| Enzyme 2 GeneCard ID |
ACLY |
| Enzyme 2 GenAtlas ID |
ACLY |
| Enzyme 2 HGNC ID |
HGNC:115 |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
17q21.2 |
| Enzyme 2 SNPs |
SNPJam Report |
| Enzyme 2 General References |
- Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS: Cloning and expression of a human ATP-citrate lyase cDNA. Eur J Biochem. 1992 Mar 1;204(2):491-9. [PubMed ]
- Lord KA, Wang XM, Simmons SJ, Bruckner RC, Loscig J, O'Connor B, Bentley R, Smallwood A, Chadwick CC, Stevis PE, Ciccarelli RB: Variant cDNA sequences of human ATP:citrate lyase: cloning, expression, and purification from baculovirus-infected insect cells. Protein Expr Purif. 1997 Feb;9(1):133-41. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5247 |
| Enzyme 3 Name |
Acetyl-CoA carboxylase 2 |
| Enzyme 3 Synonyms |
- ACC-beta
- Biotin carboxylase
|
| Enzyme 3 Gene Name |
ACACB |
| Enzyme 3 Protein Sequence |
>Acetyl-CoA carboxylase 2
MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQR
NGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGT
GTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSV
AGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHR
DFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVT
PEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKL
PELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGK
RISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQV
QSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAP
LAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNL
PAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDE
GFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVA
LKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGAL
NVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIM
NGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSP
SAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVAR
LELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIK
LKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFP
SQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRV
EHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSD
ELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCP
ENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCV
VEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTR
NFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVP
ILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQL
ELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEY
LQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGS
RLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSF
GNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPK
DILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIG
SFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFK
YLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSL
AYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQL
GGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSR
APYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVE
TRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAVKDFNREKLPLMIFANWRGF
SGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYA
DKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLK
AREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVK
QEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIR
ENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST
|
| Enzyme 3 Number of Residues |
2458 |
| Enzyme 3 Molecular Weight |
276538.6 |
| Enzyme 3 Theoretical pI |
6.46 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- CoA carboxylase activity
- acetyl-CoA carboxylase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-carbon bonds
- nucleoside binding
- purine nucleoside binding
- vitamin binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid biosynthetic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in acetyl-CoA carboxylase activity |
| Enzyme 3 Specific Function |
ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA [RN:R00742]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
134142062 |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O00763 |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
ACACB_HUMAN |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>7377 bp
ATGGTCTTGCTTCTTTGTCTATCTTGTCTGATTTTCTCCTGTCTGACCTTTTCCTGGTTA
AAAATCTGGGGGAAAATGACGGACTCCAAGCCGATCACCAAGAGTAAATCAGAAGCAAAC
CTCATCCCGAGCCAGGAGCCCTTTCCAGCCTCTGATAACTCAGGGGAGACACCGCAGAGA
AATGGGGAGGGCCACACTCTGCCCAAGACACCCAGCCAGGCCGAGCCAGCCTCCCACAAA
GGCCCCAAAGATGCCGGTCGGCGGAGAAACTCCCTACCACCCTCCCACCAGAAGCCCCCA
AGAAACCCCCTTTCTTCCAGTGACGCAGCACCCTCCCCAGAGCTTCAAGCCAACGGGACT
GGGACACAAGGTCTGGAGGCCACAGATACCAATGGCCTGTCCTCCTCAGCCAGGCCCCAG
GGCCAGCAAGCTGGCTCCCCCTCCAAAGAAGACAAGAAGCAGGCAAACATCAAGAGGCAG
CTGATGACCAACTTCATCCTGGGCTCTTTTGATGACTACTCCTCCGACGAGGACTCTGTT
GCTGGCTCATCTCGTGAGTCTACCCGGAAGGGCAGCCGGGCCAGCTTGGGGGCCCTGTCC
CTGGAGGCTTATCTGACCACAGGTGAAGCTGAGACCCGCGTCCCCACTATGAGGCCGAGC
ATGTCGGGACTCCACCTGGTGAAGAGGGGACGGGAACACAAGAAGCTGGACCTGCACAGA
GACTTTACCGTGGCTTCTCCCGCTGAGTTTGTCACACGCTTTGGGGGGGATCGGGTCATC
GAGAAGGTGCTTATTGCCAACAACGGGATTGCCGCCGTGAAGTGCATGCGCTCCATCCGC
AGGTGGGCCTATGAGATGTTCCGCAACGAGCGGGCCATCCGGTTTGTTGTGATGGTGACC
CCCGAGGACCTTAAGGCCAACGCAGAGTACATCAAGATGGCGGATCATTACGTCCCCGTC
CCAGGAGGGCCCAATAACAACAACTATGCCAACGTGGAGCTGATTGTGGACATTGCCAAG
AGAATCCCCGTGCAGGCGGTGTGGGCTGGCTGGGGCCATGCTTCAGAAAACCCTAAACTT
CCGGAGCTGCTGTGCAAGAATGGAGTTGCTTTCTTAGGCCCTCCCAGTGAGGCCATGTGG
GCCTTAGGAGATAAGATCGCCTCCACCGTTGTCGCCCAGACGCTACAGGTCCCAACCCTG
CCCTGGAGTGGAAGCGGCCTGACAGTGGAGTGGACAGAAGATGATCTGCAGCAGGGAAAA
AGAATCAGTGTCCCAGAAGATGTTTATGACAAGGGTTGCGTGAAAGACGTAGATGAGGGC
TTGGAGGCAGCAGAAAGAATTGGTTTTCCATTGATGATCAAAGCTTCTGAAGGTGGCGGA
GGGAAGGGAATCCGGAAGGCTGAGAGTGCGGAGGACTTCCCGATCCTTTTCAGACAAGTA
CAGAGTGAGATCCCAGGCTCGCCCATCTTTCTCATGAAGCTGGCCCAGCACGCCCGTCAC
CTGGAAGTTCAGATCCTCGCTGACCAGTATGGGAATGCTGTGTCTCTGTTTGGTCGCGAC
TGCTCCATCCAGCGGCGGCATCAGAAGATCGTTGAGGAAGCACCGGCCACCATCGCCCCG
CTGGCCATATTCGAGTTCATGGAGCAGTGTGCCATCCGCCTGGCCAAGACCGTGGGCTAT
GTGAGTGCAGGGACAGTGGAATACCTCTATAGTCAGGATGGCAGCTTCCACTTCTTGGAG
CTGAATCCTCGCTTGCAGGTGGAACATCCCTGCACAGAAATGATTGCTGATGTTAATCTG
CCGGCCGCCCAGCTACAGATCGCCATGGGCGTGCCACTGCACCGGCTGAAGGATATCCGG
CTTCTGTATGGAGAGTCACCATGGGGAGTGACTCCCATTTCTTTTGAAACCCCCTCAAAC
CCTCCCCTCGCCCGAGGCCACGTCATTGCCGCCAGAATCACCAGCGAAAACCCAGACGAG
GGTTTTAAGCCGAGCTCCGGGACTGTCCAGGAACTGAATTTCCGGAGCAGCAAGAACGTG
TGGGGTTACTTCAGCGTGGCCGCTACTGGAGGCCTGCACGAGTTTGCGGATTCCCAATTT
GGGCACTGCTTCTCCTGGGGAGAGAACCGGGAAGAGGCCATTTCGAACATGGTGGTGGCT
TTGAAGGAACTGTCCATCCGAGGCGACTTTAGGACTACCGTGGAATACCTCATTAACCTC
CTGGAGACCGAGAGCTTCCAGAACAACGACATCGACACCGGGTGGTTGGACTACCTCATT
GCTGAGAAAGTGCAGGCGGAGAAACCGGATATCATGCTTGGGGTGGTATGCGGGGCCTTG
AACGTGGCCGATGCGATGTTCAGAACGTGCATGACAGATTTCTTACACTCCCTGGAAAGG
GGCCAGGTCCTCCCAGCGGATTCACTACTGAACCTCGTAGATGTGGAATTAATTTACGGA
GGTGTTAAGTACATTCTCAAGGTGGCCCGGCAGTCTCTGACCATGTTCGTTCTCATCATG
AATGGCTGCCACATCGAGATTGATGCCCACCGGCTGAATGATGGGGGGCTCCTGCTCTCC
TACAATGGGAACAGCTACACCACCTACATGAAGGAAGAGGTTGACAGTTACCGAATTACC
ATCGGCAATAAGACGTGTGTGTTTGAGAAGGAGAACGATCCTACAGTCCTGAGATCCCCC
TCGGCTGGGAAGCTGACACAGTACACAGTGGAGGATGGGGGCCACGTTGAGGCTGGGAGC
AGCTACGCTGAGATGGAGGTGATGAAGATGATCATGACCCTGAACGTTCAGGAAAGAGGC
CGGGTGAAGTACATCAAGCGTCCAGGTGCCGTGCTGGAAGCAGGCTGCGTGGTGGCCAGG
CTGGAGCTCGATGACCCTTCTAAAGTCCACCCGGCTGAACCGTTCACAGGAGAACTCCCT
GCCCAGCAGACACTGCCCATCCTCGGAGAGAAACTGCACCAGGTCTTCCACAGCGTCCTG
GAAAACCTCACCAACGTCATGAGTGGCTTTTGTCTGCCAGAGCCCGTTTTTAGCATAAAG
CTGAAGGAGTGGGTGCAGAAGCTCATGATGACCCTCCGGCACCCGTCACTGCCGCTGCTG
GAGCTGCAGGAGATCATGACCAGCGTGGCAGGCCGCATCCCCGCCCCTGTGGAGAAGTCT
GTCCGCAGGGTGATGGCCCAGTATGCCAGCAACATCACCTCGGTGCTGTGCCAGTTCCCC
AGCCAGCAGATAGCCACCATCCTGGACTGCCATGCAGCCACCCTGCAGCGGAAGGCTGAT
CGAGAGGTCTTCTTCATCAACACCCAGAGCATCGTGCAGTTGGTCCAGAGATACCGCAGC
GGGATCCGCGGCTATATGAAAACAGTGGTGTTGGATCTCCTGAGAAGATACTTGCGTGTT
GAGCACCATTTTCAGCAAGCCCACTACGACAAGTGTGTGATAAACCTCAGGGAGCAGTTC
AAGCCAGACATGTCCCAGGTGCTGGACTGCATCTTCTCCCACGCACAGGTGGCCAAGAAG
AACCAGCTGGTGATCATGTTGATCGATGAGCTGTGTGGCCCAGACCCTTCCCTGTCGGAC
GAGCTGATCTCCATCCTCAACGAGCTCACTCAGCTGAGCAAAAGCGAGCACTGCAAAGTG
GCCCTCAGAGCCCGGCAGATCCTGATTGCCTCCCACCTCCCCTCCTACGAGCTGCGGCAT
AACCAGGTGGAGTCCATTTTCCTGTCTGCCATTGACATGTACGGCCACCAGTTCTGCCCC
GAGAACCTCAAGAAATTAATACTTTCGGAAACAACCATCTTCGACGTCCTGCCTACTTTC
TTCTATCACGCAAACAAAGTCGTGTGCATGGCGTCCTTGGAGGTTTACGTGCGGAGGGGC
TACATCGCCTATGAGTTAAACAGCCTGCAGCACCGGCAGCTCCCGGACGGCACCTGCGTG
GTAGAATTCCAGTTCATGCTGCCGTCCTCCCACCCAAACCGGATGACCGTGCCCATCAGC
ATCACCAACCCTGACCTGCTGAGGCACAGCACAGAGCTCTTCATGGACAGCGGCTTCTCC
CCACTGTGCCAGCGCATGGGAGCCATGGTAGCCTTCAGGAGATTCGAGGACTTCACCAGA
AATTTTGATGAAGTCATCTCTTGCTTCGCCAACGTGCCCAAAGACACCCCCCTCTTCAGC
GAGGCCCGCACCTCCCTATACTCCGAGGATGACTGCAAGAGCCTCAGAGAAGAGCCCATC
CACATTCTGAATGTGTCCATCCAGTGTGCAGACCACCTGGAGGATGAGGCACTGGTGCCG
ATTTTACGGACATTCGTACAGTCCAAGAAAAATATCCTTGTGGATTATGGACTCCGACGA
ATCACATTCTTGATTGCCCAAGAGAAAGAATTTCCCAAGTTTTTCACATTCAGAGCAAGA
GATGAGTTTGCAGAAGATCGCATTTACCGTCACTTGGAACCTGCCCTGGCCTTCCAGCTG
GAACTTAACCGGATGCGTAACTTCGATCTGACCGCCGTGCCCTGTGCCAACCACAAGATG
CACCTTTACCTGGGTGCTGCCAAGGTGAAGGAAGGTGTGGAAGTGACGGACCATAGGTTC
TTCATCCGCGCCATCATCAGGCACTCTGACCTGATCACAAAGGAAGCCTCCTTCGAATAC
CTGCAGAACGAGGGTGAGCGGCTGCTCCTGGAGGCCATGGACGAGCTGGAGGTGGCGTTC
AATAACACCAGCGTGCGCACCGACTGCAACCACATCTTCCTCAACTTCGTGCCCACTGTC
ATCATGGACCCCTTCAAGATCGAGGAGTCCGTGCGCTACATGGTTATGCGCTACGGCAGC
CGGCTGTGGAAACTCCGTGTGCTACAGGCTGAGGTCAAGATCAACATCCGCCAGACCACC
ACCGGCAGTGCCGTTCCCATCCGCCTGTTCATCACCAATGAGTCGGGCTACTACCTGGAC
ATCAGCCTCTACAAAGAAGTGACTGACTCCAGATCTGGAAATATCATGTTTCACTCCTTC
GGCAACAAGCAAGGGCCCCAGCACGGGATGCTGATCAATACTCCCTACGTCACCAAGGAT
CTGCTCCAGGCCAAGCGATTCCAGGCCCAGACCCTGGGAACCACCTACATCTATGACTTC
CCGGAAATGTTCAGGCAGGCTCTCTTTAAACTGTGGGGCTCCCCAGACAAGTATCCCAAA
GACATCCTGACATACACTGAATTAGTGTTGGACTCTCAGGGCCAGCTGGTGGAGATGAAC
CGACTTCCTGGTGGAAATGAGGTGGGCATGGTGGCCTTCAAAATGAGGTTTAAGACCCAG
GAGTACCCGGAAGGACGGGATGTGATCGTCATCGGCAATGACATCACCTTTCGCATTGGA
TCCTTTGGCCCTGGAGAGGACCTTCTGTACCTGCGGGCATCCGAGATGGCCCGGGCAGAG
GGCATTCCCAAAATTTACGTGGCAGCCAACAGTGGCGCCCGTATTGGCATGGCAGAGGAG
ATCAAACACATGTTCCACGTGGCTTGGGTGGACCCAGAAGACCCCCACAAAGGATTTAAA
TACCTGTACCTGACTCCCCAAGACTACACCAGAATCAGCTCCCTGAACTCCGTCCACTGT
AAACACATCGAGGAAGGAGGAGAGTCCAGATACATGATCACGGATATCATCGGGAAGGAT
GATGGCTTGGGCGTGGAGAATCTGAGGGGCTCAGGCATGATTGCTGGGGAGTCCTCTCTG
GCTTACGAAGAGATCGTCACCATTAGCTTGGTGACCTGCCGAGCCATTGGGATTGGGGCC
TACTTGGTGAGGCTGGGCCAGCGAGTGATCCAGGTGGAGAATTCCCACATCATCCTCACA
GGAGCAAGTGCTCTCAACAAGGTCCTGGGAAGAGAGGTCTACACATCCAACAACCAGCTG
GGTGGCGTTCAGATCATGCATTACAATGGTGTCTCCCACATCACCGTGCCAGATGACTTT
GAGGGGGTTTATACCATCCTGGAGTGGCTGTCCTATATGCCAAAGGATAATCACAGCCCT
GTCCCTATCATCACACCCACTGACCCCATTGACAGAGAAATTGAATTCCTCCCATCCAGA
GCTCCCTACGACCCCCGGTGGATGCTTGCAGGAAGGCCTCACCCAACTCTGAAGGGAACG
TGGCAGAGCGGATTCTTTGACCACGGCAGTTTCAAGGAAATCATGGCACCCTGGGCGCAG
ACCGTGGTGACAGGACGAGCAAGGCTTGGGGGGATTCCCGTGGGAGTGATTGCTGTGGAG
ACACGGACTGTGGAGGTGGCAGTCCCTGCAGACCCTGCCAACCTGGATTCTGAGGCCAAG
ATAATTCAGCAGGCAGGACAGGTGTGGTTCCCAGACTCAGCCTACAAAACCGCCCAGGCC
GTCAAGGACTTCAACCGGGAGAAGTTGCCCCTGATGATCTTTGCCAACTGGAGGGGGTTC
TCCGGTGGCATGAAAGACATGTATGACCAGGTGCTGAAGTTTGGAGCCTACATCGTGGAC
GGCCTTAGACAATACAAACAGCCCATCCTGATCTATATCCCGCCCTATGCGGAGCTCCGG
GGAGGCTCCTGGGTGGTCATAGATGCCACCATCAACCCGCTGTGCATAGAAATGTATGCA
GACAAAGAGAGCAGGGGTGGTGTTCTGGAACCAGAGGGGACAGTGGAGATTAAGTTCCGA
AAGAAAGATCTGATAAAGTCCATGAGAAGGATCGATCCAGCTTACAAGAAGCTCATGGAA
CAGCTAGGGGAACCTGATCTCTCCGACAAGGACCGAAAGGACCTGGAGGGCCGGCTAAAG
GCTCGCGAGGACCTGCTGCTCCCCATCTACCACCAGGTGGCGGTGCAGTTCGCCGACTTC
CATGACACACCCGGCCGGATGCTGGAGAAGGGCGTCATATCTGACATCCTGGAGTGGAAG
ACCGCACGCACCTTCCTGTATTGGCGTCTGCGCCGCCTCCTCCTGGAGGACCAGGTCAAG
CAGGAGATCCTGCAGGCCAGCGGGGAGCTGAGTCACGTGCATATCCAGTCCATGCTGCGT
CGCTGGTTCGTGGAGACGGAGGGGGCTGTCAAGGCCTACTTGTGGGACAACAACCAGGTG
GTTGTGCAGTGGCTGGAACAGCACTGGCAGGCAGGGGATGGCCCGCGCTCCACCATCCGT
GAGAACATCACGTACCTGAAGCACGACTCTGTCCTCAAGACCATCCGAGGCCTGGTTGAA
GAAAACCCCGAGGTGGCCGTGGACTGTGTGATATACCTGAGCCAGCACATCAGCCCAGCT
GAGCGGGCGCAGGTCGTTCACCTGCTGTCTACCATGGACAGCCCGGCCTCCACCTGA
|
| Enzyme 3 GenBank Gene ID |
NM_001093.3 |
| Enzyme 3 GeneCard ID |
ACACB |
| Enzyme 3 GenAtlas ID |
ACACB |
| Enzyme 3 HGNC ID |
HGNC:85 |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
12q24.11 |
| Enzyme 3 SNPs |
SNPJam Report |
| Enzyme 3 General References |
- Abu-Elheiga L, Almarza-Ortega DB, Baldini A, Wakil SJ: Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms. J Biol Chem. 1997 Apr 18;272(16):10669-77. [PubMed ]
- Cheng D, Chu CH, Chen L, Feder JN, Mintier GA, Wu Y, Cook JW, Harpel MR, Locke GA, An Y, Tamura JK: Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes. Protein Expr Purif. 2007 Jan;51(1):11-21. Epub 2006 Jun 10. [PubMed ]
- Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed ]
- Widmer J, Fassihi KS, Schlichter SC, Wheeler KS, Crute BE, King N, Nutile-McMenemy N, Noll WW, Daniel S, Ha J, Kim KH, Witters LA: Identification of a second human acetyl-CoA carboxylase gene. Biochem J. 1996 Jun 15;316 ( Pt 3):915-22. [PubMed ]
- Cho YS, Lee JI, Shin D, Kim HT, Cheon YH, Seo CI, Kim YE, Hyun YL, Lee YS, Sugiyama K, Park SY, Ro S, Cho JM, Lee TG, Heo YS: Crystal structure of the biotin carboxylase domain of human acetyl-CoA carboxylase 2. Proteins. 2008 Jan 1;70(1):268-72. [PubMed ]
- Jones S, Zhang X, Parsons DW, Lin JC, Leary RJ, Angenendt P, Mankoo P, Carter H, Kamiyama H, Jimeno A, Hong SM, Fu B, Lin MT, Calhoun ES, Kamiyama M, Walter K, Nikolskaya T, Nikolsky Y, Hartigan J, Smith DR, Hidalgo M, Leach SD, Klein AP, Jaffee EM, Goggins M, Maitra A, Iacobuzio-Donahue C, Eshleman JR, Kern SE, Hruban RH, Karchin R, Papadopoulos N, Parmigiani G, Vogelstein B, Velculescu VE, Kinzler KW: Core signaling pathways in human pancreatic cancers revealed by global genomic analyses. Science. 2008 Sep 26;321(5897):1801-6. Epub 2008 Sep 4. [PubMed ]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5248 |
| Enzyme 4 Name |
Pyruvate carboxylase, mitochondrial |
| Enzyme 4 Synonyms |
- Pyruvic carboxylase
- PCB
|
| Enzyme 4 Gene Name |
PC |
| Enzyme 4 Protein Sequence |
>Pyruvate carboxylase, mitochondrial
MLKFRTVHGGLRLLGIRRTSTAPAASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELG
IRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAVHPGYGF
LSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEA
HEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIE
KPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAK
QVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSLPDL
GLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISP
HYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQF
IDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAG
FRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFSK
LFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVF
KFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSL
QYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGV
AAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEG
ARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQM
LGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFP
EPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHF
KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFEL
NGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVL
SAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE
|
| Enzyme 4 Number of Residues |
1178 |
| Enzyme 4 Molecular Weight |
129632.6 |
| Enzyme 4 Theoretical pI |
6.83 |
| Enzyme 4 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-carbon bonds
- nucleoside binding
- purine nucleoside binding
- pyruvate carboxylase activity
- vitamin binding
|
| Process |
- alcohol metabolic process
- gluconeogenesis
- glucose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 4 General Function |
Involved in catalytic activity |
| Enzyme 4 Specific Function |
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate [RN:R00344]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
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| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
458236 |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P11498 |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PYC_HUMAN |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>3537 bp
ATGCTGAAGTTCCGAACAGTCCATGGGGGCCTGAGGCTCCTGGGAATCCGCCGAACCTCC
ACCGCCCCCGCTGCCTCCCCAAATGTCCGGCGCCTGGAGTATAAGCCCATCAAGAAAGTC
ATGGTGGCCAACAGAGGTGAGATTGCCATCCGTGTGTTCCGGGCCTGCACGGAGCTGGGC
ATCCGCACCGTAGCCATCTACTCTGAGCAGGACACGGGCCAGATGCACCGGCAGAAAGCA
GATGAAGCCTATCTCATCGGCCGCGGCCTGGCCCCCGTGCAGGCCTACCTGCACATCCCA
GACATCATCAAGGTGGCCAAGGAGAACAACGTAGATGCAGTGCACCCTGGCTACGGGTTC
CTCTCTGAGCGAGCGGACTTCGCCCAGGCCTGCCAGGATGCAGGGGTCCGGTTTATTGGG
CCAAGCCCAGAAGTGGTCCGCAAGATGGGAGACAAGGTGGAGGCCCGGGCCATCGCCATT
GCTGCGGGTGTTCCCGTTGTCCCTGGCACAGATGCCCCCATCACGTCCCTGCATGAGGCC
CACGAGTTCTCCAACACCTACGGCTTCCCCATCATCTTCAAGGCGGCCTATGGGGGTGGA
GGGCGTGGCATGAGGGTGGTGCACAGCTACGAGGAGCTGGAGGAGAATTACACCCGGGCC
TACTCAGAGGCTCTGGCCGCCTTTGGGAATGGGGCGCTGTTTGTGGAGAAGTTCATCGAG
AAGCCACGGCACATCGAGGTGCAGATCTTGGGGGACCAGTATGGGAACATCCTGCACCTG
TACGAGCGAGACTGCTCCATCCAGCGGCGGCACCAGAAGGTGGTCGAGATTGCCCCCGCC
GCCCACCTGGACCCGCAGCTTCGGACTCGGCTCACCAGCGACTCTGTGAAACTCGCTAAA
CAGGTGGGCTACGAGAACGCAGGCACCGTGGAGTTCCTGGTGGACAGGCACGGCAAGCAC
TACTTCATCGAGGTCAACTCCCGCCTGCAGGTGGAGCACACGGTCACAGAGGAGATCACC
GACGTAGACCTGGTCCATGCTCAGATCCACGTGGCTGAGGGCAGGAGCCTACCCGACCTG
GGCCTGCGGCAGGAGAACATCCGCATCAACGGGTGTGCCATCCAGTGCCGGGTCACCACC
GAGGACCCCGCGCGCAGCTTCCAGCCGGACACCGGCCGCATTGAGGTGTTCCGGAGCGGA
GAGGGCATGGGCATCCGCCTGGATAATGCTTCCGCCTTCCAAGGAGCCGTCATCTCGCCC
CACTACGACTCCCTGCTGGTCAAAGTCATTGCCCACGGCAAAGACCACCCCACGGCCGCC
ACCAAGATGAGCAGGGCCCTTGCGGAGTTCCGCGTCCGAGGTGTGAAGACCAACATCGCC
TTCCTGCAGAATGTGCTCAACAACCAGCAGTTCCTGGCAGGCACTGTGGACACCCAGTTC
ATCGACGAGAACCCAGAGCTGTTCCAGCTGCGGCCTGCACAGAACCGGGCCCAAAAGCTG
TTGCACTACCTCGGCCATGTCATGGTAAACGGTCCAACCACCCCGATTCCCGTCAAGGCC
AGCCCCAGCCCCACGGACCCCGTTGTCCCTGCAGTGCCCATAGGCCCGCCCCCGGCTGGT
TTCAGAGACATCCTGCTGCGAGAGGGGCCTGAGGGCTTTGCTCGAGCTGTGCGGAACCAC
CCGGGGCTGCTGCTGATGGACACGACCTTCAGGGACGCCCACCAGTCACTGCTGGCCACT
CGTGTGCGCACCCACGATCTCAAAAAGATCGCCCCCTATGTTGCCCACAACTTCAGCAAG
CTCTTCAGCATGGAGAACTGGGGAGGAGCCACGTTTGACGTCGCCATGCGCTTCCTGTAT
GAGTGCCCCTGGCGGCGGCTGCAGGAGCTCCGGGAGCTCATCCCCAACATCCCTTTCCAG
ATGCTGCTGCGGGGGGCCAATGCTGTGGGCTACACCAACTACCCAGACAACGTGGTCTTC
AAGTTCTGTGAAGTGGCCAAAGAGAATGGCATGGATGTCTTCCGTGTGTTTGACTCCCTC
AACTACTTGCCCAACATGCTGCTGGGCATGGAGGCGGCAGGAAGTGCCGGAGGCGTGGTG
GAGGCTGCCATCTCATACACGGGCGACGTGGCCGACCCCAGCCGCACCAAGTACTCACTG
CAGTACTACATGGGCTTGGCCGAAGAGCTGGTGCGAGCTGGCACCCACATCCTGTGCATC
AAGGACATGGCCGGGCTGCTGAAGCCCACGGCCTGCACCATGCTGGTCAGCTCCCTCCGG
GACCGCTTCCCCGACCTCCCACTGCACATCCACACCCACGACACGTCAGGGGCAGGCGTG
GCAGCCATGCTGGCCTGTGCCCAGGCTGGAGCTGATGTGGTGGATGTGGCAGCTGATTCC
ATGTCTGGGATGACTTCACAGCCCAGCATGGGGGCCCTGGTGGCCTGTACCAGAGGGACT
CCCCTGGACACAGAGGTGCCCATGGAGCGCGTGTTTGACTACAGTGAGTACTGGGAGGGG
GCTCGGGGACTGTACGCGGCCTTCGACTGCACGGCCACCATGAAGTCTGGCAACTCGGAC
GTGTATGAAAATGAGATCCCAGGGGGCCAGTACACCAACCTGCACTTCCAGGCCCACAGC
ATGGGGCTTGGCTCCAAGTTCAAGGAGGTCAAGAAGGCCTATGTGGAGGCCAACCAGATG
CTGGGCGATCTCATCAAGGTGACGCCCTCCTCCAAGATCGTGGGGGACCTGGCCCAGTTT
ATGGTGCAGAATGGATTGAGCCGGGCAGAGGCCGAAGCTCAGGCGGAAGAGCTGTCCTTT
CCCCGCTCCGTGGTGGAGTTCCTGCAGGGCTACATCGGTGTCCCCCATGGGGGGTTCCCC
GAACCCTTTCGCTCTAAGGTACTGAAGGACCTGCCAAGGGTGGAGGGGCGGCCTGGAGCC
TCCCTCCCTCCCCTGGATCTGCAGGCACTGGAGAAGGAGCTGGTAGACCGGCATGGGGAG
GAGGTGACGCCGGAAGATGTGCTCTCAGCAGCTATGTACCCCGATGTGTTTGCCCACTTC
AAGGACTTCACTGCCACCTTTGGCCCCCTGGATAGCCTGAATACTCGCCTCTTCCTGCAG
GGACCCAAGATCGCAGAGGAGTTTGAGGTGGAGCTGGAGCGGGGCAAGACGCTGCACATC
AAAGCCCTGGCCGTGAGCGACCTGAACCGGGCCGGCCAGAGGCAGGTCTTCTTTGAGCTC
AATGGGCAGCTGCGGTCCATCTTGGTCAAGGACACCCAGGCCATGAAGGAGATGCACTTC
CACCCCAAGGCCCTAAAGGACGTGAAGGGCCAGATCGGGGCGCCCATGCCTGGGAAGGTG
ATAGACATCAAAGTGGTGGCAGGGGCCAAGGTGGCCAAGGGCCAGCCCCTGTGTGTGCTC
AGTGCCATGAAGATGGAGACTGTGGTGACCTCACCCATGGAGGGTACTGTCCGCAAGGTT
CATGTGACCAAGGACATGACACTGGAAGGTGACGACCTCATCCTGGAGATCGAGTGA
|
| Enzyme 4 GenBank Gene ID |
U04641 |
| Enzyme 4 GeneCard ID |
PC |
| Enzyme 4 GenAtlas ID |
PC |
| Enzyme 4 HGNC ID |
HGNC:8636 |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
11q13.4-q13.5 |
| Enzyme 4 SNPs |
SNPJam Report |
| Enzyme 4 General References |
- Wexler ID, Du Y, Lisgaris MV, Mandal SK, Freytag SO, Yang BS, Liu TC, Kwon M, Patel MS, Kerr DS: Primary amino acid sequence and structure of human pyruvate carboxylase. Biochim Biophys Acta. 1994 Oct 21;1227(1-2):46-52. [PubMed ]
- MacKay N, Rigat B, Douglas C, Chen HS, Robinson BH: cDNA cloning of human kidney pyruvate carboxylase. Biochem Biophys Res Commun. 1994 Jul 29;202(2):1009-14. [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 ]
- Lamhonwah AM, Quan F, Gravel RA: Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase. Arch Biochem Biophys. 1987 May 1;254(2):631-6. [PubMed ]
- Freytag SO, Collier KJ: Molecular cloning of a cDNA for human pyruvate carboxylase. Structural relationship to other biotin-containing carboxylases and regulation of mRNA content in differentiating preadipocytes. J Biol Chem. 1984 Oct 25;259(20):12831-7. [PubMed ]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Xiang S, Tong L: Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction. Nat Struct Mol Biol. 2008 Mar;15(3):295-302. Epub 2008 Feb 24. [PubMed ]
- Carbone MA, MacKay N, Ling M, Cole DE, Douglas C, Rigat B, Feigenbaum A, Clarke JT, Haworth JC, Greenberg CR, Seargeant L, Robinson BH: Amerindian pyruvate carboxylase deficiency is associated with two distinct missense mutations. Am J Hum Genet. 1998 Jun;62(6):1312-9. [PubMed ]
- Wexler ID, Kerr DS, Du Y, Kaung MM, Stephenson W, Lusk MM, Wappner RS, Higgins JJ: Molecular characterization of pyruvate carboxylase deficiency in two consanguineous families. Pediatr Res. 1998 May;43(5):579-84. [PubMed ]
- Monnot S, Serre V, Chadefaux-Vekemans B, Aupetit J, Romano S, De Lonlay P, Rival JM, Munnich A, Steffann J, Bonnefont JP: Structural insights on pathogenic effects of novel mutations causing pyruvate carboxylase deficiency. Hum Mutat. 2009 May;30(5):734-40. [PubMed ]
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| Enzyme 4 Metabolite References |
Not Available |
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Enzyme 5
[top]
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| Enzyme 5 ID |
5276 |
| Enzyme 5 Name |
Acetyl-CoA carboxylase 1 |
| Enzyme 5 Synonyms |
- ACC-alpha
- Biotin carboxylase
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| Enzyme 5 Gene Name |
ACACA |
| Enzyme 5 Protein Sequence |
>Acetyl-CoA carboxylase 1
MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLS
DLGISSLQDGLALHIRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEK
VLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPG
GPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWAL
GDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQA
AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEV
QILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSA
GTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMY
GVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGY
FSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLET
ESFQMNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSVSNFLHSLERGQV
LPAHTLLNTVDVELIYEGVKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDG
SSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYA
EIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVLAKMQLDNPSKVQQAELHTGSLPRIQ
STALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQ
DIMTSVSGRIPPNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREV
FFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSD
MNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALR
ARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYH
SNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRM
SFSSNLNHYGMTHVASVSDVLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSP
PQSPTFPEAGHTSLYDEDKVPRDEPIHILNVAIKTDCDIEDDRLAAMFREFTQQNKATLV
DHGIRRLTFLVAQKDFRKQVNYEVDRRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQ
LELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFE
YLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYG
SRLWKLRVLQAELKINIRLTPTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQA
YGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQA
FLPSPPLPSDMLTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMTFKSPEYPEGRDIIVI
GNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGARIGLAEEIRHMFHVAWVD
PEDPYKGYRYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGIGPENLRGS
GMIAGESSLAYNEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGR
EVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDPID
RIIEFVPTKTPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGG
IPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPL
MVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECCQPVLVYIPPQAELRGGSWVVIDSSI
NPRHMEMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRRVDPVYIHLAERLGTPELSTAE
RKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRTFFYWRLR
RLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLAEWLEKQLTE
EDGVHSVIEENIKCISRDYVLKQIRSLVQANPEVAMDSIIHMTQHISPTQRAEVIRILST
MDSPST
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| Enzyme 5 Number of Residues |
2346 |
| Enzyme 5 Molecular Weight |
265551.7 |
| Enzyme 5 Theoretical pI |
6.32 |
| Enzyme 5 GO Classification |
| Function |
- ATP binding
- CoA carboxylase activity
- acetyl-CoA carboxylase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-carbon bonds
- nucleoside binding
- purine nucleoside binding
- vitamin binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid biosynthetic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxoacid metabolic process
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| Component |
| — |
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| Enzyme 5 General Function |
Involved in acetyl-CoA carboxylase activity |
| Enzyme 5 Specific Function |
Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA [RN:R00742]
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| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
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| Enzyme 5 Transmembrane Regions |
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| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
38679967 |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q13085 |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
ACACA_HUMAN |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>7041 bp
ATGGATGAACCATCTCCCTTGGCCCAACCTCTGGAGCTGAACCAGCACTCTCGATTCATA
ATAGGTTCTGTGTCTGAAGATAACTCAGAGGATGAGATCAGCAACCTGGTGAAGTTGGAC
CTACTGGAGGAGAAGGAGGGCTCCTTGTCACCTGCTTCTGTTGGCTCAGATACACTCTCT
GATTTGGGGATCTCTAGCCTACAGGATGGCTTGGCCTTGCACATAAGGTCCAGCATGTCT
GGCTTGCACCTAGTAAAGCAGGGCCGAGACAGAAAGAAAATAGATTCTCAACGAGATTTC
ACTGTGGCTTCTCCAGCAGAATTTGTTACTCGCTTTGGGGGAAATAAAGTGATTGAGAAG
GTTCTTATTGCTAACAATGGCATTGCAGCAGTGAAATGCATGCGGTCTATCCGTAGGTGG
TCTTATGAAATGTTTCGAAATGAACGTGCAATTAGATTCGTTGTCATGGTCACACCTGAA
GACCTTAAAGCCAATGCAGAATACATTAAGATGGCAGATCACTATGTGCCAGTGCCTGGA
GGACCAAACAACAACAACTATGCAAATGTGGAATTAATTCTTGATATTGCTAAAAGGATC
CCAGTACAAGCAGTGTGGGCTGGCTGGGGTCATGCTTCTGAGAATCCCAAACTACCGGAA
CTTCTCTTGAAAAATGGCATTGCCTTCATGGGTCCTCCAAGCCAGGCCATGTGGGCTTTA
GGGGATAAGATTGCATCTTCCATAGTGGCTCAAACTGCAGGTATCCCAACTCTTCCCTGG
AGCGGCAGTGGTCTTCGTGTGGACTGGCAGGAAAATGATTTTTCAAAACGTATCTTAAAT
GTTCCCCAGGAGCTATATGAAAAAGGTTATGTGAAAGATGTGGATGATGGGCTACAGGCA
GCTGAGGAAGTTGGATATCCAGTAATGATCAAGGCCTCAGAGGGAGGAGGAGGGAAGGGA
ATTAGAAAAGTCAACAATGCAGATGACTTCCCTAATCTCTTCAGACAGGTTCAAGCTGAA
GTTCCTGGATCTCCCATATTTGTGATGAGACTAGCCAAACAATCTCGTCATCTGGAGGTG
CAGATCTTAGCGGACCAATATGGCAATGCTATCTCTTTGTTTGGTCGTGATTGCTCTGTA
CAACGCAGGCATCAGAAGATTATTGAAGAAGCACCTGCTACTATTGCTACTCCAGCAGTA
TTTGAACACATGGAACAGTGTGCGGTGAAACTTGCCAAAATGGTGGGTTATGTGAGTGCT
GGGACTGTGGAATACCTGTACAGCCAGGATGGCAGCTTCTACTTTCTGGAATTGAATCCT
CGGCTGCAGGTAGAGCACCCTTGTACAGAGATGGTGGCTGATGTCAATCTCCCTGCAGCA
CAGCTCCAGATTGCCATGGGGATTCCTCTATATAGAATCAAGGATATCCGTATGATGTAT
GGGGTATCTCCCTGGGGTGATTCTCCCATTGATTTTGAAGATTCTGCACACGTTCCTTGT
CCAAGGGGCCATGTTATTGCTGCTCGGATCACTAGTGAAAATCCAGATGAGGGTTTTAAG
CCCAGCTCAGGAACAGTTCAGGAGCTAAATTTCCGCAGCAATAAGAATGTTTGGGGATAT
TTCAGTGTTGCTGCTGCAGGGGGACTTCATGAATTTGCTGATTCTCAGTTTGGTCACTGC
TTTTCTTGGGGAGAAAACAGAGAAGAGGCAATTTCAAACATGGTGGTGGCTTTGAAGGAG
CTGTCTATTCGGGGTGACTTTCGAACTACAGTTGAATACCTGATCAAATTGTTAGAGACT
GAAAGCTTTCAGATGAACAGAATTGATACTGGCTGGCTGGACAGACTGATAGCAGAAAAA
GTACAGGCTGAGCGACCTGACACCATGTTGGGGGTTGTGTGTGGTGCCCTCCACGTGGCA
GATGTGAGCCTGCGGAATAGCGTCTCTAACTTCCTTCACTCCTTAGAAAGGGGTCAAGTC
CTTCCTGCTCATACACTTCTGAATACAGTAGATGTTGAACTTATCTATGAGGGAGTCAAG
TATGTACTTAAGGTGACTCGACAGTCCCCCAACTCCTATGTGGTGATCATGAATGGCTCA
TGTGTAGAAGTAGATGTACATCGGCTGAGTGACGGTGGACTGCTCTTGTCCTATGATGGC
AGCAGTTATACTACGTATATGAAAGAGGAAGTGGATAGATATCGCATCACAATTGGCAAT
AAAACCTGTGTGTTTGAGAAGGAAAATGACCCATCGGTGATGCGCTCACCTTCTGCTGGG
AAGTTAATCCAGTACATTGTAGAAGATGGAGGTCATGTGTTTGCCGGCCAGTGCTATGCT
GAGATTGAGGTAATGAAGATGGTAATGACCTTAACAGCTGTGGAGTCTGGCTGTATCCAT
TACGTCAAGCGACCTGGAGCAGCTCTTGACCCTGGCTGTGTACTAGCCAAAATGCAACTG
GACAACCCCAGCAAGGTTCAGCAGGCTGAACTTCACACAGGTAGTCTGCCACGGATCCAG
AGCACGGCACTCAGAGGCGAGAAACTCCATCGAGTGTTCCATTATGTCCTGGATAATCTG
GTCAATGTAATGAATGGATACTGCCTTCCAGATCCTTTCTTTAGCAGCAAGGTAAAAGAC
TGGGTAGAGCGATTGATGAAAACCCTCAGAGATCCCTCCCTGCCTCTCCTAGAATTGCAA
GATATTATGACCAGTGTGTCTGGCCGCATTCCCCCCAATGTGGAGAAGTCTATCAAGAAG
GAAATGGCTCAGTATGCTAGCAACATCACATCAGTCCTCTGTCAGTTTCCCAGCCAGCAG
ATTGCAAACATCCTAGATAGCCATGCAGCTACATTGAACCGGAAATCTGAACGGGAAGTC
TTCTTTATGAATACTCAGAGCATTGTTCAGCTGGTACAGAGGTACCGAAGTGGCATCCGA
GGCCACATGAAGGCTGTGGTGATGGATCTGCTCCGGCAGTACCTGCGAGTAGAGACACAA
TTCCAGAATGGTCACTATGACAAATGTGTATTCGCCCTCCGAGAAGAGAATAAAAGTGAC
ATGAACACTGTACTGAACTACATCTTCTCTCACGCTCAAGTCACCAAGAAGAATCTTCTG
GTCACAATGCTTATTGATCAGTTGTGTGGCCGGGACCCTACTCTCACTGATGAGCTGCTG
AATATTCTCACAGAGCTAACTCAACTCAGTAAGACCACCAATGCCAAAGTAGCACTTCGA
GCACGCCAGGTTCTTATTGCCTCCCATTTGCCATCATATGAGCTTCGCCATAACCAAGTA
GAGTCTATCTTCCTATCAGCTATTGACATGTATGGACATCAATTTTGCATTGAGAACCTG
CAGAAACTCATCCTATCAGAAACATCTATTTTTGATGTCCTACCAAACTTCTTCTATCAC
AGCAACCAAGTAGTGAGGATGGCAGCTCTGGAGGTGTATGTTCGAAGGGCTTATATTGCC
TATGAACTTAACAGCGTACAACACCGCCAGCTTAAGGACAACACCTGTGTGGTGGAATTC
CAGTTCATGCTGCCCACATCTCATCCAAACAGAGGGAACATCCCTACGCTAAACAGAATG
TCCTTCTCCTCCAACCTCAACCACTATGGCATGACCCATGTAGCTAGTGTCAGCGATGTA
CTGTTGGACAACTCATTCACTCCACCTTGTCAGCGGATGGGCGGAATGGTCTCTTTTCGG
ACTTTTGAAGATTTTGTCAGGATCTTTGATGAAGTGATGGGCTGCTTCTCTGACTCCCCA
CCCCAGAGTCCCACATTCCCTGAGGCAGGTCACACGTCTCTTTATGATGAGGATAAGGTT
CCCAGGGATGAACCAATTCACATTCTCAATGTGGCTATCAAGACTGACTGTGATATTGAG
GATGACAGGCTGGCAGCTATGTTCAGAGAATTTACCCAGCAAAATAAAGCTACCCTGGTT
GACCATGGGATCCGGCGCCTTACTTTCCTGGTTGCACAAAAGGATTTCAGAAAGCAGGTC
AACTATGAGGTGGATCGGAGATTTCATAGAGAATTCCCTAAATTTTTTACATTCCGAGCA
AGGGATAAGTTTGAGGAGGATCGTATCTATCGTCATCTGGAGCCTGCTCTGGCTTTCCAG
TTAGAGCTGAACCGGATGAGAAATTTTGACCTCACTGCCATTCCATGTGCTAATCACAAG
ATGCACCTGTATCTCGGGGCAGCCAAGGTGGAAGTGGGCACAGAAGTGACAGACTACAGG
TTCTTTGTTCGTGCAATCATCAGGCATTCTGATCTGGTCACCAAGGAAGCTTCTTTTGAA
TATCTGCAAAATGAAGGGGAGCGGCTACTCCTGGAAGCCATGGATGAGTTGGAAGTTGCT
TTTAACAATACAAATGTCCGCACTGACTGTAACCACATCTTCCTCAACTTTGTGCCCACG
GTTATCATGGACCCATCAAAGATTGAGGAATCCGTGCGGAGCATGGTAATGCGGTATGGA
AGTCGCCTGTGGAAATTGCGCGTCCTCCAGGCAGAACTGAAAATCAACATTCGCCTGACG
CCAACTGGAAAAGCAATTCCCATCCGCCTCTTCCTGACAAACGAGTCTGGCTATTACTTG
GATATCAGCCTATACAAGGAAGTGACTGACTCCAGGACAGCACAGATCATGTTTCAGGCA
TATGGAGACAAACAGGGACCACTGCATGGAATGTTAATCAATACTCCATATGTGACCAAA
GACCTGCTGCAATCAAAGAGGTTCCAGGCACAATCCTTAGGGACAACATACATATATGAT
ATCCCAGAGATGTTTCGGCAGTCCCTGATCAAACTCTGGGAGTCTATGTCCACTCAAGCA
TTTCTTCCATCTCCCCCTCTGCCTTCTGACATGCTGACTTACACTGAACTGGTACTGGAT
GATCAAGGTCAGCTGGTCCACATGAACAGGCTTCCAGGAGGAAATGAGATTGGCATGGTA
GCTTGGAAAATGACCTTTAAAAGTCCTGAATATCCAGAAGGCCGAGATATCATTGTTATT
GGCAATGACATCACATACCGAATTGGGTCCTTTGGGCCTCAAGAGGATTTGTTATTTCTC
AGAGCTTCCGAACTTGCTAGGGCAGAAGGTATTCCACGCATCTATGTATCAGCCAACAGT
GGAGCAAGAATCGGACTGGCAGAAGAAATTCGCCATATGTTTCATGTGGCCTGGGTAGAT
CCTGAGGATCCTTACAAGGGATACAGGTATTTATATCTGACTCCTCAAGATTATAAGAGA
GTCAGTGCTCTCAACTCTGTCCATTGTGAACACGTGGAAGATGAAGGAGAATCCAGGTAC
AAGATAACAGATATTATTGGGAAAGAAGAGGGAATTGGACCCGAGAACCTTCGAGGTTCT
GGAATGATTGCTGGAGAATCCTCATTGGCCTATAATGAGATCATTACCATCAGCCTGGTG
ACGTGCCGGGCCATTGGGATTGGGGCTTACCTTGTCCGGCTGGGACAGAGAACCATCCAG
GTTGAGAATTCTCACTTAATTCTAACAGGAGCTGGAGCCCTCAACAAAGTCCTCGGGCGG
GAAGTGTACACCTCCAATAACCAGCTGGGGGGCATCCAGATTATGCACAACAATGGGGTG
ACCCACTGCACTGTGTGTGATGACTTTGAAGGGGTTTTCACTGTCCTGCACTGGCTGTCT
TACATGCCCAAGAGCGTGCACAGTTCAGTTCCTCTTCTGAACTCAAAGGATCCTATAGAC
AGAATCATCGAGTTTGTTCCCACAAAGACCCCATACGATCCTCGATGGATGCTAGCAGGC
CGTCCTCACCCAACCCAAAAAGGTCAGTGGTTGAGTGGCTTTTTTGACTATGGATCTTTC
TCAGAGATTATGCAGCCCTGGGCACAGACTGTGGTGGTTGGTAGAGCCAGGCTAGGAGGA
ATACCTGTGGGAGTTGTTGCTGTAGAAACCCGAACAGTAGAACTAAGTATCCCAGCTGAT
CCAGCAAACCTGGATTCTGAAGCCAAGATAATCCAGCAGGCTGGCCAGGTTTGGTTCCCA
GATTCTGCGTTTAAGACGTATCAGGCCATCAAGGACTTCAACCGGGAAGGGCTGCCTCTG
ATGGTCTTTGCCAACTGGAGAGGCTTCTCTGGTGGAATGAAAGATATGTACGACCAAGTG
CTGAAGTTTGGTGCTTACATTGTGGATGGCTTGAGGGAGTGCTGCCAGCCTGTGCTGGTT
TACATTCCTCCCCAGGCTGAGCTGCGGGGTGGCTCCTGGGTGGTGATTGACTCCTCCATC
AACCCCCGGCACATGGAGATGTATGCTGACCGAGAAAGCAGGGGATCTGTTCTGGAGCCA
GAAGGGACAGTAGAAATCAAATTCCGCAGAAAGGATCTGGTGAAAACCATGCGTCGGGTG
GACCCAGTCTACATCCACTTGGCTGAGCGATTGGGGACCCCAGAGCTAAGCACAGCTGAG
CGGAAGGAGTTGGAGAACAAGTTGAAGGAGCGGGAGGAATTCCTAATTCCCATTTACCAT
CAGGTAGCCGTGCAGTTTGCTGACTTGCACGACACACCAGGCCGGATGCAGGAGAAGGGT
GTTATTAGCGATATCCTGGATTGGAAAACATCCCGTACCTTCTTCTACTGGCGGCTGAGG
CGTCTTCTGCTGGAGGACCTGGTCAAGAAGAAAATCCACAATGCCAACCCTGAGCTGACT
GATGGCCAGATTCAAGCCATGTTAAGGCGCTGGTTTGTGGAAGTGGAAGGAACAGTGAAG
GCTTATGTTTGGGACAATAATAAGGATCTGGCGGAGTGGCTAGAGAAACAGCTGACAGAG
GAGGATGGTGTTCACTCGGTAATAGAGGAAAACATCAAATGCATCAGCAGAGACTACGTC
CTCAAGCAAATCCGCAGCTTGGTCCAGGCCAATCCAGAGGTTGCCATGGATTCCATCATC
CATATGACGCAGCACATATCACCCACTCAGCGAGCAGAAGTCATACGGATCCTCTCCACA
ATGGATTCCCCTTCCACGTAG
|
| Enzyme 5 GenBank Gene ID |
NM_198836.1 |
| Enzyme 5 GeneCard ID |
ACACA |
| Enzyme 5 GenAtlas ID |
ACACA |
| Enzyme 5 HGNC ID |
HGNC:84 |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
17q21 |
| Enzyme 5 SNPs |
SNPJam Report |
| Enzyme 5 General References |
- Abu-Elheiga L, Jayakumar A, Baldini A, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):4011-5. [PubMed ]
- Mao J, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region. Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7515-20. Epub 2003 Jun 16. [PubMed ]
- Sinilnikova OM, Ginolhac SM, Magnard C, Leone M, Anczukow O, Hughes D, Moreau K, Thompson D, Coutanson C, Hall J, Romestaing P, Gerard JP, Bonadona V, Lasset C, Goldgar DE, Joulin V, Venezia ND, Lenoir GM: Acetyl-CoA carboxylase alpha gene and breast cancer susceptibility. Carcinogenesis. 2004 Dec;25(12):2417-24. Epub 2004 Aug 27. [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 ]
- Travers MT, Vallance AJ, Clegg RA, Thomson R, Price NT, Barber MC: Characterisation of an N-terminal variant of acetyl-CoA carboxylase-alpha: expression in human tissues and evolutionary aspects. Biochim Biophys Acta. 2003 Nov 15;1634(3):97-106. [PubMed ]
- Travers MT, Cambot M, Kennedy HT, Lenoir GM, Barber MC, Joulin V: Asymmetric expression of transcripts derived from the shared promoter between the divergently oriented ACACA and TADA2L genes. Genomics. 2005 Jan;85(1):71-84. [PubMed ]
- Magnard C, Bachelier R, Vincent A, Jaquinod M, Kieffer S, Lenoir GM, Venezia ND: BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains. Oncogene. 2002 Oct 3;21(44):6729-39. [PubMed ]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Moreau K, Dizin E, Ray H, Luquain C, Lefai E, Foufelle F, Billaud M, Lenoir GM, Venezia ND: BRCA1 affects lipid synthesis through its interaction with acetyl-CoA carboxylase. J Biol Chem. 2006 Feb 10;281(6):3172-81. Epub 2005 Dec 2. [PubMed ]
- Ray H, Moreau K, Dizin E, Callebaut I, Venezia ND: ACCA phosphopeptide recognition by the BRCT repeats of BRCA1. J Mol Biol. 2006 Jun 16;359(4):973-82. Epub 2006 Apr 25. [PubMed ]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed ]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
- Blom W, de Muinck Keizer SM, Scholte HR: Acetyl-CoA carboxylase deficiency: an inborn error of de novo fatty acid synthesis. N Engl J Med. 1981 Aug 20;305(8):465-6. [PubMed ]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5312 |
| Enzyme 6 Name |
Thymidylate kinase |
| Enzyme 6 Synonyms |
- dTMP kinase
|
| Enzyme 6 Gene Name |
DTYMK |
| Enzyme 6 Protein Sequence |
>Thymidylate kinase
MAARRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLLSSYLQKK
SDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGVAFTGAKENFSLDWCKQP
DVGLPKPDLVLFLQLQLADAAKRGAFGHERYENGAFQERALRCFHQLMKDTTLNWKMVDA
SKSIEAVHEDIRVLSEDAIRTATEKPLGELWK
|
| Enzyme 6 Number of Residues |
212 |
| Enzyme 6 Molecular Weight |
23819.1 |
| Enzyme 6 Theoretical pI |
8.49 |
| Enzyme 6 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 6 General Function |
Involved in thymidylate kinase activity |
| Enzyme 6 Specific Function |
Catalyzes the conversion of dTMP to dTDP |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- ATP + dTMP = ADP + dTDP [RN:R02094]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
37206 |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P23919 |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
KTHY_HUMAN |
| Enzyme 6 PDB ID |
1E9A |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>636 bp
ATGGCGGCCCGGCGCGGGGCTCTCATAGTGCTGGAGGGCGTGGACCGCGCCGGGAAGAGC
ACGCAGAGCCGCAAGCTGGTGGAAGCGCTGTCGCGCGGGCCACCGCCCGAACTGCTCCGG
TTCCCGGAAAGATCAACTGAAATCGGCAAACTTCTGAGTTCCTACTTGCAAAAGAAAAGT
GACGTGGAGGATCACTCGGTGCACCTGCTTTTTTCTGCAAATCGCTGGGAACAAGTGCCG
TTAATTAAGGAAAAGTTGAGCCAGGGCGTGACCCTCGTCGTGGACAGATACGCATTTTCT
GGTGTGGCCTTCACCGGTGCCAAGGAGAATTTTTCCCTAGACTGGTGTAAACAGCCAGAC
GTGGGCCTTCCCAAACCCGACCTGGTCCTGTTCCTCCAGTTACAGCTGGCGGATGCTGCC
AAGCGGGGAGCGTTTGGCCATGAGCGCTATGAGAACGGGGCTTTCCAGGAGCGGGCGCTC
CGGTGTTTCCACCAGCTCATGAAAGACACGACTTTGAACTGGAAGATGGTGGATGCTTCC
AAAAGACTCGAAGCTGTCCATGAGGAACTCCGCGTGCTCTCTGAGGACGCCATCCGCACT
GCCACAGAGAAGCCGCTGGGGGAGCTATGGAAGTGA
|
| Enzyme 6 GenBank Gene ID |
X54729 |
| Enzyme 6 GeneCard ID |
DTYMK |
| Enzyme 6 GenAtlas ID |
DTYMK |
| Enzyme 6 HGNC ID |
HGNC:3061 |
| Enzyme 6 Chromosome Location |
2 |
| Enzyme 6 Locus |
2q37.3 |
| Enzyme 6 SNPs |
SNPJam Report |
| Enzyme 6 General References |
- Su JY, Sclafani RA: Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast. Nucleic Acids Res. 1991 Feb 25;19(4):823-7. [PubMed ]
- Huang SH, Tang A, Drisco B, Zhang SQ, Seeger R, Li C, Jong A: Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth. DNA Cell Biol. 1994 May;13(5):461-71. [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 ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Ostermann N, Segura-Pena D, Meier C, Veit T, Monnerjahn C, Konrad M, Lavie A: Structures of human thymidylate kinase in complex with prodrugs: implications for the structure-based design of novel compounds. Biochemistry. 2003 Mar 11;42(9):2568-77. [PubMed ]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5313 |
| Enzyme 7 Name |
Ectonucleoside triphosphate diphosphohydrolase 1 |
| Enzyme 7 Synonyms |
- NTPDase 1
- Ecto-ATP diphosphohydrolase 1
- Ecto-ATPDase 1
- Ecto-ATPase 1
- Ecto-apyrase
- Lymphoid cell activation antigen
- CD39 antigen
|
| Enzyme 7 Gene Name |
ENTPD1 |
| Enzyme 7 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
|
| Enzyme 7 Number of Residues |
510 |
| Enzyme 7 Molecular Weight |
57964.1 |
| Enzyme 7 Theoretical pI |
6.29 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in hydrolase activity |
| Enzyme 7 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 7 Pathways |
|
| Enzyme 7 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
45580700 |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P49961 |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
ENTP1_HUMAN |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 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 7 GenBank Gene ID |
NM_001776.5 |
| Enzyme 7 GeneCard ID |
ENTPD1 |
| Enzyme 7 GenAtlas ID |
ENTPD1 |
| Enzyme 7 HGNC ID |
HGNC:3363 |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
10q24 |
| Enzyme 7 SNPs |
SNPJam Report |
| Enzyme 7 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 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5314 |
| Enzyme 8 Name |
Soluble calcium-activated nucleotidase 1 |
| Enzyme 8 Synonyms |
- SCAN-1
- Apyrase homolog
- Putative MAPK-activating protein PM09
- Putative NF-kappa-B-activating protein 107
|
| Enzyme 8 Gene Name |
CANT1 |
| Enzyme 8 Protein Sequence |
>Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
|
| Enzyme 8 Number of Residues |
401 |
| Enzyme 8 Molecular Weight |
44839.2 |
| Enzyme 8 Theoretical pI |
5.98 |
| Enzyme 8 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 8 General Function |
Involved in calcium ion binding |
| Enzyme 8 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 8 Pathways |
|
| Enzyme 8 Reactions |
- a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
229577440 |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q8WVQ1 |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
CANT1_HUMAN |
| Enzyme 8 PDB ID |
1S1D |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 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 8 GenBank Gene ID |
NM_001159772.1 |
| Enzyme 8 GeneCard ID |
CANT1 |
| Enzyme 8 GenAtlas ID |
CANT1 |
| Enzyme 8 HGNC ID |
HGNC:19721 |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
17q25.3 |
| Enzyme 8 SNPs |
SNPJam Report |
| Enzyme 8 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5317 |
| Enzyme 9 Name |
Thymidine kinase, cytosolic |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
TK1 |
| Enzyme 9 Protein Sequence |
>Thymidine kinase, cytosolic
MSCINLPTVLPGSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTR
YSSSFCTHDRNTMEALPACLLRDVAQEALGVAVIGIDEGQFFPDIVEFCEAMANAGKTVI
VAALDGTFQRKPFGAILNLVPLAESVVKLTAVCMECFREAAYTKRLGTEKEVEVIGGADK
YHSVCRLCYFKKASGQPAGPDNKENCPVPGKPGEAVAARKLFAPQQILQCSPAN
|
| Enzyme 9 Number of Residues |
234 |
| Enzyme 9 Molecular Weight |
25469 |
| Enzyme 9 Theoretical pI |
8.61 |
| Enzyme 9 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- deoxynucleoside kinase activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- nucleotide binding
- purine nucleotide binding
- thymidine kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 9 General Function |
Nucleotide transport and metabolism |
| Enzyme 9 Specific Function |
ATP + thymidine = ADP + thymidine 5'- phosphate |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- ATP + thymidine = ADP + thymidine 5'-phosphate
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
339709 |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P04183 |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
KITH_HUMAN |
| Enzyme 9 PDB ID |
1XBT |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>705 bp
ATGAGCTGCATTAACCTGCCCACTGTGCTGCCCGGCTCCCCCAGCAAGACCCGGGGGCAG
ATCCAGGTGATTCTCGGGCCGATGTTCTCAGGAAAAAGCACAGAGTTGATGAGACGCGTC
CGTCGCTTCCAGATTGCTCAGTACAAGTGCCTGGTGATCAAGTATGCCAAAGACACTCGC
TACAGCAGCAGCTTCTGCACACATGACCGGAACACCATGGAGGCGCTGCCCGCCTGCCTG
CTCCGAGACGTGGCCCAGGAGGCCCTGGGCGTGGCTGTCATAGGCATCGACGAGGGGCAG
TTTTTCCCTGACATCATGGAGTTCTGCGAGGCCATGGCCAACGCCGGGAAGACCGTAATT
GTGGCTGCACTGGATGGGACCTTCCAGAGGAAGCCATTTGGGGCCATCCTGAACCTGGTG
CCGCTGGCCGAGAGCGTGGTGAAGCTGACGGCGGTGTGCATGGAGTGCTTCCGGGAAGCC
GCCTATACCAAGAGGCTCGGCACAGAGAAGGAGGTCGAGGTGATTGGGGGAGCAGACAAG
TACCACTCCGTGTGTCGGCTCTGCTACTTCAAGAAGGCCTCAGGCCAGCCTGCCGGGCCG
GACAACAAAGAGAACTGCCCAGTGCCAGGAAAGCCAGGGGAAGCCGTGGCTGCCAGGAAG
CTCTTTGCCCCACAGCAGATTCTGCAATGCAGCCCTGCCAACTGA
|
| Enzyme 9 GenBank Gene ID |
K02581 |
| Enzyme 9 GeneCard ID |
TK1 |
| Enzyme 9 GenAtlas ID |
TK1 |
| Enzyme 9 HGNC ID |
HGNC:11830 |
| Enzyme 9 Chromosome Location |
17 |
| Enzyme 9 Locus |
17q23.2-q25.3 |
| Enzyme 9 SNPs |
SNPJam Report |
| Enzyme 9 General References |
- Bradshaw HD Jr, Deininger PL: Human thymidine kinase gene: molecular cloning and nucleotide sequence of a cDNA expressible in mammalian cells. Mol Cell Biol. 1984 Nov;4(11):2316-20. [PubMed ]
- Flemington E, Bradshaw HD Jr, Traina-Dorge V, Slagel V, Deininger PL: Sequence, structure and promoter characterization of the human thymidine kinase gene. Gene. 1987;52(2-3):267-77. [PubMed ]
- Chang ZF, Huang DY, Chi LM: Serine 13 is the site of mitotic phosphorylation of human thymidine kinase. J Biol Chem. 1998 May 15;273(20):12095-100. [PubMed ]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5318 |
| Enzyme 10 Name |
Ectonucleoside triphosphate diphosphohydrolase 3 |
| Enzyme 10 Synonyms |
- NTPDase 3
- CD39 antigen-like 3
- Ecto-ATP diphosphohydrolase 3
- Ecto-ATPDase 3
- Ecto-ATPase 3
- Ecto-apyrase 3
- HB6
|
| Enzyme 10 Gene Name |
ENTPD3 |
| Enzyme 10 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 3
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
|
| Enzyme 10 Number of Residues |
529 |
| Enzyme 10 Molecular Weight |
59104.8 |
| Enzyme 10 Theoretical pI |
6.40 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in hydrolase activity |
| Enzyme 10 Specific Function |
Has a threefold preference for the hydrolysis of ATP over ADP |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
13817037 |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
O75355 |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
ENTP3_HUMAN |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1590 bp
ATGTTCACTGTGCTGACCCGCCAACCATGTGAGCAAGCAGGCCTCAAGGCCCTCTACCGA
ACTCCAACCATCATTGCCTTGGTGGTCTTGCTTGTGAGTATTGTGGTACTTGTGAGTATC
ACTGTCATCCAGATCCACAAGCAAGAGGTCCTCCCTCCAGGACTGAAGTATGGTATTGTG
CTGGATGCCGGGTCTTCAAGAACCACAGTCTACGTGTATCAATGGCCAGCAGAAAAAGAG
AATAATACCGGAGTGGTCAGTCAAACCTTCAAATGTAGTGTGAAAGGCTCTGGAATCTCC
AGCTATGGAAATAACCCCCAAGATGTCCCCAGAGCCTTTGAGGAGTGTATGCAAAAAGTC
AAGGGGCAGGTTCCATCCCACCTCCACGGATCCACCCCCATTCACCTGGGAGCCACGGCT
GGGATGCGCTTGCTGAGGTTGCAAAATGAAACAGCAGCTAATGAAGTCCTTGAAAGCATC
CAAAGCTACTTCAAGTCCCAGCCCTTTGACTTTAGGGGTGCTCAAATCATTTCTGGGCAA
GAAGAAGGGGTATATGGATGGATTACAGCCAACTATTTAATGGGAAATTTCCTGGAGAAG
AACCTGTGGCACATGTGGGTGCACCCGCATGGAGTGGAAACCACGGGTGCCCTGGACTTA
GGTGGTGCCTCCACCCAAATATCCTTCGTGGCAGGAGAGAAGATGGATCTGAACACCAGC
GACATCATGCAGGTGTCCCTGTATGGCTACGTATACACGCTCTACACACACAGCTTCCAG
TGCTATGGCCGGAATGAGGCTGAGAAGAAGTTTCTGGCAATGCTCCTGCAGAATTCTCCT
ACCAAAAACCATCTCACCAATCCCTGTTACCCTCGGGATTATAGCATCAGCTTCACCATG
GGCCATGTATTTGATAGCCTGTGCACTGTGGACCAGAGGCCAGAAAGTTATAACCCCAAT
GATGTCATCACTTTTGAAGGAACTGGGGACCCATCTCTGTGTAAGGAGAAGGTGGCTTCC
ATATTTGACTTCAAAGCTTGCCATGATCAAGAAACCTGTTCTTTTGATGGGGTTTATCAG
CCAAAGATTAAAGGGCCATTTGTGGCTTTTGCAGGATTCTACTACACAGCCAGTGCTTTA
AATCTTTCAGGTAGCTTTTCCCTGGACACCTTCAACTCCAGCACCTGGAATTTCTGCTCA
CAGAATTGGAGTCAGCTCCCACTGCTGCTCCCCAAATTTGATGAGGTATATGCCCGCTCT
TACTGCTTCTCAGCCAACTACATCTACCACTTGTTTGTGAACGGTTACAAATTCACAGAG
GAGACTTGGCCCCAAATACACTTTGAAAAAGAAGTGGGGAATAGCAGCATAGCCTGGTCT
CTTGGCTACATGCTCAGCCTGACCAACCAGATCCCAGCTGAAAGCCCTCTGATCCGTCTG
CCCATAGAACCACCTGTCTTTGTGGGCACCCTCGCTTTCTTCACAGCGGCAGCCTTGCTG
TGTCTGGCATTTCTTGCATACCTGTGTTCAGCAACCAGAAGAAAGAGGCACTCCGAGCAT
GCCTTTGACCATGCAGTGGATTCTGACTGA
|
| Enzyme 10 GenBank Gene ID |
AF034840 |
| Enzyme 10 GeneCard ID |
ENTPD3 |
| Enzyme 10 GenAtlas ID |
ENTPD3 |
| Enzyme 10 HGNC ID |
HGNC:3365 |
| Enzyme 10 Chromosome Location |
3 |
| Enzyme 10 Locus |
3p21.3 |
| Enzyme 10 SNPs |
SNPJam Report |
| Enzyme 10 General References |
- Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed ]
- Smith TM, Kirley TL: Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1. Biochim Biophys Acta. 1998 Jul 28;1386(1):65-78. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Smith TM, Lewis Carl SA, Kirley TL: Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase. Biochemistry. 1999 May 4;38(18):5849-57. [PubMed ]
- Yang F, Hicks-Berger CA, Smith TM, Kirley TL: Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry. 2001 Apr 3;40(13):3943-50. [PubMed ]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5321 |
| Enzyme 11 Name |
Serum paraoxonase/lactonase 3 |
| Enzyme 11 Synonyms |
Not Available |
| Enzyme 11 Gene Name |
PON3 |
| Enzyme 11 Protein Sequence |
>Serum paraoxonase/lactonase 3
MGKLVALVLLGVGLSLVGEMFLAFRERVNASREVEPVEPENCHLIEELESGSEDIDILPS
GLAFISSGLKYPGMPNFAPDEPGKIFLMDLNEQNPRAQALEISGGFDKELFNPHGISIFI
DKDNTVYLYVVNHPHMKSTVEIFKFEEQQRSLVYLKTIKHELLKSVNDIVVLGPEQFYAT
RDHYFTNSLLSFFEMILDLRWTYVLFYSPREVKVVAKGFCSANGITVSADQKYVYVADVA
AKNIHIMEKHDNWDLTQLKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLNYNPEDPPG
SEVLRIQNVLSEKPRVSTVYANNGSVLQGTSVASVYHGKILIGTVFHKTLYCEL
|
| Enzyme 11 Number of Residues |
354 |
| Enzyme 11 Molecular Weight |
39607.2 |
| Enzyme 11 Theoretical pI |
5.10 |
| Enzyme 11 GO Classification |
| Function |
- arylesterase activity
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
| — |
| Component |
|
|
| Enzyme 11 General Function |
Involved in arylesterase activity |
| Enzyme 11 Specific Function |
Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
- an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol [RN:R03979]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
29788996 |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q15166 |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PON3_HUMAN |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1065 bp
ATGGGGAAGCTCGTGGCGCTGGTCCTGCTGGGGGTCGGCCTGTCCTTAGTCGGGGAGATG
TTCCTGGCGTTTAGAGAAAGGGTGAATGCCTCTCGAGAAGTGGAGCCAGTAGAACCTGAA
AACTGCCACCTTATTGAGGAACTTGAAAGTGGCTCTGAAGATATTGATATACTTCCTAGT
GGGCTGGCTTTTATCTCCAGTGGATTAAAATATCCAGGCATGCCAAACTTTGCGCCAGAT
GAACCAGGAAAAATCTTCTTGATGGATCTGAATGAACAAAACCCAAGGGCACAAGCGCTA
GAAATCAGTGGTGGATTTGACAAAGAATTATTTAATCCACATGGGATCAGTATTTTCATC
GACAAAGACAATACTGTGTATCTTTATGTTGTGAATCATCCCCACATGAAGTCCACTGTG
GAGATATTTAAATTTGAGGAACAACAACGTTCTCTGGTATACCTGAAAACTATAAAACAT
GAACTTCTCAAAAGTGTGAATGACATTGTGGTTCTTGGACCAGAACAGTTCTATGCCACC
AGAGACCACTATTTTACCAACTCCCTCCTGTCATTTTTTGAGATGATCTTGGATCTTCGC
TGGACTTATGTTCTTTTCTACAGCCCAAGGGAGGTTAAAGTGGTGGCCAAAGGATTTTGT
AGTGCCAATGGGATCACAGTCTCAGCAGACCAGAAGTATGTCTATGTAGCTGATGTAGCA
GCTAAGAACATTCACATAATGGAAAAACATGATAACTGGGATTTAACTCAACTGAAGGTG
ATACAGTTGGGCACCTTAGTGGATAACCTGACTGTCGATCCTGCCACAGGAGACATTTTG
GCAGGATGCCATCCTAATCCTATGAAGCTACTGAACTATAACCCTGAGGACCCTCCAGGA
TCAGAAGTACTTCGCATCCAGAATGTTTTGTCTGAGAAGCCCAGGGTGAGCACCGTGTAT
GCCAACAATGGCTCTGTGCTTCAGGGCACCTCTGTGGCTTCTGTGTACCATGGGAAAATT
CTCATAGGCACCGTATTTCACAAAACTCTGTACTGTGAGCTCTAG
|
| Enzyme 11 GenBank Gene ID |
NM_000940.2 |
| Enzyme 11 GeneCard ID |
PON3 |
| Enzyme 11 GenAtlas ID |
PON3 |
| Enzyme 11 HGNC ID |
HGNC:9206 |
| Enzyme 11 Chromosome Location |
7 |
| Enzyme 11 Locus |
7q21.3 |
| Enzyme 11 SNPs |
SNPJam Report |
| Enzyme 11 General References |
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Primo-Parmo SL, Sorenson RC, Teiber J, La Du BN: The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics. 1996 May 1;33(3):498-507. [PubMed ]
- Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN: Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J Lipid Res. 2005 Jun;46(6):1239-47. Epub 2005 Mar 16. [PubMed ]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5338 |
| Enzyme 12 Name |
Nucleoside diphosphate kinase, mitochondrial |
| Enzyme 12 Synonyms |
- NDK
- NDP kinase, mitochondrial
- Nucleoside diphosphate kinase D
- NDPKD
- nm23-H4
|
| Enzyme 12 Gene Name |
NME4 |
| Enzyme 12 Protein Sequence |
>Nucleoside diphosphate kinase, mitochondrial
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
|
| Enzyme 12 Number of Residues |
187 |
| Enzyme 12 Molecular Weight |
20658.5 |
| Enzyme 12 Theoretical pI |
10.75 |
| Enzyme 12 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 12 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
14336697 |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
O00746 |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
NDKM_HUMAN |
| Enzyme 12 PDB ID |
1EHW |
| Enzyme 12 PDB File |
Show |
| Enzyme 12 3D Structure |
|
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCG
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
|
| Enzyme 12 GenBank Gene ID |
AE006463 |
| Enzyme 12 GeneCard ID |
NME4 |
| Enzyme 12 GenAtlas ID |
NME4 |
| Enzyme 12 HGNC ID |
HGNC:7852 |
| Enzyme 12 Chromosome Location |
1 |
| Enzyme 12 Locus |
16p13.3 |
| Enzyme 12 SNPs |
SNPJam Report |
| Enzyme 12 General References |
- Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed ]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed ]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5340 |
| Enzyme 13 Name |
Ribonucleoside-diphosphate reductase large subunit |
| Enzyme 13 Synonyms |
- Ribonucleoside-diphosphate reductase subunit M1
- Ribonucleotide reductase large subunit
|
| Enzyme 13 Gene Name |
RRM1 |
| Enzyme 13 Protein Sequence |
>Ribonucleoside-diphosphate reductase large subunit
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS
|
| Enzyme 13 Number of Residues |
792 |
| Enzyme 13 Molecular Weight |
90069.4 |
| Enzyme 13 Theoretical pI |
7.16 |
| Enzyme 13 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH or CH2 groups
- oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
- protein binding
- purine nucleoside binding
- ribonucleoside-diphosphate reductase activity
|
| Process |
- DNA metabolic process
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
- oxidation reduction
|
| Component |
- macromolecular complex
- protein complex
- ribonucleoside-diphosphate reductase complex
|
|
| Enzyme 13 General Function |
Involved in oxidation reduction |
| Enzyme 13 Specific Function |
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
36065 |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P23921 |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
RIR1_HUMAN |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>2379 bp
ATGCATGTGATCAAGCGAGATGGCCGCCAAGAACGAGTCATGTTTGACAAAATTACATCT
CGAATCCAGAAGCTTTGTTATGGACTCAATATGGATTTTGTTGATCCTGCTCAGATCACC
ATGAAAGTAATCCAAGGCTTGTACAGTGGGGTCACCACAGTGGAACTAGATACTTTGGCT
GCTGAAACAGCTGCAACCTTGACTACTAAGCACCCTGACTATGCTATCCTGGCAGCCAGG
ATCGCTGTCTCTAACTTGCACAAAGAAACAAAGAAAGTGTTCAGTGATGTGATGGAAGAC
CTCTATAACTACATAAATCCACATAATGGCAAACACTCTCCCATGGTGGCCAAGTCAACA
TTGGATATTGTTCTGGCCAATAAAGATCGCCTGAATTCTGCTATTATCTATGACCGAGAT
TTCTCTTACAATTACTTCGGCTTTAAGACGCTAGAGCGGTCTTATTTGTTGAAGATCAAT
GGAAAAGTGGCTGAAAGACCACAACATATGTTGATGAGAGTATCTGTTGGGATCCACAAA
GAAGACATTGATGCAGCAATTGAAACATATAATCTTCTTTCTGAGAGGTGGTTTACTCAT
GCTTCGCCCACTCTCTTCAATGCTGGTACCAACCGCCCACAACTTTCTAGCTGTTTTCTT
CTGAGTATGAAAGATGACAGCATTGAAGGCATTTATGACACTCTAAAGCAATGTGCATTG
ATTTCTAAGTCTGCTGGAGGAATTGGTGTTGCTGTGAGTTGTATTCGGGCTACTGGCAGC
TACATTGCTGGGACTAATGGCAATTCCAATGGCCTTGTACCGATGCTGAGAGTATATAAC
AACACAGCTCGATATGTGGATCAAGGTGGGAACAAGCGTCCTGGGGCATTTGCTATTTAC
CTGGAGCCTTGGCATTTAGACATCTTTGAATTCCTTGATTTAAAGAAGAACACAGGAAAG
GAAGAGCAGCGTGCCAGAGATCTTTTCTTTGCTCTTTGGATTCCGGATCTCTTCATGAAA
CGAGTGGAGACTAATCAGGACTGGTCTTTGATGTGTCCAAATGAGTGTCCTGGTCTGGAT
GAGGTTTGGGGAGAGGAATTTGAGAAACTATATGCAAGTTATGAGAAACAAGGTCGTGTC
CGCAAAGTTGTAAAAGCTCAGCAGCTTTGGTATGCCATCATTGAGTCTCAGACGGAAACA
GGCACCCCGTATATGCTCTACAAAGATTCCTGTAATCGAAAGAGCAACCAGCAGAACCTG
GGAACCATCAAATGCAGCAACCTGTGCACAGAAATAGTGGAGTACACCAGCAAAGATGAG
GTTGCTGTTTGTAATTTGGCTTCCCTGGCCCTGAATATGTATGTCACATCAGAACACACA
TACGACTTTAAGAAGTTGGCTGAAGTCACTAAAGTCGTTGTCCGAAACTTGAATAAAATT
ATTGATATAAACTACTATCCTGTACCAGAGGCATGCCTATCAAATAAACGCCATCGCCCC
ATTGGAATTGGGGTACAAGGTCTGGCAGATGCTTTTATCCTGATGAGATACCCTTTTGAG
AGTGCAGAAGCCCAGTTACTGAATAAGCAGATCTTTGAAACTATTTATTATGGTGCTCTG
GAAGCCAGCTGTGACCTTGCCAAGGAGCAGGGCCCATACGAAACCTATGAGGGCTCTCCA
GTTAGCAAAGGAATTCTTCAGTATGATATGTGGAATGTTACTCCTACAGACCTATGGGAC
TGGAAGGTTCTCAAGGAGAAGATTGCAAAGTATGGTATAAGAAACAGTTTACTTATTGCC
CCGATGCCTACAGCTTCCACTGCTCAGATCCTGGGGAATAATGAGTCCATTGAACCTTAC
ACCAGCAACATCTATACTCGCAGAGTCTTGTCAGGAGAATTTCAGATTGTAAATCCTCAC
TTATTGAAAGATCTTACCGAGCGGGGCCTATGGCATGAAGAGATGAAAAACCAGATTATT
GCATGCAATGGCTCTATTCAGAGCATACCAGAAATTCCTGATGACCTGAAGCAACTTTAT
AAAACTGTGTGGGAAATCTCTCAGAAAACTGTTCTCAAGATGGCAGCTGAGAGAGGTGCT
TTCATTGATCAAAGCCAATCTTTGAACATCCACATTGCTGAGCCTAACTATGGCAAACTC
ACTAGTATGCACTTCTACGGCTGGAAGCAGGGTTTGAAGACTGGGATGTATTATTTAAGG
ACGAGACCAGCAGCTAATCCAATCCAGTTCACTCTAAATAAGGAGAAGCTAAAAGATAAA
GAAAAGGTATCAAAAGAGGAAGAAGAGAAGGAGAGGAACACAGCAGCCATGGTGTGCTCT
TTGGAGAATAGAGATGAATGTCTGATGTGTGGATCCTGA
|
| Enzyme 13 GenBank Gene ID |
X59543 |
| Enzyme 13 GeneCard ID |
RRM1 |
| Enzyme 13 GenAtlas ID |
RRM1 |
| Enzyme 13 HGNC ID |
HGNC:10451 |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
11p15.5 |
| Enzyme 13 SNPs |
SNPJam Report |
| Enzyme 13 General References |
- Parker NJ, Begley CG, Fox RM: Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression in stimulated lymphocytes. Nucleic Acids Res. 1991 Jul 11;19(13):3741. [PubMed ]
- Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed ]
- Bepler G, O'briant KC, Kim YC, Schreiber G, Pitterle DM: A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region. Genomics. 1999 Jan 15;55(2):164-75. [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 ]
- Parker NJ, Begley CG, Fox RM: Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of the gene. Genomics. 1994 Jan 1;19(1):91-6. [PubMed ]
- Harrington JA, Spector T: Human ribonucleotide reductase. Activation and inhibition by analogs of ATP. Biochem Pharmacol. 1991 Jul 25;42(4):759-63. [PubMed ]
- Xue L, Zhou B, Liu X, Qiu W, Jin Z, Yen Y: Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. Cancer Res. 2003 Mar 1;63(5):980-6. [PubMed ]
- Qiu W, Zhou B, Darwish D, Shao J, Yen Y: Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. Biochem Biophys Res Commun. 2006 Feb 10;340(2):428-34. Epub 2005 Dec 15. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5341 |
| Enzyme 14 Name |
Nucleoside diphosphate kinase A |
| Enzyme 14 Synonyms |
- NDK A
- NDP kinase A
- Granzyme A-activated DNase
- GAAD
- Metastasis inhibition factor nm23
- Tumor metastatic process-associated protein
- nm23-H1
|
| Enzyme 14 Gene Name |
NME1 |
| Enzyme 14 Protein Sequence |
>Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
|
| Enzyme 14 Number of Residues |
152 |
| Enzyme 14 Molecular Weight |
17148.6 |
| Enzyme 14 Theoretical pI |
6.11 |
| Enzyme 14 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 14 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein- coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
4557797 |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P15531 |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
NDKA_HUMAN |
| Enzyme 14 PDB ID |
1JXV |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>459 bp
ATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAACCAGATGGGGTCCAGCGGGGTCTT
GTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGATTCCGCCTTGTTGGTCTGAAATTC
ATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTACGTTGACCTGAAGGACCGTCCATTC
TTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCGGTAGTTGCCATGGTCTGGGAGGGG
CTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGGGAGACCAACCCTGCAGACTCCAAG
CCTGGGACCATCCGTGGAGACTTCTGCATACAAGTTGGCAGGAACATTATACATGGCAGT
GATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTGTGGTTTCACCCTGAGGAACTGGTA
GATTACACGAGCTGTGCTCAGAACTGGATCTATGAATGA
|
| Enzyme 14 GenBank Gene ID |
NM_000269.2 |
| Enzyme 14 GeneCard ID |
NME1 |
| Enzyme 14 GenAtlas ID |
NME1 |
| Enzyme 14 HGNC ID |
HGNC:7849 |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
17q21.3 |
| Enzyme 14 SNPs |
SNPJam Report |
| Enzyme 14 General References |
- Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed ]
- Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed ]
- Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed ]
- Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed ]
- Ni X, Gu S, Dai J, Cheng H, Guo L, Li L, Ji C, Xie Y, Ying K, Mao Y: Isolation and characterization of a novel human NM23-H1B gene, a different transcript of NM23-H1. J Hum Genet. 2003;48(2):96-100. [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 ]
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed ]
- MacDonald NJ, Freije JM, Stracke ML, Manrow RE, Steeg PS: Site-directed mutagenesis of nm23-H1. Mutation of proline 96 or serine 120 abrogates its motility inhibitory activity upon transfection into human breast carcinoma cells. J Biol Chem. 1996 Oct 11;271(41):25107-16. [PubMed ]
- Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed ]
- Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed ]
- Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed ]
- Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed ]
- Garzia L, D'Angelo A, Amoresano A, Knauer SK, Cirulli C, Campanella C, Stauber RH, Steegborn C, Iolascon A, Zollo M: Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility. Oncogene. 2008 Mar 20;27(13):1853-64. Epub 2007 Oct 1. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed ]
- Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed ]
- Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed ]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5342 |
| Enzyme 15 Name |
Nucleoside diphosphate kinase 7 |
| Enzyme 15 Synonyms |
- NDK 7
- NDP kinase 7
- nm23-H7
|
| Enzyme 15 Gene Name |
NME7 |
| Enzyme 15 Protein Sequence |
>Nucleoside diphosphate kinase 7
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
|
| Enzyme 15 Number of Residues |
376 |
| Enzyme 15 Molecular Weight |
42491.4 |
| Enzyme 15 Theoretical pI |
6.44 |
| Enzyme 15 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 15 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
4960169 |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q9Y5B8 |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
NDK7_HUMAN |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1131 bp
ATGAATCATAGTGAAAGATTCGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
|
| Enzyme 15 GenBank Gene ID |
AF153191 |
| Enzyme 15 GeneCard ID |
NME7 |
| Enzyme 15 GenAtlas ID |
NME7 |
| Enzyme 15 HGNC ID |
HGNC:20461 |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
1q24 |
| Enzyme 15 SNPs |
SNPJam Report |
| Enzyme 15 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 ]
- 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 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5343 |
| Enzyme 16 Name |
Ribonucleoside-diphosphate reductase subunit M2 |
| Enzyme 16 Synonyms |
- Ribonucleotide reductase small chain
- Ribonucleotide reductase small subunit
|
| Enzyme 16 Gene Name |
RRM2 |
| Enzyme 16 Protein Sequence |
>Ribonucleoside-diphosphate reductase subunit M2
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
|
| Enzyme 16 Number of Residues |
389 |
| Enzyme 16 Molecular Weight |
44877.2 |
| Enzyme 16 Theoretical pI |
5.05 |
| Enzyme 16 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH or CH2 groups
- oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
- ribonucleoside-diphosphate reductase activity
- transition metal ion binding
|
| Process |
- cellular nitrogen compound metabolic process
- deoxyribonucleoside diphosphate metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside diphosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 16 General Function |
Involved in oxidoreductase activity |
| Enzyme 16 Specific Function |
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
36155 |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P31350 |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
RIR2_HUMAN |
| Enzyme 16 PDB ID |
1H0N |
| Enzyme 16 PDB File |
Show |
| Enzyme 16 3D Structure |
|
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1170 bp
ATGCTCTCCCTCCGTGTCCCGCTCGCGCCCATCACGGACCCGCAGCAGCTGCAGCTCTCG
CCGCTGAAGGGGCTCAGCTTGGTCGACAAGGAGAACACGCCGCCGGCCCTGAGCGGGACC
CGCGTCCTGGCCAGCAAGACCGCGAGGAGGATCTTCCAGGAGCCCACGGAGCCGAAAACT
AAAGCAGCTGCCCCCGGCGTGGAGGATGAGCCGCTGCTGAGAGAAAACCCCCGCCGCTTT
GTCATCTTCCCCATCGAGTACCATGATATCTGGCAGATGTATAAGAAGGCAGAGGCTTCC
TTTTGGACCGCCGAGGAGGTTGACCTCTCCAAGGACATTCAGCACTGGGAATCCCTGAAA
CCCGAGGAGAGATATTTTATATCCCATGTTCTGGCTTTCTTTGCAGCAAGCGATGGCATA
GTAAATGAAAACTTGGTGGAGCGATTTAGCCAAGAAGTTCAGATTACAGAAGCCCGCTGT
TTCTATGGCTTCCAAATTGCCATGGAAAACATACATTCTGAAATGTATAGTCTTCTTATT
GACACTTACATAAAAGATCCCAAAGAAAGGGAATTTCTCTTCAATGCCATTGAAACGATG
CCTTGTGTCAAGAAGAAGGCAGACTGGGCCTTGCGCTGGATTGGGGACAAAGAGGCTACC
TATGGTGAACGTGTTGTAGCCTTTGCTGCAGTGGAAGGCATTTTCTTTTCCGGTTCTTTT
GCGTCGATATTCTGGCTCAAGAAACGAGGACTGATGCCTGGCCTCACATTTTCTAATGAA
CTTATTAGCAGAGATGAGGGTTTACACTGTGATTTTGCTTGCCTGATGTTCAAACACCTG
GTACACAAACCATCGGAGGAGAGAGTAAGAGAAATAATTATCAATGCTGTTCGGATAGAA
CAGGAGTTCCTCACTGAGGCCTTGCCTGTGAAGCTCATTGGGATGAATTGCACTCTAATG
AAGCAATACATTGAGTTTGTGGCAGACAGACTTATGCTGGAACTGGGTTTTAGCAAGGTT
TTCAGAGTAGAGAACCCATTTGACTTTATGGAGAATATTTCACTGGAAGGAAAGACTAAC
TTCTTTGAGAAGAGAGTAGGCGAGTATCAGAGGATGGGAGTGATGTCAAGTCCAACAGAG
AATTCTTTTACCTTGGATGCTGACTTCTAA
|
| Enzyme 16 GenBank Gene ID |
X59618 |
| Enzyme 16 GeneCard ID |
RRM2 |
| Enzyme 16 GenAtlas ID |
RRM2 |
| Enzyme 16 HGNC ID |
HGNC:10452 |
| Enzyme 16 Chromosome Location |
2 |
| Enzyme 16 Locus |
2p25-p24 |
| Enzyme 16 SNPs |
SNPJam Report |
| Enzyme 16 General References |
- Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed ]
- Zhou B, Yen Y: Characterization of the human ribonucleotide reductase M2 subunit gene; genomic structure and promoter analyses. Cytogenet Cell Genet. 2001;95(1-2):52-9. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- 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 ]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
- Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed ]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
- 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 ]
- 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 ]
- 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 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5344 |
| Enzyme 17 Name |
Nucleoside diphosphate kinase B |
| Enzyme 17 Synonyms |
- NDK B
- NDP kinase B
- C-myc purine-binding transcription factor PUF
- nm23-H2
|
| Enzyme 17 Gene Name |
NME2 |
| Enzyme 17 Protein Sequence |
>Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
|
| Enzyme 17 Number of Residues |
152 |
| Enzyme 17 Molecular Weight |
17297.9 |
| Enzyme 17 Theoretical pI |
8.69 |
| Enzyme 17 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 17 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752) |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
4467843 |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P22392 |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
NDKB_HUMAN |
| Enzyme 17 PDB ID |
1NSK |
| Enzyme 17 PDB File |
Show |
| Enzyme 17 3D Structure |
|
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
|
| Enzyme 17 GenBank Gene ID |
X58965 |
| Enzyme 17 GeneCard ID |
NME2 |
| Enzyme 17 GenAtlas ID |
NME2 |
| Enzyme 17 HGNC ID |
HGNC:7850 |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
17q21.3 |
| Enzyme 17 SNPs |
SNPJam Report |
| Enzyme 17 General References |
- Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed ]
- Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed ]
- Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed ]
- Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed ]
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Seifert M, Seib T, Engel M, Dooley S, Welter C: Characterization of the human nm23-H2 promoter region and localization of the microsatellite D17S396. Biochem Biophys Res Commun. 1995 Oct 24;215(3):910-4. [PubMed ]
- Iwashita S, Fujii M, Mukai H, Ono Y, Miyamoto M: Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem Biophys Res Commun. 2004 Aug 6;320(4):1063-8. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed ]
- Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed ]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5345 |
| Enzyme 18 Name |
Nucleoside diphosphate kinase 3 |
| Enzyme 18 Synonyms |
- NDK 3
- NDP kinase 3
- DR-nm23
- Nucleoside diphosphate kinase C
- NDPKC
- nm23-H3
|
| Enzyme 18 Gene Name |
NME3 |
| Enzyme 18 Protein Sequence |
>Nucleoside diphosphate kinase 3
MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGFKLVALKLVQA
SEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDVVRTSRALIGATNPADAPPGT
IRGDFCIEVGKNLIHGSDSVESARREIALWFRADELLCWEDSAGHWLYE
|
| Enzyme 18 Number of Residues |
169 |
| Enzyme 18 Molecular Weight |
19014.9 |
| Enzyme 18 Theoretical pI |
7.97 |
| Enzyme 18 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 18 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
14336763 |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q13232 |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
NDK3_HUMAN |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>510 bp
ATGATCTGCCTGGTGCTGACCATCTTCGCTAACCTCTTCCCCGCGGCCTGCACCGGCGCA
CACGAACGCACCTTCCTGGCCGTGAAGCCGGACGGCGTGCAGCGGCGGCTGGTGGGCGAG
ATTGTGCGGCGCTTCGAGAGGAAGGGCTTCAAGTTGGTGGCGCTGAAGCTGGTGCAGGCC
TCCGAGGAGCTGCTGCGTGAGCACTACGCCGAGCTGCGTGAACGCCCGTTCTACGGCCGC
CTTGTCAAGTATATGGCCTCCGGGCCGGTGGTGGCCATGGTTTGGCAGGGGCTGGACGTG
GTGCGCACCTCGCGGGCGCTCATCGGAGCCACGAACCCGGCCGACGCCCCGCCCGGCACC
ATCCGCGGGGATTTCTGCATCGAGGTTGGCAAGAACCTGATTCACGGCAGCGACTCGGTG
GAGAGTGCCCGCCGCGAGATCGCTCTCTGGTTCCGCGCAGACGAGCTCCTCTGCTGGGAG
GACAGCGCTGGGCACTGGCTGTATGAGTAG
|
| Enzyme 18 GenBank Gene ID |
AE006639 |
| Enzyme 18 GeneCard ID |
NME3 |
| Enzyme 18 GenAtlas ID |
NME3 |
| Enzyme 18 HGNC ID |
HGNC:7851 |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
16q13 |
| Enzyme 18 SNPs |
SNPJam Report |
| Enzyme 18 General References |
- Venturelli D, Martinez R, Melotti P, Casella I, Peschle C, Cucco C, Spampinato G, Darzynkiewicz Z, Calabretta B: Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7435-9. [PubMed ]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed ]
- 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 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5346 |
| Enzyme 19 Name |
Nucleoside diphosphate kinase 6 |
| Enzyme 19 Synonyms |
- NDK 6
- NDP kinase 6
- Inhibitor of p53-induced apoptosis-alpha
- IPIA-alpha
- nm23-H6
|
| Enzyme 19 Gene Name |
NME6 |
| Enzyme 19 Protein Sequence |
>Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
|
| Enzyme 19 Number of Residues |
186 |
| Enzyme 19 Molecular Weight |
21142.0 |
| Enzyme 19 Theoretical pI |
8.49 |
| Enzyme 19 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 19 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 19 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
3228530 |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
O75414 |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
NDK6_HUMAN |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
|
| Enzyme 19 GenBank Gene ID |
AF051941 |
| Enzyme 19 GeneCard ID |
NME6 |
| Enzyme 19 GenAtlas ID |
NME6 |
| Enzyme 19 HGNC ID |
HGNC:20567 |
| Enzyme 19 Chromosome Location |
3 |
| Enzyme 19 Locus |
3p21 |
| Enzyme 19 SNPs |
SNPJam Report |
| Enzyme 19 General References |
- Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [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 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5442 |
| Enzyme 20 Name |
Glucokinase |
| Enzyme 20 Synonyms |
- Hexokinase type IV
- HK IV
- Hexokinase-4
- HK4
- Hexokinase-D
|
| Enzyme 20 Gene Name |
GCK |
| Enzyme 20 Protein Sequence |
>Glucokinase
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPT
YVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAE
MLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN
VVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQN
VELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGE
LVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPS
TTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK
ERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ
|
| Enzyme 20 Number of Residues |
465 |
| Enzyme 20 Molecular Weight |
52191.1 |
| Enzyme 20 Theoretical pI |
4.85 |
| Enzyme 20 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 20 General Function |
Involved in ATP binding |
| Enzyme 20 Specific Function |
Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- ATP + D-glucose = ADP + D-glucose 6-phosphate [RN:R00299]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
179427 |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
P35557 |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
HXK4_HUMAN |
| Enzyme 20 PDB ID |
1V4T |
| Enzyme 20 PDB File |
Show |
| Enzyme 20 3D Structure |
|
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1398 bp
ATGCTGGACGACAGAGCCAGGATGGAGGCCGCCAAGAAGGAGAAGGTAGAGCAGATCCTG
GCAGAGTTCCAGCTGCAGGAGGAGGACCTGAAGAAGGTGATGAGACGGATGCAGAAGGAG
ATGGACCGCGGCCTGAGGCTGGAGACCCATGAAGAGGCCAGTGTGAAGATGCTGCCCACC
TACGTGCGCTCCACCCCAGAAGGCTCAGAAGTCGGGGACTTCCTCTCCCTGGACCTGGGT
GGCACTAACTTCAGGGTGATGCTGGTGAAGGTGGGAGAAGGTGAGGAGGGGCAGTGGAGC
GTGAAGACCAAACACCAGATGTACTCCATCCCCGAGGACGCCATGACCGGCACTGCTGAG
ATGCTCTTCGACTACATCTCTGAGTGCATCTCCGACTTCCTGGACAAGCATCAGATGAAA
CACAAGAAGCTGCCCCTGGGCTTCACCTTCTCCTTTCCTGTGAGGCACGAAGACATCGAT
AAGGGCATCCTTCTCAACTGGACCAAGGGCTTCAAGGCCTCAGGAGCAGAAGGGAACAAT
GTCGTGGGGCTTCTGCGAGACGCTATCAAACGGAGAGGGGACTTTGAAATGGATGTGGTG
GCAATGGTGAATGACACGGTGGCCACGATGATCTCCTGCTACTACGAAGACCATCAGTGC
GAGGTCGGCATGATCGTGGGCACGGGCTGCAATGCCTGCTACATGGAGGAGATGCAGAAT
GTGGAGCTGGTGGAGGGGGACGAGGGCCGCATGTGCGTCAATACCGAGTGGGGCGCCTTC
GGGGACTCCGGCGAGCTGGACGAGTTCCTGCTGGAGTATGACCGCCTGGTGGACGAGAGC
TCTGCAAACCCCGGTCAGCAGCTGTATGAGAAGCTCATAGGTGGCAAGTACATGGGCGAG
CTGGTGCGGCTTGTGCTGCTCAGGCTCGTGGACGAAAACCTGCTCTTCCACGGGGAGGCC
TCCGAGCAGCTGCGCACACGCGGAGCCTTCGAGACGCGCTTCGTGTCGCAGGTGGAGAGC
GACACGGGCGACCGCAAGCAGATCTACAACATCCTGAGCACGCTGGGGCTGCGACCCTCG
ACCACCGACTGCGACATCGTGCGCCGCGCCTGCGAGAGCGTGTCTACGCGCGCTGCGCAC
ATGTGCTCGGCGGGGCTGGCGGGCGTCATCAACCGCATGCGCGAGAGCCGCAGCGAGGAC
GTAATGCGCATCACTGTGGGCGTGGATGGCTCCGTGTACAAGCTGCACCCCAGCTTCAAG
GAGCGGTTCCATGCCAGCGTGCGCAGGCTGACGCCCAGCTGCGAGATCACCTTCATCGAG
TCGGAGGAGGGCAGTGGCCGGGGCGCGGCCCTGGTCTCGGCGGTGGCCTGTAAGAAGGCC
TGTATGCTGGGCCAGTGA
|
| Enzyme 20 GenBank Gene ID |
M88011 |
| Enzyme 20 GeneCard ID |
GCK |
| Enzyme 20 GenAtlas ID |
GCK |
| Enzyme 20 HGNC ID |
HGNC:4195 |
| Enzyme 20 Chromosome Location |
7 |
| Enzyme 20 Locus |
7p15.3-p15.1 |
| Enzyme 20 SNPs |
SNPJam Report |
| Enzyme 20 General References |
- Tanizawa Y, Matsutani A, Chiu KC, Permutt MA: Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. Mol Endocrinol. 1992 Jul;6(7):1070-81. [PubMed ]
- Tanizawa Y, Koranyi LI, Welling CM, Permutt MA: Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7294-7. [PubMed ]
- Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J: Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. Diabetologia. 1992 Aug;35(8):743-7. [PubMed ]
- Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. Diabetes. 1992 Jul;41(7):807-11. [PubMed ]
- Stoffel M, Froguel P, Takeda J, Zouali H, Vionnet N, Nishi S, Weber IT, Harrison RW, Pilkis SJ, Lesage S, et al.: Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7698-702. [PubMed ]
- Sakura H, Eto K, Kadowaki H, Simokawa K, Ueno H, Koda N, Fukushima Y, Akanuma Y, Yazaki Y, Kadowaki T: Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1992 Dec;75(6):1571-3. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
- 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 ]
- St Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes. 1994 Jun;43(6):784-91. [PubMed ]
- Kamata K, Mitsuya M, Nishimura T, Eiki J, Nagata Y: Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase. Structure. 2004 Mar;12(3):429-38. [PubMed ]
- Mitsuya M, Kamata K, Bamba M, Watanabe H, Sasaki Y, Sasaki K, Ohyama S, Hosaka H, Nagata Y, Eiki J, Nishimura T: Discovery of novel 3,6-disubstituted 2-pyridinecarboxamide derivatives as GK activators. Bioorg Med Chem Lett. 2009 May 15;19(10):2718-21. Epub 2009 Mar 29. [PubMed ]
- Stoffel M, Patel P, Lo YM, Hattersley AT, Lucassen AM, Page R, Bell JI, Bell GI, Turner RC, Wainscoat JS: Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. Nat Genet. 1992 Oct;2(2):153-6. [PubMed ]
- Chiu KC, Tanizawa Y, Permutt MA: Glucokinase gene variants in the common form of NIDDM. Diabetes. 1993 Apr;42(4):579-82. [PubMed ]
- Stoffel M, Bell KL, Blackburn CL, Powell KL, Seo TS, Takeda J, Vionnet N, Xiang KS, Gidh-Jain M, Pilkis SJ, et al.: Identification of glucokinase mutations in subjects with gestational diabetes mellitus. Diabetes. 1993 Jun;42(6):937-40. [PubMed ]
- Takeda J, Gidh-Jain M, Xu LZ, Froguel P, Velho G, Vaxillaire M, Cohen D, Shimada F, Makino H, Nishi S, et al.: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants. J Biol Chem. 1993 Jul 15;268(20):15200-4. [PubMed ]
- Gidh-Jain M, Takeda J, Xu LZ, Lange AJ, Vionnet N, Stoffel M, Froguel P, Velho G, Sun F, Cohen D, et al.: Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1932-6. [PubMed ]
- Hager J, Blanche H, Sun F, Vaxillaire NV, Poller W, Cohen D, Czernichow P, Velho G, Robert JJ, Cohen N, et al.: Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique. Diabetes. 1994 May;43(5):730-3. [PubMed ]
- Velho G, Blanche H, Vaxillaire M, Bellanne-Chantelot C, Pardini VC, Timsit J, Passa P, Deschamps I, Robert JJ, Weber IT, Marotta D, Pilkis SJ, Lipkind GM, Bell GI, Froguel P: Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families. Diabetologia. 1997 Feb;40(2):217-24. [PubMed ]
- Guazzini B, Gaffi D, Mainieri D, Multari G, Cordera R, Bertolini S, Pozza G, Meschi F, Barbetti F: Three novel missense mutations in the glucokinase gene (G80S; E221K; G227C) in Italian subjects with maturity-onset diabetes of the young (MODY). Mutations in brief no. 162. Online. Hum Mutat. 1998;12(2):136. [PubMed ]
- Hattersley AT, Beards F, Ballantyne E, Appleton M, Harvey R, Ellard S: Mutations in the glucokinase gene of the fetus result in reduced birth weight. Nat Genet. 1998 Jul;19(3):268-70. [PubMed ]
- Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC: Familial hyperinsulinism caused by an activating glucokinase mutation. N Engl J Med. 1998 Jan 22;338(4):226-30. [PubMed ]
- Ng MC, Cockburn BN, Lindner TH, Yeung VT, Chow CC, So WY, Li JK, Lo YM, Lee ZS, Cockram CS, Critchley JA, Bell GI, Chan JC: Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY. Diabet Med. 1999 Nov;16(11):956-63. [PubMed ]
- Nam JH, Lee HC, Kim YH, Cha BS, Song YD, Lim SK, Kim KR, Huh KB: Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus. Diabetes Res Clin Pract. 2000 Dec;50(3):169-76. [PubMed ]
- Njolstad PR, Sovik O, Cuesta-Munoz A, Bjorkhaug L, Massa O, Barbetti F, Undlien DE, Shiota C, Magnuson MA, Molven A, Matschinsky FM, Bell GI: Neonatal diabetes mellitus due to complete glucokinase deficiency. N Engl J Med. 2001 May 24;344(21):1588-92. [PubMed ]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5444 |
| Enzyme 21 Name |
Hexokinase-3 |
| Enzyme 21 Synonyms |
- Hexokinase type III
- HK III
|
| Enzyme 21 Gene Name |
HK3 |
| Enzyme 21 Protein Sequence |
>Hexokinase-3
MDSIGSSGLRQGEETLSCSEEGLPGPSDSSELVQECLQQFKVTRAQLQQIQASLLGSMEQ
ALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP
RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRST
LISWTKGFRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVG
LVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALGPVLTTFDHTLDHESLN
PGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST
GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ
VAVATGGRVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHR
RLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLA
LDLGGTNFRVLLVRVTTGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQ
SLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQAVELNVVAI
VNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGD
DGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ
RLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLC
GAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPRCVVTFLQSE
DGSGKGAALVTAVACRLAQLTRV
|
| Enzyme 21 Number of Residues |
923 |
| Enzyme 21 Molecular Weight |
99024.6 |
| Enzyme 21 Theoretical pI |
5.06 |
| Enzyme 21 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Involved in ATP binding |
| Enzyme 21 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate [RN:R02848]
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
20380888 |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
P52790 |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
HXK3_HUMAN |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>2772 bp
ATGGACTCCATTGGGTCTTCAGGGTTGCGGCAGGGGGAAGAAACCCTGAGTTGCTCTGAG
GAGGGCTTGCCCGGGCCCTCAGACAGCTCAGAGCTGGTGCAGGAGTGCCTGCAGCAGTTC
AAGGTGACAAGGGCACAGCTACAGCAGATCCAAGCCAGCCTCTTGGGTTCCATGGAGCAG
GCGCTGAGGGGACAGGCCAGCCCTGCCCCTGCGGTCCGGATGCTGCCTACATACGTGGGG
TCCACCCCACATGGCACTGAGCAAGGAGACTTCGTGGTGCTGGAGCTGGGGGCCACAGGG
GCCTCACTGCGTGTTTTGTGGGTGACTCTAACTGGCATTGAGGGGCATAGGGTGGAGCCC
AGAAGCCAGGAGTTTGTGATCCCCCAAGAGGTGATGCTGGGTGCTGGCCAGCAGCTCTTT
GACTTTGCTGCCCACTGCCTGTCTGAGTTCCTGGATGCGCAGCCTGTGAACAAACAGGGT
CTGCAGCTTGGCTTCAGCTTCTCTTTCCCTTGTCACCAGACGGGCTTGGACAGGAGCACC
CTCATTTCCTGGACCAAAGGTTTTAGGTGCAGTGGTGTGGAAGGCCAGGATGTGGTCCAG
CTGCTGAGAGATGCCATTCGGAGGCAGGGGGCCTACAACATCGACGTGGTTGCTGTGGTG
AACGACACAGTGGGCACCATGATGGGCTGTGAGCCGGGGGTCAGGCCGTGTGAGGTTGGG
CTAGTTGTAGACACGGGCACCAACGCGTGTTACATGGAGGAGGCACGGCATGTGGCAGTG
CTGGACGAAGACCGGGGCCGCGTCTGCGTCAGCGTCGAGTGGGGCTCCTTCAGCGATGAT
GGGGCGCTGGGACCAGTGCTGACCACCTTCGACCATACCCTGGACCATGAGTCCCTGAAT
CCTGGTGCTCAGAGGTTTGAGAAGATGATCGGAGGCCTGTACCTGGGTGAGCTGGTGCGG
CTGGTGCTGGCTCACTTGGCCCGGTGTGGGGTCCTCTTTGGTGGCTGCACCTCCCCTGCC
CTGCTGAGCCAAGGCAGCATCCTCCTGGAACACGTGGCTGAGATGGAGGACCCCTCTACT
GGGGCAGCCCGTGTCCATGCTATCCTGCAGGACTTGGGCCTGAGCCCTGGGGCTTCGGAT
GTTGAGCTTGTGCAGCACGTCTGTGCGGCCGTGTGCACGCGGGCTGCCCAGCTCTGTGCT
GCCGCCCTGGCCGCTGTTCTCTCCTGCCTCCAGCACAGCCGGGAGCAACAAACACTCCAG
GTTGCTGTGGCCACCGGAGGCCGAGTGTGTGAGCGGCACCCCAGGTTCTGCAGCGTCCTG
CAGGGGACAGTGATGCTCCTGGCCCCGGAATGCGATGTCTCCTTAATCCCCTCTGTGGAT
GGTGGTGGCCGGGGAGTGGCGATGGTGACTGCTGTGGCTGCCCGTCTGGCTGCCCACCGG
CGCCTGCTGGAGGAGACCCTGGCCCCATTCCGGTTGAACCATGATCAACTGGCTGCGGTT
CAGGCACAGATGCGGAAGGCCATGGCCAAGGGGCTCCGAGGGGAGGCCTCCTCCCTTCGC
ATGCTGCCCACTTTCGTCCGGGCCACCCCTGATGGCAGCGAGCGAGGGGATTTCCTGGCC
CTGGACCTCGGGGGCACGAACTTCCGTGTCCTCCTGGTACGTGTGACCACAGGCGTGCAG
ATCACCAGCGAGATCTACTCCATTCCCGAGACTGTGGCCCAGGGTTCTGGGCAGCAGCTC
TTTGACCACATCGTGGACTGCATCGTGGACTTCCAGCAGAAGCAGGGCCTGAGCGGGCAG
AGCCTCCCACTGGGTTTTACCTTCTCCTTCCCATGTAGGCAGCTTGGCCTAGACCAGGGC
ATCCTCCTGAACTGGACCAAGGGTTTCAAGGCATCAGACTGCGAGGGCCAAGATGTCGTG
AGTCTGTTGCGGGAAGCCATCACTCGCAGACAGGCAGTGGAGCTGAATGTGGTTGCCATT
GTCAATGACACGGTGGGGACCATGATGTCCTGTGGCTATGAGGACCCCCGTTGCGAGATA
GGCCTCATTGTCGGAACCGGCACCAATGCCTGCTACATGGAGGAGCTCCGGAATGTGGCG
GGCGTGCCTGGGGACTCAGGCCGCATGTGCATCAACATGGAGTGGGGCGCCTTTGGGGAC
GATGGCTCTCTGGCCATGCTCAGCACCCGCTTTGATGCAAGTGTGGACCAGGCGTCCATC
AACCCCGGCAAGCAGAGGTTTGAAAAGATGATCAGCGGCATGTACCTGGGGGAGATCGTC
CGCCACATCCTTTTACATTTAACCAGCCTTGGCGTTCTCTTCCGGGGCCAGCAGATCCAG
CGCCTTCAGACCAGGGACATCTTCAAGACCAAGTTCCTCTCTGAGATCGAAAGTGACAGC
CTGGCCCTGCGGCAGGTCCGAGCCATCCTAGAGGATCTGGGGCTACCCCTGACCTCAGAT
GACGCCCTGATGGTGCTAGAGGTGTGCCAGGCTGTGTCCCAGAGGGCTGCCCAGCTCTGT
GGGGCGGGTGTAGCTGCCGTGGTGGAGAAGATCCGGGAGAACCGGGGCCTGGAAGAGCTG
GCAGTGTCTGTGGGGGTGGATGGAACGCTCTACAAGCTGCACCCGCGCTTCTCCAGCCTG
GTGGCGGCCACAGTGCGGGAGCTGGCCCCTCGCTGTGTGGTCACGTTCCTGCAGTCAGAG
GATGGGTCCGGCAAAGGTGCGGCCCTGGTCACCGCTGTTGCCTGCCGCCTTGCGCAGTTG
ACTCGTGTCTGA
|
| Enzyme 21 GenBank Gene ID |
BC028129 |
| Enzyme 21 GeneCard ID |
HK3 |
| Enzyme 21 GenAtlas ID |
HK3 |
| Enzyme 21 HGNC ID |
HGNC:4925 |
| Enzyme 21 Chromosome Location |
5 |
| Enzyme 21 Locus |
5q35.2 |
| Enzyme 21 SNPs |
SNPJam Report |
| Enzyme 21 General References |
- Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI: Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization. Genomics. 1996 Aug 15;36(1):206-9. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Palma F, Agostini D, Mason P, Dacha M, Piccoli G, Biagiarelli B, Fiorani M, Stocchi V: Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein. Mol Cell Biochem. 1996 Feb 9;155(1):23-9. [PubMed ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5445 |
| Enzyme 22 Name |
Hexokinase-2 |
| Enzyme 22 Synonyms |
- Hexokinase type II
- HK II
- Muscle form hexokinase
|
| Enzyme 22 Gene Name |
HK2 |
| Enzyme 22 Protein Sequence |
>Hexokinase-2
MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAA
VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMR
GSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGV
EGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYME
EMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGM
YMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLG
LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKH
PHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLS
HDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRV
LLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGF
TFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVG
TMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD
FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRG
IFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAA
VVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKG
AALITAVACRIREAGQR
|
| Enzyme 22 Number of Residues |
917 |
| Enzyme 22 Molecular Weight |
102379.1 |
| Enzyme 22 Theoretical pI |
5.93 |
| Enzyme 22 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 22 General Function |
Involved in ATP binding |
| Enzyme 22 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate [RN:R02848]
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
4809269 |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P52789 |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
HXK2_HUMAN |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>2754 bp
ATGATTGCCTCGCATCTGCTTGCCTACTTCTTCACGGAGCTCAACCATGACCAAGTGCAG
AAGGTTGACCAGTATCTCTACCACATGCGCCTCTCTGATGAGACCCTCTTGGAGATCTCT
AAGCGGTTCCGCAAGGAGATGGAGAAAGGGCTTGGAGCCACCACTCACCCTACTGCAGCA
GTGAAGATGCTGCCCACCTTTGTGAGGTCCACTCCAGATGGGACAGAACACGGAGAGTTC
CTGGCTCTGGATCTTGGAGGGACCAACTTCCGTGTGCTTTGGGTGAAAGTAACGGACAAT
GGGCTCCAGAAGGTGGAGATGGAGAATCAGATCTATGCCATCCCTGAGGACATCATGCGA
GGCAGTGGCACCCAGCTGTTTGACCACATTGCCGAATGCCTGGCTAACTTCATGGATAAG
CTACAAATCAAAGACAAGAAGCTCCCACTGGGTTTTACCTTCTCGTTCCCCTGCCACCAG
ACTAAACTAGACGAGAGTTTCCTGGTCTCATGGACCAAGGGATTCAAGTCCAGTGGAGTG
GAAGGCAGAGACGTTGTGGCTCTGATCCGGAAGGCCATCCAGAGGAGAGGGGACTTTGAT
ATCGACATTGTGGCTGTGGTGAATGACACAGTTGGGACCATGATGACCTGTGGTTATGAT
GACCACAACTGTGAGATTGGTCTCATTGTGGGCACGGGCAGCAACGCCTGCTACATGGAA
GAGATGCGCCACATCGACATGGTGGAAGGCGATGAGGGGCGGATGTGTATCAATATGGAG
TGGGGGGCCTTCGGGGACGATGGCTCGCTCAACGACATTCGCACTGAGTTTGACCAGGAG
ATTGACATGGGCTCACTGAACCCGGGAAAGCAACTGTTTGAGAAGATGATCAGTGGGATG
TACATGGGGGAGCTGGTGAGGCTTATCCTGGTGAAGATGGCCAAGGAGGAGCTGCTCTTT
GGGGGGAAGCTCAGCCCAGAGCTTCTCAACACCGGTCGCTTTGAGACCAAAGACATCTCA
GACATTGAAGGGGAGAAGGATGGCATCCGGAAGGCCCGTGAGGTCCTGATGCGGTTGGGC
CTGGACCCGACTCAGGAGGACTGCGTGGCCACTCACCGGATCTGCCAGATCGTGTCCACA
CGCTCCGCCAGCCTGTGCGCAGCCACCCTGGCCGCCGTGCTGCAGCGCATCAAGGAGAAC
AAAGGCGAGGAGCGGCTGCGCTCTACTATTGGGGTCGACGGTTCCGTCTACAAGAAACAC
CCCCATTTTGCCAAGCGTCTACATAAGACCGTGCGGCGGCTGGTGCCCGGCTGCGATGTC
CGCTTCCTCCGCTCCGAGGATGGCAGTGGCAAAGGTGCAGCCATGGTGACAGCAGTGGCT
TACCGGCTGGCCGATCAACACCGTGCCCGCCAGAAGACATTAGAGCATCTGCAGCTGAGC
CATGACCAGCTGCTGGAGGTCAAGAGGAGGATGAAGGTAGAAATGGAGCGAGGTCTGAGC
AAGGAGACTCATGCCAGTGCCCCCGTCAAGATGCTGCCCACCTACGTGTGTGCTACCCCG
GACGGCACAGAGAAAGGGGACTTCTTGGCCTTGGACCTTGGAGGAACAAATTTCCGGGTC
CTGCTGGTCCGTGTTCGGAATGGGAAGTGGGGTGGAGTGGAGATGCACAACAAGATCTAC
GCCATCCCGCAGGAGGTCATGCACGGCACCGGGGACGAGCTCTTTGACCACATTGTCCAG
TGCATCGCGGACTTCCTCGAGTACATGGGCATGAAGGGCGTGTCCCTGCCTCTGGGTTTT
ACCTTCTCCTTCCCCTGCCAGCAGAACAGCCTGGACGAGAGCATCCTCCTCAAGTGGACA
AAAGGCTTCAAGGCATCTGGCTGCGAGGGCGAGGACGTGGTGACCCTGCTGAAGGAAGCG
ATCCACCGGCGAGAGGAGTTTGACCTGGATGTGGTTGCTGTGGTGAACGACACAGTCGGA
ACTATGATGACCTGTGGCTTTGAAGACCCTCACTGTGAAGTTGGCCTCATTGTTGGCACG
GGCAGCAATGCCTGCTACATGGAGGAGATGCGCAACGTGGAACTGGTGGAAGGAGAAGAG
GGGCGGATGTGTGTGAACATGGAATGGGGGGCATTCGGGGACAATGGATGCCTAGATGAC
TTCCGCACAGAATTTGATGTGGCTGTGGATGAGCTTTCACTCAACCCCGGCAAGCAGAGG
TTCGAGAAAATGATCAGTGGAATGTACCTGGGTGAGATTGTCCGTAACATTCTCATCGAT
TTCACCAAGCGTGGACTGCTCTTCCGAGGCCGCATCTCAGAGCGGCTCAAGACAAGGGGC
ATCTTTGAAACCAAGTTCTTGTCTCAGATTGAGAGTGACTGCCTGGCCCTGCTGCAAGTC
CGAGCCATCCTGCAACACTTAGGGCTTGAGAGCACCTGTGACGACAGCATCATTGTTAAG
GAGGTGTGCACTGTGGTGGCCCGGCGGGCAGCCCAGCTCTGTGGCGCAGGCATGGCCGCT
GTGGTGGACAGGATACGAGAAAACCGTGGGCTGGACGCTCTCAAAGTGACAGTGGGTGTG
GATGGGACCCTCTACAAGCTACATCCTCACTTTGCCAAAGTCATGCATGAGACAGTGAAG
GACCTGGCTCCGAAATGTGATGTGTCTTTCCTGCAGTCAGAGGATGGCAGCGGGAAGGGG
GCGGCGCTCATCACTGCTGTGGCCTGCCGCATCCGTGAGGCTGGACAGCGATAG
|
| Enzyme 22 GenBank Gene ID |
AF148513 |
| Enzyme 22 GeneCard ID |
HK2 |
| Enzyme 22 GenAtlas ID |
HK2 |
| Enzyme 22 HGNC ID |
HGNC:4923 |
| Enzyme 22 Chromosome Location |
2 |
| Enzyme 22 Locus |
2p13 |
| Enzyme 22 SNPs |
SNPJam Report |
| Enzyme 22 General References |
- Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun. 1993 Nov 30;197(1):68-74. [PubMed ]
- Lehto M, Huang X, Davis EM, Le Beau MM, Laurila E, Eriksson KF, Bell GI, Groop L: Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia. 1995 Dec;38(12):1466-74. [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 ]
- Shinohara Y, Yamamoto K, Kogure K, Ichihara J, Terada H: Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines. Cancer Lett. 1994 Jul 15;82(1):27-32. [PubMed ]
- Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes. 1995 Mar;44(3):330-4. [PubMed ]
- Vidal-Puig A, Printz RL, Stratton IM, Granner DK, Moller DE: Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution. Diabetes. 1995 Mar;44(3):340-6. [PubMed ]
- Echwald SM, Bjorbaek C, Hansen T, Clausen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O: Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes. 1995 Mar;44(3):347-53. [PubMed ]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5465 |
| Enzyme 23 Name |
Diacylglycerol kinase alpha |
| Enzyme 23 Synonyms |
- DAG kinase alpha
- 80 kDa diacylglycerol kinase
- Diglyceride kinase alpha
- DGK-alpha
|
| Enzyme 23 Gene Name |
DGKA |
| Enzyme 23 Protein Sequence |
>Diacylglycerol kinase alpha
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS
|
| Enzyme 23 Number of Residues |
735 |
| Enzyme 23 Molecular Weight |
82629.5 |
| Enzyme 23 Theoretical pI |
6.71 |
| Enzyme 23 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- diacylglycerol kinase activity
- ion binding
- kinase activity
- metal ion binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 23 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 23 Specific Function |
Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity |
| Enzyme 23 Pathways |
- Glycerolipid Metabolism (map00561 )
- Phospholipid Synthesis (map00564 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 23 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
30823 |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
P23743 |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
DGKA_HUMAN |
| Enzyme 23 PDB ID |
1TUZ |
| Enzyme 23 PDB File |
Show |
| Enzyme 23 3D Structure |
|
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>2208 bp
ATGGCCAAGGAGAGGGGCCTAATAAGCCCCAGTGATTTTGCCCAGCTGCAAAAATACATG
GAATACTCCACCAAAAAGGTCAGTGATGTCCTAAAGCTCTTCGAGGATGGCGAGATGGCT
AAATATGTCCAAGGAGATGCCATTGGGTACGAGGGATTCCAGCAATTCCTGAAAATCTAT
CTCGAAGTGGATAATGTTCCCAGACACCTAAGCCTGGCACTGTTTCAATCCTTTGAGACT
GGTCACTGCTTAAATGAGACAAATGTGACAAAAGATGTGGTGTGTCTCAATGATGTTTCC
TGCTACTTTTCCCTTCTGGAGGGTGGTCGGCCAGAAGACAAGTTAGAATTCACCTTCAAG
CTGTACGACACGGACAGAAATGGGATCCTGGACAGCTCAGAAGTGGACAAAATTATCCTA
CAGATGATGCGAGTGGCTGAATACCTGGATTGGGATGTGTCTGAGCTGAGGCCGATTCTT
CAGGAGATGATGAAAGAGATTGACTATGATGGCAGTGGCTCTGTCTCTCAAGCTGAGTGG
GTCCGGGCTGGGGCCACCACCGTGCCACTGCTAGTGCTGCTGGGTCTGGAGATGACTCTG
AAGGACGACGGACAGCACATGTGGAGGCCCAAGAGGTTCCCCAGACCAGTCTACTGCAAT
CTGTGCGAGTCAAGCATTGGTCTTGGCAAACAGGGACTGAGCTGTAACCTCTGTAAGTAC
ACTGTTCACGACCAGTGTGCCATGAAAGCCCTGCCTTGTGAAGTCAGCACCTATGCCAAG
TCTCGGAAGGACATTGGTGTCCAATCACATGTGTGGGTGCGAGGAGGCTGTGAGTCCGGG
CGCTGCGACCGCTGTCAGAAAAAGATCCGGATCTACCACAGTCTGACCGGGCTGCATTGT
GTATGGTGCCACCTAGAGATCCACGATGACTGCCTGCAAGCGGTGGGCCATGAGTGTGAC
TGTGGGCTGCTCCGGGATCACATCCTGCCTCCATCTTCCATCTATCCCAGTGTCCTGGCC
TCTGGACCGGATCGTAAAAATAGCAAAACAAGCCAGAAGACCATGGATGATTTAAATTTG
AGCACCTCTGAGGCTCTGCGGATTGACCCTGTTCCTAACACCCACCCACTTCTCGTCTTT
GTCAATCCTAAGAGTGGCGGGAAGCAGGGGCAGAGGGTGCTCTGGAAGTTCCAGTATATA
TTAAACCCTCGACAGGTGTTCAACCTCCTAAAGGATGGTCCTGAGATAGGGCTCCGATTA
TTCAAGGATGTTCCTGATAGCCGGATTTTGGTGTGTGGTGGAGACGGCACAGTAGGCTGG
ATTCTAGAGACCATTGACAAAGCTAACTTGCCAGTTTTGCCTCCTGTTGCTGTGTTGCCC
CTGGGTACTGGAAATGATCTGGCTCGATGCCTAAGATGGGGAGGAGGTTATGAAGGACAG
AATCTGGCAAAGATCCTCAAGGATTTAGAGATGAGTAAAGTGGTACATATGGATCGATGG
TCTGTGGAGGTGATACCTCAACAAACTGAAGAAAAAAGTGACCCAGTCCCCTTTCAAATC
ATCAATAACTACTTCTCTATTGGCGTGGATGCCTCTATTGCTCATCGATTCCACATCATG
CGAGAGAAATATCCGGAGAAGTTCAACAGCAGAATGAAGAACAAGCTATGGTACTTCGAA
TTTGCCACATCTGAATCCATCTTCTCAACATGCAAAAAGCTGGAGGAGTCTTTGACAGTT
GAGATCTGTGGGAAACCGCTGGATCTGAGCAACCTGTCCCTAGAAGGCATCGCAGTGCTA
AACATCCCTAGCATGCATGGTGGCTCCAACCTCTGGGGTGATACCAGGAGACCCCATGGG
GATATCTATGGGATCAACCAGGCCTTAGGTGCTACAGCTAAAGTCATCACCGACCCTGAT
ATCCTGAAAACCTGTGTACCAGACCTAAGTGACAAGAGACTGGAAGTGGTTGGGCTGGAG
GGTGCAATTGAGATGGGCCAAATCTATACCAAGCTCAAGAATGCTGGACGTCGGCTGGCC
AAGTGCTCTGAGATCACCTTCCACACCACAAAAACCCTTCCCATGCAAATTGACGTAGAA
CCCTGGATGCAGACGCCCTGTACAATCAAGATCACCCACAAGAACCAGATGCCCATGCTC
ATGGGCCCACCCCCCCGCTCCACCAATTTCTTTGGCTTCTTGAGCTAA
|
| Enzyme 23 GenBank Gene ID |
X62535 |
| Enzyme 23 GeneCard ID |
DGKA |
| Enzyme 23 GenAtlas ID |
DGKA |
| Enzyme 23 HGNC ID |
HGNC:2849 |
| Enzyme 23 Chromosome Location |
1 |
| Enzyme 23 Locus |
12q13.3 |
| Enzyme 23 SNPs |
SNPJam Report |
| Enzyme 23 General References |
- Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL: Purification, cDNA-cloning and expression of human diacylglycerol kinase. FEBS Lett. 1990 Nov 26;275(1-2):151-8. [PubMed ]
- Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Hart TC, Champagne C, Zhou J, Van Dyke TE: Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12. Mamm Genome. 1994 Feb;5(2):123-4. [PubMed ]
- Hart TC, Zhou J, Champagne C, Van Dyke TE, Rao PN, Pettenati MJ: Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis. Genomics. 1994 Jul 1;22(1):246-7. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
5466 |
| Enzyme 24 Name |
Diacylglycerol kinase delta |
| Enzyme 24 Synonyms |
- DAG kinase delta
- 130 kDa diacylglycerol kinase
- Diglyceride kinase delta
- DGK-delta
|
| Enzyme 24 Gene Name |
DGKD |
| Enzyme 24 Protein Sequence |
>Diacylglycerol kinase delta
MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTIIKEGML
TKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITP
CRKLILCADNRKEMEDWIAALKTVQNREHFEPTQYSMDHFSGMHNWYACSHARPTYCNVC
REALSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDADGIAMPHQWLE
GNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLLTKCPLGLCKVSVIPPTA
LNSIDSDGFWKASCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPH
LGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGS
ACDDDTQLPQILEKLERASTKMLDRWSVMAYEAKLPRQASSSTVTEDFSEDSEVQQILFY
EDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSEESEVMAKKCS
VLKEKLDSLLKTLDDESQASSSLPNPPPTIAEEAEDGDGSGSICGSTGDRLVASACPARP
QIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQEGFVLGLSESEEKMDHRVC
PPLSHSESFGVPKGRSQRKVSKSPCEKLISKGSLSLGSSASLPPQPGSRDGLPALNTKIL
YPNVRAGMSGSLPGGSVISRLLINADPFNSEPETLEYYTEKCVMNNYFGIGLDAKISLDF
NNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYKNLEQKVLLECDGRPIPLPSLQGIAV
LNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIRLQHHRIAQCR
TVKISILGDEGVPVQVDGEAWVQPPGYIRIVHKNRAQTLTRDRAFESTLKSWEDKQKCEL
PRPPSCSLHPEMLSEEEATQMDQFGQAAGVLIHSIREIAQSHRDMEQELAHAVNASSKSM
DRVYGKPRTTEGLNCSFVLEMVNNFRALRSETELLLSGKMALQLDPPQKEQLGSALAEMD
RQLRRLADTPWLCQSAEPGDEESVMLDLAKRSRSGKFRLVTKFKKEKNNKNKEAHSSLGA
PVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILC
GIKELSRSAPAVEA
|
| Enzyme 24 Number of Residues |
1214 |
| Enzyme 24 Molecular Weight |
134524.2 |
| Enzyme 24 Theoretical pI |
7.58 |
| Enzyme 24 GO Classification |
| Function |
- catalytic activity
- diacylglycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 24 Specific Function |
Isoform 2 may be involved in cell growth and tumorigenesis. Involved in clathrin-dependent endocytosis |
| Enzyme 24 Pathways |
- Glycerolipid Metabolism (map00561 )
- Phospholipid Synthesis (map00564 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 24 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
22773821 |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q16760 |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
DGKD_HUMAN |
| Enzyme 24 PDB ID |
1R79 |
| Enzyme 24 PDB File |
Show |
| Enzyme 24 3D Structure |
|
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>3645 bp
ATGGCGGCGGCGGCGGGCGCCCCTCCGCCGGGTCCCCCGCAACCGCCTCCGCCGCCGCCG
CCCGAGGAGTCGTCCGACAGCGAGCCCGAGGCGGAGCCCGGCTCCCCACAGAAGCTCATC
CGCAAGGTGTCCACGTCGGGTCAGATCCGACAGAAGACCATCATCAAAGAGGGGATGCTG
ACCAAACAGAACAATTCATTCCAGCGATCAAAAAGGAGATACTTTAAGCTTCGAGGGCGA
ACGCTTTACTATGCCAAAACGGCAAAGTCAATCATATTTGATGAGGTGGATCTGACAGAT
GCCAGCGTAGCTGAATCCAGTACCAAAAACGTCAACAACAGTTTTACGGTCATAACTCCA
TGCAGGAAGCTCATCTTGTGTGCTGATAACAGAAAAGAAATGGAAGATTGGATTGCAGCA
TTAAAGACTGTGCAGAACAGGGAGCACTTTGAGCCCACCCAGTACAGCATGGACCACTTC
TCAGGGATGCACAATTGGTACGCCTGTTCCCACGCGAGGCCGACCTACTGCAATGTGTGC
CGTGAGGCTCTGTCTGGGGTCACGTCGCACGGGCTGTCCTGCGAGGTGTGCAAATTTAAG
GCCCACAAGCGCTGTGCTGTGCGTGCAACCAATAACTGCAAGTGGACCACACTGGCCTCG
ATCGGGAAGGACATCATTGAAGATGCAGATGGGATTGCAATGCCCCACCAGTGGTTGGAA
GGAAACCTACCTGTGAGCGCCAAGTGCACTGTGTGCGACAAGACCTGTGGCAGTGTGCTG
CGCCTGCAGGACTGGCGCTGCCTCTGGTGCAAGGCCATGGTTCACACATCGTGTAAAGAA
TCCTTGCTGACCAAGTGCCCACTTGGCCTGTGCAAAGTGTCAGTCATCCCACCCACGGCT
CTCAACAGCATCGACTCCGATGGGTTCTGGAAGGCCAGCTGTCCTCCTTCTTGCACAAGC
CCACTGTTGGTCTTCGTCAATTCAAAAAGTGGGGACAACCAGGGTGTGAAGTTCCTCAGA
AGATTCAAACAGCTACTAAACCCCGCCCAGGTCTTCGACCTCATGAACGGAGGCCCACAC
CTCGGCTTACGGTTATTCCAGAAGTTTGACACATTCCGGATTCTGGTTTGTGGCGGGGAT
GGAAGTGTTGGCTGGGTCCTCTCCGAAATCGACAGCCTCAACCTTCATAAACAGTGTCAG
CTGGGAGTGCTGCCGCTCGGCACAGGGAACGACTTGGCCCGAGTACTGGGCTGGGGCTCA
GCCTGCGATGACGACACCCAGCTCCCCCAGATCTTGGAGAAGTTGGAGAGAGCCAGCACC
AAGATGCTGGACAGGTGGAGCGTCATGGCATACGAGGCCAAGCTCCCCCGGCAGGCCTCC
TCCTCTACCGTCACCGAAGACTTCAGCGAGGATTCCGAGGTACAGCAGATTCTCTTCTAT
GAAGACTCGGTTGCAGCCCACCTTTCTAAAATCCTCACCTCGGACCAGCACTCGGTGGTC
ATCTCCTCGGCCAAAGTGCTCTGTGAGACGGTGAAGGACTTCGTGGCACGGGTGGGGAAG
GCCTATGAGAAGACGACCGAGAGCTCGGAGGAGTCAGAGGTCATGGCCAAGAAGTGCTCT
GTCCTGAAAGAGAAGCTGGATTCCCTTCTCAAGACCTTGGACGATGAGTCCCAGGCCTCG
TCCTCTCTGCCCAACCCGCCCCCCACCATTGCCGAGGAGGCTGAAGATGGAGATGGGTCG
GGCAGCATCTGCGGTTCCACCGGAGACCGCTTGGTGGCATCAGCTTGCCCGGCCCGGCCG
CAGATATTCCGGCCTCGAGAACAGCTCATGCTGAGAGCCAACAGCCTGAAGAAAGCAATT
CGTCAGATCATAGAACACACAGAAAAAGCTGTCGATGAGCAGAATGCCCAGACCCAGGAG
CAGGAGGGCTTCGTCCTGGGCCTCTCTGAGTCAGAGGAGAAGATGGACCACAGAGTGTGC
CCACCACTGTCCCACAGCGAGAGCTTCGGGGTCCCCAAGGGGAGGAGCCAGCGCAAAGTG
TCGAAATCTCCGTGTGAAAAGCTGATCAGCAAAGGGAGTCTGTCCCTAGGCAGTTCTGCT
TCCCTTCCGCCCCAGCCGGGAAGCCGGGACGGCCTGCCTGCGCTCAACACCAAGATCCTG
TACCCAAATGTCCGGGCTGGAATGTCTGGTTCCTTACCCGGTGGCTCAGTCATCAGTCGC
CTGTTAATTAATGCTGATCCCTTCAACTCTGAACCAGAAACCCTAGAGTATTACACGGAG
AAATGTGTCATGAACAACTATTTTGGCATTGGCCTGGATGCGAAGATATCCCTGGACTTT
AACAACAAGCGCGATGAGCACCCAGAGAAGTGCAGGAGCCGAACCAAGAACATGATGTGG
TATGGAGTTCTTGGAACCAAAGAGTTGCTGCACAGAACCTACAAGAACCTGGAGCAAAAG
GTCTTGCTGGAGTGTGACGGGCGACCCATCCCACTCCCCAGTCTTCAGGGAATTGCTGTC
CTTAACATTCCCAGCTATGCCGGAGGAACCAACTTCTGGGGGGGTACCAAGGAAGATGAT
ACTTTCGCAGCTCCATCATTCGATGACAAGATTCTGGAGGTGGTCGCCGTGTTCGGCAGC
ATGCAGATGGCCGTCTCTCGAGTCATCAGGCTACAGCATCATCGGATCGCCCAGTGTCGC
ACGGTGAAGATCTCCATCCTTGGGGATGAGGGCGTGCCTGTGCAGGTGGACGGAGAGGCC
TGGGTCCAGCCGCCAGGGTACATTCGGATTGTCCACAAGAACCGGGCACAGACACTGACC
AGAGACAGGGCATTTGAGAGCACCCTGAAGTCCTGGGAAGACAAGCAGAAGTGCGAGGTG
CCCCGCCCTCCATCCTGTTCCCTGCACCCGGAGATGCTGTCCGAGGAGGAGGCCACCCAG
ATGGACCAGTTTGGGCAGGCAGCAGGGGTCCTCATTCACAGTATCCGAGAAATAGCTCAG
TCTCACCGGGACATGGAGCAGGAACTGGCCCACGCCGTCAATGCCAGCTCCAAGTCCATG
GACCGTGTGTATGGCAAGCCCAGAACCACAGAGGGGCTCAACTGCAGCTTCGTCCTGGAA
ATGGTGAATAACTTCAGAGCTCTGCGCAGTGAGACGGAGCTGCTGCTGTCTGGGAAGATG
GCCCTGCAGCTGGATCCGCCTCAGAAGGAGCAGCTGGGGAGTGCTCTTGCCGAGATGGAC
CGACAGCTCAGGAGGCTGGCAGACACCCCGTGGCTCTGCCAGTCCGCAGAGCCCGGCGAC
GAAGAGAGTGTGATGCTGGATCTTGCCAAGCGCAGTCGCAGTGGTAAATTCCGCCTCGTG
ACCAAGTTTAAAAAGGAGAAAAACAACAAGAACAAAGAAGCTCACAGTAGCCTGGGAGCC
CCGGTTCACCTCTGGGGGACAGAGGAGGTTGCTGCCTGGCTGGAGCACCTCAGTCTCTGT
GAGTATAAGGACATCTTCACACGGCACGACATCCGGGGCTCTGAGCTCCTGCACCTGGAG
CGGAGGGACCTCAAGGACCTGGGCGTGACCAAGGTGGGCCACATGAAGAGGATCCTGTGT
GGCATCAAGGAGCTGAGCCGCAGCGCCCCCGCCGTCGAGGCCTAG
|
| Enzyme 24 GenBank Gene ID |
AB078966 |
| Enzyme 24 GeneCard ID |
DGKD |
| Enzyme 24 GenAtlas ID |
DGKD |
| Enzyme 24 HGNC ID |
HGNC:2851 |
| Enzyme 24 Chromosome Location |
2 |
| Enzyme 24 Locus |
2q37.1 |
| Enzyme 24 SNPs |
SNPJam Report |
| Enzyme 24 General References |
- Sakane F, Imai S, Yamada K, Murakami T, Tsushima S, Kanoh H: Alternative splicing of the human diacylglycerol kinase delta gene generates two isoforms differing in their expression patterns and in regulatory functions. J Biol Chem. 2002 Nov 8;277(45):43519-26. Epub 2002 Aug 27. [PubMed ]
- Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N: Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995 Aug 31;2(4):167-74, 199-210. [PubMed ]
- Sakane F, Imai S, Kai M, Wada I, Kanoh H: Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases. J Biol Chem. 1996 Apr 5;271(14):8394-401. [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 ]
- Imai S, Sakane F, Kanoh H: Phorbol ester-regulated oligomerization of diacylglycerol kinase delta linked to its phosphorylation and translocation. J Biol Chem. 2002 Sep 20;277(38):35323-32. Epub 2002 Jun 25. [PubMed ]
- Kawasaki T, Kobayashi T, Ueyama T, Shirai Y, Saito N: Regulation of clathrin-dependent endocytosis by diacylglycerol kinase delta: importance of kinase activity and binding to AP2alpha. Biochem J. 2008 Jan 15;409(2):471-9. [PubMed ]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
5470 |
| Enzyme 25 Name |
Diacylglycerol kinase beta |
| Enzyme 25 Synonyms |
- DAG kinase beta
- 90 kDa diacylglycerol kinase
- Diglyceride kinase beta
- DGK-beta
|
| Enzyme 25 Gene Name |
DGKB |
| Enzyme 25 Protein Sequence |
>Diacylglycerol kinase beta
MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDF
EGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPMVKSKPALLSGGLRMNKGAITPPR
TTSPANTCSPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIISQ
MMHVAEYLEWDVTELNPILHEMMEEIDYDHDGTVSLEEWIQGGMTTIPLLVLLGLENNVK
DDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCVARAPPSCIKTYVK
SKRNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQITLHNKCASHLKPECDC
GPLKDHILPPTTICPVVLQTLPTSGVSVPEERQSTVKKEKSGSQQPNKVIDKNKMQRANS
VTVDGQGLQVTPVPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGL
NFFRDVPDFRVLACGGDGTVGWVLDCIEKANVGKHPPVAILPLGTGNDLARCLRWGGGYE
GENLMKILKDIENSTEIMLDRWKFEVIPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFH
IMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLEGIA
ILNIPSMHGGSNLWGESKKRRSHRRIEKKGSDKRTTVTDAKELKFASQDLSDQLLEVVGL
EGAMEMGQIYTGLKSAGRRLAQCSCVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPM
LMGPPPKTGLFCSLVKRTRNRSKE
|
| Enzyme 25 Number of Residues |
804 |
| Enzyme 25 Molecular Weight |
90594.7 |
| Enzyme 25 Theoretical pI |
7.90 |
| Enzyme 25 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- diacylglycerol kinase activity
- ion binding
- kinase activity
- metal ion binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 25 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 25 Specific Function |
Exhibits high phosphorylation activity for long-chain diacylglycerols |
| Enzyme 25 Pathways |
- Glycerolipid Metabolism (map00561 )
- Phospholipid Synthesis (map00564 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 25 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
22027632 |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q9Y6T7 |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
DGKB_HUMAN |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>2415 bp
ATGACAAACCAGGAAAAATGGGCCCACCTCAGCCCTTCGGAATTTTCCCAACTTCAGAAA
TATGCTGAGTATTCTACAAAGAAATTAAAGGATGTTCTTGAAGAATTCCATGGTAATGGT
GTGCTTGCAAAGTATAATCCTGAAGGGAAACAAGACATTCTTAACCAAACAATAGATTTT
GAAGGTTTCAAACTATTCATGAAGACATTCCTGGAAGCCGAGCTTCCTGATGATTTCACT
GCACACCTTTTCATGTCATTTAGCAACAAGTTTCCTCATTCTAGTCCAATGGTAAAAAGT
AAGCCTGCTCTCCTATCAGGCGGTCTGAGAATGAATAAAGGTGCCATCACCCCTCCCCGG
ACTACTTCTCCTGCAAATACGTGTTCCCCAGAAGTAATCCATCTGAAGGACATTGTCTGT
TACCTGTCTCTGCTTGAAAGAGGAAGACCTGAGGATAAGCTTGAGTTTATGTTTCGCCTT
TATGACACGGATGGGAATGGCTTCCTGGACAGCTCGGAGCTAGAAAATATCATCAGTCAG
ATGATGCATGTTGCAGAATACCTTGAGTGGGATGTCACTGAACTTAATCCAATCCTCCAT
GAAATGATGGAAGAAATTGACTATGATCATGATGGAACCGTGTCTCTGGAGGAATGGATT
CAAGGAGGAATGACAACGATTCCACTTCTTGTGCTCCTGGGCTTAGAAAATAACGTGAAG
GATGATGGACAGCACGTGTGGCGACTGAAGCACTTTAACAAACCTGCCTATTGCAACCTT
TGCCTGAACATGCTGATTGGCGTGGGGAAGCAGGGCCTCTGCTGTTCCTTCTGCAAGTAC
ACAGTCCATGAGCGCTGTGTGGCTCGAGCACCTCCCTCTTGCATCAAGACCTATGTGAAG
TCCAAAAGGAACACTGATGTCATGCACCATTACTGGGTTGAAGGTAACTGCCCAACCAAG
TGTGATAAGTGCCACAAAACTGTTAAATGTTACCAGGGCCTGACAGGACTGCATTGTGTT
TGGTGTCAGATCACACTGCATAATAAATGTGCTTCTCATCTAAAACCTGAATGTGACTGT
GGACCTTTGAAGGACCATATTTTACCACCCACAACAATCTGTCCAGTGGTACTGCAGACT
CTGCCCACTTCAGGAGTTTCAGTTCCTGAGGAAAGACAATCAACAGTGAAAAAGGAAAAG
AGTGGTTCCCAGCAGCCAAACAAAGTGATTGACAAGAATAAAATGCAAAGAGCCAACTCT
GTTACTGTAGATGGACAAGGCCTGCAGGTCACTCCTGTGCCTGGTACTCACCCACTTTTA
GTTTTTGTGAACCCCAAAAGTGGTGGAAAACAAGGAGAACGAATTTACAGAAAATTCCAG
TATCTATTAAATCCTCGTCAGGTTTACAGTCTTTCTGGAAATGGACCAATGCCAGGGTTA
AACTTTTTCCGTGATGTTCCTGACTTCAGAGTGTTAGCCTGTGGTGGAGATGGAACCGTG
GGCTGGGTTTTGGATTGCATAGAAAAGGCCAATGTAGGCAAGCATCCTCCAGTTGCGATT
CTGCCTCTTGGGACTGGCAATGATCTAGCAAGATGCCTGCGATGGGGAGGAGGTTACGAA
GGTGAGAATCTGATGAAAATTCTAAAAGACATTGAAAACAGCACAGAAATCATGTTGGAC
AGGTGGAAGTTTGAAGTCATACCTAATGACAAAGATGAGAAAGGAGACCCAGTGCCTTAC
AGTATCATCAATAATTACTTTTCCATTGGCGTGGATGCCTCCATTGCACACAGATTCCAC
ATCATGAGAGAAAAACACCCAGAGAAATTCAACAGTAGAATGAAGAACAAATTTTGGTAT
TTTGAGTTTGGCACATCTGAAACTTTCTCAGCCACCTGCAAGAAGCTACATGAATCTGTA
GAAATAGAATGTGATGGAGTACAGATAGATTTAATAAACATCTCTCTGGAAGGAATTGCT
ATTTTGAATATACCAAGCATGCATGGAGGATCCAATCTTTGGGGAGAGTCTAAGAAAAGA
CGAAGCCATCGACGAATAGAGAAAAAAGGGTCTGACAAAAGGACCACCGTCACAGATGCC
AAAGAGTTGAAGTTTGCAAGTCAAGATCTCAGTGACCAGCTGCTGGAGGTGGTCGGCTTG
GAAGGAGCCATGGAGATGGGGCAAATATACACAGGCCTGAAAAGTGCTGGCCGGCGGCTG
GCTCAGTGCTCCTGCGTGGTCATCAGGACGAGCAAGTCTCTGCCAATGCAAATTGATGGG
GAGCCATGGATGCAGACCCCATGCACAATAAAAATTACACACAAGAACCAAGCCCCAATG
CTGATGGGCCCGCCTCCAAAAACCGGTTTATTCTGCTCCCTCGTCAAAAGGACAAGAAAC
CGAAGCAAGGAATAA
|
| Enzyme 25 GenBank Gene ID |
NM_004080.2 |
| Enzyme 25 GeneCard ID |
DGKB |
| Enzyme 25 GenAtlas ID |
DGKB |
| Enzyme 25 HGNC ID |
HGNC:2850 |
| Enzyme 25 Chromosome Location |
7 |
| Enzyme 25 Locus |
7p21.2 |
| Enzyme 25 SNPs |
SNPJam Report |
| Enzyme 25 General References |
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
- 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 ]
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed ]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
5472 |
| Enzyme 26 Name |
Diacylglycerol kinase iota |
| Enzyme 26 Synonyms |
- DAG kinase iota
- Diglyceride kinase iota
- DGK-iota
|
| Enzyme 26 Gene Name |
DGKI |
| Enzyme 26 Protein Sequence |
>Diacylglycerol kinase iota
MDAAGRGCHLLPLPAARGPARAPAAAAAAAASPPGPCSGAACAPSAAAGAGAMNPSSSAG
EEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGSAAAAGAAALDEPAAAGQKEKDEALEE
KLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLW
LETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG
SRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCF
MLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGMEQENK
GRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEL
YRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDE
PVSKILCQVEDGTVVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVT
LEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQEL
KFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGER
LHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSV
PDRLRIRVNKISLQDYEGFHYDKEKLREASISDWLRTIAGELVQSFGAIPLGILVVRGDC
DLETCRMYIDRLQEDLQSVSSGSQRVHYQDHETSFPRALSAQRLSPRWCFLDDRSQEHLH
FVMEISQDEIFILDPDMVVSQPAGTPPGMPDLVVEQASGISDWWNPALRKRMLSDSGLGM
IAPYYEDSDLKDLSHSRVLQSPVSSEDHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHC
SLLHYAAKTGNGEIVKYILDHGPSELLDMADSETGETALHKAACQRNRAVCQLLVDAGAS
LRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETAV
|
| Enzyme 26 Number of Residues |
1065 |
| Enzyme 26 Molecular Weight |
116996.2 |
| Enzyme 26 Theoretical pI |
7.81 |
| Enzyme 26 GO Classification |
| Function |
- catalytic activity
- diacylglycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 26 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 26 Specific Function |
ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl- sn-glycerol 3-phosphate |
| Enzyme 26 Pathways |
- Glycerolipid Metabolism (map00561 )
- Phospholipid Synthesis (map00564 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 26 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
3676530 |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
O75912 |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
DGKI_HUMAN |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>3198 bp
ATGGATGCTGCGGGAAGGGGCTGCCATTTGCTGCCCCTGCCAGCGGCGCGCGGACCTGCC
CGCGCTCCTGCAGCCGCCGCCGCCGCCGCCGCCAGCCCGCCCGGCCCCTGCAGCGGCGCC
GCCTGCGCTCCCTCCGCGGCCGCCGGAGCGGGCGCCATGAACCCCAGCTCCTCGGCGGGA
GAGGAGAAAGGGGCGACGGGCGGCAGCAGCAGCAGCGGAAGCGGCGCCGGGAGCTGCTGC
CTGGGCGCCGAGGGCGGCGCGGACCCGCGGGGCGCAGGGTCAGCCGCGGCGGCGGGGGCC
GCTGCCCTGGACGAGCCCGCGGCCGCCGGCCAGAAGGAGAAGGACGAAGCGCTGGAGGAG
AAGCTGAGGAACTTAACTTTCCGGAAGCAGGTCTCGTACAGGAAAGCAATCTCCCGGGCA
GGCCTCCAGCATCTGGCTCCTGCACATCCCCTCAGCCTTCCTGTGGCAAATGGTCCAGCC
AAGGAGCCCAGAGCGACTTTGGACTGGAGTGAGAATGCCGTGAATGGAGAACACCTGTGG
CTGGAGACCAACGTCTCGGGAGACCTCTGCTACCTTGGAGAGGAGAACTGCCAAGTCAGA
TTTGCAAAATCAGCTCTCAGGAGGAAGTGTGCAGTCTGTAAAATCGTCGTCCACACCGCC
TGCATTGAGCAGCTAGAAAAGATTAATTTCAGATGTAAACCAACATTTCGAGAAGGAGGC
TCAAGGTCACCAAGAGAAAATTTTGTACGTCATCACTGGGTGCACAGGCGTCGGCAGGAG
GGGAAATGTAAGCAGTGTGGTAAGGGCTTCCAGCAAAAGTTCTCCTTCCACAGTAAAGAG
ATTGTGGCTATCAGCTGTTCCTGGTGCAAGCAGGCGTTTCACAATAAGGTGACCTGCTTC
ATGCTGCATCACATTGAAGAACCCTGCTCCCTGGGGGCTCATGCTGCTGTTATTGTCCCG
CCCACTTGGATCATTAAGGTGAAGAAACCTCAGAACTCCCTGAAGGCTTCAAATCGGAAG
AAGAAGAGAACAAGCTTTAAAAGAAAAGCCAGTAAAAGAGGGATGGAACAGGAAAACAAA
GGTCGTCCTTTTGTGATAAAACCCATCTCTTCTCCTCTCATGAAACCCTTGCTTGTATTT
GTGAATCCCAAGAGTGGAGGCAACCAGGGAACCAAAGTCCTGCAGATGTTCATGTGGTAC
CTGAATCCACGGCAAGTCTTTGATCTTTCTCAGGAAGGGCCAAAAGATGCGCTTGAATTG
TATAGGAAAGTACCAAATCTGCGAATTCTGGCCTGTGGTGGGGATGGAACGGTGGGCTGG
ATCCTTTCCATCCTGGATGAACTGCAGCTGAGCCCTCAGCCTCCTGTGGGGGTCCTTCCT
CTGGGGACTGGGAATGACCTGGCTCGAACTCTCAACTGGGGAGGGGGCTACACTGATGAA
CCTGTTTCTAAGATCCTGTGTCAAGTGGAAGATGGGACAGTTGTACAGCTAGATCGCTGG
AACCTCCATGTGGAAAGAAACCCCGACTTGCCTCCAGAAGAACTTGAAGATGGCGTATGT
AAGCTCCCTCTGAATGTTTTCAATAACTACTTCAGCCTTGGATTTGATGCCCATGTCACA
CTGGAGTTCCATGAATCCAGAGAAGCAAATCCAGAGAAATTCAACAGTCGTTTTCGAAAT
AAAATGTTCTATGCAGGGGCAGCTTTTTCTGACTTCCTACAGAGAAGTTCTAGAGATCTA
TCCAAACATGTTAAAGTTGTTTGTGATGGAACAGATCTCACCCCAAAGATTCAGGAACTG
AAGTTCCAGTGTATAGTATTTTTAAATATACCCAGATATTGTGCTGGCACAATGCCCTGG
GGAAACCCAGGTGATCACCATGATTTCGAACCTCAGCGTCATGATGATGGTTATATTGAA
GTCATTGGATTTACCATGGCCTCTTTGGCAGCCCTGCAAGTTGGGGGCCATGGAGAGAGG
CTACACCAGTGTCGAGAAGTCATGCTTCTAACTTACAAATCCATCCCCATGCAAGTGGAT
GGGGAGCCCTGTAGGTTGGCCCCAGCTATGATTCGGATCTCCCTGAGGAATCAGGCCAAC
ATGGTACAGAAGAGCAAGAGGAGAACATCCATGCCTTTACTCAATGATCCCCAGTCTGTC
CCAGATCGTCTGAGGATCCGGGTGAACAAAATCAGTTTACAAGACTATGAAGGATTCCAC
TATGACAAGGAGAAACTCCGAGAAGCTTCTATTTCAGACTGGTTAAGAACCATTGCTGGG
GAACTAGTGCAGTCATTTGGAGCGATACCTCTGGGTATTCTAGTTGTGCGTGGAGACTGT
GATTTGGAGACTTGCCGTATGTACATAGACCGCCTACAGGAGGACCTACAGTCAGTTTCT
TCTGGCTCCCAGAGAGTTCATTACCAGGACCATGAAACCTCCTTCCCCAGGGCTCTCTCA
GCACAGAGGCTCTCTCCTCGGTGGTGCTTCCTAGATGACAGATCTCAGGAACATTTGCAC
TTTGTGATGGAGATTTCCCAAGATGAGATTTTTATTCTGGACCCAGATATGGTGGTGTCA
CAGCCGGCGGGGACACCTCCGGGCATGCCTGACCTGGTGGTGGAACAAGCCTCGGGGATC
TCAGACTGGTGGAATCCTGCCCTGCGGAAACGCATGCTGAGTGACAGTGGGCTGGGGATG
ATAGCTCCCTATTATGAGGACTCAGATCTGAAAGATCTCAGCCACTCCCGCGTGCTACAG
TCACCAGTCTCTTCAGAAGATCATGCAATTTTGCAGGCAGTAATAGCTGGTGATCTTATG
AAGCTAATAGAAAGCTATAAAAATGGAGGCAGTCTGCTAATTCAGGGACCAGACCACTGT
TCACTCCTTCACTACGCAGCTAAAACCGGCAACGGGGAGATTGTGAAATATATCCTTGAC
CACGGACCTTCCGAGTTATTGGATATGGCAGACAGTGAAACGGGTGAGACTGCACTGCAC
AAGGCTGCCTGCCAGCGGAACCGGGCTGTGTGCCAGCTTCTGGTGGATGCAGGAGCATCT
CTGAGAAAGACGGACTCCAAGGGTAAGACACCTCAAGAAAGAGCACAGCAGGCTGGGGAC
CCAGACTTGGCTGCTTACCTAGAAAGCCGTCAGAACTATAAGGTCATTGGCCATGAGGAC
CTGGAAACTGCTGTTTGA
|
| Enzyme 26 GenBank Gene ID |
AF061936 |
| Enzyme 26 GeneCard ID |
DGKI |
| Enzyme 26 GenAtlas ID |
DGKI |
| Enzyme 26 HGNC ID |
HGNC:2855 |
| Enzyme 26 Chromosome Location |
7 |
| Enzyme 26 Locus |
7q32.3-q33 |
| Enzyme 26 SNPs |
SNPJam Report |
| Enzyme 26 General References |
- Ding L, Traer E, McIntyre TM, Zimmerman GA, Prescott SM: The cloning and characterization of a novel human diacylglycerol kinase, DGKiota. J Biol Chem. 1998 Dec 4;273(49):32746-52. [PubMed ]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
- Bowne SJ, Sullivan LS, Ding L, Traer E, Prescott SM, Birch DG, Kennan A, Humphries P, Daiger SP: Evaluation of human diacylglycerol kinase(iota), DGKI, a homolog of Drosophila rdgA, in inherited retinopathy mapping to 7q. Mol Vis. 2000 Feb 22;6:6-9. [PubMed ]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
5478 |
| Enzyme 27 Name |
Diacylglycerol kinase zeta |
| Enzyme 27 Synonyms |
- DAG kinase zeta
- Diglyceride kinase zeta
- DGK-zeta
|
| Enzyme 27 Gene Name |
DGKZ |
| Enzyme 27 Protein Sequence |
>Diacylglycerol kinase zeta
METFFRRHFRGKVPGPGEGQQRPSSVGLPTGKARRRSPAGQASSSLAQRRRSSAQLQGCL
LSCGVRAQGSSRRRSSTVPPSCNPRFIVDKVLTPQPTTVGAQLLGAPLLLTGLVGMNEEE
GVQEDVVAEASSAIQPGTKTPGPPPPRGAQPLLPLPRYLRRASSHLLPADAVYDHALWGL
HGYYRRLSQRRPSGQHPGPGGRRASGTTAGTMLPTRVRPLSRRRQVALRRKAAGPQAWSA
LLAKAITKSGLQHLAPPPPTPGAPCSESERQIRSTVDWSESATYGEHIWFETNVSGDFCY
VGEQYCVARMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVR
HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCS
LGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSP
LMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILAC
GGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEG
NVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANP
EKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIP
RYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTT
SKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRV
SMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKL
SPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLP
TSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAV
STGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQG
DTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
|
| Enzyme 27 Number of Residues |
1117 |
| Enzyme 27 Molecular Weight |
124127.3 |
| Enzyme 27 Theoretical pI |
9.31 |
| Enzyme 27 GO Classification |
| Function |
- catalytic activity
- diacylglycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 27 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 27 Specific Function |
Displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. Isoform 2 but not isoform 1 regulates RASGRP1 activity |
| Enzyme 27 Pathways |
- Glycerolipid Metabolism (map00561 )
- Phospholipid Synthesis (map00564 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 27 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
157688564 |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q13574 |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
DGKZ_HUMAN |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>3354 bp
ATGGAGACTTTCTTTAGGAGACATTTCCGGGGGAAGGTGCCAGGCCCTGGAGAGGGGCAG
CAGCGGCCCAGCAGCGTGGGGCTGCCCACAGGCAAGGCCCGGCGTCGCTCCCCCGCTGGG
CAGGCCTCCTCCTCACTGGCACAGCGGCGCCGCTCCAGCGCCCAGCTCCAGGGCTGCCTC
CTGAGTTGCGGGGTGAGGGCCCAGGGTTCCAGCCGCCGGCGCTCCAGCACTGTGCCCCCT
TCCTGCAACCCCCGCTTCATCGTGGATAAGGTGCTCACTCCACAGCCTACCACCGTGGGG
GCCCAGCTTCTGGGTGCACCCCTGCTGTTGACCGGGCTTGTGGGCATGAATGAGGAGGAG
GGTGTCCAGGAGGATGTGGTAGCCGAGGCATCGAGCGCCATCCAGCCAGGCACCAAGACA
CCAGGGCCACCCCCACCTCGGGGCGCCCAGCCGCTGTTGCCCCTACCCCGCTACCTGCGC
CGAGCCTCCTCCCACCTGCTCCCCGCGGATGCCGTATATGACCACGCTCTCTGGGGCCTG
CACGGCTACTATCGGCGCCTCAGCCAGCGGCGGCCCTCAGGCCAGCACCCTGGCCCTGGG
GGCCGAAGAGCCTCAGGCACCACCGCCGGCACCATGCTGCCCACCCGTGTGCGCCCACTG
TCCCGCAGGCGCCAGGTAGCCCTACGGCGCAAGGCGGCCGGACCCCAGGCCTGGAGCGCC
CTGCTCGCGAAAGCCATCACCAAGTCGGGCCTCCAGCACCTGGCCCCCCCTCCGCCCACC
CCTGGGGCCCCGTGCAGCGAGTCAGAGCGGCAGATCCGGAGTACAGTGGACTGGAGCGAG
TCAGCGACATATGGGGAGCACATCTGGTTCGAGACCAACGTGTCCGGGGACTTCTGCTAC
GTTGGGGAGCAGTACTGTGTAGCCAGGATGCTGAAGTCAGTGTCTCGAAGAAAGTGCGCA
GCCTGCAAGATTGTGGTGCACACGCCCTGCATCGAGCAGCTGGAGAAGATAAATTTCCGC
TGTAAGCCGTCCTTCCGTGAATCAGGCTCCAGGAATGTCCGCGAGCCAACCTTTGTACGG
CACCACTGGGTACACAGACGACGCCAGGACGGCAAGTGTCGGCACTGTGGGAAGGGATTC
CAGCAGAAGTTCACCTTCCACAGCAAGGAGATTGTGGCCATCAGCTGCTCGTGGTGCAAG
CAGGCATACCACAGCAAGGTGTCCTGCTTCATGCTGCAGCAGATCGAGGAGCCGTGCTCG
CTGGGGGTCCACGCAGCCGTGGTCATCCCGCCCACCTGGATCCTCCGCGCCCGGAGGCCC
CAGAATACTCTGAAAGCAAGCAAGAAGAAGAAGAGGGCATCCTTCAAGAGGAAGTCCAGC
AAGAAAGGGCCTGAGGAGGGCCGCTGGAGACCCTTCATCATCAGGCCCACCCCCTCCCCG
CTCATGAAGCCCCTGCTGGTGTTTGTGAACCCCAAGAGTGGGGGCAACCAGGGTGCAAAG
ATCATCCAGTCTTTCCTCTGGTATCTCAATCCCCGACAAGTCTTCGACCTGAGCCAGGGA
GGGCCCAAGGAGGCGCTGGAGATGTACCGCAAAGTGCACAACCTGCGGATCCTGGCGTGC
GGGGGCGACGGCACGGTGGGCTGGATCCTCTCCACCCTGGACCAGCTACGCCTGAAGCCG
CCACCCCCTGTTGCCATCCTGCCCCTGGGTACTGGCAACGACTTGGCCCGAACCCTCAAC
TGGGGTGGGGGCTACACAGATGAGCCTGTGTCCAAGATCCTCTCCCACGTGGAGGAGGGG
AACGTGGTACAGCTGGACCGCTGGGACCTCCACGCTGAGCCCAACCCCGAGGCAGGGCCT
GAGGACCGAGATGAAGGCGCCACCGACCGGTTGCCCCTGGATGTCTTCAACAACTACTTC
AGCCTGGGCTTTGACGCCCACGTCACCCTGGAGTTCCACGAGTCTCGAGAGGCCAACCCA
GAGAAATTCAACAGCCGCTTTCGGAATAAGATGTTCTACGCCGGGACAGCTTTCTCTGAC
TTCCTGATGGGCAGCTCCAAGGACCTGGCCAAGCACATCCGAGTGGTGTGTGATGGAATG
GACTTGACTCCCAAGATCCAGGACCTGAAACCCCAGTGTGTTGTTTTCCTGAACATCCCC
AGGTACTGTGCGGGCACCATGCCCTGGGGCCACCCTGGGGAGCACCACGACTTTGAGCCC
CAGCGGCATGACGACGGCTACCTCGAGGTCATTGGCTTCACCATGACGTCGTTGGCCGCG
CTGCAGGTGGGCGGACACGGCGAGCGGCTGACGCAGTGTCGCGAGGTGGTGCTCACCACA
TCCAAGGCCATCCCGGTGCAGGTGGATGGCGAGCCCTGCAAGCTTGCAGCCTCACGCATC
CGCATCGCCCTGCGCAACCAGGCCACCATGGTGCAGAAGGCCAAGCGGCGGAGCGCCGCC
CCCCTGCACAGCGACCAGCAGCCGGTGCCAGAGCAGTTGCGCATCCAGGTGAGTCGCGTC
AGCATGCACGACTATGAGGCCCTGCACTACGACAAGGAGCAGCTCAAGGAGGCCTCTGTG
CCGCTGGGCACTGTGGTGGTCCCAGGAGACAGTGACCTAGAGCTCTGCCGTGCCCACATT
GAGAGACTCCAGCAGGAGCCCGATGGTGCTGGAGCCAAGTCCCCGACATGCCAGAAACTG
TCCCCCAAGTGGTGCTTCCTGGACGCCACCACTGCCAGCCGCTTCTACAGGATCGACCGA
GCCCAGGAGCACCTCAACTATGTGACTGAGATCGCACAGGATGAGATTTATATCCTGGAC
CCTGAGCTGCTGGGGGCATCGGCCCGGCCTGACCTCCCAACCCCCACTTCCCCTCTCCCC
ACCTCACCCTGCTCACCCACGCCCCGGTCACTGCAAGGGGATGCTGCACCCCCTCAAGGT
GAAGAGCTGATTGAGGCTGCCAAGAGGAACGACTTCTGTAAGCTCCAGGAGCTGCACCGA
GCTGGGGGCGACCTCATGCACCGAGACGAGCAGAGTCGCACGCTCCTGCACCACGCAGTC
AGCACTGGCAGCAAGGATGTGGTCCGCTACCTGCTGGACCACGCCCCCCCAGAGATCCTT
GATGCGGTGGAGGAAAACGGGGAGACCTGTTTGCACCAAGCAGCGGCCCTGGGCCAGCGC
ACCATCTGCCACTACATCGTGGAGGCCGGGGCCTCGCTCATGAAGACAGACCAGCAGGGC
GACACTCCCCGGCAGCGGGCTGAGAAGGCTCAGGACACCGAGCTGGCCGCCTACCTGGAG
AACCGGCAGCACTACCAGATGATCCAGCGGGAGGACCAGGAGACGGCTGTGTAG
|
| Enzyme 27 GenBank Gene ID |
NM_001105540.1 |
| Enzyme 27 GeneCard ID |
DGKZ |
| Enzyme 27 GenAtlas ID |
DGKZ |
| Enzyme 27 HGNC ID |
HGNC:2857 |
| Enzyme 27 Chromosome Location |
1 |
| Enzyme 27 Locus |
11p11.2 |
| Enzyme 27 SNPs |
SNPJam Report |
| Enzyme 27 General References |
- Bunting M, Tang W, Zimmerman GA, McIntyre TM, Prescott SM: Molecular cloning and characterization of a novel human diacylglycerol kinase zeta. J Biol Chem. 1996 Apr 26;271(17):10230-6. [PubMed ]
- Ding L, Bunting M, Topham MK, McIntyre TM, Zimmerman GA, Prescott SM: Alternative splicing of the human diacylglycerol kinase zeta gene in muscle. Proc Natl Acad Sci U S A. 1997 May 27;94(11):5519-24. [PubMed ]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed ]
- Topham MK, Bunting M, Zimmerman GA, McIntyre TM, Blackshear PJ, Prescott SM: Protein kinase C regulates the nuclear localization of diacylglycerol kinase-zeta. Nature. 1998 Aug 13;394(6694):697-700. [PubMed ]
- Hogan A, Shepherd L, Chabot J, Quenneville S, Prescott SM, Topham MK, Gee SH: Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions. J Biol Chem. 2001 Jul 13;276(28):26526-33. Epub 2001 May 14. [PubMed ]
- Topham MK, Prescott SM: Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism. J Cell Biol. 2001 Mar 19;152(6):1135-43. [PubMed ]
- Rincon E, Santos T, Avila-Flores A, Albar JP, Lalioti V, Lei C, Hong W, Merida I: Proteomics identification of sorting nexin 27 as a diacylglycerol kinase zeta-associated protein: new diacylglycerol kinase roles in endocytic recycling. Mol Cell Proteomics. 2007 Jun;6(6):1073-87. Epub 2007 Mar 9. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
5487 |
| Enzyme 28 Name |
L-fucose kinase |
| Enzyme 28 Synonyms |
- Fucokinase
|
| Enzyme 28 Gene Name |
FUK |
| Enzyme 28 Protein Sequence |
>L-fucose kinase
MEQPKGVDWTVIILTCQYKDSVQVFQRELEVRQKREQIPAGTLLLAVEDPEKRVGSGGAT
LNALLVAAEHLSARAGFTVVTSDVLHSAWILILHMGRDFPFDDCGRAFTCLPVENPEAPV
EALVCNLDCLLDIMTYRLGPGSPPGVWVCSTDMLLSVPANPGISWDSFRGARVIALPGSP
AYAQNHGVYLTDPQGLVLDIYYQGTEAEIQRCVRPDGRVPLVSGVVFFSVETAERLLATH
VSPPLDACTYLGLDSGARPVQLSLFFDILHCMAENVTREDFLVGRPPELGQGDADVAGYL
QSARAQLWRELRDQPLTMAYVSSGSYSYMTSSASEFLLSLTLPGAPGAQIVHSQVEEQQL
LAAGSSVVSCLLEGPVQLGPGSVLQHCHLQGPIHIGAGCLVTGLDTAHSKALHGRELRDL
VLQGHHTRLHGSPGHAFTLVGRLDSWERQGAGTYLNVPWSEFFKRTGVRAWDLWDPETLP
AEYCLPSARLFPVLHPSRELGPQDLLWMLDHQEDGGEALRAWRASWRLSWEQLQPCLDRA
ATLASRRDLFFRQALHKARHVLEARQDLSLRPLIWAAVREGCPGPLLATLDQVAAGAGDP
GVAARALACVADVLGCMAEGRGGLRSGPAANPEWMRPFSYLECGDLAAGVEALAQERDKW
LSRPALLVRAARHYEGAGQILIRQAVMSAQHFVSTEQVELPGPGQWVVAECPARVDFSGG
WSDTPPLAYELGGAVLGLAVRVDGRRPIGARARRIPEPELWLAVGPRQDEMTVKIVCRCL
ADLRDYCQPHAPGALLKAAFICAGIVHVHSELQLSEQLLRTFGGGFELHTWSELPHGSGL
GTSSILAGTALAALQRAAGRVVGTEALIHAVLHLEQVLTTGGGWQDQVGGLMPGIKVGRS
RAQLPLKVEVEEVTVPEGFVQKLNDHLLLVYTGKTRLARNLLQDVLRSWYARLPAVVQNA
HSLVRQTEECAEGFRQGSLPLLGQCLTSYWEQKKLMAPGCEPLTVRRMMDVLAPHVHGQS
LAGAGGGGFLYLLTKEPQQKEALEAVLAKTEGLGNYSIHLVEVDTQGLSLKLLGTEASTC
CPFP
|
| Enzyme 28 Number of Residues |
1084 |
| Enzyme 28 Molecular Weight |
117621.8 |
| Enzyme 28 Theoretical pI |
6.21 |
| Enzyme 28 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 |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 28 General Function |
Involved in ATP binding |
| Enzyme 28 Specific Function |
Takes part in the salvage pathway for reutilization of fucose from the degradation of oligosaccharides |
| Enzyme 28 Pathways |
- Fructose and Mannose Metabolism (map00051 )
|
| Enzyme 28 Reactions |
- ATP + L-fucose = ADP + beta-L-fucose 1-phosphate [RN:R03161]
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
63175654 |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q8N0W3 |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
FUK_HUMAN |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>3255 bp
ATGGAGCAGCCGAAGGGAGTTGATTGGACAGTCATCATCCTGACCTGCCAGTACAAGGAC
AGTGTCCAGGTCTTTCAGAGAGAACTGGAAGTGCGGCAGAAGCGGGAGCAGATCCCTGCT
GGGACGCTGTTACTGGCCGTGGAGGACCCAGAGAAGCGTGTGGGCAGCGGAGGAGCCACC
CTCAACGCCCTGCTGGTGGCTGCTGAACACCTGAGTGCCCGGGCAGGCTTCACTGTGGTC
ACATCCGATGTCCTGCACTCGGCCTGGATCCTCATTCTGCACATGGGTCGAGACTTCCCC
TTTGATGACTGTGGCAGGGCTTTCACCTGCCTCCCCGTGGAGAACCCCGAGGCCCCCGTG
GAAGCCTTGGTCTGCAACCTGGACTGCCTGCTGGACATCATGACCTATCGGCTGGGCCCG
GGCTCCCCGCCAGGCGTGTGGGTCTGCAGCACCGACATGCTGCTGTCTGTTCCTGCAAAT
CCTGGTATCAGCTGGGACAGCTTCCGGGGAGCCAGAGTGATCGCCCTCCCAGGGAGCCCG
GCCTACGCTCAGAATCATGGCGTCTACCTAACTGACCCCCAGGGCCTTGTTTTGGACATT
TACTACCAGGGCACTGAGGCAGAGATTCAGCGGTGTGTCAGGCCTGATGGGCGGGTGCCA
CTGGTCTCTGGGGTTGTCTTCTTCTCTGTGGAGACTGCCGAGCGCCTCCTAGCCACCCAC
GTGAGCCCGCCCCTGGATGCCTGCACCTACCTAGGCTTGGACTCCGGAGCCCGGCCTGTC
CAGCTGTCTCTGTTTTTTGACATTCTCCACTGCATGGCTGAGAACGTGACCAGGGAGGAC
TTCCTGGTGGGGAGGCCCCCAGAGTTGGGGCAAGGCGATGCAGATGTAGCGGGTTATCTG
CAGAGCGCCCGGGCCCAGCTGTGGAGGGAGCTTCGCGATCAGCCCCTTACCATGGCCTAT
GTCTCCAGCGGCAGCTACAGCTACATGACCTCCTCAGCCAGTGAGTTCCTGCTCAGCCTC
ACACTCCCCGGGGCTCCTGGGGCCCAGATTGTGCACTCCCAGGTGGAGGAGCAGCAGCTT
CTGGCGGCCGGGAGCTCTGTGGTCAGCTGCCTGCTGGAGGGCCCTGTCCAGCTGGGTCCT
GGGAGCGTCCTGCAGCACTGCCACCTGCAGGGCCCCATTCACATAGGCGCTGGCTGCTTG
GTGACTGGCCTGGATACAGCCCACTCCAAGGCCCTGCATGGCCGGGAGCTGCGTGACCTT
GTCCTGCAGGGACACCACACGCGGCTACACGGCTCCCCGGGCCACGCCTTCACCCTCGTT
GGCCGTCTGGACAGCTGGGAGAGACAGGGGGCAGGCACATATCTCAACGTGCCCTGGAGT
GAATTCTTCAAGAGGACAGGTGTTCGAGCCTGGGACCTGTGGGACCCTGAGACGCTGCCC
GCAGAGTACTGCCTTCCCAGCGCCCGCCTCTTTCCTGTGCTCCACCCCTCGAGGGAGCTG
GGACCCCAGGACCTGCTGTGGATGCTGGACCACCAGGAGGATGGGGGCGAGGCCCTGCGA
GCCTGGCGGGCCTCCTGGCGCCTGTCCTGGGAGCAGCTGCAGCCGTGCCTGGATCGGGCT
GCCACGCTGGCCTCTCGCCGGGACCTGTTCTTCCGCCAGGCCCTGCATAAGGCGCGGCAC
GTGCTGGAGGCCCGGCAGGACCTCAGCCTGCGCCCGCTGATCTGGGCTGCTGTCCGCGAG
GGCTGCCCCGGGCCCCTGCTGGCCACGCTGGACCAGGTTGCAGCTGGGGCAGGAGACCCT
GGTGTGGCGGCACGGGCACTGGCCTGTGTGGCGGACGTCCTGGGCTGCATGGCAGAGGGC
CGTGGGGGCTTGCGGAGCGGGCCAGCTGCCAACCCTGAGTGGATGCGGCCCTTCTCATAC
CTGGAGTGTGGAGACCTGGCAGCGGGCGTGGAGGCGCTTGCCCAGGAGAGGGACAAGTGG
CTAAGCAGGCCAGCCTTGCTGGTGCGAGCGGCCCGCCACTATGAGGGGGCTGGTCAGATC
CTGATCCGCCAGGCTGTGATGTCAGCCCAGCACTTTGTCTCCACAGAGCAGGTGGAACTG
CCGGGACCTGGGCAGTGGGTGGTGGCTGAGTGCCCGGCCCGTGTGGATTTCTCTGGGGGC
TGGAGTGACACGCCACCCCTTGCCTATGAGCTTGGCGGGGCTGTGCTGGGCCTGGCTGTG
CGAGTGGACGGCCGCCGGCCCATCGGAGCCAGGGCACGCCGCATCCCGGAGCCTGAGCTG
TGGCTGGCGGTGGGGCCTCGGCAGGATGAGATGACTGTGAAGATAGTGTGCCGGTGCCTG
GCTGACCTGCGGGACTACTGCCAGCCTCATGCCCCAGGGGCCCTGCTGAAGGCGGCCTTC
ATCTGTGCAGGGATCGTGCATGTCCACTCGGAACTCCAGCTGAGTGAGCAGCTGCTCCGC
ACCTTCGGGGGCGGCTTTGAGCTGCACACCTGGTCTGAGCTGCCCCACGGCTCTGGCCTG
GGCACCAGCAGCATCCTGGCAGGCACTGCCCTGGCTGCCTTGCAGCGAGCCGCAGGCCGG
GTGGTGGGCACGGAAGCCCTGATCCACGCAGTGCTGCACCTGGAGCAGGTGCTCACCACT
GGAGGTGGCTGGCAGGACCAAGTAGGTGGCCTAATGCCTGGCATCAAGGTGGGGCGCTCC
CGGGCTCAGCTGCCACTGAAGGTGGAGGTAGAAGAGGTCACGGTGCCTGAGGGCTTTGTC
CAGAAGCTCAATGACCACCTGCTCTTGGTGTACACTGGCAAGACCCGCCTGGCTCGGAAC
CTGCTGCAGGATGTGCTGAGGAGCTGGTATGCCCGACTTCCTGCTGTGGTGCAGAATGCC
CACAGCCTGGTACGGCAAACTGAGGAGTGTGCTGAAGGCTTCCGCCAAGGAAGCCTGCCT
CTGCTGGGCCAGTGCCTGACCTCGTACTGGGAGCAGAAGAAGCTCATGGCTCCAGGCTGT
GAGCCCCTGACTGTGCGGCGTATGATGGATGTCCTGGCCCCCCACGTGCATGGCCAGAGC
CTGGCTGGGGCAGGCGGTGGAGGCTTTCTCTATCTGTTGACCAAGGAGCCACAGCAAAAG
GAGGCCTTGGAGGCGGTGCTGGCCAAGACCGAGGGCCTTGGGAATTACAGCATCCACCTG
GTTGAAGTGGACACTCAGGGCCTGAGCCTGAAGCTGCTGGGGACCGAGGCCTCAACCTGT
TGCCCTTTCCCATGA
|
| Enzyme 28 GenBank Gene ID |
NM_145059.2 |
| Enzyme 28 GeneCard ID |
FUK |
| Enzyme 28 GenAtlas ID |
FUK |
| Enzyme 28 HGNC ID |
HGNC:29500 |
| Enzyme 28 Chromosome Location |
1 |
| Enzyme 28 Locus |
16q22.1 |
| Enzyme 28 SNPs |
SNPJam Report |
| Enzyme 28 General References |
- Hinderlich S, Berger M, Blume A, Chen H, Ghaderi D, Bauer C: Identification of human L-fucose kinase amino acid sequence. Biochem Biophys Res Commun. 2002 Jun 14;294(3):650-4. [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 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
5490 |
| Enzyme 29 Name |
Propionyl-CoA carboxylase beta chain, mitochondrial |
| Enzyme 29 Synonyms |
- PCCase subunit beta
- Propanoyl-CoA:carbon dioxide ligase subunit beta
|
| Enzyme 29 Gene Name |
PCCB |
| Enzyme 29 Protein Sequence |
>Propionyl-CoA carboxylase beta chain, mitochondrial
MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHK
RGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVY
VFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIF
LRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVT
QEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVP
ELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPK
VASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFA
EATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVE
AAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL
|
| Enzyme 29 Number of Residues |
539 |
| Enzyme 29 Molecular Weight |
58215.1 |
| Enzyme 29 Theoretical pI |
7.69 |
| Enzyme 29 GO Classification |
| Function |
- catalytic activity
- ligase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 29 General Function |
Involved in ligase activity |
| Enzyme 29 Specific Function |
ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA |
| Enzyme 29 Pathways |
- Propanoate Metabolism (map00640 )
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 29 Reactions |
- ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA [RN:R01859]
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
312812 |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
P05166 |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
PCCB_HUMAN |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>1620 bp
ATGGCGGCGGCATTACGGGTGGCGGCGGTCGGGGCAAGGCTCAGCGTTCTGGCGAGCGGT
CTCCGCGCCGCGGTCCGCAGCCTTTGCAGCCAGGCCACCTCTGTTAACGAACGCATCGAA
AACAAGCGCCGGACCGCGCTGCTGGGAGGGGGCCAACGCCGTATTGACGCGCAGCACAAG
CGAGGAAAGCTAACAGCCAGGGAGAGGATCAGTCTCTTGCTGGACCCTGGCAGCTTTGTT
GAGAGCGACATGTTTGTGGAACACAGATGTGCAGATTTTGGAATGGCTGCTGACAAGAAT
AAGTTTCCTGGAGACAGCGTGGTCACTGGACGAGGCCGAATCAATGGAAGATTGGTTTAT
GTCTTCAGTCAGGATTTTACAGTTTTTGGAGGCAGTCTGTCAGGAGCACATGCCCAAAAG
ATCTGCAAAATCATGGACCAGGCCATAACGGTGGGGGCTCCAGTGATTGGGCTGAATGAC
TCTGGGGGAGCACGGATCCAAGAAGGAGTGGAGTCTTTGGCTGGCTATGCAGACATCTTT
CTGAGGAATGTTACGGCATCCGGAGTCATCCCTCAGATTTCTCTGATCATGGGCCCATGT
GCTGGTGGGGCCGTCTACTCCCCAGCCCTAACAGACTTCACGTTCATGGTAAAGGACACC
TCCTACCTGTTCATCACTGGCCCTGATGTTGTGAAGTCTGTCACCAATGAGGATGTTACC
CAGGAGGAGCTCGGTGGTGCCAAGACCCACACCACCATGTCAGGTGTGGCCCACAGAGCT
TTTGAAAATGATGTTGATGCCTTGTGTAATCTCCGGGATTTCTTCAACTACCTGCCCCTG
AGCAGTCAGGACCCGGCTTCCGTCCGTGAGTGCCACGATCCCAGTGACCGTCTGGTTCCT
GAGCTTGACACAATTGTCCCTTTGGAATCAACCAAAGCCTACAACATGGTGGACATCATA
CACTCTGTTGTTGATGAGCGTGAATTTTTTGAGATCATGCCCAATTATGCCAAGAACATC
ATTGTTGGTTTTGCAAGAATGAATGGGAGGACTGTTGGAATTGTTGGCAACCAACCTAAG
GTGGCCTCAGGATGCTTGGATATTAATTCATCTGTGAAAGGGGCTCGTTTTGTCAGATTC
TGTGATGCATTCAATATTCCACTCATCACTTTTGTTGATGTCCCTGGCTTTCTACCTGGC
ACAGCACAGGAATACGGGGGCATCATCCGGCATGGTGCCAAGCTTCTCTACGCATTTGCT
GAGGCAACTGTACCCAAAGTCACAGTCATCACCAGGAAGGCCTATGGAGGTGCCTATGAT
GTCATGAGCTCTAAGCACCTTTGTGGTGATACCAACTATGCCTGGCCCACCGCAGAGATT
GCAGTCATGGGAGCAAAGGGCGCTGTGGAGATCATCTTCAAAGGGCATGAGAATGTGGAA
GCTGCTCAGGCAGAGTACATCGAGAAGTTTGCCAACCCTTTCCCTGCAGCAGTGCGAGGG
TTTGTGGATGACATCATCCAACCTTCTTCCACACGTGCCCGAATCTGCTGTGACCTGGAT
GTCTTGGCCAGCAAGAAGGTACAACGTCCTTGGAGAAAACATGCAAATATTCCATTGTAA
|
| Enzyme 29 GenBank Gene ID |
X73424 |
| Enzyme 29 GeneCard ID |
PCCB |
| Enzyme 29 GenAtlas ID |
PCCB |
| Enzyme 29 HGNC ID |
HGNC:8654 |
| Enzyme 29 Chromosome Location |
3 |
| Enzyme 29 Locus |
3q21-q22 |
| Enzyme 29 SNPs |
SNPJam Report |
| Enzyme 29 General References |
- Lamhonwah AM, Leclerc D, Loyer M, Clarizio R, Gravel RA: Correction of the metabolic defect in propionic acidemia fibroblasts by microinjection of a full-length cDNA or RNA transcript encoding the propionyl-CoA carboxylase beta subunit. Genomics. 1994 Feb;19(3):500-5. [PubMed ]
- Ohura T, Ogasawara M, Ikeda H, Narisawa K, Tada K: The molecular defect in propionic acidemia: exon skipping caused by an 8-bp deletion from an intron in the PCCB allele. Hum Genet. 1993 Oct;92(4):397-402. [PubMed ]
- Rodriguez-Pombo P, Hoenicka J, Muro S, Perez B, Perez-Cerda C, Richard E, Desviat LR, Ugarte M: Human propionyl-CoA carboxylase beta subunit gene: exon-intron definition and mutation spectrum in Spanish and Latin American propionic acidemia patients. Am J Hum Genet. 1998 Aug;63(2):360-9. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Lamhonwah AM, Barankiewicz TJ, Willard HF, Mahuran DJ, Quan F, Gravel RA: Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4864-8. [PubMed ]
- Tahara T, Kraus JP, Rosenberg LE: An unusual insertion/deletion in the gene encoding the beta-subunit of propionyl-CoA carboxylase is a frequent mutation in Caucasian propionic acidemia. Proc Natl Acad Sci U S A. 1990 Feb;87(4):1372-6. [PubMed ]
- Tahara T, Kraus JP, Ohura T, Rosenberg LE, Fenton WA: Three independent mutations in the same exon of the PCCB gene: differences between Caucasian and Japanese propionic acidaemia. J Inherit Metab Dis. 1993;16(2):353-60. [PubMed ]
- Muro S, Rodriguez-Pombo P, Perez B, Perez-Cerda C, Desviat LR, Sperl W, Skladal D, Sass JO, Ugarte M: Identification of novel mutations in the PCCB gene in European propionic acidemia patients. Mutation in brief no. 253. Online. Hum Mutat. 1999;14(1):89-90. [PubMed ]
- Ugarte M, Perez-Cerda C, Rodriguez-Pombo P, Desviat LR, Perez B, Richard E, Muro S, Campeau E, Ohura T, Gravel RA: Overview of mutations in the PCCA and PCCB genes causing propionic acidemia. Hum Mutat. 1999;14(4):275-82. [PubMed ]
- Muro S, Perez B, Desviat LR, Rodriguez-Pombo P, Perez-Cerda C, Clavero S, Ugarte M: Effect of PCCB gene mutations on the heteromeric and homomeric assembly of propionyl-CoA carboxylase. Mol Genet Metab. 2001 Dec;74(4):476-83. [PubMed ]
- Yorifuji T, Kawai M, Muroi J, Mamada M, Kurokawa K, Shigematsu Y, Hirano S, Sakura N, Yoshida I, Kuhara T, Endo F, Mitsubuchi H, Nakahata T: Unexpectedly high prevalence of the mild form of propionic acidemia in Japan: presence of a common mutation and possible clinical implications. Hum Genet. 2002 Aug;111(2):161-5. Epub 2002 Jul 4. [PubMed ]
- Perez B, Desviat LR, Rodriguez-Pombo P, Clavero S, Navarrete R, Perez-Cerda C, Ugarte M: Propionic acidemia: identification of twenty-four novel mutations in Europe and North America. Mol Genet Metab. 2003 Jan;78(1):59-67. [PubMed ]
- Yang X, Sakamoto O, Matsubara Y, Kure S, Suzuki Y, Aoki Y, Yamaguchi S, Takahashi Y, Nishikubo T, Kawaguchi C, Yoshioka A, Kimura T, Hayasaka K, Kohno Y, Iinuma K, Ohura T: Mutation spectrum of the PCCA and PCCB genes in Japanese patients with propionic acidemia. Mol Genet Metab. 2004 Apr;81(4):335-42. [PubMed ]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
5491 |
| Enzyme 30 Name |
Propionyl-CoA carboxylase alpha chain, mitochondrial |
| Enzyme 30 Synonyms |
- PCCase subunit alpha
- Propanoyl-CoA:carbon dioxide ligase subunit alpha
|
| Enzyme 30 Gene Name |
PCCA |
| Enzyme 30 Protein Sequence |
>Propionyl-CoA carboxylase alpha chain, mitochondrial
MAGFWVGTAPLVAAGRRGRWPPQQLMLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNE
KTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKS
YLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIES
KLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRD
GFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVV
EEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPV
TECITGLDLVQEMIRVAKGYPLRHKQADIRINGWAVECRVYAEDPYKSFGLPSIGRLSQY
QEPLHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTH
NIALLREVIINSRFVKGDISTKFLSDVYPDGFKGHMLTKSEKNQLLAIASSLFVAFQLRA
QHFQENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLAS
PLLSVSVDGTQRTVQCLSREAGGNMSIQFLGTVYKVNILTRLAAELNKFMLEKVTEDTSS
VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGE
GDLLVELE
|
| Enzyme 30 Number of Residues |
728 |
| Enzyme 30 Molecular Weight |
80058.3 |
| Enzyme 30 Theoretical pI |
7.56 |
| Enzyme 30 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- nucleoside binding
- purine nucleoside binding
- vitamin binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 30 General Function |
Involved in catalytic activity |
| Enzyme 30 Specific Function |
ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA |
| Enzyme 30 Pathways |
- Propanoate Metabolism (map00640 )
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 30 Reactions |
- ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA [RN:R01859]
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
18252315 |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
P05165 |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
PCCA_HUMAN |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>2187 bp
ATGGCGGGGTTCTGGGTCGGGACAGCACCGCTGGTCGCTGCCGGACGGCGTGGGCGGTGG
CCGCCGCAGCAGCTGATGCTGAGCGCGGCGCTGCGGACCCTGAAGCATGTTCTGTACTAT
TCAAGACAGTGCTTAATGGTGTCCCGTAATCTTGGTTCAGTGGGATATGATCCTAATGAA
AAAACTTTTGATAAAATTCTTGTTGCTAATAGAGGAGAAATTGCATGTCGGGTTATTAGA
ACTTGCAAGAAGATGGGCATTAAGACAGTTGCCATCCACAGTGATGTTGATGCTAGTTCT
GTTCATGTGAAAATGGCGGATGAGGCTGTCTGTGTTGGCCCAGCTCCCACCAGTAAAAGC
TACCTCAACATGGATGCCATCATGGAAGCCATTAAGAAAACCAGGGCCCAAGCTGTACAT
CCAGGTTATGGATTCCTTTCAGAAAACAAAGAATTTGCCAGATGTTTGGCAGCAGAAGAT
GTCGTTTTCATTGGACCTGACACACATGCTATTCAAGCCATGGGCGACAAGATTGAAAGC
AAATTATTAGCTAAGAAAGCAGAGGTTAATACAATCCCTGGCTTTGATGGAGTAGTCAAG
GATGCAGAAGAAGCTGTCAGAATTGCAAGGGAAATTGGCTACCCTGTCATGATCAAGGCC
TCAGCAGGTGGTGGTGGGAAAGGCATGCGCATTGCTTGGGATGATGAAGAGACCAGGGAT
GGTTTTAGATTGTCATCTCAAGAAGCTGCTTCTAGTTTTGGCGATGATAGACTACTAATA
GAAAAATTTATTGATAATCCTCGTCATATAGAAATCCAGGTTCTAGGTGATAAACATGGG
AATGCTTTATGGCTTAATGAAAGAGAGTGCTCAATTCAGAGAAGAAATCAGAAGGTGGTG
GAGGAAGCACCAAGCATTTTTTTGGATGCGGAGACTCGAAGAGCGATGGGAGAACAAGCT
GTAGCTCTTGCCAGAGCAGTAAAATATTCCTCTGCTGGGACCGTGGAGTTCCTTGTGGAC
TCTAAGAAGAATTTTTATTTCTTGGAAATGAATACAAGACTCCAGGTTGAGCATCCTGTC
ACAGAATGCATTACTGGCCTGGACCTAGTCCAGGAAATGATCCGTGTTGCTAAGGGCTAC
CCTCTCAGGCACAAACAAGCTGATATTCGCATCAACGGCTGGGCAGTTGAATGTCGGGTT
TATGCTGAGGACCCCTACAAGTCTTTTGGTTTACCATCTATTGGGAGATTGTCTCAGTAC
CAAGAACCGTTACATCTACCTGGTGTCCGAGTGGACAGTGGCATCCAACCAGGAAGTGAT
ATTAGCATTTATTATGATCCTATGATTTCAAAACTAATCACATATGGCTCTGATAGAACT
GAGGCACTGAAGAGAATGGCAGATGCACTGGATAACTATGTTATTCGAGGTGTTACACAT
AATATTGCATTACTTCGAGAGGTGATAATCAACTCACGCTTTGTAAAAGGAGACATCAGC
ACTAAATTTCTCTCCGATGTGTATCCTGATGGCTTCAAAGGACACATGCTAACCAAGAGT
GAGAAGAACCAGTTATTGGCAATAGCATCATCATTGTTTGTGGCATTCCAGTTAAGAGCA
CAACATTTTCAAGAAAATTCAAGAATGCCTGTTATTAAACCAGACATAGCCAACTGGGAG
CTCTCAGTAAAATTGCATGATAAAGTTCATACCGTAGTAGCATCAAACAATGGGTCAGTG
TTCTCGGTGGAAGTTGATGGGTCGAAACTAAATGTGACCAGCACGTGGAACCTGGCTTCG
CCCTTATTGTCTGTCAGCGTTGATGGCACTCAGAGGACTGTCCAGTGTCTTTCTCGAGAA
GCAGGTGGAAACATGAGCATTCAGTTTCTTGGTACAGTGTACAAGGTGAATATCTTAACC
AGACTTGCCGCAGAATTGAACAAATTTATGCTGGAAAAAGTGACTGAGGACACAAGCAGT
GTTCTGCGTTCCCCGATGCCCGGAGTGGTGGTGGCCGTCTCTGTCAAGCCTGGAGACGCG
GTAGCAGAAGGTCAAGAAATTTGTGTGATTGAAGCCATGAAAATGCAGAATAGTATGACA
GCTGGGAAAACTGGCACGGTGAAATCTGTGCACTGTCAAGCTGGAGACACAGTTGGAGAA
GGGGATCTGCTCGTGGAGCTGGAATGA
|
| Enzyme 30 GenBank Gene ID |
AF385926 |
| Enzyme 30 GeneCard ID |
PCCA |
| Enzyme 30 GenAtlas ID |
PCCA |
| Enzyme 30 HGNC ID |
HGNC:8653 |
| Enzyme 30 Chromosome Location |
1 |
| Enzyme 30 Locus |
13q32 |
| Enzyme 30 SNPs |
SNPJam Report |
| Enzyme 30 General References |
- Campeau E, Desviat LR, Leclerc D, Wu X, Perez B, Ugarte M, Gravel RA: Structure of the PCCA gene and distribution of mutations causing propionic acidemia. Mol Genet Metab. 2001 Sep-Oct;74(1-2):238-47. [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 ]
- Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Lamhonwah AM, Mahuran D, Gravel RA: Human mitochondrial propionyl-CoA carboxylase: localization of the N-terminus of the pro- and mature alpha chains in the deduced primary sequence of a full-length cDNA. Nucleic Acids Res. 1989 Jun 12;17(11):4396. [PubMed ]
- Stankovics J, Ledley FD: Cloning of functional alpha propionyl CoA carboxylase and correction of enzyme deficiency in pccA fibroblasts. Am J Hum Genet. 1993 Jan;52(1):144-51. [PubMed ]
- Lamhonwah AM, Barankiewicz TJ, Willard HF, Mahuran DJ, Quan F, Gravel RA: Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4864-8. [PubMed ]
- Lamhonwah AM, Quan F, Gravel RA: Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase. Arch Biochem Biophys. 1987 May 1;254(2):631-6. [PubMed ]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
- Ugarte M, Perez-Cerda C, Rodriguez-Pombo P, Desviat LR, Perez B, Richard E, Muro S, Campeau E, Ohura T, Gravel RA: Overview of mutations in the PCCA and PCCB genes causing propionic acidemia. Hum Mutat. 1999;14(4):275-82. [PubMed ]
- Richard E, Desviat LR, Perez B, Perez-Cerda C, Ugarte M: Genetic heterogeneity in propionic acidemia patients with alpha-subunit defects. Identification of five novel mutations, one of them causing instability of the protein. Biochim Biophys Acta. 1999 Mar 30;1453(3):351-8. [PubMed ]
- Perez B, Desviat LR, Rodriguez-Pombo P, Clavero S, Navarrete R, Perez-Cerda C, Ugarte M: Propionic acidemia: identification of twenty-four novel mutations in Europe and North America. Mol Genet Metab. 2003 Jan;78(1):59-67. [PubMed ]
- Yang X, Sakamoto O, Matsubara Y, Kure S, Suzuki Y, Aoki Y, Yamaguchi S, Takahashi Y, Nishikubo T, Kawaguchi C, Yoshioka A, Kimura T, Hayasaka K, Kohno Y, Iinuma K, Ohura T: Mutation spectrum of the PCCA and PCCB genes in Japanese patients with propionic acidemia. Mol Genet Metab. 2004 Apr;81(4):335-42. [PubMed ]
- Campeau E, Dupuis L, Leon-Del-Rio A, Gravel R: Coding sequence mutations in the alpha subunit of propionyl-CoA carboxylase in patients with propionic acidemia. Mol Genet Metab. 1999 May;67(1):11-22. [PubMed ]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
5566 |
| Enzyme 31 Name |
Trifunctional purine biosynthetic protein adenosine-3 |
| Enzyme 31 Synonyms |
- Phosphoribosylamine--glycine ligase
- Glycinamide ribonucleotide synthetase
- GARS
- Phosphoribosylglycinamide synthetase
- Phosphoribosylformylglycinamidine cyclo-ligase
- AIR synthase
- AIRS
- Phosphoribosyl-aminoimidazole synthetase
- Phosphoribosylglycinamide formyltransferase
- 5'-phosphoribosylglycinamide transformylase
- GAR transformylase
- GART
|
| Enzyme 31 Gene Name |
GART |
| Enzyme 31 Protein Sequence |
>Trifunctional purine biosynthetic protein adenosine-3
MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQ
FCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIP
TAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAF
GAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAP
QVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQV
ILPLLKSDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEA
QALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFEGAIYRKD
VGFRAIAFLQQPRSLTYKESGVDIAAGNMLVKKIQPLAKATSRSGCKVDLGGFAGLFDLK
AAGFKDPLLASGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSC
GKLDLSVTEAVVAGIAKACGKAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLP
HLERITEGDVVVGIASSGLHSNGFSLVRKIVAKSSLQYSSPAPDGCGDQTLGDLLLTPTR
IYSHSLLPVLRSGHVKAFAHITGGGLLENIPRVLPEKLGVDLDAQTWRIPRVFSWLQQEG
HLSEEEMARTFNCGVGAVLVVSKEQTEQILRDIQQHKEEAWVIGSVVARAEGSPRVKVKN
LIESMQINGSVLKNGSLTNHFSFEKKKARVAVLISGTGSNLQALIDSTREPNSSAQIDIV
ISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILS
GPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEA
VPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE
|
| Enzyme 31 Number of Residues |
1010 |
| Enzyme 31 Molecular Weight |
107766.3 |
| Enzyme 31 Theoretical pI |
6.68 |
| Enzyme 31 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cyclo-ligase activity
- glycine hydroxymethyltransferase activity
- hydroxymethyl-, formyl- and related transferase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- methyltransferase activity
- nucleoside binding
- phosphoribosylamine-glycine ligase activity
- phosphoribosylformylglycinamidine cyclo-ligase activity
- phosphoribosylglycinamide formyltransferase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- 'de novo' IMP biosynthetic process
- IMP biosynthetic process
- biosynthetic process
- cellular aromatic compound metabolic process
- cellular metabolic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine base biosynthetic process
- purine base metabolic process
- purine nucleoside monophosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside monophosphate biosynthetic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 31 General Function |
Involved in catalytic activity |
| Enzyme 31 Specific Function |
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide |
| Enzyme 31 Pathways |
|
| Enzyme 31 Reactions |
- ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide [RN:R04144]
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
31642 |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
P22102 |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
PUR2_HUMAN |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>3033 bp
ATGGCAGCCCGAGTACTTATAATTGGCAGTGGAGGAAGGGAACATACGCTGGCCTGGAAA
CTTGCACAGTCTCATCATGTCAAACAAGTGTTGGTTGCCCCAGGAAACGCAGGCACTGCC
TGCTCTGAAAAGATTTCAAATACCGCCATCTCAATCAGTGACCACACTGCCCTTGCTCAA
TTCTGCAAAGAGAAGAAAATTGAATTTGTAGTTGTTGGACCAGAAGCACCTCTGGCTGCT
GGGATTGTTGGGAACCTGAGGTCTGCAGGAGTGCAATGCTTTGGCCCAACAGCAGAAGCG
GCTCAGTTAGAGTCCAGCAAAAGGTTTGCCAAAGAGTTTATGGACAGACATGGAATCCCA
ACCGCACAATGGAAGGCTTTCACCAAACCTGAAGAAGCCTGCAGCTTCATTTTGAGTGCA
GACTTCCCTGCTTTGGTTGTGAAGGCCAGTGGTCTTGCAGCTGGAAAAGGGGTGATTGTT
GCAAAGAGCAAAGAAGAGGCCTGCAAAGCTGTACAAGAGATCATGCAGGAGAAAGCCTTT
GGGGCAGCTGGAGAAACAATTGTCATTGAAGAACTTCTTGACGGAGAAGAGGTGTCGTGT
CTGTGTTTCACTGATGGCAAGACTGTGGCCCCCATGCCCCCAGCACAGGACCATAAGCGA
TTACTGGAGGGAGATGGTGGCCCTAACACAGGGGGAATGGGAGCCTATTGTCCAGCCCCT
CAGGTTTCTAATGATCTATTACTAAAAATTAAAGATACTGTTCTTCAGAGGACAGTGGAT
GGCATGCAGCAAGAGGGTACTCCATATACAGGTATTCTCTATGCTGGAATAATGCTGACC
AAGAATGGCCCAAAAGTTCTAGAGTTTAATTGCCGTTTTGGTGATCCAGAGTGCCAAGTA
ATCCTCCCACTTCTTAAAAGTGATCTTTATGAAGTGATTCAGTCCACCTTAGATGGACTG
CTCTGCACATCTCTGCCTGTTTGGCTAGAAAACCACACCGCCCTAACTGTTGTCATGGCA
AGTAAAGGTTATCCTGGAGACTACACCAAGGGTGTAGAGATAACAGGGTTTCCTGAGGCT
CAAGCTCTAGGACTGGAGGTGTTCCATGCAGGCACTGCCCTCAAAAATGGCAAAGTAGTA
ACTCATGGGGGTAGAGTTCTTGCAGTCACAGCCATCCGGGAAAATCTCATATCAGCCCTT
GAGGAAGCCAAGAAAGGACTAGCTGCTATAAAGTTTGAGGGAGCAATTTATAGGAAAGAC
GTCGGCTTTCGTGCCATAGCTTTCCTCCAGCAGCCCAGGAGTTTGACTTACAAGGAATCT
GGAGTAGATATCGCAGCTGGAAATATGCTGGTCAAGAAAATTCAGCCTTTAGCAAAAGCC
ACTTCCAGATCAGGCTGTAAAGTTGATCTTGGAGGTTTTGCTGGTCTTTTTGATTTAAAA
GCAGCTGGTTTCAAAGATCCCCTTCTGGCCTCTGGAACAGATGGCGTTGGAACTAAACTA
AAGATTGCCCAGCTATGCAATAAACATGATACCATTGGTCAAGATTTGGTAGCAATGTGT
GTTAATGATATTCTGGCACAAGGAGCAGAGCCCCTCTTCTTCCTTGATTACTTTTCCTGT
GGAAAACTTGACCTCAGTGTAACTGAAGCTGTTGTTGCTGGAATTGCTAAAGCTTGTGGA
AAAGCTGGATGTGCTCTCCTTGGAGGTGAAACAGCAGAAATGCCTGACATGTATCCCCCT
GGAGAGTATGACCTAGCTGGGTTTGCCGTTGGTGCCATGGAGCGAGATCAGAAACTCCCT
CACCTGGAAAGAATCACTGAGGGTGATGTTGTTGTTGGAATAGCTTCATCTGGTCTTCAT
AGCAATGGATTTAGCCTTGTGAGGAAAATCGTTGCAAAATCTTCCCTCCAGTACTCCTCT
CCAGCACCTGATGGTTGTGGTGACCAGACTTTAGGGGACTTACTTCTCACGCCTACCAGA
ATCTACAGCCATTCACTGTTACCTGTCCTACGTTCAGGACATGTCAAAGCCTTTGCCCAT
ATTACTGGTGGAGGATTACTAGAGAACATCCCCAGAGTCCTCCCTGAGAAACTTGGGGTA
GATTTAGATGCCCAGACCTGGAGGATCCCCAGGGTTTTCTCATGGTTGCAGCAGGAAGGA
CACCTCTCTGAGGAAGAGATGGCCAGAACATTTAACTGTGGGGTTGGCGCTGTCCTTGTG
GTATCAAAGGAGCAGACAGAGCAGATTCTGAGGGATATCCAGCAGCACAAGGAAGAAGCC
TGGGTGATTGGCAGTGTGGTTGCACGAGCTGAAGGTTCCCCACGTGTGAAAGTCAAGAAT
CTGATTGAAAGCATGCAAATAAATGGGTCAGTGTTGAAGAATGGCTCCCTGACAAATCAT
TTCTCTTTTGAAAAAAAAAAGGCCAGAGTGGCTGTCTTAATATCTGGAACAGGATCGAAC
CTGCAAGCACTTATAGACAGTACTCGGGAACCAAATAGCTCTGCACAAATTGATATTGTT
ATCTCCAACAAAGCCGCAGTAGCTGGGTTAGATAAAGCGGAAAGAGCTGGTATTCCCACT
AGAGTAATTAATCATAAACTGTATAAAAATCGTGTAGAATTTGACAGTGCAATTGACCTA
GTCCTTGAAGAGTTCTCCATAGACATAGTCTGTCTTGCAGGATTCATGAGAATTCTTTCT
GGCCCCTTTGTCCAAAAGTGGAATGGAAAAATGCTCAATATCCACCCATCCTTGCTCCCT
TCTTTTAAGGGTTCAAATGCCCATGAGCAAGCCCTGGAAACCGGAGTCACAGTTACTGGG
TGCACTGTACACTTTGTAGCTGAAGATGTGGATGCTGGACAGATTATTTTGCAAGAAGCT
GTTCCCGTGAAGAGGGGTGATACTGTCGCAACTCTTTCTGAAAGAGTAAAATTAGCAGAA
CATAAAATATTTCCTGCAGCCCTTCAGCTGGTGGCCAGTGGAACTGTACAGCTTGGAGAA
AATGGCAAGATCTGTTGGGTTAAAGAGGAATGA
|
| Enzyme 31 GenBank Gene ID |
X54199 |
| Enzyme 31 GeneCard ID |
GART |
| Enzyme 31 GenAtlas ID |
GART |
| Enzyme 31 HGNC ID |
HGNC:4163 |
| Enzyme 31 Chromosome Location |
2 |
| Enzyme 31 Locus |
21q22.1|21q22.11 |
| Enzyme 31 SNPs |
SNPJam Report |
| Enzyme 31 General References |
- Aimi J, Qiu H, Williams J, Zalkin H, Dixon JE: De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E. coli. Nucleic Acids Res. 1990 Nov 25;18(22):6665-72. [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 ]
- Kan JL, Moran RG: Intronic polyadenylation in the human glycinamide ribonucleotide formyltransferase gene. Nucleic Acids Res. 1997 Aug 1;25(15):3118-23. [PubMed ]
- Schild D, Brake AJ, Kiefer MC, Young D, Barr PJ: Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations. Proc Natl Acad Sci U S A. 1990 Apr;87(8):2916-20. [PubMed ]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Zhang Y, Desharnais J, Greasley SE, Beardsley GP, Boger DL, Wilson IA: Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR. Biochemistry. 2002 Dec 3;41(48):14206-15. [PubMed ]
- Zhang Y, Desharnais J, Marsilje TH, Li C, Hedrick MP, Gooljarsingh LT, Tavassoli A, Benkovic SJ, Olson AJ, Boger DL, Wilson IA: Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid. Biochemistry. 2003 May 27;42(20):6043-56. [PubMed ]
- Dahms TE, Sainz G, Giroux EL, Caperelli CA, Smith JL: The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase. Biochemistry. 2005 Jul 26;44(29):9841-50. [PubMed ]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
5581 |
| Enzyme 32 Name |
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 |
| Enzyme 32 Synonyms |
- PAPS synthase 1
- PAPSS 1
- Sulfurylase kinase 1
- SK 1
- SK1
- Sulfate adenylyltransferase
- ATP-sulfurylase
- Sulfate adenylate transferase
- SAT
- Adenylyl-sulfate kinase
- 3'-phosphoadenosine-5'-phosphosulfate synthase
- APS kinase
- Adenosine-5'-phosphosulfate 3'-phosphotransferase
- Adenylylsulfate 3'-phosphotransferase
|
| Enzyme 32 Gene Name |
PAPSS1 |
| Enzyme 32 Protein Sequence |
>Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGL
SGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLF
ADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAG
EIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVP
ENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGG
VINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTC
KNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQL
RNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGV
LNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPS
HGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQK
PPEGFMAPKAWTVLTEYYKSLEKA
|
| Enzyme 32 Number of Residues |
624 |
| Enzyme 32 Molecular Weight |
70832.7 |
| Enzyme 32 Theoretical pI |
6.85 |
| Enzyme 32 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- adenylyltransferase activity
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- nucleotidyltransferase activity
- purine nucleoside binding
- sulfate adenylyltransferase (ATP) activity
- sulfate adenylyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- sulfate assimilation
- sulfur metabolic process
|
| Component |
| — |
|
| Enzyme 32 General Function |
Involved in ATP binding |
| Enzyme 32 Specific Function |
Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS:activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. Also involved in the biosynthesis of sulfated L-selectin ligands in endothelial cells |
| Enzyme 32 Pathways |
|
| Enzyme 32 Reactions |
- ATP + sulfate = diphosphate + adenylyl sulfate [RN:R00529]
|
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
2673862 |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
O43252 |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
PAPS1_HUMAN |
| Enzyme 32 PDB ID |
1X6V |
| Enzyme 32 PDB File |
Show |
| Enzyme 32 3D Structure |
|
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>1875 bp
ATGGAGATCCCCGGGAGCTTGTGCAAGAAAGTCAAGCTGAGCAATAACGCGCAGAACTGG
GGAATGCAGAGAGCAACCAATGTCACCTACCAAGCCCATCATGTCAGCAGGAACAAGAGA
GGTCAGGTGGTGGGGACCAGAGGTGGCTTTCGTGGTTGCACAGTTTGGCTAACAGGCTTG
TCTGGAGCGGGAAAGACTACTGTGAGCATGGCCTTGGAGGAGTACCTGGTTTGTCATGGT
ATTCCATGCTACACTCTGGATGGTGACAATATTCGTCAAGGTCTCAATAAAAATCTTGGC
TTTAGTCCTGAAGACAGAGAAGAGAATGTTCGACGCATCGCAGAAGTTGCTAAACTGTTT
GCAGATGCTGGCTTAGTGTGCATCACAAGTTTCATATCACCTTACACTCAGGATCGCAAC
AATGCAAGGCAAATTCATGAAGGTGCAAGTTTACCGTTTTTTGAAGTATTTGTTGATGCT
CCTCTGCATGTTTGTGAACAGAGGGATGTCAAAGGACTCTACAAAAAAGCCCGGGCAGGA
GAAATTAAAGGTTTCACTGGGATCGATTCTGAATATGAAAAGCCAGAGGCCCCTGAGTTG
GTGCTGAAAACAGACTCCTGTGATGTAAATGACTGTGTCCAGCAAGTTGTGGAACTTCTA
CAGGAACGGGATATTGTACCTGTGGATGCATCTTATGAAGTAAAAGAACTATATGTGCCA
GAAAATAAACTTCATTTGGCAAAAACAGATGCGGAAACATTACCAGCACTGAAAATTAAT
AAAGTGGATATGCAGTGGGTGCAGGTTTTGGCAGAAGGTTGGGCAACCCCATTGAATGGC
TTTATGAGAGAGAGGGAGTACTTGCAGTGCCTTCATTTTGATTGTCTTCTGGATGGAGGT
GTCATTAACTTGTCAGTACCTATAGTTCTGACTGCGACTCATGAAGATAAAGAGAGGCTG
GACGGCTGTACAGCATTTGCTCTGATGTATGAGGGCCGCCGTGTGGCCATTCTTCGCAAT
CCAGAGTTTTTTGAGCACAGGAAAGAGGAGCGCTGTGCCAGACAGTGGGGAACGACATGC
AAGAACCACCCCTATATTAAGATGGTGATGGAACAAGGAGATTGGCTGATTGGAGGAGAT
CTTCAAGTCTTGGATCGAGTTTATTGGAATGATGGTCTTGATCAGTATCGTCTTACTCCT
ACTGAGCTAAAGCAGAAATTTAAAGATATGAATGCTGATGCTGTCTTTGCATTTCAACTA
CGCAACCCAGTGCACAATGGACATGCCCTGTTAATGCAGGATACCCATAAGCAACTTCTA
GAGAGGGGCTACCGGCGCCCTGTCCTCCTCCTCCACCCTCTGGGTGCTTGGACAAAGGAT
GACGATGTTCCTTTGATGTGGCGTATGAAGCAGCATGCTGCAGTGTTGGAGGAAGGAGTT
CTGAATCCTGAGACGACAGTGGTGGCCATCTTCCCATCTCCCATGATGTATGCTGGACCA
ACTGAGGTCCAGTGGCATTGCAGAGCACGGATGGTTGCAGGAGCCAACTTTTACATTGTT
GGACGAGACCCTGCTGGCATGCCTCATCCAGAAACAGGGAAGGATCTTTATGAGCCAAGT
CATGGTGCCAAAGTGCTGACGATGGCCCCTGGTTTAATCACTTTGGAAATAGTTCCCTTT
CGAGTTGCAGCTTACAACAAGAAAAAGAAGCGTATGGACTACTATGACTCTGAACACCAT
GAAGACTTTGAATTTATTTCAGGAACACGAATGCGCAAACTTGCTCGAGAAGGCCAGAAA
CCACCTGAAGGTTTCATGGCTCCCAAGGCTTGGACCGTGCTGACAGAATACTACAAATCC
TTGGAGAAAGCTTAG
|
| Enzyme 32 GenBank Gene ID |
Y10387 |
| Enzyme 32 GeneCard ID |
PAPSS1 |
| Enzyme 32 GenAtlas ID |
PAPSS1 |
| Enzyme 32 HGNC ID |
HGNC:8603 |
| Enzyme 32 Chromosome Location |
4 |
| Enzyme 32 Locus |
4q24 |
| Enzyme 32 SNPs |
SNPJam Report |
| Enzyme 32 General References |
- Girard JP, Baekkevold ES, Amalric F: Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase. FASEB J. 1998 May;12(7):603-12. [PubMed ]
- Venkatachalam KV, Akita H, Strott CA: Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains. J Biol Chem. 1998 Jul 24;273(30):19311-20. [PubMed ]
- Yanagisawa K, Sakakibara Y, Suiko M, Takami Y, Nakayama T, Nakajima H, Takayanagi K, Natori Y, Liu MC: cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme. Biosci Biotechnol Biochem. 1998 May;62(5):1037-40. [PubMed ]
- Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [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 ]
- Venkatachalam KV, Fuda H, Koonin EV, Strott CA: Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase. J Biol Chem. 1999 Jan 29;274(5):2601-4. [PubMed ]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
5589 |
| Enzyme 33 Name |
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2 |
| Enzyme 33 Synonyms |
- PAPS synthase 2
- PAPSS 2
- Sulfurylase kinase 2
- SK 2
- SK2
- Sulfate adenylyltransferase
- ATP-sulfurylase
- Sulfate adenylate transferase
- SAT
- Adenylyl-sulfate kinase
- 3'-phosphoadenosine-5'-phosphosulfate synthase
- APS kinase
- Adenosine-5'-phosphosulfate 3'-phosphotransferase
- Adenylylsulfate 3'-phosphotransferase
|
| Enzyme 33 Gene Name |
PAPSS2 |
| Enzyme 33 Protein Sequence |
>Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISF
ALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS
FISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDS
DYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAE
AETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVL
PVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVM
ESGDWLVGGDLQVLEKIRWNDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHAL
LMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLDPKSTIVAI
FPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAP
GLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKA
WKVLTDYYRSLEKN
|
| Enzyme 33 Number of Residues |
614 |
| Enzyme 33 Molecular Weight |
69500.2 |
| Enzyme 33 Theoretical pI |
8.13 |
| Enzyme 33 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- adenylyltransferase activity
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- nucleotidyltransferase activity
- purine nucleoside binding
- sulfate adenylyltransferase (ATP) activity
- sulfate adenylyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- sulfate assimilation
- sulfur metabolic process
|
| Component |
| — |
|
| Enzyme 33 General Function |
Involved in ATP binding |
| Enzyme 33 Specific Function |
Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS:activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. May have a important role in skeletogenesis during postnatal growth |
| Enzyme 33 Pathways |
|
| Enzyme 33 Reactions |
- ATP + sulfate = diphosphate + adenylyl sulfate [RN:R00529]
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
5052075 |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
O95340 |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
PAPS2_HUMAN |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>1845 bp
ATGTCGGGGATCAAGAAGCAAAAGACGGAGAACCAGCAGAAATCCACCAATGTAGTCTAT
CAGGCCCACCATGTGAGCAGGAATAAGAGAGGGCAAGTGGTTGGAACAAGGGGTGGGTTC
CGAGGATGTACCGTGTGGCTAACAGGTCTCTCTGGTGCTGGAAAAACAACGATAAGTTTT
GCCCTGGAGGAGTACCTTGTCTCCCATGCCATCCCTTGTTACTCCCTGGATGGGGACAAT
GTCCGTCATGGCCTTAACAGAAATCTCGGATTCTCTCCTGGGGACAGAGAGGAAAATATC
CGCCGGATTGCTGAGGTGGCTAAGCTGTTTGCTGATGCTGGTCTGGTCTGCATTACCAGC
TTTATTTCTCCATTCGCAAAGGATCGTGAGAATGCCCGCAAAATACATGAATCAGCAGGG
CTGCCATTCTTTGAAATATTTGTAGATGCACCTCTAAATATTTGTGAAAGCAGAGACGTA
AAAGGCCTCTATAAAAAGGCCAGAGCTGGGGAGATTAAAGGATTTACAGGTATTGATTCT
GATTATGAGAAACCTGAAACTCCTGAGCGTGTGCTTAAAACCAATTTGTCCACAGTGAGT
GACTGTGTCCACCAGGTAGTGGAACTTCTGCAAGAGCAGAACATTGTACCCTATACTATA
ATCAAAGATATCCACGAACTCTTTGTGCCGGAAAACAAACTTGACCACGTCCGAGCTGAG
GCTGAAACTCTCCCTTCATTATCAATTACTAAGCTGGATCTCCAGTGGGTCCAGGTTTTG
AGCGAAGGCTGGGCCACTCCCCTCAAAGGTTTCATGCGGGAGAAGGAGTACTTACAGGTT
ATGCACTTTGACACCCTGCTAGATGATGGCGTGATCAACATGAGCATCCCCATTGTACTG
CCCGTCTCTGCAGAGGATAAGACACGGCTGGAAGGGTGCAGCAAGTTTGTCCTGGCACAT
GGTGGACGGAGGGTAGCTATCTTACGAGACGCTGAATTCTATGAACACAGAAAAGAGGAA
CGCTGTTCCCGTGTTTGGGGGACAACATGTACAAAACACCCCCATATCAAAATGGTGATG
GAAAGTGGGGACTGGCTGGTTGGTGGAGACCTTCAGGTGCTGGAGAAAATAAGATGGAAT
GATGGGCTGGACCAATACCGTCTGACACCTCTGGAGCTCAAACAGAAATGTAAAGAAATG
AATGCTGATGCGGTGTTTGCATTCCAGTTGCGCAATCCTGTCCACAATGGCCATGCCCTG
TTGATGCAGGACACTCGCCGCAGGCTCCTAGAGAGGGGCTACAAGCACCCGGTCCTCCTA
CTACACCCTCTGGGCGGCTGGACCAAGGATGACGATGTGCCTCTAGACTGGCGGATGAAG
CAGCACGCGGCTGTGCTCGAGGAAGGGGTCCTGGATCCCAAGTCAACCATTGTTGCCATC
TTTCCGTCTCCCATGTTATATGCTGGCCCCACAGAGGTCCAGTGGCACTGCAGGTCCCGG
ATGATTGCGGGTGCCAATTTCTACATTGTGGGGAGGGACCCTGCAGGAATGCCCCATCCT
GAAACCAAGAAGGATCTGTATGAACCCACTCATGGGGGCAAGGTCTTGAGCATGGCCCCT
GGCCTCACCTCTGTGGAAATCATTCCATTCCGAGTGGCTGCCTACAACAAAGCCAAAAAA
GCCATGGACTTCTATGATCTAGCAAGGCACAATGAGTTTGACTTCATCTCAGGAACTCGA
ATGAGGAAGCTCGCCCGGGAAGGAGAGAATCCCCCAGATGGCTTCATGGCCCCCAAAGCA
TGGAAGGTCCTGACAGATTATTACAGGTCCCTGGAGAAGAACTAA
|
| Enzyme 33 GenBank Gene ID |
AF074331 |
| Enzyme 33 GeneCard ID |
PAPSS2 |
| Enzyme 33 GenAtlas ID |
PAPSS2 |
| Enzyme 33 HGNC ID |
HGNC:8604 |
| Enzyme 33 Chromosome Location |
1 |
| Enzyme 33 Locus |
10q24 |
| Enzyme 33 SNPs |
SNPJam Report |
| Enzyme 33 General References |
- ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, Superti-Furga A, Haque S, Abbas H, Ahmad W, Ahmad M, Cohn DH: Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse. Nat Genet. 1998 Oct;20(2):157-62. [PubMed ]
- Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [PubMed ]
- Kurima K, Singh B, Schwartz NB: Genomic organization of the mouse and human genes encoding the ATP sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2. J Biol Chem. 1999 Nov 19;274(47):33306-12. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Ahmad M, Haque MF, Ahmad W, Abbas H, Haque S, Krakow D, Rimoin DL, Lachman RS, Cohn DH: Distinct, autosomal recessive form of spondyloepimetaphyseal dysplasia segregating in an inbred Pakistani kindred. Am J Med Genet. 1998 Aug 6;78(5):468-73. [PubMed ]
- Noordam C, Dhir V, McNelis JC, Schlereth F, Hanley NA, Krone N, Smeitink JA, Smeets R, Sweep FC, Claahsen-van der Grinten HL, Arlt W: Inactivating PAPSS2 mutations in a patient with premature pubarche. N Engl J Med. 2009 May 28;360(22):2310-8. [PubMed ]
- Xu ZH, Freimuth RR, Eckloff B, Wieben E, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 (PAPSS2) pharmacogenetics: gene resequencing, genetic polymorphisms and functional characterization of variant allozymes. Pharmacogenetics. 2002 Jan;12(1):11-21. [PubMed ]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
5595 |
| Enzyme 34 Name |
Carbamoyl-phosphate synthase [ammonia], mitochondrial |
| Enzyme 34 Synonyms |
- Carbamoyl-phosphate synthetase I
- CPSase I
|
| Enzyme 34 Gene Name |
CPS1 |
| Enzyme 34 Protein Sequence |
>Carbamoyl-phosphate synthase [ammonia], mitochondrial
MTRILTAFKVVRTLKTGFGFTNVTAHQKWKFSRPGIRLLSVKAQTAHIVLEDGTKMKGYS
FGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTALDELGLSKY
LESNGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTML
GKIEFEGQPVDFVDPNKQNLIAEVSTKDVKVYGKGNPTKVVAVDCGIKNNVIRLLVKRGA
EVHLVPWNHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILESDRKEPLFGISTGNLIT
GLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDNTLPAGWKPLFVNVNDQT
NEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGKATTITSVLPKPALVASRV
EVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEVGLKQAD
TVYFLPITPQFVTEVIKAEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVES
IMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGIC
PNRETLMDLSTKAFAMTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHT
GDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLS
RSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDR
FHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIEGFTPRLPMNKEWPSNLDLR
KELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMT
EETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYV
TYNGQEHDVNFDDHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETV
STDFDECDKLYFEELSLERILDIYHQEACGGCIISVGGQIPNNLAVPLYKNGVKIMGTSP
LQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMN
VVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAG
VHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRA
SRSFPFVSKTLGVDFIDVATKVMIGENVDEKHLPTLDHPIIPADYVAIKAPMFSWPRLRD
ADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPRFLGVAEQ
LHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPN
NNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSRKVDSKSLFHYRQYSAGKAA
|
| Enzyme 34 Number of Residues |
1500 |
| Enzyme 34 Molecular Weight |
164938.1 |
| Enzyme 34 Theoretical pI |
6.71 |
| Enzyme 34 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- carbamoyl-phosphate synthase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- glutamine metabolic process
- metabolic process
- nitrogen compound metabolic process
|
| Component |
| — |
|
| Enzyme 34 General Function |
Involved in catalytic activity |
| Enzyme 34 Specific Function |
Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell |
| Enzyme 34 Pathways |
|
| Enzyme 34 Reactions |
- 2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate [RN:R00149]
|
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
5020420 |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
P31327 |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
CPSM_HUMAN |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>4503 bp
ATGACGAGGATTTTGACAGCTTTCAAAGTGGTGAGGACACTGAAGACTGGTTTTGGCTTT
ACCAATGTGACTGCACACCAAAAATGGAAATTTTCAAGACCTGGCATCAGGCTCCTTTCT
GTCAAGGCACAGACAGCACACATTGTCCTGGAAGATGGAACTAAGATGAAAGGTTACTCC
TTTGGCCATCCATCCTCTGTTGCTGGTGAAGTGGTTTTTAATACTGGCCTGGGAGGGTAC
CCAGAAGCTATTACTGACCCTGCCTACAAAGGACAGATTCTCACAATGGCCAACCCTATT
ATTGGGAATGGTGGAGCTCCTGATACTACTGCTCTGGATGAACTGGGACTTAGCAAATAT
TTGGAGTCTAATGGAATCAAGGTTTCAGGTTTGCTGGTGCTGGATTATAGTAAAGACTAC
AACCACTGGCTGGCTACCAAGAGTTTAGGGCAATGGCTACAGGAAGAAAAGGTTCCTGCA
ATTTATGGAGTGGACACAAGAATGCTGACTAAAATAATTCGGGATAAGGGTACCATGCTT
GGGAAGATTGAATTTGAAGGTCAGCCTGTGGATTTTGTGGATCCAAATAAACAGAATTTG
ATTGCTGAGGTTTCAACCAAGGATGTCAAAGTGTACGGCAAAGGAAACCCCACAAAAGTG
GTAGCTGTAGACTGTGGGATTAAAAACAATGTAATCCGCCTGCTAGTAAAGCGAGGAGCT
GAAGTGCACTTAGTTCCCTGGAACCATGATTTCACCAAGATGGAGTATGATGGGATTTTG
ATCGCGGGAGGACCGGGGAACCCAGCTCTTGCAGAACCACTAATTCAGAATGTCAGAAAG
ATTTTGGAGAGTGATCGCAAGGAGCCATTGTTTGGAATCAGTACAGGAAACTTAATAACA
GGATTGGCTGCTGGTGCCAAAACCTACAAGATGTCCATGGCCAACAGAGGGCAGAATCAG
CCTGTTTTGAATATCACAAACAAACAGGCTTTCATTACTGCTCAGAATCATGGCTATGCC
TTGGACAACACCCTCCCTGCTGGCTGGAAACCACTTTTTGTGAATGTCAACGATCAAACA
AATGAGGGGATTATGCATGAGAGCAAACCCTTCTTCGCTGTGCAGTTCCACCCAGAGGTC
ACCCCGGGGCCAATAGACACTGAGTACCTGTTTGATTCCTTTTTCTCACTGATAAAGAAA
GGAAAAGCTACCACCATTACATCAGTCTTACCGAAGCCAGCACTAGTTGCATCTCGGGTT
GAGGTTTCCAAAGTCCTTATTCTAGGATCAGGAGGTCTGTCCATTGGTCAGGCTGGAGAA
TTTGATTACTCAGGATCTCAAGCTGTAAAAGCCATGAAGGAAGAAAATGTCAAAACTGTT
CTGATGAACCCAAACATTGCATCAGTCCAGACCAATGAGGTGGGCTTAAAGCAAGCGGAT
ACTGTCTACTTTCTTCCCATCACCCCTCAGTTTGTCACAGAGGTCATCAAGGCAGAACAG
CCAGATGGGTTAATTCTGGGCATGGGTGGCCAGACAGCTCTGAACTGTGGAGTGGAACTA
TTCAAGAGAGGTGTGCTCAAGGAATATGGTGTGAAAGTCCTGGGAACTTCAGTTGAGTCC
ATTATGGCTACGGAAGACAGGCAGCTGTTTTCAGATAAACTAAATGAGATCAATGAAAAG
ATTGCTCCAAGTTTTGCAGTGGAATCGATTGAGGATGCACTGAAGGCAGCAGACACCATT
GGCTACCCAGTGATGATCCGTTCCGCCTATGCACTGGGTGGGTTAGGCTCAGGCATCTGT
CCCAACAGAGAGACTTTGATGGACCTCAGCACAAAGGCCTTTGCTATGACCAACCAAATT
CTGGTGGAGAAGTCAGTGACAGGTTGGAAAGAAATAGAATATGAAGTGGTTCGAGATGCT
GATGACAATTGTGTCACTGTCTGTAACATGGAAAATGTTGATGCCATGGGTGTTCACACA
GGTGACTCAGTTGTTGTGGCTCCTGCCCAGACACTCTCCAATGCCGAGTTTCAGATGTTG
AGACGTACTTCAATCAATGTTGTTCGCCACTTGGGCATTGTGGGTGAATGCAACATTCAG
TTTGCCCTTCATCCTACCTCAATGGAATACTGCATCATTGAAGTGAATGCCAGACTGTCC
CGAAGCTCTGCTCTGGCCTCAAAAGCCACTGGCTACCCATTGGCATTCATTGCTGCAAAG
ATTGCCCTAGGAATCCCACTTCCAGAAATTAAGAACGTCGTATCCGGGAAGACATCAGCC
TGTTTTGAACCTAGCCTGGATTACATGGTCACCAAGATTCCCCGCTGGGATCTTGACCGT
TTTCATGGAACATCTAGCCGAATTGGTAGCTCTATGAAAAGTGTAGGAGAGGTCATGGCT
ATTGGTCGTACCTTTGAGGAGAGTTTCCAGAAAGCTTTACGGATGTGCCACCCATCTATA
GAAGGTTTCACTCCCCGTCTCCCAATGAACAAAGAATGGCCATCTAATTTAGATCTTAGA
AAAGAGTTGTCTGAACCAAGCAGCACGCGTATCTATGCCATTGCCAAGGCCATTGATGAC
AACATGTCCCTTGATGAGATTGAGAAGCTCACATACATTGACAAGTGGTTTTTGTATAAG
ATGCGTGATATTTTAAACATGGAAAAGACACTGAAAGGGCTCAACAGTGAGTCCATGACA
GAAGAAACCCTGAAAAGGGCAAAGGAGATTGGGTTCTCAGATAAGCAGATTTCAAAATGC
CTTGGGCTCACTGAGGCCCAGACAAGGGAGCTGAGGTTAAAGAAAAACATCCACCCTTGG
GTTAAACAGATTGATACACTGGCTGCAGAATACCCATCAGTAACAAACTATCTCTATGTT
ACCTACAATGGTCAGGAGCATGATGTCAATTTTGATGACCATGGAATGATGGTGCTAGGC
TGTGGTCCATATCACATTGGCAGCAGTGTGGAATTTGATTGGTGTGCTGTCTCTAGTATC
CGCACACTGCGTCAACTTGGCAAGAAGACGGTGGTGGTGAATTGCAATCCTGAGACTGTG
AGCACAGACTTTGATGAGTGTGACAAACTGTACTTTGAAGAGTTGTCCTTGGAGAGAATC
CTAGACATCTACCATCAGGAGGCATGTGGTGGCTGCATCATATCAGTTGGAGGCCAGATT
CCAAACAACCTGGCAGTTCCTCTATACAAGAATGGTGTCAAGATCATGGGCACAAGCCCC
CTGCAGATCGACAGGGCTGAGGATCGCTCCATCTTCTCAGCTGTCTTGGATGAGCTGAAG
GTGGCTCAGGCACCTTGGAAAGCTGTTAATACTTTGAATGAAGCACTGGAATTTGCAAAG
TCTGTGGACTACCCCTGCTTGTTGAGGCCTTCCTATGTTTTGAGTGGGTCTGCTATGAAT
GTGGTATTCTCTGAGGATGAGATGAAAAAATTCCTAGAAGAGGCGACTAGAGTTTCTCAG
GAGCACCCAGTGGTCCTGACAAAATTTGTTGAAGGGGCCCGAGAAGTAGAAATGGACGCT
GTTGGCAAAGATGGAAGGGTTATCTCTCATGCCATCTCTGAACATGTTGAAGATGCAGGT
GTCCACTCGGGAGATGCCACTCTGATGCTGCCCACACAAACCATCAGCCAAGGGGCCATT
GAAAAGGTGAAGGATGCTACCCGGAAGATTGCAAAGGCTTTTGCCATCTCTGGTCCATTC
AACGTCCAATTTCTTGTCAAAGGAAATGATGTCTTGGTGATTGAGTGTAACTTGAGAGCT
TCTCGATCCTTCCCCTTTGTTTCCAAGACTCTTGGGGTTGACTTCATTGATGTGGCCACC
AAGGTGATGATTGGAGAGAATGTTGATGAGAAACATCTTCCAACATTGGACCATCCCATA
ATTCCTGCTGACTATGTTGCAATTAAGGCTCCCATGTTTTCCTGGCCCCGGTTGAGGGAT
GCTGACCCCATTCTGAGATGTGAGATGGCTTCCACTGGAGAGGTGGCTTGCTTTGGTGAA
GGTATTCATACAGCCTTCCTAAAGGCAATGCTTTCCACAGGATTTAAGATACCCCAGAAA
GGCATCCTGATAGGCATCCAGCAATCATTCCGGCCAAGATTCCTTGGTGTGGCTGAACAA
TTACACAATGAAGGTTTCAAGCTGTTTGCCACGGAAGCCACATCAGACTGGCTCAACGCC
AACAATGTCCCTGCCACCCCAGTGGCATGGCCGTCTCAAGAAGGACAGAATCCCAGCCTC
TCTTCCATCAGAAAATTGATTAGAGATGGCAGCATTGACCTAGTGATTAACCTTCCCAAC
AACAACACTAAATTTGTCCATGATAATTATGTGATTCGGAGGACAGCTGTTGATAGTGGA
ATCCCTCTCCTCACTAATTTTCAGGTGACCAAACTTTTTGCTGAAGCTGTGCAGAAATCT
CGCAAGGTGGACTCCAAGAGTCTTTTCCACTACAGGCAGTACAGTGCTGGAAAAGCAGCA
TAG
|
| Enzyme 34 GenBank Gene ID |
AF154830 |
| Enzyme 34 GeneCard ID |
CPS1 |
| Enzyme 34 GenAtlas ID |
CPS1 |
| Enzyme 34 HGNC ID |
HGNC:2323 |
| Enzyme 34 Chromosome Location |
2 |
| Enzyme 34 Locus |
2q35 |
| Enzyme 34 SNPs |
SNPJam Report |
| Enzyme 34 General References |
- Haraguchi Y, Uchino T, Takiguchi M, Endo F, Mori M, Matsuda I: Cloning and sequence of a cDNA encoding human carbamyl phosphate synthetase I: molecular analysis of hyperammonemia. Gene. 1991 Nov 15;107(2):335-40. [PubMed ]
- Finckh U, Kohlschutter A, Schafer H, Sperhake K, Colombo JP, Gal A: Prenatal diagnosis of carbamoyl phosphate synthetase I deficiency by identification of a missense mutation in CPS1. Hum Mutat. 1998;12(3):206-11. [PubMed ]
- Summar ML, Hall LD, Eeds AM, Hutcheson HB, Kuo AN, Willis AS, Rubio V, Arvin MK, Schofield JP, Dawson EP: Characterization of genomic structure and polymorphisms in the human carbamyl phosphate synthetase I gene. Gene. 2003 Jun 5;311:51-7. [PubMed ]
- Funghini S, Donati MA, Pasquini E, Zammarchi E, Morrone A: Structural organization of the human carbamyl phosphate synthetase I gene (CPS1) and identification of two novel genetic lesions. Hum Mutat. 2003 Oct;22(4):340-1. [PubMed ]
- Haberle J, Schmidt E, Pauli S, Rapp B, Christensen E, Wermuth B, Koch HG: Gene structure of human carbamylphosphate synthetase 1 and novel mutations in patients with neonatal onset. Hum Mutat. 2003 Apr;21(4):444. [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 ]
- Aoshima T, Kajita M, Sekido Y, Kikuchi S, Yasuda I, Saheki T, Watanabe K, Shimokata K, Niwa T: Novel mutations (H337R and 238-362del) in the CPS1 gene cause carbamoyl phosphate synthetase I deficiency. Hum Hered. 2001;52(2):99-101. [PubMed ]
- Pearson DL, Dawling S, Walsh WF, Haines JL, Christman BW, Bazyk A, Scott N, Summar ML: Neonatal pulmonary hypertension--urea-cycle intermediates, nitric oxide production, and carbamoyl-phosphate synthetase function. N Engl J Med. 2001 Jun 14;344(24):1832-8. [PubMed ]
- Wakutani Y, Nakayasu H, Takeshima T, Adachi M, Kawataki M, Kihira K, Sawada H, Bonno M, Yamamoto H, Nakashima K: Mutational analysis of carbamoylphosphate synthetase I deficiency in three Japanese patients. J Inherit Metab Dis. 2004;27(6):787-8. [PubMed ]
- Haberle J, Koch HG: Genetic approach to prenatal diagnosis in urea cycle defects. Prenat Diagn. 2004 May;24(5):378-83. [PubMed ]
- Kurokawa K, Yorifuji T, Kawai M, Momoi T, Nagasaka H, Takayanagi M, Kobayashi K, Yoshino M, Kosho T, Adachi M, Otsuka H, Yamamoto S, Murata T, Suenaga A, Ishii T, Terada K, Shimura N, Kiwaki K, Shintaku H, Yamakawa M, Nakabayashi H, Wakutani Y, Nakahata T: Molecular and clinical analyses of Japanese patients with carbamoylphosphate synthetase 1 (CPS1) deficiency. J Hum Genet. 2007;52(4):349-54. Epub 2007 Feb 20. [PubMed ]
- Moonen RM, Reyes I, Cavallaro G, Gonzalez-Luis G, Bakker JA, Villamor E: The T1405N carbamoyl phosphate synthetase polymorphism does not affect plasma arginine concentrations in preterm infants. PLoS One. 2010 May 25;5(5):e10792. [PubMed ]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
5605 |
| Enzyme 35 Name |
ADP-dependent glucokinase |
| Enzyme 35 Synonyms |
- ADP-GK
- ADPGK
- RbBP-35
|
| Enzyme 35 Gene Name |
ADPGK |
| Enzyme 35 Protein Sequence |
>ADP-dependent glucokinase
MALWRGSAYAGFLALAVGCVFLLEPELPGSALRSLWSSLCLGPAPAPPGPVSPEGRLAAA
WDALIVRPVRRWRRVAVGVNACVDVVLSGVKLLQALGLSPGNGKDHSILHSRNDLEEAFI
HFMGKGAAAERFFSDKETFHDIAQVASEFPGAQHYVGGNAALIGQKFAANSDLKVLLCGP
VGPKLHELLDDNVFVPPESLQEVDEFHLILEYQAGEEWGQLKAPHANRFIFSHDLSNGAM
NMLEVFVSSLEEFQPDLVVLSGLHMMEGQSKELQRKRLLEVVTSISDIPTGIPVHLELAS
MTNRELMSSIVHQQVFPAVTSLGLNEQELLFLTQSASGPHSSLSSWNGVPDVGMVSDILF
WILKEHGRSKSRASDLTRIHFHTLVYHILATVDGHWANQLAAVAAGARVAGTQACATETI
DTSRVSLRAPQEFMTSHSEAGSRIVLNPNKPVVEWHREGISFHFTPVLVCKDPIRTVGLG
DAISAEGLFYSEVHPHY
|
| Enzyme 35 Number of Residues |
497 |
| Enzyme 35 Molecular Weight |
54088.3 |
| Enzyme 35 Theoretical pI |
6.17 |
| Enzyme 35 GO Classification |
| Function |
- catalytic activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 35 General Function |
Involved in phosphotransferase activity, alcohol group as acceptor |
| Enzyme 35 Specific Function |
Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. GDP and CDP can replace ADP, but with reduced efficiency |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
- ADP + D-glucose = AMP + D-glucose 6-phosphate [RN:R05804]
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
13543940 |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
Q9BRR6 |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
ADPGK_HUMAN |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>1494 bp
ATGGCGCTGTGGCGCGGCTCCGCGTACGCGGGCTTCCTGGCGCTGGCCGTGGGCTGCGTC
TTCCTGCTGGAGCCAGAGCTGCCAGGCTCGGCGCTGCGCTCTCTCTGGAGCTCGCTGTGT
CTGGGGCCCGCGCCTGCGCCCCCGGGACCCGTCTCCCCCGAGGGCCGGTTGGCGGCAGCC
TGGGACGCGCTTATCGTGCGGCCAGTCCGGCGCTGGCGCCGCGTGGCAGTGGGAGTCAAT
GCATGTGTTGATGTGGTGCTCTCAGGGGTGAAGCTCTTGCAGGCACTTGGCCTTAGTCCT
GGGAATGGGAAAGATCACAGCATTCTGCATTCAAGGAATGATCTGGAAGAAGCCTTCATT
CACTTCATGGGGAAGGGAGCAGCTGCTGAGCGCTTCTTCAGTGATAAGGAAACTTTTCAC
GACATTGCCCAGGTTGCGTCAGAGTTCCCAGGAGCCCAGCACTATGTAGGAGGAAATGCA
GCTTTAATTGGACAGAAATTTGCAGCCAACTCAGATTTAAAGGTTCTTCTTTGCGGTCCA
GTTGGTCCAAAGCTACATGAGCTTCTTGATGACAATGTCTTTGTTCCACCAGAGTCATTG
CAGGAAGTGGATGAGTTCCACCTCATTTTAGAGTATCAAGCAGGGGAGGAGTGGGGCCAG
TTAAAAGCTCCCCATGCCAACCGATTCATCTTCTCTCACGACCTCTCCAACGGGGCCATG
AATATGCTGGAGGTGTTTGTGTCTAGCCTGGAGGAGTTTCAGCCAGACCTGGTGGTCCTC
TCTGGATTGCACATGATGGAGGGACAAAGCAAGGAGCTCCAGAGGAAGAGACTCTTGGAG
GTTGTAACCTCCATTTCTGACATCCCCACTGGTATTCCAGTTCACCTAGAGCTGGCCAGT
ATGACTAACAGGGAGCTCATGAGCAGCATTGTCCATCAGCAGGTCTTTCCCGCGGTGACT
TCCCTTGGGCTGAATGAACAGGAGCTGTTATTTCTCACCCAGTCAGCCTCTGGACCTCAC
TCTTCTCTCTCTTCCTGGAACGGTGTTCCTGATGTGGGCATGGTCAGTGACATCCTCTTC
TGGATCTTGAAAGAACATGGGAGGAGTAAAAGCAGAGCCTCGGATCTCACCAGGATCCAT
TTCCACACGCTGGTCTACCACATCCTGGCAACTGTGGATGGACACTGGGCCAACCAGCTG
GCAGCCGTGGCTGCAGGAGCTCGTGTGGCTGGGACACAGGCCTGCGCCACAGAAACCATA
GACACCAGCCGAGTGTCTCTGAGGGCACCCCAAGAGTTCATGACTTCCCATTCGGAGGCA
GGCTCCAGGATTGTATTAAACCCAAACAAGCCAGTAGTAGAATGGCACAGAGAGGGAATA
TCCTTCCACTTCACACCAGTATTGGTGTGTAAAGACCCCATTCGAACTGTAGGCCTTGGA
GATGCCATTTCAGCCGAAGGACTCTTCTATTCGGAAGTACACCCTCACTATTAG
|
| Enzyme 35 GenBank Gene ID |
BC006112 |
| Enzyme 35 GeneCard ID |
ADPGK |
| Enzyme 35 GenAtlas ID |
ADPGK |
| Enzyme 35 HGNC ID |
HGNC:25250 |
| Enzyme 35 Chromosome Location |
1 |
| Enzyme 35 Locus |
15q24.1 |
| Enzyme 35 SNPs |
SNPJam Report |
| Enzyme 35 General References |
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
5755 |
| Enzyme 36 Name |
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial |
| Enzyme 36 Synonyms |
- MCCase subunit beta
- 3-methylcrotonyl-CoA carboxylase 2
- 3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit
- 3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta
|
| Enzyme 36 Gene Name |
MCCC2 |
| Enzyme 36 Protein Sequence |
>Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
MWAVLRLALRPCARASPAGPRAYHGDSVASLGTQPDLGSALYQENYKQMKALVNQLHERV
EHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDNEEVPGGGII
TGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPR
QADVFPDRDHFGRTFYNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIF
LAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKKL
DVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFA
RIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAK
DGAKMVAAVACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAAN
VLATITKDQRAREGKQFSSADEAALKEPIIKKFEEEGNPYYSSARVWDDGIIDPADTRLV
LGLSFSAALNAPIEKTDFGIFRM
|
| Enzyme 36 Number of Residues |
563 |
| Enzyme 36 Molecular Weight |
61332.7 |
| Enzyme 36 Theoretical pI |
7.75 |
| Enzyme 36 GO Classification |
| Function |
- catalytic activity
- ligase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 36 General Function |
Involved in ligase activity |
| Enzyme 36 Specific Function |
ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA |
| Enzyme 36 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 36 Reactions |
- ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA [RN:R04138]
|
| Enzyme 36 Pfam Domain Function |
|
| 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 |
Q9HCC0 |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
MCCB_HUMAN |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>1692 bp
ATGTGGGCCGTCCTGAGGTTAGCCCTGCGGCCGTGTGCCCGCGCCTCTCCCGCCGGGCCG
CGCGCCTATCACGGGGACTCGGTGGCCTCGCTGGGCACCCAGCCGGACTTGGGCTCTGCC
CTCTACCAGGAGAACTACAAGCAGATGAAAGCACTAGTAAATCAGCTCCATGAACGAGTG
GAGCATATAAAACTAGGAGGTGGTGAGAAAGCCCGAGCACTTCACATATCAAGAGGAAAA
CTATTGCCCAGAGAAAGAATTGACAATCTCATAGACCCAGGGTCTCCATTTCTGGAATTA
TCCCAGTTTGCAGGTTACCAGTTATATGACAATGAGGAGGTGCCAGGAGGTGGCATTATT
ACAGGCATTGGAAGAGTATCAGGAGTAGAATGCATGATTATTGCCAATGATGCCACCGTC
AAAGGAGGTGCCTACTACCCAGTGACTGTGAAAAAACAATTACGGGCCCAAGAAATTGCC
ATGCAAAACAGGCTCCCCTGCATCTACTTAGTTGATTCGGGAGGAGCATACTTACCTCGA
CAAGCAGATGTGTTTCCAGATCGAGACCACTTTGGCCGTACATTCTATAATCAGGCAATT
ATGTCTTCTAAAAATATTGCACAGATCGCAGTGGTCATGGGCTCCTGCACCGCAGGAGGA
GCCTATGTGCCTGCCATGGCTGATGAAAACATCATTGTACGCAAGCAGGGTACCATTTTC
TTGGCAGGACCCCCCTTGGTTAAAGCGGCAACTGGGGAAGAAGTATCTGCTGAGGATCTT
GGAGGTGCTGATCTTCATTGCAGAAAGTCTGGAGTAAGTGACCACTGGGCTTTGGATGAT
CATCATGCCCTTCACTTAACTAGGAAGGTTGTGAGGAATCTAAATTATCAGAAGAAATTG
GATGTCACCATTGAACCTTCTGAAGAGCCTTTATTTCCTGCTGATGAATTGTATGGAATA
GTTGGTGCTAACCTTAAGAGGAGCTTTGATGTCCGAGAGGTCATTGCTAGAATCGTGGAT
GGAAGCAGATTCACTGAGTTCAAAGCCTTTTATGGAGACACATTAGTTACAGGATTTGCT
CGAATATTTGGGTACCCAGTAGGTATCGTTGGAAACAACGGAGTTCTCTTTTCTGAATCT
GCAAAAAAGGGTACTCACTTTGTCCAGTTATGCTGCCAAAGAAATATTCCTCTGCTGTTC
CTTCAAAACATTACTGGATTTATGGTTGGTAGAGAGTATGAAGCTGAAGGAATTGCCAAG
GATGGTGCCAAGATGGTGGCCGCTGTGGCCTGTGCCCAAGTGCCTAAGATAACCCTCATC
ATTGGGGGCTCCTATGGAGCCGGAAACTATGGGATGTGTGGCAGAGCGTATAGCCCAAGA
TTTCTCTACATTTGGCCAAATGCTCGTATCTCAGTGATGGGAGGAGAGCAGGCAGCCAAT
GTGTTGGCCACGATAACAAAGGACCAAAGAGCCCGGGAAGGAAAGCAGTTCTCCAGTGCT
GATGAAGCGGCTTTAAAAGAGCCCATCATTAAGAAGTTTGAAGAGGAAGGAAACCCTTAC
TATTCCAGCGCAAGGGTATGGGATGATGGGATCATTGATCCAGCAGACACCAGACTGGTC
TTGGGTCTCAGTTTTAGTGCAGCCCTCAACGCACCAATAGAGAAGACTGACTTCGGTATC
TTCAGGATGTAA
|
| Enzyme 36 GenBank Gene ID |
AB050049 |
| Enzyme 36 GeneCard ID |
MCCC2 |
| Enzyme 36 GenAtlas ID |
MCCC2 |
| Enzyme 36 HGNC ID |
HGNC:6937 |
| Enzyme 36 Chromosome Location |
5 |
| Enzyme 36 Locus |
5q12-q13 |
| Enzyme 36 SNPs |
SNPJam Report |
| Enzyme 36 General References |
- Gallardo ME, Desviat LR, Rodriguez JM, Esparza-Gordillo J, Perez-Cerda C, Perez B, Rodriguez-Pombo P, Criado O, Sanz R, Morton DH, Gibson KM, Le TP, Ribes A, de Cordoba SR, Ugarte M, Penalva MA: The molecular basis of 3-methylcrotonylglycinuria, a disorder of leucine catabolism. Am J Hum Genet. 2001 Feb;68(2):334-46. Epub 2001 Jan 17. [PubMed ]
- Baumgartner MR, Almashanu S, Suormala T, Obie C, Cole RN, Packman S, Baumgartner ER, Valle D: The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency. J Clin Invest. 2001 Feb;107(4):495-504. [PubMed ]
- Holzinger A, Roschinger W, Lagler F, Mayerhofer PU, Lichtner P, Kattenfeld T, Thuy LP, Nyhan WL, Koch HG, Muntau AC, Roscher AA: Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency. Hum Mol Genet. 2001 Jun 1;10(12):1299-306. [PubMed ]
- Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
5757 |
| Enzyme 37 Name |
Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial |
| Enzyme 37 Synonyms |
- MCCase subunit alpha
- 3-methylcrotonyl-CoA carboxylase 1
- 3-methylcrotonyl-CoA carboxylase biotin-containing subunit
- 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha
|
| Enzyme 37 Gene Name |
MCCC1 |
| Enzyme 37 Protein Sequence |
>Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
MAAASAVSVLLVAAERNRWHRLPSLLLPPRTWVWRQRTMKYTTATGRNITKVLIANRGEI
ACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTS
AAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEG
YHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFN
DDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRK
KLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQL
RIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADPSTRIETGV
RQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFE
AGNVHTDFIPQHHKQLLLSRKAAAKESLCQAALGLILKEKAMTDTFTLQAHDQFSPFSSS
SGRRLNISYTRNMTLKDGKNNVAIAVTYNHDGSYSMQIEDKTFQVLGNLYSEGDCTYLKC
SVNGVASKAKLIILENTIYLFSKEGSIEIDIPVPKYLSSVSSQETQGGPLAPMTGTIEKV
FVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEESD
KRESE
|
| Enzyme 37 Number of Residues |
725 |
| Enzyme 37 Molecular Weight |
80472.4 |
| Enzyme 37 Theoretical pI |
7.86 |
| Enzyme 37 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- nucleoside binding
- purine nucleoside binding
- vitamin binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 37 General Function |
Involved in catalytic activity |
| Enzyme 37 Specific Function |
ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA |
| Enzyme 37 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 37 Reactions |
- ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA [RN:R04138]
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
Not Available |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
Q96RQ3 |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
MCCA_HUMAN |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>2178 bp
ATGGCGGCGGCCTCTGCGGTGTCGGTGCTGCTGGTGGCGGCGGAGAGGAACCGGTGGCAT
CGTCTCCCGAGCCTGCTCCTGCCGCCGAGGACATGGGTGTGGAGGCAAAGAACCATGAAG
TACACAACAGCCACAGGAAGAAACATTACCAAGGTCCTCATTGCAAACAGAGGAGAAATT
GCCTGCAGGGTGATGCGCACAGCCAAAAAACTGGGTGTACAGACTGTGGCGGTTTATAGT
GAGGCTGACAGAAATTCCATGCATGTAGATATGGCAGATGAAGCATATTCCATCGGCCCC
GCTCCCTCCCAGCAGAGCTACCTATCTATGGAGAAAATCATTCAAGTGGCCAAGACCTCT
GCTGCACAGGCTATCCATCCAGGATGCGGTTTTCTTTCAGAAAACATGGAATTTGCTGAA
CTTTGTAAGCAAGAAGGAATTATTTTTATAGGCCCTCCTCCATCTGCAATTAGAGACATG
GGTATAAAGAGCACATCCAAATCCATAATGGCTGCTGCTGGAGTACCTGTTGTGGAGGGT
TATCATGGTGAGGACCAATCAGACCAGTGCCTGAAGGAACACGCCAGGAGAATTGGCTAT
CCTGTCATGATTAAAGCCGTCCGGGGTGGAGGAGGAAAAGGAATGAGGATTGTTAGATCA
GAACAAGAATTTCAAGAACAGTTAGAGTCAGCACGGAGAGAAGCTAAGAAGTCTTTCAAT
GATGATGCTATGCTGATCGAGAAGTTTGTAGACACACCGAGGCATGTAGAAGTCCAGGTG
TTTGGTGATCACCATGGCAATGCTGTGTACTTGTTTGAAAGAGACTGTAGTGTGCAGAGG
CGACATCAGAAGATCATTGAGGAGGCCCCAGCGCCTGGTATTAAATCTGAAGTAAGAAAA
AAGCTGGGAGAAGCTGCAGTCAGAGCTGCTAAAGCTGTAAATTATGTTGGAGCAGGGACT
GTGGAGTTTATTATGGACTCAAAACATAATTTCTGTTTCATGGAGATGAATACAAGGCTG
CAAGTGGAACATCCTGTTACTGAGATGATCACAGGAACTGACTTGGTGGAGTGGCAGCTT
AGAATTGCAGCAGGAGAGAAGATTCCTTTGAGCCAGGAAGAAATAACTCTGCAGGGCCAT
GCCTTCGAAGCTAGAATATATGCAGAAGATCCTAGCAATAACTTCATGCCTGTGGCAGGC
CCATTAGTGCACCTCTCTACTCCTCGAGCAGACCCTTCCACCAGGATTGAAACTGGAGTA
CGGCAAGGAGACGAAGTTTCCGTGCATTATGACCCCATGATTGCGAAGCTGGTCGTGTGG
GCAGCAGATCGCCAGGCGGCATTGACAAAACTGAGGTACAGCCTTCGTCAGTACAATATT
GTTGGACTGCACACCAACATTGACTTCTTACTCAACCTGTCTGGCCACCCAGAGTTTGAA
GCTGGGAACGTGCACACTGATTTCATCCCTCAACACCACAAACAGTTGTTGCTCAGTCGG
AAGGCTGCAGCCAAAGAGTCTTTATGCCAGGCAGCCCTGGGTCTCATCCTCAAGGAGAAA
GCCATGACCGACACTTTCACTCTTCAGGCACATGATCAATTCTCTCCATTTTCGTCTAGC
AGTGGAAGAAGACTGAATATCTCGTATACCAGAAACATGACTCTTAAAGATGGTAAAAAC
AATGTAGCCATAGCTGTAACGTATAACCATGATGGGTCTTATAGCATGCAGATTGAAGAT
AAAACTTTCCAAGTCCTTGGTAATCTTTACAGCGAGGGAGACTGCACTTACCTGAAATGT
TCTGTTAATGGAGTTGCTAGTAAAGCGAAGCTGATTATCCTGGAAAACACTATTTACCTA
TTTTCCAAGGAAGGAAGTATTGAGATTGACATTCCAGTCCCCAAATACTTATCTTCTGTG
AGCTCACAAGAAACTCAGGGCGGCCCCTTAGCTCCTATGACTGGAACCATTGAAAAGGTG
TTTGTCAAAGCTGGAGACAAAGTGAAAGCGGGAGATTCCCTCATGGTTATGATCGCCATG
AAGATGGAGCATACCATAAAGTCTCCAAAGGATGGCACAGTAAAGAAAGTGTTCTACAGA
GAAGGTGCTCAGGCCAACAGACACACTCCTTTAGTCGAGTTTGAGGAGGAAGAATCAGAC
AAAAGGGAATCGGAATAA
|
| Enzyme 37 GenBank Gene ID |
AF310972 |
| Enzyme 37 GeneCard ID |
MCCC1 |
| Enzyme 37 GenAtlas ID |
MCCC1 |
| Enzyme 37 HGNC ID |
HGNC:6936 |
| Enzyme 37 Chromosome Location |
3 |
| Enzyme 37 Locus |
3q27 |
| Enzyme 37 SNPs |
SNPJam Report |
| Enzyme 37 General References |
- Gallardo ME, Desviat LR, Rodriguez JM, Esparza-Gordillo J, Perez-Cerda C, Perez B, Rodriguez-Pombo P, Criado O, Sanz R, Morton DH, Gibson KM, Le TP, Ribes A, de Cordoba SR, Ugarte M, Penalva MA: The molecular basis of 3-methylcrotonylglycinuria, a disorder of leucine catabolism. Am J Hum Genet. 2001 Feb;68(2):334-46. Epub 2001 Jan 17. [PubMed ]
- Obata K, Fukuda T, Morishita R, Abe S, Asakawa S, Yamaguchi S, Yoshino M, Ihara K, Murayama K, Shigemoto K, Shimizu N, Kondo I: Human biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase gene (MCCA): cDNA sequence, genomic organization, localization to chromosomal band 3q27, and expression. Genomics. 2001 Mar 1;72(2):145-52. [PubMed ]
- Holzinger A, Roschinger W, Lagler F, Mayerhofer PU, Lichtner P, Kattenfeld T, Thuy LP, Nyhan WL, Koch HG, Muntau AC, Roscher AA: Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency. Hum Mol Genet. 2001 Jun 1;10(12):1299-306. [PubMed ]
- Baumgartner MR, Almashanu S, Suormala T, Obie C, Cole RN, Packman S, Baumgartner ER, Valle D: The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency. J Clin Invest. 2001 Feb;107(4):495-504. [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 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
5759 |
| Enzyme 38 Name |
Glutamate--cysteine ligase catalytic subunit |
| Enzyme 38 Synonyms |
- GCS heavy chain
- Gamma-ECS
- Gamma-glutamylcysteine synthetase
|
| Enzyme 38 Gene Name |
GCLC |
| Enzyme 38 Protein Sequence |
>Glutamate--cysteine ligase catalytic subunit
MGLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDH
ENKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTV
EANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAI
NKHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDA
MGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVI
SASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQ
EGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDI
GWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVL
QGMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNS
YLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYS
LILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN
|
| Enzyme 38 Number of Residues |
637 |
| Enzyme 38 Molecular Weight |
72765.1 |
| Enzyme 38 Theoretical pI |
5.98 |
| Enzyme 38 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- glutamate-cysteine ligase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
|
| Process |
- cellular metabolic process
- glutathione biosynthetic process
- glutathione metabolic process
- metabolic process
- peptide metabolic process
|
| Component |
| — |
|
| Enzyme 38 General Function |
Involved in glutamate-cysteine ligase activity |
| Enzyme 38 Specific Function |
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine |
| Enzyme 38 Pathways |
|
| Enzyme 38 Reactions |
- ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine [RN:R00894]
|
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
Not Available |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
P48506 |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
GSH1_HUMAN |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>1914 bp
ATGGGGCTGCTGTCCCAGGGCTCGCCGCTGAGCTGGGAGGAAACCAAGCGCCATGCCGAC
CACGTGCGGCGGCACGGGATCCTCCAGTTCCTGCACATCTACCACGCCGTCAAGGACCGG
CACAAGGACGTTCTCAAGTGGGGCGATGAGGTGGAATACATGTTGGTATCTTTTGATCAT
GAAAATAAAAAAGTCCGGTTGGTCCTGTCTGGGGAGAAAGTTCTTGAAACTCTGCAAGAG
AAGGGGGAAAGGACAAACCCAAACCATCCTACCCTTTGGAGACCAGAGTATGGGAGTTAC
ATGATTGAAGGGACACCAGGACAGCCCTACGGAGGAACAATGTCCGAGTTCAATACAGTT
GAGGCCAACATGCGAAAACGCCGGAAGGAGGCTACTTCTATATTAGAAGAAAATCAGGCT
CTTTGCACAATAACTTCATTTCCCAGATTAGGCTGTCCTGGGTTCACACTGCCCGAGGTC
AAACCCAACCCAGTGGAAGGAGGAGCTTCCAAGTCCCTCTTCTTTCCAGATGAAGCAATA
AACAAGCACCCTCGCTTCAGTACCTTAACAAGAAATATCCGACATAGGAGAGGAGAAAAG
GTTGTCATCAATGTACCAATATTTAAGGACAAGAATACACCATCTCCATTTATAGAAACA
TTTACTGAGGATGATGAAGCTTCAAGGGCTTCTAAGCCGGATCATATTTACATGGATGCC
ATGGGATTTGGAATGGGCAATTGCTGTCTCCAGGTGACATTCCAAGCCTGCAGTATATCT
GAGGCCAGATACCTTTATGATCAGTTGGCTACTATCTGTCCAATTGTTATGGCTTTGAGT
GCTGCATCTCCCTTTTACCGAGGCTATGTGTCAGACATTGATTGTCGCTGGGGAGTGATT
TCTGCATCTGTAGATGATAGAACTCGGGAGGAGCGAGGACTGGAGCCATTGAAGAACAAT
AACTATAGGATCAGTAAATCCCGATATGACTCAATAGACAGCTATTTATCTAAGTGTGGT
GAGAAATATAATGACATCGACTTGACGATAGATAAAGAGATCTACGAACAGCTGTTGCAG
GAAGGCATTGATCATCTCCTGGCCCAGCATGTTGCTCATCTCTTTATTAGAGACCCACTG
ACACTGTTTGAAGAGAAAATACACCTGGATGATGCTAATGAGTCTGACCATTTTGAGAAT
ATTCAGTCCACAAATTGGCAGACAATGAGATTTAAGCCCCCTCCTCCAAACTCAGACATT
GGATGGAGAGTAGAATTTCGACCCATGGAGGTGCAATTAACAGACTTTGAGAACTCTGCC
TATGTGGTGTTTGTGGTACTGCTCACCAGAGTGATCCTTTCCTACAAATTGGATTTTCTC
ATTCCACTGTCAAAGGTTGATGAGAACATGAAGGTAGCACAGAAAAGAGATGCTGTCTTG
CAGGGAATGTTTTATTTCAGGAAAGATATTTGCAAAGGTGGCAATGCAGTGGTGGATGGT
TGTGGCAAGGCCCAGAACAGCACGGAGCTCGCTGCAGAGGAGTACACCCTCATGAGCATA
GACACCATCATCAATGGGAAGGAAGGTGTGTTTCCTGGACTGATCCCAATTCTGAACTCT
TACCTTGAAAACATGGAAGTGGATGTGGACACCAGATGTAGTATTCTGAACTACCTAAAG
CTAATTAAGAAGAGAGCATCTGGAGAACTAATGACAGTTGCCAGATGGATGAGGGAGTTT
ATCGCAAACCATCCTGACTACAAGCAAGACAGTGTCATAACTGATGAAATGAATTATAGC
CTTATTTTGAAGTGTAACCAAATTGCAAATGAATTATGTGAATGCCCAGAGTTACTTGGA
TCAGCATTTAGGAAAGTAAAATATAGTGGAAGTAAAACTGACTCATCCAACTAG
|
| Enzyme 38 GenBank Gene ID |
M90656 |
| Enzyme 38 GeneCard ID |
GCLC |
| Enzyme 38 GenAtlas ID |
GCLC |
| Enzyme 38 HGNC ID |
HGNC:4311 |
| Enzyme 38 Chromosome Location |
6 |
| Enzyme 38 Locus |
6p12 |
| Enzyme 38 SNPs |
SNPJam Report |
| Enzyme 38 General References |
- Gipp JJ, Chang C, Mulcahy RT: Cloning and nucleotide sequence of a full-length cDNA for human liver gamma-glutamylcysteine synthetase. Biochem Biophys Res Commun. 1992 May 29;185(1):29-35. [PubMed ]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Mulcahy RT, Gipp JJ: Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem Biophys Res Commun. 1995 Apr 6;209(1):227-33. [PubMed ]
- Beutler E, Gelbart T, Kondo T, Matsunaga AT: The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency. Blood. 1999 Oct 15;94(8):2890-4. [PubMed ]
- Misra I, Griffith OW: Expression and purification of human gamma-glutamylcysteine synthetase. Protein Expr Purif. 1998 Jul;13(2):268-76. [PubMed ]
- Ristoff E, Augustson C, Geissler J, de Rijk T, Carlsson K, Luo JL, Andersson K, Weening RS, van Zwieten R, Larsson A, Roos D: A missense mutation in the heavy subunit of gamma-glutamylcysteine synthetase gene causes hemolytic anemia. Blood. 2000 Apr 1;95(7):2193-6. [PubMed ]
- Hamilton D, Wu JH, Alaoui-Jamali M, Batist G: A novel missense mutation in the gamma-glutamylcysteine synthetase catalytic subunit gene causes both decreased enzymatic activity and glutathione production. Blood. 2003 Jul 15;102(2):725-30. Epub 2003 Mar 27. [PubMed ]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
5834 |
| Enzyme 39 Name |
Adenylate kinase isoenzyme 1 |
| Enzyme 39 Synonyms |
- AK 1
- ATP-AMP transphosphorylase 1
- Myokinase
|
| Enzyme 39 Gene Name |
AK1 |
| Enzyme 39 Protein Sequence |
>Adenylate kinase isoenzyme 1
MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRSEVSSGSARGKKLSEI
MEKGQLVPLETVLDMLRDAMVAKVNTSKGFLIDGYPREVQQGEEFERRIGQPTLLLYVDA
GPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVD
SVFSQVCTHLDALK
|
| Enzyme 39 Number of Residues |
194 |
| Enzyme 39 Molecular Weight |
21634.7 |
| Enzyme 39 Theoretical pI |
8.99 |
| Enzyme 39 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- adenylate kinase activity
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- ATP metabolic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate metabolic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 39 General Function |
Involved in ATP binding |
| Enzyme 39 Specific Function |
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth |
| Enzyme 39 Pathways |
|
| Enzyme 39 Reactions |
- ATP + AMP = 2 ADP [RN:R00127]
|
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
Not Available |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
P00568 |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
KAD1_HUMAN |
| Enzyme 39 PDB ID |
1Z83 |
| Enzyme 39 PDB File |
Show |
| Enzyme 39 3D Structure |
|
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>585 bp
ATGGAAGAGAAGCTGAAGAAAACCAAGATCATCTTTGTGGTGGGTGGGCCTGGCTCAGGG
AAGGGCACCCAGTGTGAGAAGATCGTGCAGAAGTATGGCTACACCCACCTCTCCACCGGG
GACCTCCTGCGGTCCGAGGTCAGCTCAGGCTCGGCCAGGGGCAAGAAGCTGTCGGAAATC
ATGGAGAAGGGGCAGCTGGTTCCACTGGAGACAGTGTTGGACATGCTCCGGGATGCCATG
GTGGCCAAAGTCAATACTTCCAAAGGCTTCCTGATTGATGGCTACCCGCGGGAGGTGCAG
CAAGGAGAAGAGTTTGAGCGACGGATTGGACAGCCCACACTGCTGCTGTATGTGGACGCA
GGCCCTGAGACCATGACCCAGCGGCTCTTGAAACGTGGAGAGACCAGCGGGCGTGTGGAC
GACAATGAGGAGACCATCAAAAAGCGGCTGGAGACCTATTACAAGGCCACAGAACCCGTC
ATCGCCTTCTATGAGAAACGTGGCATTGTGCGCAAGGTCAACGCTGAGGGCTCCGTGGAC
AGTGTCTTCTCCCAGGTCTGCACCCACCTGGACGCCCTAAAGTAG
|
| Enzyme 39 GenBank Gene ID |
AB021871 |
| Enzyme 39 GeneCard ID |
AK1 |
| Enzyme 39 GenAtlas ID |
AK1 |
| Enzyme 39 HGNC ID |
HGNC:361 |
| Enzyme 39 Chromosome Location |
9 |
| Enzyme 39 Locus |
9q34.1 |
| Enzyme 39 SNPs |
SNPJam Report |
| Enzyme 39 General References |
- Von Zabern I, Wittmann-Liebold B, Untucht-Grau R, Schirmer RH, Pai EF: Primary and tertiary structure of the principal human adenylate kinase. Eur J Biochem. 1976 Sep;68(1):281-90. [PubMed ]
- Matsuura S, Igarashi M, Tanizawa Y, Yamada M, Kishi F, Kajii T, Fujii H, Miwa S, Sakurai M, Nakazawa A: Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase. J Biol Chem. 1989 Jun 15;264(17):10148-55. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Qualtieri A, Pedace V, Bisconte MG, Bria M, Gulino B, Andreoli V, Brancati C: Severe erythrocyte adenylate kinase deficiency due to homozygous A-->G substitution at codon 164 of human AK1 gene associated with chronic haemolytic anaemia. Br J Haematol. 1997 Dec;99(4):770-6. [PubMed ]
- Corrons JL, Garcia E, Tusell JJ, Varughese KI, West C, Beutler E: Red cell adenylate kinase deficiency: molecular study of 3 new mutations (118G>A, 190G>A, and GAC deletion) associated with hereditary nonspherocytic hemolytic anemia. Blood. 2003 Jul 1;102(1):353-6. Epub 2003 Mar 20. [PubMed ]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
5845 |
| Enzyme 40 Name |
GTP:AMP phosphotransferase, mitochondrial |
| Enzyme 40 Synonyms |
- Adenylate kinase 3
- AK 3
- Adenylate kinase 3 alpha-like 1
|
| Enzyme 40 Gene Name |
AK3 |
| Enzyme 40 Protein Sequence |
>GTP:AMP phosphotransferase, mitochondrial
MGASARLLRAVIMGAPGSGKGTVSSRITTHFELKHLSSGDLLRDNMLRGTEIGVLAKAFI
DQGKLIPDDVMTRLALHELKNLTQYSWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEV
IKQRLTARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDDKPETVIKRLKAYEDQT
KPVLEYYQKKGVLETFSGTETNKIWPYVYAFLQTKVPQRSQKASVTP
|
| Enzyme 40 Number of Residues |
227 |
| Enzyme 40 Molecular Weight |
25565.2 |
| Enzyme 40 Theoretical pI |
9.64 |
| Enzyme 40 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- adenylate kinase activity
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside binding
- nucleotide kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
|
| Component |
| — |
|
| Enzyme 40 General Function |
Involved in ATP binding |
| Enzyme 40 Specific Function |
NTP + AMP = NDP + ADP |
| Enzyme 40 Pathways |
|
| Enzyme 40 Reactions |
- nucleoside triphosphate + AMP = nucleoside diphosphate + ADP [RN:R00333]
|
| Enzyme 40 Pfam Domain Function |
|
| Enzyme 40 Signals |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
6518533 |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
Q9UIJ7 |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
KAD3_HUMAN |
| Enzyme 40 PDB ID |
2AK3 |
| Enzyme 40 PDB File |
Show |
| Enzyme 40 3D Structure |
|
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>684 bp
ATGGGGGCGTCGGGGCGGCTGCTGCGAGCGGTGATCATGGGGGCCCCGGGCTCGGGCAAG
GGCACCGTGTCGTCCCGCATCACTACACACTTCGAGCTGAAGCACCTCTCCCGCGGGGAC
CTGCTCCGGGACAACATGCTGCGGGGCACAGAAATTGGCGTGTTAGCCCAGGCTTTCATT
GACCAAGGGAAACTCATCCCAGATTATGTCACGACTCGGCTGGCCCTTCATGAGCTGAAA
AACCTCACCCAGTATAGCTGGCTGTTGGATGGTTTTCCAAGGACACTTCCACAGGCAGAA
GCCCTAGATAGAGCTTATCAGATCGACACAGTGATTAACCTGAATGTGCCCTTTGAGGTC
ATTAAACAACGCCTTACTGCTCGCTGGATTCATCCCGCCAGTGGCCGAGTCTATAACATT
GAATTCAACCCTCCCAAAACTGTGGGCATTGATGACCTGACTGGGGAGCCTCTCATTCAG
CGTGAGGATGATAAACCAGAGACGGTTATCAAGAGACTAAAGGCTTATGAAGACCAAACA
AAGCCAGTCCTGGAATATTACCAGAAAAAAGGGGTGTTGGAAACATTCTCCGGAACAGAA
ACCAACAAGATTTGGCCCTATGTATATGCTTTCCTACAAACTAAAGTTCCACAAAGAAGC
CAGAAAGCTTCAGTTACTCCATGA
|
| Enzyme 40 GenBank Gene ID |
AB021870 |
| Enzyme 40 GeneCard ID |
AK3 |
| Enzyme 40 GenAtlas ID |
AK3 |
| Enzyme 40 HGNC ID |
HGNC:17376 |
| Enzyme 40 Chromosome Location |
9 |
| Enzyme 40 Locus |
9p24.1 |
| Enzyme 40 SNPs |
SNPJam Report |
| Enzyme 40 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
5858 |
| Enzyme 41 Name |
Adenylate kinase isoenzyme 4, mitochondrial |
| Enzyme 41 Synonyms |
- ATP-AMP transphosphorylase
- Adenylate kinase 3-like
|
| Enzyme 41 Gene Name |
AK4 |
| Enzyme 41 Protein Sequence |
>Adenylate kinase isoenzyme 4, mitochondrial
MASKLLRAVILGPPGSGKGTVCQRIAQNFGLQHLSSGHFLRENIKASTEVGEMAKQYIEK
SLLVPDHVITRLMMSELENRRGQHWLLDGFPRTLGQAEALDKICEVDLVISLNIPFETLK
DRLSRRWIHPPSGRVYNLDFNPPHVHGIDDVTGEPLVQQEDDKPEAVAARLRQYKDVAKP
VIELYKSRGVLHQFSGTETNKIWPYVYTLFSNKITPIQSKEAY
|
| Enzyme 41 Number of Residues |
223 |
| Enzyme 41 Molecular Weight |
25267.8 |
| Enzyme 41 Theoretical pI |
8.66 |
| Enzyme 41 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- adenylate kinase activity
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside binding
- nucleotide kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
|
| Component |
| — |
|
| Enzyme 41 General Function |
Involved in ATP binding |
| Enzyme 41 Specific Function |
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. May also be active with GTP |
| Enzyme 41 Pathways |
|
| Enzyme 41 Reactions |
- ATP + AMP = 2 ADP [RN:R00127]
|
| Enzyme 41 Pfam Domain Function |
|
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
189069342 |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
P27144 |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
KAD4_HUMAN |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>672 bp
ATGGCTTCCAAACTCCTGCGCGCGGTCATCCTCGGGCCGCCCGGCTCGGGCAAGGGCACC
GTGTGCCAGAGGATCGCCCAGAACTTTGGTCTCCAGCATCTCTCCAGCGGCCACTTCTTG
CGGGAGAACATCAAGGCCAGCACCGAAGTTGGTGAGATGGCAAAGCAGTATATAGAGAAA
AGTCTTTTGGTTCCAGACCATGTGATCACACGCCTAATGATGTCCGAGTTGGAGAACAGG
CGTGGCCAGCACTGGCTCCTTGATGGTTTTCCTAGGACATTAGGACAAGCCGAAGCCCTG
GACAAAATCTGTGAAGTGGATCTAGTGATCAGTTTGAATATTCCATTTGAAACACTTAAA
GATCGTCTCAGCCGCCGTTGGATTCACCCTCCTAGCGGAAGGGTATATAACCTGGACTTC
AATCCACCTCATGTACATGGTATTGATGACGTCACTGGTGAACCATTAGTCCAGCAGGAG
GATGATAAACCCGAAGCAGTTGCTGCCAGGCTAAGACAGTACAAAGACGTGGCAAAGCCA
GTCATTGAATTATACAAGAGCCGAGGAGTGCTCCACCAATTTTCCGGAACGGAGACGAAC
AAAATCTGGCCCTACGTTTACACACTTTTCTCAAACAAGATCACACCTATTCAGTCCAAA
GAAGCATATTGA
|
| Enzyme 41 GenBank Gene ID |
AK313611 |
| Enzyme 41 GeneCard ID |
AK4 |
| Enzyme 41 GenAtlas ID |
AK4 |
| Enzyme 41 HGNC ID |
HGNC:363 |
| Enzyme 41 Chromosome Location |
1 |
| Enzyme 41 Locus |
1p31.3 |
| Enzyme 41 SNPs |
SNPJam Report |
| Enzyme 41 General References |
- Xu G, O'Connell P, Stevens J, White R: Characterization of human adenylate kinase 3 (AK3) cDNA and mapping of the AK3 pseudogene to an intron of the NF1 gene. Genomics. 1992 Jul;13(3):537-42. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
5875 |
| Enzyme 42 Name |
Putative adenylate kinase 7 |
| Enzyme 42 Synonyms |
Not Available |
| Enzyme 42 Gene Name |
AK7 |
| Enzyme 42 Protein Sequence |
>Putative adenylate kinase 7
MAEEEETAALTEKVIRTQRVFINLLDSYSSGNIGKFLSNCVVGASLEEITEEEEEEDENK
SAMLEASSTKVKEGTFQIVGTLSKPDSPRPDFAVETYSAISREDLLMRLLECDVIIYNIT
ESSQQMEEAIWAVSALSEEVSHFEKRKLFILLSTVMTWARSKALDPEDSEVPFTEEDYRR
RKSHPNFLDHINAEKMVLKFGKKARKFAAYVVAAGLQYGAEGGMLHTFFKMAWLGEIPAL
PVFGDGTNVIPTIHVLDLAGVIQNVIDHVPKPHYLVAVDESVHTLEDIVKCISKNTGPGK
IQKIPRENAYLTKDLTQDCLDHLLVNLRMEALFVKENFNIRWAAQTGFVENINTILKEYK
QSRGLMPIKICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLEAIVAPNDVGE
GEEEVEEEEEEENVEDAQELLDGIKESMEQNAGQLDDQYIIRFMKEKLKSMPCRNQGYIL
DGFPKTYDQAKDLFNQEDEEEEDDVRGRMFPFDKLIIPEFVCALDASDEFLKERVINLPE
SIVAGTHYSQDRFLRALSNYRDINIDDETVFNYFDELEIHPIHIDVGKLEDAQNRLAIKQ
LIKEIGEPRNYGLTDEEKAEEERKAAEERLAREAAEEAEREHQEAVEMAEKIARWEEWNK
RLEEVKREERELLEAQSIPLRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNNP
EAQ
|
| Enzyme 42 Number of Residues |
723 |
| Enzyme 42 Molecular Weight |
82657.7 |
| Enzyme 42 Theoretical pI |
4.38 |
| Enzyme 42 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside binding
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
|
| Component |
| — |
|
| Enzyme 42 General Function |
Involved in ATP binding |
| Enzyme 42 Specific Function |
Play a role in maintaining ciliary structure and function |
| Enzyme 42 Pathways |
|
| Enzyme 42 Reactions |
- ATP + AMP = 2 ADP [RN:R00127]
|
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
16553126 |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
Q96M32 |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
KAD7_HUMAN |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>2172 bp
ATGGCTGAAGAAGAGGAAACTGCTGCTCTCACGGAGAAGGTTATCCGGACCCAGAGGGTG
TTTATAAACCTGTTGGATTCCTACAGCAGCGGAAACATCGGGAAGTTTCTATCTAACTGT
GTAGTTGGGGCTTCGCTTGAAGAAATTACAGAGGAAGAGGAAGAGGAAGATGAAAATAAG
TCAGCTATGCTGGAAGCTTCCTCAACCAAAGTGAAGGAAGGCACATTCCAGATTGTGGGC
ACGCTGTCCAAGCCTGACAGCCCGCGGCCTGACTTTGCGGTGGAGACGTACTCTGCCATC
TCTCAAGAAGACCTTCTCATGCGCCTGCTGGAGTGTGATGTTATTATTTATAACATCACT
GAGAGCTCACAGCAAATGGAGGAAGCCATCTGGGCAGTCTCTGCACTCAGTGAAGAAGTC
AGCCACTTTGAAAAGCGAAAGCTATTTATTTTACTGTCGACGGTGATGACTTGGGCGCGC
TCCAAAGCCCTGGACCCCGAGGATTCTGAGGTTCCATTCACTGAAGAAGATTATCGAAGA
AGAAAGTCTCATCCTAATTTTCTGGACCACATAAATGCTGAAAAAATGGTTCTCAAATTT
GGAAAAAAGGCCAGAAAATTTGCAGCATACGTAGTTGCTGCTGGACTCCAGTATGGAGCG
GAAGGAGGCATGTTACACACATTTTTTAAGATGGCTTGGTTGGGCGAGATTCCTGCATTA
CCAGTTTTTGGCGATGGAACAAATGTAATTCCAACAATCCATGTTCTTGATCTAGCAGGA
GTGATACAAAACGTCATAGATCACGTGCCAAAGCTTCACTACCTGGTTGCTGTGGATGAG
TCTGTTCATACCCTGGAAGACATAGTCAAGTGTATCAGTAAAAATACTGGCCCTGGGAAA
ATCCAGAAAATACCCAGAGAAAATGCATACCTAACCAAGGACTTAACGCAAGATTGTCTT
GACCATTTACTGGTCAACTTAAGAATGGAAGCGCTCTTTGTGAAGGAGAATTTTAATATT
CGATGGGCTGCCCAAACAGGATTTGTGGAAAATATCAACACTATCCTCAAGGAGTACAAG
CAAAGCAGAGGATTGATGCCAATCAAGATCTGCATTCTTGGTCCCCCTGCTGTGGGAAAA
TCCAGTATTGCTAAAGAATTGGCCAAGTACTACAAACTGCATCACATCCAACTGAAGGAT
GTCATTTCTGAAGCCATAGCAAAACTGGGGGCGATTGTTGCCCCTAACGATGTAGGGGAA
GGAGAAGAAGAAGTCGAAGAGGAAGAGGAGGAGGAGAATGTGGAAGATGCACAGGAGCTC
CTAGATGGCATCAAGGAGAGCATGGAGCAGAATGCAGGTCAACTAGACGATCAATATATA
ATTAGATTTATGAAAGAAAAGCTAAAATCAATGCCTTGCAGGAATCAAGGTTATATTTTG
GATGGATTCCCAAAGACCTATGATCAAGCAAAAGACCTGTTCAATCAGGAAGATGAGGAG
GAGGAAGATGATGTCAGAGGCAGAATGTTTCCCTTTGATAAATTAATTATACCTGAATTC
GTTTGTGCACTGGATGCTTCGGATGAGTTTCTGAAGGAGCGTGTGATAAACCTTCCTGAG
AGCATCGTGGCGGGGACCCACTACAGCCAAGACCGATTCCTCCGGGCTCTGAGCAACTAC
CGGGACATCAATATCGACGATGAGACTGTCTTCAACTATTTTGATGAACTTGAAATTCAC
CCGATACATATTGATGTAGGAAAACTTGAAGATGCTCAGAATAGACTTGCTATCAAACAG
CTCATCAAAGAGATTGGGGAGCCTCGAAATTATGGTTTAACAGACGAAGAAAAGGCAGAA
GAGGAGCGGAAGGCTGCGGAGGAGCGGCTGGCCAGGGAGGCTGCTGAGGAAGCAGAACGC
GAGCACCAGGAGGCCGTGGAGATGGCAGAGAAGATAGCTCGCTGGGAGGAGTGGAATAAA
CGACTGGAGGAAGTGAAAAGAGAAGAAAGAGAATTACTGGAGGCTCAGTCAATTCCCCTG
AGAAACTATTTAATGACCTATGTGATGCCAACTCTTATTCAGGGCCTGAATGAATGTTGC
AACGTCCGACCCGAAGACCCTGTTGATTTTCTGGCAGAATATCTCTTCAAGAACAATCCT
GAAGCACAGTGA
|
| Enzyme 42 GenBank Gene ID |
AK057426 |
| Enzyme 42 GeneCard ID |
AK7 |
| Enzyme 42 GenAtlas ID |
AK7 |
| Enzyme 42 HGNC ID |
HGNC:20091 |
| Enzyme 42 Chromosome Location |
1 |
| Enzyme 42 Locus |
14q32.2 |
| Enzyme 42 SNPs |
SNPJam Report |
| Enzyme 42 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed ]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
5887 |
| Enzyme 43 Name |
Bis(5'-adenosyl)-triphosphatase |
| Enzyme 43 Synonyms |
- AP3A hydrolase
- AP3Aase
- Diadenosine 5',5'''-P1,P3-triphosphate hydrolase
- Dinucleosidetriphosphatase
- Fragile histidine triad protein
|
| Enzyme 43 Gene Name |
FHIT |
| Enzyme 43 Protein Sequence |
>Bis(5'-adenosyl)-triphosphatase
MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQ
TTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSIYEELQKH
DKEDFPASWRSEEEMAAEAAALRVYFQ
|
| Enzyme 43 Number of Residues |
147 |
| Enzyme 43 Molecular Weight |
16858.1 |
| Enzyme 43 Theoretical pI |
7.09 |
| Enzyme 43 GO Classification |
| Function |
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 43 General Function |
Involved in catalytic activity |
| Enzyme 43 Specific Function |
Cleaves A-5'-PPP-5'A to yield AMP and ADP. Possible tumor suppressor for specific tissues |
| Enzyme 43 Pathways |
|
| Enzyme 43 Reactions |
- P1,P3-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP [RN:R00187]
|
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
261278358 |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
P49789 |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
FHIT_HUMAN |
| Enzyme 43 PDB ID |
1FHI |
| Enzyme 43 PDB File |
Show |
| Enzyme 43 3D Structure |
|
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>444 bp
ATGTCGTTCAGATTTGGCCAACATCTCATCAAGCCCTCTGTAGTGTTTCTCAAAACAGAA
CTGTCCTTCGCTCTTGTGAATAGGAAACCTGTGGTACCAGGACATGTCCTTGTGTGCCCG
CTGCGGCCAGTGGAGCGCTTCCATGACCTGCGTCCTGATGAAGTGGCCGATTTGTTTCAG
ACGACCCAGAGAGTCGGGACAGTGGTGGAAAAACATTTCCATGGGACCTCTCTCACCTTT
TCCATGCAGGATGGCCCCGAAGCCGGACAGACTGTGAAGCACGTTCACGTCCATGTTCTT
CCCAGGAAGGCTGGAGACTTTCACAGGAATGACAGCATCTATGAGGAGCTCCAGAAACAT
GACAAGGAGGACTTTCCTGCCTCTTGGAGATCAGAGGAGGAAATGGCAGCAGAAGCCGCA
GCTCTGCGGGTCTACTTTCAGTGA
|
| Enzyme 43 GenBank Gene ID |
NM_001166243.1 |
| Enzyme 43 GeneCard ID |
FHIT |
| Enzyme 43 GenAtlas ID |
FHIT |
| Enzyme 43 HGNC ID |
HGNC:3701 |
| Enzyme 43 Chromosome Location |
3 |
| Enzyme 43 Locus |
3p14.2 |
| Enzyme 43 SNPs |
SNPJam Report |
| Enzyme 43 General References |
- Ohta M, Inoue H, Cotticelli MG, Kastury K, Baffa R, Palazzo J, Siprashvili Z, Mori M, McCue P, Druck T, Croce CM, Huebner K: The FHIT gene, spanning the chromosome 3p14.2 fragile site and renal carcinoma-associated t(3;8) breakpoint, is abnormal in digestive tract cancers. Cell. 1996 Feb 23;84(4):587-97. [PubMed ]
- Druck T, Hadaczek P, Fu TB, Ohta M, Siprashvili Z, Baffa R, Negrini M, Kastury K, Veronese ML, Rosen D, Rothstein J, McCue P, Cotticelli MG, Inoue H, Croce CM, Huebner K: Structure and expression of the human FHIT gene in normal and tumor cells. Cancer Res. 1997 Feb 1;57(3):504-12. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Barnes LD, Garrison PN, Siprashvili Z, Guranowski A, Robinson AK, Ingram SW, Croce CM, Ohta M, Huebner K: Fhit, a putative tumor suppressor in humans, is a dinucleoside 5',5"'-P1,P3-triphosphate hydrolase. Biochemistry. 1996 Sep 10;35(36):11529-35. [PubMed ]
- Huang K, Arabshahi A, Wei Y, Frey PA: The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit. Biochemistry. 2004 Jun 15;43(23):7637-42. [PubMed ]
- Pekarsky Y, Garrison PN, Palamarchuk A, Zanesi N, Aqeilan RI, Huebner K, Barnes LD, Croce CM: Fhit is a physiological target of the protein kinase Src. Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3775-9. Epub 2004 Mar 8. [PubMed ]
- Lima CD, D'Amico KL, Naday I, Rosenbaum G, Westbrook EM, Hendrickson WA: MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family. Structure. 1997 Jun 15;5(6):763-74. [PubMed ]
- Lima CD, Klein MG, Hendrickson WA: Structure-based analysis of catalysis and substrate definition in the HIT protein family. Science. 1997 Oct 10;278(5336):286-90. [PubMed ]
- Pace HC, Garrison PN, Robinson AK, Barnes LD, Draganescu A, Rosler A, Blackburn GM, Siprashvili Z, Croce CM, Huebner K, Brenner C: Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit. Proc Natl Acad Sci U S A. 1998 May 12;95(10):5484-9. [PubMed ]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
5911 |
| Enzyme 44 Name |
ADP-ribose pyrophosphatase, mitochondrial |
| Enzyme 44 Synonyms |
- ADP-ribose diphosphatase
- ADP-ribose phosphohydrolase
- Adenosine diphosphoribose pyrophosphatase
- ADPR-PPase
- Nucleoside diphosphate-linked moiety X motif 9
- Nudix motif 9
|
| Enzyme 44 Gene Name |
NUDT9 |
| Enzyme 44 Protein Sequence |
>ADP-ribose pyrophosphatase, mitochondrial
MAGRLLGKALAAVSLSLALASVTIRSSRCRGIQAFRNSFSSSWFHLNTNVMSGSNGSKEN
SHNKARTSPYPGSKVERSQVPNEKVGWLVEWQDYKPVEYTAVSVLAGPRWADPQISESNF
SPKFNEKDGHVERKSKNGLYEIENGRPRNPAGRTGLVGRGLLGRWGPNHAADPIITRWKR
DSSGNKIMHPVSGKHILQFVAIKRKDCGEWAIPGGMVDPGEKISATLKREFGEEALNSLQ
KTSAEKREIEEKLHKLFSQDHLVIYKGYVDDPRNTDNAWMETEAVNYHDETGEIMDNLML
EAGDDAGKVKWVDINDKLKLYASHSQFIKLVAEKRDAHWSEDSEADCHAL
|
| Enzyme 44 Number of Residues |
350 |
| Enzyme 44 Molecular Weight |
39124.7 |
| Enzyme 44 Theoretical pI |
8.45 |
| Enzyme 44 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 44 General Function |
Involved in hydrolase activity |
| Enzyme 44 Specific Function |
Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'- phosphate |
| Enzyme 44 Pathways |
|
| Enzyme 44 Reactions |
- ADP-ribose + H2O = AMP + D-ribose 5-phosphate [RN:R01054]
|
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
14160858 |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
Q9BW91 |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
NUDT9_HUMAN |
| Enzyme 44 PDB ID |
1QVJ |
| Enzyme 44 PDB File |
Show |
| Enzyme 44 3D Structure |
|
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>1053 bp
ATGGCGGGACGCCTCCTGGGAAAGGCTTTAGCCGCGGTGTCTCTCTCTCTGGCCTTGGCC
TCTGTGACTATCAGGTCCTCGCGCTGCCGCGGCATCCAGGCGTTCAGAAACTCGTTTTCA
TCTTCTTGGTTTCATCTTAATACCAACGTCATGTCTGGTTCTAATGGTTCCAAAGAAAAT
TCTCACAATAAGGCTCGGACGTCTCCTTACCCAGGTTCAAAAGTTGAACGAAGCCAGGTT
CCTAATGAGAAAGTGGGCTGGCTTGTTGAGTGGCAAGACTATAAGCCTGTGGAATACACT
GCAGTCTCTGTCTTGGCTGGACCCAGGTGGGCAGATCCTCAGATCAGTGAAAGTAATTTT
TCTCCCAAGTTTAACGAAAAGGATGGGCATGTTGAGAGAAAGAGCAAGAATGGCCTGTAT
GAGATTGAAAATGGAAGACCGAGAAATCCTGCAGGACGGACTGGACTGGTGGGCCGGGGG
CTTTTGGGGCGATGGGGCCCAAATCACGCTGCAGATCCCATTATAACCAGATGGAAAAGG
GATAGCAGTGGAAATAAAATCATGCATCCTGTTTCTGGGAAGCATATCTTACAATTTGTT
GCAATAAAAAGGAAAGACTGTGGAGAATGGGCAATCCCAGGGGGGATGGTGGATCCAGGA
GAGAAGATTAGTGCCACACTGAAAAGAGAATTTGGTGAGGAAGCTCTCAACTCCTTACAG
AAAACCAGTGCTGAGAAGAGAGAAATAGAGGAAAAGTTGCACAAACTCTTCAGCCAAGAC
CACCTAGTGATATATAAGGGATATGTTGATGATCCTCGAAACACTGATAATGCATGGATG
GAGACAGAAGCTGTGAACTACCATGACGAAACAGGTGAGATAATGGATAATCTTATGCTA
GAAGCTGGAGATGATGCTGGAAAAGTGAAATGGGTGGACATCAATGATAAACTGAAGCTT
TATGCCAGTCACTCTCAATTCATCAAACTTGTGGCTGAGAAACGAGATGCACACTGGAGC
GAGGACTCTGAAGCTGACTGCCATGCGTTGTAG
|
| Enzyme 44 GenBank Gene ID |
AY026252 |
| Enzyme 44 GeneCard ID |
NUDT9 |
| Enzyme 44 GenAtlas ID |
NUDT9 |
| Enzyme 44 HGNC ID |
HGNC:8056 |
| Enzyme 44 Chromosome Location |
4 |
| Enzyme 44 Locus |
4q22.1 |
| Enzyme 44 SNPs |
SNPJam Report |
| Enzyme 44 General References |
- Perraud AL, Fleig A, Dunn CA, Bagley LA, Launay P, Schmitz C, Stokes AJ, Zhu Q, Bessman MJ, Penner R, Kinet JP, Scharenberg AM: ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology. Nature. 2001 May 31;411(6837):595-9. [PubMed ]
- Lin S, Gasmi L, Xie Y, Ying K, Gu S, Wang Z, Jin H, Chao Y, Wu C, Zhou Z, Tang R, Mao Y, McLennan AG: Cloning, expression and characterisation of a human Nudix hydrolase specific for adenosine 5'-diphosphoribose (ADP-ribose). Biochim Biophys Acta. 2002 Jan 31;1594(1):127-35. [PubMed ]
- Perraud AL, Shen B, Dunn CA, Rippe K, Smith MK, Bessman MJ, Stoddard BL, Scharenberg AM: NUDT9, a member of the Nudix hydrolase family, is an evolutionarily conserved mitochondrial ADP-ribose pyrophosphatase. J Biol Chem. 2003 Jan 17;278(3):1794-801. Epub 2002 Nov 8. [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 ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Zhang HT, Yan ZQ, Hu XB, Yang SL, Gong Y: Interaction of C17orf25 with ADP-ribose pyrophosphatase NUDT9 detected via yeast two-hybrid method. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003 Aug;35(8):747-51. [PubMed ]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Shen BW, Perraud AL, Scharenberg A, Stoddard BL: The crystal structure and mutational analysis of human NUDT9. J Mol Biol. 2003 Sep 12;332(2):385-98. [PubMed ]
|
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
5912 |
| Enzyme 45 Name |
Adenosine kinase |
| Enzyme 45 Synonyms |
- AK
- Adenosine 5'-phosphotransferase
|
| Enzyme 45 Gene Name |
ADK |
| Enzyme 45 Protein Sequence |
>Adenosine kinase
MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAED
KHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKA
AEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKAR
VCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGN
ETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFA
VLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPD
FH
|
| Enzyme 45 Number of Residues |
362 |
| Enzyme 45 Molecular Weight |
40545.1 |
| Enzyme 45 Theoretical pI |
6.67 |
| Enzyme 45 GO Classification |
| Function |
- adenosine kinase activity
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- metabolic process
- purine ribonucleoside salvage
- purine salvage
|
| Component |
| — |
|
| Enzyme 45 General Function |
Involved in adenosine kinase activity |
| Enzyme 45 Specific Function |
ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides |
| Enzyme 45 Pathways |
|
| Enzyme 45 Reactions |
- ATP + adenosine = ADP + AMP [RN:R00185]
|
| Enzyme 45 Pfam Domain Function |
|
| Enzyme 45 Signals |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
32484975 |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
P55263 |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
ADK_HUMAN |
| Enzyme 45 PDB ID |
1BX4 |
| Enzyme 45 PDB File |
Show |
| Enzyme 45 3D Structure |
|
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>1089 bp
ATGGCAGCTGCTGAGGAGGAGCCGAAGCCCAAAAAGCTGAAGGTGGAGGCGCCGCAAGCG
CTGAGAGAAAATATTCTCTTTGGAATGGGAAATCCTCTGCTTGACATCTCTGCTGTAGTG
GACAAAGATTTCCTTGATAAGTATTCTCTGAAACCAAATGACCAAATCTTGGCTGAAGAC
AAACACAAGGAACTGTTTGATGAACTTGTGAAAAAATTCAAAGTCGAATATCATGCTGGT
GGCTCTACCCAGAATTCAATTAAAGTGGCTCAGTGGATGATTCAACAGCCACACAAAGCA
GCAACATTTTTTGGATGCATTGGGATAGATAAATTTGGGGAGATCCTGAAGAGAAAAGCT
GCTGAAGCCCATGTGGATGCTCATTACTACGAGCAGAATGAGCAGCCAACAGGAACTTGT
GCTGCATGCATCACTGGTGACAACAGGTCCCTCATAGCTAATCTTGCTGCTGCCAATTGT
TATAAAAAGGAAAAACATCTTGATCTGGAGAAAAACTGGATGTTGGTAGAAAAAGCAAGA
GTTTGTTATATAGCAGGCTTTTTTCTTACAGTTTCCCCAGAGTCAGTATTAAAGGTGGCT
CACCATGCTTCTGAAAACAACAGGATTTTCACTTTGAATCTATCTGCACCGTTTATTAGC
CAGTTCTACAAGGAATCATTGATGAAAGTTATGCCTTATGTTGATATACTTTTTGGAAAT
GAGACAGAAGCTGCCACTTTTGCTAGAGAGCAAGGCTTTGAGACTAAAGACATTAAAGAG
ATAGCCAAAAAGACACAAGCCCTGCCAAAGATGAACTCAAAGAGGCAGCGAATCGTGATC
TTCACCCAAGGGAGAGATGACACTATAATGGCTACAGAAAGTGAAGTCACTGCTTTTGCT
GTCTTGGATCAAGACCAGAAAGAAATTATTGATACCAATGGAGCTGGAGATGCATTTGTT
GGAGGTTTTCTGTCTCAACTGGTCTCTGACAAGCCTCTGACTGAATGTATCCGTGCTGGC
CACTATGCAGCAAGCATCATAATTAGACGGACTGGCTGCACCTTTCCTGAGAAGCCAGAC
TTCCACTGA
|
| Enzyme 45 GenBank Gene ID |
NM_006721 |
| Enzyme 45 GeneCard ID |
ADK |
| Enzyme 45 GenAtlas ID |
ADK |
| Enzyme 45 HGNC ID |
HGNC:257 |
| Enzyme 45 Chromosome Location |
1 |
| Enzyme 45 Locus |
10q22|10q11-q24 |
| Enzyme 45 SNPs |
SNPJam Report |
| Enzyme 45 General References |
- Spychala J, Datta NS, Takabayashi K, Datta M, Fox IH, Gribbin T, Mitchell BS: Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and fructokinases. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1232-7. [PubMed ]
- Singh B, Hao W, Wu Z, Eigl B, Gupta RS: Cloning and characterization of cDNA for adenosine kinase from mammalian (Chinese hamster, mouse, human and rat) species. High frequency mutants of Chinese hamster ovary cells involve structural alterations in the gene. Eur J Biochem. 1996 Oct 15;241(2):564-71. [PubMed ]
- McNally T, Helfrich RJ, Cowart M, Dorwin SA, Meuth JL, Idler KB, Klute KA, Simmer RL, Kowaluk EA, Halbert DN: Cloning and expression of the adenosine kinase gene from rat and human tissues. Biochem Biophys Res Commun. 1997 Feb 24;231(3):645-50. [PubMed ]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Mathews II, Erion MD, Ealick SE: Structure of human adenosine kinase at 1.5 A resolution. Biochemistry. 1998 Nov 10;37(45):15607-20. [PubMed ]
- Maguire PB, Wynne KJ, Harney DF, O'Donoghue NM, Stephens G, Fitzgerald DJ: Identification of the phosphotyrosine proteome from thrombin activated platelets. Proteomics. 2002 Jun;2(6):642-8. [PubMed ]
|
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
5924 |
| Enzyme 46 Name |
Adenylate kinase isoenzyme 5 |
| Enzyme 46 Synonyms |
- AK 5
- ATP-AMP transphosphorylase 5
|
| Enzyme 46 Gene Name |
AK5 |
| Enzyme 46 Protein Sequence |
>Adenylate kinase isoenzyme 5
MNTNDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKELGGCDKVKWDTFV
SQEKKTLPPLNGGQSRRSFLRNVMPENSNFPYRRYDRLPPIHQFSIESDTDLSETAELIE
EYEVFDPTRPRPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKW
SLIAKIITTGELAPQETTITEIKQKLMQIPDEEGIVIDGFPRDVAQALSFEDQICTPDLV
VFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDA
DRDEDEVFYDISMAVDNKLFPNKEAAAGSSDLDPSMILDTGEIIDTGSDYEDQGDDQLNV
FGEDTMGGFMEDLRKCKIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESE
RSKLIRDIMERGDLVPSGIVLELLKEAMVASLGDTRGFLIDGYPREVKQGEEFGRRIGDP
QLVICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHK
INAEGTPEDVFLQLCTAIDSIF
|
| Enzyme 46 Number of Residues |
562 |
| Enzyme 46 Molecular Weight |
63332.4 |
| Enzyme 46 Theoretical pI |
4.69 |
| Enzyme 46 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- adenylate kinase activity
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- ATP metabolic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate metabolic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 46 General Function |
Involved in ATP binding |
| Enzyme 46 Specific Function |
Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP |
| Enzyme 46 Pathways |
|
| Enzyme 46 Reactions |
- ATP + AMP = 2 ADP [RN:R00127]
|
| Enzyme 46 Pfam Domain Function |
|
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
28144897 |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
Q9Y6K8 |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
KAD5_HUMAN |
| Enzyme 46 PDB ID |
Not Available |
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>1689 bp
ATGAACACCAACGATGCCAAGGAGTATCTGGCCCGGAGGGAAATCCCTCAGCTTTTTGAG
AGCCTTTTGAATGGACTGATGTGTTCTAAGCCCGAAGATCCAGTAGAATACTTGGAAAGT
TGTTTACAAAAAGTAAAGGAACTGGGTGGCTGTGACAAGGTGAAATGGGATACATTTGTA
AGCCAGGAAAAGAAGACCTTACCTCCACTAAATGGAGGACAGTCACGGAGATCCTTTCTA
AGAAATGTAATGCCTGAAAACTCAAACTTTCCATATCGGCGGTATGACCGGCTCCCTCCA
ATCCATCAATTCTCCATAGAAAGTGACACGGATCTCTCTGAGACTGCAGAGTTGATTGAG
GAGTATGAGGTTTTTGATCCTACCAGACCTCGACCAAAAATCATTCTTGTTATAGGTGGT
CCAGGAAGTGGAAAGGGTACTCAGAGTTTGAAAATTGCAGAACGATATGGATTCCAATAC
ATTTCTGTGGGAGAATTATTAAGAAAGAAGATCCACAGTACCAGCAGCAATAGGAAATGG
AGTCTTATTGCCAAGATAATTACAACTGGAGAATTGGCCCCACAGGAAACAACAATTACA
GAGATAAAACAAAAATTGATGCAAATACCTGATGAAGAGGGCATTGTTATTGATGGATTT
CCAAGAGATGTTGCCCAGGCTCTATCTTTTGAGGACCAAATCTGTACCCCCGATTTGGTG
GTATTCCTGGCTTGTGCTAATCAGAGACTCAAAGAAAGATTACTGAAGCGTGCAGAACAG
CAGGGCCGACCAGACGACAATGTAAAAGCTACCCAAAGGAGACTAATGAACTTCAAGCAG
AATGCTGCTCCATTGGTTAAATACTTCCAGGAAAAGGGGCTCATCATGACATTTGATGCC
GACCGCGATGAGGATGAGGTGTTCTATGACATCAGCATGGCAGTTGACAACAAGTTATTT
CCAAACAAAGAGGCTGCAGCAGGTTCAAGTGACCTTGATCCTTCGATGATATTGGACACT
GGAGAGATCATTGATACAGGATCTGATTATGAAGATCAGGGTGATGACCAGTTAAATGTA
TTTGGAGAGGACACTATGGGAGGTTTCATGGAAGATTTGAGAAAGTGTAAAATTATTTTC
ATAATTGGTGGTCCTGGCTCTGGCAAAGGCACACAGTGTGAAAAGCTGGTGGAAAAATAT
GGATTTACACATCTCTCAACTGGCGAGCTCCTGCGTGAGGAACTGGCATCAGAATCTGAA
AGAAGCAAATTGATCAGAGACATTATGGAACGTGGAGACCTGGTGCCCTCAGGCATCGTT
TTGGAGCTCCTGAAGGAGGCCATGGTGGCCAGCCTCGGGGACACCAGGGGCTTCCTGATT
GACGGCTATCCTCGGGAGGTGAAGCAAGGGGAAGAGTTCGGACGCAGGATTGGAGACCCA
CAGTTGGTGATCTGTATGGACTGCTCGGCAGACACCATGACCAACCGCCTTCTCCAAAGG
AGCCGGAGCAGCCTGCCTGTGGACGACACCACCAAGACCATCGCCAAGCGCCTAGAAGCC
TACTACCGAGCGTCCATCCCCGTGATCGCCTACTACGAGACAAAAACACAGCTACACAAG
ATAAATGCAGAGGGAACACCAGAGGACGTTTTTCTTCAACTCTGCACAGCTATTGACTCT
ATTTTCTGA
|
| Enzyme 46 GenBank Gene ID |
NM_174858.1 |
| Enzyme 46 GeneCard ID |
AK5 |
| Enzyme 46 GenAtlas ID |
AK5 |
| Enzyme 46 HGNC ID |
HGNC:365 |
| Enzyme 46 Chromosome Location |
1 |
| Enzyme 46 Locus |
1p31 |
| Enzyme 46 SNPs |
SNPJam Report |
| Enzyme 46 General References |
- Van Rompay AR, Johansson M, Karlsson A: Identification of a novel human adenylate kinase. cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein. Eur J Biochem. 1999 Apr;261(2):509-17. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
5949 |
| Enzyme 47 Name |
CTP synthase 1 |
| Enzyme 47 Synonyms |
- CTP synthetase 1
- UTP--ammonia ligase 1
|
| Enzyme 47 Gene Name |
CTPS |
| Enzyme 47 Protein Sequence |
>CTP synthase 1
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
|
| Enzyme 47 Number of Residues |
591 |
| Enzyme 47 Molecular Weight |
66689.9 |
| Enzyme 47 Theoretical pI |
6.42 |
| Enzyme 47 GO Classification |
| Function |
- CTP synthase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
|
| 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
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
|
| Component |
| — |
|
| Enzyme 47 General Function |
Involved in CTP synthase activity |
| Enzyme 47 Specific Function |
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen |
| Enzyme 47 Pathways |
|
| Enzyme 47 Reactions |
- ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571]
|
| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
|
| Enzyme 47 Transmembrane Regions |
|
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
30293 |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
P17812 |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
PYRG1_HUMAN |
| Enzyme 47 PDB ID |
Not Available |
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 Gene Sequence |
>1776 bp
ATGAAGTACATTCTGGTTACTGGTGGTGTTATATCAGGAATTGGAAAAGGAATCATTGCC
AGCAGTGTGGGCACAATACTCAAGTCATGTGGTTTACATGTAACTTCAATCAAAATTGAC
CCCTACATTAACATTGATGCAGGAACATTCTCTCCTTATGAGCATGGTGAGGTTTTTGTG
CTGGATGATGGTGGGGAAGTAGACCTTGACCTGGGTAACTATGAGCGGTTCCTTGACATC
CGCCTCACCAAGGACAATAATCTGACCACTGGAAAGATATACCAGTATGTCATTAACAAG
GAACGGAAAGGAGATTACTTGGGGAAAACTGTCCAAGTTGTCCCTCATATCACAGATGCA
ATCCAGGAGTGGGTGATGAGACAGGCGTTAATACCTGTAGATGAAGATGGCCTGGAACCT
CAAGTGTGTGTTATTGAGCTTGGTGGAACCGTGGGGGACATAGAAAGCATGCCCTTTATT
GAGGCCTTCCGTCAGTTCCAATTCAAGGTCAAAAGAGAGAACTTTTGTAACATCCACGTC
AGTCTAGTTCCCCAGCCAAGTTCAACAGGGGAACAGAAGACTAAACCTACCCAGAATAGT
GTTCGGGAACTTAGAGGACTTGGGCTTTCCCCAGATCTGGTTGTATGCAGGTGCTCAAAT
CCACTTGACACATCAGTGAAGGAGAAAATATCAATGTTCTGCCATGTTGAGCCTGAACAA
GTGATCTGTGTCCACGATGTCTCATCCATCTACCGAGTCCCCTTGTTGTTAGAGGAGCAA
GGGGTTGTAGATTATTTTCTTCGAAGACTTGACCTTCCTATTGAGAGGCAGCCAAGAAAA
ATGCTGATGAAATGGAAAGAGATGGCTGACAGATATGATCGCTTGCTGGAGACCTGCTCT
ATTGCCCTTGTGGCGAAATACACCGAGTTCTCAGACTCCTATGCCTCTGTCATTAAGGCT
CTGGAGCATTCTGCACTGGCCATCAACCACAAATTGGAAATCAAGTACATAGATTCTGCG
GACTTGGAGCCCATCACCTCGCAAGAAGAGCCCGTGCGCTACCACGAAGCTTGGCAGAAG
CTCTGTAGTGCTCATGGAGTGCTGGTTCCAGGAGGATTTGGTGTTCGAGGAACAGAAGGA
AAAATCCAAGCAATTGCCTGGGCTCGGAATCAGAAAAAGCCTTTTTTGGGCGTGTGCTTA
GGGATGCAGTTGGCAGTGGTTGAATTCTCAAGAAACGTGCTGGGATGGCAAGATGCCAAT
TCTACAGAGTTTGACCCTACGACCAGTCATCCCGTGGTCGTAGACATGCCAGAACACAAC
CCAGGGCAGATGGGCGGAACCATGAGGCTGGGCAAGAGGAGAACCCTGTTCCAGACCAAG
AACTCAGTCATGAGGAAACTCTATGGAGACGCAGACTACTTGGAAGAGAGGCACCGCCAC
CGATTTGAGGTGAATCCAGTCTGGAAAAAGTGTTTGGAAGAACAAGGCTTGAAGTTTGTT
GGCCAAGATGTTGAAGGAGAGAGAATGGAAATTGTGGAGTTAGAAGATCATCCCTTTTTT
GTTGGGGTTCAGTACCACCCTGAGTTCCTGTCCAGGCCTATCAAGCCCTCCCCACCATAC
TTTGGCCTCCTCCTGGCCTCTGTGGGGCGGCTCTCACATTACCTCCAGAAAGGCTGCAGG
CTCTCACCCAGGGACACCTATAGTGACAGGAGTGGAAGCAGCTCCCCTGACTCTGAAATC
ACCGAACTGAAGTTTCCATCAATAAATCATGACTGA
|
| Enzyme 47 GenBank Gene ID |
X52142 |
| Enzyme 47 GeneCard ID |
CTPS |
| Enzyme 47 GenAtlas ID |
CTPS |
| Enzyme 47 HGNC ID |
HGNC:2519 |
| Enzyme 47 Chromosome Location |
1 |
| Enzyme 47 Locus |
1p34.1 |
| Enzyme 47 SNPs |
SNPJam Report |
| Enzyme 47 General References |
- Yamauchi M, Yamauchi N, Meuth M: Molecular cloning of the human CTP synthetase gene by functional complementation with purified human metaphase chromosomes. EMBO J. 1990 Jul;9(7):2095-9. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
- Han GS, Sreenivas A, Choi MG, Chang YF, Martin SS, Baldwin EP, Carman GM: Expression of Human CTP synthetase in Saccharomyces cerevisiae reveals phosphorylation by protein kinase A. J Biol Chem. 2005 Nov 18;280(46):38328-36. Epub 2005 Sep 22. [PubMed ]
- Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed ]
- Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed ]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 47 Metabolite References |
Not Available |
|
Enzyme 48
[top]
|
| Enzyme 48 ID |
5993 |
| Enzyme 48 Name |
Creatine kinase S-type, mitochondrial |
| Enzyme 48 Synonyms |
- Basic-type mitochondrial creatine kinase
- Mib-CK
- Sarcomeric mitochondrial creatine kinase
- S-MtCK
|
| Enzyme 48 Gene Name |
CKMT2 |
| Enzyme 48 Protein Sequence |
>Creatine kinase S-type, mitochondrial
MASIFSKLLTGRNASLLFATMGTSVLTTGYLLNRQKVCAEVREQPRLFPPSADYPDLRKH
NNCMAECLTPAIYAKLRNKVTPNGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFA
DLFDPVIKLRHNGYDPRVMKHTTDLDASKITQGQFDEHYVLSSRVRTGRSIRGLSLPPAC
TRAERREVENVAITALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFDKPVSPLLTCAG
MARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQE
RGWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLRLQKRGTGGVD
TAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCEKKLERGQDIKVPPPLPQFGKK
|
| Enzyme 48 Number of Residues |
419 |
| Enzyme 48 Molecular Weight |
47504.1 |
| Enzyme 48 Theoretical pI |
8.31 |
| Enzyme 48 GO Classification |
| Function |
- catalytic activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 48 General Function |
Involved in kinase activity |
| Enzyme 48 Specific Function |
Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa |
| Enzyme 48 Pathways |
- Arginine and Proline Metabolism (map00330 )
|
| Enzyme 48 Reactions |
- ATP + creatine = ADP + phosphocreatine [RN:R01881]
|
| Enzyme 48 Pfam Domain Function |
|
| Enzyme 48 Signals |
|
| Enzyme 48 Transmembrane Regions |
|
| Enzyme 48 Essentiality |
Not Available |
| Enzyme 48 GenBank ID Protein |
20810521 |
| Enzyme 48 UniProtKB/Swiss-Prot ID |
P17540 |
| Enzyme 48 UniProtKB/Swiss-Prot Entry Name |
KCRS_HUMAN |
| Enzyme 48 PDB ID |
1CRK |
| Enzyme 48 PDB File |
Show |
| Enzyme 48 3D Structure |
|
| Enzyme 48 Cellular Location |
Not Available |
| Enzyme 48 Gene Sequence |
>1260 bp
ATGGCCAGTATCTTTTCTAAGTTGCTAACTGGCCGCAATGCTTCTCTGCTGTTTGCTACC
ATGGGCACCAGTGTCCTGACCACCGGGTACCTGCTGAACCGGCAGAAAGTGTGTGCCGAG
GTCCGGGAGCAGCCTAGGCTATTTCCTCCAAGCGCAGACTACCCAGACCTGCGCAAGCAC
AACAACTGCATGGCCGAGTGCCTCACCCCCGCCATTTATGCCAAGCTTCGCAACAAGGTG
ACACCCAACGGCTACACGCTGGACCAGTGCATCCAGACTGGAGTGGACAACCCTGGCCAC
CCCTTCATAAAGACTGTGGGCATGGTGGCTGGTGACGAGGAGTCCTATGAGGTGTTTGCT
GACCTTTTTGACCCCGTCATCAAACTAAGACACAACGGCTATGACCCCAGGGTGATGAAG
CACACAACGGATCTGGATGCATCAAAGATCACCCAAGGGCAGTTCGACGAGCATTACGTG
CTGTCTTCTCGGGTGCGCACTGGCCGCAGCATCCGTGGGCTGAGCCTGCCTCCAGCCTGC
ACCCGGGCCGAGCGAAGGGAGGTAGAGAACGTGGCCATCACTGCCCTGGAGGGCCTCAAG
GGGGACCTGGCTGGCCGCTACTACAAGCTGTCCGAGATGACGGAGCAGGACCAGCAGCGG
CTCATCGATGACCACTTTCTGTTTGATAAGCCAGTGTCCCCTTTATTAACATGTGCTGGG
ATGGCCCGTGACTGGCCAGATGCCAGGGGAATCTGGCATAATTATGATAAGACATTTCTC
ATCTGGATAAATGAGGAGGATCACACCAGGGTAATCTCAATGGAAAAAGGAGGCAATATG
AAACGAGTATTTGAGCGATTCTGTCGTGGACTAAAAGAAGTAGAACGGTTAATCCAAGAA
CGAGGCTGGGAGTTCATGTGGAATGAGCGCCTAGGATACATTTTGACCTGTCCTTCGAAC
CTTGGAACAGGACTACGAGCTGGTGTCCACGTTAGGATCCCAAAGCTCAGCAAGGACCCA
CGCTTTTCTAAGATCCTGGAAAACCTAAGACTCCAGAAGCGTGGCACAGGTGGTGTGGAC
ACTGCCGCGGTCGCAGATGTGTACGACATTTCCAACATAGATAGAATTGGTCGATCAGAG
GTTGAGCTTGTTCAGATAGTCATCGATGGAGTCAATTACCTGGTGGATTGTGAAAAGAAG
TTGGAGAGAGGCCAAGATATTAAGGTGCCACCCCCTCTGCCTCAGTTTGGCAAAAAGTAA
|
| Enzyme 48 GenBank Gene ID |
BC029140 |
| Enzyme 48 GeneCard ID |
CKMT2 |
| Enzyme 48 GenAtlas ID |
CKMT2 |
| Enzyme 48 HGNC ID |
HGNC:1996 |
| Enzyme 48 Chromosome Location |
5 |
| Enzyme 48 Locus |
5q13.3 |
| Enzyme 48 SNPs |
SNPJam Report |
| Enzyme 48 General References |
- Haas RC, Strauss AW: Separate nuclear genes encode sarcomere-specific and ubiquitous human mitochondrial creatine kinase isoenzymes. J Biol Chem. 1990 Apr 25;265(12):6921-7. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Haas RC, Korenfeld C, Zhang ZF, Perryman B, Roman D, Strauss AW: Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase. J Biol Chem. 1989 Feb 15;264(5):2890-7. [PubMed ]
|
| Enzyme 48 Metabolite References |
Not Available |
|
Enzyme 49
[top]
|
| Enzyme 49 ID |
5994 |
| Enzyme 49 Name |
Creatine kinase B-type |
| Enzyme 49 Synonyms |
- B-CK
- Creatine kinase B chain
|
| Enzyme 49 Gene Name |
CKB |
| Enzyme 49 Protein Sequence |
>Creatine kinase B-type
MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTG
VDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDD
LDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMT
EAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISM
QKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLP
NLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLL
IEMEQRLEQGQAIDDLMPAQK
|
| Enzyme 49 Number of Residues |
381 |
| Enzyme 49 Molecular Weight |
42643.9 |
| Enzyme 49 Theoretical pI |
5.30 |
| Enzyme 49 GO Classification |
| Function |
- catalytic activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 49 General Function |
Involved in kinase activity |
| Enzyme 49 Specific Function |
Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa |
| Enzyme 49 Pathways |
- Arginine and Proline Metabolism (map00330 )
|
| Enzyme 49 Reactions |
- ATP + creatine = ADP + phosphocreatine [RN:R01881]
|
| Enzyme 49 Pfam Domain Function |
|
| Enzyme 49 Signals |
|
| Enzyme 49 Transmembrane Regions |
|
| Enzyme 49 Essentiality |
Not Available |
| Enzyme 49 GenBank ID Protein |
180572 |
| Enzyme 49 UniProtKB/Swiss-Prot ID |
P12277 |
| Enzyme 49 UniProtKB/Swiss-Prot Entry Name |
KCRB_HUMAN |
| Enzyme 49 PDB ID |
1G0W |
| Enzyme 49 PDB File |
Show |
| Enzyme 49 3D Structure |
|
| Enzyme 49 Cellular Location |
Not Available |
| Enzyme 49 Gene Sequence |
>1146 bp
ATGCCCTTCTCCAACAGCCACAACGCACTGAAGCTGCGCTTCCCGGCCGAGGACGAGTTC
CCCGACCTGAGCGCCCACAACAACCACATGGCCAAGGTGCTGACCCCCGAGCTGTACGCG
GACGTGCGCGCCAAGAGCACGCCGAGCGGCTTCACGCTGGACGACGTCATCCAGACAGGC
GTGGACAACCCGGGCCACCCGTACATCATGACCGTGGGCTGCGTGGCGGGCGACGAGGAG
TCCTACGAAGTGTTCAAGGATCTCTTCGACCCCATCATCGAGGACCGGCACCGGCGCTAC
AAGCCCAGCGATGACGACAAGACCGACCTCAACCCCGACAACCTGCAGGGCGGCGACGAC
CTGGACCCCAACTACGTGCTGAGCTCGCGGGTGGCCACGGGCCGCAGCATCCGTGGCTTC
TGCCTCCCCCCGCACTGCAGCCGCGGGGAGCGCCGAGCCATCGAGAAGCTCGCGGTGGAA
GCCCTGTCCAGCCTGGACGGCGACCTGGCGGGCCGATACTACGCGCTCAAGAGCATGACG
GAGGCGGAGCAGCAGCAGCTCATCGACGACCACTTCCTCTTCGACAAGCCCGTGTCGCCC
CTGCTGCTGGCCTCGGGCATGGCCCGCGACTGGCCCGACGCCGCGCGTATCTGGCACAAT
GACAATAAGACCTTCCTGGTGTGGGTCAACGAGGAGGACCACCTGCGGGTCATCTCCATG
CAGAAGGGGGGCAACATGAAGGAGGTGTTCACCCGCTTCTGCACCGGCCTCACCCAGATT
GAAACTCTCTTCAAGTCTAAGGACTATGAGTTCATGTGGAACCCTCACCTGGGCTACATC
CTCACCTGCCCATCCAACCTGGGCACCGGGCTGCGGGCAGGTGTCGATATCAAGCTGCCC
AACCTGGGCAAGCATGAGAAGTTCTCGGAGGTGCTTAAGCGGCTGCGACTTCAGAAGCGA
GGCACAGGCGGTGTGGACACGGCTGCGGTGGGCGGGGTCTTCGACGTCTCCAACGCTGAC
CGCCTGGGCTTCTCAGAGGTGGAGCTGGTGCAGATGGTGGTGGACGGAGTGAAGCTGCTC
ATCGAGATGGAACAGCGGCTGGAGCAGGGCCAGGCCATCGACGACCTCATGCCTGCCCAG
AAATGA
|
| Enzyme 49 GenBank Gene ID |
M16451 |
| Enzyme 49 GeneCard ID |
CKB |
| Enzyme 49 GenAtlas ID |
CKB |
| Enzyme 49 HGNC ID |
HGNC:1991 |
| Enzyme 49 Chromosome Location |
1 |
| Enzyme 49 Locus |
14q32 |
| Enzyme 49 SNPs |
SNPJam Report |
| Enzyme 49 General References |
- Villarreal-Levy G, Ma TS, Kerner SA, Roberts R, Perryman MB: Human creatine kinase: isolation and sequence analysis of cDNA clones for the B subunit, development of subunit specific probes and determination of gene copy number. Biochem Biophys Res Commun. 1987 May 14;144(3):1116-27. [PubMed ]
- Mariman EC, Broers CA, Claesen CA, Tesser GI, Wieringa B: Structure and expression of the human creatine kinase B gene. Genomics. 1987 Oct;1(2):126-37. [PubMed ]
- Kaye FJ, McBride OW, Battey JF, Gazdar AF, Sausville EA: Human creatine kinase-B complementary DNA. Nucleotide sequence, gene expression in lung cancer, and chromosomal assignment to two distinct loci. J Clin Invest. 1987 May;79(5):1412-20. [PubMed ]
- Mariman EC, Schepens JT, Wieringa B: Complete nucleotide sequence of the human creatine kinase B gene. Nucleic Acids Res. 1989 Aug 11;17(15):6385. [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 ]
- Daouk GH, Kaddurah-Daouk R, Putney S, Kingston R, Schimmel P: Isolation of a functional human gene for brain creatine kinase. J Biol Chem. 1988 Feb 15;263(5):2442-6. [PubMed ]
- Kliffen M, de Jong PT, Luider TM: Protein analysis of human maculae in relation to age-related maculopathy. Lab Invest. 1995 Aug;73(2):267-72. [PubMed ]
- Lin L, Perryman MB, Friedman D, Roberts R, Ma TS: Determination of the catalytic site of creatine kinase by site-directed mutagenesis. Biochim Biophys Acta. 1994 May 18;1206(1):97-104. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
|
| Enzyme 49 Metabolite References |
Not Available |
|
Enzyme 50
[top]
|
| Enzyme 50 ID |
5995 |
| Enzyme 50 Name |
Creatine kinase U-type, mitochondrial |
| Enzyme 50 Synonyms |
- Acidic-type mitochondrial creatine kinase
- Mia-CK
- Ubiquitous mitochondrial creatine kinase
- U-MtCK
|
| Enzyme 50 Gene Name |
CKMT1A |
| Enzyme 50 Protein Sequence |
>Creatine kinase U-type, mitochondrial
MAGPFSRLLSARPGLRLLALAGAGSLAAGFLLRPEPVRAASERRRLYPPSAEYPDLRKHN
NCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPFIKTVGMVAGDEETYEVFAD
LFDPVIQERHNGYDPRTMKHTTDLDASKIRSGYFDERYVLSSRVRTGRSIRGLSLPPACT
RAERREVERVVVDALSGLKGDLAGRYYRLSEMTEAEQQQLIDDHFLFDKPVSPLLTAAGM
ARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQER
GWEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDSRFPKILENLRLQKRGTGGVDT
AATGGVFDISNLDRLGKSEVELVQLVIDGVNYLIDCERRLERGQDIRIPTPVIHTKH
|
| Enzyme 50 Number of Residues |
417 |
| Enzyme 50 Molecular Weight |
47036.3 |
| Enzyme 50 Theoretical pI |
8.47 |
| Enzyme 50 GO Classification |
| Function |
- catalytic activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 50 General Function |
Involved in kinase activity |
| Enzyme 50 Specific Function |
Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa |
| Enzyme 50 Pathways |
- Arginine and Proline Metabolism (map00330 )
|
| Enzyme 50 Reactions |
- ATP + creatine = ADP + phosphocreatine [RN:R01881]
|
| Enzyme 50 Pfam Domain Function |
|
| Enzyme 50 Signals |
|
| Enzyme 50 Transmembrane Regions |
|
| Enzyme 50 Essentiality |
Not Available |
| Enzyme 50 GenBank ID Protein |
Not Available |
| Enzyme 50 UniProtKB/Swiss-Prot ID |
P12532 |
| Enzyme 50 UniProtKB/Swiss-Prot Entry Name |
KCRU_HUMAN |
| Enzyme 50 PDB ID |
1QK1 |
| Enzyme 50 PDB File |
Show |
| Enzyme 50 3D Structure |
|
| Enzyme 50 Cellular Location |
Not Available |
| Enzyme 50 Gene Sequence |
>1254 bp
ATGGCTGGTCCCTTCTCCCGTCTGCTGTCCGCCCGCCCGGGACTCAGGCTCCTGGCTTTG
GCCGGAGCGGGGTCTCTAGCCGCTGGGTTTCTGCTCCGACCGGAACCTGTACGAGCTGCC
AGTGAACGACGGAGGCTGTATCCCCCGAGCGCTGAGTACCCAGACCTCCGAAAGCACAAC
AACTGCATGGCCAGTCACCTGACCCCAGCAGTCTATGCACGGCTCTGCGACAAGACCACA
CCCACTGGTTGGACGCTAGATCAGTGTATCCAGACTGGCGTGGACAACCCTGGCCACCCC
TTCATCAAGACTGTGGGCATGGTGGCTGGAGATGAGGAGACCTATGAGGTATTTGCTGAC
CTGTTTGACCCTGTGATCCAAGAGCGACACAATGGATATGACCCCCGGACAATGAAGCAC
ACCACGGATCTAGATGCCAGTAAAATCCGTTCTGGCTACTTTGATGAGAGGTATGTATTG
TCCTCTAGAGTCAGAACTGGCCGAAGCATCCGAGGACTCAGTCTGCCTCCAGCTTGCACT
CGAGCAGAGCGACGAGAGGTGGAACGTGTTGTGGTGGATGCACTGAGTGGCCTGAAGGGT
GACCTGGCTGGACGTTACTATAGGCTCAGTGAGATGACAGAGGCTGAACAGCAGCAGCTT
ATTGATGACCACTTTCTGTTTGATAAGCCTGTGTCCCCGTTGCTGACTGCAGCAGGAATG
GCTCGAGACTGGCCAGATGCTCGTGGAATTTGGCACAACAATGAGAAGAGCTTCCTGATC
TGGGTGAATGAGGAGGATCATACACGGGTGATCTCCATGGAGAAGGGTGGTAACATGAAG
AGAGTGTTTGAAAGATTCTGCCGAGGCCTCAAAGAGGTGGAGAGACTTATCCAAGAACGT
GGCTGGGAGTTCATGTGGAATGAGCGTTTGGGATACATCTTGACCTGTCCATCTAACCTG
GGCACTGGACTTCGGGCAGGAGTGCACATCAAACTGCCCCTGCTAAGCAAAGATAGCCGC
TTCCCAAAGATCCTGGAGAACCTAAGACTCCAAAAGCGTGGTACTGGAGGAGTGGACACT
GCTGCCACAGGCGGTGTCTTTGATATTTCTAATTTGGACCGACTAGGCAAATCAGAGGTG
GAGCTGGTGCAACTGGTCATCGATGGAGTAAACTATTTGATTGATTGTGAACGGCGTCTG
GAGAGAGGCCAGGATATCCGCATCCCCACACCTGTCATCCACACCAAGCATTAG
|
| Enzyme 50 GenBank Gene ID |
BT006628 |
| Enzyme 50 GeneCard ID |
CKMT1A |
| Enzyme 50 GenAtlas ID |
CKMT1A |
| Enzyme 50 HGNC ID |
HGNC:31736 |
| Enzyme 50 Chromosome Location |
1 |
| Enzyme 50 Locus |
15q15 |
| Enzyme 50 SNPs |
SNPJam Report |
| Enzyme 50 General References |
- Haas RC, Korenfeld C, Zhang ZF, Perryman B, Roman D, Strauss AW: Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase. J Biol Chem. 1989 Feb 15;264(5):2890-7. [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 ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed ]
- Eder M, Fritz-Wolf K, Kabsch W, Wallimann T, Schlattner U: Crystal structure of human ubiquitous mitochondrial creatine kinase. Proteins. 2000 May 15;39(3):216-25. [PubMed ]
|
| Enzyme 50 Metabolite References |
Not Available |
|
Enzyme 51
[top]
|
| Enzyme 51 ID |
5996 |
| Enzyme 51 Name |
Creatine kinase M-type |
| Enzyme 51 Synonyms |
- Creatine kinase M chain
- M-CK
|
| Enzyme 51 Gene Name |
CKM |
| Enzyme 51 Protein Sequence |
>Creatine kinase M-type
MPFGNTHNKFKLNYKPEEEYPDLSKHNNHMAKVLTLELYKKLRDKETPSGFTVDDVIQTG
VDNPGHPFIMTVGCVAGDEESYEVFKELFDPIISDRHGGYKPTDKHKTDLNHENLKGGDD
LDPNYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKLSVEALNSLTGEFKGKYYPLKSMT
EKEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKSFLVWVNEEDHLRVISM
EKGGNMKEVFRRFCVGLQKIEEIFKKAGHPFMWNQHLGYVLTCPSNLGTGLRGGVHVKLA
HLSKHPKFEEILTRLRLQKRGTGGVDTAAVGSVFDVSNADRLGSSEVEQVQLVVDGVKLM
VEMEKKLEKGQSIDDMIPAQK
|
| Enzyme 51 Number of Residues |
381 |
| Enzyme 51 Molecular Weight |
43100.9 |
| Enzyme 51 Theoretical pI |
7.28 |
| Enzyme 51 GO Classification |
| Function |
- catalytic activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 51 General Function |
Involved in kinase activity |
| Enzyme 51 Specific Function |
Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa |
| Enzyme 51 Pathways |
- Arginine and Proline Metabolism (map00330 )
|
| Enzyme 51 Reactions |
- ATP + creatine = ADP + phosphocreatine [RN:R01881]
|
| Enzyme 51 Pfam Domain Function |
|
| Enzyme 51 Signals |
|
| Enzyme 51 Transmembrane Regions |
|
| Enzyme 51 Essentiality |
Not Available |
| Enzyme 51 GenBank ID Protein |
180576 |
| Enzyme 51 UniProtKB/Swiss-Prot ID |
P06732 |
| Enzyme 51 UniProtKB/Swiss-Prot Entry Name |
KCRM_HUMAN |
| Enzyme 51 PDB ID |
1I0E |
| Enzyme 51 PDB File |
Show |
| Enzyme 51 3D Structure |
|
| Enzyme 51 Cellular Location |
Not Available |
| Enzyme 51 Gene Sequence |
>1146 bp
ATGCCATTCGGTAACACCCACAACAAGTTCAAGCTGAATTACAAGCCTGAGGAGGAGTAC
CCCGACCTCAGCAAACATAACAACCACATGGCCAAGGTACTGACCCTTGAACTCTACAAG
AAGCTGCGGGACAAGGAGATCCCATCTGGCTTCACTGTAGACGATGTCATCCAGACAGGA
GTGGACAACCCAGGTCACCCCTTCATCATGACCGTGGGCTGCGTGGCTGGTGATGAGGAG
TCCTACGAAGTTTTCAAGGAACTCTTTGACCCCATCATCTCGGATCGCCACGGGGGCTAC
AAACCCACTGACAAGCACAAGACTGACCTCAACCATGAAAACCTCAAGGGTGGAGACGAC
CTGGACCCCAACTACGTGCTCAGCAGCCCGGTCCGCACTGGCCGCAGCATCAAGGGCTAC
ACGTTGCCCCCACACTGCTCCCGTGGCGAGCGCCGGGCGGTGGAGAAGCTCTCTGTGGAA
GCTCTCAACAGCCTGACGGGCGAGTTCAAAGGGAAGTACTACCCTCTGAAGAGCATGACG
GAGAAGGAGCAGCAGCAGCTCATCGATGACCACTTCCAGTTCGACAAGCCCGTGTCCCCG
CTGCTGCTGGCCTCAGGCATGGCCCGCCACTGGCCCGACGCCCCTGGCATCTGGCACAAT
GACAACAAGAGCTTCCTGGTGTGGGTGAACGAGGAGGATCACCTCCGGGTCATCTCCATG
GAGAAGGGGGGCAACATGAAGGAGGTTTTCCGCCGCTTCTGCGTAGGGCTGCAGAAGATT
GAGGAGATCTTTAAGAAAGCTGGCCACCCCTTCATGTGGAACCAGCACCTGGGCTACGTG
CTCACCTGCCCATCCAACCTGGGCACTGGGCTGCGTGGAGGCGTGCATGTGAAGCTGGCG
CACCTGAGCAAGCACCCCAAGTTCGAGGAGATCCTCACCCGCCTGCGTCTGCAGAAGAGG
GGTACAGGTGCGGTGGACACAGCTGCCGTGGGCTCAGTATTTGACGTGTCCAACGCTGAT
CGGCTGGGCTCGTCCGAAGTAGAACAGGTGCAGCTGGTGGTGGATGGTGTGAAGCTCATG
GTGGAAATGGAGAAGAAGTTGGAGAAAGGCCAGTCCATCGACGACATGATCCCCGCCCAG
AAGTAG
|
| Enzyme 51 GenBank Gene ID |
M14780 |
| Enzyme 51 GeneCard ID |
CKM |
| Enzyme 51 GenAtlas ID |
CKM |
| Enzyme 51 HGNC ID |
HGNC:1994 |
| Enzyme 51 Chromosome Location |
1 |
| Enzyme 51 Locus |
19q13.2-q13.3 |
| Enzyme 51 SNPs |
SNPJam Report |
| Enzyme 51 General References |
- Perryman MB, Kerner SA, Bohlmeyer TJ, Roberts R: Isolation and sequence analysis of a full-length cDNA for human M creatine kinase. Biochem Biophys Res Commun. 1986 Nov 14;140(3):981-9. [PubMed ]
- Trask RV, Strauss AW, Billadello JJ: Developmental regulation and tissue-specific expression of the human muscle creatine kinase gene. J Biol Chem. 1988 Nov 15;263(32):17142-9. [PubMed ]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Hamburg RJ, Friedman DL, Olson EN, Ma TS, Cortez MD, Goodman C, Puleo PR, Perryman MB: Muscle creatine kinase isoenzyme expression in adult human brain. J Biol Chem. 1990 Apr 15;265(11):6403-9. [PubMed ]
- Nigro JM, Schweinfest CW, Rajkovic A, Pavlovic J, Jamal S, Dottin RP, Hart JT, Kamarck ME, Rae PM, Carty MD, et al.: cDNA cloning and mapping of the human creatine kinase M gene to 19q13. Am J Hum Genet. 1987 Feb;40(2):115-25. [PubMed ]
- Tang L, Zhou HM, Lin ZJ: Crystallization and preliminary X-ray analysis of human muscle creatine kinase. Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):669-70. [PubMed ]
|
| Enzyme 51 Metabolite References |
Not Available |
|
Enzyme 52
[top]
|
| Enzyme 52 ID |
6009 |
| Enzyme 52 Name |
6-phosphofructokinase type C |
| Enzyme 52 Synonyms |
- 6-phosphofructokinase, platelet type
- Phosphofructo-1-kinase isozyme C
- PFK-C
- Phosphofructokinase 1
- Phosphohexokinase
|
| Enzyme 52 Gene Name |
PFKP |
| Enzyme 52 Protein Sequence |
>6-phosphofructokinase type C
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFI
YEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGIT
NLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCG
TDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLP
ESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDT
RVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMEC
VQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGA
PAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTK
RVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVS
NNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGA
DAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKG
VFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQ
PWSV
|
| Enzyme 52 Number of Residues |
784 |
| Enzyme 52 Molecular Weight |
85595.4 |
| Enzyme 52 Theoretical pI |
7.60 |
| Enzyme 52 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
- 6-phosphofructokinase complex
- cell part
- cytoplasm
- intracellular part
- macromolecular complex
- protein complex
|
|
| Enzyme 52 General Function |
Involved in 6-phosphofructokinase activity |
| Enzyme 52 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 52 Pathways |
|
| Enzyme 52 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
|
| Enzyme 52 Pfam Domain Function |
|
| Enzyme 52 Signals |
|
| Enzyme 52 Transmembrane Regions |
|
| Enzyme 52 Essentiality |
Not Available |
| Enzyme 52 GenBank ID Protein |
Not Available |
| Enzyme 52 UniProtKB/Swiss-Prot ID |
Q01813 |
| Enzyme 52 UniProtKB/Swiss-Prot Entry Name |
K6PP_HUMAN |
| Enzyme 52 PDB ID |
Not Available |
| Enzyme 52 Cellular Location |
Not Available |
| Enzyme 52 Gene Sequence |
>2355 bp
ATGGACGCGGACGACTCCCGGGCCCCCAAGGGCTCCTTGCGGAAGTTCCTGGAGCACCTC
TCCGGGGCCGGCAAGGCCATCGGCGTGCTGACCAGCGGCGGGGATGCTCAAGGTATGAAC
GCTGCCGTCCGTGCCGTGGTGCGCATGGGTATCTACGTGGGGGCCAAGGTGTACTTCATC
TACGAGGGCTACCAGGGCATGGTGGACGGAGGCTCAAACATCGCAGAGGCCGACTGGGAG
AGTGTCTCCAGCATCCTGCAAGTGGGCGGGACGATCATTGGCAGTGCGCGGTGCCAGGCC
TTCCGCACGCGGGAAGGCCGCCTGAAGGCTGCTTGCAACCTGCTGCAGCGCGGCATCACC
AACCTGTGTGTGATCGGCGGGGACGGGAGCCTCACCGGGGCCAACCTCTTCCGGAAGGAG
TGGAGTGGGCTGCTGGAGGAGCTGGCCAGGAACGGCCAGATCGATAAGGAGGCCGTGCAG
AAGTACGCCTACCTCAACGTGGTGGGCATGGTGGGCTCCATCGACAATGATTTCTGCGGC
ACCGACATGACCATCGGCACGGACTCCGCCCTGCACAGGATCATCGAGGTCGTCGACGCC
ATCATGACCACGGCCCAGAGCCACCAGAGGACCTTCGTTCTGGAGGTGATGGGACGACAC
TGTGGGTACCTGGCCCTGGTGAGTGCCTTGGCCTGCGGTGCGGACTGGGTGTTCCTTCCA
GAATCTCCACCAGAGGAAGGCTGGGAGGAGCAGATGTGTGTCAAACTCTCGGAGAACCGT
GCCCGGAAAAAAAGGCTGAATATTATTATTGTGGCTGAAGGAGCAATTGATACCCAAAAT
AAACCCATCACCTCTGAGAAAATCAAAGAGCTTGTCGTCACGCAGCTGGGCTATGACACA
CGTGTGACCATCCTCGGGCACGTGCAGAGAGGAGGGACCCCTTCGGCATTCGACAGGATC
TTGGCCAGCCGCATGGGAGTGGAGGCAGTCATCGCCTTGCTAGAGGCCACCCCGGACACC
CCAGCTTGCGTCGTGTCACTGAACGGGAACCACGCCGTGCGCCTGCCGCTGATGGAGTGC
GTGCAGATGACTCAGGATGTGCAGAAGGCGATGGACGAGAGGAGATTTCAAGATGCGGTT
CGACTCCGAGGGAGGAGCTTTGCGGGCAACCTGAACACCTACAAGCGACTTGCCATCAAG
CTGCCGGATGATCAGATCCCAAAGACCAATTGCAACGTAGCTGTCATCAACGTGGGGGCA
CCCGCGGCTGGGATGAACGCGGCCGTACGCTCAGCTGTGCGCGTGGGCATTGCCGACGGC
CACAGGATGCTCGCCATCTATGATGGCTTTGACGGCTTCGCCAAGGGCCAGATCAAAGAA
ATCGGCTGGACAGATGTCGGGGGCTGGACCGGCCAAGGAGGCTCCATTCTTGGGACAAAA
CGCGTTCTCCCGGGGAAGTACTTGGAAGAGATCGCCACACAGATGCGCACGCACAGCATC
AACGCGCTGCTGATCATCGGTGGATTCGAGGCCTACCTGGGACTCCTGGAGCTGTCAGCC
GCCCGGGAGAAGCACGAGGAGTTCTGTGTCCCCATGGTCATGGTTCCCGCTACTGTGTCC
AACAATGTGCCGGGTTCCGATTTCAGCATCGGGGCAGACACCGCCCTGAACACTATCACC
GACACCTGCGACCGCATCAAGCAGTCCGCCAGCGGAACCAAGCGGCGCGTGTTCATCATC
GAGACCATGGGCGGCTACTGTGGCTACCTGGCCAACATGGGGGGGCTCGCGGCCGGAGCT
GATGCCGCATACATTTTCGAAGAGCCCTTCGACATCAGGGATCTGCAGTCCAACGTGGAG
CACCTGACGGAGAAAATGAAGACCACCATCCAGAGAGGCCTTGTGCTCAGAAATGAGAGC
TGCAGTGAAAACTACACCACCGACTTCATTTACCAGCTGTATTCAGAAGAGGGCAAAGGC
GTGTTTGACTGCAGGAAGAACGTGCTGGGTCACATGCAGCAGGGTGGGGCACCCTCTCCA
TTTGATAGAAACTTTGGAACCAAAATCTCTGCCAGAGCTATGGAGTGGATCACTGCAAAA
CTCAAGGAGGCCCGGGGCAGAGGAAAAAAATTTACCACCGATGATTCCATTTGTGTGCTG
GGAATAAGCAAAAGAAACGTTATTTTTCAACCTGTGGCAGAGCTGAAGAAGCAAACGGAT
TTTGAGCACAGGATTCCCAAAGAACAGTGGTGGCTCAAGCTACGGCCCCTCATGAAAATC
CTGGCCAAGTACAAGGCCAGCTATGACGTGTCGGACTCAGGCCAGCTGGAACATGTGCAG
CCCTGGAGTGTCTGA
|
| Enzyme 52 GenBank Gene ID |
D25328 |
| Enzyme 52 GeneCard ID |
PFKP |
| Enzyme 52 GenAtlas ID |
PFKP |
| Enzyme 52 HGNC ID |
HGNC:8878 |
| Enzyme 52 Chromosome Location |
1 |
| Enzyme 52 Locus |
10p15.3-p15.2 |
| Enzyme 52 SNPs |
SNPJam Report |
| Enzyme 52 General References |
- Eto K, Sakura H, Yasuda K, Hayakawa T, Kawasaki E, Moriuchi R, Nagataki S, Yazaki Y, Kadowaki T: Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet. Biochem Biophys Res Commun. 1994 Feb 15;198(3):990-8. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- 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 ]
- Simpson CJ, Fothergill-Gilmore LA: Isolation and sequence of a cDNA encoding human platelet phosphofructokinase. Biochem Biophys Res Commun. 1991 Oct 15;180(1):197-203. [PubMed ]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
- 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 ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 52 Metabolite References |
Not Available |
|
Enzyme 53
[top]
|
| Enzyme 53 ID |
6033 |
| Enzyme 53 Name |
6-phosphofructokinase, liver type |
| Enzyme 53 Synonyms |
- Phosphofructo-1-kinase isozyme B
- PFK-B
- Phosphofructokinase 1
- Phosphohexokinase
|
| Enzyme 53 Gene Name |
PFKL |
| Enzyme 53 Protein Sequence |
>6-phosphofructokinase, liver type
MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVE
GGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDG
SLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDS
ALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWE
NFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQ
RGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQK
AMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRS
AVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESI
VENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLG
SDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFN
IHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGH
LQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFS
PVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF
|
| Enzyme 53 Number of Residues |
780 |
| Enzyme 53 Molecular Weight |
85017.8 |
| Enzyme 53 Theoretical pI |
7.54 |
| Enzyme 53 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
- 6-phosphofructokinase complex
- cell part
- cytoplasm
- intracellular part
- macromolecular complex
- protein complex
|
|
| Enzyme 53 General Function |
Involved in 6-phosphofructokinase activity |
| Enzyme 53 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 53 Pathways |
|
| Enzyme 53 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
|
| Enzyme 53 Pfam Domain Function |
|
| Enzyme 53 Signals |
|
| Enzyme 53 Transmembrane Regions |
|
| Enzyme 53 Essentiality |
Not Available |
| Enzyme 53 GenBank ID Protein |
35431 |
| Enzyme 53 UniProtKB/Swiss-Prot ID |
P17858 |
| Enzyme 53 UniProtKB/Swiss-Prot Entry Name |
K6PL_HUMAN |
| Enzyme 53 PDB ID |
Not Available |
| Enzyme 53 Cellular Location |
Not Available |
| Enzyme 53 Gene Sequence |
>2343 bp
ATGGCCGCGGTGGACCTGGAGAAGCTGCGGGCGTCGGGCGCGGGCAAGGCCATCGGCGTC
CTGACCAGCGGCGGCGACCGGCAAGGCATGAACGCTGCTGTCCGGGCTGTGACGCGCATG
GGCATTTATGTGGGTGCCAAAGTCTTCCTCATCTACGAGGGCTATGAGGGCCTCGTGGAG
GGAGGTGAGAACATCAAGCAGGCCAACTGGCTGAGCGTCTCCAACATCATCCAGCTGGGC
GGCACTATCATTGGCAGCGCTCGCTCGAAGGCCTTTACCACCAGGGAGGGGCGCCGGGCA
GCGGCCTACAACCTGGTCCAGCACGGCATCACCAACCTGTGCGTCATCGGCGGGGATGGC
AGCCTCACAGGTGCCAACATCTTCCGCAGCGAGTGGGGCAGCCTGCTGGAGGAGCTGGTG
GCGGAAGGTAAGATCTCAGAGACTACAGCCTGGACCTACTCGCACCTGAACATCGCGGGC
CTAGTGGGCTCCATCGATAACGACTTCTGCGGCACCGACATGACCATCGGCACGGACTCG
GCCCTCCACCGCATCATGGAGGTCATCGATGCCATCACCACCACTGCCCAGAGCCACCAG
AGGACCTTCGTGCTGGAAGTGATGGGCCGGCACTGCGGGTACCTGGCGCTGGTATCTGCA
CTGGCCTCAGGGGCCGACTGGCTGTTCATCCCCGAGGCTCCACCCGAGGACGGCTGGGAG
AACTTCATGTGTGAGAGGCTGGGTGAGACTCGGAGCCGTGGGTCCCGACTGAACATCATC
ATCATCGCTGAGGGTGCCATTGACCGCAACGGGAAGCCCATCTCGTCCAGCTACGTGAAG
GACCTGGTGGTTCAGAGGCTGGGCTTCGACACCCGTGTAACTGTGCTGGGCCACGTGCAG
CGGGGAGGGACGCCCTCTGCCTTCGACCGGATCCTGAGCAGCAAGATGGGCATGGAGGCG
GTGATGGCGCTGCTGGAAGCCACGCCTGACACGCCGGCCTGCGTGGTCACCCTCTCGGGG
AACCAGTCAGTGCGGCTGCCCCTCATGGAGTGCGTGCAGATGACCAAGGAAGTGCAGAAA
GCCATGGATGACAAGAGGTTTGACGAGGCCACCCAGCTCCGTGGTGGGAGCTTCGAGAAC
AACTGGAACATTTACAAGCTCCTCACCCACCAGAAGCCCCCCAAGGAGAAGTCTAACTTC
TCCCTGGCCATCCTGAATGTGGGGGCCCCGGCGGCTGGCATGAATGCGGCCGTGCGCTCG
GCGGTGCGGACCGGCATCTCCCATGGACACACAGTATACGTGGTGCACGATGGCTTCGAA
GGCCTAGCCAAGGGTCAGGTGCAAGAAGTAGGCTGGCACGACGTGGCCGGCTGGTTGGGG
CGTGGTGGCTCCATGCTGGGGACCAAGAGGACCCTGCCCAAGGGCCAGCTGGAGTCCATT
GTGGAGAACATCCGCATCTATGGTATTCACGCCCTGCTGGTGGTCGGTGGGTTTGAGGCC
TATGAAGGGGTGCTGCAGCTGGTGGAGGCTCGCGGGCGCTACGAGGAGCTCTGCATCGTC
ATGTGTGTCATCCCAGCCACCATCAGCAACAACGTCCCTGGCACCGACTTCAGCCTGGGC
TCCGACACTGCTGTAAATGCCGCCATGGAGAGCTGTGACCGCATCAAACAGTCTGCCTCG
GGGACCAAGCGCCGTGTGTTCATCGTGGAGACCATGGGGGGTTACTGTGGCTACCTGGCC
ACCGTGACTGGCATTGCTGTGGGGGCCGACGCCGCCTACGTCTTCGAGGACCCTTTCAAC
ATCCACGACTTAAAGGTCAACGTGGAGCACATGACGGAGAAGATGAAGACAGACATTCAG
AGGGGCCTGGTGCTGCGGAACGAGAAGTGCCATGACTACTACACCACGGAGTTCCTGTAC
AACCTGTACTCATCAGAGGGCAAGGGCGTCTTCGACTGCAGGACCAATGTCCTGGGCCAC
CTGCAGCAGGGTGGCGCTCCAACCCCCTTTGACCGGAACTATGGGACCAAGCTGGGGGTG
AAGGCCATGCTGTGGTTGTCGGAGAAGCTGCGCGAGGTTTACCGCAAGGGACGGGTGTTC
GCCAATGCCCCAGACTCGGCCTGCGTGATCGGCCTGAAGAAGAAGGCGGTGGCCTTCAGC
CCCGTCACTGAGCTCAAGAAAGACACTGATTTCGAGCACCGCATGCCACGGGAGCAGTGG
TGGCTGAGCCTGCGGCTCATGCTGAAGATGCTGGCACAATACCGCATCAGTATGGCCGCC
TACGTGTCAGGGGAGCTGGAGCACGTGACCCGCCGCACCCTGAGCATGGACAAGGGCTTC
TGA
|
| Enzyme 53 GenBank Gene ID |
X15573 |
| Enzyme 53 GeneCard ID |
PFKL |
| Enzyme 53 GenAtlas ID |
PFKL |
| Enzyme 53 HGNC ID |
HGNC:8876 |
| Enzyme 53 Chromosome Location |
2 |
| Enzyme 53 Locus |
21q22.3 |
| Enzyme 53 SNPs |
SNPJam Report |
| Enzyme 53 General References |
- Levanon D, Danciger E, Dafni N, Bernstein Y, Elson A, Moens W, Brandeis M, Groner Y: The primary structure of human liver type phosphofructokinase and its comparison with other types of PFK. DNA. 1989 Dec;8(10):733-43. [PubMed ]
- Elson A, Levanon D, Brandeis M, Dafni N, Bernstein Y, Danciger E, Groner Y: The structure of the human liver-type phosphofructokinase gene. Genomics. 1990 May;7(1):47-56. [PubMed ]
- Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
|
| Enzyme 53 Metabolite References |
Not Available |
|
Enzyme 54
[top]
|
| Enzyme 54 ID |
6037 |
| Enzyme 54 Name |
6-phosphofructokinase, muscle type |
| Enzyme 54 Synonyms |
- Phosphofructo-1-kinase isozyme A
- PFK-A
- Phosphofructokinase-M
- Phosphofructokinase 1
- Phosphohexokinase
|
| Enzyme 54 Gene Name |
PFKM |
| Enzyme 54 Protein Sequence |
>6-phosphofructokinase, muscle type
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVD
GGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDG
SLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDS
ALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWE
EHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQ
RGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTK
AMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVR
STVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQ
ISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSV
GADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPF
TIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLG
HMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVF
QPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV
|
| Enzyme 54 Number of Residues |
780 |
| Enzyme 54 Molecular Weight |
85181.9 |
| Enzyme 54 Theoretical pI |
8.07 |
| Enzyme 54 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
- 6-phosphofructokinase complex
- cell part
- cytoplasm
- intracellular part
- macromolecular complex
- protein complex
|
|
| Enzyme 54 General Function |
Involved in 6-phosphofructokinase activity |
| Enzyme 54 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 54 Pathways |
|
| Enzyme 54 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
|
| Enzyme 54 Pfam Domain Function |
|
| Enzyme 54 Signals |
|
| Enzyme 54 Transmembrane Regions |
|
| Enzyme 54 Essentiality |
Not Available |
| Enzyme 54 GenBank ID Protein |
189855 |
| Enzyme 54 UniProtKB/Swiss-Prot ID |
P08237 |
| Enzyme 54 UniProtKB/Swiss-Prot Entry Name |
K6PF_HUMAN |
| Enzyme 54 PDB ID |
Not Available |
| Enzyme 54 Cellular Location |
Not Available |
| Enzyme 54 Gene Sequence |
>2343 bp
ATGACCCATGAAGAGCACCATGCAGCCAAAACCCTGGGGATTGGCAAAGCCATTGCTGTC
TTAACCTCTGGTGGAGATGCCCAAGGTATGAATGCTGCTGTCAGGGCTGTGGTTCGAGTT
GGTATCTTCACCGGTGCCCGTGTCTTCTTTGTCCATGAGGGTTATCAAGGCCTGGTGGAT
GGTGGAGATCACATCAAGGAAGCCACCTGGGAGAGCGTTTCGATGATGCTTCAGCTGGGA
GGCACGGTGATTGGAAGTGCCCGGTGCAAGGACTTTCGGGAACGAGAAGGACGACTCCGA
GCTGCCTACAACCTGGTGAAGCGTGGGATCACCAATCTCTGTGTCATTGGGGGTGATGGC
AGCCTCACTGGGGCTGACACCTTCCGTTCTGAGTGGAGTGACTTGTTGAGTGACCTCCAG
AAAGCAGGTAAGATCACAGATGAGGAGGCTACGAAGTCCAGCTACCTGAACATTGTGGGC
CTGGTTGGGTCAATTGACAATGACTTCTGTGGCACCGATATGACCATTGGCACTGACTCT
GCCCTGCATCGGATCATGGAAATTGTAGATGCCATCACTACCACTGCCCAGAGCCACCAG
AGGACATTTGTGTTAGAAGTAATGGGCCGCCACTGTGGATACCTGGCCCTTGTCACCTCT
CTGTCCTGTGGGGCCGACTGGGTTTTTATTCCTGAATGTCCACCAGATGACGACTGGGAG
GAACACCTTTGTCGCCGACTCAGCGAGACAAGGACCCGTGGTTCTCGTCTCAACATCATC
ATTGTGGCTGAGGGTGCAATTGACAAGAATGGAAAACCAATCACCTCAGAAGACATCAAG
AATCTGGTGGTTAAGCGTCTGGGATATGACACCCGGGTTACTGTCTTGGGGCATGTGCAG
AGGGGTGGGACGCCATCAGCCTTTGACAGAATTCTGGGCAGCAGGATGGGTGTGGAAGCA
GTGATGGCACTTTTGGAGGGGACCCCAGATACCCCAGCCTGTGTAGTGAGCCTCTCTGGT
AACCAGGCTGTGCGCCTGCCCCTCATGGAATGTGTCCAGGTGACCAAAGATGTGACCAAG
GCCATGGATGAGAAGAAATTTGACGAAGCCCTGAAGCTGAGAGGCCGGAGCTTCATGAAC
AACTGGGAGGTGTACAAGCTTCTAGCTCATGTCAGACCCCCGGTATCTAAGAGTGGTTCG
CACACAGTGGCTGTGATGAACGTGGGGGCTCCGGCTGCAGGCATGAATGCTGCTGTTCGC
TCCACTGTGAGGATTGGCCTTATCCAGGGCAACCGAGTGCTCGTTGTCCATGATGGTTTC
GAGGGCCTGGCCAAGGGGCAGATAGAGGAAGCTGGCTGGAGCTATGTTGGGGGCTGGACT
GGCCAAGGTGGCTCTAAACTTGGGACTAAAAGGACTCTACCCAAGAAGAGCTTTGAACAG
ATCAGTGCCAATATAACTAAGTTTAACATTCAGGGCCTTGTCATCATTGGGGGCTTTGAG
GCTTACACAGGGGGCCTGGAACTGATGGAGGGCAGGAAGCAGTTTGATGAGCTCTGCATC
CCATTTGTGGTCATTCCTGCTACAGTCTCCAACAATGTCCCTGGCTCAGACTTCAGCGTT
GGGGCTGACACAGCACTCAATACTATCTGCACAACCTGTGACCGCATCAAGCAGTCAGCA
GCTGGCACCAAGCGTCGGGTGTTTATCATTGAGACTATGGGTGGCTACTGTGGCTACCTG
GCTACCATGGCTGGACTGGCAGCTGGGGCCGATGCTGCCTACATTTTTGAGGAGCCCTTC
ACCATTCGAGACCTGCAGGCAAATGTTGAACATCTGGTGCAAAAGATGAAAACAACTGTG
AAAAGGGGCTTGGTGTTAAGGAATGAAAAGTGCAATGAGAACTATACCACTGACTTCATT
TTCAACCTGTACTCTGAGGAGGGGAAGGGCATCTTCGACAGCAGGAAGAATGTGCTTGGT
CACATGCAGCAGGGTGGGAGCCCAACCCCATTTGATAGGAATTTTGCCACTAAGATGGGC
GCCAAGGCTATGAACTGGATGTCTGGGAAAATCAAAGAGAGTTACCGTAATGGGCGGATC
TTTGCCAATACTCCAGATTCGGGCTGTGTTCTGGGGATGCGTAAGAGGGCTCTGGTCTTC
CAACCAGTGGCTGAGCTGAAGGACCAGACAGATTTTGAGCATCGAATCCCCAAGGAACAG
TGGTGGCTGAAACTGAGGCCCATCCTCAAAATCCTAGCCAAGTACGAGATTGACTTGGAC
ACTTCAGACCATGCCCACCTGGAGCACATCACCCGGAAGCGGTCCGGGGAAGCTGCCGTC
TAA
|
| Enzyme 54 GenBank Gene ID |
M26066 |
| Enzyme 54 GeneCard ID |
PFKM |
| Enzyme 54 GenAtlas ID |
PFKM |
| Enzyme 54 HGNC ID |
HGNC:8877 |
| Enzyme 54 Chromosome Location |
1 |
| Enzyme 54 Locus |
12q13.3 |
| Enzyme 54 SNPs |
SNPJam Report |
| Enzyme 54 General References |
- Yamasaki T, Nakajima H, Kono N, Hotta K, Yamada K, Imai E, Kuwajima M, Noguchi T, Tanaka T, Tarui S: Structure of the entire human muscle phosphofructokinase-encoding gene: a two-promoter system. Gene. 1991 Aug 15;104(2):277-82. [PubMed ]
- Sharma PM, Reddy GR, Vora S, Babior BM, McLachlan A: Cloning and expression of a human muscle phosphofructokinase cDNA. Gene. 1989 Apr 15;77(1):177-83. [PubMed ]
- Nakajima H, Noguchi T, Yamasaki T, Kono N, Tanaka T, Tarui S: Cloning of human muscle phosphofructokinase cDNA. FEBS Lett. 1987 Oct 19;223(1):113-6. [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 ]
- Sharma PM, Reddy GR, Babior BM, McLachlan A: Alternative splicing of the transcript encoding the human muscle isoenzyme of phosphofructokinase. J Biol Chem. 1990 Jun 5;265(16):9006-10. [PubMed ]
- Valdez BC, Chen Z, Sosa MG, Younathan ES, Chang SH: Human 6-phosphofructo-1-kinase gene has an additional intron upstream of start codon. Gene. 1989 Mar 15;76(1):167-9. [PubMed ]
- Raben N, Sherman JB: Mutations in muscle phosphofructokinase gene. Hum Mutat. 1995;6(1):1-6. [PubMed ]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed ]
- Tsujino S, Servidei S, Tonin P, Shanske S, Azan G, DiMauro S: Identification of three novel mutations in non-Ashkenazi Italian patients with muscle phosphofructokinase deficiency. Am J Hum Genet. 1994 May;54(5):812-9. [PubMed ]
- Raben N, Exelbert R, Spiegel R, Sherman JB, Nakajima H, Plotz P, Heinisch J: Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency. Am J Hum Genet. 1995 Jan;56(1):131-41. [PubMed ]
- Hamaguchi T, Nakajima H, Noguchi T, Nakagawa C, Kuwajima M, Kono N, Tarui S, Matsuzawa Y: Novel missense mutation (W686C) of the phosphofructokinase-M gene in a Japanese patient with a mild form of glycogenosis VII. Hum Mutat. 1996;8(3):273-5. [PubMed ]
|
| Enzyme 54 Metabolite References |
Not Available |
|
Enzyme 55
[top]
|
| Enzyme 55 ID |
6039 |
| Enzyme 55 Name |
Pyruvate kinase isozymes M1/M2 |
| Enzyme 55 Synonyms |
- Cytosolic thyroid hormone-binding protein
- CTHBP
- Opa-interacting protein 3
- OIP-3
- Pyruvate kinase 2/3
- Pyruvate kinase muscle isozyme
- Thyroid hormone-binding protein 1
- THBP1
- Tumor M2-PK
- p58
|
| Enzyme 55 Gene Name |
PKM2 |
| Enzyme 55 Protein Sequence |
>Pyruvate kinase isozymes M1/M2
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR
TGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGL
ISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMV
FASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEAS
FKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQE
AWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
|
| Enzyme 55 Number of Residues |
531 |
| Enzyme 55 Molecular Weight |
57936.4 |
| Enzyme 55 Theoretical pI |
7.94 |
| Enzyme 55 GO Classification |
| Function |
- alkali metal ion binding
- binding
- catalytic activity
- cation binding
- ion binding
- kinase activity
- magnesium ion binding
- metal ion binding
- potassium ion binding
- pyruvate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 55 General Function |
Involved in magnesium ion binding |
| Enzyme 55 Specific Function |
Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival |
| Enzyme 55 Pathways |
|
| Enzyme 55 Reactions |
- ATP + pyruvate = ADP + phosphoenolpyruvate [RN:R00200]
|
| Enzyme 55 Pfam Domain Function |
|
| Enzyme 55 Signals |
|
| Enzyme 55 Transmembrane Regions |
|
| Enzyme 55 Essentiality |
Not Available |
| Enzyme 55 GenBank ID Protein |
33286418 |
| Enzyme 55 UniProtKB/Swiss-Prot ID |
P14618 |
| Enzyme 55 UniProtKB/Swiss-Prot Entry Name |
KPYM_HUMAN |
| Enzyme 55 PDB ID |
1F3X |
| Enzyme 55 PDB File |
Show |
| Enzyme 55 3D Structure |
|
| Enzyme 55 Cellular Location |
Not Available |
| Enzyme 55 Gene Sequence |
>1596 bp
ATGTCGAAGCCCCATAGTGAAGCCGGGACTGCCTTCATTCAGACCCAGCAGCTGCACGCA
GCCATGGCTGACACATTCCTGGAGCACATGTGCCGCCTGGACATTGATTCACCACCCATC
ACAGCCCGGAACACTGGCATCATCTGTACCATTGGCCCAGCTTCCCGATCAGTGGAGACG
TTGAAGGAGATGATTAAGTCTGGAATGAATGTGGCTCGTCTGAACTTCTCTCATGGAACT
CATGAGTACCATGCGGAGACCATCAAGAATGTGCGCACAGCCACGGAAAGCTTTGCTTCT
GACCCCATCCTCTACCGGCCCGTTGCTGTGGCTCTAGACACTAAAGGACCTGAGATCCGA
ACTGGGCTCATCAAGGGCAGCGGCACTGCAGAGGTGGAGCTGAAGAAGGGAGCCACTCTC
AAAATCACGCTGGATAACGCCTACATGGAAAAGTGTGACGAGAACATCCTGTGGCTGGAC
TACAAGAACATCTGCAAGGTGGTGGAAGTGGGCAGCAAGATCTACGTGGATGATGGGCTT
ATTTCTCTCCAGGTGAAGCAGAAAGGTGCCGACTTCCTGGTGACGGAGGTGGAAAATGGT
GGCTCCTTGGGCAGCAAGAAGGGTGTGAACCTTCCTGGGGCTGCTGTGGACTTGCCTGCT
GTGTCGGAGAAGGACATCCAGGATCTGAAGTTTGGGGTCGAGCAGGATGTTGATATGGTG
TTTGCGTCATTCATCCGCAAGGCATCTGATGTCCATGAAGTTAGGAAGGTCCTGGGAGAG
AAGGGAAAGAACATCAAGATTATCAGCAAAATCGAGAATCATGAGGGGGTTCGGAGGTTT
GATGAAATCCTGGAGGCCAGTGATGGGATCATGGTGGCTCGTGGTGATCTAGGCATTGAG
ATTCCTGCAGAGAAGGTCTTCCTTGCTCAGAAGATGATGATTGGACGGTGCAACCGAGCT
GGGAAGCCTGTCATCTGTGCTACTCAGATGCTGGAGAGCATGATCAAGAAGCCCCGCCCC
ACTCGGGCTGAAGGCAGTGATGTGGCCAATGCAGTCCTGGATGGAGCCGACTGCATCATG
CTGTCTGGAGAAACAGCCAAAGGGGACTATCCTCTGGAGGCTGTGCGCATGCAGCACCTG
ATTGCCCGTGAGGCAGAGGCTGCCATCTACCACTTGCAATTATTTGAGGAACTCCGCCGC
CTGGCGCCCATTACCAGCGACCCCACAGAAGCCACCGCCGTGGGTGCCGTGGAGGCCTCC
TTCAAGTGCTGCAGTGGGGCCATAATCGTCCTCACCAAGTCTGGCAGGTCTGCTCACCAG
GTGGCCAGATACCGCCCACGTGCCCCCATCATTGCTGTGACCCGGAATCCCCAGACAGCT
CGTCAGGCCCACCTGTACCGTGGCATCTTCCCTGTGCTGTGCAAGGACCCAGTCCAGGAG
GCCTGGGCTGAGGACGTGGACCTCCGGGTGAACTTTGCCATGAATGTTGGCAAGGCCCGA
GGCTTCTTCAAGAAGGGAGATGTGGTCATTGTGCTGACCGGATGGCGCCCTGGCTCCGGC
TTCACCAACACCATGCGTGTTGTTCCTGTGCCGTGA
|
| Enzyme 55 GenBank Gene ID |
NM_002654.3 |
| Enzyme 55 GeneCard ID |
PKM2 |
| Enzyme 55 GenAtlas ID |
PKM2 |
| Enzyme 55 HGNC ID |
HGNC:9021 |
| Enzyme 55 Chromosome Location |
1 |
| Enzyme 55 Locus |
15q22 |
| Enzyme 55 SNPs |
SNPJam Report |
| Enzyme 55 General References |
- Tani K, Yoshida MC, Satoh H, Mitamura K, Noguchi T, Tanaka T, Fujii H, Miwa S: Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment and expression in hepatoma. Gene. 1988 Dec 20;73(2):509-16. [PubMed ]
- Kato H, Fukuda T, Parkison C, McPhie P, Cheng SY: Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7861-5. [PubMed ]
- Takenaka M, Noguchi T, Sadahiro S, Hirai H, Yamada K, Matsuda T, Imai E, Tanaka T: Isolation and characterization of the human pyruvate kinase M gene. Eur J Biochem. 1991 May 23;198(1):101-6. [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 ]
- Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [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 ]
- Ashizawa K, McPhie P, Lin KH, Cheng SY: An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate. Biochemistry. 1991 Jul 23;30(29):7105-11. [PubMed ]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
- Williams JM, Chen GC, Zhu L, Rest RF: Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth. Mol Microbiol. 1998 Jan;27(1):171-86. [PubMed ]
- Garcia-Gonzalo FR, Cruz C, Munoz P, Mazurek S, Eigenbrodt E, Ventura F, Bartrons R, Rosa JL: Interaction between HERC1 and M2-type pyruvate kinase. FEBS Lett. 2003 Mar 27;539(1-3):78-84. [PubMed ]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
- Stetak A, Veress R, Ovadi J, Csermely P, Keri G, Ullrich A: Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death. Cancer Res. 2007 Feb 15;67(4):1602-8. [PubMed ]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed ]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed ]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
- Shimada N, Shinagawa T, Ishii S: Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein. Genes Cells. 2008 Mar;13(3):245-54. [PubMed ]
- Lee J, Kim HK, Han YM, Kim J: Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription. Int J Biochem Cell Biol. 2008;40(5):1043-54. Epub 2007 Nov 29. [PubMed ]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Dombrauckas JD, Santarsiero BD, Mesecar AD: Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis. Biochemistry. 2005 Jul 12;44(27):9417-29. [PubMed ]
|
| Enzyme 55 Metabolite References |
Not Available |
|
Enzyme 56
[top]
|
| Enzyme 56 ID |
6041 |
| Enzyme 56 Name |
Pyruvate kinase isozymes R/L |
| Enzyme 56 Synonyms |
- Pyruvate kinase 1
- R-type/L-type pyruvate kinase
- Red cell/liver pyruvate kinase
|
| Enzyme 56 Gene Name |
PKLR |
| Enzyme 56 Protein Sequence |
>Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
|
| Enzyme 56 Number of Residues |
574 |
| Enzyme 56 Molecular Weight |
61829.6 |
| Enzyme 56 Theoretical pI |
7.83 |
| Enzyme 56 GO Classification |
| Function |
- alkali metal ion binding
- binding
- catalytic activity
- cation binding
- ion binding
- kinase activity
- magnesium ion binding
- metal ion binding
- potassium ion binding
- pyruvate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 56 General Function |
Involved in magnesium ion binding |
| Enzyme 56 Specific Function |
Plays a key role in glycolysis |
| Enzyme 56 Pathways |
|
| Enzyme 56 Reactions |
- ATP + pyruvate = ADP + phosphoenolpyruvate [RN:R00200]
|
| Enzyme 56 Pfam Domain Function |
|
| Enzyme 56 Signals |
|
| Enzyme 56 Transmembrane Regions |
|
| Enzyme 56 Essentiality |
Not Available |
| Enzyme 56 GenBank ID Protein |
Not Available |
| Enzyme 56 UniProtKB/Swiss-Prot ID |
P30613 |
| Enzyme 56 UniProtKB/Swiss-Prot Entry Name |
KPYR_HUMAN |
| Enzyme 56 PDB ID |
1LIU |
| Enzyme 56 PDB File |
Show |
| Enzyme 56 3D Structure |
|
| Enzyme 56 Cellular Location |
Not Available |
| Enzyme 56 Gene Sequence |
>1725 bp
ATGTCGATCCAGGAGAACATATCATCCCTGCAGCTTCGGTCATGGGTCTCTAAGTCCCAA
AGAGACTTAGCAAAGTCCATCCTGATTGGGGCTCCAGGAGGGCCAGCGGGGTATCTGCGG
CGGGCCAGTGTGGCCCAACTGACCCAGGAGCTGGGCACTGCCTTCTTCCAGCAGCAGCAG
CTGCCAGCTGCTATGGCAGACACCTTCCTGGAACACCTCTGCCTACTGGACATTGACTCC
GAGCCCGTGGCTGCTCGCAGTACCAGCATCATTGCCACCATCGGGCCAGCATCTCGCTCC
GTGGAGCGCCTCAAGGAGATGATCAAGGCCGGGATGAACATTGCGCGACTCAACTTCTCC
CACGGCTCCCACGAGTACCATGCTGAGTCCATCGCCAACGTCCGGGAGGCGGTGGAGAGC
TTTGCAGGTTCCCCACTCAGCTACCGGCCCGTGGCCATCGCCCTGGACACCAAGGGACCG
GAGATCCGCACTGGGATCCTGCAGGGGGGTCCAGAGTCGGAAGTGGAGCTGGTGAAGGGC
TCCCAGGTGCTGGTGACTGTGGACCCCGCGTTCCGGACGCGGGGGAACGCGAACACCGTG
TGGGTGGACTACCCCAATATTGTCCGGGTCGTGCCGGTGGGGGGCCGCATCTACATTGAC
GACGGGCTCATCTCCCTAGTGGTCCAGAAAATCGGCCCAGAGGGACTGGTGACCCAAGTG
GAGAACGGCGGCGTCCTGGGCAGCCGGAAGGGCGTGAACTTGCCAGGGGCCCAGGTGGAC
TTGCCCGGGCTGTCCGAGCAGGACGTCCGAGACCTGCGCTTCGGGGTGGAGCATGGGGTG
GACATCGTCTTTGCCTCCTTTGTGCGGAAAGCCAGCGACGTGGCTGCCGTCAGGGCTGCT
CTGGGTCCGGAAGGACACGGCATCAAGATCATCAGCAAAATTGAGAACCACGAAGGCGTG
AAGAGGTTTGATGAAATCCTGGAGGTGAGCGACGGCATCATGGTGGCACGGGGGGACCTA
GGCATCGAGATCCCAGCAGAGAAGGTTTTCCTGGCTCAGAAGATGATGATTGGGCGCTGC
AACTTGGCGGGCAAGCCTGTTGTCTGTGCCACACAGATGCTGGAGAGCATGATTACCAAG
CCCCGGCCAACGAGGGCAGAGACAAGCGATGTCGCCAATGCTGTGCTGGATGGGGCTGAC
TGCATCATGCTGTCAGGGGAGACTGCCAAGGGCAACTTCCCTGTGGAAGCGGTGAAGATG
CAGCATGCGATTGCCCGGGAGGCAGAGGCCGCAGTGTACCACCGGCAGCTGTTTGAGGAG
CTACGTCGGGCAGCGCCACTAAGCCGTGATCCCACTGAGGTCACCGCCATTGGTGCTGTG
GAGGCTGCCTTCAAGTGCTGTGCTGCTGCCATCATTGTGCTGACCACAACTGGCCGCTCA
GCCCAGCTTCTGTCTCGGTACCGACCTCGGGCAGCAGTCATTGCTGTCACCCGCTCTGCC
CAGGCTGCCCGCCAGGTCCACTTATGCCGAGGAGTCTTCCCCTTGCTTTACCGTGAACCT
CCAGAAGCCATCTGGGCAGATGATGTAGATCGCCGGGTGCAATTTGGCATTGAAAGTGGA
AAGCTCCGTGGCTTCCTCCGTGTTGGAGACCTGGTGATTGTGGTGACAGGCTGGCGACCT
GGCTCCGGCTACACCAACATCATGAGGGTGCTAAGCATATCCTGA
|
| Enzyme 56 GenBank Gene ID |
AB015983 |
| Enzyme 56 GeneCard ID |
PKLR |
| Enzyme 56 GenAtlas ID |
PKLR |
| Enzyme 56 HGNC ID |
HGNC:9020 |
| Enzyme 56 Chromosome Location |
1 |
| Enzyme 56 Locus |
1q21 |
| Enzyme 56 SNPs |
SNPJam Report |
| Enzyme 56 General References |
- Kanno H, Fujii H, Hirono A, Miwa S: cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8218-21. [PubMed ]
- Tani K, Fujii H, Nagata S, Miwa S: Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1792-5. [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 ]
- Tani K, Fujii H, Tsutsumi H, Sukegawa J, Toyoshima K, Yoshida MC, Noguchi T, Tanaka T, Miwa S: Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment. Biochem Biophys Res Commun. 1987 Mar 13;143(2):431-8. [PubMed ]
- Kanno H, Fujii H, Tsujino G, Miwa S: Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. Biochem Biophys Res Commun. 1993 Apr 15;192(1):46-52. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed ]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase. Blood Cells Mol Dis. 1996;22(1):85-9. [PubMed ]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (1st update). Blood Cells Mol Dis. 1996;22(3):259-64. [PubMed ]
- Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (2nd update). Blood Cells Mol Dis. 1998 Sep;24(3):273-9. [PubMed ]
- Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (Third update). Blood Cells Mol Dis. 2000 Feb;26(1):47-53. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A: Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia. J Biol Chem. 2002 Jun 28;277(26):23807-14. Epub 2002 Apr 17. [PubMed ]
- Neubauer B, Lakomek M, Winkler H, Parke M, Hofferbert S, Schroter W: Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency. Blood. 1991 May 1;77(9):1871-5. [PubMed ]
- Kanno H, Fujii H, Hirono A, Omine M, Miwa S: Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. Blood. 1992 Mar 1;79(5):1347-50. [PubMed ]
- Kanno H, Fujii H, Miwa S: Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. Blood. 1993 May 1;81(9):2439-41. [PubMed ]
- Baronciani L, Beutler E: Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1993 May 1;90(9):4324-7. [PubMed ]
- Kanno H, Ballas SK, Miwa S, Fujii H, Bowman HS: Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish. Blood. 1994 Apr 15;83(8):2311-6. [PubMed ]
- Lenzner C, Nurnberg P, Thiele BJ, Reis A, Brabec V, Sakalova A, Jacobasch G: Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia. Blood. 1994 May 15;83(10):2817-22. [PubMed ]
- Baronciani L, Beutler E: Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia. J Clin Invest. 1995 Apr;95(4):1702-9. [PubMed ]
- Beutler E, Westwood B, van Zwieten R, Roos D: G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Hum Mutat. 1997;9(3):282-5. [PubMed ]
- Zarza R, Alvarez R, Pujades A, Nomdedeu B, Carrera A, Estella J, Remacha A, Sanchez JM, Morey M, Cortes T, Perez Lungmus G, Bureo E, Vives Corrons JL: Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients. Red Cell Pathology Group of the Spanish Society of Haematology (AEHH). Br J Haematol. 1998 Nov;103(2):377-82. [PubMed ]
- Cohen-Solal M, Prehu C, Wajcman H, Poyart C, Bardakdjian-Michau J, Kister J, Prome D, Valentin C, Bachir D, Galacteros F: A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha2 globin gene variant (Hb Conakry). Br J Haematol. 1998 Dec;103(4):950-6. [PubMed ]
- Pastore L, Della Morte R, Frisso G, Alfinito F, Vitale D, Calise RM, Ferraro F, Zagari A, Rotoli B, Salvatore F: Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy. Hum Mutat. 1998;11(2):127-34. [PubMed ]
- Zanella A, Bianchi P, Fermo E, Iurlo A, Zappa M, Vercellati C, Boschetti C, Baronciani L, Cotton F: Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients. Br J Haematol. 2001 Apr;113(1):43-8. [PubMed ]
- van Wijk R, Huizinga EG, van Wesel AC, van Oirschot BA, Hadders MA, van Solinge WW: Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency: structural implications of amino acid substitutions in PK. Hum Mutat. 2009 Mar;30(3):446-53. [PubMed ]
|
| Enzyme 56 Metabolite References |
Not Available |
|
Enzyme 57
[top]
|
| Enzyme 57 ID |
6043 |
| Enzyme 57 Name |
Deoxyguanosine kinase, mitochondrial |
| Enzyme 57 Synonyms |
- dGK
|
| Enzyme 57 Gene Name |
DGUOK |
| Enzyme 57 Protein Sequence |
>Deoxyguanosine kinase, mitochondrial
MAAGRLFLSRLRAPFSSMAKSPLEGVSSSRGLHAGRGPRRLSIEGNIAVGKSTFVKLLTK
TYPEWHVATEPVATWQNIQAAGTQKACTAQSLGNLLDMMYREPARWSYTFQTFSFLSRLK
VQLEPFPEKLLQARKPVQIFERSVYSDRYIFAKNLFENGSLSDIEWHIYQDWHSFLLWEF
ASRITLHGFIYLQASPQVCLKRLYQRAREEEKGIELAYLEQLHGQHEAWLIHKTTKLHFE
ALMNIPVLVLDVNDDFSEEVTKQEDLMREVNTFVKNL
|
| Enzyme 57 Number of Residues |
277 |
| Enzyme 57 Molecular Weight |
32055.5 |
| Enzyme 57 Theoretical pI |
8.97 |
| Enzyme 57 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
|
| Component |
| — |
|
| Enzyme 57 General Function |
Involved in ATP binding |
| Enzyme 57 Specific Function |
Required for the phosphorylation of several deoxyribonucleosides and certain nucleoside analogs widely employed as antiviral and chemotherapeutic agents |
| Enzyme 57 Pathways |
|
| Enzyme 57 Reactions |
- ATP + deoxyguanosine = ADP + dGMP [RN:R01967]
|
| Enzyme 57 Pfam Domain Function |
|
| Enzyme 57 Signals |
|
| Enzyme 57 Transmembrane Regions |
|
| Enzyme 57 Essentiality |
Not Available |
| Enzyme 57 GenBank ID Protein |
16041753 |
| Enzyme 57 UniProtKB/Swiss-Prot ID |
Q16854 |
| Enzyme 57 UniProtKB/Swiss-Prot Entry Name |
DGUOK_HUMAN |
| Enzyme 57 PDB ID |
1JAG |
| Enzyme 57 PDB File |
Show |
| Enzyme 57 3D Structure |
|
| Enzyme 57 Cellular Location |
Not Available |
| Enzyme 57 Gene Sequence |
>834 bp
ATGGCCGCGGGCCGCCTCTTTCTAAGTCGGCTTCGAGCACCCTTCAGTTCCATGGCCAAG
AGCCCACTCGAGGGCGTTTCCTCCTCCAGAGGCCTGCACGCGGGGCGCGGGCCCCGAAGG
CTCTCCATCGAAGGCAACATTGCTGTGGGAAAGTCCACGTTTGTGAAGTTACTCACGAAA
ACTTACCCAGAATGGCACGTAGCTACAGAACCTGTAGCAACATGGCAGAATATCCAGGCT
GCTGGCACCCAAAAAGCCTGCACTGCCCAAAGTCTTGGAAACTTGCTGGATATGATGTAC
CGGGAGCCAGCACGATGGTCCTACACATTCCAGACATTTTCCTTTTTGAGCCGCCTGAAA
GTACAGCTGGAGCCCTTCCCTGAGAAACTCTTACAGGCCAGGAAGCCAGTACAGATCTTT
GAGAGGTCTGTGTACAGTGACAGGTATATCTTTGCAAAGAATCTTTTTGAAAATGGTTCC
CTCAGTGACATCGAGTGGCATATCTATCAGGACTGGCATTCTTTTCTCCTGTGGGAGTTT
GCCAGCCGGATCACATTACATGGCTTCATCTACCTCCAGGCTTCTCCCCAGGTTTGTTTG
AAGAGACTGTACCAGAGGGCCAGGGAGGAGGAGAAAGGAATTGAGCTGGCCTATCTAGAG
CAGCTGCATGGCCAACACGAAGCCTGGCTTATTCACAAGACAACGAAGCTCCACTTTGAG
GCTCTGATGAACATTCCAGTGCTGGTGTTGGATGTCAATGATGATTTTTCTGAGGAAGTA
ACCAAACAAGAAGACCTCATGAGAGAGGTAAACACCTTTGTAAAGAATCTGTAA
|
| Enzyme 57 GenBank Gene ID |
BC015757 |
| Enzyme 57 GeneCard ID |
DGUOK |
| Enzyme 57 GenAtlas ID |
DGUOK |
| Enzyme 57 HGNC ID |
HGNC:2858 |
| Enzyme 57 Chromosome Location |
2 |
| Enzyme 57 Locus |
2p13 |
| Enzyme 57 SNPs |
SNPJam Report |
| Enzyme 57 General References |
- Johansson M, Karlsson A: Cloning and expression of human deoxyguanosine kinase cDNA. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7258-62. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Wang L, Hellman U, Eriksson S: Cloning and expression of human mitochondrial deoxyguanosine kinase cDNA. FEBS Lett. 1996 Jul 15;390(1):39-43. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Salviati L, Sacconi S, Mancuso M, Otaegui D, Camano P, Marina A, Rabinowitz S, Shiffman R, Thompson K, Wilson CM, Feigenbaum A, Naini AB, Hirano M, Bonilla E, DiMauro S, Vu TH: Mitochondrial DNA depletion and dGK gene mutations. Ann Neurol. 2002 Sep;52(3):311-7. [PubMed ]
- Wang L, Limongelli A, Vila MR, Carrara F, Zeviani M, Eriksson S: Molecular insight into mitochondrial DNA depletion syndrome in two patients with novel mutations in the deoxyguanosine kinase and thymidine kinase 2 genes. Mol Genet Metab. 2005 Jan;84(1):75-82. [PubMed ]
|
| Enzyme 57 Metabolite References |
Not Available |
|
Enzyme 58
[top]
|
| Enzyme 58 ID |
6057 |
| Enzyme 58 Name |
Choline kinase alpha |
| Enzyme 58 Synonyms |
- CK
- CHETK-alpha
- Ethanolamine kinase
- EK
|
| Enzyme 58 Gene Name |
CHKA |
| Enzyme 58 Protein Sequence |
>Choline kinase alpha
MKTKFCTGGEAEPSPLGLLLSCGSGSAAPAPGVGQQRDAASDLESKQLGGQQPPLALPPP
PPLPLPLPLPQPPPPQPPADEQPEPRTRRRAYLWCKEFLPGAWRGLREDEFHISVIRGGL
SNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQMRSCNKEGSEQAQKENEFQGAEAMVLE
SVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKM
PFNKEPKWLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPV
VFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYP
FFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLW
GLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKLGV
|
| Enzyme 58 Number of Residues |
457 |
| Enzyme 58 Molecular Weight |
52248.5 |
| Enzyme 58 Theoretical pI |
6.52 |
| Enzyme 58 GO Classification |
Not Available |
| Enzyme 58 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 58 Specific Function |
Has a key role in phospholipid biosynthesis and may contribute to tumor cell growth. Catalyzes the first step in phosphatidylcholine biosynthesis. Contributes to phosphatidylethanolamine biosynthesis. Phosphorylates choline and ethanolamine. Has higher activity with choline |
| Enzyme 58 Pathways |
- Phospholipid Synthesis (map00564 )
- Glycine, Serine and Threonine Metabolism (map00260 )
|
| Enzyme 58 Reactions |
- ATP + ethanolamine = ADP + O-phosphoethanolamine [RN:R01468]
|
| Enzyme 58 Pfam Domain Function |
|
| Enzyme 58 Signals |
|
| Enzyme 58 Transmembrane Regions |
|
| Enzyme 58 Essentiality |
Not Available |
| Enzyme 58 GenBank ID Protein |
47078276 |
| Enzyme 58 UniProtKB/Swiss-Prot ID |
P35790 |
| Enzyme 58 UniProtKB/Swiss-Prot Entry Name |
CHKA_HUMAN |
| Enzyme 58 PDB ID |
Not Available |
| Enzyme 58 Cellular Location |
Not Available |
| Enzyme 58 Gene Sequence |
>1374 bp
ATGAAAACCAAATTCTGCACCGGGGGCGAGGCGGAGCCCTCGCCGCTCGGGCTGCTGCTG
AGCTGCGGTAGCGGCAGCGCGGCCCCGGCGCCCGGCGTGGGGCAGCAGCGCGACGCCGCC
AGCGACCTCGAGTCCAAGCAGCTGGGCGGCCAACAGCCGCCGCTCGCGCTGCCCCCTCCG
CCGCCGCTGCCGCTGCCGCTGCCGCTGCCCCAGCCCCCGCCGCCGCAGCCGCCCGCAGAC
GAGCAGCCGGAGCCCCGGACGCGGCGCAGGGCCTATCTGTGGTGCAAGGAGTTCCTGCCC
GGCGCCTGGCGGGGCCTCCGCGAGGACGAGTTCCACATCAGTGTCATCAGAGGCGGCCTT
AGCAACATGCTGTTCCAGTGCTCCCTACCTGACACCACAGCCACCCTTGGTGATGAGCCT
CGGAAAGTGCTCCTGCGGCTGTATGGAGCGATTTTGCAGATGAGGTCCTGTAATAAAGAG
GGATCCGAACAAGCTCAGAAAGAAAATGAATTTCAAGGGGCTGAGGCCATGGTTCTGGAG
AGCGTTATGTTTGCCATTCTCGCAGAGAGGTCACTTGGGCCAAAACTCTATGGCATCTTT
CCCCAAGGCCGACTGGAGCAGTTCATCCCGAGCCGGCGATTAGATACTGAAGAATTAAGT
TTGCCAGATATTTCTGCAGAAATCGCCGAGAAAATGGCTACATTTCATGGTATGAAAATG
CCATTCAATAAGGAACCAAAATGGCTTTTTGGCACAATGGAAAAGTATCTAAAGGAAGTG
CTGAGAATTAAATTTACTGAGGAATCCAGAATTAAAAAGCTCCACAAATTGCTCAGTTAC
AATCTGCCCTTGGAACTGGAAAACCTGAGATCATTGCTTGAATCTACTCCATCTCCAGTT
GTATTTTGTCATAATGACTGTCAAGAAGGTAATATCTTGTTGCTGGAAGGCCGAGAGAAT
TCTGAAAAACAGAAACTGATGCTCATTGATTTCGAATACAGCAGTTACAATTACAGGGGA
TTCGACATTGGAAATCACTTCTGTGAGTGGATGTATGATTATAGCTATGAAAAATACCCT
TTTTTCAGAGCAAACATCCGGAAGTATCCCACCAAGAAACAACAGCTCCATTTTATTTCC
AGTTACTTGCCTGCATTCCAAAATGACTTTGAAAACCTCAGTACTGAAGAAAAATCCATT
ATAAAAGAAGAAATGTTGCTTGAAGTTAATAGGTTTGCCCTTGCATCTCATTTCCTCTGG
GGACTGTGGTCCATTGTACAAGCCAAGATTTCATCTATTGAATTTGGGTACATGGACTAC
GCCCAAGCAAGGTTTGATGCCTATTTCCACCAGAAGAGGAAGCTTGGGGTGTGA
|
| Enzyme 58 GenBank Gene ID |
NM_001277.2 |
| Enzyme 58 GeneCard ID |
CHKA |
| Enzyme 58 GenAtlas ID |
CHKA |
| Enzyme 58 HGNC ID |
HGNC:1937 |
| Enzyme 58 Chromosome Location |
1 |
| Enzyme 58 Locus |
11q13.2 |
| Enzyme 58 SNPs |
SNPJam Report |
| Enzyme 58 General References |
- Hosaka K, Tanaka S, Nikawa J, Yamashita S: Cloning of a human choline kinase cDNA by complementation of the yeast cki mutation. FEBS Lett. 1992 Jun 15;304(2-3):229-32. [PubMed ]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Gallego-Ortega D, Ramirez de Molina A, Ramos MA, Valdes-Mora F, Barderas MG, Sarmentero-Estrada J, Lacal JC: Differential role of human choline kinase alpha and beta enzymes in lipid metabolism: implications in cancer onset and treatment. PLoS One. 2009 Nov 12;4(11):e7819. [PubMed ]
- Malito E, Sekulic N, Too WC, Konrad M, Lavie A: Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine. J Mol Biol. 2006 Nov 24;364(2):136-51. Epub 2006 Sep 3. [PubMed ]
|
| Enzyme 58 Metabolite References |
Not Available |
|
Enzyme 59
[top]
|
| Enzyme 59 ID |
6071 |
| Enzyme 59 Name |
Glutathione synthetase |
| Enzyme 59 Synonyms |
- GSH synthetase
- GSH-S
- Glutathione synthase
|
| Enzyme 59 Gene Name |
GSS |
| Enzyme 59 Protein Sequence |
>Glutathione synthetase
MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSA
LLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVF
LGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKIL
SNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFE
DISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQ
LAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSR
FVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVV
QCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV
|
| Enzyme 59 Number of Residues |
474 |
| Enzyme 59 Molecular Weight |
52384.3 |
| Enzyme 59 Theoretical pI |
5.73 |
| Enzyme 59 GO Classification |
| Function |
- ATP binding
- acid-amino acid ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- glutathione synthase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
|
| Process |
- cellular metabolic process
- glutathione biosynthetic process
- glutathione metabolic process
- metabolic process
- peptide metabolic process
|
| Component |
| — |
|
| Enzyme 59 General Function |
Involved in catalytic activity |
| Enzyme 59 Specific Function |
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione |
| Enzyme 59 Pathways |
|
| Enzyme 59 Reactions |
- ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione [RN:R00497]
|
| Enzyme 59 Pfam Domain Function |
|
| Enzyme 59 Signals |
|
| Enzyme 59 Transmembrane Regions |
|
| Enzyme 59 Essentiality |
Not Available |
| Enzyme 59 GenBank ID Protein |
Not Available |
| Enzyme 59 UniProtKB/Swiss-Prot ID |
P48637 |
| Enzyme 59 UniProtKB/Swiss-Prot Entry Name |
GSHB_HUMAN |
| Enzyme 59 PDB ID |
2HGS |
| Enzyme 59 PDB File |
Show |
| Enzyme 59 3D Structure |
|
| Enzyme 59 Cellular Location |
Not Available |
| Enzyme 59 Gene Sequence |
>1425 bp
ATGGCCACCAACTGGGGGAGCCTCTTGCAGGATAAACAGCAGCTAGAGGAGCTGGCACGG
CAGGCCGTGGACCGGGCCCTGGCTGAGGGAGTATTGCTGAGGACCTCACAGGAGCCCACT
TCCTCGGAGGTGGTGAGCTATGCCCCATTCACGCTCTTCCCCTCACTGGTCCCCAGTGCC
CTGCTGGAGCAAGCCTATGCTGTGCAGATGGACTTCAACCTGCTAGTGGATGCTGTCAGC
CAGAACGCTGCCTTCCTGGAGCAAACTCTTTCCAGCACCATCAAACAGGATGACTTTACC
GCTCGTCTCTTTGACATCCACAAGCAAGTCCTAAAAGAGGGCATTGCCCAGACTGTGTTC
CTGGGCCTGAATCGCTCAGACTACATGTTCCAGCGCAGCGCAGATGGCTCCCCAGCCCTG
AAACAGATCGAAATCAACACCATCTCTGCCAGCTTTGGGGGCCTGGCCTCCCGGACCCCA
GCTGTGCACCGACATGTTCTCAGTGTCCTGAGTAAGACCAAAGAAGCTGGCAAGATCCTC
TCTAATAATCCCAGCAAGGGACTGGCCCTGGGAATTGCCAAAGCCTGGGAGCTCTACGGC
TCACCCAATGCTCTGGTGCTACTGATTGCTCAAGAGAAGGAAAGAAACATATTTGACCAG
CGTGCCATAGAGAATGAGCTACTGGCCAGGAACATCCATGTGATCCGACGAACATTTGAA
GATATCTCTGAAAAGGGGTCTCTGGACCAAGACCGAAGGCTGTTTGTGGATGGCCAGGAA
ATTGCTGTGGTTTACTTCCGGGATGGCTACATGCCTCGTCAGTACAGTCTACAGAATTGG
GAAGCACGTCTACTGCTGGAGAGGTCACATGCTGCCAAGTGCCCAGACATTGCCACCCAG
CTGGCTGGGACTAAGAAGGTGCAGCAGGAGCTAAGCAGGCCGGGCATGCTGGAGATGTTG
CTCCCTGGCCAGCCTGAGGCTGTGGCCCGCCTCCGCGCCACCTTTGCTGGCCTCTACTCA
CTGGATGTGGGTGAAGAAGGGGACCAGGCCATCGCCGAGGCCCTTGCTGCCCCTAGCCGG
TTTGTGCTAAAGCCCCAGAGAGAGGGTGGAGGTAACAACCTATATGGGGAGGAAATGGTA
CAGGCCCTGAAACAGCTGAAGGACAGTGAGGAGAGGGCCTCCTACATCCTCATGGAGAAG
ATCGAACCTGAGCCTTTTGAGAATTGCCTGCTACGGCCTGGCAGCCCTGCCCGAGTGGTC
CAGTGCATTTCAGAGCTGGGCATCTTTGGGGTCTATGTCAGGCAGGAAAAGACACTCGTG
ATGAACAAGCACGTGGGGCATCTACTTCGAACCAAAGCCATCGAGCATGCAGATGGTGGT
GTGGCAGCGGGAGTGGCAGTCCTGGACAACCCATACCCTGTGTGA
|
| Enzyme 59 GenBank Gene ID |
L42531 |
| Enzyme 59 GeneCard ID |
GSS |
| Enzyme 59 GenAtlas ID |
GSS |
| Enzyme 59 HGNC ID |
HGNC:4624 |
| Enzyme 59 Chromosome Location |
2 |
| Enzyme 59 Locus |
20q11.2 |
| Enzyme 59 SNPs |
SNPJam Report |
| Enzyme 59 General References |
- Gali RR, Board PG: Sequencing and expression of a cDNA for human glutathione synthetase. Biochem J. 1995 Aug 15;310 ( Pt 1):353-8. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- 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 ]
- 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 ]
- Polekhina G, Board PG, Gali RR, Rossjohn J, Parker MW: Molecular basis of glutathione synthetase deficiency and a rare gene permutation event. EMBO J. 1999 Jun 15;18(12):3204-13. [PubMed ]
- Shi ZZ, Habib GM, Rhead WJ, Gahl WA, He X, Sazer S, Lieberman MW: Mutations in the glutathione synthetase gene cause 5-oxoprolinuria. Nat Genet. 1996 Nov;14(3):361-5. [PubMed ]
- Dahl N, Pigg M, Ristoff E, Gali R, Carlsson B, Mannervik B, Larsson A, Board P: Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction. Hum Mol Genet. 1997 Jul;6(7):1147-52. [PubMed ]
|
| Enzyme 59 Metabolite References |
Not Available |
|
Enzyme 60
[top]
|
| Enzyme 60 ID |
6076 |
| Enzyme 60 Name |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 |
| Enzyme 60 Synonyms |
- 6PF-2-K/Fru-2,6-P2ase 3
- PFK/FBPase 3
- 6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme
- Renal carcinoma antigen NY-REN-56
- iPFK-2
- 6-phosphofructo-2-kinase
- Fructose-2,6-bisphosphatase
|
| Enzyme 60 Gene Name |
PFKFB3 |
| Enzyme 60 Protein Sequence |
>6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3
MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLN
WIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQ
IAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNS
AEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLM
NIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQ
LKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTG
ESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKL
TPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFE
EHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH
|
| Enzyme 60 Number of Residues |
520 |
| Enzyme 60 Molecular Weight |
59608.6 |
| Enzyme 60 Theoretical pI |
8.29 |
| Enzyme 60 GO Classification |
| Function |
- 6-phosphofructo-2-kinase activity
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- fructose 2,6-bisphosphate metabolic process
- fructose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 60 General Function |
Involved in catalytic activity |
| Enzyme 60 Specific Function |
Synthesis and degradation of fructose 2,6-bisphosphate |
| Enzyme 60 Pathways |
- Fructose and Mannose Metabolism (map00051 )
|
| Enzyme 60 Reactions |
- beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate [RN:R00763]
|
| Enzyme 60 Pfam Domain Function |
|
| Enzyme 60 Signals |
|
| Enzyme 60 Transmembrane Regions |
|
| Enzyme 60 Essentiality |
Not Available |
| Enzyme 60 GenBank ID Protein |
2827312 |
| Enzyme 60 UniProtKB/Swiss-Prot ID |
Q16875 |
| Enzyme 60 UniProtKB/Swiss-Prot Entry Name |
F263_HUMAN |
| Enzyme 60 PDB ID |
Not Available |
| Enzyme 60 Cellular Location |
Not Available |
| Enzyme 60 Gene Sequence |
>1563 bp
ATGCCGTTGGAACTGACGCAGAGCCGAGTGCAGAAGATCTGGGTGCCCGTGGACCACAGG
CCCTCGTTGCCCAGATCCTGTGGGCCAAAGCTGACCAACTCCCCCACCGTCATCGTCATG
GTGGGCCTCCCCGCCCGGGGCAAGACCTACATCTCCAAGAAGCTGACTCGCTACCTCAAC
TGGATTGGCGTCCCCACAAAAGTGTTCAACGTCGGGGAGTATCGCCGGGAGGCTGTGAAG
CAGTACAGCTCCTACAACTTCTTCCGCCCCGACAATGAGGAAGCCATGAAAGTCCGGAAG
CAATGTGCCTTAGCTGCCTTGAGAGATGTCAAAAGCTACCTGGCGAAAGAAGGGGGACAA
ATTGCGGTTTTCGATGCCACCAATACTACTAGAGAGAGGAGACATGTGATCCTTCATTTT
GCCAAAGAAAATGACTTTAAGGCGTTTTTCATCGAGTCGGTGTGCGACGACCCTACAGTT
GTGGCCTCCAATATCATGGAAGTTAAAATCTCCAGCCCGGATTACAAAGACTGCAACTCG
GCAGAAGCCATGGACGACTTCATGAAGAGGATCAGTTGCTATGAAGCCAGCTACCAGCCC
CTCGACCCCGACAAATGCGACAGGGACTTGTCGCTGATCAAGGTGATTGACGTGGGCCGG
AGGTTCCTGGTGAACCGGGTGCAGGACCACATCCAGAGCCGCATCGTGTACTACCTGATG
AACATCCACGTGCAGCCGCGTACCATCTACCTGTGCCGGCACGGCGAGAACGAGCACAAC
CTCCAGGGCCGCATCGGGGGCGACTCAGGCCTGTCCAGCCGGGGCAAGAAGTTTGCCAGT
GCTCTGAGCAAGTTCGTGGAGGAGCAGAACCTGAAGGACCTGCGCGTGTGGACCAGCCAG
CTGAAGAGCACCATCCAGACGGCCGAGGCGCTGCGGCTGCCCTACGAGCAGTGGAAGGCG
CTCAATGAGATCGACGCGGGCGTCTGTGAGGAGCTGACCTACGAGGAGATCAGGGACACC
TACCCTGAGGAGTATGCGCTGCGGGAGCAGGACAAGTACTATTACCGCTACCCCACCGGG
GAGTCCTACCAGGACCTGGTCCAGCGCTTGGAGCCAGTGATCATGGAGCTGGAGCGGCAG
GAGAATGTGCTGGTCATCTGCCACCAGGCCGTCCTGCGCTGCCTGCTTGCCTACTTCCTG
GATAAGAGTGCAGAGGAGATGCCCTACCTGAAATGCCCTCTTCACACCGTCCTGAAACTG
ACGCCTGTCGCTTATGGCTGCCGTGTGGAATCCATCTACCTGAACGTGGAGTCCGTCTGC
ACACACCGGGAGAGGTCAGAGGATGCAAAGAAGGGACCTAACCCGCTCATGAGACGCAAT
AGTGTCACCCCGCTAGCCAGCCCCGAACCCACCAAAAAGCCTCGCATCAACAGCTTTGAG
GAGCATGTGGCCTCCACCTCGGCCGCCCTGCCCAGCTGCCTGCCCCCGGAGGTGCCCACG
CAGCTGCCTGGACAAAACATGAAAGGCTCCCGGAGCAGCGCTGACTCCTCCAGGAAACAC
TGA
|
| Enzyme 60 GenBank Gene ID |
AF041831 |
| Enzyme 60 GeneCard ID |
PFKFB3 |
| Enzyme 60 GenAtlas ID |
PFKFB3 |
| Enzyme 60 HGNC ID |
HGNC:8874 |
| Enzyme 60 Chromosome Location |
1 |
| Enzyme 60 Locus |
10p15.1 |
| Enzyme 60 SNPs |
SNPJam Report |
| Enzyme 60 General References |
- Sakai A, Kato M, Fukasawa M, Ishiguro M, Furuya E, Sakakibara R: Cloning of cDNA encoding for a novel isozyme of fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase from human placenta. J Biochem (Tokyo). 1996 Mar;119(3):506-11. [PubMed ]
- Manzano A, Rosa JL, Ventura F, Perez JX, Nadal M, Estivill X, Ambrosio S, Gil J, Bartrons R: Molecular cloning, expression, and chromosomal localization of a ubiquitously expressed human 6-phosphofructo-2-kinase/ fructose-2, 6-bisphosphatase gene (PFKFB3). Cytogenet Cell Genet. 1998;83(3-4):214-7. [PubMed ]
- Chesney J, Mitchell R, Benigni F, Bacher M, Spiegel L, Al-Abed Y, Han JH, Metz C, Bucala R: An inducible gene product for 6-phosphofructo-2-kinase with an AU-rich instability element: role in tumor cell glycolysis and the Warburg effect. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):3047-52. [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 ]
- Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed ]
- 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 ]
|
| Enzyme 60 Metabolite References |
Not Available |
|
Enzyme 61
[top]
|
| Enzyme 61 ID |
6078 |
| Enzyme 61 Name |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 |
| Enzyme 61 Synonyms |
- 6PF-2-K/Fru-2,6-P2ase 4
- PFK/FBPase 4
- 6PF-2-K/Fru-2,6-P2ase testis-type isozyme
- 6-phosphofructo-2-kinase
- Fructose-2,6-bisphosphatase
|
| Enzyme 61 Gene Name |
PFKFB4 |
| Enzyme 61 Protein Sequence |
>6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4
MASPRELTQNPLKKIWMPYSNGRPALHACQRGVCMTNCPTLIVMVGLPARGKTYISKKLT
RYLNWIGVPTREFNVGQYRRDVVKTYKSFEFFLPDNEEGLKIRKQCALAALRDVRRFLSE
EGGHVAVFDATNTTRERRATIFNFGEQNGYKTFFVESICVDPEVIAANIVQVKLGSPDYV
NRDSDEATEDFMRRIECYENSYESLDEDLDRDLSYIKIMDVGQSYVVNRVADHIQSRIVY
YLMNIHVTPRSIYLCRHGESELNLKGRIGGDPGLSPRGREFAKSLAQFISDQNIKDLKVW
TSQMKRTIQTAEALGVPYEQWKVLNEIDAGVCEEMTYEEIQDNYPLEFALRDQDKYRYRY
PKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKAAEQLPYLKCPLHTV
LKLTPVAYGCKVESIFLNVAAVNTHRDRPQNVDISRPPEEALVTVPAHQ
|
| Enzyme 61 Number of Residues |
469 |
| Enzyme 61 Molecular Weight |
54039.3 |
| Enzyme 61 Theoretical pI |
6.60 |
| Enzyme 61 GO Classification |
| Function |
- 6-phosphofructo-2-kinase activity
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- fructose 2,6-bisphosphate metabolic process
- fructose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 61 General Function |
Involved in catalytic activity |
| Enzyme 61 Specific Function |
Synthesis and degradation of fructose 2,6-bisphosphate |
| Enzyme 61 Pathways |
- Fructose and Mannose Metabolism (map00051 )
|
| Enzyme 61 Reactions |
- beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate [RN:R00763]
|
| Enzyme 61 Pfam Domain Function |
|
| Enzyme 61 Signals |
|
| Enzyme 61 Transmembrane Regions |
|
| Enzyme 61 Essentiality |
Not Available |
| Enzyme 61 GenBank ID Protein |
Not Available |
| Enzyme 61 UniProtKB/Swiss-Prot ID |
Q16877 |
| Enzyme 61 UniProtKB/Swiss-Prot Entry Name |
F264_HUMAN |
| Enzyme 61 PDB ID |
1BIF |
| Enzyme 61 PDB File |
Show |
| Enzyme 61 3D Structure |
|
| Enzyme 61 Cellular Location |
Not Available |
| Enzyme 61 Gene Sequence |
>1410 bp
ATGGCGTCCCCACGGGAATTGACACAGAACCCCCTGAAGAAGATCTGGATGCCATACAGC
AATGGGCGGCCCGCTCTGCACGCTTGCCAGCGCGGTGTGTGCATGACCAACTGCCCAACT
CTCATTGTCATGGTGGGCCTGCCCGCCAGGGGCAAGACCTACATCTCCAAGAAGCTGACT
CGATACCTGAACTGGATTGGTGTGCCCACTCGGGAGTTCAATGTTGGCCAGTACCGCCGG
GACGTGGTCAAGACCTACAAATCTTTTGAATTTTTTCTCCCCGACAATGAAGAGGGCCTG
AAAATCAGGAAGCAGTGTGCCCTGGCAGCCCTCCGTGACGTCCGGCGGTTCCTTAGTGAG
GAGGGGGGACATGTGGCGGTTTTTGATGCCACAAACACCACCCGAGAACGGAGAGCGACC
ATCTTTAATTTTGGAGAACAGAATGGCTACAAGACCTTTTTTGTCGAGTCCATCTGTGTG
GATCCTGAGGTCATAGCTGCCAACATCGTGCAAGTGAAACTGGGCAGCCCTGACTATGTC
AACCGCGACAGTGATGAGGCTACGGAGGACTTCATGAGGCGCATTGAGTGCTATGAGAAC
TCCTACGAGTCGCTAGATGAGGACCTGGATAGGGACCTGTCCTATATCAAGATCATGGAT
GTGGGCCAGAGCTACGTGGTGAACCGTGTGGCTGACCACATCCAGAGCCGCATCGTATAT
TACCTCATGAACATCCACGTGACCCCCCGCTCCATCTACCTCTGCCGGCACGGGGAGAGC
GAGCTCAACCTCAAGGGCCGGATTGGCGGGGACCCAGGACTGTCCCCTCGGGGCAGGGAG
TTTGCCAAGAGTCTAGCCCAGTTCATCAGTGACCAAAATATCAAGGATCTGAAGGTCTGG
ACAAGCCAGATGAAGAGGACAATCCAGACGGCTGAGGCACTGGGTGTGCCCTATGAACAG
TGGAAGGTCCTCAACGAGATCGATGCGGGCGTCTGTGAGGAAATGACCTACGAGGAAATT
CAGGATAATTATCCACTGGAGTTCGCCCTGCGGGACCAGGACAAGTACCGGTACCGGTAC
CCTAAAGGGGAGTCCTACGAGGACCTGGTCCAGAGACTGGAGCCTGTCATCATGGAGCTG
GAGAGGCAAGAGAATGTGCTGGTCATCTGCCACCAGGCTGTGATGCGCTGCCTGCTGGCC
TACTTCCTCGACAAGGCAGCAGAACAGCTGCCCTACCTCAAGTGTCCGCTGCACACAGTC
CTGAAGCTGACTCCTGTGGCATATGGTTGTAAAGTGGAGTCCATATTCCTGAACGTGGCT
GCTGTGAACACGCACCGGGACAGGCCTCAGAACGTGGACATCTCAAGACCTCCAGAGGAA
GCCCTTGTCACGGTGCCTGCTCACCAGTGA
|
| Enzyme 61 GenBank Gene ID |
D49818 |
| Enzyme 61 GeneCard ID |
PFKFB4 |
| Enzyme 61 GenAtlas ID |
PFKFB4 |
| Enzyme 61 HGNC ID |
HGNC:8875 |
| Enzyme 61 Chromosome Location |
3 |
| Enzyme 61 Locus |
3p22-p21 |
| Enzyme 61 SNPs |
SNPJam Report |
| Enzyme 61 General References |
- Manzano A, Perez JX, Nadal M, Estivill X, Lange A, Bartrons R: Cloning, expression and chromosomal localization of a human testis 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene. Gene. 1999 Mar 18;229(1-2):83-9. [PubMed ]
- Gomez M, Manzano A, Navarro-Sabate A, Duran J, Obach M, Perales JC, Bartrons R: Specific expression of pfkfb4 gene in spermatogonia germ cells and analysis of its 5'-flanking region. FEBS Lett. 2005 Jan 17;579(2):357-62. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Sakai A, Kato M, Fukasawa M, Ishiguro M, Furuya E, Sakakibara R: Cloning of cDNA encoding for a novel isozyme of fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase from human placenta. J Biochem (Tokyo). 1996 Mar;119(3):506-11. [PubMed ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 61 Metabolite References |
Not Available |
|
Enzyme 62
[top]
|
| Enzyme 62 ID |
6079 |
| Enzyme 62 Name |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 |
| Enzyme 62 Synonyms |
- 6PF-2-K/Fru-2,6-P2ase 1
- PFK/FBPase 1
- 6PF-2-K/Fru-2,6-P2ase liver isozyme
- 6-phosphofructo-2-kinase
- Fructose-2,6-bisphosphatase
|
| Enzyme 62 Gene Name |
PFKFB1 |
| Enzyme 62 Protein Sequence |
>6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1
MSPEMGELTQTRLQKIWIPHSSGSSRLQRRRGSSIPQFTNSPTMVIMVGLPARGKTYIST
KLTRYLNWIGTPTKVFNLGQYRREAVSYKNYEFFLPDNMEALQIRKQCALAALKDVHNYL
SHEEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPGIIAENIRQVKLGSPD
YIDCDREKVLEDFLKRIECYEVNYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHIQSRT
VYYLMNIHVTPRSIYLCRHGESELNIRGRIGGDSGLSVRGKQYAYALANFIQSQGISSLK
VWTSHMKRTIQTAEALGVPYEQWKALNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRY
RYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKSSDELPYLKCPLH
TVLKLTPVAYGCKVESIYLNVEAVNTHREKPENVDITREPEEALDTVPAHY
|
| Enzyme 62 Number of Residues |
471 |
| Enzyme 62 Molecular Weight |
54680.9 |
| Enzyme 62 Theoretical pI |
6.56 |
| Enzyme 62 GO Classification |
| Function |
- 6-phosphofructo-2-kinase activity
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- fructose 2,6-bisphosphate metabolic process
- fructose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 62 General Function |
Involved in catalytic activity |
| Enzyme 62 Specific Function |
Synthesis and degradation of fructose 2,6-bisphosphate |
| Enzyme 62 Pathways |
- Fructose and Mannose Metabolism (map00051 )
|
| Enzyme 62 Reactions |
- beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate [RN:R00763]
|
| Enzyme 62 Pfam Domain Function |
|
| Enzyme 62 Signals |
|
| Enzyme 62 Transmembrane Regions |
|
| Enzyme 62 Essentiality |
Not Available |
| Enzyme 62 GenBank ID Protein |
35503 |
| Enzyme 62 UniProtKB/Swiss-Prot ID |
P16118 |
| Enzyme 62 UniProtKB/Swiss-Prot Entry Name |
F261_HUMAN |
| Enzyme 62 PDB ID |
1K6M |
| Enzyme 62 PDB File |
Show |
| Enzyme 62 3D Structure |
|
| Enzyme 62 Cellular Location |
Not Available |
| Enzyme 62 Gene Sequence |
>1416 bp
ATGTCTCCAGAGATGGGAGAGCTCACCCAAACCAGGTTGCAGAAGATCTGGATTCCACAC
AGCAGCGGCAGCAGCAGGCTGCAACGGAGAAGGGGCTCATCCATACCCCAGTTTACCAAT
TCCCCCACAATGGTGATCATGGTGGGTTTACCAGCTCGAGGCAAGACCTATATCTCCACA
AAGCTCACACGATATCTCAACTGGATAGGAACACCAACTAAAGTGTTTAATTTAGGCCAG
TATCGACGAGAGGCAGTGAGCTACAAGAACTATGAATTCTTTCTTCCAGACAACATGGAA
GCCCTGCAAATCAGGAAGCAGTGCGCCCTGGCAGCCCTGAAGGATGTTCACAACTATCTC
AGCCATGAGGAAGGTCATGTTGCGGTTTTTGATGCCACCAACACTACCAGAGAACGACGG
TCACTGATCCTGCAGTTTGCAAAAGAACATGGTTACAAGGTGTTTTTCATTGAGTCCATT
TGTAATGACCCTGGCATAATTGCAGAAAACATCAGGCAAGTGAAACTTGGCAGCCCTGAT
TATATAGACTGTGACCGGGAAAAGGTTCTGGAAGACTTTCTAAAGAGAATTGAGTGCTAT
GAGGTCAACTACCAACCCTTGGATGAGGAACTGGACAGCCACCTGTCCTACATCAAGATC
TTCGACGTGGGCACACGCTACATGGTGAACCGAGTGCAGGATCACATCCAGAGCCGCACA
GTCTACTACCTCATGAATATCCATGTCACACCTCGCTCCATCTACCTTTGCCGACATGGC
GAGAGTGAACTCAACATCAGAGGCCGCATCGGAGGTGACTCTGGCCTCTCAGTTCGCGGC
AAGCAGTATGCCTATGCCCTGGCCAACTTCATTCAGTCCCAGGGCATCAGCTCCCTGAAG
GTGTGGACCAGTCGCATGAAGAGGACCATCCAGACAGCTGAGGCCCTGGGTGTCCCCTAT
GAGCAGTGGAAGGCCCTGAATGAGATTGATGCGGGTGTCTGTGAGGAGATGACCTATGAA
GAAATCCAGGAACATTACCCTGAAGAATTTGCACTGCGAGACCAAGATAAATATCGCTAC
CGCTATCCCAAGGGAGAGTCCTATGAGGATCTGGTTCAGCGTCTGGAGCCAGTGATAATG
GAGCTAGAACGACAGGAGAATGTACTGGTGATCTGCCACCAGGCTGTCATGCGGTGCCTC
CTGGCCTATTTCCTGGATAAAAGTTCAGATGAGCTTCCATATCTCAAGTGCCCTCTGCAC
ACAGTGCTCAAACTCACTCCTGTGGCTTATGGCTGCAAAGTGGAATCCATCTACCTGAAT
GTGGAGGCCGTGAACACACACCGGGAGAAGCCTGAGAATGTGGACATCACCCGGGAACCT
GAGGAAGCCCTGGATACTGTCCCAGCCCACTACTGA
|
| Enzyme 62 GenBank Gene ID |
X52638 |
| Enzyme 62 GeneCard ID |
PFKFB1 |
| Enzyme 62 GenAtlas ID |
PFKFB1 |
| Enzyme 62 HGNC ID |
HGNC:8872 |
| Enzyme 62 Chromosome Location |
Not Available |
| Enzyme 62 Locus |
Not Available |
| Enzyme 62 SNPs |
SNPJam Report |
| Enzyme 62 General References |
- Lange AJ, Pilkis SJ: Sequence of human liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Nucleic Acids Res. 1990 Jun 25;18(12):3652. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Algaier J, Uyeda K: Molecular cloning, sequence analysis, and expression of a human liver cDNA coding for fructose-6-P,2-kinase:fructose-2,6-bisphosphatase. Biochem Biophys Res Commun. 1988 May 31;153(1):328-33. [PubMed ]
|
| Enzyme 62 Metabolite References |
Not Available |
|
Enzyme 63
[top]
|
| Enzyme 63 ID |
6084 |
| Enzyme 63 Name |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 |
| Enzyme 63 Synonyms |
- 6PF-2-K/Fru-2,6-P2ase 2
- PFK/FBPase 2
- 6PF-2-K/Fru-2,6-P2ase heart-type isozyme
- 6-phosphofructo-2-kinase
- Fructose-2,6-bisphosphatase
|
| Enzyme 63 Gene Name |
PFKFB2 |
| Enzyme 63 Protein Sequence |
>6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2
MSGASSSEQNNNSYETKTPNLRMSEKKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTR
YLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQCALVALEDVKAYLTEE
NGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVESVCDDPDVIAANILEVKVSSPDYPE
RNRENVMEDFLKRIECYKVTYRPLDPDNYDKDLSFIKVINVGQRFLVNRVQDYIQSKIVY
YLMNIHVQPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQFAQALRKFLEEQEITDLKVW
TSQLKRTIQTAESLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRY
PGGESYQDLVQRLEPVIMELERQGNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTI
FKLTPVAYGCKVETIKLNVEAVNTHRDKPTNNFPKNQTPVRMRRNSFTPLSSSNTIRRPR
NYSVGSRPLKPLSPLRAQDMQEGAD
|
| Enzyme 63 Number of Residues |
505 |
| Enzyme 63 Molecular Weight |
58476.3 |
| Enzyme 63 Theoretical pI |
8.54 |
| Enzyme 63 GO Classification |
| Function |
- 6-phosphofructo-2-kinase activity
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- fructose 2,6-bisphosphate metabolic process
- fructose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 63 General Function |
Involved in catalytic activity |
| Enzyme 63 Specific Function |
Synthesis and degradation of fructose 2,6-bisphosphate |
| Enzyme 63 Pathways |
- Fructose and Mannose Metabolism (map00051 )
|
| Enzyme 63 Reactions |
- beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate [RN:R00763]
|
| Enzyme 63 Pfam Domain Function |
|
| Enzyme 63 Signals |
|
| Enzyme 63 Transmembrane Regions |
|
| Enzyme 63 Essentiality |
Not Available |
| Enzyme 63 GenBank ID Protein |
64762406 |
| Enzyme 63 UniProtKB/Swiss-Prot ID |
O60825 |
| Enzyme 63 UniProtKB/Swiss-Prot Entry Name |
F262_HUMAN |
| Enzyme 63 PDB ID |
Not Available |
| Enzyme 63 Cellular Location |
Not Available |
| Enzyme 63 Gene Sequence |
>1518 bp
ATGTCTGGGGCATCTTCCTCAGAACAGAACAACAACAGCTATGAAACCAAAACCCCAAAT
CTTCGAATGTCAGAGAAGAAATGTTCATGGGCCTCCTACATGACCAACTCCCCGACTCTG
ATCGTTATGATTGGTTTGCCAGCCCGGGGTAAAACCTACGTGTCCAAGAAACTAACACGC
TACCTCAACTGGATTGGAGTCCCCACCAAAGTGTTTAATCTTGGGGTGTATCGGCGTGAA
GCAGTCAAGTCCTATAAGTCCTACGACTTCTTTCGGCATGACAATGAGGAGGCCATGAAG
ATCCGCAAACAGTGTGCTCTGGTGGCGCTGGAAGATGTTAAGGCGTATCTCACTGAGGAG
AATGGTCAGATTGCGGTGTTTGATGCCACCAATACAACCCGGGAGAGGAGGGACATGATT
TTGAACTTTGCTGAACAGAATTCCTTCAAGGTATTCTTTGTGGAATCCGTCTGTGATGAT
CCTGATGTCATTGCTGCCAATATTCTGGAGGTTAAGGTATCAAGCCCTGACTATCCTGAA
AGGAACAGAGAGAACGTGATGGAGGACTTCCTGAAGAGAATTGAATGCTACAAAGTTACC
TACCGACCTCTTGACCCAGACAACTATGACAAGGATCTTTCTTTCATCAAGGTGATAAAC
GTGGGCCAGCGATTTTTAGTCAACAGAGTCCAGGACTACATCCAGAGCAAGATAGTCTAC
TACCTCATGAATATCCACGTCCAGCCTCGCACCATTTACCTTTGCCGGCATGGAGAAAGC
GAGTTCAATCTCTTGGGGAAGATTGGGGGTGACTCTGGCCTCTCGGTGCGGGGAAAGCAG
TTTGCCCAAGCTCTAAGGAAATTTCTGGAGGAACAGGAAATAACAGACCTCAAAGTGTGG
ACAAGCCAGTTGAAGAGGACCATACAGACTGCTGAATCTCTCGGGGTGCCCTATGAGCAG
TGGAAGATTCTGAATGAGATTGATGCTGGTGTGTGTGAAGAGATGACCTATGCAGAGATT
GAGAAACGGTACCCAGAAGAGTTTGCACTTCGAGATCAAGAGAAGTATCTGTATCGATAT
CCTGGTGGGGAGTCATACCAGGACCTGGTGCAGCGGCTGGAGCCTGTCATCATGGAGCTG
GAACGTCAGGGCAATGTCCTCGTCATCTCCCACCAGGCTGTCATGCGCTGCCTCCTGGCC
TACTTCTTGGATAAGGGCGCAGATGAGCTACCATACTTGAGATGCCCTCTCCATACCATC
TTCAAACTTACTCCTGTGGCCTATGGGTGCAAAGTGGAAACAATTAAACTTAACGTGGAG
GCTGTGAACACGCACCGTGACAAGCCAACTAACAACTTCCCCAAGAACCAAACCCCTGTA
AGGATGAGAAGGAACAGCTTTACGCCTCTGTCCAGTTCGAATACAATAAGGCGTCCAAGA
AATTACAGTGTTGGGAGCCGGCCCCTCAAGCCCCTCAGCCCTCTCCGTGCCCAGGACATG
CAAGAAGGGGCCGACTAG
|
| Enzyme 63 GenBank Gene ID |
NM_006212.2 |
| Enzyme 63 GeneCard ID |
PFKFB2 |
| Enzyme 63 GenAtlas ID |
PFKFB2 |
| Enzyme 63 HGNC ID |
HGNC:8873 |
| Enzyme 63 Chromosome Location |
1 |
| Enzyme 63 Locus |
1q31 |
| Enzyme 63 SNPs |
SNPJam Report |
| Enzyme 63 General References |
- Heine-Suner D, Diaz-Guillen MA, Lange AJ, Rodriguez de Cordoba S: Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2). Eur J Biochem. 1998 May 15;254(1):103-10. [PubMed ]
- Soejima H, Kawamoto S, Akai J, Miyoshi O, Arai Y, Morohka T, Matsuo S, Niikawa N, Kimura A, Okubo K, Mukai T: Isolation of novel heart-specific genes using the BodyMap database. Genomics. 2001 May 15;74(1):115-20. [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 ]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- 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 63 Metabolite References |
Not Available |
|
Enzyme 64
[top]
|
| Enzyme 64 ID |
6116 |
| Enzyme 64 Name |
Glycerol kinase 2 |
| Enzyme 64 Synonyms |
- GK 2
- Glycerokinase 2
- ATP:glycerol 3-phosphotransferase 2
- Glycerol kinase, testis specific 2
|
| Enzyme 64 Gene Name |
GK2 |
| Enzyme 64 Protein Sequence |
>Glycerol kinase 2
MAAPKTAAVGPLVGAVVQGTNSTRFLVFNSKTAELLSHHKVELTQEFPKEGWVEQDPKEI
LQSVYECIARTCEKLDELNIDISNIKAVGVSNQRETTVIWDKLTGEPLYNAVVWLDLRTQ
TTVEDLSKKIPGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVEEGRALFGTIDS
WLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIY
GLIKTGALEGVPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGL
LTTVAYKLGREKPAYYALEGSVAIAGAVIRWLRDNLGIIETSGDIERLAKEVGTSYGCYF
VPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEAMNRDCGIPLR
HLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTALGAAMAAGAAEGVSVWSLEPQALS
VLRMERFEPQIQATESEIRYATWKKAVMKSMGWVTSQSPEGGDPSIFSSLPLGFFIVSSM
VMLIGARYISGVP
|
| Enzyme 64 Number of Residues |
553 |
| Enzyme 64 Molecular Weight |
60593.3 |
| Enzyme 64 Theoretical pI |
5.53 |
| Enzyme 64 GO Classification |
| Function |
- catalytic activity
- glycerol kinase activity
- kinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- alditol metabolic process
- carbohydrate metabolic process
- glycerol metabolic process
- glycerol-3-phosphate metabolic process
- metabolic process
- polyol metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 64 General Function |
Involved in phosphotransferase activity, alcohol group as acceptor |
| Enzyme 64 Specific Function |
Key enzyme in the regulation of glycerol uptake and metabolism |
| Enzyme 64 Pathways |
|
| Enzyme 64 Reactions |
- ATP + glycerol = ADP + sn-glycerol 3-phosphate [RN:R00847]
|
| Enzyme 64 Pfam Domain Function |
|
| Enzyme 64 Signals |
|
| Enzyme 64 Transmembrane Regions |
|
| Enzyme 64 Essentiality |
Not Available |
| Enzyme 64 GenBank ID Protein |
158257914 |
| Enzyme 64 UniProtKB/Swiss-Prot ID |
Q14410 |
| Enzyme 64 UniProtKB/Swiss-Prot Entry Name |
GLPK2_HUMAN |
| Enzyme 64 PDB ID |
Not Available |
| Enzyme 64 Cellular Location |
Not Available |
| Enzyme 64 Gene Sequence |
>1662 bp
ATGGCAGCCCCGAAGACAGCAGCTGTGGGGCCGTTGGTGGGAGCGGTGGTCCAGGGCACC
AACTCCACTCGCTTTCTGGTTTTCAATTCAAAAACAGCGGAACTACTTAGTCATCACAAA
GTGGAATTAACACAAGAGTTCCCAAAAGAAGGATGGGTGGAACAAGACCCTAAAGAAATT
CTTCAGTCTGTCTACGAGTGTATAGCGAGAACGTGTGAGAAACTTGACGAACTGAATATT
GATATATCCAACATAAAAGCTGTTGGTGTCAGCAATCAGAGGGAAACCACTGTAATCTGG
GACAAGTTAACAGGAGAGCCTCTCTACAATGCTGTGGTGTGGCTTGATCTAAGAACCCAG
ACTACTGTTGAGGATCTTAGTAAAAAAATTCCAGGAAATAGTAACTTCGTCAAGTCTAAG
ACAGGCCTTCCACTCAGCACTTACTTCAGTGCAGTAAAACTTCGTTGGATGCTTGACAAT
GTGAGAAACGTCCAAAAGGCTGTTGAAGAAGGTAGAGCTCTTTTTGGTACCATTGATTCA
TGGCTTATCTGGAGTTTGACAGGAGGAGTTAATGGAGGCGTGCATTGTACAGATGTAACA
AATGCAAGTAGGACAATGCTTTTTAATATCCATTCTTTGGAATGGGATAAAGAGCTCTGT
GACTTTTTTGAAATTCCAATGGACCTTCTTCCAAATGTCTTCAGTTCTTCTGGGATCTAT
GGCCTAATTAAAACTGGAGCCCTGGAAGGTGTGCCAATATCTGGGTGTTTGGGGGACCAA
TGTGCTGCATTAGTAGGACAAATGTGCTTCCAGGAGGGACAAGCCAAAAACACCTATGGA
ACAGGTTGCTTCTTACTGTGTAATACGGGTCGTAAATGTGTGTTTTCTGAACATGGCCTT
TTGACCACAGTAGCTTACAAACTAGGCAGAGAGAAGCCAGCATATTATGCACTGGAAGGT
TCTGTTGCTATAGCAGGTGCTGTTATTCGTTGGCTAAGAGACAATCTTGGAATTATAGAG
ACCTCAGGAGACATTGAAAGACTTGCTAAAGAAGTAGGAACTTCTTATGGCTGTTACTTT
GTCCCAGCCTTTTCAGGGTTATATACACCTTATTGGGAGCCTAGTGCAAGAGGGATACTC
TGTGGCCTCACTCAGTTTACCAATAAATGTCATATTGCTTTTGCTGCATTAGAAGCTGTT
TGTTTCCAAACCCGAGAGATTTTGGAAGCCATGAACCGTGACTGTGGAATTCCACTTCGT
CATTTGCAGGTAGATGGAGGAATGACCAACAACAAAGTTCTTATGCAGCTACAAGCAGAT
ATTCTTCATATTCCAGTAATAAAACCCTTTATGCCTGAAACAACTGCACTAGGAGCTGCC
ATGGCAGCAGGGGCTGCAGAGGGAGTAAGCGTTTGGAGCCTTGAACCCCAGGCTTTGTCA
GTTCTCAGGATGGAACGATTTGAACCACAGATCCAGGCCACAGAAAGTGAAATTTGTTAT
GCCACATGGAAGAAAGCCGTAATGAAGTCAATGGGTTGGGTTACCAGTCAGTCTCCTGAA
GGTGGTGATCCTTCTATCTTCTCTAGTCTGCCTTTGGGATTTTTTATAGTGAGTAGCATG
GTAATGCTAATTGGAGCAAGATATATCTCGGGTGTGCCATAA
|
| Enzyme 64 GenBank Gene ID |
AK292241 |
| Enzyme 64 GeneCard ID |
GK2 |
| Enzyme 64 GenAtlas ID |
GK2 |
| Enzyme 64 HGNC ID |
HGNC:4291 |
| Enzyme 64 Chromosome Location |
4 |
| Enzyme 64 Locus |
4q13 |
| Enzyme 64 SNPs |
SNPJam Report |
| Enzyme 64 General References |
- Sargent CA, Young C, Marsh S, Ferguson-Smith MA, Affara NA: The glycerol kinase gene family: structure of the Xp gene, and related intronless retroposons. Hum Mol Genet. 1994 Aug;3(8):1317-24. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 64 Metabolite References |
Not Available |
|
Enzyme 65
[top]
|
| Enzyme 65 ID |
6117 |
| Enzyme 65 Name |
Glycerol kinase |
| Enzyme 65 Synonyms |
- GK
- Glycerokinase
- ATP:glycerol 3-phosphotransferase
|
| Enzyme 65 Gene Name |
GK |
| Enzyme 65 Protein Sequence |
>Glycerol kinase
MAASKKAVLGPLVGAVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEI
LHSVYECIEKTCEKLGQLNIDISNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQ
STVESLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDS
WLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIY
GLMKISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCV
FSDHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGT
SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRD
CGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMAAGAAEGVGVWSL
EPEDLSAVTMERFEPQINAEESEIRYSTWKKAVMKSMGWVTTQSPESGDPSIFCSLPLGF
FIVSSMVMLIGARYISGIP
|
| Enzyme 65 Number of Residues |
559 |
| Enzyme 65 Molecular Weight |
61244.1 |
| Enzyme 65 Theoretical pI |
6.50 |
| Enzyme 65 GO Classification |
| Function |
- catalytic activity
- glycerol kinase activity
- kinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- alditol metabolic process
- carbohydrate metabolic process
- glycerol metabolic process
- glycerol-3-phosphate metabolic process
- metabolic process
- polyol metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 65 General Function |
Involved in phosphotransferase activity, alcohol group as acceptor |
| Enzyme 65 Specific Function |
Key enzyme in the regulation of glycerol uptake and metabolism |
| Enzyme 65 Pathways |
|
| Enzyme 65 Reactions |
- ATP + glycerol = ADP + sn-glycerol 3-phosphate [RN:R00847]
|
| Enzyme 65 Pfam Domain Function |
|
| Enzyme 65 Signals |
|
| Enzyme 65 Transmembrane Regions |
|
| Enzyme 65 Essentiality |
Not Available |
| Enzyme 65 GenBank ID Protein |
5834428 |
| Enzyme 65 UniProtKB/Swiss-Prot ID |
P32189 |
| Enzyme 65 UniProtKB/Swiss-Prot Entry Name |
GLPK_HUMAN |
| Enzyme 65 PDB ID |
Not Available |
| Enzyme 65 Cellular Location |
Not Available |
| Enzyme 65 Gene Sequence |
>1680 bp
ATGGCAGCCTCAAAGAAGGCAGTTTTGGGGCCATTGGTGGGGGCGGTGGACCAGGGCACC
AGTTCGACGCGCTTTTTGGTTTTCAATTCAAAAACAGCTGAACTACTTAGTCATCATCAA
GTAGAAATAAAACAAGAGTTCCCAAGAGAAGGATGGGTGGAACAGGACCCTAAGGAAATT
CTACATTCTGTCTATGAGTGTATAGAGAAAACATGTGAGAAACTTGGACAGCTCAATATT
GATATTTCCAACATAAAAGCTATTGGTGTCAGCAACCAGAGGGAAACCACTGTAGTCTGG
GACAAGATAACTGGAGAGCCTCTCTACAATGCTGTGGTGTGGCTTGATCTAAGAACCCAG
TCTACCGTTGAGAGTCTTAGTAAAAGAATTCCAGGAAATAATAACTTTGTCAAGTCCAAG
ACAGGCCTTCCACTTAGCACTTACTTCAGTGCAGTGAAACTTCGTTGGCTCCTTGACAAT
GTGAGAAAAGTTCAAAAGGCCGTTGAAGAAAAACGAGCTCTTTTTGGGACTATTGATTCA
TGGCTTATTTGGAGTTTGACAGGAGGAGTCAATGGAGGTGTCCACTGTACAGATGTAACA
AATGCAAGTAGGACTATGCTTTTCAACATTCATTCTTTGGAATGGGATAAACAACTCTGC
GAATTTTTTGGAATTCCAATGGAAATTCTTCCAAATGTCCGGAGTTCTTCTGAGATCTAT
GGCCTAATGAAAATCTCTCATAGCGTGAAAGCTGGGGCCTTGGAAGGTGTGCCAATATCT
GGGTGTTTAGGGGACCAGTCTGCTGCATTGGTGGGACAAATGTGCTTCCAGATTGGACAA
GCCAAAAATACGTATGGAACAGGATGTTTCTTACTATGTAATACAGGCCATAAGTGTGTA
TTTTCTGATCATGGCCTTCTCACCACAGTGGCTTACAAACTTGGCAGAGACAAACCAGTA
TATTATGCTTTGGAAGGTTCTGTAGCTATAGCTGGTGCTGTTATTCGCTGGCTAAGAGAC
AATCTTGGAATTATAAAGACCTCAGAAGAAATTGAAAAACTTGCTAAAGAAGTAGGTACT
TCTTATGGCTGCTACTTCGTCCCAGCATTTTCGGGGTTATATGCACCTTATTGGGAGCCC
AGCGCAAGAGGGATAATCTGTGGACTCACTCAGTTCACCAATAAATGCCATATTGCTTTT
GCTGCATTAGAAGCTGTTTGTTTCCAAACTCGAGAGATTTTGGATGCCATGAATCGAGAC
TGTGGAATTCCACTCAGTCATTTGCAGGTAGATGGAGGAATGACCAGCAACAAAATTCTT
ATGCAGCTACAAGCAGACATTCTGTATATACCAGTAGTGAAGCCCTCAATGCCCGAAACC
ACTGCACTGGGTGCGGCTATGGCGGCAGGGGCTGCAGAAGGAGTCGGCGTATGGAGTCTC
GAACCCGAGGATTTGTCTGCCGTCACGATGGAGCGGTTTGAACCTCAGATTAATGCGGAG
GAAAGTGAAATTCGTTATTCTACATGGAAGAAAGCTGTGATGAAGTCAATGGGTTGGGTT
ACAACTCAATCTCCAGAAAGTGGTGACCCTAGTATCTTCTGTAGTCTGCCCTTGGGCTTT
TTTATAGTGAGTAGCATGGTAATGTTAATCGGAGCAAGGTACATCTCAGGTATTCCATAA
|
| Enzyme 65 GenBank Gene ID |
AJ252550 |
| Enzyme 65 GeneCard ID |
GK |
| Enzyme 65 GenAtlas ID |
GK |
| Enzyme 65 HGNC ID |
HGNC:4289 |
| Enzyme 65 Chromosome Location |
Not Available |
| Enzyme 65 Locus |
Not Available |
| Enzyme 65 SNPs |
SNPJam Report |
| Enzyme 65 General References |
- Guo W, Worley K, Adams V, Mason J, Sylvester-Jackson D, Zhang YH, Towbin JA, Fogt DD, Madu S, Wheeler DA, et al.: Genomic scanning for expressed sequences in Xp21 identifies the glycerol kinase gene. Nat Genet. 1993 Aug;4(4):367-72. [PubMed ]
- Sargent CA, Young C, Marsh S, Ferguson-Smith MA, Affara NA: The glycerol kinase gene family: structure of the Xp gene, and related intronless retroposons. Hum Mol Genet. 1994 Aug;3(8):1317-24. [PubMed ]
- Sargent CA, Kidd A, Moore S, Dean J, Besley GT, Affara NA: Five cases of isolated glycerol kinase deficiency, including two families: failure to find genotype:phenotype correlation. J Med Genet. 2000 Jun;37(6):434-41. [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 ]
- Sargent CA, Affara NA, Bentley E, Pelmear A, Bailey DM, Davey P, Dow D, Leversha M, Aplin H, Besley GT, et al.: Cloning of the X-linked glycerol kinase deficiency gene and its identification by sequence comparison to the Bacillus subtilis homologue. Hum Mol Genet. 1993 Feb;2(2):97-106. [PubMed ]
- Walker AP, Muscatelli F, Monaco AP: Isolation of the human Xp21 glycerol kinase gene by positional cloning. Hum Mol Genet. 1993 Feb;2(2):107-14. [PubMed ]
- Walker AP, Muscatelli F, Stafford AN, Chelly J, Dahl N, Blomquist HK, Delanghe J, Willems PJ, Steinmann B, Monaco AP: Mutations and phenotype in isolated glycerol kinase deficiency. Am J Hum Genet. 1996 Jun;58(6):1205-11. [PubMed ]
- Sjarif DR, Sinke RJ, Duran M, Beemer FA, Kleijer WJ, Ploos van Amstel JK, Poll-The BT: Clinical heterogeneity and novel mutations in the glycerol kinase gene in three families with isolated glycerol kinase deficiency. J Med Genet. 1998 Aug;35(8):650-6. [PubMed ]
- Gaudet D, Arsenault S, Perusse L, Vohl MC, St-Pierre J, Bergeron J, Despres JP, Dewar K, Daly MJ, Hudson T, Rioux JD: Glycerol as a correlate of impaired glucose tolerance: dissection of a complex system by use of a simple genetic trait. Am J Hum Genet. 2000 May;66(5):1558-68. Epub 2000 Mar 27. [PubMed ]
|
| Enzyme 65 Metabolite References |
Not Available |
|
Enzyme 66
[top]
|
| Enzyme 66 ID |
6130 |
| Enzyme 66 Name |
Folylpolyglutamate synthase, mitochondrial |
| Enzyme 66 Synonyms |
- Folylpoly-gamma-glutamate synthetase
- FPGS
- Tetrahydrofolylpolyglutamate synthase
- Tetrahydrofolate synthase
|
| Enzyme 66 Gene Name |
FPGS |
| Enzyme 66 Protein Sequence |
>Folylpolyglutamate synthase, mitochondrial
MSRARSHLRAALFLAAASARGITTQVAARRGLSAWPVPQEPSMEYQDAVRMLNTLQTNAG
YLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGSTCAFTECILRS
YGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGSCVSMPPYFRF
LTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIA
WQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGPPLTLGLEGE
HQRSNAALALQLAHCWLQRQDRHGAGEPKASRPGLLWQLPLAPVFQPTSHMRLGLRNTEW
PGRTQVLRRGPLTWYLDGAHTASSAQACVRWFRQALQGRERPSGGPEVRVLLFNATGDRD
PAALLKLLQPCQFDYAVFCPNLTEVSSTGNADQQNFTVTLDQVLLRCLEHQQHWNHLDEE
QASPDLWSAPSPEPGGSASLLLAPHPPHTCSASSLVFSCISHALQWISQGRDPIFQPPSP
PKGLLTHPVAHSGASILREAAAIHVLVTGSLHLVGGVLKLLEPALSQ
|
| Enzyme 66 Number of Residues |
587 |
| Enzyme 66 Molecular Weight |
64608.5 |
| Enzyme 66 Theoretical pI |
8.00 |
| Enzyme 66 GO Classification |
| Function |
- ATP binding
- acid-amino acid ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
- tetrahydrofolylpolyglutamate synthase activity
|
| Process |
- biosynthetic process
- cellular aromatic compound metabolic process
- cellular metabolic process
- folic acid and derivative biosynthetic process
- folic acid and derivative metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 66 General Function |
Involved in tetrahydrofolylpolyglutamate synthase activity |
| Enzyme 66 Specific Function |
Conversion of folates to polyglutamate derivatives. This allows tissues to concentrate folate at higher levels than in plasma |
| Enzyme 66 Pathways |
- Folate and Pterine Biosynthesis (map00790 )
|
| Enzyme 66 Reactions |
- ATP + tetrahydropteroyl-[gamma-Glu]n + L-glutamate = ADP + phosphate + tetrahydropteroyl-[gamma-Glu]n+1 [RN:R04241]
|
| Enzyme 66 Pfam Domain Function |
Not Available |
| Enzyme 66 Signals |
|
| Enzyme 66 Transmembrane Regions |
|
| Enzyme 66 Essentiality |
Not Available |
| Enzyme 66 GenBank ID Protein |
39992602 |
| Enzyme 66 UniProtKB/Swiss-Prot ID |
Q05932 |
| Enzyme 66 UniProtKB/Swiss-Prot Entry Name |
FOLC_HUMAN |
| Enzyme 66 PDB ID |
Not Available |
| Enzyme 66 Cellular Location |
Not Available |
| Enzyme 66 Gene Sequence |
>1764 bp
ATGTCGCGGGCGCGGAGCCACCTGCGCGCCGCTCTATTCCTGGCAGCGGCGTCTGCGCGC
GGCGTAACGACCCAGGTCGCGGCGCGGCGGGGCTTGAGCGCGTGGCCGGTGCCGCAGGAG
CCGAGCATGGAGTACCAGGATGCCGTGCGCATGCTCAATACCCTGCAGACCAATGCCGGC
TACCTGGAGCAGGTGAAGCGCCAGCGGGGTGACCCTCAGACACAGTTGGAAGCCATGGAA
CTGTACCTGGCACGGAGTGGGCTGCAGGTGGAGGACTTGGACCGGCTGAACATCATCCAC
GTCACTGGGACGAAGGGGAAGGGCTCCACCTGTGCCTTCACGGAATGTATCCTCCGAAGC
TATGGCCTGAAGACGGGATTCTTTAGCTCTCCCCACCTGGTGCAGGTTCGGGAGCGGATC
CGCATCAATGGGCAGCCCATCAGTCCTGAGCTCTTCACCAAGTACTTCTGGCGCCTCTAC
CACCGGCTGGAGGAGACCAAGGATGGCAGCTGTGTCTCCATGCCCCCCTACTTCCGCTTC
CTGACACTCATGGCCTTCCACGTCTTCCTCCAAGAGAAGGTGGACCTGGCAGTGGTGGAG
GTGGGCATTGGCGGGGCTTATGACTGCACCAACATCATCAGGAAGCCTGTGGTGTGCGGA
GTCTCCTCTCTTGGCATCGACCACACCAGCCTCCTGGGGGATACGGTGGAGAAGATCGCA
TGGCAGAAAGGGGGCATCTTTAAGCAAGGTGTCCCTGCCTTCACTGTGCTCCAACCTGAA
GGTCCCCTGGCAGTGCTGAGGGACCGAGCCCAGCAGATCTCATGTCCTCTATACCTGTGT
CCGATGCTGGAGGCCCTCGAGGAAGGGGGGCCGCCGCTGACCCTGGGCCTGGAGGGGGAG
CACCAGCGGTCCAACGCCGCCTTGGCCTTGCAGCTGGCCCACTGCTGGCTGCAGCGGCAG
GACCGCCATGGTGCTGGGGAGCCAAAGGCATCCAGGCCAGGGCTCCTGTGGCAGCTGCCC
CTGGCACCTGTGTTCCAGCCCACATCCCACATGCGGCTCGGGCTTCGGAACACGGAGTGG
CCGGGCCGGACGCAGGTGCTGCGGCGCGGGCCCCTCACCTGGTACCTGGACGGTGCGCAC
ACCGCCAGCAGCGCGCAGGCCTGCGTGCGCTGGTTCCGCCAGGCGCTGCAGGGCCGCGAG
AGGCCGAGCGGTGGCCCCGAGGTTCGAGTCTTGCTCTTCAATGCTACCGGGGACCGGGAC
CCGGCGGCCCTGCTGAAGCTGCTGCAGCCCTGCCAGTTTGACTATGCCGTCTTCTGCCCT
AACCTGACAGAGGTGTCATCCACAGGCAACGCAGACCAACAGAACTTCACAGTGACACTG
GACCAGGTCCTGCTCCGCTGCCTGGAACACCAGCAGCACTGGAACCACCTGGACGAAGAG
CAGGCCAGCCCGGACCTCTGGAGTGTCCCCAGCCCAGAGCCCGGTGGGTCCGCATCCCTG
CTTCTGGCGCCCCACCCACCCCACACCTGCAGTGCCAGCTCCCTCGTCTTCAGCTGCATT
TCACATGCCTTGCAATGGATCAGCCAAGGCCGAGACCCCATCTTCCAGCCACCTAGTCCC
CCAAAGGGCCTCCTCACCCACCCTGTGGCTCACAGTGGGGCCAGCATACTCCGTGAGGCT
GCTGCCATCCATGTGCTAGTCACTGGCAGCCTGCACCTGGTGGGTGGTGTCCTGAAGCTG
CTGGAGCCCGCACTGTCCCAGTAG
|
| Enzyme 66 GenBank Gene ID |
BC064393 |
| Enzyme 66 GeneCard ID |
FPGS |
| Enzyme 66 GenAtlas ID |
FPGS |
| Enzyme 66 HGNC ID |
HGNC:3824 |
| Enzyme 66 Chromosome Location |
9 |
| Enzyme 66 Locus |
9q34.1 |
| Enzyme 66 SNPs |
SNPJam Report |
| Enzyme 66 General References |
- 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 ]
- Garrow TA, Admon A, Shane B: Expression cloning of a human cDNA encoding folylpoly(gamma-glutamate) synthetase and determination of its primary structure. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9151-5. [PubMed ]
- Freemantle SJ, Taylor SM, Krystal G, Moran RG: Upstream organization of and multiple transcripts from the human folylpoly-gamma-glutamate synthetase gene. J Biol Chem. 1995 Apr 21;270(16):9579-84. [PubMed ]
- Taylor SM, Freemantle SJ, Moran RG: Structural organization of the human folypoly-gamma-glutamate synthetase gene: evidence for a single genomic locus. Cancer Res. 1995 Dec 15;55(24):6030-4. [PubMed ]
- Cichowicz DJ, Shane B: Mammalian folylpoly-gamma-glutamate synthetase. 1. Purification and general properties of the hog liver enzyme. Biochemistry. 1987 Jan 27;26(2):504-12. [PubMed ]
|
| Enzyme 66 Metabolite References |
Not Available |
|
Enzyme 67
[top]
|
| Enzyme 67 ID |
6135 |
| Enzyme 67 Name |
Delta-1-pyrroline-5-carboxylate synthase |
| Enzyme 67 Synonyms |
- P5CS
- Aldehyde dehydrogenase family 18 member A1
- Glutamate 5-kinase
- GK
- Gamma-glutamyl kinase
- Gamma-glutamyl phosphate reductase
- GPR
- Glutamate-5-semialdehyde dehydrogenase
- Glutamyl-gamma-semialdehyde dehydrogenase
|
| Enzyme 67 Gene Name |
ALDH18A1 |
| Enzyme 67 Protein Sequence |
>Delta-1-pyrroline-5-carboxylate synthase
MLSQVYRCGFQPFNQHLLPWVKCTTVFRSHCIQPSVIRHVRSWSNIPFITVPLSRTHGKS
FAHRSELKHAKRIVVKLGSAVVTRGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAV
AFGKQRLRHEILLSQSVRQALHSGQNQLKEMAIPVLEARACAAAGQSGLMALYEAMFTQY
SICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAEPNSDLQGVNV
ISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQSVTFGTK
SRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVSGHVITDIVEGKKVGTFFSEVKPAG
PTVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGRLAA
PLLKRLSLSTSKLNSLAIGLRQIAASSQDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIF
ESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQLVNTRE
EVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRL
VRDSKCEYPAACNALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSE
VKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVF
WNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSDFSEHGSL
KYLHENLPIPQRNTN
|
| Enzyme 67 Number of Residues |
795 |
| Enzyme 67 Molecular Weight |
87301.5 |
| Enzyme 67 Theoretical pI |
7.13 |
| Enzyme 67 GO Classification |
| Function |
- catalytic activity
- glutamate 5-kinase activity
- glutamate-5-semialdehyde dehydrogenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
- phosphotransferase activity, carboxyl group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid biosynthetic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- metabolic process
- oxidation reduction
- proline biosynthetic process
- proline metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 67 General Function |
Involved in oxidoreductase activity |
| Enzyme 67 Specific Function |
ATP + L-glutamate = ADP + L-glutamate 5- phosphate |
| Enzyme 67 Pathways |
Not Available |
| Enzyme 67 Reactions |
- ATP + L-glutamate = ADP + L-glutamate 5-phosphate [RN:R00239]
|
| Enzyme 67 Pfam Domain Function |
|
| Enzyme 67 Signals |
|
| Enzyme 67 Transmembrane Regions |
|
| Enzyme 67 Essentiality |
Not Available |
| Enzyme 67 GenBank ID Protein |
1304314 |
| Enzyme 67 UniProtKB/Swiss-Prot ID |
P54886 |
| Enzyme 67 UniProtKB/Swiss-Prot Entry Name |
P5CS_HUMAN |
| Enzyme 67 PDB ID |
Not Available |
| Enzyme 67 Cellular Location |
Not Available |
| Enzyme 67 Gene Sequence |
>2388 bp
ATGTTGAGTCAAGTTTACCGCTGTGGGTTCCAGCCCTTCAACCAACATCTTCTGCCCTGG
GTCAAGTGTACAACCGTCTTCAGATCTCATTGTATCCAGCCTTCAGTCATCAGACATGTT
CGTTCTTGGAGCAACATCCCGTTTATCACTGTACCCCTCAGTCGTACACATGGCAAGTCC
TTCGCCCACCGCAGTGAGCTGAAGCATGCCAAGAGAATCGTGGTGAAGCTCGGCAGTGCC
GTGGTGACCCGAGGGGATGAATGTGGCCTGGCCCTGGGGCGCTTGGCATCTATTGTTGAG
CAGGTATCAGTGCTGCAGAATCAGGGCAGAGAGATGATGCTGGTGACCAGTGGAGCCGTA
GCCTTTGGCAAACAAACGTTGCGCCATGAGATCCTTCTGTCTCAGAGCGTGCGGCAGGCC
CTCCACTCGGGGCAGAACCAGCTGAAAGAAATGGCAATTCCAGTCTTAGAGGCACGAGCC
TGTGCAGCTGCCGGACAGAGTGGGCTGATGGCCTTGTATGAGGCTATGTTTACCCAGTAC
AGCATCTGTGCTGCCCAGATTTTGGTGACCAATTTGGATTTCCATGATGAGCAGAAGCGC
CGGAACCTCAATGGAACACTTCATGAACTCCTTAGAATGAACATTGTCCCCATTGTCAAC
ACAAATGATGCTGTTGTCCCCCCAGCTGAGCCCAACAGTGACCTGCAGGGGGTAAATGTT
ATTAGTGTTAAAGATAATGATAGCCTGGCTGCCCGACTGGCTGTGGAAATGAAAACTGAT
CTCTTGATTGTCCTTCCAGATGTAGAAGGCCTTTTTGACAGCCCCCCAGGTTCAGATGAT
GCAAAGCTTATTGATATATTTTATCCCGGAGATCAGCAGTCTGTGACATTTGGACCCAAG
TCTAGAGTGGGAAATGGGTGCATGGAAGCCAAGGTGAAAAGCACCCTCTGGGCTTTGCAA
GGTGGCACTTCTGTTGTTATTGCCAATGGAACCCACCCAAAGGTGTCTGGGCACGTCATC
ACAGACATTGTGGAGGGGAAGAAAGTTGGTACCTTCTTTTCAGAAGTAAAGCCTGCAGGC
CCTACTGTTGAGCAGCAGGGAGAAATGGCGCGATCTGGAGGAAGGATGTTGGCCACCTTG
GAACCTGAGCAGAGAGCAGAAATTATCCATCATCTGGCTGATCTGTTGACGGACCAGCGT
GATGAGATCCTGTTAGCCAACAAAAAAGACTTGGAGGAGGCAGAGGGGAGACTTGCAGCT
CCTCTGCTGAAACGTTTAAGCCTCTCCACATCCAAATTGAACAGCCTGGCCATCGGTCTG
CGACAGATCGCAGCCTCCTCCCAGGACAGCGTGGGACGTGTTTTGCGCCGCACCCGAATC
GCCAAAAACTTGGAACTGGAACAAGTGACTGTCCCAATTGGAGTTCTGCTGGTGATCTTT
GAATCTCGTCCTGACTGTCCTACCCCAGGTGGCAGCTTTGCTATCGCAAGTGGCAATGGC
TTGTTACTCAAAGGAGGGAAGGAGGCTGCACACAGCAACCGGATTCTCCACCTCCTGACC
CAGGAGGCTCTCTCAATCCATGGAGTCAAGGAGGCCGTGCAACTGGTGAATACCAGAGAA
GAAGTTGAAGATCTTTGCCGCCTAGACAAAATGATAGATCTGATCATTCCACGTGGCTCT
TCCCAGCTGGTCAGAGACATCCAGAAAGCTGCTAAGGGGATTCCAGTGATGGGGCACAGC
GAAGGGATCTGTCACATGTATGTGGATTCCGAGGCCAGTGTTGATAAGGTCACCAGGCTA
GTCAGAGACTCTAAATGTGAATATCCAGCTGCCTGTAATGCTTTGGAGACTTTGTTAATC
CACCGGGATCTGCTCAGGACACCATTATTTGACCAGATCATTGATATGCTGAGAGTGGAA
CAGGTAAAAATTCATGCAGGCCCCAAATTTGCCTCCTATCTGACCTTCAGCCCCTCCGAA
GTGAAGTCACTCCGAACTGAGTATGGGGACCTGGAATTATGCATTGAAGTAGTGGACAAC
GTTCAGGATGCCATTGACCACATCCACAAGTATGGCAGCTCCCACACGGATGTCATCGTC
ACAGAGGACGAAAACACAGCGGAGTTCTTCCTGCAGCACGTAGACAGTGCCTGTGTGTTC
TGGAATGCCAGCACTCGCTTTTCTGATGGTTACCGCTTTGGACTGGGAGCTGAAGTGGGA
ATCAGTACATCGAGAATCCACGCCCGGGGACCAGTAGGACTTGAGGGACTGCTTACTACT
AAGTGGCTGCTGCGAGGGAAGGACCACGTGGTCTCAGATTTCTCAGAGCATGGAAGTTTA
AAATATCTTCATGAGAACCTCCCTATTCCTCAGAGAAACACCAACTGA
|
| Enzyme 67 GenBank Gene ID |
X94453 |
| Enzyme 67 GeneCard ID |
ALDH18A1 |
| Enzyme 67 GenAtlas ID |
ALDH18A1 |
| Enzyme 67 HGNC ID |
HGNC:9722 |
| Enzyme 67 Chromosome Location |
1 |
| Enzyme 67 Locus |
10q24.3 |
| Enzyme 67 SNPs |
SNPJam Report |
| Enzyme 67 General References |
- Aral B, Schlenzig JS, Liu G, Kamoun P: Database cloning human delta 1-pyrroline-5-carboxylate synthetase (P5CS) cDNA: a bifunctional enzyme catalyzing the first 2 steps in proline biosynthesis. C R Acad Sci III. 1996 Mar;319(3):171-8. [PubMed ]
- Hu CA, Lin WW, Obie C, Valle D: Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. J Biol Chem. 1999 Mar 5;274(10):6754-62. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Baumgartner MR, Hu CA, Almashanu S, Steel G, Obie C, Aral B, Rabier D, Kamoun P, Saudubray JM, Valle D: Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase. Hum Mol Genet. 2000 Nov 22;9(19):2853-8. [PubMed ]
- Bicknell LS, Pitt J, Aftimos S, Ramadas R, Maw MA, Robertson SP: A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-carboxylate synthase (P5CS), causes an autosomal recessive neurocutaneous syndrome. Eur J Hum Genet. 2008 Oct;16(10):1176-86. Epub 2008 May 14. [PubMed ]
|
| Enzyme 67 Metabolite References |
Not Available |
|
Enzyme 68
[top]
|
| Enzyme 68 ID |
6136 |
| Enzyme 68 Name |
5-oxoprolinase |
| Enzyme 68 Synonyms |
- 5-oxo-L-prolinase
- 5-OPase
- Pyroglutamase
|
| Enzyme 68 Gene Name |
OPLAH |
| Enzyme 68 Protein Sequence |
>5-oxoprolinase
MGSPEGRFHFAIDRGGTFTDVFAQCPGGHVRVLKLLSEDPANYADAPTEGIRRILEQEAG
MLLPRDQPLDSSHIASIRMGTTVATNALLERKGERVALLVTRGFRDLLHIGTQARGDLFD
LAVPMPEVLYEEVLEVDERVVLHRGEAGTGTPVKGRTGDLLEVQQPVDLGALRGKLEGLL
SRGIRSLAVVLMHSYTWAQHEQQVGVLARELGFTHVSLSSEAMPMVRIVPRGHTACADAY
LTPAIQRYVQGFCRGFQGQLKDVQVLFMRSDGGLAPMDTFSGSSAVLSGPAGGVVGYSAT
TYQQEGGQPVIGFDMGGTSTDVSRYAGEFEHVFEASTAGVTLQAPQLDINTVAAGGGSRL
FFRSGLFVVGPESAGAHPGPACYRKGGPVTVTDANLVLGRLLPASFPCIFGPGENQPLSP
EASRKALEAVATEVNSFLTNGPCPASPLSLEEVAMGFVRVANEAMCRPIRALTQARGHDP
SAHVLACFGGAGGQHACAIARALGMDTVHIHRHSGLLSALGLALADVVHEAQEPCSLLYA
PETFVQLDQRLSRLEEQCVDALQAQGFPRSQISTESFLHLRYQGTDCALMVSAHQHPATA
RSPRAGDFGAAFVERYMREFGFVIPERPVVVDDVRVRGTGRSGLRLEDAPKAQTGPPRVD
KMTQCYFEGGYQETPVYLLAELGYGHKLHGPCLIIDSNSTILVEPGCQAEVTKTGDICIS
VGAEVPGTVGPQLDPIQLSIFSHRFMSIAEQMGRILQRTAISTNIKERLDFSCALFGPDG
GLVSNAPHIPVHLGAMQETVQFQIQHLGADLHPGDVLLSNHPSAGGSHLPDLTVITPVFW
PGQTRPVFYVASRGHHADIGGITPGSMPPHSTMLQQEGAVFLSFKLVQGGVFQEEAVTEA
LRAPGKVPNCSGTRNLHDNLSDLRAQVAANQKGIQLVGELIGQYGLDVVQAYMGHIQANA
ELAVRDMLRAFGTSRQARGLPLEVSSEDHMDDGSPIRLRVQISLSQGSAVFDFSGTGPEV
FGNLNAPRAVTLSALIYCLRCLVGRDIPLNQGCLAPVRVVIPRGSILDPSPEAAVVGGNV
LTSQRVVDVILGAFGACAASQGCMNNVTLGNAHMGYYETVAGGAGAGPSWHGRSGVHSHM
TNTRITDPEILESRYPVILRRFELRRGSGGRGRFRGGDGVTRELLFREEALLSVLTERRA
FRPYGLHGGEPGARGLNLLIRKNGRTVNLGGKTSVTVYPGDVFCLHTPGGGGYGDPEDPA
PPPGSPPQALAFPEHGSVYEYRRAQEAV
|
| Enzyme 68 Number of Residues |
1288 |
| Enzyme 68 Molecular Weight |
137456.2 |
| Enzyme 68 Theoretical pI |
6.56 |
| Enzyme 68 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 68 General Function |
Involved in hydrolase activity |
| Enzyme 68 Specific Function |
Catalyzes the cleavage of 5-oxo-L-proline to form L- glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate |
| Enzyme 68 Pathways |
|
| Enzyme 68 Reactions |
- ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate [RN:R00251]
|
| Enzyme 68 Pfam Domain Function |
|
| Enzyme 68 Signals |
|
| Enzyme 68 Transmembrane Regions |
|
| Enzyme 68 Essentiality |
Not Available |
| Enzyme 68 GenBank ID Protein |
Not Available |
| Enzyme 68 UniProtKB/Swiss-Prot ID |
O14841 |
| Enzyme 68 UniProtKB/Swiss-Prot Entry Name |
OPLA_HUMAN |
| Enzyme 68 PDB ID |
Not Available |
| Enzyme 68 Cellular Location |
Not Available |
| Enzyme 68 Gene Sequence |
>3867 bp
ATGGGCAGCCCCGAGGGCCGCTTCCACTTTGCCATCGACCGTGGGGGTACCTTCACAGAC
GTCTTTGCCCAGTGCCCAGGGGGGCACGTGCGGGTCTTAAAACTGCTCTCAGAGGACCCT
GCCAACTATGCGGACGCGCCAACCGAAGGCATCCGCCGCATCCTGGAGCAGGAGGCCGGC
ATGCTCCTGCCCCGGGACCAGCCGCTGGACTCCAGTCATATCGCCAGCATCCGCATGGGC
ACCACAGTGGCCACCAACGCACTGCTGGAGCGGAAGGGGGAGCGGGTGGCGCTGCTGGTG
ACACGTGGCTTCCGAGACCTGCTGCACATTGGCACCCAAGCCCGTGGGGACCTCTTTGAC
CTGGCCGTGCCCATGCCTGAGGTGCTGTATGAAGAGGTGCTGGAGGTGGACGAACGCGTG
GTGCTGCACCGTGGAGAGGCGGGCACCGGGACGCCTGTGAAAGGCCGCACGGGGGACCTG
CTGGAAGTGCAGCAGCCTGTGGACCTGGGGGCCCTGCGTGGGAAGCTGGAGGGGCTGCTA
TCTCGAGGCATCCGCAGCCTGGCTGTGGTGCTCATGCACTCGTACACGTGGGCCCAGCAT
GAGCAGCAGGTGGGTGTGCTGGCCCGGGAGCTGGGCTTCACGCACGTGTCACTGTCCTCG
GAGGCCATGCCCATGGTGCGCATCGTCCCTCGGGGGCACACGGCCTGTGCCGACGCCTAC
CTCACGCCCGCCATCCAGCGCTACGTGCAGGGCTTCTGCCGTGGCTTCCAGGGCCAACTC
AAGGATGTGCAGGTGTTGTTCATGCGCTCCGATGGCGGCCTGGCGCCCATGGACACCTTC
AGCGGCTCCAGTGCTGTGCTCTCGGGCCCGGCCGGCGGCGTGGTGGGCTACTCAGCCACC
ACCTACCAGCAGGAGGGTGGCCAGCCTGTCATCGGCTTTGACATGGGAGGCACGTCCACG
GATGTGAGCCGCTATGCTGGGGAATTCGAGCACGTCTTCGAGGCCAGCACAGCTGGCGTC
ACCCTCCAGGCCCCGCAGCTGGACATCAACACCGTGGCAGCGGGAGGGGGTTCCCGCCTC
TTCTTCAGGTCTGGCCTCTTTGTGGTTGGGCCCGAGTCAGCAGGAGCCCACCCAGGACCC
GCCTGCTACCGCAAAGGGGGCCCTGTGACAGTGACGGATGCTAATCTGGTCCTGGGTCGC
CTGCTGCCTGCCTCCTTCCCCTGCATTTTTGGGCCGGGAGAGAACCAACCACTTTCCCCT
GAGGCCTCCCGCAAAGCCCTGGAGGCTGTGGCCACTGAGGTCAACAGCTTCCTGACCAAC
GGGCCCTGCCCGGCCTCCCCGCTGAGCCTGGAGGAGGTGGCCATGGGGTTCGTGCGCGTG
GCCAACGAGGCCATGTGCCGGCCCATCCGTGCACTCACGCAGGCAAGAGGCCATGACCCC
TCAGCCCATGTGCTGGCCTGCTTTGGGGGAGCTGGTGGGCAGCATGCATGTGCCATCGCC
CGGGCCCTGGGCATGGACACGGTGCACATCCACAGGCACAGTGGGCTGCTGTCGGCCCTG
GGGCTGGCCCTGGCTGACGTGGTGCATGAGGCACAGGAACCCTGCTCCCTGCTCTACGCG
CCTGAGACCTTCGTGCAGCTGGACCAGAGGCTGAGCCGCCTGGAGGAGCAGTGTGTGGAT
GCTCTGCAGGCCCAGGGCTTCCCCAGGTCCCAGATCAGCACTGAGAGCTTCCTGCACCTG
CGCTACCAGGGCACGGACTGTGCTCTGATGGTGTCTGCCCACCAGCACCCAGCCACAGCC
CGCTCGCCCCGTGCGGGGGACTTCGGGGCAGCCTTTGTGGAGCGGTACATGAGGGAGTTT
GGCTTTGTCATACCTGAGCGGCCGGTGGTCGTGGACGATGTGCGAGTGCGGGGCACCGGC
CGCAGTGGTCTTCGCCTCGAGGATGCCCCCAAAGCCCAGACCGGGCCTCCCCGGGTGGAC
AAGATGACCCAGTGCTACTTTGAGGGGGGCTACCAGGAGACCCCTGTGTACCTGCTGGCA
GAGCTGGGCTATGGGCACAAGCTCCATGGGCCCTGCCTCATCATCGACAGTAACAGCACC
ATCCTGGTGGAGCCAGGTTGCCAGGCAGAGGTGACCAAGACAGGGGACATCTGCATCTCC
GTGGGGGCCGAAGTCCCCGGCACAGTGGGCCCCCAGCTGGACCCTATCCAGCTGTCCATC
TTCTCACACCGCTTCATGAGCATTGCTGAGCAGATGGGCCGCATCCTGCAGCGCACAGCC
ATCTCCACCAACATCAAGGAGCGTCTGGACTTCTCCTGTGCCCTCTTTGGGCCCGATGGG
GGGCTGGTGTCCAATGCCCCCCACATCCCTGTGCACCTGGGTGCCATGCAGGAGACGGTG
CAGTTCCAGATTCAGCACCTGGGGGCCGATCTCCACCCTGGCGACGTGCTACTGAGCAAC
CATCCCAGTGCCGGGGGCAGCCACCTGCCAGACCTGACTGTTATCACACCGGTGTTTTGG
CCGGGTCAGACGCGGCCTGTGTTCTATGTGGCCAGCCGAGGGCACCACGCAGACATCGGG
GGCATCACACCAGGCTCCATGCCCCCCCACTCCACCATGCTGCAACAGGAGGGTGCCGTC
TTTCTGTCCTTCAAACTTGTCCAGGGGGGCGTCTTCCAGGAGGAGGCGGTGACGGAGGCC
CTGCGGGCGCCAGGCAAGGTCCCCAACTGCAGCGGAACCAGAAACCTGCACGACAACCTG
TCGGACCTCCGTGCCCAGGTGGCAGCCAACCAGAAGGGCATCCAGCTGGTGGGGGAGCTC
ATTGGGCAGTACGGCCTGGACGTGGTGCAGGCCTACATGGGCCATATTCAGGCAAACGCT
GAGCTGGCCGTGCGAGACATGTTGCGTGCCTTTGGAACCTCCCGGCAGGCCCGGGGCCTG
CCCCTGGAGGTGTCCTCGGAAGACCACATGGACGACGGTTCCCCCATCCGCCTCCGTGTG
CAGATCAGCCTGAGTCAGGGCAGCGCTGTGTTTGACTTCAGCGGCACTGGGCCGGAGGTG
TTTGGTAATCTCAACGCACCGCGGGCCGTAACCCTGTCCGCCCTCATCTACTGCCTGCGC
TGTCTGGTGGGCCGCGACATCCCACTCAACCAGGGCTGCCTGGCGCCAGTGCGCGTGGTC
ATTCCCCGAGGCTCCATCCTGGACCCGTCGCCCGAGGCGGCGGTGGTGGGCGGCAACGTG
CTCACGTCGCAGCGCGTGGTGGATGTCATCCTGGGGGCCTTTGGGGCCTGCGCCGCCTCC
CAGGGCTGCATGAACAACGTGACCCTGGGCAACGCCCACATGGGCTACTACGAGACGGTG
GCGGGCGGCGCGGGCGCGGGTCCCAGCTGGCACGGGCGCAGCGGTGTGCACAGCCACATG
ACCAACACACGCATCACCGACCCTGAGATCCTGGAGAGCCGGTACCCGGTCATCCTGCGC
CGCTTCGAGCTGCGGCGGGGCTCGGGGGGCAGAGGCCGCTTCCGAGGCGGCGACGGCGTC
ACCCGCGAGCTGCTCTTTCGTGAGGAGGCGCTGCTGTCAGTGCTGACCGAGCGCCGCGCC
TTCCGGCCATACGGGCTCCACGGGGGCGAGCCTGGCGCCCGCGGCCTAAACCTGCTGATC
CGCAAAAACGGCCGGACGGTGAATCTGGGCGGCAAGACGTCGGTGACCGTGTACCCCGGG
GATGTGTTCTGTCTCCACACGCCCGGCGGCGGTGGCTATGGGGACCCGGAGGACCCCGCC
CCACCGCCGGGGTCGCCCCCGCAAGCACTGGCCTTTCCCGAGCACGGCAGCGTCTATGAG
TATCGCCGGGCCCAGGAGGCCGTGTGA
|
| Enzyme 68 GenBank Gene ID |
AB122018 |
| Enzyme 68 GeneCard ID |
OPLAH |
| Enzyme 68 GenAtlas ID |
OPLAH |
| Enzyme 68 HGNC ID |
HGNC:8149 |
| Enzyme 68 Chromosome Location |
8 |
| Enzyme 68 Locus |
8q24.3 |
| Enzyme 68 SNPs |
SNPJam Report |
| Enzyme 68 General References |
- Watanabe T, Abe K, Ishikawa H, Iijima Y: Bovine 5-oxo-L-prolinase: simple assay method, purification, cDNA cloning, and detection of mRNA in the coronary artery. Biol Pharm Bull. 2004 Mar;27(3):288-94. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- 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 ]
|
| Enzyme 68 Metabolite References |
Not Available |
|
Enzyme 69
[top]
|
| Enzyme 69 ID |
6137 |
| Enzyme 69 Name |
Ethanolamine kinase 1 |
| Enzyme 69 Synonyms |
- EKI 1
|
| Enzyme 69 Gene Name |
ETNK1 |
| Enzyme 69 Protein Sequence |
>Ethanolamine kinase 1
MLCGRPRSSSDNRNFLRERAGLSSAAVQTRIGNSAASRRSPAARPPVPAPPALPRGRPGT
EGSTSLSAPAVLVVAVAVVVVVVSAVAWAMANYIHVPPGSPEVPKLNVTVQDQEEHRCRE
GALSLLQHLRPHWDPQEVTLQLFTDGITNKLIGCYVGNTMEDVVLVRIYGNKTELLVDRD
EEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPKHVCNPAIFRLIARQLAKIHAI
HAHNGWIPKSNLWLKMGKYFSLIPTGFADEDINKRFLSDIPSSQILQEEMTWMKEILSNL
GSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDVDYSLY
PDRELQSQWLRAYLEAYKEFKGFGTEVTEKEVEILFIQVNQFALASHFFWGLWALIQAKY
STIEFDFLGYAIVRFNQYFKMKPEVTALKVPE
|
| Enzyme 69 Number of Residues |
452 |
| Enzyme 69 Molecular Weight |
50967.9 |
| Enzyme 69 Theoretical pI |
6.51 |
| Enzyme 69 GO Classification |
Not Available |
| Enzyme 69 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 69 Specific Function |
Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylethanolamine biosynthesis |
| Enzyme 69 Pathways |
|
| Enzyme 69 Reactions |
- ATP + ethanolamine = ADP + O-phosphoethanolamine [RN:R01468]
|
| Enzyme 69 Pfam Domain Function |
|
| Enzyme 69 Signals |
|
| Enzyme 69 Transmembrane Regions |
|
| Enzyme 69 Essentiality |
Not Available |
| Enzyme 69 GenBank ID Protein |
9998952 |
| Enzyme 69 UniProtKB/Swiss-Prot ID |
Q9HBU6 |
| Enzyme 69 UniProtKB/Swiss-Prot Entry Name |
EKI1_HUMAN |
| Enzyme 69 PDB ID |
Not Available |
| Enzyme 69 Cellular Location |
Not Available |
| Enzyme 69 Gene Sequence |
>1359 bp
ATGCTCTGCGGCCGCCCGCGGTCCAGCTCCGACAACAGGAATTTTCTCCGAGAGCGGGCC
GGGCTCAGTTCAGCTGCTGTCCAGACCCGGATCGGCAACAGTGCCGCCTCCAGACGTTCT
CCTGCCGCTCGCCCGCCCGTCCCAGCGCCCCCAGCCCTCCCGCGAGGGCGCCCCGGGACG
GAAGGATCCACCAGTCTGTCGGCGCCCGCCGTTCTCGTGGTCGCCGTCGCCGTCGTCGTG
GTGGTAGTCTCCGCCGTCGCCTGGGCCATGGCCAATTACATCCACGTCCCTCCCGGCTCC
CCGGAGGTGCCCAAGCTGAACGTCACCGTTCAGGATCAGGAGGAGCATCGCTGCCGGGAG
GGGGCCCTGAGCCTCCTGCAACACCTGCGGCCTCACTGGGACCCCCAGGAGGTGACCCTG
CAGCTCTTCACAGATGGAATCACAAATAAACTTATTGGCTGTTACGTGGGAAACACCATG
GAGGATGTAGTCCTGGTGAGAATTTATGGCAATAAGACTGAGTTATTAGTCGATCGAGAT
GAGGAAGTAAAGAGTTTTCGAGTGTTGCAGGCTCATGGGTGTGCACCACAACTCTACTGT
ACCTTCAATAATGGACTATGCTATGAATTTATACAAGGAGAAGCACTGGATCCAAAGCAT
GTCTGCAACCCAGCCATTTTCAGGCTAATAGCTCGTCAGCTTGCTAAAATCCATGCTATT
CATGCACACAATGGCTGGATCCCCAAATCTAATCTTTGGCTAAAGATGGGAAAGTATTTC
TCTCTCATTCCCACAGGATTTGCAGATGAAGACATTAATAAAAGGTTCCTAAGTGATATC
CCAAGCTCTCAGATTCTCCAGGAAGAGATGACTTGGATGAAGGAGATTCTTTCCAACCTG
GGCTCACCTGTTGTGCTTTGCCATAATGACCTATTGTGTAAGAATATAATCTACAATGAG
AAACAAGGTGATGTACAGTTCATTGATTATGAATATTCTGGATACAACTACCTGGCATAT
GATATTGGAAATCATTTCAATGAATTTGCAGGTGTGAGTGATGTAGACTATAGTCTGTAT
CCAGATAGAGAACTACAGAGTCAGTGGCTGCGTGCTTACCTTGAAGCCTACAAAGAATTT
AAGGGCTTTGGGACTGAAGTTACTGAAAAGGAGGTAGAAATACTCTTCATTCAAGTCAAT
CAGTTTGCATTGGCTTCTCATTTCTTTTGGGGATTGTGGGCTTTGATTCAAGCCAAATAC
TCCACTATTGAGTTTGATTTCCTTGGGTATGCAATTGTTCGTTTTAACCAGTACTTTAAA
ATGAAGCCTGAGGTTACTGCATTAAAAGTGCCTGAGTAA
|
| Enzyme 69 GenBank Gene ID |
AF207600 |
| Enzyme 69 GeneCard ID |
ETNK1 |
| Enzyme 69 GenAtlas ID |
ETNK1 |
| Enzyme 69 HGNC ID |
HGNC:24649 |
| Enzyme 69 Chromosome Location |
1 |
| Enzyme 69 Locus |
12p12.1 |
| Enzyme 69 SNPs |
SNPJam Report |
| Enzyme 69 General References |
- Lykidis A, Wang J, Karim MA, Jackowski S: Overexpression of a mammalian ethanolamine-specific kinase accelerates the CDP-ethanolamine pathway. J Biol Chem. 2001 Jan 19;276(3):2174-9. Epub 2000 Oct 23. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 69 Metabolite References |
Not Available |
|
Enzyme 70
[top]
|
| Enzyme 70 ID |
6159 |
| Enzyme 70 Name |
Ectonucleoside triphosphate diphosphohydrolase 4 |
| Enzyme 70 Synonyms |
- NTPDase 4
- Lysosomal apyrase-like protein of 70 kDa
- Uridine-diphosphatase
- UDPase
|
| Enzyme 70 Gene Name |
ENTPD4 |
| Enzyme 70 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 4
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTVSFASSQQEEVAKN
LLAEFNLGCDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTP
DMPYLDPCLPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPP
IHFQNSEFYGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASH
ADLHRLKYQCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPL
RDIQQEAFRASHTHWRGVSFVYNHYLFSGCFLVVLLAILLYLLRLRRIHRRTPRSSSAAA
LWMEEGLPAQNAPGTL
|
| Enzyme 70 Number of Residues |
616 |
| Enzyme 70 Molecular Weight |
70254.8 |
| Enzyme 70 Theoretical pI |
8.39 |
| Enzyme 70 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 70 General Function |
Involved in hydrolase activity |
| Enzyme 70 Specific Function |
Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. The order of activity with different substrates is UDP >> GDP = CDP = TDP, AMP, ADP, ATP and UMP are not substrates. Preferred substrates for isoform 2 are CTP, UDP, CDP, GTP and GDP, while isoform 1 utilizes UTP and TTP |
| Enzyme 70 Pathways |
|
| Enzyme 70 Reactions |
- a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
|
| Enzyme 70 Pfam Domain Function |
|
| Enzyme 70 Signals |
|
| Enzyme 70 Transmembrane Regions |
|
| Enzyme 70 Essentiality |
Not Available |
| Enzyme 70 GenBank ID Protein |
4758662 |
| Enzyme 70 UniProtKB/Swiss-Prot ID |
Q9Y227 |
| Enzyme 70 UniProtKB/Swiss-Prot Entry Name |
ENTP4_HUMAN |
| Enzyme 70 PDB ID |
Not Available |
| Enzyme 70 Cellular Location |
Not Available |
| Enzyme 70 Gene Sequence |
>1851 bp
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGGCGA
CTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCTACA
GACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGGTCT
CGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGATATC
AGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATTTCA
GAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTTGCT
GCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACGGCT
GGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACCGAT
ATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGGAAA
CAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCATATT
GAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAAGCC
ATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATAGCG
TACGAAGTCCCCAAAACTGTAAGCTTTGCGTCCTCACAGCAGGAAGAAGTAGCTAAAAAC
TTGTTAGCTGAATTTAACTTGGGATGTGATGTTCACCAAACTGAGCATGTGTATCGAGTC
TATGTGGCCACGTTTCTTGGGTTTGGTGGCAATGCTGCTCGACAGAGATACGAAGACAGA
ATATTTGCCAACACCATTCAAAAGAACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCT
GATATGCCGTACTTGGACCCCTGCCTACCCCTAGACATTAAAGATGAAATCCAGCAAAAT
GGACAAACCATATACCTACGAGGGACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAG
CCTTTCATGAATAAAACAAACGAGACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCA
ATTCACTTCCAGAACAGTGAATTCTATGGCTTCTCCGAATTCTACTACTGCACCGAGGAT
GTGTTACGAATGGGGGGAGACTACAATGCTGCTAAATTTACTAAAGCTGCAAAGGATTAT
TGTGCAACAAAGTGGTCCATTTTGCGGGAACGCTTTGACCGAGGACTGTACGCCTCTCAT
GCTGACCTCCACAGGCTTAAGTATCAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTT
CATAGGGGCTTTTCGTTTCCTGTCAACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTAC
GACAAGGAGGTTCAGTGGACCCTTGGAGCCATCCTCTACAGGACCCGCTTTCTACCATTA
AGAGACATCCAGCAGGAGGCCTTCCGAGCCAGTCACACCCACTGGCGGGGCGTTTCCTTT
GTCTACAACCACTACCTGTTCTCTGGCTGCTTCCTGGTGGTGCTGCTGGCCATCCTGCTG
TACCTGCTGCGGCTGCGGCGCATCCACAGGCGCACTCCCCGGAGCAGCTCGGCCGCCGCC
CTCTGGATGGAGGAGGGCCTTCCCGCCCAGAATGCCCCGGGGACCTTGTGA
|
| Enzyme 70 GenBank Gene ID |
NM_004901.3 |
| Enzyme 70 GeneCard ID |
ENTPD4 |
| Enzyme 70 GenAtlas ID |
ENTPD4 |
| Enzyme 70 HGNC ID |
HGNC:14573 |
| Enzyme 70 Chromosome Location |
8 |
| Enzyme 70 Locus |
8p21.3 |
| Enzyme 70 SNPs |
SNPJam Report |
| Enzyme 70 General References |
- Wang TF, Guidotti G: Golgi localization and functional expression of human uridine diphosphatase. J Biol Chem. 1998 May 1;273(18):11392-9. [PubMed ]
- Biederbick A, Rose S, Elsasser HP: A human intracellular apyrase-like protein, LALP70, localizes to lysosomal/autophagic vacuoles. J Cell Sci. 1999 Aug;112 ( Pt 15):2473-84. [PubMed ]
- Biederbick A, Kosan C, Kunz J, Elsasser HP: First apyrase splice variants have different enzymatic properties. J Biol Chem. 2000 Jun 23;275(25):19018-24. [PubMed ]
- Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed ]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
|
| Enzyme 70 Metabolite References |
Not Available |
|
Enzyme 71
[top]
|
| Enzyme 71 ID |
6160 |
| Enzyme 71 Name |
Ectonucleoside triphosphate diphosphohydrolase 6 |
| Enzyme 71 Synonyms |
- NTPDase 6
- CD39 antigen-like 2
|
| Enzyme 71 Gene Name |
ENTPD6 |
| Enzyme 71 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 6
MKKGIRYETSRKTSYIFQQPQHGPWQTRMRKISNHGSLRVAKVAYPLGLCVGVFIYVAYI
KWHRATATQAFFSITRAAPGARWGQQAHSPLGTAADGHEVFYGIMFDAGSTGTRVHVFQF
TRPPRETPTLTHETFKALKPGLSAYADDVEKSAQGIRELLDVAKQDIPFDFWKATPLVLK
ATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITINFLTGSLK
TPGGSSVGMLDLGGGSTQIAFLPRVEGTLQASPPGYLTALRMFNRTYKLYSYSYLGLGLM
SARLAILGGVEGQPAKDGKELVSPCLSPSFKGEWEHAEVTYRVSGQKAAASLHELCAARV
SEVLQNRVHRTEEVKHVDFYAFSYYYDLAAGVGLIDAEKGGSLVVGDFEIAAKYVCRTLE
TQPQSSPFSCMDLTYVSLLLQEFGFPRSKVLKLTRKIDNVETSWALGAIFHYIDSLNRQK
SPAS
|
| Enzyme 71 Number of Residues |
484 |
| Enzyme 71 Molecular Weight |
53246.7 |
| Enzyme 71 Theoretical pI |
9.52 |
| Enzyme 71 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 71 General Function |
Involved in hydrolase activity |
| Enzyme 71 Specific Function |
Might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides. Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent, there is no hydrolysis of nucleoside 5'-monophosphates. The order of activity with different substrates is GDP > IDP >> UDP = CDP >> ADP |
| Enzyme 71 Pathways |
|
| Enzyme 71 Reactions |
- a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
|
| Enzyme 71 Pfam Domain Function |
|
| Enzyme 71 Signals |
|
| Enzyme 71 Transmembrane Regions |
|
| Enzyme 71 Essentiality |
Not Available |
| Enzyme 71 GenBank ID Protein |
3335098 |
| Enzyme 71 UniProtKB/Swiss-Prot ID |
O75354 |
| Enzyme 71 UniProtKB/Swiss-Prot Entry Name |
ENTP6_HUMAN |
| Enzyme 71 PDB ID |
Not Available |
| Enzyme 71 Cellular Location |
Not Available |
| Enzyme 71 Gene Sequence |
>1455 bp
ATGAAAAAAGGTATCCGTTATGAAACTTCCAGAAAAACGAGCTACATTTTTCAGCAGCCG
CAGCACGGTCCTTGGCAAACAAGGATGAGAAAAATATCCAACCACGGGAGCCTGCGGGTG
GCGAAGGTGGCATACCCCCTGGGGCTGTGTGTGGGCGTGTTCATCTATGTTGCCTACATC
AAGTGGCACCGGGCCACCGCCACCCAGGCCTTCTTCAGCATCACCAGGGCAGCCCCGGGG
GCCCGGTGGGGTCAGCAGGCCCACAGCCCCCTGGGGACAGCTGCAGACGGGCACGAGGTC
TTCTACGGGATCATGTTTGATGCAGGAAGCACTGGCACCCGAGTACACGTCTTCCAGTTC
ACCCGGCCCCCCAGAGAAACTCCCACGTTAACCCACGAAACCTTCAAAGCAGTGAAGCCA
GGTCTTTCTGCCTATGCTGATGATGTTGAAAAGAGCGCTCAGGGAATCCGGGAACTACTG
GATGTTGCTAAACAGGACATTCCGTTCGACTTCTGGAAGGCCACCCCTCTGGTCCTCAAG
GCCACAGCTGGCTTACGCCTGTTACCTGGAGAAAAGGCCCAGAAGTTACTGCAGAAGGTG
AAAGAAGTATTTAAAGCATCGCCTTTCCTTGTAGGGGATGACTGTGTTTCCATCATGAAC
GGAACAGATGAAGGCGTTTCGGCGTGGATCACCATCAACTTCCTGACAGGCAGCTTGAAA
ACTCCAGGAGGGAGCAGCGTGGGCATGCTGGACTTGGGCGGAGGATCCACTCAGATCGCC
TTCCTGCCACGCGTGGAGGGCACCCTGCAGGCCTCCCCACCCGGCTACCTGACGGCACTG
CGGATGTTTAACAGGACCTACAAGCTCTATTCCTACAGCTACCTCGGGCTCGGGCTGATG
TCGGCACGCCTGGCGATCCTGGGCGGCGTGGAGGGGCAGCCTGCTAAGGATGGAAAGGAG
TTGGTCAGCCCTTGCTTGTCTCCCAGTTTCAAAGGAGAGTGGGAACACGCAGAAGTCACG
TACAGGGTTTCAGGGCAGAAAGCAGCGGCAAGCCTGCACGAGCTGTGTGCTGCCAGAGTG
TCAGAGGTCCTTCAAAACAGAGTGCACAGGACGGAGGAAGTGAAGCATGTGGACTTCTAT
GCTTTCTCCTACTATTACGACCTTGCAGCTGGTGTGGGCCTCATAGATGCGGAGAAGGGA
GGCAGCCTGGTGGTGGGGGACTTCGAGATCGCAGCCAAGTACGTGTGTCGGACCCTGGAG
ACACAGCCGCAGAGCAGCCCCTTCTCATGCATGGACCTCACCTACGTCAGCCTGCTACTC
CAGGAGTTCGGCTTTCCCAGGAGCAAAGTGCTGAAGCTCACTCGGAAAATTGACAATGTT
GAGACCAGCTGGGCTCTGGGGGCCATTTTTCATTACATCGACTCCCTGAACAGACAGAAG
AGTCCAGCCTCATAG
|
| Enzyme 71 GenBank Gene ID |
AF039916 |
| Enzyme 71 GeneCard ID |
ENTPD6 |
| Enzyme 71 GenAtlas ID |
ENTPD6 |
| Enzyme 71 HGNC ID |
HGNC:3368 |
| Enzyme 71 Chromosome Location |
2 |
| Enzyme 71 Locus |
20p11.21 |
| Enzyme 71 SNPs |
SNPJam Report |
| Enzyme 71 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 ]
- Ivanenkov VV, Murphy-Piedmonte DM, Kirley TL: Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function. Biochemistry. 2003 Oct 14;42(40):11726-35. [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 ]
- 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 ]
- Yeung G, Mulero JJ, McGowan DW, Bajwa SS, Ford JE: CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly expressed in the heart. Biochemistry. 2000 Oct 24;39(42):12916-23. [PubMed ]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed ]
|
| Enzyme 71 Metabolite References |
Not Available |
|
Enzyme 72
[top]
|
| Enzyme 72 ID |
6161 |
| Enzyme 72 Name |
Ectonucleoside triphosphate diphosphohydrolase 5 |
| Enzyme 72 Synonyms |
- NTPDase 5
- CD39 antigen-like 4
- ER-UDPase
- Nucleoside diphosphatase
|
| Enzyme 72 Gene Name |
ENTPD5 |
| Enzyme 72 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 5
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGT
RIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHW
KKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTV
NFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTH
SYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGF
EPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAR
EVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHL
LQSLGISH
|
| Enzyme 72 Number of Residues |
428 |
| Enzyme 72 Molecular Weight |
47517.0 |
| Enzyme 72 Theoretical pI |
6.29 |
| Enzyme 72 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 72 General Function |
Involved in hydrolase activity |
| Enzyme 72 Specific Function |
Likely to promote reglycosylation reactions involved in glycoproteins folding and quality control in the endoplasmic reticulum. Hydrolyzes UDP, GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate |
| Enzyme 72 Pathways |
|
| Enzyme 72 Reactions |
- a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
|
| Enzyme 72 Pfam Domain Function |
|
| Enzyme 72 Signals |
|
| Enzyme 72 Transmembrane Regions |
|
| Enzyme 72 Essentiality |
Not Available |
| Enzyme 72 GenBank ID Protein |
3335102 |
| Enzyme 72 UniProtKB/Swiss-Prot ID |
O75356 |
| Enzyme 72 UniProtKB/Swiss-Prot Entry Name |
ENTP5_HUMAN |
| Enzyme 72 PDB ID |
Not Available |
| Enzyme 72 Cellular Location |
Not Available |
| Enzyme 72 Gene Sequence |
>1287 bp
ATGGCCACTTCTTGGGGCACAGTCTTTTTCATGCTGGTGGTATCCTGTGTTTGCAGCGCT
GTCTCCCACAGGAACCAGCAGACTTGGTTTGAGGGTATCTTCCTGTCTTCCATGTGCCCC
ATCAATGTCAGCGCCAGCACCTTGTATGGAATTATGTTTGATGCAGGGAGCACTGGAACT
CGAATTCATGTTTACACCTTTGTGCAGAAAATGCCAGGACAGCTTCCAATTCTAGAAGGG
GAAGTTTTTGATTCTGTGAAGCCAGGACTTTCTGCTTTTGTAGATCAACCTAAGCAGGGT
GCTGAGACCGTTCAAGGGCTCTTAGAGGTGGCCAAAGACTCAATCCCCCGAAGTCACTGG
AAAAAGACCCCAGTGGTCCTAAAGGCAACAGCAGGACTACGCTTACTGCCAGAACACAAA
GCCAAGGCTCTGCTCTTTGAGGTAAAGGAGATCTTCAGGAAGTCACCTTTCCTGGTACCA
AAGGGCAGTGTTAGCATCATGGATGGATCCGACGAAGGCATATTAGCTTGGGTTACTGTG
AATTTTCTGACAGGTCAGCTGCATGGCCACAGACAGGAGACTGTGGGGACCTTGGACCTA
GGGGGAGCCTCCACCCAAATCACGTTCCTGCCCCAGTTTGAGAAAACTCTGGAACAAACT
CCTAGGGGCTACCTCACTTCCTTTGAGATGTTTAACAGCACTTATAAGCTCTATACACAT
AGTTACTTGGGATTTGGATTGAAAGCTGCAAGACTAGCAACCCTGGGAGCCCTGGAGACA
GAAGGGACTGATGGGCACACTTTCCGGAGTGCCTGTTTACCGAGATGGTTGGAAGCAGAG
TGGATCTTTGGGGGTGTGAAATACCAGTATGGTGGCAACCAAGAAGGGGAGGTGGGCTTT
GAGCCCTGCTATGCCGAAGTGCTGAGGGTGGTACGAGGAAAACTTCACCAGCCAGAGGAG
GTCCAGAGAGGTTCCTTCTATGCTTTCTCTTACTATTATGACCGAGCTGTTGACACAGAC
ATGATTGATTATGAAAAGGGGGGTATTTTAAAAGTTGAAGATTTTGAAAGAAAAGCCAGG
GAAGTGTGTGATAACTTGGAAAACTTCACCTCAGGCAGTCCTTTCCTGTGCATGGATCTC
AGCTACATCACAGCCCTGTTAAAGGATGGCTTTGGCTTTGCAGACAGCACAGTCTTACAG
CTCACAAAGAAAGTGAACAACATAGAGACGGGCTGGGCCTTGGGGGCCACCTTTCACCTG
TTGCAGTCTCTGGGCATCTCCCATTGA
|
| Enzyme 72 GenBank Gene ID |
AF039918 |
| Enzyme 72 GeneCard ID |
ENTPD5 |
| Enzyme 72 GenAtlas ID |
ENTPD5 |
| Enzyme 72 HGNC ID |
HGNC:3367 |
| Enzyme 72 Chromosome Location |
1 |
| Enzyme 72 Locus |
14q24 |
| Enzyme 72 SNPs |
SNPJam Report |
| Enzyme 72 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 ]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed ]
- 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 72 Metabolite References |
Not Available |
|
Enzyme 73
[top]
|
| Enzyme 73 ID |
6176 |
| Enzyme 73 Name |
Multifunctional protein ADE2 |
| Enzyme 73 Synonyms |
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- SAICAR synthetase
- Phosphoribosylaminoimidazole carboxylase
- AIR carboxylase
- AIRC
|
| Enzyme 73 Gene Name |
PAICS |
| Enzyme 73 Protein Sequence |
>Multifunctional protein ADE2
MATAEVLNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKI
TSCIFQLLQEAGIKTAFTRKCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYK
FYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQTEVDIMSHATQAIFEILEKSW
LPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPE
GLQMVKKNFEWVAERVELLLKSESQCRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVT
SAHKGPDETLRIKAEYEGDGIPTVFVAVAGRSNGLGPVMSGNTAYPVISCPPLTPDWGVQ
DVWSSLRLPSGLGCSTVLSPEGSAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKI
RECNL
|
| Enzyme 73 Number of Residues |
425 |
| Enzyme 73 Molecular Weight |
47078.8 |
| Enzyme 73 Theoretical pI |
7.26 |
| Enzyme 73 GO Classification |
| Function |
- ATP binding
- acid-amino acid ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- lyase activity
- nucleoside binding
- phosphoribosylaminoimidazole carboxylase activity
- phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
- purine nucleoside binding
|
| Process |
- 'de novo' IMP biosynthetic process
- IMP biosynthetic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside monophosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside monophosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 73 General Function |
Involved in phosphoribosylaminoimidazole carboxylase activity |
| Enzyme 73 Specific Function |
ATP + 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate |
| Enzyme 73 Pathways |
|
| Enzyme 73 Reactions |
- ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido]succinate [RN:R04591]
|
| Enzyme 73 Pfam Domain Function |
|
| Enzyme 73 Signals |
|
| Enzyme 73 Transmembrane Regions |
|
| Enzyme 73 Essentiality |
Not Available |
| Enzyme 73 GenBank ID Protein |
28384 |
| Enzyme 73 UniProtKB/Swiss-Prot ID |
P22234 |
| Enzyme 73 UniProtKB/Swiss-Prot Entry Name |
PUR6_HUMAN |
| Enzyme 73 PDB ID |
Not Available |
| Enzyme 73 Cellular Location |
Not Available |
| Enzyme 73 Gene Sequence |
>1278 bp
ATGGCGACAGCTGAGGTACTGAACATTGGTAAAAAATTATATGAGGGTAAAACAAAAGAA
GTCTACGAATTGTTAGACAGTCCAGGAAAAGTCCTCCTGCAGTCCAAGGACCAGATTACA
GCAGGAAATGCAGCTAGAAAAAACCACCTGGAAGGAAAAGCTGCAATCTCAAATAAAATC
ACCAGTTGTATTTTTCAGTTATTACAGGAAGCAGGTATTAAAACTGCCTTCACCAGAAAA
TGTGGGGAGACAGCTTTCATTGCACCGCAGTGTGAAATGATTCCAATTGAATGGGTTTGC
AGAAGAATAGCAACTGGTTCTTTTCTCAAAAGAAATCCTGGTGTCAAGGAAGGATATAAG
TTTTACCCACCTAAAGTGGAGTTGTTTTTCAAGGATGATGCCAATAATGACCCACAGTGG
TCTGAGGAACAGCTGATTGCTGCAAAATTTTGCTTTGCTGGACTTCTTATAGGCCAGACT
GAAGTGGATATCATGAGTCATGCTACACAGGCTATATTTGAAATACTGGAGAAATCCTGG
TTGCCCCAGAATTGTACACTGGTTGATATGAAGATTGAATTTGGTGTTGATGTAACCACC
AAAGAAATTGTTCTTGCTGATGTTATTGACAATGATTCCTGGAGACTCTGGCCATCAGGA
GATCGAAGCCAACAGAAAGACAAACAGTCTTATCGGGACCTCAAAGAAGTAACTCCTGAA
GGGCTCCAAATGGTAAAGAAAAACTTTGAGTGGGTTGCAGAGAGAGTAGAGTTGCTTTTG
AAATCAGAAAGTCAGTGCAGGGTTGTAGTGTTGATGGGCTCTACTTCTGATCTTGGTCAC
TGTGAAAAAATCAAGAAGGCCTGTGGAAATTTTGGCATTCCATGTGAACTTCGAGTAACA
TCTGCGCATAAAGGACCAGATGAAACTCTGAGGATTAAAGCTGAGTATGAAGGGGATGGC
ATTCCTACTGTATTTGTGGCAGTGGCAGGCAGAAGTAATGGTTTGGGACCAGTGATGTCT
GGGAACACTGCATATCCAGTTATCAGCTGTCCTCCCCTCACACCAGACTGGGGAGTTCAG
GATGTGTGGTCTTCTCTTCGACTACCCAGTGGTCTTGGCTGTTCAACCGTACTTTCTCCA
GAAGGATCAGCTCAATTTGCTGCTCAGATATTTGGGTTAAGCAACCATTTGGTATGGAGC
AAACTGCGAGCAAGCATTTTGAACACATGGATTTCCTTGAAGCAGGCTGACAAGAAAATC
AGAGAATGTAATTTATAA
|
| Enzyme 73 GenBank Gene ID |
X53793 |
| Enzyme 73 GeneCard ID |
PAICS |
| Enzyme 73 GenAtlas ID |
PAICS |
| Enzyme 73 HGNC ID |
HGNC:8587 |
| Enzyme 73 Chromosome Location |
4 |
| Enzyme 73 Locus |
4q12 |
| Enzyme 73 SNPs |
SNPJam Report |
| Enzyme 73 General References |
- Minet M, Lacroute F: Cloning and sequencing of a human cDNA coding for a multifunctional polypeptide of the purine pathway by complementation of the ade2-101 mutant in Saccharomyces cerevisiae. Curr Genet. 1990 Nov;18(4):287-91. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Li SX, Tong YP, Xie XC, Wang QH, Zhou HN, Han Y, Zhang ZY, Gao W, Li SG, Zhang XC, Bi RC: Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis. J Mol Biol. 2007 Mar 9;366(5):1603-14. Epub 2006 Dec 16. [PubMed ]
|
| Enzyme 73 Metabolite References |
Not Available |
|
Enzyme 74
[top]
|
| Enzyme 74 ID |
6205 |
| Enzyme 74 Name |
NAD kinase |
| Enzyme 74 Synonyms |
- Poly(P)/ATP NAD kinase
|
| Enzyme 74 Gene Name |
NADK |
| Enzyme 74 Protein Sequence |
>NAD kinase
MEMEQEKMTMNKELSPDAAAYCCSACHGDETWSYNHPIRGRAKSRSLSASPALGSTKEFR
RTRSLHGPCPVTTFGPKACVLQNPQTIMHIQDPASQRLTWNKSPKSVLVIKKMRDASLLQ
PFKELCTHLMEENMIVYVEKKVLEDPAIASDESFGAVKKKFCTFREDYDDISNQIDFIIC
LGGDGTLLYASSLFQGSVPPVMAFHLGSLGFLTPFSFENFQSQVTQVIEGNAAVVLRSRL
KVRVVKELRGKKTAVHNGLGENGSQAAGLDMDVGKQAMQYQVLNEVVIDRGPSSYLSNVD
VYLDGHLITTVQGDGVIVSTPTGSTAYAAAAGASMIHPNVPAIMITPICPHSLSFRPIVV
PAGVELKIMLSPEARNTAWVSFDGRKRQEIRHGDSISITTSCYPLPSICVRDPVSDWFES
LAQCLHWNVRKKQAHFEEEEEEEEEG
|
| Enzyme 74 Number of Residues |
446 |
| Enzyme 74 Molecular Weight |
49227.8 |
| Enzyme 74 Theoretical pI |
6.44 |
| Enzyme 74 GO Classification |
| Function |
- NAD+ kinase activity
- NAD+ kinase activity
- NAD+ kinase activity
- NAD+ kinase activity
- catalytic activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 74 General Function |
Involved in NAD+ kinase activity |
| Enzyme 74 Specific Function |
ATP + NAD(+) = ADP + NADP(+) |
| Enzyme 74 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760 )
|
| Enzyme 74 Reactions |
- ATP + NAD+ = ADP + NADP+ [RN:R00104]
|
| Enzyme 74 Pfam Domain Function |
|
| Enzyme 74 Signals |
|
| Enzyme 74 Transmembrane Regions |
|
| Enzyme 74 Essentiality |
Not Available |
| Enzyme 74 GenBank ID Protein |
312222779 |
| Enzyme 74 UniProtKB/Swiss-Prot ID |
O95544 |
| Enzyme 74 UniProtKB/Swiss-Prot Entry Name |
NADK_HUMAN |
| Enzyme 74 PDB ID |
Not Available |
| Enzyme 74 Cellular Location |
Not Available |
| Enzyme 74 Gene Sequence |
>1341 bp
ATGGAAATGGAACAAGAAAAAATGACCATGAATAAGGAATTGAGTCCAGACGCGGCTGCT
TACTGCTGCTCGGCCTGCCACGGCGATGAGACCTGGAGTTACAACCACCCCATCCGGGGC
CGGGCCAAGTCTCGCAGCCTGTCTGCCTCGCCCGCCCTGGGGAGCACCAAGGAGTTCAGG
AGGACACGCTCTCTTCATGGGCCATGCCCGGTGACCACTTTTGGACCAAAGGCCTGTGTG
CTGCAGAACCCCCAGACCATCATGCACATTCAGGACCCCGCGAGCCAGCGGCTGACGTGG
AACAAGTCCCCAAAGAGCGTCCTTGTCATCAAGAAGATGAGAGATGCCAGCCTACTGCAG
CCGTTCAAGGAGCTCTGCACGCACCTCATGGAGGAGAACATGATCGTGTATGTGGAAAAG
AAAGTGCTAGAAGACCCTGCCATCGCCAGCGATGAAAGCTTTGGGGCAGTGAAGAAGAAA
TTCTGTACCTTTCGAGAAGATTATGATGACATTTCCAATCAGATAGACTTCATCATCTGC
CTGGGGGGAGACGGGACGCTGCTGTACGCTTCCTCGCTTTTCCAGGGCAGCGTCCCTCCG
GTCATGGCCTTCCACCTGGGCTCCCTGGGCTTCCTGACCCCATTCAGCTTTGAGAACTTT
CAGTCCCAAGTTACTCAGGTGATAGAGGGGAACGCAGCTGTTGTTCTCCGGAGTCGGCTG
AAGGTCAGGGTGGTGAAGGAGCTCCGGGGGAAGAAGACGGCCGTGCACAATGGGCTGGGT
GAGAACGGCTCGCAGGCTGCAGGCCTGGACATGGATGTCGGGAAGCAGGCCATGCAGTAC
CAGGTCCTGAATGAGGTGGTGATTGACAGAGGCCCCTCCTCCTACCTGTCCAATGTGGAT
GTCTACCTGGACGGACACCTCATCACCACGGTGCAGGGCGACGGAGTGATCGTGTCCACC
CCGACGGGCAGCACGGCGTATGCGGCCGCGGCCGGGGCCTCCATGATCCACCCCAACGTG
CCGGCCATCATGATCACGCCCATCTGCCCCCACTCGCTGTCCTTCCGGCCCATCGTGGTC
CCCGCAGGGGTCGAGCTGAAGATCATGCTGTCACCTGAAGCAAGGAACACAGCATGGGTG
TCCTTTGATGGACGGAAGAGACAAGAGATCCGCCATGGAGACAGCATCAGCATCACTACC
TCATGCTACCCGCTCCCCTCCATCTGTGTGCGGGACCCCGTGAGCGACTGGTTTGAGAGC
CTCGCCCAGTGCCTGCATTGGAACGTCCGGAAGAAGCAAGCCCACTTCGAGGAGGAGGAG
GAGGAGGAGGAGGAGGGCTAG
|
| Enzyme 74 GenBank Gene ID |
NM_001198993.1 |
| Enzyme 74 GeneCard ID |
NADK |
| Enzyme 74 GenAtlas ID |
NADK |
| Enzyme 74 HGNC ID |
HGNC:29831 |
| Enzyme 74 Chromosome Location |
1 |
| Enzyme 74 Locus |
1p36.33 |
| Enzyme 74 SNPs |
SNPJam Report |
| Enzyme 74 General References |
- Lerner F, Niere M, Ludwig A, Ziegler M: Structural and functional characterization of human NAD kinase. Biochem Biophys Res Commun. 2001 Oct 19;288(1):69-74. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- 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 ]
|
| Enzyme 74 Metabolite References |
Not Available |
|
Enzyme 75
[top]
|
| Enzyme 75 ID |
6206 |
| Enzyme 75 Name |
ADP-ribosyl cyclase 1 |
| Enzyme 75 Synonyms |
- Cyclic ADP-ribose hydrolase 1
- cADPr hydrolase 1
- T10
- CD38 antigen
|
| Enzyme 75 Gene Name |
CD38 |
| Enzyme 75 Protein Sequence |
>ADP-ribosyl cyclase 1
MANCEFSPVSGDKPCCRLSRRAQLCLGVSILVLILVVVLAVVVPRWRQQWSGPGTTKRFP
ETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCN
KILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDC
SNNPVSVFWKTVSRRFAEAACDVVHVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEA
WVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKFLQCVKNPEDSSCTSEI
|
| Enzyme 75 Number of Residues |
300 |
| Enzyme 75 Molecular Weight |
34328.1 |
| Enzyme 75 Theoretical pI |
7.72 |
| Enzyme 75 GO Classification |
| Function |
- NAD+ nucleosidase activity
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing N-glycosyl compounds
|
| Process |
|
| Component |
| — |
|
| Enzyme 75 General Function |
Involved in NAD+ nucleosidase activity |
| Enzyme 75 Specific Function |
Synthesizes cyclic ADP-ribose, a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity. Also moonlights as a receptor in cells of the immune system |
| Enzyme 75 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760 )
|
| Enzyme 75 Reactions |
- NAD+ + H2O = ADP-ribose + nicotinamide [RN:R00102]
|
| Enzyme 75 Pfam Domain Function |
|
| Enzyme 75 Signals |
|
| Enzyme 75 Transmembrane Regions |
|
| Enzyme 75 Essentiality |
Not Available |
| Enzyme 75 GenBank ID Protein |
14044085 |
| Enzyme 75 UniProtKB/Swiss-Prot ID |
P28907 |
| Enzyme 75 UniProtKB/Swiss-Prot Entry Name |
CD38_HUMAN |
| Enzyme 75 PDB ID |
Not Available |
| Enzyme 75 Cellular Location |
Not Available |
| Enzyme 75 Gene Sequence |
>903 bp
ATGGCCAACTGCGAGTTCAGCCCGGTGTCCGGGGACAAACCCTGCTGCCGGCTCTCTAGG
AGAGCCCAACTCTGTCTTGGCGTCAGTATCCTGGTCCTGATCCTCGTCGTGGTGCTCGCG
GTGGTCGTCCCGAGGTGGCGCCAGCAGTGGAGCGGTCCGGGCACCACCAAGCGCTTTCCC
GAGACCGTCCTGGCGCGATGCGTCAAGTACACTGAAATTCATCCTGAGATGAGACATGTA
GACTGCCAAAGTGTATGGGATGCTTTCAAGGGTGCATTTATTTCAAAACATCCTTGCAAC
ATTACTGAAGAAGACTATCAGCCACTAATGAAGTTGGGAACTCAGACCGTACCTTGCAAC
AAGATTCTTCTTTGGAGCAGAATAAAAGATCTGGCCCATCAGTTCACACAGGTCCAGCGG
GACATGTTCACCCTGGAGGACACGCTGCTAGGCTACCTTGCTGATGACCTCACATGGTGT
GGTGAATTCAACACTTCCAAAATAAACTATCAATCTTGCCCAGACTGGAGAAAGGACTGC
AGCAACAACCCTGTTTCAGTATTCTGGAAAACGGTTTCCCGCAGGTTTGCAGAAGCTGCC
TGTGATGTGGTCCATGTGATGCTCAATGGATCCCGCAGTAAAATCTTTGACAAAAACAGC
ACTTTTGGGAGTGTGGAAGTCCATAATTTGCAACCAGAGAAGGTTCAGACACTAGAGGCC
TGGGTGATACATGGTGGAAGAGAAGATTCCAGAGACTTATGCCAGGATCCCACCATAAAA
GAGCTGGAATCGATTATAAGCAAAAGGAATATTCAATTTTCCTGCAAGAATATCTACAGA
CCTGACAAGTTTCTTCAGTGTGTGAAAAATCCTGAGGATTCATCTTGCACATCTGAGATC
TGA
|
| Enzyme 75 GenBank Gene ID |
BC007964 |
| Enzyme 75 GeneCard ID |
CD38 |
| Enzyme 75 GenAtlas ID |
CD38 |
| Enzyme 75 HGNC ID |
HGNC:1667 |
| Enzyme 75 Chromosome Location |
4 |
| Enzyme 75 Locus |
4p15 |
| Enzyme 75 SNPs |
SNPJam Report |
| Enzyme 75 General References |
- Jackson DG, Bell JI: Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation. J Immunol. 1990 Apr 1;144(7):2811-5. [PubMed ]
- Nata K, Takamura T, Karasawa T, Kumagai T, Hashioka W, Tohgo A, Yonekura H, Takasawa S, Nakamura S, Okamoto H: Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing. Gene. 1997 Feb 28;186(2):285-92. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- States DJ, Walseth TF, Lee HC: Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38. Trends Biochem Sci. 1992 Dec;17(12):495. [PubMed ]
- Takasawa S, Tohgo A, Noguchi N, Koguma T, Nata K, Sugimoto T, Yonekura H, Okamoto H: Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP. J Biol Chem. 1993 Dec 15;268(35):26052-4. [PubMed ]
- Tohgo A, Takasawa S, Noguchi N, Koguma T, Nata K, Sugimoto T, Furuya Y, Yonekura H, Okamoto H: Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38. J Biol Chem. 1994 Nov 18;269(46):28555-7. [PubMed ]
- Hillman RT, Green RE, Brenner SE: An unappreciated role for RNA surveillance. Genome Biol. 2004;5(2):R8. Epub 2004 Feb 2. [PubMed ]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
- Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed ]
- Liu Q, Kriksunov IA, Graeff R, Munshi C, Lee HC, Hao Q: Crystal structure of human CD38 extracellular domain. Structure. 2005 Sep;13(9):1331-9. [PubMed ]
- Yagui K, Shimada F, Mimura M, Hashimoto N, Suzuki Y, Tokuyama Y, Nata K, Tohgo A, Ikehata F, Takasawa S, Okamoto H, Makino H, Saito Y, Kanatsuka A: A missense mutation in the CD38 gene, a novel factor for insulin secretion: association with Type II diabetes mellitus in Japanese subjects and evidence of abnormal function when expressed in vitro. Diabetologia. 1998 Sep;41(9):1024-8. [PubMed ]
|
| Enzyme 75 Metabolite References |
Not Available |
|
Enzyme 76
[top]
|
| Enzyme 76 ID |
6211 |
| Enzyme 76 Name |
C-1-tetrahydrofolate synthase, cytoplasmic |
| Enzyme 76 Synonyms |
- C1-THF synthase
- Methylenetetrahydrofolate dehydrogenase
- Methenyltetrahydrofolate cyclohydrolase
- Formyltetrahydrofolate synthetase
|
| Enzyme 76 Gene Name |
MTHFD1 |
| Enzyme 76 Protein Sequence |
>C-1-tetrahydrofolate synthase, cytoplasmic
MAPAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAILQVGNRDDSNLYINVKLKAA
EEIGIKATHIKLPRTTTESEVMKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAP
EKDVDGLTSINAGRLARGDLNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAP
MHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY
VPDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEKFKP
GKWMIQYNNLNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSAL
ERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLYQNVFACVRQPSQGPTFGI
KGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLV
PSVNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRF
LRKITIGQAPTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPV
SAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVG
PEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGLPLP
KAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAF
DAVKCTHWAEGGKGALALAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIE
LLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFILPIRDIRASVGAGFL
YPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
|
| Enzyme 76 Number of Residues |
935 |
| Enzyme 76 Molecular Weight |
101558.4 |
| Enzyme 76 Theoretical pI |
7.32 |
| Enzyme 76 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- formate-tetrahydrofolate ligase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
|
| Process |
- cellular aromatic compound metabolic process
- cellular metabolic process
- folic acid and derivative biosynthetic process
- folic acid and derivative metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 76 General Function |
Involved in formate-tetrahydrofolate ligase activity |
| Enzyme 76 Specific Function |
5,10-methylenetetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH |
| Enzyme 76 Pathways |
- Glyoxylate and Dicarboxylate Metabolism (map00630 )
- One Carbon Pool By Folate (map00670 )
|
| Enzyme 76 Reactions |
- ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate [RN:R00943]
|
| Enzyme 76 Pfam Domain Function |
|
| Enzyme 76 Signals |
|
| Enzyme 76 Transmembrane Regions |
|
| Enzyme 76 Essentiality |
Not Available |
| Enzyme 76 GenBank ID Protein |
189065440 |
| Enzyme 76 UniProtKB/Swiss-Prot ID |
P11586 |
| Enzyme 76 UniProtKB/Swiss-Prot Entry Name |
C1TC_HUMAN |
| Enzyme 76 PDB ID |
1DIA |
| Enzyme 76 PDB File |
Show |
| Enzyme 76 3D Structure |
|
| Enzyme 76 Cellular Location |
Not Available |
| Enzyme 76 Gene Sequence |
>2808 bp
ATGGCGCCAGCAGAAATCCTGAACGGGAAGGAGATCTCCGCGCAAATAAGGGCGAGACTG
AAAAATCAAGTCACTCAGTTGAAGGAGCAAGTACCTGGTTTCACACCACGCCTGGCAATA
TTACAGGTTGGCAACAGAGATGATTCCAATCTTTATATAAATGTGAAGCTGAAGGCTGCT
GAAGAGATTGGGATCAAAGCCACTCACATTAAGTTACCAAGAACAACCACAGAATCTGAG
GTGATGAAGTACATTACATCTTTGAATGAAGACTCTACTGTACATGGGTTCTTAGTGCAG
CTACCTTTAGATTCAGAGAATTCCATTAACACTGAAGAAGTGATCAATGCTATTGCACCC
GAGAAGGATGTGGATGGATTGACTAGCATCAATGCTGGGAGACTTGCTAGAGGTGACCTC
AATGACTGTTTCATTCCTTGTACGCCTAAGGGATGCTTGGAACTCATCAAAGAGACAGGG
GTGCCGATTGCCGGAAGGCATGCTGTGGTGGTTGGGCGCAGTAAAATAGTTGGGGCCCCG
ATGCATGACTTGCTTCTGTGGAACAATGCCACAGTGACCACCTGCCACTCCAAGACTGCC
CATCTGGATGAGGAGGTAAATAAAGGTGACATCCTGGTGGTTGCAACTGGTCAGCCTGAA
ATGGTTAAAGGGGAGTGGATCAAACCTGGGGCAATAGTCATCGACTGTGGAATCAATTAT
GTCCCAGATGATAAAAAACCAAATGGGAGAAAAGTTGTGGGTGATGTGGCATACGACGAG
GCCAAAGAGAGGGCGAGCTTCATCACTCCTGTTCCTGGCGGCGTAGGGCCCATGACAGTT
GCAATGCTCATGCAGAGCACAGTAGAGAGTGCCAAGCGTTTCCTGGAGAAATTTAAGCCA
GGAAAGTGGATGATTCAGTATAACAACCTTAACCTCAAGACACCTGTTCCAAGTGACATT
GATATATCACGATCTTGTAAACCGAAGCCCATTGGTAAGCTGGCTCGAGAAATTGGTCTG
CTGTCTGAAGAGGTAGAATTATATGGTGAAACAAAGGCCAAAGTTCTGCTGTCAGCACTA
GAACGCCTGAAGCACCGGCCTGATGGGAAATACGTGGTGGTGACTGGAATAACTCCAACA
CCCCTGGGAGAAGGGAAAAGCACAACTACAATCGGGCTAGTGCAAGCCCTTGGTGCCCAT
CTCTACCAGAATGTCTTTGCGTGTGTGCGACAGCCTTCTCAGGGCCCCACCTTTGGAATA
AAAGGTGGCGCTGCAGGAGGCGGCTACTCCCAGGTCATTCCTATGGAAGAGTTTAATCTC
CACCTCACAGGTGACATCCATGCCATCACTGCAGCTAATAACCTCGTTGCTGCGGCCATT
GATGCTCGGATATTTCATGAACTGACCCAGACAGACAAGGCTCTCTTTAATCGTTTGGTG
CCATCAGTAAATGGAGTGAGAAGGTTCTCTGACATCCAAATCCGAAGGTTAAAGAGACTA
GGCATTGAAAAGACTGACCCTACCACACTGACAGATGAAGAGATAAACAGATTTGCAAGA
TTGGACATTGATCCAGAAACCATAACTTGGCAAAGAGTGTTGGATACCAATGATAGATTC
CTGAGGAAGATCACGATTGGACAGGCTCCAACGGAGAAGGGTCACACACGGACGGCCCAG
TTTGATATCTCTGTGGCCAGTGAAATTATGGCTGTCCTGGCTCTCACCACTTCTCTAGAA
GACATGAGAGAGAGACTGGGCAAAATGGTGGTGGCATCCAGTAAGAAAGGAGAGCCCGTC
AGTGCCGAAGATCTGGGGGTGAGTGGTGCACTGACAGTGCTTATGAAGGACGCAATCAAG
CCCAATCTCATGCAGACACTGGAGGGCACTCCAGTGTTTGTCCATGCTGGCCCGTTTGCC
AACATCGCACATGGCAATTCCTCCATCATTGCAGACCAGATCGCACTCAAGCTTGTTGGC
CCAGAAGGGTTTGTAGTGACGGAAGCAGGATTTGGAGCAGACATTGGAATGGAAAAGTTT
TTTAACATCAAATGCCGGTATTCCGGCCTCTGCCCCCACGTGGTGGTGCTTGTTGCCACT
GTCAGGGCTCTCAAGATGCACGGGGGCGGCCCCACGGTCACTGCTGGACTGCCTCTTCCC
AAGGCTTACATACAGGAGAACCTGGAGCTGGTTGAAAAAGGCTTCAGTAACTTGAAGAAA
CAAATTGAAAATGCCAGAATGTTTGGAATTCCAGTAGTAGTGGCCGTGAATGCATTCAAG
ACGGATACAGAGTCTGAGCTGGACCTCATCAGCCGCCTTTCCAGAGAACATGGGGCTTTT
GATGCCGTGAAGTGCACTCACTGGGCAGAAGGGGGCAAGGGTGCCTTAGCCCTGGCTCAG
GCCGTCCAGAGAGCAGCACAAGCACCCAGCAGCTTCCAGCTCCTTTATGACCTCAAGCTC
CCAGTTGAGGATAAAATCAGGATCATTGCACAGAAGATCTATGGAGCAGATGACATTGAA
TTACTTCCCGAAGCTCAACACAAAGCTGAAGTCTACACGAAGCAGGGCTTTGGGAATCTC
CCCATCTGCATGGCTAAAACACACTTGTCTTTGTCTCACAACCCAGAGCAAAAAGGTGTC
CCTACAGGCTTCATTCTGCCCATTCGCGACATCCGCGCCAGCGTTGGGGCTGGTTTTCTG
TACCCCTTAGTAGGAACGATGAGCACAATGCCTGGACTCCCCACCCGGCCCTGTTTTTAT
GATATTGATTTGGACCCTGAAACAGAACAGGTGAATGGATTATTCTAA
|
| Enzyme 76 GenBank Gene ID |
AK312361 |
| Enzyme 76 GeneCard ID |
MTHFD1 |
| Enzyme 76 GenAtlas ID |
MTHFD1 |
| Enzyme 76 HGNC ID |
HGNC:7432 |
| Enzyme 76 Chromosome Location |
1 |
| Enzyme 76 Locus |
14q24 |
| Enzyme 76 SNPs |
SNPJam Report |
| Enzyme 76 General References |
- Hum DW, Bell AW, Rozen R, MacKenzie RE: Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. J Biol Chem. 1988 Nov 5;263(31):15946-50. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Allaire M, Li Y, MacKenzie RE, Cygler M: The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution. Structure. 1998 Feb 15;6(2):173-82. [PubMed ]
- Schmidt A, Wu H, MacKenzie RE, Chen VJ, Bewly JR, Ray JE, Toth JE, Cygler M: Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase. Biochemistry. 2000 May 30;39(21):6325-35. [PubMed ]
- Hol FA, van der Put NM, Geurds MP, Heil SG, Trijbels FJ, Hamel BC, Mariman EC, Blom HJ: Molecular genetic analysis of the gene encoding the trifunctional enzyme MTHFD (methylenetetrahydrofolate-dehydrogenase, methenyltetrahydrofolate-cyclohydrolase, formyltetrahydrofolate synthetase) in patients with neural tube defects. Clin Genet. 1998 Feb;53(2):119-25. [PubMed ]
- Brody LC, Conley M, Cox C, Kirke PN, McKeever MP, Mills JL, Molloy AM, O'Leary VB, Parle-McDermott A, Scott JM, Swanson DA: A polymorphism, R653Q, in the trifunctional enzyme methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase is a maternal genetic risk factor for neural tube defects: report of the Birth Defects Research Group. Am J Hum Genet. 2002 Nov;71(5):1207-15. Epub 2002 Oct 16. [PubMed ]
- Parle-McDermott A, Kirke PN, Mills JL, Molloy AM, Cox C, O'Leary VB, Pangilinan F, Conley M, Cleary L, Brody LC, Scott JM: Confirmation of the R653Q polymorphism of the trifunctional C1-synthase enzyme as a maternal risk for neural tube defects in the Irish population. Eur J Hum Genet. 2006 Jun;14(6):768-72. [PubMed ]
- Webb EL, Rudd MF, Sellick GS, El Galta R, Bethke L, Wood W, Fletcher O, Penegar S, Withey L, Qureshi M, Johnson N, Tomlinson I, Gray R, Peto J, Houlston RS: Search for low penetrance alleles for colorectal cancer through a scan of 1467 non-synonymous SNPs in 2575 cases and 2707 controls with validation by kin-cohort analysis of 14 704 first-degree relatives. Hum Mol Genet. 2006 Nov 1;15(21):3263-71. Epub 2006 Sep 25. [PubMed ]
- Christensen KE, Rohlicek CV, Andelfinger GU, Michaud J, Bigras JL, Richter A, Mackenzie RE, Rozen R: The MTHFD1 p.Arg653Gln variant alters enzyme function and increases risk for congenital heart defects. Hum Mutat. 2009 Feb;30(2):212-20. [PubMed ]
|
| Enzyme 76 Metabolite References |
Not Available |
|
Enzyme 77
[top]
|
| Enzyme 77 ID |
6218 |
| Enzyme 77 Name |
Guanylate kinase |
| Enzyme 77 Synonyms |
- GMP kinase
|
| Enzyme 77 Gene Name |
GUK1 |
| Enzyme 77 Protein Sequence |
>Guanylate kinase
MSGPRPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREV
MQRDIAAGDFIEHAEFSGNLYGTSKVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYI
SVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEPGLFDVVIINDSLDQAYAE
LKEALSEEIKKAQRTGA
|
| Enzyme 77 Number of Residues |
197 |
| Enzyme 77 Molecular Weight |
21725.4 |
| Enzyme 77 Theoretical pI |
6.53 |
| Enzyme 77 GO Classification |
| Function |
- catalytic activity
- guanylate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleotide metabolic process
|
| Component |
| — |
|
| Enzyme 77 General Function |
Involved in guanylate kinase activity |
| Enzyme 77 Specific Function |
Essential for recycling GMP and indirectly, cGMP |
| Enzyme 77 Pathways |
|
| Enzyme 77 Reactions |
- ATP + GMP = ADP + GDP [RN:R00332]
|
| Enzyme 77 Pfam Domain Function |
|
| Enzyme 77 Signals |
|
| Enzyme 77 Transmembrane Regions |
|
| Enzyme 77 Essentiality |
Not Available |
| Enzyme 77 GenBank ID Protein |
1196436 |
| Enzyme 77 UniProtKB/Swiss-Prot ID |
Q16774 |
| Enzyme 77 UniProtKB/Swiss-Prot Entry Name |
KGUA_HUMAN |
| Enzyme 77 PDB ID |
Not Available |
| Enzyme 77 Cellular Location |
Not Available |
| Enzyme 77 Gene Sequence |
>594 bp
ATGTCGGGCCCCAGGCCTGTGGTGCTGAGCGGGCCTTCGGGAGCTGGGAAGAGCACCCTG
CTGAAGAGGCTGCTCCAGGAGCACAGCGGCATCTTTGGCTTCAGCGTGTCCCATACCACG
AGGAACCCGAGGCCCGGCGAGGAGAACGGCAAAGATTACTACTTTGTAACCAGGGAGGTG
ATGCAGCGTGACATAGCAGCCGGCGACTTCATCGAGCATGCCGAGTTCTCGGGGAACCTG
TATGGCACGAGCAAGGTGGCGGTGCAGGCCGTGCAGGCCATGAACCGCATCTGTGTGCTG
GACGTGGACCTGCAGGGTGTGCGGAACATCAAGGCCACCGATCTGCGGCCCATCTACATC
TCTGTGCAGCCGCCTTCACTGCACGTGCTGGAGCAGCGGCTGCGGCAGCGCAACACTGAA
ACCGAGGAGAGCCTGGTGAAGCGGCTGGCTGCTGCCCAGGCCGACATGGAGAGCAGCAAG
GAGCCCGGCCTGTTTGATGTGGTCATCATTAACGACAGCCTGGACCAGGCCTACGCAGAG
CTGAAGGAGGCGCTCTCTGAGGAAATCAAGAAAGCTCAAAGGACCGGCGCCTGA
|
| Enzyme 77 GenBank Gene ID |
L76200 |
| Enzyme 77 GeneCard ID |
GUK1 |
| Enzyme 77 GenAtlas ID |
GUK1 |
| Enzyme 77 HGNC ID |
HGNC:4693 |
| Enzyme 77 Chromosome Location |
1 |
| Enzyme 77 Locus |
1q32-q41 |
| Enzyme 77 SNPs |
SNPJam Report |
| Enzyme 77 General References |
- Fitzgibbon J, Katsanis N, Wells D, Delhanty J, Vallins W, Hunt DM: Human guanylate kinase (GUK1): cDNA sequence, expression and chromosomal localisation. FEBS Lett. 1996 May 6;385(3):185-8. [PubMed ]
- Brady WA, Kokoris MS, Fitzgibbon M, Black ME: Cloning, characterization, and modeling of mouse and human guanylate kinases. J Biol Chem. 1996 Jul 12;271(28):16734-40. [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 77 Metabolite References |
Not Available |
|
Enzyme 78
[top]
|
| Enzyme 78 ID |
6271 |
| Enzyme 78 Name |
Inositol-trisphosphate 3-kinase B |
| Enzyme 78 Synonyms |
- Inositol 1,4,5-trisphosphate 3-kinase B
- IP3 3-kinase B
- IP3K B
- InsP 3-kinase B
|
| Enzyme 78 Gene Name |
ITPKB |
| Enzyme 78 Protein Sequence |
>Inositol-trisphosphate 3-kinase B
MAVYCYALNSLVIMNSANEMKSGGGPGPSGSETPPPPRRAVLSPGSVFSPGRGASFLFPP
AESLSPEEPRSPGGWRSGRRRLNSSSGSGSGSSGSSVSSPSWAGRLRGDRQQVVAAGTLS
PPGPEEAKRKLRILQRELQNVQVNQKVGMFEAHIQAQSSAIQAPRSPRLGRARSPSPCPF
RSSSQPPGRVLVQGARSEERRTKSWGEQCPETSGTDSGRKGGPSLCSSQVKKGMPPLPGR
AAPTGSEAQGPSAFVRMEKGIPASPRCGSPTAMEIDKRGSPTPGTRSCLAPSLGLFGASL
TMATEVAARVTSTGPHRPQDLALTEPSGRARELEDLQPPEALVERQGQFLGSETSPAPER
GGPRDGEPPGKMGKGYLPCGMPGSGEPEVGKRPEETTVSVQSAESSDSLSWSRLPRALAS
VGPEEARSGAPVGGGRWQLSDRVEGGSPTLGLLGGSPSAQPGTGNVEAGIPSGRMLEPLP
CWDAAKDLKEPQCPPGDRVGVQPGNSRVWQGTMEKAGLAWTRGTGVQSEGTWESQRQDSD
ALPSPELLPQDPDKPFLRKACSPSNIPAVIITDMGTQEDGALEETQGSPRGNLPLRKLSS
SSASSTGFSSSYEDSEEDISSDPERTLDPNSAFLHTLDQQKPRVSKSWRKIKNMVHWSPF
VMSFKKKYPWIQLAGHAGSFKAAANGRILKKHCESEQRCLDRLMVDVLRPFVPAYHGDVV
KDGERYNQMDDLLADFDSPCVMDCKMGIRTYLEEELTKARKKPSLRKDMYQKMIEVDPEA
PTEEEKAQRAVTKPRYMQWRETISSTATLGFRIEGIKKEDGTVNRDFKKTKTREQVTEAF
REFTKGNHNILIAYRDRLKAIRTTLEVSPFFKCHEVIGSSLLFIHDKKEQAKVWMIDFGK
TTPLPEGQTLQHDVPWQEGNREDGYLSGLNNLVDILTEMSQDAPLA
|
| Enzyme 78 Number of Residues |
946 |
| Enzyme 78 Molecular Weight |
102375.3 |
| Enzyme 78 Theoretical pI |
8.56 |
| Enzyme 78 GO Classification |
| Function |
- catalytic activity
- inositol or phosphatidylinositol kinase activity
- inositol trisphosphate 3-kinase activity
- inositol trisphosphate kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 78 General Function |
Involved in inositol trisphosphate 3-kinase activity |
| Enzyme 78 Specific Function |
ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate |
| Enzyme 78 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 78 Reactions |
- ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate [RN:R03433]
|
| Enzyme 78 Pfam Domain Function |
|
| Enzyme 78 Signals |
|
| Enzyme 78 Transmembrane Regions |
|
| Enzyme 78 Essentiality |
Not Available |
| Enzyme 78 GenBank ID Protein |
14329672 |
| Enzyme 78 UniProtKB/Swiss-Prot ID |
P27987 |
| Enzyme 78 UniProtKB/Swiss-Prot Entry Name |
IP3KB_HUMAN |
| Enzyme 78 PDB ID |
Not Available |
| Enzyme 78 Cellular Location |
Not Available |
| Enzyme 78 Gene Sequence |
>2841 bp
ATGGCTGTGTACTGCTATGCGCTCAATAGCCTGGTGATCATGAATAGCGCCAACGAGATG
AAGAGCGGCGGCGGCCCGGGGCCCAGTGGCAGCGAGACGCCCCCGCCCCCGAGGAGGGCA
GTGCTGAGCCCCGGCAGCGTTTTCAGCCCCGGGAGAGGCGCCTCTTTCCTCTTCCCCCCA
GCCGAGTCGCTGTCCCCCGAGGAGCCCCGGAGCCCCGGGGGCTGGCGGAGCGGCCGGCGC
AGGCTGAATAGTAGCAGCGGCAGTGGCAGCGGCAGCAGCGGCAGTAGCGTGAGCAGCCCA
AGTTGGGCTGGTCGCCTGCGAGGGGACCGGCAGCAGGTGGTGGCAGCCGGTACCCTCTCC
CCGCCAGGGCCGGAGGAGGCCAAGAGGAAGCTGCGGATCTTGCAGCGCGAGTTGCAGAAC
GTGCAGGTGAACCAGAAAGTGGGCATGTTTGAGGCGCACATCCAGGCACAGAGCTCCGCC
ATTCAAGCGCCCCGCAGCCCGCGTTTGGGCAGGGCTCACTCGCCCTCCCCGTGCCCCTTC
CGCAGCAGCAGTCAGCCCCCTGGAAGGGTCCTGGTTCAGGGCGCCCGGAGCGAGGAACGG
AGGACAAAGTCCTGGGGGGAGCAATGTTCAGAGACTTCAGGAACCGACTCCGGGAGGAAA
GGAGGGCCCAGCCTATGCTCCTCGCAGGTGAAGAAAGGAATGCCACCTCTTCCCGGCCGG
GCTGCCCCTACAGGATCAGAGGCTCAGGGTCCATCCGCTTTTGTAAGGATGGAGAAGGGT
ATCCCTGCCAGTCCCCGCTGTGGCTCACCCACAGCTATGGAAATTGACAAAAGGGGCTCT
CCTACCCCGGGAACTCGGAGCTGCCTAGCTCCCTCATTGGGGCTGTTCGCCCCTAGCTTC
CCGATGGCCACGGAAGTGGCAGCGAGAGTTACATCCACTGGGCCACACCGTCCACAGGAT
CTTGCCCTCACTGAGCCGTCTGGGAGAGCCCGTGAGCTTGAGGACCTGCAGCCCCCAGAG
GCCCTGGTGGAGAGGCAGGGGCAGTTTCTGGGCAGTGAGACAAGCCCAGCCCCAGAAAGG
GGCGGGCCCCGCGATGGAGAACCCCCTGGGAAGATGGGGAAAGGATATCTGCCCTGTGGC
ATGCCGGGCTCTGGGGAGCCTGAAGTGGGCAAAAGGCCAGAGGAGACGACTGTGAGCGTG
CAAAGCGCAGAGTCCTCTGATTCCCTGAGCTGGTCCAGGCTGCCCAGGGCCCTGGCCTCC
GTAGGCCCTGAGGAGGCCCGAAGTGGGGCCCCCGTGGGCGGGGGGCGTTGGCAGCTCTCC
GACAGAGTGGAGGGAGGGTCCCCAACGCTGGGCTTGCTTGGGGGCAGCCCCTCAGCACAG
CCGGGGACCGGGAATGTGGAGGCGGGAATTCCTTCTGGCAGAATGCTGGAGCCTTTGCCC
TGTTGGGACGCTGCGAAAGATCTGAAAGAACCTCAGTGCCCTCCTGGGGACAGGGTGGGT
GTGCAGCCTGGGAACTCCAGGGTTTGGCAGGGCACCATGGAGAAAGCCGGTTTGGCTTGG
ACGCGTGGCACAGGGGTGCAATCAGAGGGGACTTGGGAAAGCCAGCGGCAGGACAGTGAT
GCCCTCCCAAGTCCGGAGCTGCTACCCCAAGATCAGGACAAGCCTTTCCTGAGGAAGGCC
TGCAGCCCCAGCAACATACCTGCTGTCATCATTACAGACATGGGCACCCAGGAGGATGGG
GCCTTGGAGGAGACGCAGGGAAGCCCTCGGGGCAACCTGCCCCTGAGGAAACTGTCCTCT
TCCTCGGCCTCCTCCACGGGCTTCTCCTCATCCTACGAAGACTCAGAGGAGGACATCTCC
AGTGACCCTGAGCGCACCCTGGACCCCAACTCAGCTTTCCTGCATACCCTGGACCAGCAG
AAACCTAGAGTGAGCAAATCATGGAGGAAGATAAAAAACATGGTGCACTGGTCTCCCTTC
GTCATGTCCTTCAAGAAGAAGTACCCCTGGATCCAGCTGGCAGGACACGCAGGGAGTTTC
AAGGCAGCTGCCAATGGCAGGATCCTGAAGAAGCACTGTGAGTCAGAGCAGCGCTGCCTG
GACCGGCTGATGGTGGATGTGCTGAGGCCCTTCGTACCTGCCTACCATGGGGATGTGGTG
AAGGACGGGGAGCGCTACAACCAGATGGACGACCTGCTGGCCGACTTCGACTCGCCCTGT
GTGATGGACTGCAAGATGGGAATCAGGACCTACCTGGAGGAGGAGCTCACGAAGGCCCGG
AAGAAGCCCAGCCTGCGGAAGGACATGTACCAGAAGATGATCGAGGTGGACCCCGAGGCC
CCCACCGAGGAGGAAAAAGCACAGCGGGCTGTGACCAAGCCACGGTACATGCAGTGGCGG
GAGACCATCAGCTCCACGGCCACCCTGGGGTTCAGGATCGAGGGAATCAAGAAAGAAGAC
GGCACCGTGAACCGGGACTTCAAGAAGACCAAAACGAGGGAGCAGGTCACCGAGGCCTTC
AGAGAGTTCACTAAAGGAAACCATAACATCCTGATCGCCTATCGGGACCGGCTGAAGGCC
ATTCGAACCACTCTAGAAGTTTCTCCCTTCTTCAAGTGCCACGAGGTCATTGGCAGCTCC
CTCCTCTTCATCCACGACAAGAAGGAACAGGCCAAAGTGTGGATGATCGACTTTGGGAAA
ACCACGCCCCTGCCTGAGGGCCAGACCCTGCAGCATGACGTCCCCTGGCAGGAGGGGAAC
CGGGAGGATGGCTACCTCTCGGGGCTCAATAACCTCGTCGACATCCTGACCGAGATGTCC
CAGGATGCCCCACTCGCCTGA
|
| Enzyme 78 GenBank Gene ID |
AJ242780 |
| Enzyme 78 GeneCard ID |
ITPKB |
| Enzyme 78 GenAtlas ID |
ITPKB |
| Enzyme 78 HGNC ID |
HGNC:6179 |
| Enzyme 78 Chromosome Location |
1 |
| Enzyme 78 Locus |
1q42.13 |
| Enzyme 78 SNPs |
SNPJam Report |
| Enzyme 78 General References |
- Dewaste V, Roymans D, Moreau C, Erneux C: Cloning and expression of a full-length cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase B. Biochem Biophys Res Commun. 2002 Feb 22;291(2):400-5. [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 ]
- Takazawa K, Perret J, Dumont JE, Erneux C: Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme. Biochem J. 1991 Sep 15;278 ( Pt 3):883-6. [PubMed ]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
|
| Enzyme 78 Metabolite References |
Not Available |
|
Enzyme 79
[top]
|
| Enzyme 79 ID |
6272 |
| Enzyme 79 Name |
Inositol-trisphosphate 3-kinase A |
| Enzyme 79 Synonyms |
- Inositol 1,4,5-trisphosphate 3-kinase A
- IP3 3-kinase A
- IP3K A
- InsP 3-kinase A
|
| Enzyme 79 Gene Name |
ITPKA |
| Enzyme 79 Protein Sequence |
>Inositol-trisphosphate 3-kinase A
MTLPGGPTGMARPGGARPCSPGLERAPRRSVGELRLLFEARCAAVAAAAAAGEPRARGAK
RRGGQVPNGLPRAPPAPVIPQLTVTAEEPDVPPTSPGPPERERDCLPAAGSSHLQQPRRL
STSSVSSTGSSSLLEDSEDDLLSDSESRSRGNVQLEAGEDVGQKNHWQKIRTMVNLPVIS
PFKKRYAWVQLAGHTGSFKAAGTSGLILKRCSEPERYCLARLMADALRGCVPAFHGVVER
DGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAP
TEEEHAQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVLRVFE
EFVQGDEEVLRRYLNRLQQIRDTLEVSEFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKT
TPLPDGQILDHRRPWEEGNREDGYLLGLDNLIGILASLAER
|
| Enzyme 79 Number of Residues |
461 |
| Enzyme 79 Molecular Weight |
51008.3 |
| Enzyme 79 Theoretical pI |
7.72 |
| Enzyme 79 GO Classification |
| Function |
- catalytic activity
- inositol or phosphatidylinositol kinase activity
- inositol trisphosphate 3-kinase activity
- inositol trisphosphate kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 79 General Function |
Involved in inositol trisphosphate 3-kinase activity |
| Enzyme 79 Specific Function |
ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate |
| Enzyme 79 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 79 Reactions |
- ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate [RN:R03433]
|
| Enzyme 79 Pfam Domain Function |
|
| Enzyme 79 Signals |
|
| Enzyme 79 Transmembrane Regions |
|
| Enzyme 79 Essentiality |
Not Available |
| Enzyme 79 GenBank ID Protein |
32105 |
| Enzyme 79 UniProtKB/Swiss-Prot ID |
P23677 |
| Enzyme 79 UniProtKB/Swiss-Prot Entry Name |
IP3KA_HUMAN |
| Enzyme 79 PDB ID |
1W2F |
| Enzyme 79 PDB File |
Show |
| Enzyme 79 3D Structure |
|
| Enzyme 79 Cellular Location |
Not Available |
| Enzyme 79 Gene Sequence |
>1386 bp
ATGACCCTGCCCGGGGGCCCAACGGGCATGGCGCGGCCGGGGGGCGCGAGGCCCTGCAGC
CCGGGGCTGGAGCGGGCCCCGCGCCGGAGTGTCGGGGAGCTGCGCCTGCTCTTCGAGGCG
CGCTGTGCGGCGGTCGCTGCGGCCGCCGCCGCGGGGGAGCCCCGGGCCCGCGGGGCCAAG
CGGCGTGGGGGACAGGTCCCCAACGGGCTTCCGCGGGCTCCCCCGGCCCCGGTGATCCCT
CAGCTGACCGTGACAGCCGAGGAGCCCGACGTGCCCCCGACCAGCCCTGGGCCGCCGGAG
CGGGAGAGGGACTGCCTCCCGGCAGCGGGCTCTTCGCACCTGCAGCAGCCGCGCCGCCTT
TCCACCTCGTCGGTCTCCTCCACTGGCTCCTCGTCGCTGCTCGAGGACTCGGAGGACGAC
CTGCTGAGCGACAGTGAGAGCCGGAGCCGCGGCAACGTGCAGCTGGAAGCGGGCGAGGAC
GTGGGTCAGAAAAACCACTGGCAGAAGATCCGGACCATGGTCAATCTGCCGGTCATAAGC
CCTTTCAAGAAGCGCTACGCCTGGGTGCAGCTGGCAGGGCACACTGGGAGTTTTAAGGCG
GCGGGCACCAGCGGGCTGATCCTGAAGCGCTGCTCGGAGCCGGAGCGCTACTGCCTGGCG
CGGCTGATGGCTGACGCGCTGCGCGGCTGCGTGCCTGCCTTCCACGGCGTGGTGGAGCGC
GACGGCGAAAGCTACCTGCAGCTGCAGGACCTGCTCGATGGCTTCGACGGACCTTGTGTG
CTCGACTGCAAAATGGGCGTCAGGACTTACCTAGAGGAGGAGCTGACCAAGGCCCGTGAG
CGGCCCAAGCTGCGGAAGGACATGTACAAGAAAATGCTGGCGGTGGATCCTGAAGCTCCC
ACGGAGGAGGAGCACGCGCAGCGCGCCGTCACCAAGCCGCGCTACATGCAGTGGCGGGAA
GGCATCAGCTCCAGCACCACCCTCGGCTTCCGCATCGAGGGCATCAAGAAAGCGGACGGC
TCCTGCAGCACCGACTTCAAGACTACGCGAAGCCGAGAGCAGGTGCTTCGCGTCTTTGAA
GAGTTTGTGCAAGGAGATGAGGAAGTGCTGAGGCGGTATCTGAACCGCCTGCAGCAGATC
CGGGACACCCTGGAGGTATCCGAGTTCTTCAGGAGGCACGAGGTGATCGGCAGCTCGCTC
CTCTTTGTGCACGATCACTGCCATCGCGCCGGCGTGTGGCTCATCGACTTCGGCAAGACC
ACGCCCCTCCCCGATGGCCAGATCCTGGACCACCGGCGGCCCTGGGAGGAGGGCAACCGC
GAGGACGGCTATTTGCTGGGGCTGGACAATCTCATTGGCATCCTGGCCAGCCTGGCTGAG
AGATGA
|
| Enzyme 79 GenBank Gene ID |
X54938 |
| Enzyme 79 GeneCard ID |
ITPKA |
| Enzyme 79 GenAtlas ID |
ITPKA |
| Enzyme 79 HGNC ID |
HGNC:6178 |
| Enzyme 79 Chromosome Location |
1 |
| Enzyme 79 Locus |
15q15.1 |
| Enzyme 79 SNPs |
SNPJam Report |
| Enzyme 79 General References |
- Takazawa K, Perret J, Dumont JE, Erneux C: Molecular cloning and expression of a human brain inositol 1,4,5-trisphosphate 3-kinase. Biochem Biophys Res Commun. 1991 Jan 31;174(2):529-35. [PubMed ]
- Takazawa K, Perret J, Dumont JE, Erneux C: Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence. Nucleic Acids Res. 1990 Dec 11;18(23):7141. [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 ]
- Gonzalez B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL: Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase. Mol Cell. 2004 Sep 10;15(5):689-701. [PubMed ]
|
| Enzyme 79 Metabolite References |
Not Available |
|
Enzyme 80
[top]
|
| Enzyme 80 ID |
6304 |
| Enzyme 80 Name |
Diphosphomevalonate decarboxylase |
| Enzyme 80 Synonyms |
- Mevalonate (diphospho)decarboxylase
- MDDase
- Mevalonate pyrophosphate decarboxylase
|
| Enzyme 80 Gene Name |
MVD |
| Enzyme 80 Protein Sequence |
>Diphosphomevalonate decarboxylase
MASEKPLAAVTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLHQDQLKTTTTAVISKDF
TEDRIWLNGREEDVGQPRLQACLREIRCLARKRRNSRDGDPLPSSLSCKVHVASVNNFPT
AAGLASSAAGYACLAYTLARVYGVESDLSEVARRGSGSACRSLYGGFVEWQMGEQADGKD
SIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEM
ARCIRERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAHHGDTKV
AYTFDAGPNAVIFTLDDTVAEFVAAVWHGFPPGSNGDTFLKGLQVRPAPLSAELQAALAM
EPTPGGVKYIIVTQVGPGPQILDDPCAHLLGPDGLPKPAA
|
| Enzyme 80 Number of Residues |
400 |
| Enzyme 80 Molecular Weight |
43404.1 |
| Enzyme 80 Theoretical pI |
7.25 |
| Enzyme 80 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- diphosphomevalonate decarboxylase activity
- kinase activity
- lyase activity
- nucleoside binding
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular lipid metabolic process
- cellular metabolic process
- isoprenoid biosynthetic process
- isoprenoid metabolic process
- lipid metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 80 General Function |
Involved in ATP binding |
| Enzyme 80 Specific Function |
Performs the first committed step in the biosynthesis of isoprenes |
| Enzyme 80 Pathways |
|
| Enzyme 80 Reactions |
- ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2 [RN:R01121]
|
| Enzyme 80 Pfam Domain Function |
|
| Enzyme 80 Signals |
|
| Enzyme 80 Transmembrane Regions |
|
| Enzyme 80 Essentiality |
Not Available |
| Enzyme 80 GenBank ID Protein |
12652543 |
| Enzyme 80 UniProtKB/Swiss-Prot ID |
P53602 |
| Enzyme 80 UniProtKB/Swiss-Prot Entry Name |
MVD1_HUMAN |
| Enzyme 80 PDB ID |
Not Available |
| Enzyme 80 Cellular Location |
Not Available |
| Enzyme 80 Gene Sequence |
>1203 bp
ATGGCCTCGGAGAAGCCGCTGGCGGCAGTCACTTGTACAGCGCCGGTCAACATCGCGGTC
ATCAAGTACTGGGGCAAGCGCGATGAAGAGCTGGTTCTGCCCATCAACTCCTCCCTGAGC
GTCACTCTGCACCAGGACCAGTTAAAAACCACCACAACAGCCGTCATCAGCAAGGACTTC
ACCGAGGACCGGATTTGGCTGAATGGCCGGGAGGAGGATGTGGGGCAGCCGAGGCTGCAG
GCCTGCCTGCGGGAGATCCGCTGCCTGGCCCGGAAGCGGAGGAACTCACGGGATGGGGAC
CCGCTGCCCTCCAGCCTCAGCTGCAAGGTGCACGTGGCATCGGTGAACAACTTCCCCACG
GCTGCGGGCCTGGCCTCCTCAGCGGCGGGCTATGCCTGCCTAGCCTACACCCTGGCCCGT
GTCTACGGCGTGGAGAGTGACCTCTCAGAAGTGGCTCGCCGGGGCTCAGGCAGCGCCTGC
CGGAGCCTGTATGGGGGCTTTGTGGAGTGGCAGATGGGAGAGCAGGCCGACGGGAAGGAC
AGCATCGCTCGGCAAGTGGCCCCCGAGTCACACTGGCCTGAACTCCGCGTGCTCATCCTT
GTGGTGAGCGCTGAGAAGAAGCTGACAGGCAGTACCGTGGGCATGCGGGCCAGTGTGGAG
ACCAGCCCCCTGCTTCGGTTCCGGGCCGAGTCCGTGGTGCCCGCGCGCATGGCGGAGATG
GCCCGCTGCATCCGGGAGCGAGACTTCCCCAGCTTCGCCCAGCTGACCATGAAGGACAGC
AACCAGTTCCACGCCACCTGCCTCGACACCTTCCCGCCCATCTCTTACCTCAATGCCATC
TCCTGGCGCATCATCCACCTGGTGCACCGCTTCAACGCCCACCACGGGGACACCAAGGTG
GCGTACACCTTTGACGCGGGCCCCAATGCCGTGATCTTCACCCTGGACGACACTGTGGCT
GAGTTTGTGGCTGCTGTGTGGCACGGCTTTCCCCCAGGCTCGAATGGAGACACGTTTCTG
AAGGGGCTGCAGGTGAGGCCGGCCCCTCTCTCAGCTGAGCTTCAGGCTGCGCTGGCCATG
GAGCCGACCCCCGGTGGGGTCAAATACATCATTGTCACTCAGGTGGGGCCAGGGCCTCAA
ATCCTGGATGACCCCTGCGCCCACCTCCTGGGTCCTGACGGCCTGCCGAAGCCAGCTGCC
TGA
|
| Enzyme 80 GenBank Gene ID |
BC000011 |
| Enzyme 80 GeneCard ID |
MVD |
| Enzyme 80 GenAtlas ID |
MVD |
| Enzyme 80 HGNC ID |
HGNC:7529 |
| Enzyme 80 Chromosome Location |
1 |
| Enzyme 80 Locus |
16q24.3 |
| Enzyme 80 SNPs |
SNPJam Report |
| Enzyme 80 General References |
- Toth MJ, Huwyler L: Molecular cloning and expression of the cDNAs encoding human and yeast mevalonate pyrophosphate decarboxylase. J Biol Chem. 1996 Apr 5;271(14):7895-8. [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 ]
- Hinson DD, Chambliss KL, Toth MJ, Tanaka RD, Gibson KM: Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and nonsterol isoprene biosynthetic pathways. J Lipid Res. 1997 Nov;38(11):2216-23. [PubMed ]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
|
| Enzyme 80 Metabolite References |
Not Available |
|
Enzyme 81
[top]
|
| Enzyme 81 ID |
6305 |
| Enzyme 81 Name |
Phosphomevalonate kinase |
| Enzyme 81 Synonyms |
- PMKase
- hPMK
|
| Enzyme 81 Gene Name |
PMVK |
| Enzyme 81 Protein Sequence |
>Phosphomevalonate kinase
MAPLGGAPRLVLLFSGKRKSGKDFVTEALQSRLGADVCAVLRLSGPLKEQYAQEHGLNFQ
RLLDTSTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGISQPIWLVSDTRRVSDIQWFRE
AYGAVTQTVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDWVIENHGVEQRLEEQ
LENLIEFIRSRL
|
| Enzyme 81 Number of Residues |
192 |
| Enzyme 81 Molecular Weight |
21994.7 |
| Enzyme 81 Theoretical pI |
5.41 |
| Enzyme 81 GO Classification |
| Function |
- catalytic activity
- kinase activity
- phosphomevalonate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- cholesterol biosynthetic process
- cholesterol metabolic process
- metabolic process
- small molecule metabolic process
- sterol metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 81 General Function |
Involved in phosphomevalonate kinase activity |
| Enzyme 81 Specific Function |
ATP + (R)-5-phosphomevalonate = ADP + (R)-5- diphosphomevalonate |
| Enzyme 81 Pathways |
|
| Enzyme 81 Reactions |
- ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate [RN:R03245]
|
| Enzyme 81 Pfam Domain Function |
|
| Enzyme 81 Signals |
|
| Enzyme 81 Transmembrane Regions |
|
| Enzyme 81 Essentiality |
Not Available |
| Enzyme 81 GenBank ID Protein |
Not Available |
| Enzyme 81 UniProtKB/Swiss-Prot ID |
Q15126 |
| Enzyme 81 UniProtKB/Swiss-Prot Entry Name |
PMVK_HUMAN |
| Enzyme 81 PDB ID |
Not Available |
| Enzyme 81 Cellular Location |
Not Available |
| Enzyme 81 Gene Sequence |
>579 bp
ATGGCCCCGCTGGGAGGCGCCCCGCGGCTGGTACTGCTGTTCAGCGGCAAGAGGAAATCC
GGGAAGGACTTCGTGACCGAGGCGCTGCAGAGCAGACTTGGAGCTGATGTCTGTGCTGTC
CTCCGGCTCTCTGGTCCACTCAAGGAACAGTATGCTCAGGAGCATGGCTTGAACTTCCAG
AGACTCCTGGACACCAGCACCTACAAGGAGGCCTTTCGGAAGGACATGATCCGCTGGGGA
GAGGAGAAACGCCAGGCTGACCCAGGCTTCTTTTGCAGGAAGATTGTGGAGGGCATCTCC
CAGCCCATCTGGCTGGTGAGTGACACACGGAGAGTGTCTGACATCCAGTGGTTTCGGGAG
GCCTATGGGGCCGTGACGCAGACGGTCCGCGTTGTAGCGTTGGAGCAGAGCCGACAGCAG
CGGGGCTGGGTGTTCACGCCAGGGGTGGACGATGCTGAGTCAGAATGTGGCCTGGACAAC
TTCGGGGACTTTGACTGGGTCATCGAGAACCATGGAGTTGAACAGCGCCTGGAGGAGCAG
TTGGAGAACCTGATAGAATTTATCCGCTCCAGACTTTAG
|
| Enzyme 81 GenBank Gene ID |
L77213 |
| Enzyme 81 GeneCard ID |
PMVK |
| Enzyme 81 GenAtlas ID |
PMVK |
| Enzyme 81 HGNC ID |
HGNC:9141 |
| Enzyme 81 Chromosome Location |
1 |
| Enzyme 81 Locus |
1q22 |
| Enzyme 81 SNPs |
SNPJam Report |
| Enzyme 81 General References |
- Chambliss KL, Slaughter CA, Schreiner R, Hoffmann GF, Gibson KM: Molecular cloning of human phosphomevalonate kinase and identification of a consensus peroxisomal targeting sequence. J Biol Chem. 1996 Jul 19;271(29):17330-4. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Olivier LM, Chambliss KL, Gibson KM, Krisans SK: Characterization of phosphomevalonate kinase: chromosomal localization, regulation, and subcellular targeting. J Lipid Res. 1999 Apr;40(4):672-9. [PubMed ]
- Hinson DD, Chambliss KL, Toth MJ, Tanaka RD, Gibson KM: Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and nonsterol isoprene biosynthetic pathways. J Lipid Res. 1997 Nov;38(11):2216-23. [PubMed ]
- Herdendorf TJ, Miziorko HM: Phosphomevalonate kinase: functional investigation of the recombinant human enzyme. Biochemistry. 2006 Mar 14;45(10):3235-42. [PubMed ]
- Herdendorf TJ, Miziorko HM: Functional evaluation of conserved basic residues in human phosphomevalonate kinase. Biochemistry. 2007 Oct 23;46(42):11780-8. Epub 2007 Sep 29. [PubMed ]
- Chang Q, Yan XX, Gu SY, Liu JF, Liang DC: Crystal structure of human phosphomevalonate kinase at 1.8 A resolution. Proteins. 2008 Oct;73(1):254-8. [PubMed ]
|
| Enzyme 81 Metabolite References |
Not Available |
|
Enzyme 82
[top]
|
| Enzyme 82 ID |
6312 |
| Enzyme 82 Name |
Pantothenate kinase 4 |
| Enzyme 82 Synonyms |
- hPanK4
- Pantothenic acid kinase 4
|
| Enzyme 82 Gene Name |
PANK4 |
| Enzyme 82 Protein Sequence |
>Pantothenate kinase 4
MAECGASGSGSSGDSLDKSITLPPDEIFRNLENAKRFAIDIGGSLTKLAYYSTVQHKVAK
VRSFDHSGKDTEREHEPPYEISVQEEITARLHFIKFENTYIEACLDFIKDHLVNTETKVI
QATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYQKDSDPEFRFQ
TNHPHIFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLH
LASRGQHSNVDMLVRDVYGGAHQTLGLSGNLIASSFGKSATADQEFSKEDMAKSLLHMIS
NDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLG
AIGAFLKGAEQDNPNQYSWGENYAGSSGLMSASPELGPAQRARSGTFDLLEMDRLERPLV
DLPLLLDPPSYVPDTVDLTDDALARKYWLTCFEEALDGVVKRAVASQPDSVDAAERAEKF
RQKYWNKLQTLRQQPFAYGTLTVRSLLDTREHCLNEFNFPDPYSKVKQRENGVALRCFPG
VVRSLDALGWEERQLALVKGLLAGNVFDWGAKAVSAVLESDPYFGFEEAKRKLQERPWLV
DSYSEWLQRLKGPPHKCALIFADNSGIDIILGVFPFVRELLLRGTEVILACNSGPALNDV
THSESLIVAERIAGMDPVVHSALQEERLLLVQTGSSSPCLDLSRLDKGLAALVRERGADL
VVIEGMGRAVHTNYHAALRCESLKLAVIKNAWLAERLGGRLFSVIFKYEVPAE
|
| Enzyme 82 Number of Residues |
773 |
| Enzyme 82 Molecular Weight |
85990.1 |
| Enzyme 82 Theoretical pI |
6.22 |
| Enzyme 82 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- pantothenate kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- coenzyme A biosynthetic process
- coenzyme biosynthetic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 82 General Function |
Involved in pantothenate kinase activity |
| Enzyme 82 Specific Function |
Plays a role in the physiological regulation of the intracellular CoA concentration |
| Enzyme 82 Pathways |
- Pantothenate and CoA Biosynthesis (map00770 )
|
| Enzyme 82 Reactions |
- ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate [RN:R03018]
|
| Enzyme 82 Pfam Domain Function |
|
| Enzyme 82 Signals |
|
| Enzyme 82 Transmembrane Regions |
|
| Enzyme 82 Essentiality |
Not Available |
| Enzyme 82 GenBank ID Protein |
7023024 |
| Enzyme 82 UniProtKB/Swiss-Prot ID |
Q9NVE7 |
| Enzyme 82 UniProtKB/Swiss-Prot Entry Name |
PANK4_HUMAN |
| Enzyme 82 PDB ID |
Not Available |
| Enzyme 82 Cellular Location |
Not Available |
| Enzyme 82 Gene Sequence |
>2322 bp
ATGGCGGAGTGTGGAGCGAGCGGCAGCGGGAGCAGCGGGGACAGTCTGGACAAGAGCATC
ACGCTGCCCCCCGACGAGATCTTCCGCAACCTGGAGAACGCCAAGCGCTTCGCCATCGAC
ATAGGCGGGTCGTTAACCAAGCTGGCCTACTATTCAACGGTACAGCACAAAGTCGCCAAG
GTGCGGTCTTTCGACCACTCCGGAAAGGACACAGAACGTGAACATGAGCCGCCCTATGAG
ATTTCAGTTCAAGAAGAGATCACTGCTCGACTGCACTTCATTAAGTTTGAGAATACCTAC
ATCGAAGCCTGCCTGGACTTCATCAAAGACCATCTCGTCAACACAGAGACCAAGGTCATC
CAGGCGACCGGGGGCGGGGCCTACAAGTTCAAGGACCTCATCGAAGAGAAGCTGCGGCTG
AAAGTCGACAAGGAGGACGTGATGACGTGCCTGATTAAGGGGTGCAACTTCGTGCTCAAG
AACATCCCCCATGAGGCCTTCGTGTACCAGAAGGATTCCGACCCTGAGTTCCGGTTCCAG
ACCAACCACCCCCACATTTTCCCCTATCTTCTTGTCAATATCGGCTCTGGAGTCTCCATC
GTGAAGGTGGAGACGGAGGACAGGTTCGAGTGGGTCGGCGGCAGCTCCATTGGAGGCGGC
ACCTTCTGGGGGCTTGGCGCTCTGCTCACCAAAACGAAGAAGTTTGACGAGCTCCTGCAC
CTGGCCTCGAGGGGCCAGCACAGCAATGTGGACATGCTGGTGCGGGACGTCTACGGCGGC
GCCCACCAGACTCTCGGGCTGAGCGGGAACCTCATCGCCAGCAGCTTCGGGAAGTCGGCC
ACCGCCGACCAAGAGTTCTCCAAAGAAGACATGGCGAAGAGCCTGCTGCACATGATCAGC
AACGACATTGGGCAGCTGGCCTGCCTCCACGCACGGCTGCACAGCCTGGACCGCGTGTAC
TTTGGAGGCTTCTTTATCCGGGGCCACCCCGTGACCATGCGCACCATCACCTATAGCATC
AACTTCTTCTCCAAGGGGGAAGTGCAGGCGCTGTTTCTGAGGCACGAAGGCTACCTGGGA
GCCATCGGAGCGTTCCTGAAAGGAGCTGAGCAGGACAATCCTAACCAGTACAGCTGGGGA
GAGAACTATGCAGGCAGCTCCGGGCTGATGAGTGCATCACCCGAGCTCGGCCCGGCGCAG
CGGGCGCGGAGTGGCACTTTTGACTTGCTGGAAATGGACCGGCTGGAGAGGCCACTGGTT
GACCTGCCGCTCCTCCTGGACCCGCCCTCCTACGTGCCCGACACGGTGGACCTCACCGAT
GACGCTCTGGCCCGAAAATACTGGCTCACCTGCTTTGAGGAGGCCCTGGACGGGGTAGTG
AAGCGCGCAGTGGCGAGCCAGCCAGACTCTGTGGATGCAGCCGAGAGGGCGGAGAAGTTC
CGGCAGAAGTACTGGAACAAGCTTCAGACCCTGAGGCAGCAGCCCTTCGCCTATGGGACC
CTGACCGTGCGCAGCCTGCTGGACACCAGGGAGCACTGTCTGAACGAGTTCAACTTCCCG
GATCCCTACTCCAAAGTGAAGCAGCGGGAGAATGGCGTGGCGCTGAGGTGCTTCCCCGGG
GTCGTGCGCTCCCTGGACGCGCTGGGCTGGGAGGAACGGCAGCTGGCGCTGGTGAAAGGC
CTCCTGGCGGGGAATGTCTTCGACTGGGGGGCCAAAGCCGTGTCTGCTGTCCTTGAATCC
GACCCCTACTTTGGGTTTGAAGAAGCAAAGAGGAAGTTACAAGAAAGACCCTGGCTCGTG
GATTCCTACAGCGAGTGGCTTCAGAGATTAAAGGGGCCCCCTCATAAATGTGCCTTAATT
TTCGCAGATAACAGTGGAATAGACATCATTTTGGGAGTCTTCCCCTTTGTCAGGGAGCTA
CTCCTTAGAGGGACAGAGGTCATCCTGGCGTGCAACTCAGGCCCCGCCCTGAACGACGTG
ACCCACAGCGAGTCCCTCATCGTGGCAGAGCGTATTGCGGGCATGGACCCTGTCGTGCAC
TCTGCGCTCCAGGAAGAGAGGCTGCTGCTGGTGCAGACGGGCTCCAGCTCCCCGTGCCTC
GACCTCAGCCGCCTGGATAAGGGGCTGGCCGCACTGGTGCGGGAGCGTGGCGCGGATCTG
GTGGTCATCGAGGGCATGGGCCGTGCTGTCCACACAAACTACCACGCAGCCCTGCGCTGC
GAGAGCCTCAAGCTGGCCGTCATCAAGAACGCGTGGCTGGCCGAGCGGCTGGGCGGCCGG
CTCTTCAGCGTCATCTTCAAGTACGAGGTCCCAGCCGAGTGA
|
| Enzyme 82 GenBank Gene ID |
AK001644 |
| Enzyme 82 GeneCard ID |
PANK4 |
| Enzyme 82 GenAtlas ID |
PANK4 |
| Enzyme 82 HGNC ID |
HGNC:19366 |
| Enzyme 82 Chromosome Location |
1 |
| Enzyme 82 Locus |
1p36.32 |
| Enzyme 82 SNPs |
SNPJam Report |
| Enzyme 82 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 ]
- 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 ]
- 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 ]
- Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, Hayflick SJ: A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet. 2001 Aug;28(4):345-9. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 82 Metabolite References |
Not Available |
|
Enzyme 83
[top]
|
| Enzyme 83 ID |
6313 |
| Enzyme 83 Name |
Pantothenate kinase 2, mitochondrial |
| Enzyme 83 Synonyms |
- hPanK2
- Pantothenic acid kinase 2
|
| Enzyme 83 Gene Name |
PANK2 |
| Enzyme 83 Protein Sequence |
>Pantothenate kinase 2, mitochondrial
MRRLGPFHPRVHWAAPPSLSSGLHRLLFLRGTRIPSSTTLSPPRHDSLSLDGGTVNPPRV
REPTGREAFGPSPASSDWLPARWRNGRGGRPRARLCSGWTAAEEARRNPTLGGLLGRQRL
LLRMGGGRLGAPMERHGRASATSVSSAGEQAAGDPEGRRQEPLRRRASSASVPAVGASAE
GTRRDRLGSYSGPTSVSRQRVESLRKKRPLFPWFGLDIGGTLVKLVYFEPKDITAEEEEE
EVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDMPAFIQMGR
DKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQC
YYFENPADSEKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFG
LCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEK
REAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDY
WSKGQLKALFSEHEGYFGAVGALLELLKIP
|
| Enzyme 83 Number of Residues |
570 |
| Enzyme 83 Molecular Weight |
62679.9 |
| Enzyme 83 Theoretical pI |
9.64 |
| Enzyme 83 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- pantothenate kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- coenzyme A biosynthetic process
- coenzyme biosynthetic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 83 General Function |
Involved in pantothenate kinase activity |
| Enzyme 83 Specific Function |
May be the master regulator of the CoA biosynthesis |
| Enzyme 83 Pathways |
- Pantothenate and CoA Biosynthesis (map00770 )
|
| Enzyme 83 Reactions |
- ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate [RN:R03018]
|
| Enzyme 83 Pfam Domain Function |
|
| Enzyme 83 Signals |
|
| Enzyme 83 Transmembrane Regions |
|
| Enzyme 83 Essentiality |
Not Available |
| Enzyme 83 GenBank ID Protein |
23452046 |
| Enzyme 83 UniProtKB/Swiss-Prot ID |
Q9BZ23 |
| Enzyme 83 UniProtKB/Swiss-Prot Entry Name |
PANK2_HUMAN |
| Enzyme 83 PDB ID |
Not Available |
| Enzyme 83 Cellular Location |
Not Available |
| Enzyme 83 Gene Sequence |
>1713 bp
ATGAGGAGGCTCGGGCCCTTCCACCCACGCGTCCATTGGGCGGCGCCGCCATCACTCTCT
TCTGGGCTACACCGCCTTCTCTTCCTCCGCGGAACCCGGATCCCCTCCTCCACCACCCTC
TCCCCGCCCCGTCACGATAGCCTCTCATTGGACGGAGGCACGGTCAATCCTCCTCGAGTT
AGGGAGCCGACTGGACGCGAGGCCTTTGGGCCGTCCCCAGCCTCGTCGGATTGGCTTCCT
GCGCGTTGGCGCAACGGAAGAGGCGGCCGGCCGAGGGCGCGCCTCTGCTCTGGCTGGACC
GCCGCGGAGGAGGCGAGAAGGAATCCGACGCTGGGGGGCTTGCTCGGGCGGCAGCGACTG
CTGCTGCGGATGGGAGCGGGCCGGCTCGGCGCGCCCATGGAGCGCCACGGCAGGGCTTCC
GCCACCTCCGTCTCGTCGGCTGGGGAGCAGGCGGCCGGGGACCCCGAAGGGCGGCGGCAG
GAGCCACTGCGGCGCCGGGCGAGCAGCGCGTCGGTGCCCGCGGTCGGGGCCTCGGCTGAG
GGCACGAGGCGGGATCGACTGGGCTCTTACAGCGGCCCCACCTCGGTCTCCCGCCAGCGC
GTCGAAAGCCTGAGGAAAAAGCGGCCGCTTTTTCCATGGTTTGGACTGGATATCGGTGGA
ACTCTGGTCAAGCTGGTATATTTTGAACCCAAAGACATCACTGCTGAAGAAGAAGAGGAA
GAGGTGGAAAGTCTTAAAAGTATTCGGAAGTACCTGACCTCCAATGTGGCTTATGGGTCT
ACAGGCATTCGGGACGTGCACCTCGAGCTGAAGGACCTGACTCTGTGTGGACGCAAAGGC
AATCTGCACTTTATACGCTTTCCCACTCATGACATGCCTGCTTTTATTCAAATGGGCAGA
GATAAAAACTTCTCGAGTCTCCACACTGTCTTTTGTGCCACTGGAGGTGGAGCGTACAAA
TTTGAGCAGGATTTTCTCACAATAGGTGATCTTCAGCTTTGCAAACTGGATGAACTAGAT
TGCTTGATCAAAGGAATTTTATACATTGACTCAGTCGGATTCAATGGACGGTCACAGTGC
TATTACTTTGAAAACCCTGCTGATTCTGAAAAGTGTCAGAAGTTACCATTTGATTTGAAA
AATCCGTATCCTCTGCTTCTGGTGAACATTGGCTCAGGGGTTAGCATCTTAGCAGTATAT
TCCAAAGATAATTACAAACGGGTCACAGGTACTAGTCTTGGAGGAGGAACTTTTTTTGGT
CTCTGCTGTCTTCTTACTGGCTGTACCACTTTTGAAGAAGCTCTTGAAATGGCATCTCGT
GGAGATAGCACCAAAGTGGATAAACTAGTACGAGATATTTATGGAGGGGACTATGAGAGG
TTTGGACTGCCAGGCTGGGCTGTGGCTTCAAGCTTTGGAAACATGATGAGCAAGGAGAAG
CGAGAGGCTGTCAGTAAAGAGGACCTGGCCAGAGCGACTTTGATCACCATCACCAACAAC
ATTGGCTCAATAGCAAGAATGTGTGCCCTTAATGAAAACATTAACCAGGTGGTATTTGTT
GGAAATTTCTTGAGAATTAATACGATCGCCATGCGGCTTTTGGCATATGCTTTGGATTAT
TGGTCCAAGGGGCAGTTGAAAGCACTTTTTTCGGAACACGAGGGTTATTTTGGAGCTGTT
GGAGCACTCCTTGAGCTGTTGAAGATCCCGTGA
|
| Enzyme 83 GenBank Gene ID |
AF494409 |
| Enzyme 83 GeneCard ID |
PANK2 |
| Enzyme 83 GenAtlas ID |
PANK2 |
| Enzyme 83 HGNC ID |
HGNC:15894 |
| Enzyme 83 Chromosome Location |
2 |
| Enzyme 83 Locus |
20p13 |
| Enzyme 83 SNPs |
SNPJam Report |
| Enzyme 83 General References |
- Hortnagel K, Prokisch H, Meitinger T: An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria. Hum Mol Genet. 2003 Feb 1;12(3):321-7. [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 ]
- 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 ]
- 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 ]
- Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, Hayflick SJ: A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet. 2001 Aug;28(4):345-9. [PubMed ]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- 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 ]
- Ching KH, Westaway SK, Gitschier J, Higgins JJ, Hayflick SJ: HARP syndrome is allelic with pantothenate kinase-associated neurodegeneration. Neurology. 2002 Jun 11;58(11):1673-4. [PubMed ]
- Hayflick SJ, Westaway SK, Levinson B, Zhou B, Johnson MA, Ching KH, Gitschier J: Genetic, clinical, and radiographic delineation of Hallervorden-Spatz syndrome. N Engl J Med. 2003 Jan 2;348(1):33-40. [PubMed ]
- Nicholas AP, Earnst KS, Marson DC: Atypical Hallervorden-Spatz disease with preserved cognition and obtrusive obsessions and compulsions. Mov Disord. 2005 Jul;20(7):880-6. [PubMed ]
|
| Enzyme 83 Metabolite References |
Not Available |
|
Enzyme 84
[top]
|
| Enzyme 84 ID |
6314 |
| Enzyme 84 Name |
Pantothenate kinase 1 |
| Enzyme 84 Synonyms |
- hPanK
- hPanK1
- Pantothenic acid kinase 1
|
| Enzyme 84 Gene Name |
PANK1 |
| Enzyme 84 Protein Sequence |
>Pantothenate kinase 1
MLKLVGGGGGQDWACSVAGTSLGGEEAAFEVARPGDQGKAGGGSPGWGCAGIPDSAPGAG
VLQAGAVGPARGGQGAEEVGESAGGGEERRVRHPQAPALRLLNRKPQGGSGEIKTPENDL
QRGRLSRGPRTAPPAPGMGDRSGQQERSVPHSPGAPVGTSAAAVNGLLHNGFHPPPVQPP
HVCSRGPVGGSDAAPQRLPLLPELQPQPLLPQHDSPAKKCRLRRRMDSGRKNRPPFPWFG
MDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTM
CGRKGNLHFIRFPSCAMHRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHK
LDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELCQKKPYCLDNPYPMLLVNMGSGVS
ILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKDIYG
GDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENID
RVVFVGNFLRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALLELFKMTDDK
|
| Enzyme 84 Number of Residues |
598 |
| Enzyme 84 Molecular Weight |
64338.9 |
| Enzyme 84 Theoretical pI |
7.61 |
| Enzyme 84 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- pantothenate kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- coenzyme A biosynthetic process
- coenzyme biosynthetic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 84 General Function |
Involved in pantothenate kinase activity |
| Enzyme 84 Specific Function |
Plays a role in the physiological regulation of the intracellular CoA concentration |
| Enzyme 84 Pathways |
- Pantothenate and CoA Biosynthesis (map00770 )
|
| Enzyme 84 Reactions |
- ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate [RN:R03018]
|
| Enzyme 84 Pfam Domain Function |
|
| Enzyme 84 Signals |
|
| Enzyme 84 Transmembrane Regions |
|
| Enzyme 84 Essentiality |
Not Available |
| Enzyme 84 GenBank ID Protein |
23510400 |
| Enzyme 84 UniProtKB/Swiss-Prot ID |
Q8TE04 |
| Enzyme 84 UniProtKB/Swiss-Prot Entry Name |
PANK1_HUMAN |
| Enzyme 84 PDB ID |
Not Available |
| Enzyme 84 Cellular Location |
Not Available |
| Enzyme 84 Gene Sequence |
>1797 bp
ATGTTGAAACTCGTCGGTGGCGGTGGCGGGCAGGACTGGGCATGCTCAGTGGCGGGGACC
AGTCTGGGAGGCGAGGAAGCCGCGTTTGAAGTCGCGCGGCCTGGGGATCAGGGGAAGGCG
GGCGGCGGGAGCCCCGGCTGGGGGTGCGCGGGGATCCCCGATTCCGCGCCCGGGGCTGGC
GTGCTCCAGGCCGGCGCCGTGGGGCCGGCGCGCGGGGGGCAGGGCGCAGAGGAGGTGGGG
GAGTCGGCAGGAGGAGGGGAGGAGCGCCGGGTTCGCCATCCCCAGGCGCCGGCTCTGCGG
CTGCTGAATCGGAAGCCGCAGGGAGGATCCGGGGAAATAAAGACGCCGGAGAATGACCTC
CAGCGAGGCCGCCTGAGCCGGGGCCCGCGCACAGCCCCGCCAGCCCCCGGCATGGGCGAC
CGCAGCGGGCAGCAGGAGCGCTCGGTCCCGCACTCTCCAGGGGCCCCCGTGGGCACCAGC
GCCGCCGCTGTGAACGGGCTGCTGCACAACGGCTTCCATCCGCCGCCAGTCCAGCCGCCG
CACGTCTGCAGCCGGGGTCCAGTGGGCGGCAGCGACGCGGCGCCCCAGCGCCTCCCGCTC
CTGCCGGAGCTGCAGCCGCAGCCACTGCTCCCTCAGCATGACTCCCCGGCCAAGAAATGC
CGGCTGCGGAGGAGGATGGACTCGGGGAGAAAGAACAGGCCGCCATTCCCATGGTTTGGC
ATGGACATCGGTGGAACGCTGGTTAAATTGGTGTATTTCGAGCCGAAGGATATTACAGCC
GAAGAGGAGCAAGAGGAAGTGGAGAACCTGAAGAGCATCCGGAAGTATTTGACTTCTAAT
ACTGCTTATGGGAAAACTGGGATCCGAGACGTCCACCTGGAACTGAAAAACCTGACCATG
TGTGGACGCAAAGGGAACCTGCACTTCATCCGCTTTCCCAGCTGTGCTATGCACAGGTTC
ATTCAGATGGGCAGCGAGAAGAACTTCTCTAGCCTTCACACCACCCTCTGTGCCACAGGA
GGCGGGGCTTTCAAATTCGAAGAGGACTTCAGAATGATTGCTGACCTGCAGCTGCATAAA
CTGGATGAACTGGACTGTCTGATTCAGGGCCTGCTTTATGTCGACTCTGTTGGCTTCAAC
GGCAAGCCAGAATGTTACTATTTTGAAAATCCCACAAATCCTGAATTGTGTCAAAAAAAG
CCGTACTGCCTTGATAACCCATACCCTATGTTGCTGGTTAACATGGGCTCAGGTGTCAGC
ATTCTAGCCGTGTACTCCAAGGACAACTATAAAAGAGTTACAGGGACCAGTCTTGGAGGT
GGAACATTCCTAGGCCTATGTTGCTTGCTGACTGGTTGTGAGACCTTTGAAGAAGCTCTG
GAAATGGCAGCTAAAGGCGACAGCACCAATGTTGATAAACTGGTGAAGGACATTTACGGA
GGAGACTATGAACGATTTGGCCTTCAAGGATCTGCTGTAGCATCAAGCTTTGGCAACATG
ATGAGTAAAGAAAAGCGAGATTCCATCAGCAAGGAAGACCTCGCCCGGGCCACATTGGTC
ACCATCACCAACAACATTGGCTCCATTGCTCGGATGTGCGCGTTGAATGAGAACATAGAC
AGAGTTGTGTTTGTTGGAAATTTTCTCAGAATCAATATGGTCTCCATGAAGCTGCTGGCA
TATGCCATGGATTTTTGGTCCAAAGGACAACTGAAAGCTCTGTTTTTGGAACATGAGGGT
TATTTTGGAGCCGTTGGGGCACTGTTGGAACTGTTCAAAATGACTGATGACAAGTAG
|
| Enzyme 84 GenBank Gene ID |
NM_148977.1 |
| Enzyme 84 GeneCard ID |
PANK1 |
| Enzyme 84 GenAtlas ID |
PANK1 |
| Enzyme 84 HGNC ID |
HGNC:8598 |
| Enzyme 84 Chromosome Location |
1 |
| Enzyme 84 Locus |
10q23.31 |
| Enzyme 84 SNPs |
SNPJam Report |
| Enzyme 84 General References |
- Ni X, Ma Y, Cheng H, Jiang M, Ying K, Xie Y, Mao Y: Cloning and characterization of a novel human pantothenate kinase gene. Int J Biochem Cell Biol. 2002 Feb;34(2):109-15. [PubMed ]
- Ramaswamy G, Karim MA, Murti KG, Jackowski S: PPARalpha controls the intracellular coenzyme A concentration via regulation of PANK1alpha gene expression. J Lipid Res. 2004 Jan;45(1):17-31. Epub 2003 Oct 1. [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 ]
- Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, Hayflick SJ: A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet. 2001 Aug;28(4):345-9. [PubMed ]
|
| Enzyme 84 Metabolite References |
Not Available |
|
Enzyme 85
[top]
|
| Enzyme 85 ID |
6315 |
| Enzyme 85 Name |
Pantothenate kinase 3 |
| Enzyme 85 Synonyms |
- hPanK3
- Pantothenic acid kinase 3
|
| Enzyme 85 Gene Name |
PANK3 |
| Enzyme 85 Protein Sequence |
>Pantothenate kinase 3
MKIKDAKKPSFPWFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGS
TGIRDVHLELKDLTLFGRRGNLHFIRFPTQDLPTFIQMGRDKNFSTLQTVLCATGGGAYK
FEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPERCQKMPFNLD
DPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASK
GDSTQADKLVRDIYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNN
IGSVARMCAVNEKINRVVFVGNFLRVNTLSMKLLAYALDYWSKGQLKALFLEHEGYFGAV
GALLGLPNFS
|
| Enzyme 85 Number of Residues |
370 |
| Enzyme 85 Molecular Weight |
41093.7 |
| Enzyme 85 Theoretical pI |
6.52 |
| Enzyme 85 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- pantothenate kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- coenzyme A biosynthetic process
- coenzyme biosynthetic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 85 General Function |
Involved in pantothenate kinase activity |
| Enzyme 85 Specific Function |
Plays a role in the physiological regulation of the intracellular CoA concentration |
| Enzyme 85 Pathways |
- Pantothenate and CoA Biosynthesis (map00770 )
|
| Enzyme 85 Reactions |
- ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate [RN:R03018]
|
| Enzyme 85 Pfam Domain Function |
|
| Enzyme 85 Signals |
|
| Enzyme 85 Transmembrane Regions |
|
| Enzyme 85 Essentiality |
Not Available |
| Enzyme 85 GenBank ID Protein |
10434655 |
| Enzyme 85 UniProtKB/Swiss-Prot ID |
Q9H999 |
| Enzyme 85 UniProtKB/Swiss-Prot Entry Name |
PANK3_HUMAN |
| Enzyme 85 PDB ID |
Not Available |
| Enzyme 85 Cellular Location |
Not Available |
| Enzyme 85 Gene Sequence |
>1113 bp
ATGAAGATCAAAGATGCCAAGAAACCCTCTTTCCCATGGTTTGGCATGGACATTGGGGGA
ACTCTAGTAAAGCTCTCGTACTTTGAACCTATTGATATCACAGCAGAGGAAGAGCAAGAA
GAAGTTGAGAGTTTAAAAAGTATTCGGAAATATTTGACTTCTAACGTGGCATATGGATCC
ACCGGCATTCGGGATGTACACCTTGAACTGAAAGATTTAACACTTTTTGGCCGAAGAGGG
AACTTGCACTTTATCAGGTTTCCAACCCAGGACCTGCCTACTTTTATCCAAATGGGAAGA
GATAAAAACTTCTCAACATTGCAGACGGTGCTATGTGCTACAGGAGGTGGTGCTTACAAG
TTTGAAAAAGATTTTCGCACAATTGGAAACCTCCACCTGCACAAACTGGATGAACTTGAC
TGCCTTGTAAAGGGCTTGCTGTATATAGACTCTGTCAGTTTCAATGGACAAGCCGAGTGC
TATTATTTTGCTAATGCCTCAGAACCTGAGCGATGCCAAAAGATGCCTTTTAACCTGGAT
GATCCCTATCCACTGCTTGTAGTGAACATTGGCTCAGGAGTCAGTATTTTAGCAGTCCAT
TCCAAAGACAACTATAAACGAGTGACTGGGACAAGCCTTGGAGGGGGTACCTTTCTGGGT
TTATGCAGTTTATTGACTGGCTGTGAAAGTTTTGAAGAGGCTCTTGAAATGGCATCCAAA
GGTGATAGCACACAAGCTGACAAGCTGGTCCGTGATATTTATGGAGGAGATTATGAAAGA
TTTGGTTTGCCAGGTTGGGCTGTAGCATCTAGTTTTGGGAATATGATTTATAAGGAGAAG
CGAGAATCTGTTAGTAAAGAAGATCTGGCAAGAGCTACTTTAGTTACTATCACCAATAAC
ATTGGTTCTGTGGCACGAATGTGTGCTGTTAATGAGAAAATAAACAGAGTTGTCTTTGTT
GGAAACTTTTTACGTGTCAATACCCTCTCAATGAAACTTTTGGCATATGCACTGGATTAC
TGGTCAAAAGGTCAACTAAAAGCATTGTTTCTAGAACATGAGGGTTACTTTGGAGCAGTT
GGTGCACTTCTTGGGCTGCCAAATTTCAGCTAA
|
| Enzyme 85 GenBank Gene ID |
AK022961 |
| Enzyme 85 GeneCard ID |
PANK3 |
| Enzyme 85 GenAtlas ID |
PANK3 |
| Enzyme 85 HGNC ID |
HGNC:19365 |
| Enzyme 85 Chromosome Location |
5 |
| Enzyme 85 Locus |
5q34 |
| Enzyme 85 SNPs |
SNPJam Report |
| Enzyme 85 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 ]
- Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, Hayflick SJ: A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet. 2001 Aug;28(4):345-9. [PubMed ]
|
| Enzyme 85 Metabolite References |
Not Available |
|
Enzyme 86
[top]
|
| Enzyme 86 ID |
6316 |
| Enzyme 86 Name |
N-acetyl-D-glucosamine kinase |
| Enzyme 86 Synonyms |
- N-acetylglucosamine kinase
- GlcNAc kinase
|
| Enzyme 86 Gene Name |
NAGK |
| Enzyme 86 Protein Sequence |
>N-acetyl-D-glucosamine kinase
MAAIYGGVEGGGTRSEVLLVSEDGKILAEADGLSTNHWLIGTDKCVERINEMVNRAKRKA
GVDPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPYLSESYLITTDAAGSIATATPDGG
VVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHD
IGYVKQAMFHYFQVPDRLGILTHLYRDFDKCRFAGFCRKIAEGAQQGDPLSRYIFRKAGE
MLGRHIVAVLPEIDPVLFQGKIGLPILCVGSVWKSWELLKEGFLLALTQGREIQAQNFFS
SFTLMKLRHSSALGGASLGARHIGHLLPMDYSANAIAFYSYTFS
|
| Enzyme 86 Number of Residues |
344 |
| Enzyme 86 Molecular Weight |
37375.3 |
| Enzyme 86 Theoretical pI |
6.18 |
| Enzyme 86 GO Classification |
Not Available |
| Enzyme 86 General Function |
Carbohydrate transport and metabolism |
| Enzyme 86 Specific Function |
Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Also has ManNAc kinase activity |
| Enzyme 86 Pathways |
|
| Enzyme 86 Reactions |
- ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate [RN:R01201]
|
| Enzyme 86 Pfam Domain Function |
|
| Enzyme 86 Signals |
|
| Enzyme 86 Transmembrane Regions |
|
| Enzyme 86 Essentiality |
Not Available |
| Enzyme 86 GenBank ID Protein |
6491737 |
| Enzyme 86 UniProtKB/Swiss-Prot ID |
Q9UJ70 |
| Enzyme 86 UniProtKB/Swiss-Prot Entry Name |
NAGK_HUMAN |
| Enzyme 86 PDB ID |
Not Available |
| Enzyme 86 Cellular Location |
Not Available |
| Enzyme 86 Gene Sequence |
>1035 bp
ATGGCCGCGATCTATGGGGGTGTAGAGGGGGGAGGCACACGATCCGAGGTCCTTTTAGTC
TCAGAGGATGGGAAGATCCTGGCAGAAGCAGATGGACTGAGCACAAACCACTGGCTGATC
GGGACAGACAAGTGTGTGGAGAGGATCAATGAGATGGTGAACAGGGCCAAACGGAAAGCA
GGGGTGGATCCTCTGGTACCGCTGCGAATTTTGGGCCTATCTCTGAGCGGTGGGGACCAG
GAGGACGCGGGGAGGATCCTGATCGAGGAGCTGAGGGACCGATTTCCCTACCTGAGTGAA
AGCTACTTAATCACCACCGATGCCGCCGGCTCCATCGCCACAGCTACACCGGATGGTGGG
ATTGTGCTCATATCTGGAACAGGCTCCAACTGCAGGCTCATCAACCCTGATGGCTCCGAG
AGTGGCTGCGGCGGCTGGGGCCATATGATGGGTGATGAGGGTTCAGCCTACTGGATCGCA
CACCAAGCAGTGAAAATAGTGTTTGACTCCATTGACAACCTAGAGGCGGCTCCTCATGAT
ATCGGCTACGTCAAACAGGCCATGTTCCACTATTTCCAGGTGCCAGATCGGCTAGGGATA
CTCACTCACCTGTATAGGGACTTTGATAAATGCAGGTTTGCTGGGTTTTGCCGGAAAATT
GCAGAAGGTGCTCAGCAGGGAGACCCCCTTTCCCGCTATATCTTCAGGAAGGCTGGGGAG
ATGCTGGGCAGACACATCGTAGCAGTGTTGCCCGAGATTGACCCGGTCTTGTTCCAGGGC
AAGATTGGACTCCCCATCCTGTGCGTGGGCTCTGTGTGGAAGAGCTGGGAGCTGCTGAAG
GAAGGTTTTCTTTTGGCGCTGACCCAGGGCAGAGAGATCCAGGCTCAGAACTTCTTCTCC
AGCTTCACCCTGATGAAGCTGAGGCACTCCTCCGCTCTGGGTGGGGCCAGCCTAGGGGCC
AGGCACATCGGGCACCTCCTCCCCATGGACTATAGCGCCAATGCCATTGCCTTCTATTCC
TACACCTTTTCCTAG
|
| Enzyme 86 GenBank Gene ID |
AJ242910 |
| Enzyme 86 GeneCard ID |
NAGK |
| Enzyme 86 GenAtlas ID |
NAGK |
| Enzyme 86 HGNC ID |
HGNC:17174 |
| Enzyme 86 Chromosome Location |
2 |
| Enzyme 86 Locus |
2p13.3 |
| Enzyme 86 SNPs |
SNPJam Report |
| Enzyme 86 General References |
- Hinderlich S, Berger M, Schwarzkopf M, Effertz K, Reutter W: Molecular cloning and characterization of murine and human N-acetylglucosamine kinase. Eur J Biochem. 2000 Jun;267(11):3301-8. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- 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 ]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
- Maguire PB, Wynne KJ, Harney DF, O'Donoghue NM, Stephens G, Fitzgerald DJ: Identification of the phosphotyrosine proteome from thrombin activated platelets. Proteomics. 2002 Jun;2(6):642-8. [PubMed ]
- 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 ]
- Weihofen WA, Berger M, Chen H, Saenger W, Hinderlich S: Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation. J Mol Biol. 2006 Dec 1;364(3):388-99. Epub 2006 Sep 3. [PubMed ]
|
| Enzyme 86 Metabolite References |
Not Available |
|
Enzyme 87
[top]
|
| Enzyme 87 ID |
6344 |
| Enzyme 87 Name |
Pyridoxal kinase |
| Enzyme 87 Synonyms |
- Pyridoxine kinase
|
| Enzyme 87 Gene Name |
PDXK |
| Enzyme 87 Protein Sequence |
>Pyridoxal kinase
MEEECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSD
ELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKW
DGEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGP
DTVVITSSDLPSPQGSNYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVFVGTGDLFAAM
LLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEGVRPSPMQLELRMVQSKRDI
EDPEIVVQATVL
|
| Enzyme 87 Number of Residues |
312 |
| Enzyme 87 Molecular Weight |
35102.1 |
| Enzyme 87 Theoretical pI |
6.05 |
| Enzyme 87 GO Classification |
| Function |
- catalytic activity
- kinase activity
- pyridoxal kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolic process
- pyridoxine biosynthetic process
- pyridoxine metabolic process
- small molecule metabolic process
- vitamin B6 metabolic process
- vitamin metabolic process
- water-soluble vitamin metabolic process
|
| Component |
| — |
|
| Enzyme 87 General Function |
Involved in pyridoxal kinase activity |
| Enzyme 87 Specific Function |
Required for synthesis of pyridoxal-5-phosphate from vitamin B6 |
| Enzyme 87 Pathways |
|
| Enzyme 87 Reactions |
- ATP + pyridoxal = ADP + pyridoxal 5'-phosphate [RN:R00174]
|
| Enzyme 87 Pfam Domain Function |
|
| Enzyme 87 Signals |
|
| Enzyme 87 Transmembrane Regions |
|
| Enzyme 87 Essentiality |
Not Available |
| Enzyme 87 GenBank ID Protein |
Not Available |
| Enzyme 87 UniProtKB/Swiss-Prot ID |
O00764 |
| Enzyme 87 UniProtKB/Swiss-Prot Entry Name |
PDXK_HUMAN |
| Enzyme 87 PDB ID |
1RFV |
| Enzyme 87 PDB File |
Show |
| Enzyme 87 3D Structure |
|
| Enzyme 87 Cellular Location |
Not Available |
| Enzyme 87 Gene Sequence |
>939 bp
ATGGAGGAGGAGTGCCGGGTGCTCTCCATACAGAGCCACGTCATCCGCGGCTACGTGGGC
AACCGGGCGGCCACGTTCCCGCTGCAGGTTTTGGGATTTGAGATTGACGCGGTGAACTCT
GTCCAGTTTTCAAACCACACAGGCTATGCCCACTGGAAGGGCCAAGTGCTGAATTCAGAT
GAGCTCCAGGAGTTGTACGAAGGCCTGAGGCTGAACAACATGAATAAATATGACTACGTG
CTCACAGGTTATACGAGGGACAAGTCGTTCCTGGCCATGGTGGTGGACATTGTGCAGGAG
CTGAAGCAGCAGAACCCCAGGCTGGTGTACGTGTGTGATCCAGTCTTGGGTGACAAGTGG
GACGGCGAAGGCTCGATGTACGTCCCGGAGGACCTCCTTCCCGTCTACAAAGAAAAAGTG
GTGCCGCTTGCAGACATTATCACGCCCAACCAGTTTGAGGCCGAGTTACTGAGTGGCCGG
AAGATCCACAGCCAGGAGGAAGCCTTGCGGGTGATGGACATGCTGCACTCTATGGGCCCC
GACACCGTGGTCATCACCAGCTCCGACCTGCCCTCCCCGCAGGGCAGCAACTACCTGATT
GTGCTGGGGAGTCAGAGGAGGAGGAATCCCGCTGGCTCCGTGGTGATGGAACGCATCCGG
ATGGACATTCGCAAAGTGGACGCCGTCTTTGTGGGCACTGGGGACCTGTTTGCTGCCATG
CTCCTGGCGTGGACACACAAGCACCCCAATAACCTCAAGGTGGCCTGTGAGAAGACCGTG
TCTACCTTGCACCACGTTCTGCAGAGGACCATCCAGTGTGCAAAAGCCCAGGCCGGGGAA
GGAGTGAGGCCCAGCCCCATGCAGCTGGAGCTGCGGATGGTGCAGAGCAAAAGGGACATC
GAGGACCCAGAGATCGTCGTCCAGGCCACGGTGCTGTGA
|
| Enzyme 87 GenBank Gene ID |
U89606 |
| Enzyme 87 GeneCard ID |
PDXK |
| Enzyme 87 GenAtlas ID |
PDXK |
| Enzyme 87 HGNC ID |
HGNC:8819 |
| Enzyme 87 Chromosome Location |
2 |
| Enzyme 87 Locus |
21q22.3 |
| Enzyme 87 SNPs |
SNPJam Report |
| Enzyme 87 General References |
- Hanna MC, Turner AJ, Kirkness EF: Human pyridoxal kinase. cDNA cloning, expression, and modulation by ligands of the benzodiazepine receptor. J Biol Chem. 1997 Apr 18;272(16):10756-60. [PubMed ]
- Fang X, Zhou ZM, Lu L, Yin LL, Li JM, Zhen Y, Wang H, Sha JH: Expression of a novel pyridoxal kinase mRNA splice variant, PKH-T, in human testis. Asian J Androl. 2004 Jun;6(2):83-91. [PubMed ]
- Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Lee HS, Moon BJ, Choi SY, Kwon OS: Human pyridoxal kinase: overexpression and properties of the recombinant enzyme. Mol Cells. 2000 Aug 31;10(4):452-9. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
|
| Enzyme 87 Metabolite References |
Not Available |
|
Enzyme 88
[top]
|
| Enzyme 88 ID |
6348 |
| Enzyme 88 Name |
Riboflavin kinase |
| Enzyme 88 Synonyms |
- ATP:riboflavin 5'-phosphotransferase
- Flavokinase
|
| Enzyme 88 Gene Name |
RFK |
| Enzyme 88 Protein Sequence |
>Riboflavin kinase
MRHLPYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASVGSGDVHK
MVVSIGWNPYYKNTKKSMETHIMHTFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQ
GDIEEAKKRLELPEHLKIKEDNFFQVSKSKIMNGH
|
| Enzyme 88 Number of Residues |
155 |
| Enzyme 88 Molecular Weight |
17623.1 |
| Enzyme 88 Theoretical pI |
8.43 |
| Enzyme 88 GO Classification |
| Function |
- catalytic activity
- kinase activity
- riboflavin kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolic process
- nitrogen compound metabolic process
- riboflavin biosynthetic process
- riboflavin metabolic process
|
| Component |
| — |
|
| Enzyme 88 General Function |
Involved in riboflavin kinase activity |
| Enzyme 88 Specific Function |
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN) |
| Enzyme 88 Pathways |
|
| Enzyme 88 Reactions |
- ATP + riboflavin = ADP + FMN [RN:R00549]
|
| Enzyme 88 Pfam Domain Function |
|
| Enzyme 88 Signals |
|
| Enzyme 88 Transmembrane Regions |
|
| Enzyme 88 Essentiality |
Not Available |
| Enzyme 88 GenBank ID Protein |
269973877 |
| Enzyme 88 UniProtKB/Swiss-Prot ID |
Q969G6 |
| Enzyme 88 UniProtKB/Swiss-Prot Entry Name |
RIFK_HUMAN |
| Enzyme 88 PDB ID |
1Q9S |
| Enzyme 88 PDB File |
Show |
| Enzyme 88 3D Structure |
|
| Enzyme 88 Cellular Location |
Not Available |
| Enzyme 88 Gene Sequence |
>468 bp
ATGAGGCACCTGCCTTACTTCTGCCGGGGTCAAGTGGTGCGGGGCTTCGGCCGCGGCTCC
AAGCAGCTGGGCATCCCCACAGCTAATTTTCCTGAGCAAGTGGTAGATAATCTTCCAGCT
GATATATCCACTGGTATTTACTATGGTTGGGCCAGTGTTGGAAGTGGAGATGTCCATAAG
ATGGTGGTGAGCATAGGATGGAACCCATATTACAAGAATACGAAGAAGTCTATGGAAACA
CATATCATGCATACCTTCAAAGAGGACTTCTATGGGGAAATCCTCAATGTGGCCATTGTT
GGCTACCTGAGACCAGAAAAGAACTTTGATTCTTTAGAGTCACTTATTTCAGCAATTCAA
GGTGATATTGAAGAAGCTAAGAAACGACTAGAGTTACCAGAACATTTGAAAATCAAAGAA
GACAATTTCTTCCAGGTTTCTAAAAGCAAAATAATGAATGGCCACTGA
|
| Enzyme 88 GenBank Gene ID |
NM_018339.5 |
| Enzyme 88 GeneCard ID |
RFK |
| Enzyme 88 GenAtlas ID |
RFK |
| Enzyme 88 HGNC ID |
HGNC:30324 |
| Enzyme 88 Chromosome Location |
9 |
| Enzyme 88 Locus |
9q21.13 |
| Enzyme 88 SNPs |
SNPJam Report |
| Enzyme 88 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Karthikeyan S, Zhou Q, Mseeh F, Grishin NV, Osterman AL, Zhang H: Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch. Structure. 2003 Mar;11(3):265-73. [PubMed ]
|
| Enzyme 88 Metabolite References |
Not Available |
|
Enzyme 89
[top]
|
| Enzyme 89 ID |
6372 |
| Enzyme 89 Name |
Sphingosine kinase 2 |
| Enzyme 89 Synonyms |
- SK 2
- SPK 2
|
| Enzyme 89 Gene Name |
SPHK2 |
| Enzyme 89 Protein Sequence |
>Sphingosine kinase 2
MNGHLEAEEQQDQRPDQELTGSWGHGPRSTLVRAKAMAPPPPPLAASTPLLHGEFGSYPA
RGPRFALTLTSQALHIQRLRPKPEARPRGGLVPLAEVSGCCTLRSRSPSDSAAYFCIYTY
PRGRRGARRRATRTFRADGAATYEENRAEAQRWATALTCLLRGLPLPGDGEITPDLLPRP
PRLLLLVNPFGGRGLAWQWCKNHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDG
IVTVSGDGLLHEVLNGLLDRPDWEEAVKMPVGILPCGSGNALAGAVNQHGGFEPALGLDL
LLNCSLLLCRGGGHPLDLLSVTLASGSRCFSFLSVAWGFVSDVDIQSERFRALGSARFTL
GTVLGLATLHTYRGRLSYLPATVEPASPTPAHSLPRAKSELTLTPDPAPPMAHSPLHRSV
SDLPLPLPQPALASPGSPEPLPILSLNGGGPELAGDWGGAGDAPLSPDPLLSSPPGSPKA
ALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCGPPDHLLPPLGTPLPPDWVTLEGDFVL
MLAISPSHLGADLVAAPHARFDDGLVHLCWVRSGISRAALLRLFLAMERGSHFSLGCPQL
GYAAARAFRLEPLTPRGVLTVDGEQVEYGPLQAQMHPGIGTLLTGPPGCPGREP
|
| Enzyme 89 Number of Residues |
654 |
| Enzyme 89 Molecular Weight |
69216.4 |
| Enzyme 89 Theoretical pI |
6.94 |
| Enzyme 89 GO Classification |
| Function |
- catalytic activity
- diacylglycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 89 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 89 Specific Function |
Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro- dihydrosphingosine, D-erythro-sphingosine and L-threo- dihydrosphingosine. Binds phosphoinositides |
| Enzyme 89 Pathways |
Not Available |
| Enzyme 89 Reactions |
- ATP + sphinganine = ADP + sphinganine 1-phosphate [RN:R02976]
|
| Enzyme 89 Pfam Domain Function |
|
| Enzyme 89 Signals |
|
| Enzyme 89 Transmembrane Regions |
|
| Enzyme 89 Essentiality |
Not Available |
| Enzyme 89 GenBank ID Protein |
21361699 |
| Enzyme 89 UniProtKB/Swiss-Prot ID |
Q9NRA0 |
| Enzyme 89 UniProtKB/Swiss-Prot Entry Name |
SPHK2_HUMAN |
| Enzyme 89 PDB ID |
Not Available |
| Enzyme 89 Cellular Location |
Not Available |
| Enzyme 89 Gene Sequence |
>1965 bp
ATGAATGGACACCTTGAAGCAGAGGAGCAGCAGGACCAGAGGCCAGACCAGGAGCTGACC
GGGAGCTGGGGCCACGGGCCTAGGAGCACCCTGGTCAGGGCTAAGGCCATGGCCCCGCCC
CCACCGCCACTGGCTGCCAGCACCCCGCTCCTCCATGGCGAGTTTGGCTCCTACCCAGCC
CGAGGCCCACGCTTTGCCCTCACCCTTACATCGCAGGCCCTGCACATACAGCGGCTGCGC
CCCAAACCTGAAGCCAGGCCCCGGGGTGGCCTGGTCCCGTTGGCCGAGGTCTCAGGCTGC
TGCACCCTGCGAAGCCGCAGCCCCTCAGACTCAGCGGCCTACTTCTGCATCTACACCTAC
CCTCGGGGCCGGCGCGGGGCCCGGCGCAGAGCCACTCGCACCTTCCGGGCAGATGGGGCC
GCCACCTACGAAGAGAACCGTGCCGAGGCCCAGCGCTGGGCCACTGCCCTCACCTGTCTG
CTCCGAGGACTGCCACTGCCCGGGGATGGGGAGATCACCCCTGACCTGCTACCTCGGCCG
CCCCGGTTGCTTCTATTGGTCAATCCCTTTGGGGGTCGGGGCCTGGCCTGGCAGTGGTGT
AAGAACCACGTGCTTCCCATGATCTCTGAAGCTGGGCTGTCCTTCAACCTCATCCAGACA
GAACGACAGAACCACGCCCGGGAGCTGGTCCAGGGGCTGAGCCTGAGTGAGTGGGATGGC
ATCGTCACGGTCTCGGGAGACGGGCTGCTCCATGAGGTGCTGAACGGGCTCCTAGATCGC
CCTGACTGGGAGGAAGCTGTGAAGATGCCTGTGGGCATCCTCCCCTGCGGCTCGGGCAAC
GCGCTGGCCGGAGCAGTGAACCAGCACGGGGGATTTGAGCCAGCCCTGGGCCTCGACCTG
TTGCTCAACTGCTCACTGTTGCTGTGCCGGGGTGGTGGCCACCCACTGGACCTGCTCTCC
GTGACGCTGGCCTCGGGCTCCCGCTGTTTCTCCTTCCTGTCTGTGGCCTGGGGCTTCGTG
TCAGATGTGGATATCCAGAGCGAGCGCTTCAGGGCCTTGGGCAGTGCCCGCTTCACACTG
GGCACGGTGCTGGGCCTCGCCACACTGCACACCTACCGCGGACGCCTCTCCTACCTCCCC
GCCACTGTGGAACCTGCCTCGCCCACCCCTGCCCATAGCCTGCCTCGTGCCAAGTCGGAG
CTGACCCTAACCCCAGACCCAGCCCCGCCCATGGCCCACTCACCCCTGCATCGTTCTGTG
TCTGACCTGCCTCTTCCCCTGCCCCAGCCTGCCCTGGCCTCTCCTGGCTCGCCAGAACCC
CTGCCCATCCTGTCCCTCAACGGTGGGGGCCCAGAGCTGGCTGGGGACTGGGGTGGGGCT
GGGGATGCTCCGCTGTCCCCGGACCCACTGCTGTCTTCACCTCCTGGCTCTCCCAAGGCA
GCTCTACACTCACCCGTCTCCGAAGGGGCCCCCGTAATTCCCCCATCCTCTGGGCTCCCA
CTTCCCACCCCTGATGCCCGGGTAGGGGCCTCCACCTGCGGCCCGCCCGACCACCTGCTG
CCTCCGCTGGGCACCCCGCTGCCCCCAGACTGGGTGACGCTGGAGGGGGACTTTGTGCTC
ATGTTGGCCATCTCGCCCAGCCACCTAGGCGCTGACCTGGTGGCAGCTCCGCATGCGCGC
TTCGACGACGGCCTGGTGCACCTGTGCTGGGTGCGTAGCGGCATCTCGCGGGCTGCGCTG
CTGCGCCTTTTCTTGGCCATGGAGCGTGGTAGCCACTTCAGCCTGGGCTGTCCGCAGCTG
GGCTACGCCGCGGCCCGTGCCTTCCGCCTAGAGCCGCTCACACCACGCGGCGTGCTCACA
GTGGACGGGGAGCAGGTGGAGTATGGGCCGCTACAGGCACAGATGCACCCTGGCATCGGT
ACACTGCTCACTGGGCCTCCTGGCTGCCCGGGGCGGGAGCCCTGA
|
| Enzyme 89 GenBank Gene ID |
NM_020126.3 |
| Enzyme 89 GeneCard ID |
SPHK2 |
| Enzyme 89 GenAtlas ID |
SPHK2 |
| Enzyme 89 HGNC ID |
HGNC:18859 |
| Enzyme 89 Chromosome Location |
1 |
| Enzyme 89 Locus |
19q13.2 |
| Enzyme 89 SNPs |
SNPJam Report |
| Enzyme 89 General References |
- Liu H, Sugiura M, Nava VE, Edsall LC, Kono K, Poulton S, Milstien S, Kohama T, Spiegel S: Molecular cloning and functional characterization of a novel mammalian sphingosine kinase type 2 isoform. J Biol Chem. 2000 Jun 30;275(26):19513-20. [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 ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Schroder B, Wrocklage C, Pan C, Jager R, Kosters B, Schafer H, Elsasser HP, Mann M, Hasilik A: Integral and associated lysosomal membrane proteins. Traffic. 2007 Dec;8(12):1676-86. Epub 2007 Sep 26. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Don AS, Rosen H: A lipid binding domain in sphingosine kinase 2. Biochem Biophys Res Commun. 2009 Feb 27;380(1):87-92. Epub 2009 Jan 23. [PubMed ]
|
| Enzyme 89 Metabolite References |
Not Available |
|
Enzyme 90
[top]
|
| Enzyme 90 ID |
6377 |
| Enzyme 90 Name |
Ribokinase |
| Enzyme 90 Synonyms |
Not Available |
| Enzyme 90 Gene Name |
RBKS |
| Enzyme 90 Protein Sequence |
>Ribokinase
MAASGEPQRQWQEEVAAVVVVGSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCV
QAARLGAMTSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNI
IVIVAGANLLLNTEDLRAAANVISRAKVMVCQLEITPATSLEALTMARRSGVKTLFNPAP
AIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIITLGAEG
CVVLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPNLSLEDMLNRSNFIAAV
SVQAAGTQSSYPYKKDLPLTLF
|
| Enzyme 90 Number of Residues |
322 |
| Enzyme 90 Molecular Weight |
34142.7 |
| Enzyme 90 Theoretical pI |
4.68 |
| Enzyme 90 GO Classification |
| Function |
- catalytic activity
- phosphotransferase activity, alcohol group as acceptor
- ribokinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- D-ribose metabolic process
- alcohol metabolic process
- metabolic process
- monosaccharide metabolic process
- pentose metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 90 General Function |
Involved in ribokinase activity |
| Enzyme 90 Specific Function |
ATP + D-ribose = ADP + D-ribose 5-phosphate |
| Enzyme 90 Pathways |
|
| Enzyme 90 Reactions |
- ATP + D-ribose = ADP + D-ribose 5-phosphate [RN:R01051]
|
| Enzyme 90 Pfam Domain Function |
|
| Enzyme 90 Signals |
|
| Enzyme 90 Transmembrane Regions |
|
| Enzyme 90 Essentiality |
Not Available |
| Enzyme 90 GenBank ID Protein |
10799803 |
| Enzyme 90 UniProtKB/Swiss-Prot ID |
Q9H477 |
| Enzyme 90 UniProtKB/Swiss-Prot Entry Name |
RBSK_HUMAN |
| Enzyme 90 PDB ID |
Not Available |
| Enzyme 90 Cellular Location |
Not Available |
| Enzyme 90 Gene Sequence |
>969 bp
ATGGCGGCGTCTGGGGAACCCCAGAGGCAGTGGCAAGAGGAGGTGGCGGCGGTGGTAGTG
GTGGGCTCCTGCATGACCGACCTGGTCAGTCTTACTTCTCGTTTGCCAAAAACTGGAGAA
ACCATCCATGGACATAAGTTTTTTATTGGCTTTGGAGGGAAAGGTGCCAACCAGTGTGTC
CAAGCTGCTCGGCTTGGAGCAATGACGTCCATGGTGTGTAAGGTTGGCAAAGATTCTTTT
GGCAATGATTATATAGAAAACTTAAAACAGAATGATATTTCTACAGAATTTACATATCAG
ACTAAAGATGCTGCTACAGGAACTGCTTCTATAATTGTCAATAATGAAGGCCAGAATATC
ATTGTCATAGTGGCTGGAGCAAATTTACTTTTGAATACGGAGGATCTGAGGGCAGCAGCC
AATGTCATTAGCAGAGCCAAAGTCATGGTCTGCCAGCTCGAAATAACTCCAGCAACTTCT
TTGGAAGCCCTAACAATGGCCCGCAGGAGTGGAGTGAAAACCTTGTTCAATCCAGCCCCT
GCCATTGCTGACCTGGATCCCCAGTTCTACACCCTCTCAGATGTGTTCTGCTGCAATGAA
AGTGAGGCTGAGATTTTAACTGGCCTCACGGTGGGCAGCGCTGCAGATGCTGGGGAGGCT
GCATTAGTGCTCTTGAAAAGGGGCTGCCAGGTGGTAATCATTACCTTAGGGGCTGAAGGA
TGTGTGGTGCTGTCACAGACAGAACCTGAGCCAAAGCACATTCCCACAGAGAAAGTCAAG
GCTGTGGATACCACGGGTGCTGGTGACAGCTTTGTGGGAGCTCTGGCCTTCTACCTGGCT
TACTATCCAAATCTGTCCTTGGAAGACATGCTCAACAGATCCAATTTCATTGCAGCAGTC
AGTGTCCAGGCTGCAGGAACACAGTCATCTTACCCTTACAAAAAAGACCTTCCGCTTACT
CTGTTTTGA
|
| Enzyme 90 GenBank Gene ID |
AJ404857 |
| Enzyme 90 GeneCard ID |
RBKS |
| Enzyme 90 GenAtlas ID |
RBKS |
| Enzyme 90 HGNC ID |
HGNC:30325 |
| Enzyme 90 Chromosome Location |
2 |
| Enzyme 90 Locus |
2p23.3 |
| Enzyme 90 SNPs |
SNPJam Report |
| Enzyme 90 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Park J, van Koeverden P, Singh B, Gupta RS: Identification and characterization of human ribokinase and comparison of its properties with E. coli ribokinase and human adenosine kinase. FEBS Lett. 2007 Jul 10;581(17):3211-6. Epub 2007 Jun 15. [PubMed ]
|
| Enzyme 90 Metabolite References |
Not Available |
|
Enzyme 91
[top]
|
| Enzyme 91 ID |
6415 |
| Enzyme 91 Name |
cGMP-dependent protein kinase 1 |
| Enzyme 91 Synonyms |
- cGK 1
- cGK1
- cGMP-dependent protein kinase I
- cGKI
|
| Enzyme 91 Gene Name |
PRKG1 |
| Enzyme 91 Protein Sequence |
>cGMP-dependent protein kinase 1
MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTR
AQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMY
PVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTAT
VKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEET
HYENGEYIIRQGARGDTFFIISKGTVNVTREDSPSEDPVFLRTLGKGDWFGEKALQGEDV
RTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDF
NIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDF
IVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGI
IYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISAD
YWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPS
ERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDSFPEDNDEPP
PDDNSGWDIDF
|
| Enzyme 91 Number of Residues |
671 |
| Enzyme 91 Molecular Weight |
76363.8 |
| Enzyme 91 Theoretical pI |
5.87 |
| Enzyme 91 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- cGMP-dependent protein kinase activity
- catalytic activity
- cyclic nucleotide-dependent protein kinase activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 91 General Function |
Involved in protein serine/threonine kinase activity |
| Enzyme 91 Specific Function |
Phosphorylates PPP1R12A |
| Enzyme 91 Pathways |
Not Available |
| Enzyme 91 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 91 Pfam Domain Function |
|
| Enzyme 91 Signals |
|
| Enzyme 91 Transmembrane Regions |
|
| Enzyme 91 Essentiality |
Not Available |
| Enzyme 91 GenBank ID Protein |
148612818 |
| Enzyme 91 UniProtKB/Swiss-Prot ID |
Q13976 |
| Enzyme 91 UniProtKB/Swiss-Prot Entry Name |
KGP1_HUMAN |
| Enzyme 91 PDB ID |
Not Available |
| Enzyme 91 Cellular Location |
Not Available |
| Enzyme 91 Gene Sequence |
>2016 bp
ATGAGCGAGCTAGAGGAAGACTTTGCCAAGATTCTCATGCTCAAGGAGGAGAGGATCAAA
GAGCTGGAGAAGCGGCTGTCAGAGAAGGAGGAAGAAATTCAGGAGCTGAAGAGGAAACTC
CACAAATGCCAGTCGGTGCTCCCAGTGCCCTCGACCCACATCGGCCCCCGGACCACCCGG
GCGCAGGGCATCTCGGCCGAGCCGCAGACGTACAGGTCCTTCCACGACCTCCGACAGGCA
TTCCGGAAGTTCACCAAGTCCGAAAGGTCCAAGGATCTTATAAAGGAAGCTATCCTTGAC
AATGACTTTATGAAGAACTTGGAGCTGTCGCAGATCCAGGAGATTGTGGATTGTATGTAC
CCGGTGGAGTATGGCAAGGACAGTTGCATCATCAAAGAAGGAGACGTGGGGTCACTGGTG
TATGTCATGGAAGATGGTAAGGTTGAAGTTACAAAAGAAGGTGTGAAGTTGTGTACCATG
GGTCCAGGAAAAGTGTTTGGGGAATTGGCTATTCTTTACAACTGTACCCGGACAGCGACC
GTCAAGACTCTTGTAAATGTAAAACTCTGGGCCATTGATCGACAATGTTTTCAAACAATA
ATGATGAGGACAGGACTCATCAAGCATACCGAGTATATGGAATTTTTAAAAAGCGTTCCA
ACATTCCAGAGCCTTCCTGAAGAGATCCTCAGCAAGCTTGCTGATGTCCTTGAAGAGACC
CACTATGAAAATGGAGAATATATTATCAGGCAAGGTGCAAGAGGGGACACCTTCTTTATC
ATCAGCAAAGGAACGGTAAATGTCACTCGTGAAGACTCACCGAGTGAAGACCCAGTCTTT
CTTAGAACTTTAGGAAAAGGAGACTGGTTTGGAGAGAAAGCCTTGCAGGGGGAAGATGTG
AGAACAGCAAACGTAATTGCTGCAGAAGCTGTAACCTGCCTTGTGATTGACAGAGACTCT
TTTAAACATTTGATTGGAGGGCTGGATGATGTTTCTAATAAAGCATATGAAGATGCAGAA
GCTAAAGCAAAATATGAAGCTGAAGCGGCTTTCTTCGCCAACCTGAAGCTGTCTGATTTC
AACATCATTGATACCCTTGGAGTTGGAGGTTTCGGACGAGTAGAACTGGTCCAGTTGAAA
AGTGAAGAATCCAAAACGTTTGCAATGAAGATTCTCAAGAAACGTCACATTGTGGACACA
AGACAGCAGGAGCACATCCGCTCAGAGAAGCAGATCATGCAGGGGGCTCATTCCGATTTC
ATAGTGAGACTGTACAGAACATTTAAGGACAGCAAATATTTGTATATGTTGATGGAAGCT
TGTCTAGGTGGAGAGCTCTGGACCATTCTCAGGGATAGAGGTTCGTTTGAAGATTCTACA
ACCAGATTTTACACAGCATGTGTGGTAGAAGCTTTTGCCTATCTGCATTCCAAAGGAATC
ATTTACAGGGACCTCAAGCCAGAAAATCTCATCCTAGATCACCGAGGTTATGCCAAACTG
GTTGATTTTGGCTTTGCAAAGAAAATAGGATTTGGAAAGAAAACATGGACTTTTTGTGGG
ACTCCAGAGTATGTAGCCCCAGAGATCATCCTGAACAAAGGCCATGACATTTCAGCCGAC
TACTGGTCACTGGGAATCCTAATGTATGAACTCCTGACTGGCAGCCCACCTTTCTCAGGC
CCAGATCCTATGAAAACCTATAACATCATATTGAGGGGGATTGACATGATAGAATTTCCA
AAGAAGATTGCCAAAAATGCTGCTAATTTAATTAAAAAACTATGCAGGGACAATCCATCA
GAAAGATTAGGGAATTTGAAAAATGGAGTAAAAGACATTCAAAAGCACAAATGGTTTGAG
GGCTTTAACTGGGAAGGCTTAAGAAAAGGTACCTTGACACCTCCTATAATACCAAGTGTT
GCATCACCCACAGACACAAGTAATTTTGACAGTTTCCCTGAGGACAACGATGAACCACCA
CCTGATGACAACTCAGGATGGGATATAGACTTCTAA
|
| Enzyme 91 GenBank Gene ID |
NM_001098512.1 |
| Enzyme 91 GeneCard ID |
PRKG1 |
| Enzyme 91 GenAtlas ID |
PRKG1 |
| Enzyme 91 HGNC ID |
HGNC:9414 |
| Enzyme 91 Chromosome Location |
1 |
| Enzyme 91 Locus |
10q11.2 |
| Enzyme 91 SNPs |
SNPJam Report |
| Enzyme 91 General References |
- Sandberg M, Natarajan V, Ronander I, Kalderon D, Walter U, Lohmann SM, Jahnsen T: Molecular cloning and predicted full-length amino acid sequence of the type I beta isozyme of cGMP-dependent protein kinase from human placenta. Tissue distribution and developmental changes in rat. FEBS Lett. 1989 Sep 25;255(2):321-9. [PubMed ]
- Tamura N, Itoh H, Ogawa Y, Nakagawa O, Harada M, Chun TH, Suga S, Yoshimasa T, Nakao K: cDNA cloning and gene expression of human type Ialpha cGMP-dependent protein kinase. Hypertension. 1996 Mar;27(3 Pt 2):552-7. [PubMed ]
- Orstavik S, Natarajan V, Tasken K, Jahnsen T, Sandberg M: Characterization of the human gene encoding the type I alpha and type I beta cGMP-dependent protein kinase (PRKG1). Genomics. 1997 Jun 1;42(2):311-8. [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 ]
- Surks HK, Mochizuki N, Kasai Y, Georgescu SP, Tang KM, Ito M, Lincoln TM, Mendelsohn ME: Regulation of myosin phosphatase by a specific interaction with cGMP- dependent protein kinase Ialpha. Science. 1999 Nov 19;286(5444):1583-7. [PubMed ]
- Wooldridge AA, MacDonald JA, Erdodi F, Ma C, Borman MA, Hartshorne DJ, Haystead TA: Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides. J Biol Chem. 2004 Aug 13;279(33):34496-504. Epub 2004 Jun 11. [PubMed ]
- Antl M, von Bruhl ML, Eiglsperger C, Werner M, Konrad I, Kocher T, Wilm M, Hofmann F, Massberg S, Schlossmann J: IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation. Blood. 2007 Jan 15;109(2):552-9. Epub 2006 Sep 21. [PubMed ]
- Lee E, Hayes DB, Langsetmo K, Sundberg EJ, Tao TC: Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase. J Mol Biol. 2007 Nov 9;373(5):1198-212. Epub 2007 Aug 25. [PubMed ]
- Sharma AK, Zhou GP, Kupferman J, Surks HK, Christensen EN, Chou JJ, Mendelsohn ME, Rigby AC: Probing the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase. J Biol Chem. 2008 Nov 21;283(47):32860-9. Epub 2008 Sep 9. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Schnell JR, Zhou GP, Zweckstetter M, Rigby AC, Chou JJ: Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha. Protein Sci. 2005 Sep;14(9):2421-8. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 91 Metabolite References |
Not Available |
|
Enzyme 92
[top]
|
| Enzyme 92 ID |
6419 |
| Enzyme 92 Name |
cGMP-dependent protein kinase 2 |
| Enzyme 92 Synonyms |
- cGK 2
- cGK2
- cGMP-dependent protein kinase II
- cGKII
|
| Enzyme 92 Gene Name |
PRKG2 |
| Enzyme 92 Protein Sequence |
>cGMP-dependent protein kinase 2
MGNGSVKPKHSKHPDGHSGNLTTDALRNKVTELERELRRKDAEIQEREYHLKELREQLSK
QTVAIAELTEELQNKCIQLNKLQDVVHMQGGSPLQASPDKVPLEVHRKTSGLVSLHSRRG
AKAGVSAEPTTRTYDLNKPPEFSFEKARVRKDSSEKKLITDALNKNQFLKRLDPQQIKDM
VECMYGRNYQQGSYIIKQGEPGNHIFVLAEGRLEVFQGEKLLSSIPMWTTFGELAILYNC
TRTASVKAITNVKTWALDREVFQNIMRRTAQARDEQYRNFLRSVSLLKNLPEDKLTKIID
CLEVEYYDKGDYIIREGEEGSTFFILAKGKVKVTQSTEGHDQPQLIKTLQKGEYFGEKAL
ISDDVRSANIIAEENDVACLVIDRETFNQTVGTFEELQKYLEGYVANLNRDDEKRHAKRS
MSNWKLSKALSLEMIQLKEKVARFSSSSPFQNLEIIATLGVGGFGRVELVKVKNENVAFA
MKCIRKKHIVDTKQQEHVYSEKRILEELCSPFIVKLYRTFKDNKYVYMLLEACLGGELWS
ILRDRGSFDEPTSKFCVACVTEAFDYLHRLGIIYRDLKPENLILDAEGYLKLVDFGFAKK
IGSGQKTWTFCGTPEYVAPEVILNKGHDFSVDFWSLGILVYELLTGNPPFSGVDQMMTYN
LILKGIEKMDFPRKITRRPEDLIRRLCRQNPTERLGNLKNGINDIKKHRWLNGFNWEGLK
ARSLPSPLQRELKGPIDHSYFDKYPPEKGMPPDELSGWDKDF
|
| Enzyme 92 Number of Residues |
762 |
| Enzyme 92 Molecular Weight |
87431.5 |
| Enzyme 92 Theoretical pI |
8.67 |
| Enzyme 92 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- cGMP-dependent protein kinase activity
- catalytic activity
- cyclic nucleotide-dependent protein kinase activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 92 General Function |
Involved in protein serine/threonine kinase activity |
| Enzyme 92 Specific Function |
ATP + a protein = ADP + a phosphoprotein |
| Enzyme 92 Pathways |
Not Available |
| Enzyme 92 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 92 Pfam Domain Function |
|
| Enzyme 92 Signals |
|
| Enzyme 92 Transmembrane Regions |
|
| Enzyme 92 Essentiality |
Not Available |
| Enzyme 92 GenBank ID Protein |
1906312 |
| Enzyme 92 UniProtKB/Swiss-Prot ID |
Q13237 |
| Enzyme 92 UniProtKB/Swiss-Prot Entry Name |
KGP2_HUMAN |
| Enzyme 92 PDB ID |
Not Available |
| Enzyme 92 Cellular Location |
Not Available |
| Enzyme 92 Gene Sequence |
>2289 bp
ATGGGAAATGGTTCAGTGAAACCTAAACATTCTAAGCACCCAGATGGACACTCTGGGAAC
CTCACCACTGATGCTCTGCGGAACAAGGTGACAGAGCTGGAGAGAGAGTTGAGGAGGAAG
GATGCTGAGATCCAGGAGCGGGAGTACCATTTGAAGGAGCTGCGGGAGCATGGTTCGAAG
CAGACTGTGGCCATTGCTGAACTCACAGAGGAGCTCCAGAACAAGTGCATCCAGCTGAAC
AAGCTGCAGGATGTGGTGCATATGCAGGGAGGAAGCCCGCTTCAGGCCTCTCCAGATAAA
GTGCCTCTTGAGGTCCACCGGAAGACCTCTGGATTGGTCTCTCTCCATAGCAGGAGGGGA
GCAAAGGCTGGCGTGTCTGCTGAGCCAACAACCCGGACCTATGACCTGAACAAACCCCCT
GAATTTTCCTTTGAGAAAGCAAGAGTCAGAAAAGACTCCAGTGAGAAGAAGCTCATTACA
GATGCCCTTAATAAAAATCAGTTTCTGAAAAGACTGGATCCTCAGCAGATCAAAGACATG
GTGGAATGCATGTATGGGAGAAACTATCAGCAAGGGAGTTACATTATTAAGCAAGGAGAA
CCAGGAAACCATATCTTTGTGCTGGCAGAGGGTCGACTAGAGGTGTTCCAAGGGGAGAAA
TTGCTGTCCTCCATCCCTATGTGGACCACATTTGGGGAGCTTGCCATTTTATACAATTGT
ACAAGGACTGCCTCTGTGAAAGCTATTACCAATGTTAAAACATGGGCACTAGATCGAGAG
GTATTCCAGAATATAATGAGGAGGACAGCCCAAGCTAGAGATGAACAATACAGAAACTTC
CTCAGAAGTGTATCCTTGCTGAAGAATTTACCTGAAGATAAATTAACCAAGATCATTGAC
TGCTTGGAAGTGGAATACTATGACAAAGGAGATTACATCATTAGAGAGGGCGAGGAAGGA
AGTACCTTTTTCATTTTGGCAAAAGGAAAGGTAAAAGTAACACAGAGCACAGAAGGCCAT
GATCAACCACAGCTGATAAAAACACTGCAGAAAGGAGAATACTTTGGAGAAAAAGCTCTT
ATCAGTGATGATGTCAGGTCAGCTAACATTATTGCTGAAGAAAATGATGTTGCATGCCTG
GTTATAGATCGAGAAACATTCAACCAAACTGTCGGTACATTTGAAGAGCTGCAAAAATAC
CTTGAAGGATATGTGGCAAACCTGAACCGTGATGATGAAAAAAGACATGCGAAGCGGTCC
ATGTCTAACTGGAAGCTGTCCAAAGCACTCTCTCTGGAAATGATTCAGCTGAAGGAGAAG
GTGGCCAGATTTTCCTCATCATCCCCATTCCAGAACCTTGAGATTATTGCAACACTGGCC
GTTGGTGGGTTCGGAAGAGTTGAGCTTGTTAAAGTAAAAAATGAGAATGTTGCTTTTGCT
ATGAAGTGTATAAGGAAGAAGCACATAGTTGACACCAAGCAGCAGGAGCATGTCTACTCA
GAGAAGAGGATCCTAGAGGAGCTGTGCTCTCCATTCATTGTGAAATTATATCGTACTTTC
AAGGACAATAAGTATGTATACATGCTTCTGGAGGCCTGCTTAGGTGGGGAGCTCTGGAGT
ATATTAAGGGACAGAGGCAGCTTTGATGAACCCACCTCCAAATTCTGCGTTGCTTGTGTG
ACAGAAGCATTTGATTACCTGCATCGACTAGGTATTATCTACAGAGACTTGAAACCAGAA
AACTTAATTCTAGATGCTGAGGGTTACCTTAAATTGGTTGACTTTGGATTTGCGAAGAAA
ATAGGGTCTGGACAGAAAACATGGACATTCTGTGGGACTCCAGAATATGTAGCTCCTGAA
GTCATTCTCAACAAGGGACATGACTTCAGTGTGGATTTCTGGTCACTGGGAATTCTAGTG
TATGAGCTCCTAACGGGCAACCCACCCTTTTCTGGGGTTGACCAAATGATGACCTACAAT
TTGATTCTCAAAGGAATTGAAAAAATGGATTTTCCCAGGAAGATAACACGACGACCTGAG
GATTTGATTCGGAGGCTTTGCAGGCAAAATCCAACAGAAAGGCTGGGAAATCTGAAGAAT
GGAATAAATGACATTAAGAAACACAGGTGGTTAAATGGTTTTAATTGGGAGGGACTGAAA
GCACGGAGCCTTCCATCACCTTTGCAAAGAGAGCTCAAGGGACCCATAGATCACAGCTAC
TTTGACAAATATCCTCCTGAAAAGGGAATGCCTCCAGATGAGCTATCAGGCTGGGATAAA
GACTTCTGA
|
| Enzyme 92 GenBank Gene ID |
D70899 |
| Enzyme 92 GeneCard ID |
PRKG2 |
| Enzyme 92 GenAtlas ID |
PRKG2 |
| Enzyme 92 HGNC ID |
HGNC:9416 |
| Enzyme 92 Chromosome Location |
4 |
| Enzyme 92 Locus |
4q13.1-q21.1 |
| Enzyme 92 SNPs |
SNPJam Report |
| Enzyme 92 General References |
- Orstavik S, Solberg R, Tasken K, Nordahl M, Altherr MR, Hansson V, Jahnsen T, Sandberg M: Molecular cloning, cDNA structure, and chromosomal localization of the human type II cGMP-dependent protein kinase. Biochem Biophys Res Commun. 1996 Mar 27;220(3):759-65. [PubMed ]
- Fujii M, Ogata T, Takahashi E, Yamada K, Nakabayashi K, Oishi M, Ayusawa D: Expression of the human cGMP-dependent protein kinase II gene is lost upon introduction of SV40 T antigen or immortalization in human cells. FEBS Lett. 1995 Nov 20;375(3):263-7. [PubMed ]
- Witczak O, Orstavik S, Natarajan V, Frengen E, Jahnsen T, Sandberg M: Characterization of the gene encoding the human type II cGMP-dependent protein kinase. Biochem Biophys Res Commun. 1998 Apr 7;245(1):113-9. [PubMed ]
- Zhan X, Desiderio DM: The human pituitary nitroproteome: detection of nitrotyrosyl-proteins with two-dimensional Western blotting, and amino acid sequence determination with mass spectrometry. Biochem Biophys Res Commun. 2004 Dec 24;325(4):1180-6. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 92 Metabolite References |
Not Available |
|
Enzyme 93
[top]
|
| Enzyme 93 ID |
6426 |
| Enzyme 93 Name |
Microtubule-associated serine/threonine-protein kinase 1 |
| Enzyme 93 Synonyms |
- Syntrophin-associated serine/threonine-protein kinase
|
| Enzyme 93 Gene Name |
MAST1 |
| Enzyme 93 Protein Sequence |
>Microtubule-associated serine/threonine-protein kinase 1
MSDSLWTALSNFSMPSFPGGSMFRRTKSCRTSNRKSLILTSTSPTLPRPHSPLPGHLGSS
PLDSPRNFSPNTPAHFSFASSRRADGRRWSLASLPSSGYGTNTPSSTVSSSCSSQERLHQ
LPYQPTVDELHFLSKHFGSTESITDEDGGRRSPAVRPRSRSLSPGRSPSSYDNEIVMMNH
VYKERFPKATAQMEEKLRDFTRAYEPDSVLPLADGVLSFIHHQIIELARDCLTKSRDGLI
TTVYFYELQENLEKLLQDAYERSESLEVAFVTQLVKKLLIIISRPARLLECLEFNPEEFY
HLLEAAEGHAKEGHLVKTDIPRYIIRQLGLTRDPFPDVVHLEEQDSGGSNTPEQDDLSEG
RSSKAKKPPGENDFDTIKLISNGAYGAVYLVRHRDTRQRFAMKKINKQNLILRNQIQQAF
VERDILTFAENPFVVGMFCSFETRRHLCMVMEYVEGGDCATLLKNIGALPVEMARMYFAE
TVLALEYLHNYGIVHRDLKPDNLLITSMGHIKLTDFGLSKMGLMSLTTNLYEGHIEKDAR
EFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI
SDDILWPEGDEALPTEAQLLISSLLQTNPLVRLGAGGAFEVKQHSFFRDLDWTGLLRQKA
EFIPHLESEDDTSYFDTRSDRYHHVNSYDEDDTTEEEPVEIRQFSSCSPRFSKVYSSMEQ
LSQHEPKTPVAAAGSSKREPSTKGPEEKVAGKREGLGGLTLREKTWRGGSPEIKRFSASE
ASFLEGEASPPLGARRRFSALLEPSRFSAPQEDEDEARLRRPPRPSSDPAGSLDARAPKE
ETQGEGTSSAGDSEATDRPRPGDLCPPSKDGDASGPRATNDLVLRRARHQQMSGDVAVEK
RPSRTGGKVIKSASATALSVMIPAVDPHGSSPLASPMSPRSLSSNPSSRDSSPSRDYSPA
VSGLRSPITIQRSGKKYGFTLRAIRVYMGDTDVYSVHHIVWHVEEGGPAQEAGLCAGDLI
THVNGEPVHGMVHPEVVELILKSGNKVAVTTTPFENTSIRIGPARRSSYKAKMARRNKRP
SAKEGQESKKRSSLFRKITKQSNLLHTSRSLSSLNRSLSSSDSLPGSPTHGLPARSPTHS
YRSTPDSAYLGASSQSSSPASSTPNSPASSASHHIRPSTLHGLSPKLHRQYRSARCKSAG
NIPLSPLAHTPSPTQASPPPLPGHTVGSSHTTQSFPAKLHSSPPVVRPRPKSAEPPRSPL
LKRVQSAEKLGASLSADKKGALRKHSLEVGHPDFRKDFHGELALHSLAESDGETPPVEGL
GAPRQVAVRRLGRQESPLSLGADPLLPEGASRPPVSSKEKESPGGAEACTPPRATTPGGR
TLERDVGCTRHQSVQTEDGTGGMARAVAKAALSPVQEHETGRRSSSGEAGTPLVPIVVEP
ARPGAKAVVPQPLGADSKGLQEPAPLAPSVPEAPRGRERWVLEVVEERTTLSGPRSKPAS
PKLSPEPQTPSLAPAKCSAPSSAVTPVPPASLLGSGTKPQVGLTSRCPAEAVPPAGLTKK
GVSSPAPPGP
|
| Enzyme 93 Number of Residues |
1570 |
| Enzyme 93 Molecular Weight |
170675.2 |
| Enzyme 93 Theoretical pI |
8.60 |
| Enzyme 93 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- ion binding
- kinase activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- protein binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 93 General Function |
Involved in protein serine/threonine kinase activity |
| Enzyme 93 Specific Function |
Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins |
| Enzyme 93 Pathways |
Not Available |
| Enzyme 93 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 93 Pfam Domain Function |
|
| Enzyme 93 Signals |
|
| Enzyme 93 Transmembrane Regions |
|
| Enzyme 93 Essentiality |
Not Available |
| Enzyme 93 GenBank ID Protein |
45120119 |
| Enzyme 93 UniProtKB/Swiss-Prot ID |
Q9Y2H9 |
| Enzyme 93 UniProtKB/Swiss-Prot Entry Name |
MAST1_HUMAN |
| Enzyme 93 PDB ID |
Not Available |
| Enzyme 93 Cellular Location |
Not Available |
| Enzyme 93 Gene Sequence |
>4713 bp
ATGTCTGACTCTCTCTGGACCGCGCTTTCTAATTTCTCGATGCCCTCCTTCCCCGGCGGC
AGTATGTTCCGCCGCACCAAGAGCTGCCGCACCAGTAATCGGAAAAGCCTCATCCTGACC
AGCACTTCACCCACGCTACCGAGACCCCACTCCCCGCTGCCAGGTCACCTAGGCAGCAGT
CCCCTGGACAGCCCCCGAAACTTCTCCCCCAACACCCCCGCCCACTTCTCGTTTGCCTCC
TCCCGAAGGGCGGACGGACGCCGGTGGTCTCTGGCCTCGCTCCCTTCATCTGGCTATGGC
ACCAACACGCCCAGTTCCACCGTCTCGTCCTCCTGCTCCTCCCAGGAGCGCCTTCACCAG
CTGCCCTACCAGCCCACGGTGGACGAGCTCCACTTCCTCTCCAAACACTTCGGGAGCACC
GAGAGCATCACAGACGAGGATGGTGGCCGTCGCTCCCCAGCCGTGCGGCCCCGCTCACGG
AGCCTCAGCCCCGGGCGCTCCCCCTCCTCCTACGACAACGAGATCGTGATGATGAATCAC
GTCTACAAGGAGAGGTTCCCGAAGGCCACTGCGCAGATGGAGGAGAAGCTGCGCGACTTT
ACCCGCGCCTACGAACCCGACAGCGTTCTGCCTCTGGCCGATGGCGTGCTCAGCTTCATC
CACCACCAGATCATCGAGCTGGCCCGGGACTGCCTGACCAAGTCCCGTGACGGCCTCATC
ACCACGGTCTACTTCTATGAATTGCAGGAGAACCTGGAGAAGCTCCTTCAAGACGCCTAT
GAACGCTCTGAGAGCTTGGAGGTGGCCTTCGTTACTCAGCTGGTGAAGAAGTTGCTTATT
ATCATCTCACGCCCTGCGAGGCTGCTGGAGTGCCTGGAATTCAACCCCGAGGAGTTCTAC
CACCTGCTGGAGGCGGCCGAAGGACACGCCAAGGAGGGCCACCTTGTGAAGACGGACATC
CCCCGCTACATCATCCGCCAGCTGGGCCTCACCCGTGACCCCTTTCCAGATGTGGTGCAT
CTGGAGGAACAGGACAGTGGTGGTTCCAACACCCCTGAGCAAGACGATCTCTCTGAGGGC
CGCAGCAGCAAGGCCAAGAAACCGCCGGGGGAGAATGACTTCGATACCATCAAGCTCATA
AGCAACGGTGCCTACGGCGCTGTCTACCTGGTGCGGCACCGCGACACGCGGCAGCGCTTT
GCCATGAAAAAGATCAACAAGCAGAACTTGATCCTCCGCAACCAGATCCAGCAGGCCTTT
GTGGAGCGCGATATCCTCACCTTCGCCGAGAACCCGTTTGTGGTCGGCATGTTCTGCTCC
TTTGAGACTCGGCGCCACCTCTGCATGGTCATGGAATATGTGGAAGGCGGCGACTGTGCC
ACCCTGCTGAAGAATATTGGAGCGCTGCCCGTAGAGATGGCCCGCATGTACTTTGCTGAG
ACGGTGCTAGCCCTGGAGTATTTGCACAACTATGGCATCGTGCACCGCGACCTCAAGCCT
GACAACCTCCTTATCACCTCCATGGGTCACATCAAGCTCACAGATTTCGGCCTCTCCAAG
ATGGGGCTCATGAGCCTCACCACCAACTTATATGAAGGCCACATCGAGAAGGACGCCCGA
GAGTTCCTGGACAAACAGGTGTGTGGGACCCCAGAGTACATCGCGCCCGAGGTCATCCTG
CGTCAAGGCTACGGCAAGCCAGTGGACTGGTGGGCTATGGGGATCATCCTCTACGAGTTC
CTGGTGGGCTGTGTGCCCTTCTTCGGAGACACACCAGAGGAGCTATTTGGACAGGTCATC
AGTGATGACATCCTGTGGCCCGAGGGGGATGAGGCCCTACCTACGGAGGCCCAACTCCTC
ATATCCAGCCTCCTGCAGACCAACCCTCTGGTCAGGCTTGGGGCAGGCGGCGCTTTTGAG
GTGAAGCAGCACAGTTTCTTTCGAGACCTGGACTGGACAGGGCTGCTGAGGCAGAAGGCC
GAGTTCATCCCCCACCTAGAGTCGGAAGATGACACTAGCTACTTTGACACCCGCTCAGAC
AGGTATCACCACGTGAACTCCTATGACGAGGATGACACGACGGAGGAGGAGCCCGTGGAA
ATCCGCCAGTTCTCTTCCTGCTCTCCGCGCTTCAGCAAGGTGTATAGCAGCATGGAGCAG
CTGTCGCAGCACGAGCCCAAGACCCCAGTAGCAGCTGCAGGGAGCAGCAAGCGGGAGCCG
AGCACCAAGGGCCCCGAGGAGAAGGTGGCCGGCAAGCGGGAGGGGCTGGGCGGCCTGACC
CTGCGTGAGAAGACCTGGAGAGGGGGCTCTCCGGAGATCAAGCGATTCTCCGCGTCCGAG
GCCAGTTTCCTGGAGGGAGAGGCCAGTCCCCCTTTGGGCGCCCGCCGCCGTTTCTCGGCG
CTGCTGGAGCCCAGCCGCTTCAGCGCCCCCCAAGAGGACGAGGATGAGGCCCGGCTGCGC
AGGCCTCCCCGGCCCAGCTCCGACCCCGCGGGATCCCTGGATGCACGGGCCCCCAAAGAG
GAGACTCAAGGGGAAGGCACCTCCAGCGCCGGGGACTCCGAGGCCACTGACCGTCCACGC
CCAGGTGACCTCTGCCCACCCTCGAAGGATGGGGATGCATCAGGCCCAAGGGCTACCAAT
GACTTGGTTCTGCGCCGGGCGCGGCACCAGCAGATGTCAGGGGATGTGGCAGTAGAGAAG
AGGCCTTCTCGAACTGGGGGCAAAGTCATCAAATCAGCCTCAGCCACTGCCTTATCTGTC
ATGATTCCTGCAGTGGACCCACATGGAAGTTCACCCCTTGCTAGTCCCATGTCTCCACGA
TCTCTGTCCTCCAACCCATCCTCACGGGACTCCTCACCCAGCCGGGACTACTCACCAGCT
GTCAGTGGGCTCCGCTCCCCCATCACCATCCAGCGCTCGGGCAAGAAGTATGGCTTCACA
CTGCGTGCCATCCGTGTCTACATGGGTGACACGGATGTCTATAGTGTCCACCACATTGTC
TGGCATGTGGAGGAAGGAGGCCCAGCCCAGGAGGCAGGACTCTGTGCTGGGGACCTCATC
ACCCACGTGAATGGGGAGCCTGTGCATGGCATGGTGCATCCTGAGGTCGTGGAGCTGATC
CTTAAGAGTGGCAACAAGGTAGCAGTGACCACAACGCCCTTCGAAAATACCTCTATCCGC
ATTGGTCCCGCAAGGCGCAGCAGCTACAAGGCTAAAATGGCTCGGAGGAACAAGCGACCC
TCCGCCAAGGAGGGCCAGGAGAGCAAGAAGCGCAGCTCCCTCTTCCGGAAGATCACGAAG
CAGTCGAACCTGCTGCATACTAGCCGCTCGCTGTCGTCGCTGAACCGCTCGCTGTCATCC
AGCGATAGTCTCCCGGGCTCGCCTACGCACGGGCTGCCGGCGCGCTCGCCCACGCACAGC
TACCGCTCCACGCCTGACTCCGCCTACCTAGGCGCCTCATCCCAGAGCAGCTCCCCAGCC
TCGAGCACGCCCAACTCGCCTGCGTCGTCGGCGTCGCACCACATTCGGCCCAGCACGCTG
CACGGACTGTCGCCAAAGCTCCATCGCCAGTACCGCTCTGCGCGATGCAAGTCGGCCGGC
AACATCCCTCTATCGCCGCTGGCACACACGCCGTCCCCCACGCAGGCGTCACCGCCGCCA
CTGCCGGGCCACACGGTGGGCAGCTCGCACACTACTCAGAGCTTCCCGGCCAAACTGCAC
TCATCGCCTCCCGTCGTGCGCCCGCGCCCCAAGAGTGCCGAGCCCCCTCGCTCGCCGCTC
CTCAAGCGCGTGCAGTCGGCCGAGAAGCTGGGAGCCTCTTTGAGTGCGGACAAGAAGGGC
GCGCTGCGCAAACACAGCCTCGAGGTGGGCCACCCGGATTTCCGCAAGGACTTCCATGGC
GAGCTGGCGCTGCATAGCCTTGCCGAGTCCGACGGTGAGACGCCCCCAGTCGAGGGCCTT
GGCGCGCCCCGGCAGGTCGCCGTCCGCCGCCTGGGCCGACAGGAGTCACCTTTGAGCCTG
GGCGCGGACCCGTTGCTGCCCGAGGGTGCCTCCAGGCCACCAGTGTCGAGCAAGGAGAAG
GAATCCCCGGGGGGCGCCGAGGCGTGCACCCCACCCCGCGCGACGACCCCCGGTGGCCGG
ACCCTGGAGCGGGACGTCGGCTGCACGCGGCATCAGAGCGTGCAGACGGAGGATGGCACT
GGCGGGATGGCCAGGGCTGTGGCCAAGGCGGCGCTGAGCCCGGTGCAGGAACACGAGACA
GGCCGGCGCAGCAGCTCTGGCGAGGCGGGCACACCCCTGGTACCCATTGTCGTAGAGCCT
GCGCGGCCCGGGGCTAAGGCTGTGGTGCCTCAGCCTCTGGGCGCGGACTCCAAGGGGTTG
CAGGAACCCGCACCCCTGGCGCCTTCCGTGCCCGAGGCCCCCCGGGGCCGGGAGCGCTGG
GTGTTGGAGGTGGTGGAGGAGCGCACCACGCTGAGCGGTCCTCGCTCCAAGCCCGCCTCC
CCAAAGCTCTCCCCGGAGCCCCAGACACCCTCCCTAGCCCCAGCGAAGTGCAGTGCACCC
AGCAGTGCAGTGACCCCAGTCCCACCCGCATCCCTCTTGGGCTCAGGCACCAAGCCTCAA
GTGGGGCTGACCTCCCGGTGCCCTGCTGAAGCTGTGCCCCCAGCAGGCCTGACCAAAAAA
GGAGTGTCCAGTCCCGCACCCCCGGGACCATAG
|
| Enzyme 93 GenBank Gene ID |
NM_014975.2 |
| Enzyme 93 GeneCard ID |
MAST1 |
| Enzyme 93 GenAtlas ID |
MAST1 |
| Enzyme 93 HGNC ID |
HGNC:19034 |
| Enzyme 93 Chromosome Location |
1 |
| Enzyme 93 Locus |
19p13.2 |
| Enzyme 93 SNPs |
SNPJam Report |
| Enzyme 93 General References |
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed ]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 93 Metabolite References |
Not Available |
|
Enzyme 94
[top]
|
| Enzyme 94 ID |
6427 |
| Enzyme 94 Name |
Probable phospholipid-transporting ATPase IG |
| Enzyme 94 Synonyms |
- ATPase IQ
- ATPase class VI type 11C
|
| Enzyme 94 Gene Name |
ATP11C |
| Enzyme 94 Protein Sequence |
>Probable phospholipid-transporting ATPase IG
MQMVPSLPPASECAGEEKRVGTRTVFVGNHPVSETEAYIAQRFCDNRIVSSKYTLWNFLP
KNLFEQFRRIANFYFLIIFLVQVTVDTPTSPVTSGLPLFFVITVTAIKQGYEDCLRHRAD
NEVNKSTVYIIENAKRVRKESEKIKVGDVVEVQADETFPCDLILLSSCTTDGTCYVTTAS
LDGESNCKTHYAVRDTIALCTAESIDTLRAAIECEQPQPDLYKFVGRINIYSNSLEAVAR
SLGPENLLLKGATLKNTEKIYGVAVYTGMETKMALNYQGKSQKRSAVEKSINAFLIVYLF
ILLTKAAVCTTLKYVWQSTPYNDEPWYNQKTQKERETLKVLKMFTDFLSFMVLFNFIIPV
SMYVTVEMQKFLGSFFISWDKDFYDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTEN
SMEFIECCIDGHKYKGVTQEVDGLSQTDGTLTYFDKVDKNREELFLRALCLCHTVEIKTN
DAVDGATESAELTYISSSPDEIALVKGAKRYGFTFLGNRNGYMRVENQRKEIEEYELLHT
LNFDAVRRRMSVIVKTQEGDILLFCKGADSAVFPRVQNHEIELTKVHVERNAMDGYRTLC
VAFKEIAPDDYERINRQLIEAKMALQDREEKMEKVFDDIETNMNLIGATAVEDKLQDQAA
ETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHE
LLIEYRKKLLHEFPKSTRSFKKAWTEHQEYGLIIDGSTLSLILNSSQDSSSNNYKSIFLQ
ICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKE
GRQAARNSDYSVPKFKHLKKLLLAHGHLYYVRIAHLVQYFFYKNLCFILPQFLYQFFCGF
SQQPLYDAAYLTMYNICFTSLPILAYSLLEQHINIDTLTSDPRLYMKISGNAMLQLGPFL
YWTFLAAFEGTVFFFGTYFLFQTASLEENGKVYGNWTFGTIVFTVLVFTVTLKLALDTRF
WTWINHFVIWGSLAFYVFFSFFWGGIIWPFLKQQRMYFVFAQMLSSVSTWLAIILLIFIS
LFPEILLIVLKNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNVL
|
| Enzyme 94 Number of Residues |
1132 |
| Enzyme 94 Molecular Weight |
129476.0 |
| Enzyme 94 Theoretical pI |
6.63 |
| Enzyme 94 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 94 General Function |
Involved in ATP binding |
| Enzyme 94 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 94 Pathways |
Not Available |
| Enzyme 94 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 94 Pfam Domain Function |
|
| Enzyme 94 Signals |
|
| Enzyme 94 Transmembrane Regions |
- 67-85
87-107
291-311
347-367
880-900
909-929
956-976
996-1016
1027-1047
1070-1090
|
| Enzyme 94 Essentiality |
Not Available |
| Enzyme 94 GenBank ID Protein |
39573513 |
| Enzyme 94 UniProtKB/Swiss-Prot ID |
Q8NB49 |
| Enzyme 94 UniProtKB/Swiss-Prot Entry Name |
AT11C_HUMAN |
| Enzyme 94 PDB ID |
Not Available |
| Enzyme 94 Cellular Location |
Not Available |
| Enzyme 94 Gene Sequence |
>3399 bp
ATGCAGATGGTCCCATCTCTCCCTCCAGCCTCTGAGTGTGCTGGAGAAGAGAAACGAGTT
GGCACACGCACAGTGTTTGTTGGCAATCATCCAGTTTCGGAAACAGAAGCTTACATTGCA
CAAAGATTTTGTGATAATAGAATAGTCTCATCTAAGTATACACTTTGGAATTTTCTCCCA
AAGAATCTGTTTGAACAGTTTAGAAGAATTGCAAATTTTTATTTTCTCATAATCTTCCTT
GTACAGGTCACAGTAGACACACCAACTAGCCCAGTTACCAGTGGACTTCCACTTTTCTTT
GTTATAACTGTTACAGCCATCAAGCAGGGATATGAGGATTGGCTGAGACACAGAGCTGAC
AATGAAGTCAACAAAAGCACTGTTTACATTATTGAAAATGCAAAGCGAGTGAGAAAAGAA
AGTGAAAAAATCAAGGTTGGTGATGTAGTAGAAGTACAGGCAGATGAAACCTTTCCCTGT
GATCTTATTCTTCTATCATCTTGCACCACTGATGGAACCTGTTATGTCACTACAGCCAGT
CTTGATGGGGAATCCAATTGCAAGACACATTATGCAGTACGTGATACCATTGCACTGTGT
ACAGCAGAATCCATCGATACCCTCCGAGCAGCAATTGAATGTGAACAGCCTCAACCTGAC
CTCTACAAATTTGTTGGGCGAATCAATATCTACAGTAATAGTCTTGAGGCTGTTGCCAGG
TCTTTGGGACCTGAAAATCTCTTGCTGAAAGGAGCTACGCTAAAAAATACCGAGAAGATA
TATGGAGTTGCTGTTTACACTGGAATGGAAACCAAAATGGCTTTGAACTACCAAGGGAAA
TCTCAGAAACGTTCTGCTGTTGAAAAATCTATTAATGCTTTCCTGATTGTATATTTATTT
ATCTTACTGACCAAAGCTGCAGTATGCACTACTCTAAAGTATGTTTGGCAAAGTACCCCA
TACAATGATGAACCTTGGTATAACCAAAAGACTCAGAAAGAGCGAGAGACCTTGAAGGTT
TTAAAAATGTTCACCGACTTCCTATCATTTATGGTTCTATTCAACTTTATCATTCCTGTC
TCCATGTACGTCACAGTAGAAATGCAGAAATTCTTGGGCTCCTTCTTCATCTCATGGGAT
AAGGACTTTTATGATGAAGAAATTAATGAAGGAGCCCTGGTTAACACATCAGACCTTAAT
GAAGAACTTGGTCAGGTGGATTATGTATTTACAGATAAGACTGGAACACTCACTGAAAAC
AGCATGGAATTCATTGAATGCTGCATAGATGGCCACAAATATAAAGGTGTAACTCAAGAG
GTTGATGGATTATCTCAAACTGATGGAACTTTAACATATTTTGACAAAGTAGATAAGAAT
CGAGAAGAGCTGTTTCTACGTGCCTTGTGTTTATGTCATACTGTAGAAATCAAAACAAAC
GATGCTGTTGATGGAGCTACAGAATCAGCTGAATTAACCTATATCTCCTCTTCACCAGAT
GAAATAGCTTTGGTGAAAGGAGCTAAAAGGTACGGGTTCACATTTTTAGGAAATCGAAAT
GGATATATGAGAGTAGAGAACCAAAGAAAAGAAATAGAAGAATATGAACTTCTTCACACC
TTAAACTTTGATGCTGTCCGGCGACGTATGAGTGTAATTGTGAAGACTCAAGAAGGAGAC
ATACTTCTCTTTTGTAAAGGAGCAGACTCGGCAGTTTTTCCCAGAGTGCAAAATCATGAA
ATTGAGTTAACTAAAGTCCATGTGGAACGTAATGCAATGGATGGGTATCGGACACTCTGT
GTAGCCTTCAAAGAAATTGCTCCAGATGATTATGAAAGAATTAACAGACAGCTCATAGAG
GCAAAAATGGCCTTACAAGACAGAGAAGAAAAAATGGAAAAAGTTTTCGATGATATTGAG
ACAAACATGAATTTAATTGGAGCCACTGCAGTTGAAGACAAGCTACAAGATCAAGCTGCA
GAGACCATTGAAGCTCTGCATGCAGCAGGCCTGAAAGTCTGGGTGCTCACTGGGGACAAG
ATGGAGACAGCTAAATCCACATGCTATGCCTGCCGCCTTTTCCAGACCAACACTGAGCTC
TTAGAACTAACCACAAAAACCATTGAAGAAAGTGAAAGGAAAGAAGATCGATTACATGAA
TTATTGATAGAATATCGCAAGAAATTGCTGCATGAGTTTCCTAAAAGTACTAGAAGCTTT
AAAAAAGCATGGACAGAACATCAGGAATATGGATTAATCATAGATGGCTCCACATTGTCA
CTCATACTAAATTCTAGTCAAGACTCTAGTTCAAACAATTACAAAAGCATTTTCCTACAA
ATATGTATGAAGTGTACTGCAGTGCTCTGCTGTCGGATGGCACCATTACAGAAAGCCCAG
ATTGTCAGAATGGTGAAGAATTTAAAAGGCAGCCCAATAACTCTGTCGATAGGTGATGGT
GCCAATGATGTTAGTATGATCTTGGAATCCCATGTGGGAATAGGTATTAAAGGCAAAGAA
GGTCGCCAAGCAGCTAGGAATAGCGATTATTCTGTTCCAAAGTTTAAACACTTAAAGAAA
CTGCTGTTGGCTCATGGACATCTATATTATGTGAGAATAGCACACCTTGTACAGTACTTC
TTCTATAAGAACCTTTGTTTCATTTTGCCACAGTTTTTGTACCAGTTCTTCTGTGGATTC
TCACAACAGCCACTGTATGATGCTGCTTACCTTACAATGTACAATATCTGCTTCACATCC
TTGCCCATCCTGGCCTATAGTCTACTGGAACAGCACATCAACATTGACACTCTGACCTCA
GATCCCCGATTGTATATGAAAATTTCTGGCAATGCCATGCTACAGTTGGGCCCCTTCTTA
TATTGGACATTTCTGGCTGCCTTTGAAGGGACAGTGTTCTTCTTTGGGACTTACTTTCTT
TTTCAGACTGCATCCCTAGAAGAAAATGGAAAGGTATACGGAAACTGGACTTTTGGAACC
ATTGTTTTTACAGTCTTAGTATTCACTGTAACCCTGAAGCTTGCCTTGGATACCCGATTC
TGGACGTGGATAAATCACTTTGTGATTTGGGGTTCTTTAGCCTTCTATGTATTTTTCTCA
TTCTTCTGGGGAGGAATTATTTGGCCTTTTCTCAAGCAACAGAGAATGTATTTTGTATTT
GCCCAAATGCTGTCTTCTGTATCCACATGGTTGGCTATAATTCTTCTAATATTTATCAGC
CTGTTCCCTGAGATTCTTCTGATAGTATTAAAGAATGTAAGAAGAAGAAGTGCCAGGAGA
AATCTGAGCTGTAGAAGGGCATCTGACTCATTATCCGCCAGACCTTCAGTCAGACCTCTT
CTTTTACGAACATTCTCAGACGAATCTAATGTATTGTAA
|
| Enzyme 94 GenBank Gene ID |
AJ580093 |
| Enzyme 94 GeneCard ID |
ATP11C |
| Enzyme 94 GenAtlas ID |
ATP11C |
| Enzyme 94 HGNC ID |
HGNC:13554 |
| Enzyme 94 Chromosome Location |
Not Available |
| Enzyme 94 Locus |
Not Available |
| Enzyme 94 SNPs |
SNPJam Report |
| Enzyme 94 General References |
- Andrew Nesbit M, Bowl MR, Harding B, Schlessinger D, Whyte MP, Thakker RV: X-linked hypoparathyroidism region on Xq27 is evolutionarily conserved with regions on 3q26 and 13q34 and contains a novel P-type ATPase. Genomics. 2004 Dec;84(6):1060-70. [PubMed ]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed ]
- 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 ]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed ]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- 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 ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 94 Metabolite References |
Not Available |
|
Enzyme 95
[top]
|
| Enzyme 95 ID |
6428 |
| Enzyme 95 Name |
Probable phospholipid-transporting ATPase IH |
| Enzyme 95 Synonyms |
- ATPase IS
- ATPase class VI type 11A
|
| Enzyme 95 Gene Name |
ATP11A |
| Enzyme 95 Protein Sequence |
>Probable phospholipid-transporting ATPase IH
MDCSLVRTLVHRYCAGEENWVDSRTIYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNF
IPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHK
ADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTT
ASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPV
VRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVY
LCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYII
PVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLT
ENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHT
VQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNREN
HIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVER
NAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATA
VEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEE
QSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNY
RELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGI
GVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLY
QFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALL
RWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKL
ALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIV
LLVTISLLPDVLKKVLCRQLWPTATERVQTKSQCLSVEQSTIFMLSQTSSSLSF
|
| Enzyme 95 Number of Residues |
1134 |
| Enzyme 95 Molecular Weight |
129754.6 |
| Enzyme 95 Theoretical pI |
6.58 |
| Enzyme 95 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 95 General Function |
Involved in ATP binding |
| Enzyme 95 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 95 Pathways |
Not Available |
| Enzyme 95 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 95 Pfam Domain Function |
|
| Enzyme 95 Signals |
|
| Enzyme 95 Transmembrane Regions |
- 62-82
89-110
297-318
350-372
882-902
915-934
965-986
1001-1023
1030-1050
1069-1093
|
| Enzyme 95 Essentiality |
Not Available |
| Enzyme 95 GenBank ID Protein |
150421684 |
| Enzyme 95 UniProtKB/Swiss-Prot ID |
P98196 |
| Enzyme 95 UniProtKB/Swiss-Prot Entry Name |
AT11A_HUMAN |
| Enzyme 95 PDB ID |
Not Available |
| Enzyme 95 Cellular Location |
Not Available |
| Enzyme 95 Gene Sequence |
>3405 bp
ATGGACTGCAGCCTCGTGCGGACGCTCGTGCACAGATACTGTGCAGGAGAAGAGAATTGG
GTGGACAGCAGGACCATCTACGTGGGACACAGGGAGCCACCTCCGGGCGCAGAGGCCTAC
ATCCCACAGAGATACCCAGACAACAGGATCGTCTCGTCCAAGTACACATTTTGGAACTTT
ATACCCAAGAATTTATTTGAACAATTCAGAAGAGTAGCCAACTTTTATTTCCTTATCATA
TTTCTGGTGCAGTTGATTATTGATACACCCACAAGTCCAGTGACAAGCGGACTTCCACTC
TTCTTTGTCATTACTGTGACGGCTATCAAACAGGGTTATGAAGACTGGCTTCGACATAAA
GCAGACAATGCCATGAACCAGTGTCCTGTTCATTTCATTCAGCACGGCAAGCTCGTTCGG
AAACAAAGTCGAAAGCTGCGAGTTGGGGACATTGTCATGGTTAAGGAGGACGAGACCTTT
CCCTGCGACTTGATCTTCCTTTCCAGCAACCGGGGAGATGGGACGTGCCACGTCACCACC
GCCAGCTTGGATGGAGAATCCAGCCATAAAACGCATTACGCGGTCCAGGACACCAAAGGC
TTCCACACAGAGGAGGATATCGGCGGACTTCACGCCACCATCGAGTGTGAGCAGCCCCAG
CCCGACCTCTACAAGTTCGTGGGTCGCATCAACGTTTACAGTGACCTGAATGACCCCGTG
GTGAGGCCCTTAGGATCGGAAAACCTGCTGCTTAGAGGAGCTACACTGAAGAACACTGAG
AAAATCTTTGGTGTGGCTATTTACACGGGAATGGAAACCAAGATGGCATTAAATTATCAA
TCAAAATCTCAGAAGCGATCTGCCGTGGAAAAATCGATGAATGCGTTCCTCATTGTGTAT
CTCTGCATTCTGATCAGCAAAGCCCTGATAAACACTGTGCTGAAATACATGTGGCAGAGT
GAGCCCTTTCGGGATGAGCCGTGGTATAATCAGAAAACGGAGTCGGAAAGGCAGAGGAAT
CTGTTCCTCAAGGCATTCACGGACTTCCTGGCCTTCATGGTCCTCTTTAACTACATCATC
CCTGTGTCCATGTACGTCACGGTCGAGATGCAGAAGTTCCTCGGCTCTTACTTCATCACC
TGGGACGAAGACATGTTTGACGAGGAGACTGGCGAGGGGCCTCTGGTGAACACGTCGGAC
CTCAATGAAGAGCTGGGACAGGTGGAGTACATCTTCACAGACAAGACCGGCACCCTCACG
GAAAACAACATGGAGTTCAAGGAGTGCTGCATCGAAGGCCATGTCTACGTGCCCCACGTC
ATCTGCAACGGGCAGGTCCTCCCAGAGTCGTCAGGAATCGACATGATTGACTCGTCCCCC
AGCGTCAACGGGAGGGAGCGCGAGGAGCTGTTTTTCCGGGCCCTCTGTCTCTGCCACACC
GTCCAGGTGAAAGACGATGACAGCGTAGACGGCCCCAGGAAATCGCCGGACGGGGGGAAA
TCCTGTGTGTACATCTCATCCTCGCCCGACGAGGTGGCGCTGGTCGAAGGTGTCCAGAGA
CTTGGCTTTACCTACCTAAGGCTGAAGGACAATTACATGGAGATATTAAACAGGGAGAAC
CACATCGAAAGGTTTGAATTGCTGGAAATTTTGAGTTTTGACTCAGTCAGAAGGAGAATG
AGTGTAATTGTAAAATCTGCTACAGGAGAAATTTATCTGTTTTGCAAAGGAGCAGATTCT
TCGATATTCCCCCGAGTGATAGAAGGCAAAGTTGACCAGATCCGAGCCAGAGTGGAGCGT
AACGCAGTGGAGGGGCTCCGAACTTTGTGTGTTGCTTATAAAAGGCTGATCCAAGAAGAA
TATGAAGGCATTTGTAAGCTGCTGCAGGCTGCCAAAGTGGCCCTTCAAGATCGAGAGAAA
AAGTTAGCAGAAGCCTATGAGCAAATAGAGAAAGATCTTACTCTGCTTGGTGCTACAGCT
GTTGAGGACCGGCTGCAGGAGAAAGCTGCAGACACCATCGAGGCCCTGCAGAAGGCCGGG
ATCAAAGTCTGGGTTCTCACGGGAGACAAGATGGAGACGGCCGCGGCCACGTGCTACGCC
TGCAAGCTCTTCCGCAGGAACACGCAGCTGCTGGAGCTGACCACCAAGAGGATCGAGGAG
CAGAGCCTGCACGACGTCCTGTTCGAGCTGAGCAAGACGGTCCTGCGCCACAGCGGGAGC
CTGACCAGAGACAACCTGTCCGGACTTTCAGCAGATATGCAGGACTACGGTTTAATTATC
GACGGAGCTGCACTGTCTCTGATAATGAAGCCTCGAGAAGACGGGAGTTCCGGCAACTAC
AGGGAGCTCTTCCTGGAAATCTGCCGGAGCTGCAGCGCGGTGCTCTGCTGCCGCATGGCG
CCCTTGCAGAAGGCTCAGATTGTTAAATTAATCAAATTTTCAAAAGAGCACCCAATCACG
TTAGCAATTGGCGATGGTGCAAATGATGTCAGCATGATTCTGGAAGCGCACGTGGGCATA
GGTGTCATCGGCAAGGAAGGCCGCCAGGCTGCCAGGAACAGCGACTATGCAATCCCAAAG
TTTAAGCATTTGAAGAAGATGCTGCTTGTTCACGGGCATTTTTATTACATTAGGATCTCT
GAGCTCGTGCAGTACTTCTTCTATAAGAACGTCTGCTTCATCTTCCCTCAGTTTTTATAC
CAGTTCTTCTGTGGGTTTTCACAACAGACTTTGTACGACACCGCGTATCTGACCCTCTAC
AACATCAGCTTCACCTCCCTCCCCATCCTCCTGTACAGCCTCATGGAGCAGCATGTTGGC
ATTGACGTGCTCAAGAGAGACCCGACCCTGTACAGGGACGTCGCCAAGAATGCCCTGCTG
CGCTGGCGCGTGTTCATCTACTGGACGCTCCTGGGACTGTTTGACGCACTGGTGTTCTTC
TTTGGTGCTTATTTCGTGTTTGAAAATACAACTGTGACAAGCAACGGGCAGATATTTGGA
AACTGGACGTTTGGAACGCTGGTATTCACCGTGATGGTGTTCACAGTTACACTAAAGCTT
GCATTGGACACACACTACTGGACTTGGATCAACCATTTTGTCATCTGGGGGTCGCTGCTG
TTCTACGTTGTCTTTTCGCTTCTCTGGGGAGGAGTGATCTGGCCGTTCCTCAACTACCAG
AGGATGTACTACGTGTTCATCCAGATGCTGTCCAGCGGGCCCGCCTGGCTGGCCATCGTG
CTGCTGGTGACCATCAGCCTCCTTCCCGACGTCCTCAAGAAAGTCCTGTGCCGGCAGCTG
TGGCCAACAGCAACAGAGAGAGTCCAGACTAAGAGCCAGTGCCTTTCTGTCGAGCAGTCA
ACCATCTTTATGCTTTCTCAGACTTCCAGCAGCCTGAGTTTCTGA
|
| Enzyme 95 GenBank Gene ID |
NM_015205.2 |
| Enzyme 95 GeneCard ID |
ATP11A |
| Enzyme 95 GenAtlas ID |
ATP11A |
| Enzyme 95 HGNC ID |
HGNC:13552 |
| Enzyme 95 Chromosome Location |
1 |
| Enzyme 95 Locus |
13q34 |
| Enzyme 95 SNPs |
SNPJam Report |
| Enzyme 95 General References |
- Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed ]
- Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed ]
|
| Enzyme 95 Metabolite References |
Not Available |
|
Enzyme 96
[top]
|
| Enzyme 96 ID |
6429 |
| Enzyme 96 Name |
Serine/threonine-protein kinase RIO2 |
| Enzyme 96 Synonyms |
- RIO kinase 2
|
| Enzyme 96 Gene Name |
RIOK2 |
| Enzyme 96 Protein Sequence |
>Serine/threonine-protein kinase RIO2
MGKVNVAKLRYMSRDDFRVLTAVEMGMKNHEIVPGSLIASIASLKHGGCNKVLRELVKHK
LIAWERTKTVQGYRLTNAGYDYLALKTLSSRQVVESVGNQMGVGKESDIYIVANEEGQQF
ALKLHRLGRTSFRNLKNKRDYHKHRHNVSWLYLSRLSAMKEFAYMKALYERKFPVPKPID
YNRHAVVMELINGYPLCQIHHVEDPASVYDEAMELIVKLANHGLIHGDFNEFNLILDESD
HITMIDFPQMVSTSHPNAEWYFDRDVKCIKDFFMKRFSYESELFPTFKDIRREDTLDVEV
SASGYTKEMQADDELLHPLGPDDKNIETKEGSEFSFSDGEVAEKAEVYGSENESERNCLE
ESEGCYCRSSGDPEQIKEDSLSEESADARSFEMTEFNQALEEIKGQVVENNSVTEFSEEK
NRTENYNRQDGQRVQGGVPAGSDEYEDECPHLIALSSLNREFRPFRDEENVGAMNQYRTR
TLSITSSGSAVSCSTIPPELVKQKVKRQLTKQQKSAVRRRLQKGEANIFTKQRRENMQNI
KSSLEAASFWGE
|
| Enzyme 96 Number of Residues |
552 |
| Enzyme 96 Molecular Weight |
63282.6 |
| Enzyme 96 Theoretical pI |
5.78 |
| Enzyme 96 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 96 General Function |
Involved in catalytic activity |
| Enzyme 96 Specific Function |
ATP + a protein = ADP + a phosphoprotein |
| Enzyme 96 Pathways |
Not Available |
| Enzyme 96 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 96 Pfam Domain Function |
|
| Enzyme 96 Signals |
|
| Enzyme 96 Transmembrane Regions |
|
| Enzyme 96 Essentiality |
Not Available |
| Enzyme 96 GenBank ID Protein |
7023651 |
| Enzyme 96 UniProtKB/Swiss-Prot ID |
Q9BVS4 |
| Enzyme 96 UniProtKB/Swiss-Prot Entry Name |
RIOK2_HUMAN |
| Enzyme 96 PDB ID |
Not Available |
| Enzyme 96 Cellular Location |
Not Available |
| Enzyme 96 Gene Sequence |
>1659 bp
ATGGGGAAAGTGAATGTGGCCAAGTTGCGTTACATGAGCCGAGATGACTTCAGGGTCTTG
ACCGCGGTTGAAATGGGCATGAAGAACCATGAAATTGTTCCCGGCAGTTTGATTGCTTCT
ATAGCCAGCCTTAAACATGGTGGCTGTAATAAAGTTTTAAGAGAATTAGTGAAACATAAA
CTCATAGCTTGGGAGCGTACCAAAACTGTCCAGGGCTATCGGTTGACAAATGCAGGATAT
GATTACCTAGCTTTGAAAACACTTTCTTCTAGGCAAGTAGTTGAGTCTGTTGGAAACCAG
ATGGGTGTTGGCAAAGAATCAGATATTTACATTGTTGCAAATGAAGAAGGACAACAATTT
GCATTAAAGCTTCACAGACTAGGAAGAACCTCGTTTCGAAATTTGAAAAACAAACGCGAT
TATCATAAACATAGGCACAATGTGTCTTGGCTTTATTTATCTCGTCTCTCTGCCATGAAG
GAATTTGCCTATATGAAGGCATTGTATGAGAGGAAATTTCCAGTTCCAAAGCCAATTGAT
TACAATCGTCATGCAGTGGTCATGGAACTCATAAATGGTTATCCACTATGTCAGATACAC
CATGTTGAAGATCCTGCATCAGTATATGATGAAGCTATGGAACTAATTGTCAAACTTGCA
AATCATGGGCTGATTCATGGAGATTTTAATGAATTTAATCTCATTTTGGATGAAAGTGAC
CATATCACCATGATTGATTTTCCACAGATGGTTTCAACTTCTCATCCCAATGCTGAGTGG
TATTTTGACAGAGATGTTAAATGCATTAAAGATTTCTTTATGAAACGTTTCAGCTACGAA
AGTGAGCTTTTTCCAACTTTTAAGGATATCAGGAGAGAAGACACTCTTGATGTGGAGGTT
TCTGCCAGTGGCTACACAAAGGAAATGCAGGCAGATGATGAACTGCTTCATCCATTAGGT
CCAGATGATAAAAATATTGAAACAAAAGAGGGATCTGAATTCTCATTTTCAGATGGAGAA
GTGGCAGAAAAAGCAGAGGTTTACAGGTCAGAAAATGAAAGTGAACGGAACTGTCTAGAA
GAATCAGAGGGCTGCTATTGCAGATCATCTGGAGACCCTGAACAAATAAAGGAAGACAGT
TTATCAGAAGAGAGTGCTGATGCACGGAGTTTTGAAATGACTGAATTCAATCAAGCTTTA
GAAGAAATAAAAGGGCAGGTTGTTGAAAACAACTCTGTAACTGAATTTTCTGAGGAGAAA
AACAGAACTGAAAATTACAACAGGCAAGATGGTCAGAGAGTTCAAGGAGGAGTCCCTGCT
GGCTCTGACGAGTATGAAGATGAATGCCCTCATCTAATTGCCTTGTCGTCATTAAATAGA
GAATTCAGGCCTTTCAGAGATGAAGAAAATGTGGGAGCTATGAATCAGTATAGAACAAGA
ACTCTGAGTATCACTTCTTCAGGCAGTGCTGTAAGCTGTTCAACAATTCCTCCAGAACTG
GTGAAACAGAAGGTGAAACGTCAGTTGACAAAACAGCAAAAATCAGCTGTCAGACGTCGA
TTGCAGAAAGGAGAAGCAAATATATTTACCAAGCAACGTAGGGAAAACATGCAAAATATC
AAATCAAGTTTGGAAGCAGCTAGCTTTTGGGGAGAATAA
|
| Enzyme 96 GenBank Gene ID |
AK002021 |
| Enzyme 96 GeneCard ID |
RIOK2 |
| Enzyme 96 GenAtlas ID |
RIOK2 |
| Enzyme 96 HGNC ID |
HGNC:18999 |
| Enzyme 96 Chromosome Location |
5 |
| Enzyme 96 Locus |
5q15 |
| Enzyme 96 SNPs |
SNPJam Report |
| Enzyme 96 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 ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed ]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 96 Metabolite References |
Not Available |
|
Enzyme 97
[top]
|
| Enzyme 97 ID |
6430 |
| Enzyme 97 Name |
Mitogen-activated protein kinase kinase kinase 1 |
| Enzyme 97 Synonyms |
- MAPK/ERK kinase kinase 1
- MEK kinase 1
- MEKK 1
|
| Enzyme 97 Gene Name |
MAP3K1 |
| Enzyme 97 Protein Sequence |
>Mitogen-activated protein kinase kinase kinase 1
MAAAAGNRASSSGFPGARATSPEAGGGGGALKASSAPAAAAGLLREAGSGGRERADWRRR
QLRKVRSVELDQLPEQPLFLAASPPASSTSPSPEPADAAGSGTGFQPVAVPPPHGAASRG
GAHLTESVAAPDSGASSPAAAEPGEKRAPAAEPSPAAAPAGREMENKETLKGLHKMDDRP
EERMIREKLKATCMPAWKHEWLERRNRRGPVVVKPIPVKGDGSEMNHLAAESPGEVQASA
ASPASKGRRSPSPGNSPSGRTVKSESPGVRRKRVSPVPFQSGRITPPRRAPSPDGFSPYS
PEETNRRVNKVMRARLYLLQQIGPNSFLIGGDSPDNKYRVFIGPQNCSCARGTFCIHLLF
VMLRVFQLEPSDPMLWRKTLKNFEVESLFQKYHSRRSSRIKAPSRNTIQKFVSRMSNSHT
LSSSSTSTSSSENSIKDEEEQMCPICLLGMLDEESLTVCEDGCRNKLHHHCMSIWAEECR
RNREPLICPLCRSKWRSHDFYSHELSSPVDSPSSLRAAQQQTVQQQPLAGSRRNQESNFN
LTHYGTQQIPPAYKDLAEPWIQVFGMELVGCLFSRNWNVREMALRRLSHDVSGALLLANG
ESTGNSGGSSGSSPSGGATSGSSQTSISGDVVEACCSVLSMVCADPVYKVYVAALKTLRA
MLVYTPCHSLAERIKLQRLLQPVVDTILVKCADANSRTSQLSISTLLELCKGQAGELAVG
REILKAGSIGIGGVDYVLNCILGNQTESNNWQELLGRLCLIDRLLLEFPAEFYPHIVSTD
VSQAEPVEIRYKKLLSLLTFALQSIDNSHSMVGKLSRRIYLSSARMVTTVPHVFSKLLEM
LSVSSSTHFTRMRRRLMAIADEVEIAEAIQLGVEDTLDGQQDSFLQASVPNNYLETTENS
SPECTVHLEKTGKGLCATKLSASSEDISERLASISVGPSSSTTTTTTTTEQPKPMVQTKG
RPHSQCLNSSPLSHHSQLMFPALSTPSSSTPSVPAGTATDVSKHRLQGFIPCRIPSASPQ
TQRKFSLQFHRNCPENKDSDKLSPVFTQSRPLPSSNIHRPKPSRPTPGNTSKQGDPSKNS
MTLDLNSSSKCDDSFGCSSNSSNAVIPSDETVFTPVEEKCRLDVNTELNSSIEDLLEASM
PSSDTTVTFKSEVAVLSPEKAENDDTYKDDVNHNQKCKEKMEAEEEEALAIAMAMSASQD
ALPIVPQLQVENGEDIIIIQQDTPETLPGHTKAKQPYREDTEWLKGQQIGLGAFSSCYQA
QDVGTGTLMAVKQVTYVRNTSSEQEEVVEALREEIRMMSHLNHPNIIRMLGATCEKSNYN
LFIEWMAGGSVAHLLSKYGAFKESVVINYTEQLLRGLSYLHENQIIHRDVKGANLLIDST
GQRLRIADFGAAARLASKGTGAGEFQGQLLGTIAFMAPEVLRGQQYGRSCDVWSVGCAII
EMACAKPPWNAEKHSNHLALIFKIASATTAPSIPSHLSPGLRDVALRCLELQPQDRPPSR
ELLKHPVFRTTW
|
| Enzyme 97 Number of Residues |
1512 |
| Enzyme 97 Molecular Weight |
164468.3 |
| Enzyme 97 Theoretical pI |
7.77 |
| Enzyme 97 GO Classification |
| Function |
- ATP binding
- MAP kinase kinase kinase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- ion binding
- kinase activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- protein binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- receptor signaling protein serine/threonine kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- MAPKKK cascade
- cellular metabolic process
- intracellular protein kinase cascade
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- signal transmission
- signal transmission via phosphorylation event
- signaling process
|
| Component |
| — |
|
| Enzyme 97 General Function |
Involved in magnesium ion binding |
| Enzyme 97 Specific Function |
Component of a protein kinase signal transduction cascade. Activates the ERK and JNK kinase pathways by phosphorylation of MAP2K1 and MAP2K4. Activates CHUK and IKBKB, the central protein kinases of the NF-kappa-B pathway |
| Enzyme 97 Pathways |
Not Available |
| Enzyme 97 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 97 Pfam Domain Function |
|
| Enzyme 97 Signals |
|
| Enzyme 97 Transmembrane Regions |
|
| Enzyme 97 Essentiality |
Not Available |
| Enzyme 97 GenBank ID Protein |
153945765 |
| Enzyme 97 UniProtKB/Swiss-Prot ID |
Q13233 |
| Enzyme 97 UniProtKB/Swiss-Prot Entry Name |
M3K1_HUMAN |
| Enzyme 97 PDB ID |
Not Available |
| Enzyme 97 Cellular Location |
Not Available |
| Enzyme 97 Gene Sequence |
>4539 bp
ATGGCGGCGGCGGCGGGGAATCGCGCCTCGTCGTCGGGATTCCCGGGCGCCAGGGCTACG
AGCCCTGAGGCAGGCGGCGGCGGAGGAGCCCTCAAGGCGAGCAGCGCGCCCGCGGCTGCC
GCGGGACTGCTGCGGGAGGCGGGCAGCGGGGGCCGCGAGCGGGCGGACTGGCGGCGGCGG
CAGCTGCGCAAAGTGCGGAGTGTGGAGCTGGACCAGCTGCCTGAGCAGCCGCTCTTCCTT
GCCGCCTCACCGCCGGCCTCCTCGACTTCCCCGTCGCCGGAGCCCGCGGACGCAGCGGGG
AGTGGGACCGGCTTCCAGCCTGTGGCGGTGCCGCCGCCCCACGGAGCCGCGAGCCGCGGC
GGCGCCCACCTTACCGAGTCGGTGGCGGCGCCGGACAGCGGCGCCTCGAGTCCCGCAGCG
GCCGAGCCCGGGGAGAAGCGGGCGCCCGCCGCCGAGCCGTCTCCTGCAGCGGCCCCCGCC
GGTCGTGAGATGGAGAATAAAGAAACTCTCAAAGGGTTGCACAAGATGGATGATCGTCCA
GAGGAACGAATGATCAGGGAGAAACTGAAGGCAACCTGTATGCCAGCCTGGAAGCACGAA
TGGTTGGAAAGGAGAAATAGGCGAGGGCCTGTGGTGGTAAAACCAATCCCAGTTAAAGGA
GATGGATCTGAAATGAATCACTTAGCAGCTGAGTCTCCAGGAGAGGTCCAGGCAAGTGCG
GCTTCACCAGCTTCCAAAGGCCGACGCAGTCCTTCTCCTGGCAACTCCCCATCAGGTCGC
ACAGTGAAATCAGAATCTCCAGGAGTAAGGAGAAAAAGAGTTTCCCCAGTGCCTTTTCAG
AGTGGCAGAATCACACCACCCCGAAGAGCCCCTTCACCAGATGGCTTCTCACCATATAGC
CCTGAGGAAACAAACCGCCGTGTTAACAAAGTGATGCGGGCCAGACTGTACTTACTGCAG
CAGATAGGGCCTAACTCTTTCCTGATTGGAGGAGACAGCCCAGACAATAAATACCGGGTG
TTTATTGGGCCTCAGAACTGCAGCTGTGCACGTGGAACATTCTGTATTCATCTGCTATTT
GTGATGCTCCGGGTGTTTCAACTAGAACCTTCAGACCCAATGTTATGGAGAAAAACTTTA
AAGAATTTTGAGGTTGAGAGTTTGTTCCAGAAATATCACAGTAGGCGTAGCTCAAGGATC
AAAGCTCCATCTCGTAACACCATCCAGAAGTTTGTTTCACGCATGTCAAATTCTCATACA
TTGTCATCATCTAGTACTTCTACGTCTAGTTCAGAAAACAGCATAAAGGATGAAGAGGAA
CAGATGTGTCCTATTTGCTTGTTGGGCATGCTTGATGAAGAAAGTCTTACAGTGTGTGAA
GACGGCTGCAGGAACAAGCTGCACCACCACTGCATGTCAATTTGGGCAGAAGAGTGTAGA
AGAAATAGAGAACCTTTAATATGTCCCCTTTGTAGATCTAAGTGGAGATCTCATGATTTC
TACAGCCACGAGTTGTCAAGTCCTGTGGATTCCCCTTCTTCCCTCAGAGCTGCACAGCAG
CAAACCGTACAGCAGCAGCCTTTGGCTGGATCACGAAGGAATCAAGAGAGCAATTTTAAC
CTTACTCATTATGGAACTCAGCAAATCCCTCCTGCTTACAAAGATTTAGCTGAGCCATGG
ATTCAGGTGTTTGGAATGGAACTCGTTGGCTGCTTATTTTCTAGAAACTGGAATGTGAGA
GAGATGGCCCTCAGGCGTCTTTCCCATGATGTCAGTGGGGCCCTGCTGTTGGCAAATGGG
GAGAGCACTGGAAATTCTGGGGGCAGCAGTGGAAGCAGCCCGAGTGGGGGAGCCACCAGT
GGGTCTTCCCAGACCAGTATCTCAGGAGATGTGGTGGAGGCATGCTGCAGCGTTCTGTCA
ATGGTCTGTGCTGACCCTGTCTACAAAGTGTACGTTGCTGCTTTAAAAACATTGAGAGCC
ATGCTGGTATATACTCCTTGCCACAGTTTAGCGGAAAGAATCAAACTTCAGAGACTTCTC
CAGCCAGTTGTAGACACCATCCTAGTCAAATGTGCAGATGCCAATAGCCGCACAAGTCAG
CTGTCCATATCAACACTGTTGGAACTGTGCAAAGGCCAAGCAGGAGAGTTGGCAGTTGGC
AGAGAAATACTAAAAGCTGGATCCATTGGTATTGGTGGTGTTGATTATGTCTTAAATTGT
ATTCTTGGAAACCAAACTGAATCAAACAATTGGCAAGAACTTCTTGGCCGCCTTTGTCTT
ATAGATAGACTGTTGTTGGAATTTCCTGCTGAATTTTATCCTCATATTGTCAGTACTGAT
GTTTCACAAGCTGAGCCTGTTGAAATCAGGTATAAGAAGCTGCTGTCCCTCTTAACCTTT
GCTTTGCAGTCCATTGATAATTCCCACTCAATGGTTGGCAAACTTTCCAGAAGGATCTAC
TTGAGTTCTGCAAGAATGGTTACTACAGTACCCCATGTGTTTTCAAAACTGTTAGAAATG
CTGAGTGTTTCCAGTTCCACTCACTTCACCAGGATGCGTCGCCGTTTGATGGCTATTGCA
GATGAGGTGGAAATTGCCGAAGCCATCCAGTTGGGCGTAGAAGACACTTTGGATGGTCAA
CAGGACAGCTTCTTGCAGGCATCTGTTCCCAACAACTATCTGGAAACCACAGAGAACAGT
TCCCCTGAGTGCACAGTCCATTTAGAGAAAACTGGAAAAGGATTATGTGCTACAAAATTG
AGTGCCAGTTCAGAGGACATTTCTGAGAGACTGGCCAGCATTTCAGTAGGACCTTCTAGT
TCAACAACAACAACAACAACAACAACAGAGCAACCAAAGCCAATGGTTCAAACAAAAGGC
AGACCCCACAGTCAGTGTTTGAACTCCTCTCCTTTATCTCATCATTCCCAATTAATGTTT
CCAGCCTTGTCAACCCCTTCTTCTTCTACCCCATCTGTACCAGCTGGCACTGCAACAGAT
GTCTCTAAGCATAGACTTCAGGGATTCATTCCCTGCAGAATACCTTCTGCATCTCCTCAA
ACACAGCGCAAGTTTTCTCTACAATTCCACAGAAACTGTCCTGAAAACAAAGACTCAGAT
AAACTTTCCCCAGTCTTTACTCAGTCAAGACCCTTGCCCTCCAGTAACATACACAGGCCA
AAGCCATCTAGACCTACCCCAGGTAATACAAGTAAACAGGGAGATCCCTCAAAAAATAGC
ATGACACTTGATCTGAACAGTAGTTCCAAATGTGATGACAGCTTTGGCTGTAGCAGCAAT
AGTAGTAATGCTGTTATACCCAGTGACGAGACAGTGTTCACCCCAGTAGAGGAGAAATGC
AGATTAGATGTCAATACAGAGCTCAACTCCAGTATTGAGGACCTTCTTGAAGCATCTATG
CCTTCAAGTGATACAACAGTAACTTTTAAGTCAGAAGTTGCTGTCCTGTCTCCTGAAAAG
GCTGAAAATGATGATACCTACAAAGATGATGTGAATCATAATCAAAAGTGCAAAGAGAAG
ATGGAAGCTGAAGAAGAAGAAGCTTTAGCAATTGCCATGGCAATGTCAGCGTCTCAGGAT
GCCCTCCCCATAGTTCCTCAGCTGCAGGTTGAAAATGGAGAAGATATCATCATTATTCAA
CAGGATACACCAGAGACTCTACCAGGACATACCAAAGCAAAACAACCGTATAGAGAAGAC
ACTGAATGGCTGAAAGGTCAACAGATAGGCCTTGGAGCATTTTCTTCTTGTTATCAGGCT
CAAGATGTGGGAACTGGAACTTTAATGGCTGTTAAACAGGTGACTTATGTCAGAAACACA
TCTTCTGAGCAAGAAGAAGTAGTAGAAGCACTAAGAGAAGAGATAAGAATGATGAGCCAT
CTGAATCATCCAAACATCATTAGGATGTTGGGAGCCACGTGTGAGAAGAGCAATTACAAT
CTCTTCATTGAATGGATGGCAGGGGGATCGGTGGCTCATTTGCTGAGTAAATATGGAGCC
TTCAAAGAATCAGTAGTTATTAACTACACTGAACAGTTACTCCGTGGCCTTTCGTATCTC
CATGAAAACCAAATCATTCACAGAGATGTCAAAGGTGCCAATTTGCTAATTGACAGCACT
GGTCAGAGACTAAGAATTGCAGATTTTGGAGCTGCAGCCAGGTTGGCATCAAAAGGAACT
GGTGCAGGAGAGTTTCAGGGACAATTACTGGGGACAATTGCATTTATGGCACCTGAGGTA
CTAAGAGGTCAACAGTATGGAAGGAGCTGTGATGTATGGAGTGTTGGCTGTGCTATTATA
GAAATGGCTTGTGCAAAACCACCATGGAATGCAGAAAAACACTCCAATCATCTTGCTTTG
ATATTTAAGATTGCTAGTGCAACTACTGCTCCATCGATCCCTTCACATTTGTCTCCTGGT
TTACGAGATGTGGCTCTTCGTTGTTTAGAACTTCAACCTCAGGACAGACCTCCATCAAGA
GAGCTACTGAAGCATCCAGTCTTTCGTACTACATGGTAG
|
| Enzyme 97 GenBank Gene ID |
NM_005921.1 |
| Enzyme 97 GeneCard ID |
MAP3K1 |
| Enzyme 97 GenAtlas ID |
MAP3K1 |
| Enzyme 97 HGNC ID |
HGNC:6848 |
| Enzyme 97 Chromosome Location |
5 |
| Enzyme 97 Locus |
5q11.2 |
| Enzyme 97 SNPs |
SNPJam Report |
| Enzyme 97 General References |
- Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed ]
- Xia Y, Wu Z, Su B, Murray B, Karin M: JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino-terminal extension. Genes Dev. 1998 Nov 1;12(21):3369-81. [PubMed ]
- Vinik BS, Kay ES, Fiedorek FT Jr: Mapping of the MEK kinase gene (Mekk) to mouse chromosome 13 and human chromosome 5. Mamm Genome. 1995 Nov;6(11):782-3. [PubMed ]
- Rui HL, Fan E, Zhou HM, Xu Z, Zhang Y, Lin SC: SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling. J Biol Chem. 2002 Nov 8;277(45):42981-6. Epub 2002 Sep 9. [PubMed ]
- Wong CK, Luo W, Deng Y, Zou H, Ye Z, Lin SC: The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase activation by Axin and dishevelled through distinct mechanisms. J Biol Chem. 2004 Sep 17;279(38):39366-73. Epub 2004 Jul 15. [PubMed ]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
- 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 ]
- Enomoto A, Kido N, Ito M, Morita A, Matsumoto Y, Takamatsu N, Hosoi Y, Miyagawa K: Negative regulation of MEKK1/2 signaling by serine-threonine kinase 38 (STK38). Oncogene. 2008 Mar 20;27(13):1930-8. Epub 2007 Oct 1. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 97 Metabolite References |
Not Available |
|
Enzyme 98
[top]
|
| Enzyme 98 ID |
6431 |
| Enzyme 98 Name |
Mitogen-activated protein kinase 12 |
| Enzyme 98 Synonyms |
- MAP kinase 12
- MAPK 12
- Extracellular signal-regulated kinase 6
- ERK-6
- Mitogen-activated protein kinase p38 gamma
- MAP kinase p38 gamma
- Stress-activated protein kinase 3
|
| Enzyme 98 Gene Name |
MAPK12 |
| Enzyme 98 Protein Sequence |
>Mitogen-activated protein kinase 12
MSSPPPARSGFYRQEVTKTAWEVRAVYRDLQPVGSGAYGAVCSAVDGRTGAKVAIKKLYR
PFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLM
KHEKLGEDRIQFLVYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQADS
EMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKTLFKGSDHLDQLKEIMK
VTGTPPAEFVQRLQSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLVLDAEQRV
TAGEALAHPYFESLHDTEDEPQVQKYDDSFDDVDRTLDEWKRVTYKEVLSFKPPRQLGAR
VSKETPL
|
| Enzyme 98 Number of Residues |
367 |
| Enzyme 98 Molecular Weight |
41939.8 |
| Enzyme 98 Theoretical pI |
6.33 |
| Enzyme 98 GO Classification |
| Function |
- ATP binding
- MAP kinase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- receptor signaling protein serine/threonine kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 98 General Function |
Involved in MAP kinase activity |
| Enzyme 98 Specific Function |
Responds to activation by environmental stress and pro- inflammatory cytokines by phosphorylating downstream targets. Plays a role in myoblast differentiation and also in the down- regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation |
| Enzyme 98 Pathways |
Not Available |
| Enzyme 98 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 98 Pfam Domain Function |
|
| Enzyme 98 Signals |
|
| Enzyme 98 Transmembrane Regions |
|
| Enzyme 98 Essentiality |
Not Available |
| Enzyme 98 GenBank ID Protein |
1486363 |
| Enzyme 98 UniProtKB/Swiss-Prot ID |
P53778 |
| Enzyme 98 UniProtKB/Swiss-Prot Entry Name |
MK12_HUMAN |
| Enzyme 98 PDB ID |
1CM8 |
| Enzyme 98 PDB File |
Show |
| Enzyme 98 3D Structure |
|
| Enzyme 98 Cellular Location |
Not Available |
| Enzyme 98 Gene Sequence |
>1104 bp
ATGAGCTCTCCGCCGCCCACCCGCAGTGGCTTTTACCGCCAGGAGGTGACCAAGACGGCC
TGGGAGGTGCGCGCCGTGTACCGGGACCTGCAGCCCGTGGGCTCGGGCGCCTACGGCGCG
GTGTGCTCGGCCGTGGACGGCCGCACCGGCGCTAAGGTTGCCATCAAGAAGCTGTATCGG
CCCTTCCAGTCCGAGCTGTTCGCCAAGCTCGCCTACCGCGAGCTGCGCCTGCTCAAGCAC
ATGCGCCACGAGAACGTGATCGGGCTGCTGGACGTATTCACTCCTGATGAGACCCTGGAT
GACTTCACGGACTTTTACCTGGTGATGCCGTTCATGGGCACCGACCTGGGCAAGCTCATG
AAACATGAGAAGCTAGGCGAGGACCGGATCCAGTTCCTCGTGTACCAGATGATGAAGGGG
CTGAGGTATATCCACGCTGCCGGCATCATCCACAGAGACCTGAAGCCCGGCAACCTGGCT
GTGAACGAAGACTGTGAGCTGAAGATCCTGGACTTCGGCCTGGCCAGGCAGGCAGACAGT
GAGATGACTGGGTACGTGGTGACCCGGTGGTACCGGGCTCCCGAGGTCATCTTGAATTGG
ATCGCGTACACGCAGACGGTGGACATCTGGTCTGTGGGCTGCATCATGGCGGAGATGATC
ACAGGCAAGACGCTGTTCAAGGGCAGCGACCACCTGGACCAGCTGAAGGAGATCATGAAG
GTGACGGGGACGCCTCCGGCTGAGTTTGTGCAGCGGCTGCAGAGCGATGAGGCCAAGAAC
TACATGAAGGGCCTCCCCGAATTGGAGAAGAAGGATTTTGCCTCTATCCTGACCAATGCA
AGCCCTCTGGCTGTGAACCTCCTGGAGAAGATGCTGGTGCTGGACGCGGACATCAGGTTG
ACTGCAGGCGAGTTTCTTTCCCATCCCTACTTCGAGTCCCTGCACGACACGGAAGATGAG
CCCCAGGTCCAGAAGTATGATGACTCCTTTGACTACTTTGACCGCACACTGGATGAATGG
AAGCGTGTTACTTACAAAGAGGTGCTCAGCTTCAAGCCTCCCCGGCAGCTGGGGGCCAGG
GTCTCCAAGGAGACGCCTCTGTGA
|
| Enzyme 98 GenBank Gene ID |
X79483 |
| Enzyme 98 GeneCard ID |
MAPK12 |
| Enzyme 98 GenAtlas ID |
MAPK12 |
| Enzyme 98 HGNC ID |
HGNC:6874 |
| Enzyme 98 Chromosome Location |
2 |
| Enzyme 98 Locus |
22q13.33 |
| Enzyme 98 SNPs |
SNPJam Report |
| Enzyme 98 General References |
- Lechner C, Zahalka MA, Giot JF, Moller NP, Ullrich A: ERK6, a mitogen-activated protein kinase involved in C2C12 myoblast differentiation. Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4355-9. [PubMed ]
- Goedert M, Hasegawa J, Craxton M, Leversha MA, Clegg S: Assignment of the human stress-activated protein kinase-3 gene (SAPK3) to chromosome 22q13.3 by fluorescence in situ hybridization. Genomics. 1997 May 1;41(3):501-2. [PubMed ]
- Li Z, Jiang Y, Ulevitch RJ, Han J: The primary structure of p38 gamma: a new member of p38 group of MAP kinases. Biochem Biophys Res Commun. 1996 Nov 12;228(2):334-40. [PubMed ]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Hasegawa M, Cuenda A, Spillantini MG, Thomas GM, Buee-Scherrer V, Cohen P, Goedert M: Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition. J Biol Chem. 1999 Apr 30;274(18):12626-31. [PubMed ]
- Court NW, dos Remedios CG, Cordell J, Bogoyevitch MA: Cardiac expression and subcellular localization of the p38 mitogen-activated protein kinase member, stress-activated protein kinase-3 (SAPK3). J Mol Cell Cardiol. 2002 Apr;34(4):413-26. [PubMed ]
- Wiltshire C, Matsushita M, Tsukada S, Gillespie DA, May GH: A new c-Jun N-terminal kinase (JNK)-interacting protein, Sab (SH3BP5), associates with mitochondria. Biochem J. 2002 Nov 1;367(Pt 3):577-85. [PubMed ]
- Diskin R, Askari N, Capone R, Engelberg D, Livnah O: Active mutants of the human p38alpha mitogen-activated protein kinase. J Biol Chem. 2004 Nov 5;279(45):47040-9. Epub 2004 Jul 28. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Bellon S, Fitzgibbon MJ, Fox T, Hsiao HM, Wilson KP: The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation. Structure. 1999 Sep 15;7(9):1057-65. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 98 Metabolite References |
Not Available |
|
Enzyme 99
[top]
|
| Enzyme 99 ID |
6434 |
| Enzyme 99 Name |
Cell division protein kinase 3 |
| Enzyme 99 Synonyms |
Not Available |
| Enzyme 99 Gene Name |
CDK3 |
| Enzyme 99 Protein Sequence |
>Cell division protein kinase 3
MDMFQKVEKIGEGTYGVVYKAKNRETGQLVALKKIRLDLEMEGVPSTAIREISLLKELKH
PNIVRLLDVVHNERKLYLVFEFLSQDLKKYMDSTPGSELPLHLIKSYLFQLLQGVSFCHS
HRVIHRDLKPQNLLINELGAIKLADFGLARAFGVPLRTYTHEVVTLWYRAPEILLGSKFY
TTAVDIWSIGCIFAEMVTRKALFPGDSEIDQLFRIFRMLGTPSEDTWPGVTQLPDYKGSF
PKWTRKGLEEIVPNLEPEGRDLLMQLLQYDPSQRITAKTALAHPYFSSPEPSPAARQYVL
QRFRH
|
| Enzyme 99 Number of Residues |
305 |
| Enzyme 99 Molecular Weight |
35045.4 |
| Enzyme 99 Theoretical pI |
9.14 |
| Enzyme 99 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 99 General Function |
Involved in protein kinase activity |
| Enzyme 99 Specific Function |
Probably involved in the control of the cell cycle. Interacts with a yet unknown type of cyclin. Can phosphorylate histone H1 |
| Enzyme 99 Pathways |
Not Available |
| Enzyme 99 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 99 Pfam Domain Function |
|
| Enzyme 99 Signals |
|
| Enzyme 99 Transmembrane Regions |
|
| Enzyme 99 Essentiality |
Not Available |
| Enzyme 99 GenBank ID Protein |
54781357 |
| Enzyme 99 UniProtKB/Swiss-Prot ID |
Q00526 |
| Enzyme 99 UniProtKB/Swiss-Prot Entry Name |
CDK3_HUMAN |
| Enzyme 99 PDB ID |
Not Available |
| Enzyme 99 Cellular Location |
Not Available |
| Enzyme 99 Gene Sequence |
>918 bp
ATGGATATGTTCCAGAAGGTAGAGAAGATCGGAGAGGGCACCTATGGGGTGGTGTACAAG
GCCAAGAACAGGGAGACAGGGCAGCTGGTGGCCCTGAAGAAGATCAGACTGGATTTGGAG
ATGGAGGGGGTCCCAAGCACTGCCATCAGGGAGATCTCGCTGCTCAAGGAACTGAAGCAC
CCCAACATCGTCCGACTGCTGGACGTGGTGCACAACGAGAGGAAGCTCTATCTGGTGTTT
GAGTTCCTCAGCCAGGACCTGAAGAAGTACATGGACTCCACCCCAGGCTCAGAGCTCCCC
CTGCACCTCATCAAGAGCTACCTCTTCCAGCTGCTGCAGGGGGTGAGTTTCTGCCACTCA
CATCGGGTCATCCACCGAGACCTGAAGCCCCAGAACCTGCTCATCAATGAGTTGGGTGCC
ATCAAGCTGGCTGACTTCGGCCTGGCTCGCGCCTTCGGGGTGCCCCTGCGCACCTACACC
CATGAGGTGGTGACACTGTGGTATCGCGCCCCCGAGATTCTCTTGGGCAGCAAGTTCTAT
ACCACAGCTGTGGATATCTGGAGCATTGGTTGCATCTTTGCAGAGATGGTGACTCGAAAA
GCCCTGTTTCCTGGTGACTCTGAGATTGACCAGCTCTTTCGTATCTTTCGTATGCTGGGG
ACACCCAGCGAAGACACATGGCCCGGGGTCACCCAGCTGCCTGACTATAAGGGCAGCTTC
CCTAAGTGGACCAGGAAGGGACTGGAAGAGATTGTGCCCAATCTGGAGCCAGAGGGCAGG
GACCTGCTCATGCAACTCCTGCAGTATGACCCCAGCCAGCGGATCACAGCCAAGACTGCC
CTGGCCCACCCGTACTTCTCATCCCCTGAGCCCTCCCCAGCTGCCCGCCAGTATGTGCTG
CAGCGATTCCGCCATTGA
|
| Enzyme 99 GenBank Gene ID |
AY789470 |
| Enzyme 99 GeneCard ID |
CDK3 |
| Enzyme 99 GenAtlas ID |
CDK3 |
| Enzyme 99 HGNC ID |
HGNC:1772 |
| Enzyme 99 Chromosome Location |
1 |
| Enzyme 99 Locus |
17q22-qter |
| Enzyme 99 SNPs |
SNPJam Report |
| Enzyme 99 General References |
- Meyerson M, Enders GH, Wu CL, Su LK, Gorka C, Nelson C, Harlow E, Tsai LH: A family of human cdc2-related protein kinases. EMBO J. 1992 Aug;11(8):2909-17. [PubMed ]
- Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed ]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed ]
- Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed ]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 99 Metabolite References |
Not Available |
|
Enzyme 100
[top]
|
| Enzyme 100 ID |
6435 |
| Enzyme 100 Name |
Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit gamma |
| Enzyme 100 Synonyms |
- PI3K-C2-gamma
- PtdIns-3-kinase C2 subunit gamma
- Phosphoinositide 3-kinase-C2-gamma
|
| Enzyme 100 Gene Name |
PIK3C2G |
| Enzyme 100 Protein Sequence |
>Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit gamma
MAYSWQTDPNPNESHEKQYEHQEFLFVNQPHSSSQVSLGFDQIVDEISGKIPHYESEIDE
NTFFVPTAPKWDSTGHSLNEAHQISLNEFTSKSRELSWHQVSKAPAIGFSPSVLPKPQNT
NKECSWGSIGKHHGADDSRFSILALSFTSLDKINLEKELENENHNYHIGFESSIPPTNSS
FSSDFMPKEENKRSGHVNIVEPSLMLLKGSLQPGMWESTWQKNIESIGCSIQLVEVPQSS
NTSLASFCNKVKKIRERYHAADVNFNSGKIWSTTTAFPYQLFSKTKFNIHIFIDNSTQPL
HFMPCANYLVKDLIAEILHFCTNDQLLPKDHILSVCGSEEFLQNDHCLGSHKMFQKDKSV
IQLHLQKSREAPGKLSRKHEEDHSQFYLNQLLEFMHIWKVSRQCLLTLIRKYDFHLKYLL
KTQENVYNIIEEVKKICSVLGCVETKQITDAVNELSLILQRKGENFYQSSETSAKGLIEK
VTTELSTSIYQLINVYCNSFYADFQPVNVPRCTSYLNPGLPSHLSFTVYAAHNIPETWVH
RINFPLEIKSLPRESMLTVKLFGIACATNNANLLAWTCLPLFPKEKSILGSMLFSMTLQS
EPPVEMITPGVWDVSQPSPVTLQIDFPATGWEYMKPDSEENRSNLEEPLKECIKHIARLS
QKQTPLLLSEEKKRYLWFYRFYCNNENCSLPLVLGSAPGWDERTVSEMHTILRRWTFSQP
LEALGLLTSSFPDQEIRKVAVQQLDNLLNDELLEYLPQLVQAVKFEWNLESPLVQLLLHR
SLQSIQVAHRLYWLLKNAENEAYFKSWYQKLLAALQFCAGKALNDEFSKEQKLIKILGDI
GERVKSASDHQRQEVLKKEIGRLEEFFQDVNTCHLPLNPALCIKGIDHDACSYFTSNALP
LKITFINANLMGKNISIIFKAGDDLRQDMLVLQLIQVMDNIWLQEGLDMQMIIYRCLSTG
KDQGLVQMVPDAVTLAKIHRHSGLIGPLKENTIKKWFSQHNHLKADYEKALRNFFYSCAG
WCVVTFILGVCDRHNDNIMLTKSGHMFHIDFGKFLGHAQTFGGIKRDRAPFIFTSEMEYF
ITEGGKNPQHFQDFVELCCRAYNIIRKHSQLLLNLLEMMLYAGLPELSGIQDLKYVYNNL
RPQDTDLEATSHFTKKIKESLECFPVKLNNLIHTLAQMSAISPAKSTSQTFPQESCLLST
TRSIERATILGFSKKSSNLYLIQVTHSNNETSLTEKSFEQFSKLHSQLQKQFASLTLPEF
PHWWHLPFTNSDHRRFRDLNHYMEQILNVSHEVTNSDCVLSFFLSEAVQQTVEESSPVYL
GEKFPDKKPKVQLVISYEDVKLTILVKHMKNIHLPDGSAPSAHVEFYLLPYPSEVRRRKT
KSVPKCTDPTYNEIVVYDEVTELQGHVLMLIVKSKTVFVGAINIRLCSVPLDKEKWYPLG
NSII
|
| Enzyme 100 Number of Residues |
1444 |
| Enzyme 100 Molecular Weight |
165648.3 |
| Enzyme 100 Theoretical pI |
6.92 |
| Enzyme 100 GO Classification |
| Function |
- 1-phosphatidylinositol-3-kinase activity
- binding
- catalytic activity
- inositol or phosphatidylinositol kinase activity
- kinase activity
- lipid binding
- lipid kinase activity
- phosphoinositide 3-kinase activity
- phosphoinositide binding
- phospholipid binding
- phosphotransferase activity, alcohol group as acceptor
- protein binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biological regulation
- cell communication
- cellular process
- glycerophospholipid metabolic process
- intracellular signal transduction
- metabolic process
- organophosphate metabolic process
- phosphoinositide metabolic process
- phosphoinositide phosphorylation
- phosphoinositide-mediated signaling
- phospholipid metabolic process
- regulation of biological process
- regulation of cellular process
- second-messenger-mediated signaling
- signal transduction
|
| Component |
- macromolecular complex
- phosphoinositide 3-kinase complex
- protein complex
|
|
| Enzyme 100 General Function |
Involved in binding |
| Enzyme 100 Specific Function |
In vitro, phosphorylates PtdIns and PtdIns4P but not PtdIns(4,5)P2 |
| Enzyme 100 Pathways |
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 100 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate [RN:R05795]
|
| Enzyme 100 Pfam Domain Function |
|
| Enzyme 100 Signals |
|
| Enzyme 100 Transmembrane Regions |
|
| Enzyme 100 Essentiality |
Not Available |
| Enzyme 100 GenBank ID Protein |
120659792 |
| Enzyme 100 UniProtKB/Swiss-Prot ID |
O75747 |
| Enzyme 100 UniProtKB/Swiss-Prot Entry Name |
P3C2G_HUMAN |
| Enzyme 100 PDB ID |
Not Available |
| Enzyme 100 Cellular Location |
Not Available |
| Enzyme 100 Gene Sequence |
>4335 bp
ATGGCATATTCTTGGCAAACGGATCCAAATCCTAATGAATCACACGAAAAGCAGTATGAA
CACCAAGAATTTCTCTTTGTAAATCAACCCCATTCTTCTAGCCAAGTCAGTCTGGGTTTT
GATCAGATAGTAGATGAGATCAGTGGCAAAATTCCACACTACGAGAGTGAAATTGATGAA
AACACCTTTTTTGTGCCCACTGCACCAAAATGGGACTCAACAGGGCATTCATTAAATGAA
GCACACCAAATATCCTTGAATGAATTCACTTCTAAAAGCCGTGAACTCTCCTGGCATCAA
GTTAGCAAAGCACCAGCAATTGGTTTTAGTCCTTCTGTGTTACCAAAACCTCAAAATACG
AATAAAGAATGCTCCTGGGGAAGCATAGGAAAACATCATGGTGCTGATGATTCCAGATTC
AGTATTTTAGCTCTATCATTCACAAGTTTGGATAAAATTAATCTAGAGAAAGAATTAGAA
AATGAAAATCATAACTACCATATAGGATTTGAAAGTAGCATTCCTCCAACAAATTCATCC
TTCTCAAGTGACTTCATGCCGAAAGAAGAGAATAAAAGGAGTGGACATGTGAACATTGTG
GAACCATCTTTGATGCTTTTGAAAGGCTCTCTTCAACCCGGAATGTGGGAAAGTACATGG
CAGAAGAATATAGAGTCAATAGGTTGTTCCATTCAGCTAGTGGAAGTACCTCAAAGCAGC
AATACGAGTCTGGCCTCTTTTTGCAACAAAGTAAAAAAAATCAGAGAAAGATATCATGCA
GCTGATGTTAATTTCAATTCTGGGAAGATCTGGAGCACTACTACAGCATTTCCGTATCAG
CTCTTTTCTAAGACCAAGTTTAATATACATATTTTTATTGATAACTCAACACAACCTCTT
CATTTTATGCCATGTGCTAATTATCTTGTCAAAGATCTAATTGCAGAAATTCTGCATTTT
TGCACAAATGACCAGCTACTCCCCAAAGATCATATTCTAAGTGTATGTGGCTCTGAAGAA
TTTTTACAAAACGACCACTGTTTGGGGAGCCACAAAATGTTTCAAAAAGATAAATCTGTT
ATTCAGCTCCACCTGCAGAAAAGTAGGGAAGCTCCAGGAAAGCTATCTCGAAAGCATGAA
GAGGACCACAGTCAGTTTTATCTGAATCAACTTCTAGAATTTATGCATATTTGGAAAGTA
TCCAGACAATGTCTCTTAACACTCATCAGAAAATATGACTTCCACCTGAAATACCTATTG
AAAACCCAGGAAAACGTGTATAATATTATTGAAGAAGTTAAAAAAATATGCAGTGTTCTA
GGGTGTGTGGAAACCAAACAAATTACAGATGCAGTAAATGAACTAAGTCTAATTCTTCAG
AGAAAAGGAGAGAATTTTTATCAAAGTTCAGAGACTTCAGCAAAAGGCTTGATAGAGAAG
GTAACAACTGAACTATCCACATCCATCTACCAGCTAATCAATGTCTACTGTAACAGCTTT
TATGCAGATTTTCAGCCTGTAAATGTACCTAGATGCACTTCCTATCTAAATCCCGGGCTT
CCTTCCCACCTCAGCTTCACAGTGTATGCAGCACACAACATTCCAGAAACCTGGGTGCAC
AGGATCAATTTTCCCCTTGAAATAAAGTCACTTCCAAGGGAATCCATGCTCACTGTAAAA
CTGTTTGGGATTGCCTGTGCAACCAACAATGCAAATTTACTGGCGTGGACTTGTCTTCCA
CTGTTTCCAAAAGAAAAATCCATTCTCGGGTCTATGCTGTTCAGCATGACATTACAGAGT
GAGCCTCCCGTAGAAATGATAACTCCAGGAGTGTGGGATGTAAGTCAGCCATCCCCGGTG
ACCCTGCAGATTGATTTTCCAGCTACTGGGTGGGAGTATATGAAACCTGATTCTGAAGAG
AATAGAAGTAATCTTGAAGAGCCACTAAAGGAGTGTATAAAACATATTGCCAGACTTTCA
CAGAAACAGACTCCCCTACTACTCTCTGAAGAAAAGAAAAGATATTTATGGTTTTATCGC
TTCTACTGCAATAATGAAAACTGCTCCCTTCCTTTAGTCCTGGGTAGTGCCCCTGGATGG
GATGAAAGGACTGTTTCAGAAATGCATACCATTTTGAGAAGATGGACATTTTCTCAACCT
TTAGAGGCTCTTGGGCTTTTGACTTCCAGTTTTCCAGATCAAGAAATTCGTAAAGTGGCA
GTTCAACAATTAGACAACCTCTTGAATGATGAACTACTGGAATATCTCCCACAGCTAGTT
CAGGCTGTCAAGTTTGAATGGAACCTTGAGAGTCCTTTAGTGCAACTTCTACTCCACCGC
TCCTTGCAGAGCATCCAGGTTGCCCATCGTCTTTACTGGCTGCTAAAAAATGCAGAAAAT
GAAGCTTATTTTAAAAGCTGGTATCAGAAGCTACTAGCTGCTCTCCAATTCTGTGCAGGT
AAAGCCTTGAATGATGAGTTTTCCAAGGAGCAGAAACTTATCAAAATTCTGGGAGATATT
GGGGAAAGAGTCAAGTCTGCCAGTGACCATCAAAGACAGGAGGTACTGAAGAAAGAAATT
GGCAGACTAGAAGAGTTCTTTCAAGATGTAAATACTTGTCATCTTCCTCTGAACCCTGCC
CTATGTATAAAAGGGATTGATCACGATGCATGTTCATATTTTACATCTAATGCTTTGCCA
TTGAAGATTACTTTCATCAATGCTAATCTGATGGGCAAAAACATCAGCATTATTTTTAAG
GCTGGAGATGATCTTCGTCAGGATATGCTTGTTCTGCAGCTTATTCAAGTGATGGACAAT
ATTTGGCTGCAGGAAGGCTTGGATATGCAAATGATCATTTATAGATGTCTATCCACAGGA
AAAGACCAAGGATTGGTGCAGATGGTACCTGATGCTGTGACCCTAGCAAAGATTCATCGC
CATTCTGGACTGATAGGACCATTGAAAGAAAATACAATTAAAAAGTGGTTCAGTCAGCAC
AACCACTTAAAGGCAGATTATGAAAAGGCCTTGAGGAACTTTTTCTACTCCTGTGCTGGC
TGGTGTGTGGTAACATTCATCCTGGGAGTATGTGACCGTCACAATGATAATATCATGCTG
ACAAAGTCGGGCCACATGTTTCATATTGACTTTGGAAAATTCTTAGGTCATGCACAAACA
TTTGGAGGGATAAAAAGGGACCGAGCTCCTTTCATTTTTACTTCAGAGATGGAATACTTT
ATTACAGAGGGTGGGAAAAACCCACAGCATTTTCAAGATTTTGTGGAACTTTGCTGTCGT
GCTTATAATATTATCAGAAAGCACAGCCAACTGCTCTTGAACCTGCTGGAAATGATGCTG
TATGCAGGACTGCCTGAGCTAAGTGGAATTCAAGACCTGAAATATGTGTATAATAATCTT
CGTCCACAAGACACAGACCTGGAAGCAACAAGTCATTTTACCAAGAAAATAAAGGAAAGT
CTGGAGTGTTTCCCTGTTAAATTGAATAACTTGATCCACACACTTGCACAAATGTCAGCC
ATAAGCCCTGCCAAATCTACTTCACAGACTTTTCCTCAGGAATCCTGTTTGCTGAGTACA
ACTAGGTCGATTGAAAGAGCAACAATTTTAGGGTTCAGCAAGAAATCCAGTAATCTGTAT
CTGATCCAGGTGACACACAGCAACAACGAAACAAGCCTGACAGAAAAATCATTTGAGCAG
TTTTCAAAACTTCACAGCCAACTTCAGAAGCAGTTTGCATCACTGACTCTCCCAGAGTTT
CCTCATTGGTGGCACCTACCTTTTACAAATTCAGATCACAGAAGATTCAGAGATCTAAAT
CATTACATGGAACAGATATTAAATGTATCACATGAAGTTACAAACAGTGATTGTGTACTT
AGCTTTTTCCTCTCTGAGGCTGTGCAACAAACAGTTGAAGAATCATCACCTGTGTACCTA
GGTGAGAAGTTTCCAGACAAGAAGCCTAAGGTGCAGTTAGTCATATCCTACGAGGATGTG
AAGCTGACCATACTAGTGAAACACATGAAAAACATTCATCTCCCAGATGGCTCTGCGCCC
AGTGCACATGTTGAATTTTATCTTTTACCATATCCCAGTGAAGTTCGTAGGAGGAAAACA
AAATCTGTTCCAAAATGTACGGACCCAACTTACAATGAAATTGTAGTATATGATGAAGTC
ACAGAGCTCCAAGGACATGTCTTAATGCTTATTGTGAAGAGTAAAACTGTATTTGTGGGA
GCAATTAACATCCGACTCTGTAGTGTCCCACTCGATAAAGAAAAATGGTATCCATTAGGA
AACAGTATAATTTGA
|
| Enzyme 100 GenBank Gene ID |
BC130277 |
| Enzyme 100 GeneCard ID |
PIK3C2G |
| Enzyme 100 GenAtlas ID |
PIK3C2G |
| Enzyme 100 HGNC ID |
HGNC:8973 |
| Enzyme 100 Chromosome Location |
1 |
| Enzyme 100 Locus |
12p12 |
| Enzyme 100 SNPs |
SNPJam Report |
| Enzyme 100 General References |
- Rozycka M, Lu YJ, Brown RA, Lau MR, Shipley JM, Fry MJ: cDNA cloning of a third human C2-domain-containing class II phosphoinositide 3-kinase, PI3K-C2gamma, and chromosomal assignment of this gene (PIK3C2G) to 12p12. Genomics. 1998 Dec 15;54(3):569-74. [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 ]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
|
| Enzyme 100 Metabolite References |
Not Available |
|
Enzyme 101
[top]
|
| Enzyme 101 ID |
6437 |
| Enzyme 101 Name |
Mitogen-activated protein kinase kinase kinase kinase 3 |
| Enzyme 101 Synonyms |
- Germinal center kinase-related protein kinase
- GLK
- MAPK/ERK kinase kinase kinase 3
- MEK kinase kinase 3
- MEKKK 3
|
| Enzyme 101 Gene Name |
MAP4K3 |
| Enzyme 101 Protein Sequence |
>Mitogen-activated protein kinase kinase kinase kinase 3
MNPGFDLSRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQ
EIIMMKDCKHPNIVAYFGSYLRRDKLWICMEFCGGGSLQDIYHVTGPLSELQIAYVSRET
LQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSFIGTPYWMAP
EVAAVERKGGYNQLCDLWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLKDKM
KWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFVTQHLTRSLAIELLDKVNNPDHSTYHDF
DDDDPEPLVAVPHRIHSTSRNVREEKTRSEITFGQVKFDPPLRKETEPHHELPDSDGFLD
SSEEIYYTARSNLDLQLEYGQGHQGGYFLGANKSLLKSVEEELHQRGHVAHLEDDEGDDD
ESKHSTLKAKIPPPLPPKPKSIFIPQEMHSTEDENQGTIKRCPMSGSPAKPSQVPPRPPP
PRLPPHKPVALGNGMSSFQLNGERDGSLCQQQNEHRGTNLSRKEKKDVPKPISNGLPPTP
KVHMGACFSKVFNGCPLKIHCASSWINPDTRDQYLIFGAEEGIYTLNLNELHETSMEQLF
PRRCTWLYVMNNCLLSISGKASQLYSHNLPGLFDYARQMQKLPVAIPAHKLPDRILPRKF
SVSAKIPETKWCQKCCVVRNPYTGHKYLCGALQTSIVLLEWVEPMQKFMLIKHIDFPIPC
PLRMFEMLVVPEQEYPLVCVGVSRGRDFNQVVRFETVNPNSTSSWFTESDTPQTNVTHVT
QLERDTILVCLDCCIKIVNLQGRLKSSRKLSSELTFDFQIESIVCLQDSVLAFWKHGMQG
RSFRSNEVTQEISDSTRIFRLLGSDRVVVLESRPTDNPTANSNLYILAGHENSY
|
| Enzyme 101 Number of Residues |
894 |
| Enzyme 101 Molecular Weight |
101315.1 |
| Enzyme 101 Theoretical pI |
7.60 |
| Enzyme 101 GO Classification |
| Function |
- ATP binding
- GTPase regulator activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- enzyme regulator activity
- kinase activity
- nucleoside binding
- nucleoside-triphosphatase regulator activity
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- small GTPase regulator activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 101 General Function |
Involved in small GTPase regulator activity |
| Enzyme 101 Specific Function |
May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway |
| Enzyme 101 Pathways |
Not Available |
| Enzyme 101 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 101 Pfam Domain Function |
|
| Enzyme 101 Signals |
|
| Enzyme 101 Transmembrane Regions |
|
| Enzyme 101 Essentiality |
Not Available |
| Enzyme 101 GenBank ID Protein |
15451902 |
| Enzyme 101 UniProtKB/Swiss-Prot ID |
Q8IVH8 |
| Enzyme 101 UniProtKB/Swiss-Prot Entry Name |
M4K3_HUMAN |
| Enzyme 101 PDB ID |
Not Available |
| Enzyme 101 Cellular Location |
Not Available |
| Enzyme 101 Gene Sequence |
>2685 bp
ATGAACCCCGGCTTCGATTTGTCCCGCCGGAACCCGCAGGAGGACTTCGAGCTGATTCAG
CGCATCGGCAGCGGCACCTACGGCGACGTCTACAAGGCACGGAATGTTAACACTGGTGAA
TTAGCAGCAATTAAAGTAATAAAATTGGAACCAGGAGAAGACTTTGCAGTTGTGCAGCAA
GAAATTATTATGATGAAAGACTGTAAACACCCAAATATTGTTGCTTATTTTGGAAGCTAT
CTCAGGCGAGATAAGCTTTGGATTTGCATGGAGTTTTGTGGAGGTGGTTCTTTACAGGAT
ATTTATCACGTAACTGGACCTCTGTCAGAACTGCAAATTGCATATGTTAGCAGAGAAACA
CTGCAGGGATTATATTATCTTCACAGTAAAGGAAAAATGCACAGAGATATAAAGGGAGCT
AACATTCTATTAACGGATAATGGTCATGTGAAATTGGCTGATTTTGGAGTATCTGCACAG
ATAACAGCTACAATTGCCAAACGGAAGTCTTTCATTGGCACACCATATTGGATGGCTCCA
GAAGTTGCAGCTGTTGAGAGGAAGGGGGGTTACAATCAACTCTGTGATCTCTGGGCAGTG
GGAATCACTGCCATAGAACTTGCAGAGCTTCAGCCTCCTATGTTTGACTTACACCCAATG
AGAGCATTATTTCTAATGACAAAAAGCAATTTTCAGCCTCCTAAACTAAAGGATAAAATG
AAATGGTCAAATAGTTTTCATCACTTTGTGAAAATGGCACTTACCAAAAATCCGAAAAAA
AGACCTACTGCTGAAAAATTATTACAGCATCCTTTTGTAACACAACATTTGACACGGTCT
TTGGCAATCGAGCTGTTGGATAAAGTAAATAATCCAGATCATTCCACTTACCATGATTTC
GATGATGATGATCCTGAGCCTCTTGTTGCTGTACCACATAGAATTCACTCAACAAGTAGA
AACGTGAGAGAAGAAAAAACACGCTCAGAGATAACCTTTGGCCAAGTGAAATTTGATCCA
CCCTTAAGAAAGGAGACAGAACCACATCATGAACTTCCCGACAGTGATGGTTTTTTGGAC
AGTTCAGAAGAAATATACTACACTGCAAGATCTAATCTGGATCTGCAACTGGAATATGGA
CAAGGACACCAAGGTGGTTACTTTTTAGGTGCAAACAAGAGTCTTCTCAAGTCTGTTGAA
GAAGAATTGCATCAGCGAGGACACGTCGCACATTTAGAAGATGATGAAGGAGATGATGAT
GAATCTAAACACTCAACTCTGAAAGCAAAAATTCCACCTCCTTTGCCACCAAAGCCTAAG
TCTATCTTCATACCACAGGAAATGCATTCTACTGAGGATGAAAATCAAGGAACAATCAAG
AGATGTCCCATGTCAGGGAGCCCAGCAAAGCCATCCCAAGTTCCACCTAGACCACCACCT
CCCAGATTACCCCCACACAAACCTGTTGCCTTAGGAAATGGAATGAGCTCCTTCCAGTTA
AATGGTGAACGAGATGGCTCATTATGTCAACAACAGAATGAACATAGAGGCACAAACCTT
TCAAGAAAAGAAAAGAAAGATGTACCAAAGCCTATTAGTAATGGTCTTCCTCCAACACCT
AAAGTGCATATGGGTGCATGTTTTTCAAAAGTTTTTAATGGGTGTCCCTTGAAAATTCAC
TGTGCATCATCATGGATAAACCCAGATACAAGAGATCAGTACTTGATATTTGGTGCCGAA
GAAGGGATTTATACCCTCAATCTTAATGAACTTCATGAAACATCAATGGAACAGCTATTC
CCTCGAAGGTGTACATGGTTGTATGTAATGAACAATTGCTTGCTATCAATATCTGGTAAA
GCTTCTCAGCTTTATTCCCATAATTTACCAGGGCTTTTTGATTATGCAAGACAAATGCAA
AAGTTACCTGTTGCTATTCCAGCACACAAACTCCCTGACAGAATACTGCCAAGGAAATTT
TCTGTATCAGCAAAAATCCCTGAAACCAAATGGTGCCAGAAGTGTTGTGTTGTAAGAAAT
CCTTACACGGGCCATAAATACCTATGTGGAGCACTTCAGACTAGCATTGTTCTATTAGAA
TGGGTTGAACCAATGCAGAAATTTATGTTAATTAAGCACATAGATTTTCCTATACCATGT
CCACTTAGAATGTTTGAAATGCTGGTAGTTCCTGAACAGGAGTACCCTTTAGTTTGTGTT
GGTGTCAGTAGAGGTAGAGACTTCAACCAAGTGGTTCGATTTGAGACGGTCAATCCAAAT
TCTACCTCTTCATGGTTTACAGAATCAGATACCCCACAGACAAATGTTACTCATGTAACC
CAACTGGAGAGAGATACCATCCTTGTATGCTTGGACTGTTGTATAAAAATAGTAAATCTC
CAAGGAAGATTAAAATCTAGCAGGAAATTGTCATCAGAACTCACCTTTGATTTCCAGATT
GAATCAATAGTGTGCCTACAAGACAGTGTGCTAGCTTTCTGGAAACATGGAATGCAAGGT
AGAAGTTTTAGATCTAATGAGGTAACACAAGAAATTTCAGATAGCACAAGAATTTTCAGG
CTGCTTGGATCTGACAGGGTCGTGGTTTTGGAAAGTAGGCCAACTGATAACCCCACAGCA
AATAGCAATTTGTACATCCTGGCGGGTCATGAAAACAGTTACTGA
|
| Enzyme 101 GenBank Gene ID |
NM_003618.2 |
| Enzyme 101 GeneCard ID |
MAP4K3 |
| Enzyme 101 GenAtlas ID |
MAP4K3 |
| Enzyme 101 HGNC ID |
HGNC:6865 |
| Enzyme 101 Chromosome Location |
2 |
| Enzyme 101 Locus |
2p22.1 |
| Enzyme 101 SNPs |
SNPJam Report |
| Enzyme 101 General References |
- Diener K, Wang XS, Chen C, Meyer CF, Keesler G, Zukowski M, Tan TH, Yao Z: Activation of the c-Jun N-terminal kinase pathway by a novel protein kinase related to human germinal center kinase. Proc Natl Acad Sci U S A. 1997 Sep 2;94(18):9687-92. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 101 Metabolite References |
Not Available |
|
Enzyme 102
[top]
|
| Enzyme 102 ID |
6438 |
| Enzyme 102 Name |
Mitogen-activated protein kinase kinase kinase 3 |
| Enzyme 102 Synonyms |
- MAPK/ERK kinase kinase 3
- MEK kinase 3
- MEKK 3
|
| Enzyme 102 Gene Name |
MAP3K3 |
| Enzyme 102 Protein Sequence |
>Mitogen-activated protein kinase kinase kinase 3
MDEQEALNSIMNDLVALQMNRRHRMPGYETMKNKDTGHSNRQSDVRIKFEHNGERRIIAF
SRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILL
LSQDRNHNSSSPHSGVSRQVRIKASQSAGDINTIYQPPEPRSRHLSVSSQNPGRSSPPPG
YVPERQQHIARQGSYTSINSEGEFIPETSEQCMLDPLSSAENSLSGSCQSLDRSADSPSF
RKSRMSRAQSFPDNRQEYSDRETQLYDKGVKGGTYPRRYHVSVHHKDYSDGRRTFPRIRR
HQGNLFTLVPSSRSLSTNGENMGLAVQYLDPRGRLRSADSENALSVQERNVPTKSPSAPI
NWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQ
HERIVQYYGCLRDRAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYL
HSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGMRSVTGTPYWMSPEVIS
GEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFL
RRIFVEARQRPSAEELLTHHFAQLMY
|
| Enzyme 102 Number of Residues |
626 |
| Enzyme 102 Molecular Weight |
70897.1 |
| Enzyme 102 Theoretical pI |
9.09 |
| Enzyme 102 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 102 General Function |
Involved in protein serine/threonine kinase activity |
| Enzyme 102 Specific Function |
Component of a protein kinase signal transduction cascade. Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators |
| Enzyme 102 Pathways |
Not Available |
| Enzyme 102 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 102 Pfam Domain Function |
|
| Enzyme 102 Signals |
|
| Enzyme 102 Transmembrane Regions |
|
| Enzyme 102 Essentiality |
Not Available |
| Enzyme 102 GenBank ID Protein |
42794765 |
| Enzyme 102 UniProtKB/Swiss-Prot ID |
Q99759 |
| Enzyme 102 UniProtKB/Swiss-Prot Entry Name |
M3K3_HUMAN |
| Enzyme 102 PDB ID |
Not Available |
| Enzyme 102 Cellular Location |
Not Available |
| Enzyme 102 Gene Sequence |
>1881 bp
ATGGACGAACAGGAGGCATTGAACTCAATCATGAACGATCTGGTGGCCCTCCAGATGAAC
CGACGTCACCGGATGCCTGGATATGAGACCATGAAGAACAAAGACACAGGTCACTCAAAT
AGGCAGAGTGACGTCAGAATCAAGTTCGAGCACAACGGGGAGAGGCGAATTATAGCGTTC
AGCCGGCCTGTGAAATATGAAGATGTGGAGCACAAGGTGACAACAGTATTTGGACAACCT
CTTGATCTACATTACATGAACAATGAGCTCTCCATCCTGCTGAAAAACCAAGATGATCTT
GATAAAGCAATTGACATTTTAGATAGAAGCTCAAGCATGAAAAGCCTTAGGATATTGCTG
TTGTCCCAGGACAGAAACCATAACAGTTCCTCTCCCCACTCTGGGGTGTCCAGACAGGTG
CGGATCAAGGCTTCCCAGTCCGCAGGGGATATAAATACTATCTACCAGCCCCCCGAGCCC
AGAAGCAGGCACCTCTCTGTCAGCTCCCAGAACCCTGGCCGAAGCTCACCTCCCCCTGGC
TATGTTCCTGAGCGGCAGCAGCACATTGCCCGGCAGGGGTCCTACACCAGCATCAACAGT
GAGGGGGAGTTCATCCCAGAGACCAGCGAGCAGTGCATGCTGGATCCCCTGAGCAGTGCA
GAAAATTCCTTGTCTGGAAGCTGCCAATCCTTGGACAGGTCAGCAGACAGCCCATCCTTC
CGGAAATCACGAATGTCCCGTGCCCAGAGCTTCCCTGACAACAGACAGGAATACTCAGAT
CGGGAAACTCAGCTTTATGACAAAGGGGTCAAAGGTGGAACCTACCCCCGGCGCTACCAC
GTGTCTGTGCACCACAAGGACTACAGTGATGGCAGAAGAACATTTCCCCGAATACGGCGT
CATCAAGGCAACTTGTTCACCCTGGTGCCCTCCAGCCGCTCCCTGAGCACAAATGGCGAG
AACATGGGTCTGGCTGTGCAATACCTGGACCCCCGTGGGCGCCTGCGGAGTGCGGACAGC
GAGAATGCCCTCTCTGTGCAGGAGAGGAATGTGCCAACCAAGTCTCCCAGTGCCCCCATC
AACTGGCGCCGGGGAAAGCTCCTGGGCCAGGGTGCCTTCGGCAGGGTCTATTTGTGCTAT
GACGTGGACACGGGACGTGAACTTGCTTCCAAGCAGGTCCAATTTGATCCAGACAGTCCT
GAGACAAGCAAGGAGGTGAGTGCTCTGGAGTGCGAGATCCAGTTGCTAAAGAACTTGCAG
CATGAGCGCATCGTGCAGTACTATGGCTGTCTGCGGGACCGCGCTGAGAAGACCCTGACC
ATCTTCATGGAGTACATGCCAGGGGGCTCGGTGAAAGACCAGTTGAAGGCTTACGGTGCT
CTGACAGAGAGCGTGACCCGAAAGTACACGCGGCAGATCCTGGAGGGCATGTCCTACCTG
CACAGCAACATGATTGTTCACCGGGACATTAAGGGAGCCAACATCCTCCGAGACTCTGCT
GGGAATGTAAAGCTGGGGGACTTTGGGGCCAGCAAACGCCTGCAGACGATCTGTATGTCG
GGGACGGGCATGCGCTCCGTCACTGGCACACCCTACTGGATGAGCCCTGAGGTGATCAGC
GGCGAGGGCTATGGAAGGAAAGCAGACGTGTGGAGCCTGGGCTGCACTGTGGTGGAGATG
CTGACAGAGAAACCACCGTGGGCAGAGTATGAAGCTATGGCCGCCATCTTCAAGATTGCC
ACCCAGCCCACCAATCCTCAGCTGCCCTCCCACATCTCTGAACATGGCCGGGACTTCCTG
AGGCGCATTTTTGTGGAGGCTCGCCAGAGACCTTCAGCTGAGGAGCTGCTCACACACCAC
TTTGCACAGCTCATGTACTGA
|
| Enzyme 102 GenBank Gene ID |
NM_002401.3 |
| Enzyme 102 GeneCard ID |
MAP3K3 |
| Enzyme 102 GenAtlas ID |
MAP3K3 |
| Enzyme 102 HGNC ID |
HGNC:6855 |
| Enzyme 102 Chromosome Location |
1 |
| Enzyme 102 Locus |
17q23.3 |
| Enzyme 102 SNPs |
SNPJam Report |
| Enzyme 102 General References |
- Ellinger-Ziegelbauer H, Brown K, Kelly K, Siebenlist U: Direct activation of the stress-activated protein kinase (SAPK) and extracellular signal-regulated protein kinase (ERK) pathways by an inducible mitogen-activated protein Kinase/ERK kinase kinase 3 (MEKK) derivative. J Biol Chem. 1997 Jan 31;272(5):2668-74. [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 ]
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Nakamura K, Johnson GL: PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain for activation of the ERK5 pathway. J Biol Chem. 2003 Sep 26;278(39):36989-92. Epub 2003 Aug 11. [PubMed ]
- Huang Q, Yang J, Lin Y, Walker C, Cheng J, Liu ZG, Su B: Differential regulation of interleukin 1 receptor and Toll-like receptor signaling by MEKK3. Nat Immunol. 2004 Jan;5(1):98-103. Epub 2003 Dec 7. [PubMed ]
- Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G: A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. Nat Cell Biol. 2004 Feb;6(2):97-105. Epub 2004 Jan 25. [PubMed ]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 102 Metabolite References |
Not Available |
|
Enzyme 103
[top]
|
| Enzyme 103 ID |
6439 |
| Enzyme 103 Name |
Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform |
| Enzyme 103 Synonyms |
- PI3-kinase subunit delta
- PI3K-delta
- PtdIns-3-kinase subunit delta
- Phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta
- PtdIns-3-kinase subunit p110-delta
|
| Enzyme 103 Gene Name |
PIK3CD |
| Enzyme 103 Protein Sequence |
>Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform
MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFH
MLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLL
IGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGP
GTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYT
LQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPR
AKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSS
SEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAW
ANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAP
HPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQE
HFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSL
RKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSV
ALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMR
QEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKN
GDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLN
KSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIM
IRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYC
ERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFN
EALRESWKTKVNWLAHNVSKDNRQ
|
| Enzyme 103 Number of Residues |
1044 |
| Enzyme 103 Molecular Weight |
119478.1 |
| Enzyme 103 Theoretical pI |
7.18 |
| Enzyme 103 GO Classification |
| Function |
- 1-phosphatidylinositol-3-kinase activity
- binding
- catalytic activity
- inositol or phosphatidylinositol kinase activity
- kinase activity
- lipid kinase activity
- phosphatidylinositol-4,5-bisphosphate 3-kinase activity
- phosphoinositide 3-kinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biological regulation
- glycerophospholipid metabolic process
- intracellular signal transduction
- metabolic process
- organophosphate metabolic process
- phosphoinositide metabolic process
- phosphoinositide phosphorylation
- phosphoinositide-mediated signaling
- phospholipid metabolic process
- regulation of biological process
- regulation of cellular process
- second-messenger-mediated signaling
- signal transduction
|
| Component |
- macromolecular complex
- phosphoinositide 3-kinase complex
- protein complex
|
|
| Enzyme 103 General Function |
Involved in binding |
| Enzyme 103 Specific Function |
ATP + 1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5- trisphosphate |
| Enzyme 103 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 103 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate [RN:R04545]
|
| Enzyme 103 Pfam Domain Function |
|
| Enzyme 103 Signals |
|
| Enzyme 103 Transmembrane Regions |
|
| Enzyme 103 Essentiality |
Not Available |
| Enzyme 103 GenBank ID Protein |
37496959 |
| Enzyme 103 UniProtKB/Swiss-Prot ID |
O00329 |
| Enzyme 103 UniProtKB/Swiss-Prot Entry Name |
PK3CD_HUMAN |
| Enzyme 103 PDB ID |
Not Available |
| Enzyme 103 Cellular Location |
Not Available |
| Enzyme 103 Gene Sequence |
>3135 bp
ATGCCCCCTGGGGTGGACTGCCCCATGGAATTCTGGACCAAGGAGGAGAATCAGAGCGTT
GTGGTTGACTTCCTGCTGCCCACAGGGGTCTACCTGAACTTCCCTGTGTCCCGCAATGCC
AACCTCAGCACCATCAAGCAGCTGCTGTGGCACCGCGCCCAGTATGAGCCGCTCTTCCAC
ATGCTCAGTGGCCCCGAGGCCTATGTGTTCACCTGCATCAACCAGACAGCGGAGCAGCAA
GAGCTGGAGGACGAGCAACGGCGTCTGTGTGACGTGCAGCCCTTCCTGCCCGTCCTGCGC
CTGGTGGCCCGTGAGGGCGACCGCGTGAAGAAGCTCATCAACTCACAGATCAGCCTCCTC
ATCGGCAAAGGCCTCCACGAGTTTGACTCCTTGTGCGACCCAGAAGTGAACGACTTTCGC
GCCAAGATGTGCCAATTCTGCGAGGAGGCGGCCGCCCGCCGGCAGCAGCTGGGCTGGGAG
GCCTGGCTGCAGTACAGTTTCCCCCTGCAGCTGGAGCCCTCGGCTCAAACCTGGGGGCCT
GGTACCCTGCGGCTCCCGAACCGGGCCCTTCTGGTCAACGTTAAGTTTGAGGGCAGCGAG
GAGAGCTTCACCTTCCAGGTGTCCACCAAGGACGTGCCGCTGGCGCTGATGGCCTGTGCC
CTGCGGAAGAAGGCCACAGTGTTCCGGCAGCCGCTGGTGGAGCAGCCGGAAGACTACACG
CTGCAGGTGAACGGCAGGCATGAGTACCTGTATGGCAGCTACCCGCTCTGCCAGTTCCAG
TACATCTGCAGCTGCCTGCACAGTGGGTTGACCCCTCACCTGACCATGGTCCATTCCTCC
TCCATCCTCGCCATGCGGGATGAGCAGAGCAACCCTGCCCCCCAGGTCCAGAAACCGCGT
GCCAAACCACCTCCCATTCCTGCGAAGAAGCCTTCCTCTGTGTCCCTGTGGTCCCTGGAG
CAGCCGTTCCGCATCGAGCTCATCCAGGGCAGCAAAGTGAACGCCGACGAGCGGATGAAG
CTGGTGGTGCAGGCCGGGCTTTTCCACGGCAACGAGATGCTGTGCAAGACGGTGTCCAGC
TCGGAGGTGAGCGTGTGCTCGGAGCCCGTGTGGAAGCAGCGGCTGGAGTTCGACATCAAC
ATCTGCGACCTGCCCCGCATGGCCCGTCTCTGCTTTGCGCTGTACGCCGTGATCGAGAAA
GCCAAGAAGGCTCGCTCCACCAAGAAGAAGTCCAAGAAGGCGGACTGCCCCATTGCCTGG
GCCAACCTCATGCTGTTTGACTACAAGGACCAGCTTAAGACCGGGGAACGCTGCCTCTAC
ATGTGGCCCTCCGTCCCAGATGAGAAGGGCGAGCTGCTGAACCCCACGGGCACTGTGCGC
AGTAACCCCAACACGGATAGCGCCGCTGCCCTGCTCATCTGCCTGCCCGAGGTGGCCCCG
CACCCCGTGTACTACCCCGCCCTGGAGAAGATCTTGGAGCTGGGGCGACACAGCGAGTGT
GTGCATGTCACCGAGGAGGAGCAGCTGCAGCTGCGGGAAATCCTGGAGCGGCGGGGGTCT
GGGGAGCTGTATGAGCACGAGAAGGACCTGGTGTGGAAGCTGCGGCATGAAGTCCAGGAG
CACTTCCCGGAGGCGCTAGCCCGGCTGCTGCTGGTCACCAAGTGGAACAAGCATGAGGAT
GTGGCCCAGATGCTCTACCTGCTGTGCTCCTGGCCGGAGCTGCCCGTCCTGAGCGCCCTG
GAGCTGCTAGACTTCAGCTTCCCCGATTGCCACGTAGGCTCCTTCGCCATCAAGTCGCTG
CGGAAACTGACGGACGATGAGCTGTTCCAGTACCTGCTGCAGCTGGTGCAGGTGCTCAAG
TACGAGTCCTACCTGGACTGCGAGCTGACCAAATTCCTGCTGGACCGGGCCCTGGCCAAC
CGCAAGATCGGCCACTTCCTTTTCTGGCACCTCCGCTCCGAGATGCACGTGCCGTCGGTG
GCCCTGCGCTTCGGCCTCATCCTGGAGGCCTACTGCAGGGGCAGCACCCACCACATGAAG
GTGCTGATGAAGCAGGGGGAAGCACTGAGCAAACTGAAGGCCCTGAATGACTTCGTCAAG
CTGAGCTCTCAGAAGACCCCCAAGCCCCAGACCAAGGAGCTGATGCACTTGTGCATGCGG
CAGGAGGCCTACCTAGAGGCCCTCTCCCACCTGCAGTCCCCACTCGACCCCAGCACCCTG
CTGGCTGAAGTCTGCGTGGAGCAGTGCACCTTCATGGACTCCAAGATGAAGCCCCTGTGG
ATCATGTACAGCAACGAGGAGGCAGGCAGCGGCGGCAGCGTGGGCATCATCTTTAAGAAC
GGGGATGACCTCCGGCAGGACATGCTGACCCTGCAGATGATCCAGCTCATGGACGTCCTG
TGGAAGCAGGAGGGGCTGGACCTGAGGATGACCCCCTATGGCTGCCTCCCCACCGGGGAC
CGCACAGGCCTCATTGAGGTGGTACTCCGTTCAGACACCATCGCCAACATCCAACTCAAC
AAGAGCAACATGGCAGCCACAGCCGCCTTCAACAAGGATGCCCTGCTCAACTGGCTGAAG
TCCAAGAACCCGGGGGAGGCCCTGGATCGAGCCATTGAGGAGTTCACCCTCTCCTGTGCT
GGCTATTGTGTGGCCACATATGTGCTGGGCATTGGCGATCGGCACAGCGACAACATCATG
ATCCGAGAGAGTGGGCAGCTGTTCCACATTGATTTTGGCCACTTTCTGGGGAATTTCAAG
ACCAAGTTTGGAATCAACCGCGAGCGTGTCCCATTCATCCTCACCTACGACTTTGTCCAT
GTGATTCAGCAGGGGAAGACTAATAATAGTGAGAAATTTGAACGGTTCCGGGGCTACTGT
GAAAGGGCCTACACCATCCTGCGGCGCCACGGGCTTCTCTTCCTCCACCTCTTTGCCCTG
ATGCGGGCGGCAGGCCTGCCTGAGCTCAGCTGCTCCAAAGACATCCAGTATCTCAAGGAC
TCCCTGGCACTGGGGAAAACAGAGGAGGAGGCACTGAAGCACTTCCGAGTGAAGTTTAAC
GAAGCCCTCCGTGAGAGCTGGAAAACCAAAGTGAACTGGCTGGCCCACAACGTGTCCAAA
GACAACAGGCAGTAG
|
| Enzyme 103 GenBank Gene ID |
Y10055 |
| Enzyme 103 GeneCard ID |
PIK3CD |
| Enzyme 103 GenAtlas ID |
PIK3CD |
| Enzyme 103 HGNC ID |
HGNC:8977 |
| Enzyme 103 Chromosome Location |
1 |
| Enzyme 103 Locus |
1p36.2 |
| Enzyme 103 SNPs |
SNPJam Report |
| Enzyme 103 General References |
- Vanhaesebroeck B, Welham MJ, Kotani K, Stein R, Warne PH, Zvelebil MJ, Higashi K, Volinia S, Downward J, Waterfield MD: P110delta, a novel phosphoinositide 3-kinase in leukocytes. Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4330-5. [PubMed ]
- Chantry D, Vojtek A, Kashishian A, Holtzman DA, Wood C, Gray PW, Cooper JA, Hoekstra MF: p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes. J Biol Chem. 1997 Aug 1;272(31):19236-41. [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 ]
- Vanhaesebroeck B, Higashi K, Raven C, Welham M, Anderson S, Brennan P, Ward SG, Waterfield MD: Autophosphorylation of p110delta phosphoinositide 3-kinase: a new paradigm for the regulation of lipid kinases in vitro and in vivo. EMBO J. 1999 Mar 1;18(5):1292-302. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
|
| Enzyme 103 Metabolite References |
Not Available |
|
Enzyme 104
[top]
|
| Enzyme 104 ID |
6440 |
| Enzyme 104 Name |
Death-associated protein kinase 3 |
| Enzyme 104 Synonyms |
- DAP kinase 3
- DAP-like kinase
- Dlk
- ZIP-kinase
|
| Enzyme 104 Gene Name |
DAPK3 |
| Enzyme 104 Protein Sequence |
>Death-associated protein kinase 3
MSTFRQEDVEDHYEMGEELGSGQFAIVRKCRQKGTGKEYAAKFIKKRRLSSSRRGVSREE
IEREVNILREIRHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFL
KQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIFGT
PEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEY
FSNTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKAIRRRNVRGEDSGRKPERRRLKTT
RLKEYTIKSHSSLPPNNSYADFERFSKVLEEAAAAEEGLRELQRSRRLCHEDVEALAAIY
EEKEAWYREESDSLGQDLRRLRQELLKTEALKRQAQEEAKGALLGTSGLKRRFSRLENRY
EALAKQVASEMRFVQDLVRALEQEKLQGVECGLR
|
| Enzyme 104 Number of Residues |
454 |
| Enzyme 104 Molecular Weight |
52535.2 |
| Enzyme 104 Theoretical pI |
6.87 |
| Enzyme 104 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 104 General Function |
Involved in protein kinase activity |
| Enzyme 104 Specific Function |
Serine/threonine kinase which acts as a positive regulator of apoptosis. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis. Regulates myosin light chain phosphatase through phosphorylation of MYPT1 thereby regulating the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. Involved in the formation of promyelocytic leukemia protein nuclear body (PML-NB), one of many subnuclear domains in the eukaryotic cell nucleus, and which is involved in oncogenesis and viral infection |
| Enzyme 104 Pathways |
Not Available |
| Enzyme 104 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 104 Pfam Domain Function |
|
| Enzyme 104 Signals |
|
| Enzyme 104 Transmembrane Regions |
|
| Enzyme 104 Essentiality |
Not Available |
| Enzyme 104 GenBank ID Protein |
Not Available |
| Enzyme 104 UniProtKB/Swiss-Prot ID |
O43293 |
| Enzyme 104 UniProtKB/Swiss-Prot Entry Name |
DAPK3_HUMAN |
| Enzyme 104 PDB ID |
Not Available |
| Enzyme 104 Cellular Location |
Not Available |
| Enzyme 104 Gene Sequence |
>1365 bp
ATGTCCACGTTCAGGCAGGAGGACGTGGAGGACCATTATGAGATGGGGGAGGAGCTGGGC
AGCGGCCAGTTTGCGATCGTGCGGAAGTGCCGGCAGAAGGGCACGGGCAAGGAGTACGCA
GCCAAGTTCATCAAGAAGCGCCGCCTGTCATCCAGCCGGCGTGGGGTGAGCCGGGAGGAG
ATCGAGCGGGAGGTGAACATCCTGCGGGAGATCCGGCACCCCAACATCATCACCCTGCAC
GACATCTTCGAGAACAAGACGGACGTGGTCCTCATCCTGGAGCTGGTCTCTGGCGGGGAG
CTCTTTGACTTCCTGGCGGAGAAAGAGTCGCTGACGGAGGACGAGGCCACCCAGTTCCTC
AAGCAGATCCTGGACGGCGTTCACTACCTGCACTCTAAGCGCATCGCACACTTTGACCTG
AAGCCGGAAAACATCATGCTGCTGGACAAGAACGTGCCCAACCCACGAATCAAGCTCATC
GACTTCGGCATCGCGCACAAGATCGAGGCGGGGAACGAGTTCAAGAACATCTTCGGCACC
CCGGAGTTTGTGGCCCCAGAGATTGTGAACTATGAGCCGCTGGGCCTGGAGGCGGACATG
TGGAGCATCGGTGTCATCACCTATATCCTCCTGAGCGGTGCATCCCCGTTCCTGGGCGAG
ACCAAGCAGGAGACGCTCACCAACATCTCAGCCGTGAACTACGACTTCGACGAGGAGTAC
TTCAGCAACACCAGCGAGCTGGCCAAGGACTTCATTCGCCGGCTGCTCGTCAAAGATCCC
AAGCGGAGAATGACCATTGCCCAGAGCCTGGAACATTCCTGGATTAAGGCGATCCGGCGG
CGGAACGTGCGTGGTGAGGACAGCGGCCGCAAGCCCGAGCGGCGGCGCCTGAAGACCACG
CGTCTGAAGGAGTACACCATCAAGTCGCACTCCAGCTTGCCGCCCAACAACAGCTACGCC
GACTTCGAGCGCTTCTCCAAGGTGCTGGAGGAGGCGGCGGCCGCCGAGGAGGGCCTGCGC
GAGCTGCAGCGCAGCCGGCGGCTCTGCCACGAGGACGTGGAGGCGCTGGCCGCCATCTAC
GAGGAGAAGGAGGCCTGGTACCGCGAGGAGAGCGACAGCCTGGGCCAGGACCTGCGGAGG
CTACGGCAGGAGCTGCTCAAGACCGAGGCGCTCAAGCGGCAGGCGCAGGAGGAGGCCAAG
GGCGCGCTGCTGGGGACCAGCGGCCTCAAGCGCCGCTTCAGCCGCCTGGAGAACCGCTAC
GAGGCGCTGGCCAAGCAAGTAGCCTCCGAGATGCGCTTCGTGCAGGACCTCGTGCGCGCC
CTGGAGCAGGAGAAGCTGCAGGGCGTGGAGTGCGGGCTGCGCTAG
|
| Enzyme 104 GenBank Gene ID |
AB007144 |
| Enzyme 104 GeneCard ID |
DAPK3 |
| Enzyme 104 GenAtlas ID |
DAPK3 |
| Enzyme 104 HGNC ID |
HGNC:2676 |
| Enzyme 104 Chromosome Location |
1 |
| Enzyme 104 Locus |
19p13.3 |
| Enzyme 104 SNPs |
SNPJam Report |
| Enzyme 104 General References |
- Kawai T, Matsumoto M, Takeda K, Sanjo H, Akira S: ZIP kinase, a novel serine/threonine kinase which mediates apoptosis. Mol Cell Biol. 1998 Mar;18(3):1642-51. [PubMed ]
- Murata-Hori M, Suizu F, Iwasaki T, Kikuchi A, Hosoya H: ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells. FEBS Lett. 1999 May 14;451(1):81-4. [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 ]
- Kawai T, Akira S, Reed JC: ZIP kinase triggers apoptosis from nuclear PML oncogenic domains. Mol Cell Biol. 2003 Sep;23(17):6174-86. [PubMed ]
- Preuss U, Landsberg G, Scheidtmann KH: Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase. Nucleic Acids Res. 2003 Feb 1;31(3):878-85. [PubMed ]
- Hagerty L, Weitzel DH, Chambers J, Fortner CN, Brush MH, Loiselle D, Hosoya H, Haystead TA: ROCK1 phosphorylates and activates zipper-interacting protein kinase. J Biol Chem. 2007 Feb 16;282(7):4884-93. Epub 2006 Dec 8. [PubMed ]
- Ohbayashi N, Okada K, Kawakami S, Togi S, Sato N, Ikeda O, Kamitani S, Muromoto R, Sekine Y, Kawai T, Akira S, Matsuda T: Physical and functional interactions between ZIP kinase and UbcH5. Biochem Biophys Res Commun. 2008 Aug 8;372(4):708-12. Epub 2008 Jun 2. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 104 Metabolite References |
Not Available |
|
Enzyme 105
[top]
|
| Enzyme 105 ID |
6441 |
| Enzyme 105 Name |
Tyrosine-protein kinase TXK |
| Enzyme 105 Synonyms |
- Protein-tyrosine kinase 4
|
| Enzyme 105 Gene Name |
TXK |
| Enzyme 105 Protein Sequence |
>Tyrosine-protein kinase TXK
MILSSYNTIQSVFCCCCCCSVQKRQMRTQISLSTDEELPEKYTQRRRPWLSQLSNKKQSN
TGRVQPSKRKPLPPLPPSEVAEEKIQVKALYDFLPREPCNLALRRAEEYLILEKYNPHWW
KARDRLGNEGLIPSNYVTENKITNLEIYEWYHRNITRNQAEHLLRQESKEGAFIVRDSRH
LGSYTISVFMGARRSTEAAIKHYQIKKNDSGQWYVAERHAFQSIPELIWYHQHNAAGLMT
RLRYPVGLMGSCLPATAGFSYEKWEIDPSELAFIKEIGSGQFGVVHLGEWRSHIQVAIKA
INEGSMSEEDFIEEAKVMMKLSHSKLVQLYGVCIQRKPLYIVTEFMENGCLLNYLRENKG
KLRKEMLLSVCQDICEGMEYLERNGYIHRDLAARNCLVSSTCIVKISDFGMTRYVLDDEY
VSSFGAKFPIKWSPPEVFLFNKYSSKSDVWSFGVLMWEVFTEGKMPFENKSNLQVVEAIS
EGFRLYRPHLAPMSIYEVMYSCWHEKPEGRPTFAELLRAVTEIAETW
|
| Enzyme 105 Number of Residues |
527 |
| Enzyme 105 Molecular Weight |
61257.9 |
| Enzyme 105 Theoretical pI |
8.05 |
| Enzyme 105 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- non-membrane spanning protein tyrosine kinase activity
- nucleoside binding
- protein binding
- protein kinase activity
- protein tyrosine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- intracellular protein kinase cascade
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- signal transmission
- signal transmission via phosphorylation event
- signaling process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 105 General Function |
Involved in protein kinase activity |
| Enzyme 105 Specific Function |
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate |
| Enzyme 105 Pathways |
Not Available |
| Enzyme 105 Reactions |
- ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate [RN:R02584]
|
| Enzyme 105 Pfam Domain Function |
|
| Enzyme 105 Signals |
|
| Enzyme 105 Transmembrane Regions |
|
| Enzyme 105 Essentiality |
Not Available |
| Enzyme 105 GenBank ID Protein |
684986 |
| Enzyme 105 UniProtKB/Swiss-Prot ID |
P42681 |
| Enzyme 105 UniProtKB/Swiss-Prot Entry Name |
TXK_HUMAN |
| Enzyme 105 PDB ID |
Not Available |
| Enzyme 105 Cellular Location |
Not Available |
| Enzyme 105 Gene Sequence |
>1584 bp
ATGATCCTTTCCTCCTATAACACCATCCAGTCGGTTTTCTGTTGCTGCTGTTGCTGTTCA
GTGCAGAAGCGACAAATGAGAACACAGATAAGCCTGAGCACAGATGAAGAGCTTCCAGAA
AAATACACCCAGCATCGCAGGCCGTGGCTCAGCCAATTGTCAAATAAGAAGCAATCCAAC
ACGGGCCGTGTGCAGCCGTCAAAACGAAAGCCACTGCCTCCCCTCCCACCCTCTGAGGTT
GCTGAAGAGAAGATCCAAGTCAAGGCACTTTATGATTTTCTGCCCAGAGAACCCTGTAAT
TTAGCCTTAAGGAGAGCAGAAGAATACCTGATACTGGAGAAATACAATCCTCACTGGTGG
AAGGCAAGAGACCGTTTGGGGAATGAAGGCTTAATCCCAAGCAACTATGTGACTGAAAAC
AAAATAACTAATTTAGAAATATATGAGTGGTACCATAGAAACATTACCAGAAATCAGGCA
GAACATCTATTGAGACAAGAGTCTAAAGAAGGTGCATTTATTGTCAGAGATTCAAGACAT
TTAGGATCCTACACAATTTCCGTATTTATGGGAGCTAGAAGAAGTACGGAGGCTGCCATA
AAACATTATCAGATAAAAAAGAATGACTCAGGACAGTGGTATGTGGCTGAAAGACACGCC
TTTCAATCAATCCCTGAGTTAATCTGGTATCACCAGCACAATGCAGCCGGTCTCATGACT
CGTCTCCGATATCCAGTTGGGCTGATGGGCAGTTGTTTACCAGCCACAGCTGGGTTTAGC
TACGAAAAGTGGGAGATAGATCCATCTGAGTTGGCTTTTATAAAGGAGATTGGAAGCGGT
CAGTTTGGAGTGGTCCATTTAGGTGAATGGCGGTCACATATCCAGGTAGCTATCAAGGCC
ATCAATGAAGGCTCCATGTCTGAAGAGGATTTCATTGAAGAGGCCAAAGTGATGATGAAA
TTATCTCATTCAAAGCTAGTGCAACTTTATGGAGTCTGTATACAGCGGAAGCCCCTTTAC
ATTGTGACAGAGTTCATGGAAAATGGCTGCCTGCTTAACTATCTCAGGGAGAATAAAGGA
AAGCTTAGGAAGGAAATGCTACTGAGTGTATGCCAGGATATATGTGAAGGAATGGAATAT
CTGGAGAGGAATGGCTATATTCATAGGGATTTGGCGGCAAGGAATTGTTTGGTCAGTTCA
ACATGCATAGTAAAAATTTCAGACTTTGGAATGACAAGGTACGTTTTGGATGATGAGTAT
GTCAGTTCTTTTGGAGCCAAGTTCCCAATCAAGTGGTCCCCTCCTGAAGTTTTTCTTTTC
AATAAGTACAGCAGTAAATCTGATGTCTGGTCATTTGGAGTTTTAATGTGGGAAGTTTTT
ACAGAAGGAAAAATGCCTTTTGAAAATAAGTCAAATTTGCAAGTCGTGGAAGCTATTTCT
GAAGGCTTCAGGCTATATCGCCCTCACCTGGCACCAATGTCCATATATGAAGTCATGTAC
AGCTGCTGGCATGAGAAACCTGAAGGCCGCCCTACATTTGCGGAGCTGCTGCGGGCTGTC
ACAGAGATTGCGGAAACCTGGTGA
|
| Enzyme 105 GenBank Gene ID |
L27071 |
| Enzyme 105 GeneCard ID |
TXK |
| Enzyme 105 GenAtlas ID |
TXK |
| Enzyme 105 HGNC ID |
HGNC:12434 |
| Enzyme 105 Chromosome Location |
4 |
| Enzyme 105 Locus |
4p12 |
| Enzyme 105 SNPs |
SNPJam Report |
| Enzyme 105 General References |
- Haire RN, Ohta Y, Lewis JE, Fu SM, Kroisel P, Litman GW: TXK, a novel human tyrosine kinase expressed in T cells shares sequence identity with Tec family kinases and maps to 4p12. Hum Mol Genet. 1994 Jun;3(6):897-901. [PubMed ]
- Ohta Y, Haire RN, Amemiya CT, Litman RT, Trager T, Riess O, Litman GW: Human Txk: genomic organization, structure and contiguous physical linkage with the Tec gene. Oncogene. 1996 Feb 15;12(4):937-42. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 105 Metabolite References |
Not Available |
|
Enzyme 106
[top]
|
| Enzyme 106 ID |
6442 |
| Enzyme 106 Name |
Epithelial discoidin domain-containing receptor 1 |
| Enzyme 106 Synonyms |
- Epithelial discoidin domain receptor 1
- CD167 antigen-like family member A
- Cell adhesion kinase
- Discoidin receptor tyrosine kinase
- HGK2
- Mammary carcinoma kinase 10
- MCK-10
- Protein-tyrosine kinase 3A
- Protein-tyrosine kinase RTK-6
- TRK E
- Tyrosine kinase DDR
- Tyrosine-protein kinase CAK
- CD167a antigen
|
| Enzyme 106 Gene Name |
DDR1 |
| Enzyme 106 Protein Sequence |
>Epithelial discoidin domain-containing receptor 1
MGPEALSSLLLLLLVASGDADMKGHFDPAKCRYALGMQDRTIPDSDISASSSWSDSTAAR
HSRLESSDGDGAWCPAGSVFPKEEEYLQVDLQRLHLVALVGTQGRHAGGLGKEFSRSYRL
RYSRDGRRWMGWKDRWGQEVISGNEDPEGVVLKDLGPPMVARLVRFYPRADRVMSVCLRV
ELYGCLWRDGLLSYTAPVGQTMYLSEAVYLNDSTYDGHTVGGLQYGGLGQLADGVVGLDD
FRKSQELRVWPGYDYVGWSNHSFSSGYVEMEFEFDRLRAFQAMQVHCNNMHTLGARLPGG
VECRFRRGPAMAWEGEPMRHNLGGNLGDPRARAVSVPLGGRVARFLQCRFLFAGPWLLFS
EISFISDVVNNSSPALGGTFPPAPWWPPGPPPTNFSSLELEPRGQQPVAKAEGSPTAILI
GCLVAIILLLLLIIALMLWRLHWRRLLSKAERRVLEEELTVHLSVPGDTILINNRPGPRE
PPPYQEPRPRGNPPHSAPCVPNGSALLLSNPAYRLLLATYARPPRGPGPPTPAWAKPTNT
QAYSGDYMEPEKPGAPLLPPPPQNSVPHYAEADIVTLQGVTGGNTYAVPALPPGAVGDGP
PRVDFPRSRLRFKEKLGEGQFGEVHLCEVDSPQDLVSLDFPLNVRKGHPLLVAVKILRPD
ATKNARNDFLKEVKIMSRLKDPNIIRLLGVCVQDDPLCMITDYMENGDLNQFLSAHQLED
KAAEGAPGDGQAAQGPTISYPMLLHVAAQIASGMRYLATLNFVHRDLATRNCLVGENFTI
KIADFGMSRNLYAGDYYRVQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEVLMLC
RAQPFGQLTDEQVIENAGEFFRDQGRQVYLSRPPACPQGLYELMLRCWSRESEQRPPFSQ
LHRFLAEDALNTV
|
| Enzyme 106 Number of Residues |
913 |
| Enzyme 106 Molecular Weight |
101126.7 |
| Enzyme 106 Theoretical pI |
6.81 |
| Enzyme 106 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein binding
- protein kinase activity
- protein tyrosine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transmembrane receptor protein tyrosine kinase activity
|
| Process |
- biological regulation
- cell adhesion
- cell surface receptor linked signaling pathway
- cellular metabolic process
- cellular process
- enzyme linked receptor protein signaling pathway
- metabolic process
- peptidyl-tyrosine phosphorylation
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- regulation of biological process
- regulation of cell growth
- regulation of growth
- signaling
- signaling pathway
- transmembrane receptor protein tyrosine kinase signaling pathway
|
| Component |
- cell part
- integral to membrane
- integral to plasma membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 106 General Function |
Involved in cell adhesion |
| Enzyme 106 Specific Function |
May be involved in cell-cell interactions and recognition |
| Enzyme 106 Pathways |
Not Available |
| Enzyme 106 Reactions |
- ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate [RN:R02584]
|
| Enzyme 106 Pfam Domain Function |
|
| Enzyme 106 Signals |
|
| Enzyme 106 Transmembrane Regions |
|
| Enzyme 106 Essentiality |
Not Available |
| Enzyme 106 GenBank ID Protein |
27544401 |
| Enzyme 106 UniProtKB/Swiss-Prot ID |
Q08345 |
| Enzyme 106 UniProtKB/Swiss-Prot Entry Name |
DDR1_HUMAN |
| Enzyme 106 PDB ID |
Not Available |
| Enzyme 106 Cellular Location |
Not Available |
| Enzyme 106 Gene Sequence |
>2742 bp
ATGGGACCAGAGGCCCTGTCATCTTTACTGCTGCTGCTCTTGGTGGCAAGTGGAGATGCT
GACATGAAGGGACATTTTGATCCTGCCAAGTGCCGCTATGCCCTGGGCATGCAGGACCGG
ACCATCCCAGACAGTGACATCTCTGCTTCCAGCTCCTGGTCAGATTCCACTGCCGCCCGC
CACAGCAGGTTGGAGAGCAGTGACGGGGATGGGGCCTGGTGCCCCGCAGGGTCGGTGTTT
CCCAAGGAGGAGGAGTACTTGCAGGTGGATCTACAACGACTCCACCTGGTGGCTCTGGTG
GGCACCCAGGGACGGCATGCCGGGGGCCTGGGCAAGGAGTTCTCCCGGAGCTACCGGCTG
CGTTACTCCCGGGATGGTCGCCGCTGGATGGGCTGGAAGGACCGCTGGGGTCAGGAGGTG
ATCTCAGGCAATGAGGACCCTGAGGGAGTGGTGCTGAAGGACCTTGGGCCCCCCATGGTT
GCCCGACTGGTTCGCTTCTACCCCCGGGCTGACCGGGTCATGAGTGTCTGTCTGCGGGTA
GAGCTCTATGGCTGCCTCTGGAGGGATGGACTCCTGTCTTACACCGCCCCTGTGGGGCAG
ACAATGTATTTATCTGAGGCCGTGTACCTCAACGACTCCACCTATGACGGACATACCGTG
GGCGGACTGCAGTATGGGGGTCTGGGCCAGCTGGCAGATGGTGTGGTGGGGCTGGATGAC
TTTAGGAAGAGTCAGGAGCTGCGGGTCTGGCCAGGCTATGACTATGTGGGATGGAGCAAC
CACAGCTTCTCCAGTGGCTATGTGGAGATGGAGTTTGAGTTTGACCGGCTGAGGGCCTTC
CAGGCTATGCAGGTCCACTGTAACAACATGCACACGCTGGGAGCCCGTCTGCCTGGCGGG
GTGGAATGTCGCTTCCGGCGTGGCCCTGCCATGGCCTGGGAGGGGGAGCCCATGCGCCAC
AACCTAGGGGGCAACCTGGGGGACCCCAGAGCCCGGGCTGTCTCAGTGCCCCTTGGCGGC
CGTGTGGCTCGCTTTCTGCAGTGCCGCTTCCTCTTTGCGGGGCCCTGGTTACTCTTCAGC
GAAATCTCCTTCATCTCTGATGTGGTGAACAATTCCTCTCCGGCACTGGGAGGCACCTTC
CCGCCAGCCCCCTGGTGGCCGCCTGGCCCACCTCCCACCAACTTCAGCAGCTTGGAGCTG
GAGCCCAGAGGCCAGCAGCCCGTGGCCAAGGCCGAGGGGAGCCCGACCGCCATCCTCATC
GGCTGCCTGGTGGCCATCATCCTGCTCCTGCTGCTCATCATTGCCCTCATGCTCTGGCGG
CTGCACTGGCGCAGGCTCCTCAGCAAGGCTGAACGGAGGGTGTTGGAAGAGGAGCTGACG
GTTCACCTCTCTGTCCCTGGGGACACTATCCTCATCAACAACCGCCCAGGTCCTAGAGAG
CCACCCCCGTACCAGGAGCCCCGGCCTCGTGGGAATCCGCCCCACTCCGCTCCCTGTGTC
CCCAATGGCTCTGCGTTGCTGCTCTCCAATCCAGCCTACCGCCTCCTTCTGGCCACTTAC
GCCCGTCCCCCTCGAGGCCCGGGCCCCCCCACACCCGCCTGGGCCAAACCCACCAACACC
CAGGCCTACAGTGGGGACTATATGGAGCCTGAGAAGCCAGGCGCCCCGCTTCTGCCCCCA
CCTCCCCAGAACAGCGTCCCCCATTATGCCGAGGCTGACATTGTTACCCTGCAGGGCGTC
ACCGGGGGCAACACCTATGCTGTGCCTGCACTGCCCCCAGGGGCAGTCGGGGATGGGCCC
CCCAGAGTGGATTTCCCTCGATCTCGACTCCGCTTCAAGGAGAAGCTTGGCGAGGGCCAG
TTTGGGGAGGTGCACCTGTGTGAGGTCGACAGCCCTCAAGATCTGGTCAGTCTTGATTTC
CCCCTTAATGTGCGTAAGGGACACCCTTTGCTGGTAGCTGTCAAGATCTTACGGCCAGAT
GCCACCAAGAATGCCAGGAATGATTTCCTGAAAGAGGTGAAGATCATGTCGAGGCTCAAG
GACCCCAACATCATTCGGCTGCTGGGCGTGTGTGTGCAGGACGACCCCCTCTGCATGATT
ACTGACTACATGGAGAACGGCGACCTCAACCAGTTCCTCAGTGCCCACCAGCTGGAGGAC
AAGGCAGCCGAGGGGGCCCCTGGGGACGGGCAGGCTGCGCAGGGGCCCACCATCAGCTAC
CCAATGCTGCTGCATGTGGCAGCCCAGATCGCCTCCGGCATGCGCTATCTGGCCACACTC
AACTTTGTACATCGGGACCTGGCCACGCGGAACTGCCTAGTTGGGGAAAATTTCACCATC
AAAATCGCAGACTTTGGCATGAGCCGGAACCTCTATGCTGGGGACTATTACCGTGTGCAG
GGCCGGGCAGTGCTGCCCATCCGCTGGATGGCCTGGGAGTGCATCCTCATGGGGAAGTTC
ACGACTGCGAGTGACGTGTGGGCCTTTGGTGTGACCCTGTGGGAGGTGCTGATGCTCTGT
AGGGCCCAGCCCTTTGGGCAGCTCACCGACGAGCAGGTCATCGAGAACGCGGGGGAGTTC
TTCCGGGACCAGGGCCGGCAGGTGTACCTGTCCCGGCCGCCTGCCTGCCCGCAGGGCCTA
TATGAGCTGATGCTTCGGTGCTGGAGCCGGGAGTCTGAGCAGCGACCACCCTTTTCCCAG
CTGCATCGGTTCCTGGCAGAGGATGCACTCAACACGGTGTGA
|
| Enzyme 106 GenBank Gene ID |
AB088102 |
| Enzyme 106 GeneCard ID |
DDR1 |
| Enzyme 106 GenAtlas ID |
DDR1 |
| Enzyme 106 HGNC ID |
HGNC:2730 |
| Enzyme 106 Chromosome Location |
6 |
| Enzyme 106 Locus |
6p21.3 |
| Enzyme 106 SNPs |
SNPJam Report |
| Enzyme 106 General References |
- Di Marco E, Cutuli N, Guerra L, Cancedda R, De Luca M: Molecular cloning of trkE, a novel trk-related putative tyrosine kinase receptor isolated from normal human keratinocytes and widely expressed by normal human tissues. J Biol Chem. 1993 Nov 15;268(32):24290-5. [PubMed ]
- Johnson JD, Edman JC, Rutter WJ: A receptor tyrosine kinase found in breast carcinoma cells has an extracellular discoidin I-like domain. Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5677-81. [PubMed ]
- Laval S, Butler R, Shelling AN, Hanby AM, Poulsom R, Ganesan TS: Isolation and characterization of an epithelial-specific receptor tyrosine kinase from an ovarian cancer cell line. Cell Growth Differ. 1994 Nov;5(11):1173-83. [PubMed ]
- Perez JL, Shen X, Finkernagel S, Sciorra L, Jenkins NA, Gilbert DJ, Copeland NG, Wong TW: Identification and chromosomal mapping of a receptor tyrosine kinase with a putative phospholipid binding sequence in its ectodomain. Oncogene. 1994 Jan;9(1):211-9. [PubMed ]
- Sakuma S, Saya H, Tada M, Nakao M, Fujiwara T, Roth JA, Sawamura Y, Shinohe Y, Abe H: Receptor protein tyrosine kinase DDR is up-regulated by p53 protein. FEBS Lett. 1996 Dec 2;398(2-3):165-9. [PubMed ]
- Playford MP, Butler RJ, Wang XC, Katso RM, Cooke IE, Ganesan TS: The genomic structure of discoidin receptor tyrosine kinase. Genome Res. 1996 Jul;6(7):620-7. [PubMed ]
- Perez JL, Jing SQ, Wong TW: Identification of two isoforms of the Cak receptor kinase that are coexpressed in breast tumor cell lines. Oncogene. 1996 Apr 4;12(7):1469-77. [PubMed ]
- Jin P, Zhang J, Sumariwalla PF, Ni I, Jorgensen B, Crawford D, Phillips S, Feldmann M, Shepard HM, Paleolog EM: Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis. Arthritis Res Ther. 2008;10(4):R73. Epub 2008 Jul 1. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Shiina T, Ota M, Shimizu S, Katsuyama Y, Hashimoto N, Takasu M, Anzai T, Kulski JK, Kikkawa E, Naruse T, Kimura N, Yanagiya K, Watanabe A, Hosomichi K, Kohara S, Iwamoto C, Umehara Y, Meyer A, Wanner V, Sano K, Macquin C, Ikeo K, Tokunaga K, Gojobori T, Inoko H, Bahram S: Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity. Genetics. 2006 Jul;173(3):1555-70. Epub 2006 May 15. [PubMed ]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Alves F, Vogel W, Mossie K, Millauer B, Hofler H, Ullrich A: Distinct structural characteristics of discoidin I subfamily receptor tyrosine kinases and complementary expression in human cancer. Oncogene. 1995 Feb 2;10(3):609-18. [PubMed ]
- Weiner TM, Liu ET, Craven RJ, Cance WG: Expression of growth factor receptors, the focal adhesion kinase, and other tyrosine kinases in human soft tissue tumors. Ann Surg Oncol. 1994 Jan;1(1):18-27. [PubMed ]
- Lee ST, Strunk KM, Spritz RA: A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes. Oncogene. 1993 Dec;8(12):3403-10. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Hilton HN, Stanford PM, Harris J, Oakes SR, Kaplan W, Daly RJ, Ormandy CJ: KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling. Biochim Biophys Acta. 2008 Mar;1783(3):383-93. Epub 2008 Jan 9. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 106 Metabolite References |
Not Available |
|
Enzyme 107
[top]
|
| Enzyme 107 ID |
6443 |
| Enzyme 107 Name |
Proto-oncogene tyrosine-protein kinase Src |
| Enzyme 107 Synonyms |
- Proto-oncogene c-Src
- pp60c-src
- p60-Src
|
| Enzyme 107 Gene Name |
SRC |
| Enzyme 107 Protein Sequence |
>Proto-oncogene tyrosine-protein kinase Src
MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAE
PKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGD
WWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRES
ETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGL
CHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTL
KPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKY
LRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYT
ARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVER
GYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
|
| Enzyme 107 Number of Residues |
536 |
| Enzyme 107 Molecular Weight |
59834.3 |
| Enzyme 107 Theoretical pI |
7.47 |
| Enzyme 107 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- non-membrane spanning protein tyrosine kinase activity
- nucleoside binding
- protein binding
- protein kinase activity
- protein tyrosine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biological regulation
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- regulation of biological process
- regulation of cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 107 General Function |
Involved in protein kinase activity |
| Enzyme 107 Specific Function |
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate |
| Enzyme 107 Pathways |
Not Available |
| Enzyme 107 Reactions |
- ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate [RN:R02584]
|
| Enzyme 107 Pfam Domain Function |
|
| Enzyme 107 Signals |
|
| Enzyme 107 Transmembrane Regions |
|
| Enzyme 107 Essentiality |
Not Available |
| Enzyme 107 GenBank ID Protein |
15079460 |
| Enzyme 107 UniProtKB/Swiss-Prot ID |
P12931 |
| Enzyme 107 UniProtKB/Swiss-Prot Entry Name |
SRC_HUMAN |
| Enzyme 107 PDB ID |
2SRC |
| Enzyme 107 PDB File |
Show |
| Enzyme 107 3D Structure |
|
| Enzyme 107 Cellular Location |
Not Available |
| Enzyme 107 Gene Sequence |
>1611 bp
ATGGGTAGCAACAAGAGCAAGCCCAAGGATGCCAGCCAGCGGCGCCGCAGCCTGGAGCCC
GCCGAGAACGTGCACGGCGCTGGCGGGGGCGCTTTCCCCGCCTCGCAGACCCCCAGCAAG
CCAGCCTCGGCCGACGGCCACCGCGGCCCCAGCGCGGCCTTCGCCCCCGCGGCCGCCGAG
CCCAAGCTGTTCGGAGGCTTCAACTCCTCGGACACCGTCACCTCCCCGCAGAGGGCGGGC
CCGCTGGCCGGTGGAGTGACCACCTTTGTGGCCCTCTATGACTATGAGTCTAGGACGGAG
ACAGACCTGTCCTTCAAGAAAGGCGAGCGGCTCCAGATTGTCAACAACACAGAGGGAGAC
TGGTGGCTGGCCCACTCGCTCAGCACAGGACAGACAGGCTACATCCCCAGCAACTACGTG
GCGCCCTCCGACTCCATCCAGGCTGAGGAGTGGTATTTTGGCAAGATCACCAGACGGGAG
TCAGAGCGGTTACTGCTCAATGCAGAGAACCCGAGAGGGACCTTCCTCGTGCGAGAAAGT
GAGACCACGAAAGGTGCCTACTGCCTCTCAGTGTCTGACTTCGACAACGCCAAGGGCCTC
AACGTGAAGCACTACAAGATCCGCAAGCTGGACAGCGGCGGCTTCTACATCACCTCCCGC
ACCCAGTTCAACAGCCTGCAGCAGCTGGTGGCCTACTACTCCAAACACGCCGATGGCCTG
TGCCACCGCCTCACCACCGTGTGCCCCACGTCCAAGCCGCAGACTCAGGGCCTGGCCAAG
GATGCCTGGGAGATCCCTCGGGAGTCGCTGCGGCTGGAGGTCAAGCTGGGCCAGGGCTGC
TTTGGCGAGGTGTGGATGGGGACCTGGAACGGTACCACCAGGGTGGCCATCAAAACCCTG
AAGCCTGGCACGATGTCTCCAGAGGCCTTCCTGCAGGAGGCCCAGGTCATGAAGAAGCTG
AGGCATGAGAAGCTGGTGCAGTTGTATGCTGTGGTTTCAGAGGAGCCCATTTACATCGTC
ACGGAGTACATGAGCAAGGGGAGTTTGCTGGACTTTCTCAAGGGGGAGACAGGCAAGTAC
CTGCGGCTGCCTCAGCTGGTGGACATGGCTGCTCAGATCGCCTCAGGCATGGCGTACGTG
GAGCGGATGAACTACGTCCACCGGGACCTTCGTGCAGCCAACATCCTGGTGGGAGAGAAC
CTGGTGTGCAAAGTGGCCGACTTTGGGCTGGCTCGGCTCATTGAAGACAATGAGTACACG
GCGCGGCAAGGTGCCAAATTCCCCATCAAGTGGACGGCTCCAGAAGCTGCCCTCTATGGC
CGCTTCACCATCAAGTCGGACGTGTGGTCCTTCGGGATCCTGCTGACTGAGCTCACCACA
AAGGGACGGGTGCCCTACCCTGGGATGGTGAACCGCGAGGTGCTGGACCAGGTGGAGCGG
GGCTACCGGATGCCCTGCCCGCCGGAGTGTCCCGAGTCCCTGCACGACCTCATGTGCCAG
TGCTGGCGGAAGGAGCCTGAGGAGCGGCCCACCTTCGAGTACCTGCAGGCCTTCCTGGAG
GACTACTTCACGTCCACCGAGCCCCAGTACCAGCCCGGGGAGAACCTCTAG
|
| Enzyme 107 GenBank Gene ID |
BC011566 |
| Enzyme 107 GeneCard ID |
SRC |
| Enzyme 107 GenAtlas ID |
SRC |
| Enzyme 107 HGNC ID |
HGNC:11283 |
| Enzyme 107 Chromosome Location |
2 |
| Enzyme 107 Locus |
20q12-q13 |
| Enzyme 107 SNPs |
SNPJam Report |
| Enzyme 107 General References |
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Tanaka A, Gibbs CP, Arthur RR, Anderson SK, Kung HJ, Fujita DJ: DNA sequence encoding the amino-terminal region of the human c-src protein: implications of sequence divergence among src-type kinase oncogenes. Mol Cell Biol. 1987 May;7(5):1978-83. [PubMed ]
- Anderson SK, Gibbs CP, Tanaka A, Kung HJ, Fujita DJ: Human cellular src gene: nucleotide sequence and derived amino acid sequence of the region coding for the carboxy-terminal two-thirds of pp60c-src. Mol Cell Biol. 1985 May;5(5):1122-9. [PubMed ]
- Pyper JM, Bolen JB: Neuron-specific splicing of C-SRC RNA in human brain. J Neurosci Res. 1989 Sep;24(1):89-96. [PubMed ]
- Parker RC, Mardon G, Lebo RV, Varmus HE, Bishop JM: Isolation of duplicated human c-src genes located on chromosomes 1 and 20. Mol Cell Biol. 1985 Apr;5(4):831-8. [PubMed ]
- Pyper JM, Bolen JB: Identification of a novel neuronal C-SRC exon expressed in human brain. Mol Cell Biol. 1990 May;10(5):2035-40. [PubMed ]
- Luttrell LM, Ferguson SS, Daaka Y, Miller WE, Maudsley S, Della Rocca GJ, Lin F, Kawakatsu H, Owada K, Luttrell DK, Caron MG, Lefkowitz RJ: Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes. Science. 1999 Jan 29;283(5402):655-61. [PubMed ]
- Miller WE, Maudsley S, Ahn S, Khan KD, Luttrell LM, Lefkowitz RJ: beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis. J Biol Chem. 2000 Apr 14;275(15):11312-9. [PubMed ]
- Rebhun JF, Chen H, Quilliam LA: Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral. J Biol Chem. 2000 May 5;275(18):13406-10. [PubMed ]
- Li Y, Kuwahara H, Ren J, Wen G, Kufe D: The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1 carcinoma-associated antigen with GSK3 beta and beta-catenin. J Biol Chem. 2001 Mar 2;276(9):6061-4. Epub 2001 Jan 10. [PubMed ]
- Korkaya H, Jameel S, Gupta D, Tyagi S, Kumar R, Zafrullah M, Mazumdar M, Lal SK, Xiaofang L, Sehgal D, Das SR, Sahal D: The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK. J Biol Chem. 2001 Nov 9;276(45):42389-400. Epub 2001 Aug 22. [PubMed ]
- Lee H, Park DS, Wang XB, Scherer PE, Schwartz PE, Lisanti MP: Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1. J Biol Chem. 2002 Sep 13;277(37):34556-67. Epub 2002 Jun 28. [PubMed ]
- Wong CW, McNally C, Nickbarg E, Komm BS, Cheskis BJ: Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14783-8. Epub 2002 Nov 1. [PubMed ]
- Wang XB, Lee H, Capozza F, Marmon S, Sotgia F, Brooks JW, Campos-Gonzalez R, Lisanti MP: Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27). Biochemistry. 2004 Nov 2;43(43):13694-706. [PubMed ]
- Benes CH, Wu N, Elia AE, Dharia T, Cantley LC, Soltoff SP: The C2 domain of PKCdelta is a phosphotyrosine binding domain. Cell. 2005 Apr 22;121(2):271-80. [PubMed ]
- Franco M, Furstoss O, Simon V, Benistant C, Hong WJ, Roche S: The adaptor protein Tom1L1 is a negative regulator of Src mitogenic signaling induced by growth factors. Mol Cell Biol. 2006 Mar;26(5):1932-47. [PubMed ]
- Maudsley S, Davidson L, Pawson AJ, Freestone SH, Lopez de Maturana R, Thomson AA, Millar RP: Gonadotropin-releasing hormone functionally antagonizes testosterone activation of the human androgen receptor in prostate cells through focal adhesion complexes involving Hic-5. Neuroendocrinology. 2006;84(5):285-300. Epub 2007 Jan 4. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Di Stefano P, Damiano L, Cabodi S, Aramu S, Tordella L, Praduroux A, Piva R, Cavallo F, Forni G, Silengo L, Tarone G, Turco E, Defilippi P: p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity. EMBO J. 2007 Jun 20;26(12):2843-55. Epub 2007 May 24. [PubMed ]
- Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed ]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Mund T, Pelham HR: Regulation of PTEN/Akt and MAP kinase signaling pathways by the ubiquitin ligase activators Ndfip1 and Ndfip2. Proc Natl Acad Sci U S A. 2010 Jun 22;107(25):11429-34. Epub 2010 Jun 7. [PubMed ]
- Xu W, Harrison SC, Eck MJ: Three-dimensional structure of the tyrosine kinase c-Src. Nature. 1997 Feb 13;385(6617):595-602. [PubMed ]
- Charifson PS, Shewchuk LM, Rocque W, Hummel CW, Jordan SR, Mohr C, Pacofsky GJ, Peel MR, Rodriguez M, Sternbach DD, Consler TG: Peptide ligands of pp60(c-src) SH2 domains: a thermodynamic and structural study. Biochemistry. 1997 May 27;36(21):6283-93. [PubMed ]
- Xu RX, Word JM, Davis DG, Rink MJ, Willard DH Jr, Gampe RT Jr: Solution structure of the human pp60c-src SH2 domain complexed with a phosphorylated tyrosine pentapeptide. Biochemistry. 1995 Feb 21;34(7):2107-21. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 107 Metabolite References |
Not Available |
|
Enzyme 108
[top]
|
| Enzyme 108 ID |
6444 |
| Enzyme 108 Name |
Receptor-interacting serine/threonine-protein kinase 3 |
| Enzyme 108 Synonyms |
- RIP-like protein kinase 3
- Receptor-interacting protein 3
- RIP-3
|
| Enzyme 108 Gene Name |
RIPK3 |
| Enzyme 108 Protein Sequence |
>Receptor-interacting serine/threonine-protein kinase 3
MSCVKLWPSGAPAPLVSIEELENQELVGKGGFGTVFRAQHRKWGYDVAVKIVNSKAISRE
VKAMASLDNEFVLRLEGVIEKVNWDQDPKPALVTKFMENGSLSGLLQSQCPRPWPLLCRL
LKEVVLGMFYLHDQNPVLLHRDLKPSNVLLDPELHVKLADFGLSTFQGGSQSGTGSGEPG
GTLGYLAPELFVNVNRKASTASDVYSFGILMWAVLAGREVELPTEPSLVYEAVCNRQNRP
SLAELPQAGPETPGLEGLKELMQLCWSSEPKDRPSFQECLPKTDEVFQMVENNMNAAVST
VKDFLSQLRSSNRRFSIPESGQGGTEMDGFRRTIENQHSRNDVMVSEWLNKLNLEEPPSS
VPKKCPSLTKRSRAQEEQVPQAWTAGTSSDSMAQPPQTPETSTFRNQMPSPTSTGTPSPG
PRGNQGAERQGMNWSCRTPEPNPVTGRPLVNIYNCSGVQVGDNNYLTMQQTTALPTWGLA
PSGKGRGLQHPPPVGSQEGPKDPEAWSRPQGWYNHSGK
|
| Enzyme 108 Number of Residues |
518 |
| Enzyme 108 Molecular Weight |
56886.9 |
| Enzyme 108 Theoretical pI |
6.41 |
| Enzyme 108 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 108 General Function |
Involved in protein kinase activity |
| Enzyme 108 Specific Function |
Promotes apoptosis |
| Enzyme 108 Pathways |
Not Available |
| Enzyme 108 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 108 Pfam Domain Function |
|
| Enzyme 108 Signals |
|
| Enzyme 108 Transmembrane Regions |
|
| Enzyme 108 Essentiality |
Not Available |
| Enzyme 108 GenBank ID Protein |
5059425 |
| Enzyme 108 UniProtKB/Swiss-Prot ID |
Q9Y572 |
| Enzyme 108 UniProtKB/Swiss-Prot Entry Name |
RIPK3_HUMAN |
| Enzyme 108 PDB ID |
Not Available |
| Enzyme 108 Cellular Location |
Not Available |
| Enzyme 108 Gene Sequence |
>1557 bp
ATGTCGTGCGTCAAGTTATGGCCCAGCGGTGCCCCCGCCCCCTTGGTGTCCATCGAGGAA
CTGGAGAACCAGGAGCTCGTCGGCAAAGACGGGTTCGGCACAGTGTTCCGGGCGCAACAT
AGGAAGTGGGGCTACGATGTGGCGGTCAAGATCGTAAACTCGAAGGCGATATCCAGGGAG
GTCAAGGCCATGGCAAGTCTGGATAACGAATTCGTGTTGCGCCTAGAAGGGGTTATCGAG
AAGGTGAACTGGGACCAAGATCCCAAGCCGGCTCTGGTGACTAAATTCATGGAGAACGGC
TCCCTGTCGGGGCTGCTGCAGTCCCAGTGCCCTCGGCCCTGGCCGCTCCTTTGCCGCCTG
CTGAAAGAAGTGGTGCTTGGGATGTTTTACCTGCACGACCAGAACCCGGTGCTCCTGCAC
CGGGACCTCAAGCCATCCAACGTCCTGCCGGACCCAGAGCTGCACGTCAAGCTGGCAGAT
TTTGGCCTGTCCACATTTCAGGGAGGCTCACAGTCAGGGACAGGGTCCGGGGAGCCAGGG
GGCACCCTGGGCTACTTGGCCCCAGAACTGTTTGTTAACGTAAACCGGAAGGCCTCCACA
GCCAGTGACGTCTACAGCTTCGGGATCCTAATGTGGGCAGTGCTTGCTGGAAGAGAAGTT
GAGTTGCCAACCGAACCATCACTCGTGTACGAAGCAGTGTGCAACAGGCAGAACCGGCCT
TCATTGGCTGAGCTGCCCCAAGCCGGGCCTGAGACTCCCGGCTTAGAAGGACTGAAGGAG
CTAATGCAGCTCTGCTGGAGCAGTGAGCCCAAGGACAGACCCTCCTTCCAGGAATGCCTA
CCAAAAACTGATGAAGTCTTCCAGATGGTGGAGAACAATATGAATGCTGCTGTCTCCACG
GTAAAGGATTTCCTGTCTCAGCTCAAGAGCAGCAATAGGAGATTTTCTATCCCAGAGTCA
GGCCAAGGAGGGACAGAAATGGATGGCTTTAGGAGAACCATAGAAAACCAGCACTCTCGT
AATGATGTCATGGTTTCTGAGTGGCTAAACAAACTGAATCTAGAGGAGCCTCCCAGCTCT
GTTCCTAAAAAATGCCCGAGCCTTACCAAGAGGAGCAGGGCACAAGAGGAGCAGGTTCCA
CAAGCCTGGACAGCAGGCACATCTTCAGATTCGATGGCCCAACCTCCCCAGACTCCAGAG
ACCTCAACTTTCAGAAACCAGATGCCCAGCCCTACCTCAACTGGAACACCAAGTCCTGGA
CCCCGAGGGAATCAGGGGGCTGAGAGACAAGGCATGAACTGGTCCTGCAGGACCCCGGAG
CCAAATCCAGTAACAGGGCGACCGCTCGTTAACATATACAACTGCTCTGGGGTGCAAGTT
GGAGACAACAACTACTTGACTATGCAACAGACAACTGCCTTGCCCACATGGGGCTTGGCA
CCTTCGGGCAAGGGGAGGGGCTTGCAGCACCCCCCACCAGTAGGTTCGCAAGAAGGCCCT
AAAGATCCTGAAGCCTGGAGCAGGCCACAGGGTTGGTATAATCATAGCGGGAAATAA
|
| Enzyme 108 GenBank Gene ID |
AF156884 |
| Enzyme 108 GeneCard ID |
RIPK3 |
| Enzyme 108 GenAtlas ID |
RIPK3 |
| Enzyme 108 HGNC ID |
HGNC:10021 |
| Enzyme 108 Chromosome Location |
1 |
| Enzyme 108 Locus |
14q11.2 |
| Enzyme 108 SNPs |
SNPJam Report |
| Enzyme 108 General References |
- Yu PW, Huang BC, Shen M, Quast J, Chan E, Xu X, Nolan GP, Payan DG, Luo Y: Identification of RIP3, a RIP-like kinase that activates apoptosis and NFkappaB. Curr Biol. 1999 May 20;9(10):539-42. [PubMed ]
- Sun X, Lee J, Navas T, Baldwin DT, Stewart TA, Dixit VM: RIP3, a novel apoptosis-inducing kinase. J Biol Chem. 1999 Jun 11;274(24):16871-5. [PubMed ]
- Yang Y, Hu W, Feng S, Ma J, Wu M: RIP3 beta and RIP3 gamma, two novel splice variants of receptor-interacting protein 3 (RIP3), downregulate RIP3-induced apoptosis. Biochem Biophys Res Commun. 2005 Jun 24;332(1):181-7. [PubMed ]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed ]
- 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 ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 108 Metabolite References |
Not Available |
|
Enzyme 109
[top]
|
| Enzyme 109 ID |
6445 |
| Enzyme 109 Name |
BDNF/NT-3 growth factors receptor |
| Enzyme 109 Synonyms |
- GP145-TrkB
- Trk-B
- Neurotrophic tyrosine kinase receptor type 2
- TrkB tyrosine kinase
|
| Enzyme 109 Gene Name |
NTRK2 |
| Enzyme 109 Protein Sequence |
>BDNF/NT-3 growth factors receptor
MSSWIRWHGPAMARLWGFCWLVVGFWRAAFACPTSCKCSASRIWCSDPSPGIVAFPRLEP
NSVDPENITEIFIANQKRLEIINEDDVEAYVGLRNLTIVDSGLKFVAHKAFLKNSNLQHI
NFTRNKLTSLSRKHFRHLDLSELILVGNPFTCSCDIMWIKTLQEAKSSPDTQDLYCLNES
SKNIPLANLQIPNCGLPSANLAAPNLTVEEGKSITLSCSVAGDPVPNMYWDVGNLVSKHM
NETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHH
WCIPFTVKGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYT
LIAKNEYGKDEKQISAHFMGWPGIDDGANPNYPDVIYEDYGTAANDIGDTTNRSNEIPST
DVTDKTGREHLSVYAVVVIASVVGFCLLVMLFLLKLARHSKFGMKGPASVISNDDDSASP
LHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVL
KRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHI
VKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQI
AAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWM
PPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQ
EVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDILG
|
| Enzyme 109 Number of Residues |
822 |
| Enzyme 109 Molecular Weight |
91998.2 |
| Enzyme 109 Theoretical pI |
6.45 |
| Enzyme 109 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- molecular transducer activity
- neurotrophin receptor activity
- nucleoside binding
- protein binding
- protein kinase activity
- protein tyrosine kinase activity
- purine nucleoside binding
- receptor activity
- signal transducer activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transmembrane receptor protein tyrosine kinase activity
|
| Process |
- cell surface receptor linked signaling pathway
- cellular metabolic process
- enzyme linked receptor protein signaling pathway
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- signaling
- signaling pathway
- transmembrane receptor protein tyrosine kinase signaling pathway
|
| Component |
- cell part
- integral to membrane
- integral to plasma membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 109 General Function |
Involved in protein kinase activity |
| Enzyme 109 Specific Function |
Receptor for brain-derived neurotrophic factor (BDNF), neurotrophin-3 and neurotrophin-4/5 but not nerve growth factor (NGF). Involved in the development and/or maintenance of the nervous system. This is a tyrosine-protein kinase receptor. Known substrates for the TRK receptors are SHC1, PI-3 kinase, and PLC- gamma-1 |
| Enzyme 109 Pathways |
Not Available |
| Enzyme 109 Reactions |
- ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate [RN:R02584]
|
| Enzyme 109 Pfam Domain Function |
|
| Enzyme 109 Signals |
|
| Enzyme 109 Transmembrane Regions |
|
| Enzyme 109 Essentiality |
Not Available |
| Enzyme 109 GenBank ID Protein |
Not Available |
| Enzyme 109 UniProtKB/Swiss-Prot ID |
Q16620 |
| Enzyme 109 UniProtKB/Swiss-Prot Entry Name |
NTRK2_HUMAN |
| Enzyme 109 PDB ID |
Not Available |
| Enzyme 109 Cellular Location |
Not Available |
| Enzyme 109 Gene Sequence |
>2469 bp
ATGTCGTCCTGGATAAGGTGGCATGGACCCGCCATGGCGCGGCTCTGGGGCTTCTGCTGG
CTGGTTGTGGGCTTCTGGAGGGCCGCTTTCGCCTGTCCCACGTCCTGCAAATGCAGTGCC
TCTCGGATCTGGTGCAGCGACCCTTCTCCTGGCATCGTGGCATTTCCGAGATTGGAGCCT
AACAGTGTAGATCCTGAGAACATCACCGAAATTTTCATCGCAAACCAGAAAAGGTTAGAA
ATCATCAACGAAGATGATGTTGAAGCTTATGTGGGACTGAGAAATCTGACAATTGTGGAT
TCTGGATTAAAATTTGTGGCTCATAAAGCATTTCTGAAAAACAGCAACCTGCAGCACATC
AATTTTACCCGAAACAAACTGACGAGTTTGTCTAGGAAACATTTCCGTCACCTTGACTTG
TCTGAACTGATCCTGGTGGGCAATCCATTTACATGCTCCTGTGACATTATGTGGATCAAG
ACTCTCCAAGAGGCTAAATCCAGTCCAGACACTCAGGATTTGTACTGCCTGAATGAAAGC
AGCAAGAATATTCCCCTGGCAAACCTGCAGATACCCAATTGTGGTTTGCCATCTGCAAAT
CTGGCCGCACCTAACCTCACTGTGGAGGAAGGAAAGTCTATCACATTATCCTGTAGTGTG
GCAGGTGATCCGGTTCCTAATATGTATTGGGATGTTGGTAACCTGGTTTCCAAACATATG
AATGAAACAAGCCACACACAGGGCTCCTTAAGGATAACTAACATTTCATCCGATGACAGT
GGGAAGCAGATCTCTTGTGTGGCGGAAAATCTTGTAGGAGAAGATCAAGATTCTGTCAAC
CTCACTGTGCATTTTGCACCAACTATCACATTTCTCGAATCTCCAACCTCAGACCACCAC
TGGTGCATTCCATTCACTGTGAAAGGCAACCCCAAACCAGCGCTTCAGTGGTTCTATAAC
GGGGCAATATTGAATGAGTCCAAATACATCTGTACTAAAATACATGTTACCAATCACACG
GAGTACCACGGCTGCCTCCAGCTGGATAATCCCACTCACATGAACAATGGGGACTACACT
CTAATAGCCAAGAATGAGTATGGGAAGGATGAGAAACAGATTTCTGCTCACTTCATGGGC
TGGCCTGGAATTGACGATGGTGCAAACCCAAATTATCCTGATGTAATTTATGAAGATTAT
GGAACTGCAGCGAATGACATCGGGGACACCACGAACAGAAGTAATGAAATCCCTTCCACA
GACGTCACTGATAAAACCGGTCGGGAACATCTCTCGGTCTATGCTGTGGTGGTGATTGCG
TCTGTGGTGGGATTTTGCCTTTTGGTAATGCTGTTTCTGCTTAAGTTGGCAAGACACTCC
AAGTTTGGCATGAAAGGCCCAGCCTCCGTTATCAGCAATGATGATGACTCTGCCAGCCCA
CTCCATCACATCTCCAATGGGAGTAACACTCCATCTTCTTCGGAAGGTGGCCCAGATGCT
GTCATTATTGGAATGACCAAGATCCCTGTCATTGAAAATCCCCAGTACTTTGGCATCACC
AACAGTCAGCTCAAGCCAGACACATTTGTTCAGCACATCAAGCGACATAACATTGTTCTG
AAAAGGGAGCTAGGCGAAGGAGCCTTTGGAAAAGTGTTCCTAGCTGAATGCTATAACCTC
TGTCCTGAGCAGGACAAGATCTTGGTGGCAGTGAAGACCCTGAAGGATGCCAGTGACAAT
GCACGCAAGGACTTCCACCGTGAGGCCGAGCTCCTGACCAACCTCCAGCATGAGCACATC
GTCAAGTTCTATGGCGTCTGCGTGGAGGGCGACCCCCTCATCATGGTCTTTGAGTACATG
AAGCATGGGGACCTCAACAAGTTCCTCAGGGCACACGGCCCTGATGCCGTGCTGATGGCT
GAGGGCAACCCGCCCACGGAACTGACGCAGTCGCAGATGCTGCATATAGCCCAGCAGATC
GCCGCGGGCATGGTCTACCTGGCGTCCCAGCACTTCGTGCACCGCGATTTGGCCACCAGG
AACTGCCTGGTCGGGGAGAACTTGCTGGTGAAAATCGGGGACTTTGGGATGTCCCGGGAC
GTGTACAGCACTGACTACTACAGGGTCGGTGGCCACACAATGCTGCCCATTCGCTGGATG
CCTCCAGAGAGCATCATGTACAGGAAATTCACGACGGAAAGCGACGTCTGGAGCCTGGGG
GTCGTGTTGTGGGAGATTTTCACCTATGGCAAACAGCCCTGGTACCAGCTGTCAAACAAT
GAGGTGATAGAGTGTATCACTCAGGGCCGAGTCCTGCAGCGACCCCGCACGTGCCCCCAG
GAGGTGTATGAGCTGATGCTGGGGTGCTGGCAGCGAGAGCCCCACATGAGGAAGAACATC
AAGGGCATCCATACCCTCCTTCAGAACTTGGCCAAGGCATCTCCGGTCTACCTGGACATT
CTAGGCTAG
|
| Enzyme 109 GenBank Gene ID |
U12140 |
| Enzyme 109 GeneCard ID |
NTRK2 |
| Enzyme 109 GenAtlas ID |
NTRK2 |
| Enzyme 109 HGNC ID |
HGNC:8032 |
| Enzyme 109 Chromosome Location |
9 |
| Enzyme 109 Locus |
9q22.1 |
| Enzyme 109 SNPs |
SNPJam Report |
| Enzyme 109 General References |
- Nakagawara A, Liu XG, Ikegaki N, White PS, Yamashiro DJ, Nycum LM, Biegel JA, Brodeur GM: Cloning and chromosomal localization of the human TRK-B tyrosine kinase receptor gene (NTRK2). Genomics. 1995 Jan 20;25(2):538-46. [PubMed ]
- Shelton DL, Sutherland J, Gripp J, Camerato T, Armanini MP, Phillips HS, Carroll K, Spencer SD, Levinson AD: Human trks: molecular cloning, tissue distribution, and expression of extracellular domain immunoadhesins. J Neurosci. 1995 Jan;15(1 Pt 2):477-91. [PubMed ]
- Allen SJ, Dawbarn D, Eckford SD, Wilcock GK, Ashcroft M, Colebrook SM, Feeney R, MacGowan SH: Cloning of a non-catalytic form of human trkB and distribution of messenger RNA for trkB in human brain. Neuroscience. 1994 Jun;60(3):825-34. [PubMed ]
- Stoilov P, Castren E, Stamm S: Analysis of the human TrkB gene genomic organization reveals novel TrkB isoforms, unusual gene length, and splicing mechanism. Biochem Biophys Res Commun. 2002 Jan 25;290(3):1054-65. [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 ]
- Haniu M, Talvenheimo J, Le J, Katta V, Welcher A, Rohde MF: Extracellular domain of neurotrophin receptor trkB: disulfide structure, N-glycosylation sites, and ligand binding. Arch Biochem Biophys. 1995 Sep 10;322(1):256-64. [PubMed ]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed ]
- Ultsch MH, Wiesmann C, Simmons LC, Henrich J, Yang M, Reilly D, Bass SH, de Vos AM: Crystal structures of the neurotrophin-binding domain of TrkA, TrkB and TrkC. J Mol Biol. 1999 Jul 2;290(1):149-59. [PubMed ]
- Banfield MJ, Naylor RL, Robertson AG, Allen SJ, Dawbarn D, Brady RL: Specificity in Trk receptor:neurotrophin interactions: the crystal structure of TrkB-d5 in complex with neurotrophin-4/5. Structure. 2001 Dec;9(12):1191-9. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
- Marchetti A, Felicioni L, Pelosi G, Del Grammastro M, Fumagalli C, Sciarrotta M, Malatesta S, Chella A, Barassi F, Mucilli F, Camplese P, D'Antuono T, Sacco R, Buttitta F: Frequent mutations in the neurotrophic tyrosine receptor kinase gene family in large cell neuroendocrine carcinoma of the lung. Hum Mutat. 2008 May;29(5):609-16. [PubMed ]
|
| Enzyme 109 Metabolite References |
Not Available |
|
Enzyme 110
[top]
|
| Enzyme 110 ID |
6446 |
| Enzyme 110 Name |
Activin receptor type-2B |
| Enzyme 110 Synonyms |
- Activin receptor type IIB
- ACTR-IIB
|
| Enzyme 110 Gene Name |
ACVR2B |
| Enzyme 110 Protein Sequence |
>Activin receptor type-2B
MTAPWVALALLWGSLCAGSGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCY
ASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEAG
GPEVTYEPPPTAPTLLTVLAYSLLPIGGLSLIVLLAFWMYRHRKPPYGHVDIHEDPGPPP
PSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMK
HENLLQFIAAEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSY
LHEDVPWCRGEGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGDTHGQVG
TRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQ
HPSLEELQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERVSL
IRRSVNGTTSDCLVSLVTSVTNVDLPPKESSI
|
| Enzyme 110 Number of Residues |
512 |
| Enzyme 110 Molecular Weight |
57723.5 |
| Enzyme 110 Theoretical pI |
5.48 |
| Enzyme 110 GO Classification |
| Function |
- ATP binding
- activin receptor activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- receptor signaling protein serine/threonine kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transforming growth factor beta receptor activity
- transmembrane receptor protein serine/threonine kinase activity
|
| Process |
- activin receptor signaling pathway
- cell surface receptor linked signaling pathway
- cellular metabolic process
- enzyme linked receptor protein signaling pathway
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- signaling
- signaling pathway
- transmembrane receptor protein serine/threonine kinase signaling pathway
|
| Component |
|
|
| Enzyme 110 General Function |
Involved in receptor signaling protein serine/threonine kinase activity |
| Enzyme 110 Specific Function |
On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A |
| Enzyme 110 Pathways |
Not Available |
| Enzyme 110 Reactions |
- ATP + [receptor-protein] = ADP + [receptor-protein] phosphate
|
| Enzyme 110 Pfam Domain Function |
|
| Enzyme 110 Signals |
|
| Enzyme 110 Transmembrane Regions |
|
| Enzyme 110 Essentiality |
Not Available |
| Enzyme 110 GenBank ID Protein |
5731735 |
| Enzyme 110 UniProtKB/Swiss-Prot ID |
Q13705 |
| Enzyme 110 UniProtKB/Swiss-Prot Entry Name |
AVR2B_HUMAN |
| Enzyme 110 PDB ID |
1NYU |
| Enzyme 110 PDB File |
Show |
| Enzyme 110 3D Structure |
|
| Enzyme 110 Cellular Location |
Not Available |
| Enzyme 110 Gene Sequence |
>1539 bp
ATGACGGCGCCCTGGGTGGCCCTCGCCCTCCTCTGGGGATCGCTGTGCGCCGGCTCTGGG
CGTGGGGAGGCTGAGACACGGGAGTGCATCTACTACAACGCCAACTGGGAGCTGGAGCGC
ACCAACCAGAGCGGCCTGGAGCGCTGCGAAGGCGAGCAGGACAAGCGGCTGCACTGCTAC
GCCTCCTGGGCCAACAGCTCTGGCACCATCGAGCTCGTGAAGAAGGGCTGCTGGCTAGAT
GACTTCAACTGCTACGATAGGCAGGAGTGTGTGGCCACTGAGGAGAACCCCCAGGTGTAC
TTCTGCTGCTGTGAAGGCAACTTCTGCAACGAGCGCTTCACTCATTTGCCAGAGGCTGGG
GGCCCGGAAGTCACGTACGAGCCACCCCCGACAGCCCCCACCCTGCTCACGGTGCTGGCC
TACTCACTGCTGCCCATCGGGGGCCTTTCCCTCATCGTCCTGCTGGCCTTTTGGATGTAC
CGGCATCGCAAGCCCCCCTACGGTCATGTGGACATCCATGAGGACCCTGGGCCTCCACCA
CCATCCCCTCTGGTGGGCCTGAAGCCACTGCAGCTGCTGGAGATCAAGGCTCGGGGGCGC
TTTGGCTGTGTCTGGAAGGCCCAGCTCATGAATGACTTTGTAGCTGTCAAGATCTTCCCA
CTCCAGGACAAGCAGTCGTGGCAGAGTGAACGGGAGATCTTCAGCACACCTGGCATGAAG
CACGAGAACCTGCTACAGTTCATTGCTGCCGAGAAGCGAGGCTCCAACCTCGAAGTAGAG
CTGTGGCTCATCACGGCCTTCCATGACAAGGGCTCCCTCACGGATTACCTCAAGGGGAAC
ATCATCACATGGAACGAACTGTGTCATGTAGCAGAGACGATGTCACGAGGCCTCTCATAC
CTGCATGAGGATGTGCCCTGGTGCCGTGGCGAGGGCCACAAGCCGTCTATTGCCCACAGG
GACTTTAAAAGTAAGAATGTATTGCTGAAGAGCGACCTCACAGCCGTGCTGGCTGACTTT
GGCTTGGCTGTTCGATTTGAGCCAGGGAAACCTCCAGGGGACACCCACGGACAGGTAGGC
ACGAGACGGTACATGGCTCCTGAGGTGCTCGAGGGAGCCATCAACTTCCAGAGAGATGCC
TTCCTGCGCATTGACATGTATGCCATGGGGTTGGTGCTGTGGGAGCTTGTGTCTCGCTGC
AAGGCTGCAGACGGACCCGTGGATGAGTACATGCTGCCCTTTGAGGAAGAGATTGGCCAG
CACCCTTCGTTGGAGGAGCTGCAGGAGGTGGTGGTGCACAAGAAGATGAGGCCCACCATT
AAAGATCACTGGTTGAAACACCCGGGCCTGGCCCAGCTTTGTGTGACCATCGAGGATTGC
TGGGACCATGATGCAGAGGCTCGCTTGTCCGCGGGCTGTGTGGAGGAGCGGGTGTCCCTG
ATTCGGAGGTCGGTCAATGGCACTACCTCGGACTGTCTCGTTTCCCTGGTGACCTCTGTC
ACCAATGTGGACCTGCCCCCTAAAGAGTCAAGCATCTAA
|
| Enzyme 110 GenBank Gene ID |
AB008681 |
| Enzyme 110 GeneCard ID |
ACVR2B |
| Enzyme 110 GenAtlas ID |
ACVR2B |
| Enzyme 110 HGNC ID |
HGNC:174 |
| Enzyme 110 Chromosome Location |
3 |
| Enzyme 110 Locus |
3p22 |
| Enzyme 110 SNPs |
SNPJam Report |
| Enzyme 110 General References |
- Hilden K, Tuuri T, Eramaa M, Ritvos O: Expression of type II activin receptor genes during differentiation of human K562 cells and cDNA cloning of the human type IIB activin receptor. Blood. 1994 Apr 15;83(8):2163-70. [PubMed ]
- Ishikawa S, Kai M, Murata Y, Tamari M, Daigo Y, Murano T, Ogawa M, Nakamura Y: Genomic organization and mapping of the human activin receptor type IIB (hActR-IIB) gene. J Hum Genet. 1998;43(2):132-4. [PubMed ]
- Kosaki R, Gebbia M, Kosaki K, Lewin M, Bowers P, Towbin JA, Casey B: Left-right axis malformations associated with mutations in ACVR2B, the gene for human activin receptor type IIB. Am J Med Genet. 1999 Jan 1;82(1):70-6. [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 ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 110 Metabolite References |
Not Available |
|
Enzyme 111
[top]
|
| Enzyme 111 ID |
6447 |
| Enzyme 111 Name |
Death-associated protein kinase 2 |
| Enzyme 111 Synonyms |
- DAP kinase 2
- DAP-kinase-related protein 1
- DRP-1
|
| Enzyme 111 Gene Name |
DAPK2 |
| Enzyme 111 Protein Sequence |
>Death-associated protein kinase 2
MFQASMRSPNMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSR
ASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKES
LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIED
GVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANIT
AVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESV
VNLENFRKQYVRRRWKLSFSIVSLCNHLTRSLMKKVHLRPDEDLRNCESDTEEDIARRKA
LHPRRRSSTS
|
| Enzyme 111 Number of Residues |
370 |
| Enzyme 111 Molecular Weight |
42897.7 |
| Enzyme 111 Theoretical pI |
6.92 |
| Enzyme 111 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 111 General Function |
Involved in protein kinase activity |
| Enzyme 111 Specific Function |
Calcium/calmodulin-dependent serine/threonine kinase which acts as a positive regulator of apoptosis |
| Enzyme 111 Pathways |
Not Available |
| Enzyme 111 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 111 Pfam Domain Function |
|
| Enzyme 111 Signals |
|
| Enzyme 111 Transmembrane Regions |
|
| Enzyme 111 Essentiality |
Not Available |
| Enzyme 111 GenBank ID Protein |
6521210 |
| Enzyme 111 UniProtKB/Swiss-Prot ID |
Q9UIK4 |
| Enzyme 111 UniProtKB/Swiss-Prot Entry Name |
DAPK2_HUMAN |
| Enzyme 111 PDB ID |
Not Available |
| Enzyme 111 Cellular Location |
Not Available |
| Enzyme 111 Gene Sequence |
>1113 bp
ATGTTCCAGGCCTCAATGAGGAGTCCAAACATGGAGCCATTCAAGCAGCAGAAGGTGGAG
GACTTTTATGACATCGGAGAGGAGCTGGGGAGTGGCCAGTTTGCCATCGTGAAGAAGTGC
CGGGAGAAGAGCACGGGGCTTGAGTATGCAGCCAAGTTCATCAAGAAGCGGCAGAGCCGG
GCGAGCCGGCGCGGTGTGAGCCGGGAGGAGATCGAGCGGGAGGTGAGCATCCTGCGGCAG
GTGCTGCACCACAATGTCATCACGCTGCACGACGTCTATGAGAACCGCACCGACGTGGTG
CTCATCCTTGAGCTAGTGTCTGGAGGAGAGCTCTTCGATTTCCTGGCCCAGAAGGAGTCA
CTGAGTGAGGAGGAGGCCACCAGCTTCATTAAGCAGATCCTGGATGGGGTGAACTACCTT
CACACAAAGAAAATTGCTCACTTTGATCTCAAGCCAGAAAACATTATGTTGTTAGACAAG
AATATTCCCATTCCACACATCAAGCTGATTGACTTTGGTCTGGCTCACGAAATAGAAGAT
GGAGTTGAATTTAAGAATATTTTTGGGACGCCGGAATTTGTTGCTCCAGAAATTGTGAAC
TACGAGCCCCTGGGTCTGGAGGCTGACATGTGGAGCATAGGCGTCATCACCTACATCCTC
TTAAGTGGAGCATCCCCTTTCCTGGGAGACACGAAGCAGGAAACACTGGCAAATATCACA
GCAGTGAGTTACGACTTTGATGAGGAATTCTTCAGCCAGACGAGCGAGCTGGCCAAGGAC
TTTATTCGGAAGCTTCTGGTTAAAGAGACCCGGAAACGGCTCACAATCCAAGAGGCTCTC
AGACACCCCTGGATCACGCCGGTGGACAACCAGCAAGCCATGGTGCGCAGGGAGTCTGTG
GTCAATCTGGAGAACTTCAGGAAGCAGTATGTCCGCAGGCGGTGGAAGCTTTCCTTCAGC
ATCGTGTCCCTGTGCAACCACCTCACCCGCTCGCTGATGAAGAAGGTGCACCTGAGGCCG
GATGAGGACCTGAGGAACTGTGAGAGTGACACTGAGGAGGACATCGCCAGGAGGAAAGCC
CTCCACCCACGGAGGAGGAGCAGCACCTCCTAA
|
| Enzyme 111 GenBank Gene ID |
AB018001 |
| Enzyme 111 GeneCard ID |
DAPK2 |
| Enzyme 111 GenAtlas ID |
DAPK2 |
| Enzyme 111 HGNC ID |
HGNC:2675 |
| Enzyme 111 Chromosome Location |
1 |
| Enzyme 111 Locus |
15q22.31 |
| Enzyme 111 SNPs |
SNPJam Report |
| Enzyme 111 General References |
- Kawai T, Nomura F, Hoshino K, Copeland NG, Gilbert DJ, Jenkins NA, Akira S: Death-associated protein kinase 2 is a new calcium/calmodulin-dependent protein kinase that signals apoptosis through its catalytic activity. Oncogene. 1999 Jun 10;18(23):3471-80. [PubMed ]
- Inbal B, Shani G, Cohen O, Kissil JL, Kimchi A: Death-associated protein kinase-related protein 1, a novel serine/threonine kinase involved in apoptosis. Mol Cell Biol. 2000 Feb;20(3):1044-54. [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 ]
- Shani G, Henis-Korenblit S, Jona G, Gileadi O, Eisenstein M, Ziv T, Admon A, Kimchi A: Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding. EMBO J. 2001 Mar 1;20(5):1099-113. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 111 Metabolite References |
Not Available |
|
Enzyme 112
[top]
|
| Enzyme 112 ID |
6448 |
| Enzyme 112 Name |
Plasma membrane calcium-transporting ATPase 3 |
| Enzyme 112 Synonyms |
- PMCA3
- Plasma membrane calcium ATPase isoform 3
- Plasma membrane calcium pump isoform 3
|
| Enzyme 112 Gene Name |
ATP2B3 |
| Enzyme 112 Protein Sequence |
>Plasma membrane calcium-transporting ATPase 3
MGDMANSSIEFHPKPQQQRDVPQAGGFGCTLAELRTLMELRGAEALQKIEEAYGDVSGLC
RRLKTSPTEGLADNTNDLEKRRQIYGQNFIPPKQPKTFLQLVWEALQDVTLIILEVAAIV
SLGLSFYAPPGEESEACGNVSGGAEDEGEAEAGWIEGAAILLSVICVVLVTAFNDWSKEK
QFRGLQSRIEQEQKFTVIRNGQLLQVPVAALVVGDIAQVKYGDLLPADGVLIQANDLKID
ESSLTGESDHVRKSADKDPMLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEE
KKDKKGKQQDGAMESSQTKAKKQDGAVAMEMQPLKSAEGGEMEEREKKKANAPKKEKSVL
QGKLTKLAVQIGKAGLVMSAITVIILVLYFVIETFVVEGRTWLAECTPVYVQYFVKFFII
GVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTT
NRMTVVQSYLGDTHYKEIPAPSALTPKILDLLVHAISINSAYTTKILPPEKEGALPRQVG
NKTECALLGFVLDLKRDFQPVREQIPEDKLYKVYTFNSVRKSMSTVIRMPDGGFRLFSKG
ASEILLKKCTNILNSNGELRGFRPRDRDDMVRKIIEPMACDGLRTICIAYRDFSAGQEPD
WDNENEVVGDLTCIAVVGIEDPVRPEVPEAIRKCQRAGITVRMVTGDNINTARAIAAKCG
IIQPGEDFLCLEGKEFNRRIRNEKGEIEQERLDKVWPKLRVLARSSPTDKHTLVKGIIDS
TTGEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVM
WGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALA
TEPPTESLLLRKPYGRDKPLISRTMMKNILGHAVYQLAIIFTLLFVGELFFDIDSGRNAP
LHSPPSEHYTIIFNTFVMMQLFNEINARKIHGERNVFDGIFSNPIFCTIVLGTFGIQIVI
VQFGGKPFSCSPLSTEQWLWCLFVGVGELVWGQVIATIPTSQLKCLKEAGHGPGKDEMTD
EELAEGEEEIDHAERELRRGQILWFRGLNRIQTQIRVVKAFRSSLYEGLEKPESKTSIHN
FMATPEFLINDYTHNIPLIDDTDVDENEERLRAPPPPSPNQNNNAIDSGIYLTTHVTKSA
TSSVFSSSPGSPLHSVETSL
|
| Enzyme 112 Number of Residues |
1220 |
| Enzyme 112 Molecular Weight |
134196.0 |
| Enzyme 112 Theoretical pI |
5.29 |
| Enzyme 112 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- calcium ion transmembrane transporter activity
- calcium-transporting ATPase activity
- catalytic activity
- cation transmembrane transporter activity
- di-, tri-valent inorganic cation transmembrane transporter activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- inorganic cation transmembrane transporter activity
- ion transmembrane transporter activity
- nucleoside binding
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- calcium ion transport
- cation transport
- cellular nitrogen compound metabolic process
- di-, tri-valent inorganic cation transport
- divalent metal ion transport
- establishment of localization
- ion transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
|
|
| Enzyme 112 General Function |
Involved in ATP binding |
| Enzyme 112 Specific Function |
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell |
| Enzyme 112 Pathways |
Not Available |
| Enzyme 112 Reactions |
- ATP + H2O + Ca2+cis = ADP + phosphate + Ca2+trans [RN:R00086]
|
| Enzyme 112 Pfam Domain Function |
|
| Enzyme 112 Signals |
|
| Enzyme 112 Transmembrane Regions |
- 98-118
156-176
365-384
418-435
850-869
880-900
921-943
962-983
1003-1024
1035-1056
|
| Enzyme 112 Essentiality |
Not Available |
| Enzyme 112 GenBank ID Protein |
48255955 |
| Enzyme 112 UniProtKB/Swiss-Prot ID |
Q16720 |
| Enzyme 112 UniProtKB/Swiss-Prot Entry Name |
AT2B3_HUMAN |
| Enzyme 112 PDB ID |
Not Available |
| Enzyme 112 Cellular Location |
Not Available |
| Enzyme 112 Gene Sequence |
>3663 bp
ATGGGCGACATGGCCAATAGTTCCATCGAGTTCCACCCCAAGCCCCAGCAGCAGCGGGAT
GTCCCCCAGGCTGGAGGCTTTGGGTGCACGCTGGCGGAGCTGCGCACCCTCATGGAGCTG
CGAGGGGCCGAGGCGCTGCAGAAGATCGAGGAGGCCTACGGGGATGTCAGCGGGCTCTGC
CGGAGGCTGAAGACCTCACCCACAGAGGGCCTGGCGGACAACACCAATGACCTGGAGAAG
CGCAGGCAGATCTACGGGCAGAACTTCATCCCCCCAAAGCAACCCAAGACCTTCCTGCAG
CTGGTGTGGGAGGCCCTGCAGGACGTGACCCTCATCATCCTGGAGGTGGCTGCCATCGTC
TCTCTGGGCCTCTCGTTCTATGCGCCGCCAGGAGAGGAGAGTGAAGCCTGTGGGAATGTG
TCGGGAGGCGCAGAAGATGAGGGCGAGGCCGAAGCTGGCTGGATCGAGGGGGCTGCCATC
CTGCTGTCCGTCATCTGTGTGGTGCTGGTCACGGCCTTCAATGACTGGAGCAAGGAGAAG
CAGTTCCGAGGCCTGCAGAGCCGAATTGAGCAGGAGCAGAAGTTCACGGTCATCCGGAAC
GGGCAGCTCCTCCAGGTCCCCGTGGCTGCGCTGGTGGTGGGGGACATTGCCCAGGTCAAG
TACGGCGACCTGCTGCCAGCCGACGGCGTGCTCATCCAGGCCAATGACCTCAAGATCGAC
GAGAGCTCCCTGACGGGCGAGTCTGACCACGTGCGCAAGTCAGCTGACAAAGATCCCATG
CTGCTCTCAGGCACTCATGTCATGGAAGGTTCTGGAAGAATGGTGGTGACCGCCGTTGGC
GTGAATTCCCAGACAGGCATCATCTTCACGCTGCTTGGAGCTGGCGGAGAGGAGGAAGAG
AAGAAAGATAAGAAAGGCAAGCAGCAGGATGGGGCCATGGAGAGTAGCCAGACCAAAGCT
AAGAAGCAGGATGGTGCAGTGGCCATGGAGATGCAGCCCCTGAAGAGCGCGGAGGGTGGG
GAGATGGAGGAGCGGGAGAAGAAGAAAGCCAACGCACCCAAAAAGGAGAAGTCTGTCCTT
CAGGGGAAGCTCACAAAGCTAGCCGTGCAGATCGGGAAAGCAGGGCTGGTGATGTCTGCC
ATCACCGTCATCATCCTGGTCCTCTACTTTGTGATTGAGACGTTTGTCGTGGAAGGCCGG
ACATGGCTGGCAGAGTGCACGCCGGTCTATGTACAATACTTCGTGAAGTTCTTCATCATT
GGTGTCACTGTGCTGGTCGTGGCTGTCCCAGAGGGCCTGCCTCTTGCTGTCACCATCTCC
TTAGCTTACTCTGTCAAGAAAATGATGAAAGACAACAACCTGGTGCGCCACCTGGATGCC
TGCGAGACCATGGGCAACGCCACAGCCATCTGCTCCGACAAGACGGGCACGCTCACCACC
AACCGTATGACCGTGGTCCAGTCCTACCTAGGAGACACCCACTACAAAGAGATTCCGGCC
CCCAGCGCCCTGACCCCTAAGATCCTCGACCTCCTGGTCCATGCCATCTCCATCAACAGT
GCCTATACCACCAAAATACTACCTCCTGAGAAGGAAGGCGCCCTCCCACGCCAGGTGGGC
AATAAGACGGAGTGCGCCCTGCTGGGCTTCGTCTTGGACCTGAAGCGGGACTTCCAGCCC
GTGCGCGAGCAGATCCCGGAAGACAAGCTTTACAAAGTGTACACCTTCAACTCGGTCCGC
AAGTCCATGAGCACAGTCATCCGCATGCCCGACGGTGGCTTCCGCCTCTTCAGCAAGGGG
GCCTCAGAGATCCTCTTGAAAAAGTGCACCAACATCTTGAACAGCAATGGCGAACTCCGG
GGCTTTCGGCCTCGGGACCGGGACGACATGGTGAGGAAGATCATCGAGCCGATGGCTTGC
GATGGCCTCCGCACCATCTGCATCGCCTACCGGGACTTCTCTGCAGGCCAGGAGCCCGAC
TGGGACAACGAGAATGAGGTCGTGGGTGACCTCACCTGCATAGCTGTCGTGGGCATTGAG
GACCCTGTGCGGCCCGAGGTCCCTGAAGCTATCCGAAAATGCCAGCGTGCTGGCATCACA
GTCCGCATGGTGACTGGGGACAACATCAACACGGCCCGGGCCATCGCAGCCAAATGCGGC
ATCATCCAGCCCGGGGAGGACTTCCTGTGCCTAGAAGGGAAGGAGTTCAACCGGCGGATC
CGCAATGAGAAAGGCGAGATAGAACAGGAGCGGCTGGACAAGGTGTGGCCCAAGCTGAGG
GTGCTGGCCCGGTCGTCTCCCACCGACAAGCACACACTGGTCAAAGGGATTATCGACAGC
ACCACTGGTGAGCAGCGGCAGGTGGTGGCTGTGACAGGGGATGGCACCAACGATGGGCCG
GCCCTCAAGAAGGCGGACGTGGGCTTCGCCATGGGCATCGCAGGGACCGACGTGGCCAAG
GAGGCCTCCGACATCATCCTGACCGATGACAACTTCACCAGCATCGTCAAGGCAGTCATG
TGGGGCCGTAACGTCTATGACAGCATCTCCAAGTTCCTGCAGTTTCAACTGACGGTCAAT
GTGGTGGCTGTGATCGTGGCCTTCACAGGTGCCTGCATTACTCAGGACTCTCCTCTCAAA
GCCGTGCAGATGTTGTGGGTGAACTTGATCATGGACACATTTGCCTCTCTGGCCCTGGCG
ACGGAGCCACCCACAGAGTCGCTGCTGCTGCGGAAGCCGTACGGCCGCGACAAGCCCCTC
ATCTCCCGCACCATGATGAAGAACATTCTGGGCCACGCCGTGTACCAGCTCGCCATCATC
TTCACCCTGCTGTTTGTCGGGGAGCTCTTCTTCGACATCGACAGCGGGAGGAATGCGCCC
CTGCACTCGCCACCCTCAGAGCACTACACCATCATCTTCAACACGTTCGTCATGATGCAG
CTCTTTAACGAGATCAACGCCCGCAAGATCCACGGCGAGAGGAACGTGTTCGACGGCATC
TTCAGCAACCCCATCTTCTGCACCATCGTTTTGGGCACTTTCGGGATTCAGATTGTCATC
GTCCAGTTTGGCGGGAAGCCCTTCAGCTGCTCCCCACTATCCACAGAACAGTGGCTCTGG
TGCCTGTTTGTTGGTGTTGGGGAGCTGGTCTGGGGACAGGTCATTGCCACCATCCCCACC
AGCCAGCTCAAGTGCCTGAAGGAAGCCGGGCACGGGCCCGGGAAGGACGAGATGACCGAC
GAGGAGCTGGCCGAAGGCGAGGAAGAGATCGACCATGCCGAGCGGGAGCTCCGCAGGGGC
CAGATCCTCTGGTTCCGGGGCCTGAACCGGATTCAGACGCAGATCCGGGTGGTGAAAGCG
TTCCGTAGCTCGCTCTATGAAGGCCTGGAGAAACCAGAATCCAAGACCTCCATTCACAAC
TTCATGGCCACGCCCGAGTTTCTGATCAATGACTACACCCACAACATCCCGCTCATTGAC
GACACGGACGTGGACGAGAACGAGGAGCGCCTCCGGGCCCCCCCGCCCCCGTCCCCCAAC
CAGAACAACAACGCCATAGACAGCGGCATCTACCTGACCACGCATGTCACCAAGTCAGCT
ACCTCTTCAGTGTTTTCCTCCAGTCCCGGGAGCCCGCTCCACAGCGTGGAGACGTCCCTC
TAA
|
| Enzyme 112 GenBank Gene ID |
NM_001001344.2 |
| Enzyme 112 GeneCard ID |
ATP2B3 |
| Enzyme 112 GenAtlas ID |
ATP2B3 |
| Enzyme 112 HGNC ID |
HGNC:816 |
| Enzyme 112 Chromosome Location |
Not Available |
| Enzyme 112 Locus |
Not Available |
| Enzyme 112 SNPs |
SNPJam Report |
| Enzyme 112 General References |
- Brown BJ, Hilfiker H, DeMarco SJ, Zacharias DA, Greenwood TM, Guerini D, Strehler EE: Primary structure of human plasma membrane Ca(2+)-ATPase isoform 3. Biochim Biophys Acta. 1996 Aug 14;1283(1):10-3. [PubMed ]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed ]
- Wang MG, Yi H, Hilfiker H, Carafoli E, Strehler EE, McBride OW: Localization of two genes encoding plasma membrane Ca2+ ATPases isoforms 2 (ATP2B2) and 3 (ATP2B3) to human chromosomes 3p26-->p25 and Xq28, respectively. Cytogenet Cell Genet. 1994;67(1):41-5. [PubMed ]
- Mallon AM, Platzer M, Bate R, Gloeckner G, Botcherby MR, Nordsiek G, Strivens MA, Kioschis P, Dangel A, Cunningham D, Straw RN, Weston P, Gilbert M, Fernando S, Goodall K, Hunter G, Greystrong JS, Clarke D, Kimberley C, Goerdes M, Blechschmidt K, Rump A, Hinzmann B, Mundy CR, Miller W, Poustka A, Herman GE, Rhodes M, Denny P, Rosenthal A, Brown SD: Comparative genome sequence analysis of the Bpa/Str region in mouse and Man. Genome Res. 2000 Jun;10(6):758-75. [PubMed ]
- Stauffer TP, Hilfiker H, Carafoli E, Strehler EE: Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. J Biol Chem. 1993 Dec 5;268(34):25993-6003. [PubMed ]
- Stauffer TP, Hilfiker H, Carafoli E, Strehler EE: Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. J Biol Chem. 1994 Dec 16;269(50):32022. [PubMed ]
|
| Enzyme 112 Metabolite References |
Not Available |
|
Enzyme 113
[top]
|
| Enzyme 113 ID |
6449 |
| Enzyme 113 Name |
RAF proto-oncogene serine/threonine-protein kinase |
| Enzyme 113 Synonyms |
- Proto-oncogene c-RAF
- cRaf
- Raf-1
|
| Enzyme 113 Gene Name |
RAF1 |
| Enzyme 113 Protein Sequence |
>RAF proto-oncogene serine/threonine-protein kinase
MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRV
FLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAAS
LIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKV
PTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTF
NTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNL
SPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSF
GTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIV
TQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL
TVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYE
LMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFP
QILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF
|
| Enzyme 113 Number of Residues |
648 |
| Enzyme 113 Molecular Weight |
73051.0 |
| Enzyme 113 Theoretical pI |
9.62 |
| Enzyme 113 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- molecular transducer activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- receptor signaling protein activity
- signal transducer activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biological regulation
- cellular metabolic process
- intracellular signaling pathway
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 113 General Function |
Involved in intracellular signaling pathway |
| Enzyme 113 Specific Function |
Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. Part of the Ras-dependent signaling pathway from receptors to the nucleus. Protects cells from apoptosis mediated by STK3 |
| Enzyme 113 Pathways |
Not Available |
| Enzyme 113 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 113 Pfam Domain Function |
|
| Enzyme 113 Signals |
|
| Enzyme 113 Transmembrane Regions |
|
| Enzyme 113 Essentiality |
Not Available |
| Enzyme 113 GenBank ID Protein |
35842 |
| Enzyme 113 UniProtKB/Swiss-Prot ID |
P04049 |
| Enzyme 113 UniProtKB/Swiss-Prot Entry Name |
RAF1_HUMAN |
| Enzyme 113 PDB ID |
Not Available |
| Enzyme 113 Cellular Location |
Not Available |
| Enzyme 113 Gene Sequence |
>1947 bp
ATGGAGCACATACAGGGAGCTTGGAAGACGATCAGCAATGGTTTTGGATTCAAAGATGCC
GTGTTTGATGGCTCCAGCTGCATCTCTCCTACAATAGTTCAGCAGTTTGGCTATCAGCGC
CGGGCATCAGATGATGGCAAACTCACAGATCCTTCTAAGACAAGCAACACTATCCGTGTT
TTCTTGCCGAACAAGCAAAGAACAGTGGTCAATGTGCGAAATGGAATGAGCTTGCATGAC
TGCCTTATGAAAGCACTCAAGGTGAGGGGCCTGCAACCAGAGTGCTGTGCAGTGTTCAGA
CTTCTCCACGAACACAAAGGTAAAAAAGCACGCTTAGATTGGAATACTGATGCTGCGTCT
TTGATTGGAGAAGAACTTCAAGTAGATTTCCTGGATCATGTTCCCCTCACAACACACAAC
TTTGCTCGGAAGACGTTCCTGAAGCTTGCCTTCTGTGACATCTGTCAGAAATTCCTGCTC
AATGGATTTCGATGTCAGACTTGTGGCTACAAATTTCATGAGCACTGTAGCACCAAAGTA
CCTACTATGTGTGTGGACTGGAGTAACATCAGACAACTCTTATTGTTTCCAAATTCCACT
ATTGGTGATAGTGGAGTCCCAGCACTACCTTCTTTGACTATGCGTCGTATGCGAGAGTCT
GTTTCCAGGATGCCTGTTAGTTCTCAGCACAGATATTCTACACCTCACGCCTTCACCTTT
AACACCTCCAGTCCCTCATCTGAAGGTTCCCTCTCCCAGAGGCAGAGGTCGACATCCACA
CCTAATGTCCACATGGTCAGCACCACGCTGCCTGTGGACAGCAGGATGATTGAGGATGCA
ATTCGAAGTCACAGCGAATCAGCCTCACCTTCAGCCCTGTCCAGTAGCCCCAACAATCTG
AGCCCAACAGGCTGGTCACAGCCGAAAACCCCCGTGCCAGCACAAAGAGAGCGGGCACCA
GTATCTGGGACCCAGGAGAAAAACAAAATTAGGCCTCGTGGACAGAGAGATTCAAGCTAT
TATTGGGAAATAGAAGCCAGTGAAGTGATGCTGTCCACTCGGATTGGGTCAGGCTCTTTT
GGAACTGTTTATAAGGGTAAATGGCACGGAGATGTTGCAGTAAAGATCCTAAAGGTTGTC
GACCCAACCCCAGAGCAATTCCAGGCCTTCAGGAATGAGGTGGCTGTTCTGCGCAAAACA
CGGCATGTGAACATTCTGCTTTTCATGGGGTACATGACAAAGGACAACCTGGCAATTGTG
ACCCAGTGGTGCGAGGGCAGCAGCCTCTACAAACACCTGCATGTCCAGGAGACCAAGTTT
CAGATGTTCCAGCTAATTGACATTGCCCGGCAGACGGCTCAGGGAATGGACTATTTGCAT
GCAAAGAACATCATCCATAGAGACATGAAATCCAACAATATATTTCTCCATGAAGGCTTA
ACAGTGAAAATTGGAGATTTTGGTTTGGCAACAGTAAAGTCACGCTGGAGTGGTTCTCAG
CAGGTTGAACAACCTACTGGCTCTGTCCTCTGGATGGCCCCAGAGGTGATCCGAATGCAG
GATAACAACCCATTCAGTTTCCAGTCGGATGTCTACTCCTATGGCATCGTATTGTATGAA
CTGATGACGGGGGAGCTTCCTTATTCTCACATCAACAACCGAGATCAGATCATCTTCATG
GTGGGCCGAGGATATGCCTCCCCAGATCTTAGTAAGCTATATAAGAACTGCCCCAAAGCA
ATGAAGAGGCTGGTAGCTGACTGTGTGAAGAAAGTAAAGGAAGAGAGGCCTCTTTTTCCC
CAGATCCTGTCTTCCATTGAGCTGCTCCAACACTCTCTACCGAAGATCAACCGGAGCGCT
TCCGAGCCATCCTTGCATCGGGCAGCCCACACTGAGGATATCAATGCTTGCACGCTGACC
ACGTCCCCGAGGCTGCCTGTCTTCTAG
|
| Enzyme 113 GenBank Gene ID |
X03484 |
| Enzyme 113 GeneCard ID |
RAF1 |
| Enzyme 113 GenAtlas ID |
RAF1 |
| Enzyme 113 HGNC ID |
HGNC:9829 |
| Enzyme 113 Chromosome Location |
3 |
| Enzyme 113 Locus |
3p25 |
| Enzyme 113 SNPs |
SNPJam Report |
| Enzyme 113 General References |
- Bonner TI, Oppermann H, Seeburg P, Kerby SB, Gunnell MA, Young AC, Rapp UR: The complete coding sequence of the human raf oncogene and the corresponding structure of the c-raf-1 gene. Nucleic Acids Res. 1986 Jan 24;14(2):1009-15. [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 ]
- Bonner TI, Kerby SB, Sutrave P, Gunnell MA, Mark G, Rapp UR: Structure and biological activity of human homologs of the raf/mil oncogene. Mol Cell Biol. 1985 Jun;5(6):1400-7. [PubMed ]
- Yao B, Zhang Y, Delikat S, Mathias S, Basu S, Kolesnick R: Phosphorylation of Raf by ceramide-activated protein kinase. Nature. 1995 Nov 16;378(6554):307-10. [PubMed ]
- Dozier C, Ansieau S, Ferreira E, Coll J, Stehelin D: An alternatively spliced c-mil/raf mRNA is predominantly expressed in chicken muscular tissues and conserved among vertebrate species. Oncogene. 1991 Aug;6(8):1307-11. [PubMed ]
- Morrison DK, Heidecker G, Rapp UR, Copeland TD: Identification of the major phosphorylation sites of the Raf-1 kinase. J Biol Chem. 1993 Aug 15;268(23):17309-16. [PubMed ]
- Dubois T, Rommel C, Howell S, Steinhussen U, Soneji Y, Morrice N, Moelling K, Aitken A: 14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction. J Biol Chem. 1997 Nov 14;272(46):28882-8. [PubMed ]
- King AJ, Sun H, Diaz B, Barnard D, Miao W, Bagrodia S, Marshall MS: The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338. Nature. 1998 Nov 12;396(6707):180-3. [PubMed ]
- Wang Y, Waldron RT, Dhaka A, Patel A, Riley MM, Rozengurt E, Colicelli J: The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-3 proteins. Mol Cell Biol. 2002 Feb;22(3):916-26. [PubMed ]
- Kunapuli P, Kasyapa CS, Hawthorn L, Cowell JK: LGI1, a putative tumor metastasis suppressor gene, controls in vitro invasiveness and expression of matrix metalloproteinases in glioma cells through the ERK1/2 pathway. J Biol Chem. 2004 May 28;279(22):23151-7. Epub 2004 Mar 26. [PubMed ]
- O'Neill E, Rushworth L, Baccarini M, Kolch W: Role of the kinase MST2 in suppression of apoptosis by the proto-oncogene product Raf-1. Science. 2004 Dec 24;306(5705):2267-70. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Rodriguez-Viciana P, Oses-Prieto J, Burlingame A, Fried M, McCormick F: A phosphatase holoenzyme comprised of Shoc2/Sur8 and the catalytic subunit of PP1 functions as an M-Ras effector to modulate Raf activity. Mol Cell. 2006 Apr 21;22(2):217-30. [PubMed ]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed ]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed ]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A: The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature. 1995 Jun 15;375(6532):554-60. [PubMed ]
- Nassar N, Horn G, Herrmann C, Block C, Janknecht R, Wittinghofer A: Ras/Rap effector specificity determined by charge reversal. Nat Struct Biol. 1996 Aug;3(8):723-9. [PubMed ]
- Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC: Solution structure of the Ras-binding domain of c-Raf-1 and identification of its Ras interaction surface. Biochemistry. 1995 May 30;34(21):6911-8. [PubMed ]
- Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL: The solution structure of the Raf-1 cysteine-rich domain: a novel ras and phospholipid binding site. Proc Natl Acad Sci U S A. 1996 Aug 6;93(16):8312-7. [PubMed ]
- Pandit B, Sarkozy A, Pennacchio LA, Carta C, Oishi K, Martinelli S, Pogna EA, Schackwitz W, Ustaszewska A, Landstrom A, Bos JM, Ommen SR, Esposito G, Lepri F, Faul C, Mundel P, Lopez Siguero JP, Tenconi R, Selicorni A, Rossi C, Mazzanti L, Torrente I, Marino B, Digilio MC, Zampino G, Ackerman MJ, Dallapiccola B, Tartaglia M, Gelb BD: Gain-of-function RAF1 mutations cause Noonan and LEOPARD syndromes with hypertrophic cardiomyopathy. Nat Genet. 2007 Aug;39(8):1007-12. Epub 2007 Jul 1. [PubMed ]
- Razzaque MA, Nishizawa T, Komoike Y, Yagi H, Furutani M, Amo R, Kamisago M, Momma K, Katayama H, Nakagawa M, Fujiwara Y, Matsushima M, Mizuno K, Tokuyama M, Hirota H, Muneuchi J, Higashinakagawa T, Matsuoka R: Germline gain-of-function mutations in RAF1 cause Noonan syndrome. Nat Genet. 2007 Aug;39(8):1013-7. Epub 2007 Jul 1. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 113 Metabolite References |
Not Available |
|
Enzyme 114
[top]
|
| Enzyme 114 ID |
6452 |
| Enzyme 114 Name |
Myosin-IIIa |
| Enzyme 114 Synonyms |
Not Available |
| Enzyme 114 Gene Name |
MYO3A |
| Enzyme 114 Protein Sequence |
>Myosin-IIIa
MFPLIGKTIIFDNFPDPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDE
EIEAEYNILKALSDHPNVVRFYGIYFKKDKVNGDKLWLVLELCSGGSVTDLVKGFLKRGE
RMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRH
RRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALF
KIPRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQKQ
LTEFIGIHQCMGGTEKARRERIHTKKGNFNRPLISNLKDVDDLATLEILDENTVSEQLEK
CYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMIT
YNSDQCIVISGESGAGKTENAHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTII
NDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKK
KLAHYKLPENKPPRYLQNDHLRTVQDIMNNSFYKSQYELIEQCFKVIGFTMEQLGSIYSI
LAAILNVGNIEFSSVATEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGE
TIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNGDELSIGILDIFG
FENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFL
QKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRPKRMELSFGIHHYAGKVLYNA
SGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGNLPHSKTKNVINYQMRTSEKL
INLAKGDTGEATRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQA
RKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPDTCA
TILEKAGLDNWALGKTKVFLKYYHVEQLNLMRKEAIDKLILIQACVRAFLCSRRYQKIQE
KRKESAIIIQSAARGHLVRKQRKEIVDMKNTAVTTIQTSDQEFDYKKNFENTRESFVKKQ
AENAISANERFISAPNNKGSVSVVKTSTFKPEEETTNAVESNNRVYQTPKKMNNVYEEEV
KQEFYLVGPEVSPKQKSVKDLEENSNLRKVEKEEAMIQSYYQRYTEERNCEESKAAYLER
KAISERPSYPVPWLAENETSFKKTLEPTLSQRSIYQNANSMEKEKKTSVVTQRAPICSQE
EGRGRLRHETVKERQVEPVTQAQEEEDKAAVFIQSKYRGYKRRQQLRKDKMSSFKHQRIV
TTPTEVARNTHNLYSYPTKHEEINNIKKKDNKDSKATSEREACGLAIFSKQISKLSEEYF
ILQKKLNEMILSQQLKSLYLGVSHHKPINRRVSSQQCLSGVCKGEEPKILRPPRRPRKPK
TLNNPEDSTYYYLLHKSIQEEKRRPRKDSQGKLLDLEDFYYKEFLPSRSGPKEHSPSLRE
RRPQQELQNQCIKANERCWAAESPEKEEEREPAANPYDFRRLLRKTSQRRRLVQQS
|
| Enzyme 114 Number of Residues |
1616 |
| Enzyme 114 Molecular Weight |
186207.0 |
| Enzyme 114 Theoretical pI |
9.25 |
| Enzyme 114 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
- kinase activity
- motor activity
- nucleoside binding
- nucleoside-triphosphatase activity
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- pyrophosphatase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
- macromolecular complex
- myosin complex
- protein complex
|
|
| Enzyme 114 General Function |
Involved in motor activity |
| Enzyme 114 Specific Function |
Probable actin-based motor with a protein kinase activity. Probably plays a role in vision and hearing |
| Enzyme 114 Pathways |
Not Available |
| Enzyme 114 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 114 Pfam Domain Function |
|
| Enzyme 114 Signals |
|
| Enzyme 114 Transmembrane Regions |
|
| Enzyme 114 Essentiality |
Not Available |
| Enzyme 114 GenBank ID Protein |
7958618 |
| Enzyme 114 UniProtKB/Swiss-Prot ID |
Q8NEV4 |
| Enzyme 114 UniProtKB/Swiss-Prot Entry Name |
MYO3A_HUMAN |
| Enzyme 114 PDB ID |
Not Available |
| Enzyme 114 Cellular Location |
Not Available |
| Enzyme 114 Gene Sequence |
>4848 bp
ATGTTTCCATTAATTGGAAAAACAATCATCTTTGATAACTTTCCTGATCCTTCTGATACA
TGGGAAATCACTGAGACAATTGGCAAAGGAACTTATGGGAAAGTTTTTAAAGTATTGAAT
AAGAAAAATGGCCAAAAAGCAGCAGTCAAAATTCTTGATCCAATTCACGATATTGACGAA
GAGATTGAAGCAGAATATAACATCTTAAAAGCACTTTCTGACCACCCTAATGTGGTCAGA
TTCTATGGGATATACTTTAAGAAGGATAAAGTAAATGGAGACAAGCTGTGGTTGGTTCTT
GAGCTCTGCAGTGGAGGATCAGTGACTGACCTTGTGAAAGGATTTCTGAAGAGGGGTGAA
AGAATGAGTGAGCCTCTAATTGCCTATATTTTACATGAAGCACTAATGGGACTTCAACAT
TTGCATAACAACAAAACTATCCACAGAGATGTGAAAGGCAATAACATTCTATTGACCACG
GAAGGTGGAGTGAAACTAGTAGATTTTGGTGTGTCTGCACAGCTCACCAGTACCCGGCAC
CGTCGGAACACATCCGTAGGAACACCGTTTTGGATGGCTCCTGAGGTGATTGCATGTGAA
CAGCAATTGGATACCACTTATGACGCCAGATGTGACACTTGGTCCCTGGGTATCACGGCC
ATTGAGCTGGGTGATGGAGATCCTCCACTAGCTGACCTTCATCCCATGAGAGCACTCTTC
AAAATACCAAGGAATCCACCCCCAAAACTAAGGCAGCCTGAGCTATGGTCAGCAGAATTC
AATGACTTCATAAGCAAGTGCTTGACTAAAGATTATGAAAAGCGTCCAACAGTGTCAGAA
CTTTTACAGCATAAATTCATTACTCAAATTGAGGGCAAAGATGTGATGCTACAAAAACAA
CTAACGGAATTCATTGGCATCCATCAATGCATGGGAGGCACAGAAAAGGCCAGACGTGAA
CGTATTCACACGAAGAAAGGGAACTTCAACCGACCTCTAATATCCAATCTGAAGGATGTA
GATGATTTAGCAACCCTAGAAATTTTGGATGAGAATACAGTCTCAGAGCAACTTGAGAAG
TGTTATTCCAGAGATCAGATCTACGTCTATGTGGGAGACATACTCATTGCTCTTAACCCT
TTTCAGAGTCTGGGTCTTTACTCCACAAAGCATTCCAAACTATATATTGGATCAAAGAGA
ACTGCCAGTCCTCCTCACATTTTTGCAATGGCTGACTTAGGATATCAATCTATAATAACA
TATAATTCAGATCAGTGCATTGTTATTTCTGGAGAAAGTGGTGCTGGAAAGACTGAAAAT
GCTCATCTTTTAGTTCAGCAGCTGACAGTGCTTGGAAAGGCTAATAACAGAACCTTGCAA
GAGAAGATTTTACAAGTGAACAATTTGGTAGAAGCCTTTGGCAATGCCTGCACTATTATA
AATGACAATTCTAGCAGATTTGGAAAATACTTAGAAATGAAATTCACCTCTTCTGGAGCG
GTAGTGGGAGCACAGATTTCTGAATATCTCCTGGAAAAATCCCGAGTTATCCACCAAGCT
ATTGGAGAAAAAAATTTTCATATTTTTTACTACATTTATGCTGGTTTGGCTGAAAAGAAG
AAACTAGCCCATTACAAACTGCCTGAAAATAAGCCTCCCAGGTACCTACAAAATGACCAC
CTCAGAACAGTACAAGACATCATGAATAATAGTTTCTATAAATCCCAGTATGAATTAATT
GAGCAATGTTTCAAAGTCATAGGTTTTACAATGGAGCAACTTGGTAGTATATACAGCATA
CTCGCTGCAATCTTGAATGTTGGCAACATTGAATTTTCTTCTGTGGCAACTGAACACCAG
ATTGACAAGAGCCACATTTCTAATCATACAGCCCTGGAGAACTGTGTTTCTTTGCTTTGC
ATTCGGGCAGATGAGCTACAAGAAGCTCTCACCTCCCACTGTGTGGTCACTAGAGGAGAA
ACAATTATACGACCCAATACTGTAGAAAAAGCTACCGATGTCAGGGATGCCATGGCTAAA
ACTTTATATGGACGTCTCTTTAGTTGGATAGTCAATTGCATTAACAGTTTGTTGAAGCAT
GACTCATCACCAAGTGGGAATGGTGATGAGCTGAGCATTGGCATTCTTGATATATTTGGT
TTTGAAAATTTCAAAAAAAATTCCTTCGAGCAGCTGTGCATTAACATTGCAAATGAACAA
ATTCAGTATTATTATAATCAACATGTGTTTGCATGGGAACAGAATGAATACCTAAATGAA
GATGTGGATGCTAGAGTTATTGAATATGAGGATAACTGGCCCCTCTTAGATATGTTTCTG
CAAAAGCCAATGGGTTTACTTTCCCTACTTGATGAAGAAAGTAGATTTCCCAAGGCCACT
GACCAGACTCTTGTAGAAAAATTTGAAGGTAACCTGAAATCACAATACTTCTGGAGACCC
AAAAGAATGGAACTTAGTTTTGGAATTCACCATTATGCAGGAAAGGTCCTCTATAATGCA
AGTGGATTCTTAGCCAAAAACAAGACACTAGTTCCTACTGACATTGTGCTACTTTTGAGG
TCATCCGACAACAGTGTAATTAGGCAACTAGTCAACCACCCTCTGACCAAAACAGGTAAT
CTGCCACATTCTAAACTAAAAATGTTAAACTATCAAATGAGGACTTCAGAAAAATTAATC
AACCTGGCAAAGGGCGACACTGGAGAAGCCACACGTCATGCCAGAGAGACAACCAACATG
AAAACACAAACGGTTGCATCATATTTTAGATATTCCCTGATGGATTTGTTGTCTAAAATG
GTGGTGGGCCAACCTCATTTTGTCCGTTGCATCAAACCAAATAGTGAGCGTCAGGCAAGA
AAATATGACAAAGAGAAAGTTCTGCTACAGCTTCGGTACACAGGAATTCTGGAAACAGCA
AGAATTCGAAGACTAGGATTCTCCCATCGGATACTTTTTGCTAACTTTATAAAGCGGTAC
TACCTTCTCTGCTACAAGTCGAGCGAGGAGCCCCGCATGAGCCCTGACACCTGTGCCACC
ATTTTGGAAAAAGCTGGTCTCGATAACTGGGCTCTTGGAAAAACAAAAGTGTTCCTTAAG
TATTATCACGTGGAGCAGTTAAATCTAATGCGAAAGGAAGCTATTGACAAGCTTATTTTG
ATTCAAGCTTGTGTCAGAGCATTCTTGTGTTCAAGAAGATACCAAAAAATACAGGAGAAA
AGGAAAGAAAGCGCTATAATAATACAGTCAGCTGCAAGAGGACACCTTGTCGGGAAACAA
AGAAAAGAAATTGTTGACATGAAAAACACAGCAGTAACAACCATTCAAACTTCTGATCAG
GAATTCGACTACAAGAAAAACTTTGAAAATACAAGGGAATCTTTCGTGAAGAAACAAGCA
GAAAATGCAATCTCTGCTAATGAAAGATTCATTTCAGCTCCAAATAATAAAGGAAGTGTA
TCTGTAGTGAAGACTTCCACTTTCAAACCTGAAGAGGAAACCACCAATGCTGTGGAGAGT
AACAACAGAGTGTATCAGACTCCAAAAAAAATGAATAATGTGTATGAGGAAGAGGTTAAG
CAAGAATTTTACCTTGTAGGGCCAGAAGTAAGCCCCAAACAGAAGTTTGTCAAAGACCTG
GAAGAGAACAGCAATCTAAGGAAAGTGGAGAAAGAGGAAGCTATGATCCAGAGTTACTAT
CAGAGGTACACAGAGGAGAGGAATTGTGAAGAGTCAAAAGCAGCATATCTAGAAAGGAAG
GCCATATCAGAAAGGCCAAGCTACCCAGTGCCTTGGTTAGCTGAAAATGAGACTTCCTTT
AAAAAAACTTTGGAACCTACACTTAGCCAAAGGTCAATTTATCAAAATGCAAACAGCATG
GAAAAAGAAAAGAAGACATCTGTAGTTACCCAGAGTGCACCGATATGCAGCCAGGAGGAA
GGCAGAGGCCGTCTGAGGCATGAGACAGTCAAAGAGAGGCAAGTTGAACCAGTGACACAG
GCCCAGGAGGAAGAAGATAAAGCAGCGGTATTCATTCAGAGCAAATACCGGGGTTACAAG
AGAAGGCAGCAGTTGAGGAAGGACAAGATGTCTTCTTTTAAGCATCAGAAGATTGTCACA
ACACCAACAGAAGTAGCAAGAAACACTCATAATTTGTATTCCTATCCCACAAAACATGAG
GAAATCAATAACATCAAGAAGAAGGATAACAAAGACTCGAAAGCAACTTCAGAAAGAGAA
GCATGTGGTTTGGCAATTTTTTCAAAACAGATATCAAAGTTATCTGAAGAATATTTCATT
CTGCAGAAAAAATTGAATGAAATGATTTTGTCACAGCAACTGAAGTCACTTTATCTGGGT
GTCTCGCACCATAAGCCAATTAATAGACGAGTTTCTTCTCAGCAGTGCCTCTCAGGTGTC
TGTAAAGGAGAGGAGCCAAAAATATTGAGACCCCCAAGACGACCCCGGAAACCCAAAACA
TTAAATAACCCTGAAGACTCCACATACTATTATCTACTTCATAAGTCAATCCAAGAAGAA
AAACGAAGACCAAGGAAAGACAGTCAGGGAAAATTATTAGATTTGGAAGATTTCTATTAT
AAGGAATTTTTGCCCAGTCGTTCTGGACCAAAGGAACATAGCCCTAGTTTAAGAGAACGA
AGACCACAGCAAGAACTCCAGAATCAATGTATTAAGGCTAATGAAAGGTGCTGGGCGGCG
GAGAGCCCCGAGAAGGAGGAGGAGAGAGAGCCAGCAGCCAACCCCTACGACTTCAGGAGG
CTCCTGCGCAAAACCTCCCAGCGCCGGCGCCTCGTCCAGCAGTCCTAA
|
| Enzyme 114 GenBank Gene ID |
AF229172 |
| Enzyme 114 GeneCard ID |
MYO3A |
| Enzyme 114 GenAtlas ID |
MYO3A |
| Enzyme 114 HGNC ID |
HGNC:7601 |
| Enzyme 114 Chromosome Location |
1 |
| Enzyme 114 Locus |
10p11.1 |
| Enzyme 114 SNPs |
SNPJam Report |
| Enzyme 114 General References |
- Dose AC, Burnside B: Cloning and chromosomal localization of a human class III myosin. Genomics. 2000 Aug 1;67(3):333-42. [PubMed ]
- Walsh T, Walsh V, Vreugde S, Hertzano R, Shahin H, Haika S, Lee MK, Kanaan M, King MC, Avraham KB: From flies' eyes to our ears: mutations in a human class III myosin cause progressive nonsyndromic hearing loss DFNB30. Proc Natl Acad Sci U S A. 2002 May 28;99(11):7518-23. [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 ]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 114 Metabolite References |
Not Available |
|
Enzyme 115
[top]
|
| Enzyme 115 ID |
6453 |
| Enzyme 115 Name |
Macrophage-stimulating protein receptor |
| Enzyme 115 Synonyms |
- MSP receptor
- CDw136
- Protein-tyrosine kinase 8
- p185-Ron
- CD136 antigen
- Macrophage-stimulating protein receptor alpha chain
- Macrophage-stimulating protein receptor beta chain
|
| Enzyme 115 Gene Name |
MST1R |
| Enzyme 115 Protein Sequence |
>Macrophage-stimulating protein receptor
MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVT
YEGDRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPGCQTCAACGPGPHGPPGDTDT
KVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVAS
PLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPK
HLVSYSIEYVHSFHTGAFVYFLTVQPASVTDDPSALHTRLARLSATEPELGDYRELVLDC
RFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGV
GPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNT
SCRHFPLLVSSSFSRVDLFNGLLGPVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSL
NYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAW
HFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSG
LVPEGTHQVTVGQSPCRPLPKDSSKLRPVPRKDFVEEFECELEPLGTQAVGPTNVSLTVT
NMPPGKHFRVDGTSVLRGFSFMEPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVN
GTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWTFQYREDPVVLSISPNCG
YINSHITICGQHLTSAWHLVLSFHDGLRAVESRCERQLPEQQLCRLPEYVVRDPQGWVAG
NLSARGDGAAGFTLPGFRFLPPPHPPSANLVPLKPEEHAIKFEYIGLGAVADCVGINVTV
GGESCQHEFRGDMVVCPLPPSLQLGQDGAPLQVCVDGECHILGRVVRPGPDGVPQSTLLG
ILLPLLLLVAALATALVFSYWWRRKQLVLPPNLNDLASLDQTAGATPLPILYSGSDYRSG
LALPAIDGLDSTTCVHGASFSDSEDESCVPLLRKESIQLRDLDSALLAEVKDVLIPHERV
VTHSDRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNH
PNVLALIGIMLPPEGLPHVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARSMEYLA
EQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHRHARLPVKWMALESLQ
TYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVM
QQCWEADPAVRPTFRVLVGEVEQIVSALLGDHYVQLPATYMNLGPSTSHEMNVRPEQPQF
SPMPGNVRRPRPLSEPPRPT
|
| Enzyme 115 Number of Residues |
1400 |
| Enzyme 115 Molecular Weight |
152270.1 |
| Enzyme 115 Theoretical pI |
6.53 |
| Enzyme 115 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- molecular transducer activity
- nucleoside binding
- protein binding
- protein kinase activity
- protein tyrosine kinase activity
- purine nucleoside binding
- receptor activity
- signal transducer activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transmembrane receptor protein tyrosine kinase activity
|
| Process |
- cell surface receptor linked signaling pathway
- cellular metabolic process
- enzyme linked receptor protein signaling pathway
- metabolic process
- multicellular organismal development
- multicellular organismal process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- signaling
- signaling pathway
- transmembrane receptor protein tyrosine kinase signaling pathway
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 115 General Function |
Involved in receptor activity |
| Enzyme 115 Specific Function |
Receptor for macrophage stimulating protein (MSP). Has a tyrosine-protein kinase activity |
| Enzyme 115 Pathways |
Not Available |
| Enzyme 115 Reactions |
- ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate [RN:R02584]
|
| Enzyme 115 Pfam Domain Function |
|
| Enzyme 115 Signals |
|
| Enzyme 115 Transmembrane Regions |
|
| Enzyme 115 Essentiality |
Not Available |
| Enzyme 115 GenBank ID Protein |
153946393 |
| Enzyme 115 UniProtKB/Swiss-Prot ID |
Q04912 |
| Enzyme 115 UniProtKB/Swiss-Prot Entry Name |
RON_HUMAN |
| Enzyme 115 PDB ID |
Not Available |
| Enzyme 115 Cellular Location |
Not Available |
| Enzyme 115 Gene Sequence |
>4203 bp
ATGGAGCTCCTCCCGCCGCTGCCTCAGTCCTTCCTGTTGCTGCTGCTGTTGCCTGCCAAG
CCCGCGGCGGGCGAGGACTGGCAGTGCCCGCGCACCCCCTACGCGGCCTCTCGCGACTTT
GACGTGAAGTACGTGGTGCCCAGCTTCTCCGCCGGAGGCCTGGTACAGGCCATGGTGACC
TACGAGGGCGACAGAAATGAGAGTGCTGTGTTTGTAGCCATACGCAATCGCCTGCATGTG
CTTGGGCCTGACCTGAAGTCTGTCCAGAGCCTGGCCACGGGCCCTGCTGGAGACCCTGGC
TGCCAGACGTGTGCAGCCTGTGGCCCAGGACCCCACGGCCCTCCCGGTGACACAGACACA
AAGGTGCTGGTGCTGGATCCCGCGCTGCCTGCGCTGGTCAGTTGTGGCTCCAGCCTGCAG
GGCCGCTGCTTCCTGCATGACCTAGAGCCCCAAGGGACAGCCGTGCATCTGGCAGCGCCA
GCCTGCCTCTTCTCAGCCCACCATAACCGGCCCGATGACTGCCCCGACTGTGTGGCCAGC
CCATTGGGCACCCGTGTAACTGTGGTTGAGCAAGGCCAGGCCTCCTATTTCTACGTGGCA
TCCTCACTGGACGCAGCCGTGGCTGCCAGCTTCAGCCCACGCTCAGTGTCTATCAGGCGT
CTCAAGGCTGACGCCTCGGGATTCGCACCGGGCTTTGTGGCGTTGTCAGTGCTGCCCAAG
CATCTTGTCTCCTACAGTATTGAATACGTGCACAGCTTCCACACGGGAGCCTTCGTATAC
TTCCTGACTGTACAGCCGGCCAGCGTGACAGATGATCCTAGTGCCCTGCACACACGCCTG
GCACGGCTTAGCGCCACTGAGCCAGAGTTGGGTGACTATCGGGAGCTGGTCCTCGACTGC
AGATTTGCTCCAAAACGCAGGCGCCGGGGGGCCCCAGAAGGCGGACAGCCCTACCCTGTG
CTGCGGGTGGCCCACTCCGCTCCAGTGGGTGCCCAACTTGCCACTGAGCTGAGCATCGCC
GAGGGCCAGGAAGTACTATTTGGGGTCTTTGTGACTGGCAAGGATGGTGGTCCTGGCGTG
GGCCCCAACTCTGTCGTCTGTGCCTTCCCCATTGACCTGCTGGACACACTAATTGATGAG
GGTGTGGAGCGCTGTTGTGAATCCCCAGTCCATCCAGGCCTCCGGCGAGGCCTCGACTTC
TTCCAGTCGCCCAGTTTTTGCCCCAACCCGCCTGGCCTGGAAGCCCTCAGCCCCAACACC
AGCTGCCGCCACTTCCCTCTGCTGGTCAGTAGCAGCTTCTCACGTGTGGACCTATTCAAT
GGGCTGTTGGGACCAGTACAGGTCACTGCATTGTATGTGACACGCCTTGACAACGTCACA
GTGGCACACATGGGCACAATGGATGGGCGTATCCTGCAGGTGGAGCTGGTCAGGTCACTA
AACTACTTGCTGTATGTGTCCAACTTCTCACTGGGTGACAGTGGGCAGCCCGTGCAGCGG
GATGTCAGTCGTCTTGGGGACCACCTACTCTTTGCCTCTGGGGACCAGGTTTTCCAGGTA
CCTATCCAAGGCCCTGGCTGCCGCCACTTCCTGACCTGTGGGCGTTGCCTAAGGGCATGG
CATTTCATGGGCTGTGGCTGGTGTGGGAACATGTGCGGCCAGCAGAAGGAGTGTCCTGGC
TCCTGGCAACAGGACCACTGCCCACCTAAGCTTACTGAGTTCCACCCCCACAGTGGACCT
CTAAGGGGCAGTACAAGGCTGACCCTGTGTGGCTCCAACTTCTACCTTCACCCTTCTGGT
CTGGTGCCTGAGGGAACCCATCAGGTCACTGTGGGCCAAAGTCCCTGCCGGCCACTGCCC
AAGGACAGCTCAAAACTCAGACCAGTGCCCCGGAAAGACTTTGTAGAGGAGTTTGAGTGT
GAACTGGAGCCCTTGGGCACCCAGGCAGTGGGGCCTACCAACGTCAGCCTCACCGTGACT
AACATGCCACCGGGCAAGCACTTCCGGGTAGACGGCACCTCCGTGCTGAGAGGCTTCTCT
TTCATGGAGCCAGTGCTGATAGCAGTGCAACCCCTCTTTGGCCCACGGGCAGGAGGCACC
TGTCTCACTCTTGAAGGCCAGAGTCTGTCTGTAGGCACCAGCCGGGCTGTGCTGGTCAAT
GGGACTGAGTGTCTGCTAGCACGGGTCAGTGAGGGGCAGCTTTTATGTGCCACACCCCCT
GGGGCCACGGTGGCCAGTGTCCCCCTTAGCCTGCAGGTGGGGGGTGCCCAGGTACCTGGT
TCCTGGACCTTCCAGTACAGAGAAGACCCTGTCGTGCTAAGCATCAGCCCCAACTGTGGC
TACATCAACTCCCACATCACCATCTGTGGCCAGCATCTAACTTCAGCATGGCACTTAGTG
CTGTCATTCCATGACGGGCTTAGGGCAGTGGAAAGCAGGTGTGAGAGGCAGCTTCCAGAG
CAGCAGCTGTGCCGCCTTCCTGAATATGTGGTCCGAGACCCCCAGGGATGGGTGGCAGGG
AATCTGAGTGCCCGAGGGGATGGAGCTGCTGGCTTTACACTGCCTGGCTTTCGCTTCCTA
CCCCCACCCCATCCACCCAGTGCCAACCTAGTTCCACTGAAGCCTGAGGAGCATGCCATT
AAGTTTGAGTATATTGGGCTGGGCGCTGTGGCTGACTGTGTGGGTATCAACGTGACCGTG
GGTGGTGAGAGCTGCCAGCACGAGTTCCGGGGGGACATGGTTGTCTGCCCCCTGCCCCCA
TCCCTGCAGCTTGGCCAGGATGGTGCCCCATTGCAGGTCTGCGTAGATGGTGAATGTCAT
ATCCTGGGTAGAGTGGTGCGGCCAGGGCCAGATGGGGTCCCACAGAGCACGCTCCTTGGT
ATCCTGCTGCCTTTGCTGCTGCTTGTGGCTGCACTGGCGACTGCACTGGTCTTCAGCTAC
TGGTGGCGGAGGAAGCAGCTAGTTCTTCCTCCCAACCTGAATGACCTGGCATCCCTGGAC
CAGACTGCTGGAGCCACACCCCTGCCTATTCTGTACTCGGGCTCTGACTACAGAAGTGGC
CTTGCACTCCCTGCCATTGATGGTCTGGATTCCACCACTTGTGTCCATGGAGCATCCTTC
TCCGATAGTGAAGATGAATCCTGTGTGCCACTGCTGCGGAAAGAGTCCATCCAGCTAAGG
GACCTGGACTCTGCGCTCTTGGCTGAGGTCAAGGATGTGCTGATTCCCCATGAGCGGGTG
GTCACCCACAGTGACCGAGTCATTGGCAAAGGCCACTTTGGAGTTGTCTACCACGGAGAA
TACATAGACCAGGCCCAGAATCGAATCCAATGTGCCATCAAGTCACTAAGTCGCATCACA
GAGATGCAGCAGGTGGAGGCCTTCCTGCGAGAGGGGCTGCTCATGCGTGGCCTGAACCAC
CCGAATGTGCTGGCTCTCATTGGTATCATGTTGCCACCTGAGGGCCTGCCCCATGTGCTG
CTGCCCTATATGTGCCACGGTGACCTGCTCCAGTTCATCCGCTCACCTCAGCGGAACCCC
ACCGTGAAGGACCTCATCAGCTTTGGCCTGCAGGTAGCCCGCGGCATGGAGTACCTGGCA
GAGCAGAAGTTTGTGCACAGGGACCTGGCTGCGCGGAACTGCATGCTGGACGAGTCATTC
ACAGTCAAGGTGGCTGACTTTGGTTTGGCCCGCGACATCCTGGACAGGGAGTACTATAGT
GTTCAACAGCATCGCCACGCTCGCCTACCTGTGAAGTGGATGGCGCTGGAGAGCCTGCAG
ACCTATAGATTTACCACCAAGTCTGATGTGTGGTCATTTGGTGTGCTGCTGTGGGAACTG
CTGACACGGGGTGCCCCACCATACCGCCACATTGACCCTTTTGACCTTACCCACTTCCTG
GCCCAGGGTCGGCGCCTGCCCCAGCCTGAGTATTGCCCTGATTCTCTGTACCAAGTGATG
CAGCAATGCTGGGAGGCAGACCCAGCAGTGCGACCCACCTTCAGAGTACTAGTGGGGGAG
GTGGAGCAGATAGTGTCTGCACTGCTTGGGGACCATTATGTGCAGCTGCCAGCAACCTAC
ATGAACTTGGGCCCCAGCACCTCGCATGAGATGAATGTGCGTCCAGAACAGCCGCAGTTC
TCACCCATGCCAGGGAATGTACGCCGGCCCCGGCCACTCTCAGAGCCTCCTCGGCCCACT
TGA
|
| Enzyme 115 GenBank Gene ID |
NM_002447.2 |
| Enzyme 115 GeneCard ID |
MST1R |
| Enzyme 115 GenAtlas ID |
MST1R |
| Enzyme 115 HGNC ID |
HGNC:7381 |
| Enzyme 115 Chromosome Location |
3 |
| Enzyme 115 Locus |
3p21.3 |
| Enzyme 115 SNPs |
SNPJam Report |
| Enzyme 115 General References |
- Ronsin C, Muscatelli F, Mattei MG, Breathnach R: A novel putative receptor protein tyrosine kinase of the met family. Oncogene. 1993 May;8(5):1195-202. [PubMed ]
- Collesi C, Santoro MM, Gaudino G, Comoglio PM: A splicing variant of the RON transcript induces constitutive tyrosine kinase activity and an invasive phenotype. Mol Cell Biol. 1996 Oct;16(10):5518-26. [PubMed ]
- Jin P, Zhang J, Sumariwalla PF, Ni I, Jorgensen B, Crawford D, Phillips S, Feldmann M, Shepard HM, Paleolog EM: Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis. Arthritis Res Ther. 2008;10(4):R73. Epub 2008 Jul 1. [PubMed ]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed ]
- Wang MH, Ronsin C, Gesnel MC, Coupey L, Skeel A, Leonard EJ, Breathnach R: Identification of the ron gene product as the receptor for the human macrophage stimulating protein. Science. 1994 Oct 7;266(5182):117-9. [PubMed ]
- Danilkovitch-Miagkova A, Duh FM, Kuzmin I, Angeloni D, Liu SL, Miller AD, Lerman MI: Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and mediates transformation of epithelial cells by jaagsiekte sheep retrovirus. Proc Natl Acad Sci U S A. 2003 Apr 15;100(8):4580-5. Epub 2003 Apr 3. [PubMed ]
- Conrotto P, Corso S, Gamberini S, Comoglio PM, Giordano S: Interplay between scatter factor receptors and B plexins controls invasive growth. Oncogene. 2004 Jul 1;23(30):5131-7. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 115 Metabolite References |
Not Available |
|
Enzyme 116
[top]
|
| Enzyme 116 ID |
6456 |
| Enzyme 116 Name |
Vascular endothelial growth factor receptor 3 |
| Enzyme 116 Synonyms |
- VEGFR-3
- Fms-like tyrosine kinase 4
- FLT-4
- Tyrosine-protein kinase receptor FLT4
|
| Enzyme 116 Gene Name |
FLT4 |
| Enzyme 116 Protein Sequence |
>Vascular endothelial growth factor receptor 3
MQRGAALCLRLWLCLGLLDGLVSGYSMTPPTLNITEESHVIDTGDSLSISCRGQHPLEWA
WPGAQEAPATGDKDSEDTGVVRDCEGTDARPYCKVLLLHEVHANDTGSYVCYYKYIKARI
EGTTAASSYVFVRDFEQPFINKPDTLLVNRKDAMWVPCLVSIPGLNVTLRSQSSVLWPDG
QEVVWDDRRGMLVSTPLLHDALYLQCETTWGDQDFLSNPFLVHITGNELYDIQLLPRKSL
ELLVGEKLVLNCTVWAEFNSGVTFDWDYPGKQAERGKWVPERRSQQTHTELSSILTIHNV
SQHDLGSYVCKANNGIQRFRESTEVIVHENPFISVEWLKGPILEATAGDELVKLPVKLAA
YPPPEFQWYKDGKALSGRHSPHALVLKEVTEASTGTYTLALWNSAAGLRRNISLELVVNV
PPQIHEKEASSPSIYSRHSRQALTCTAYGVPLPLSIQWHWRPWTPCKMFAQRSLRRRQQQ
DLMPQCRDWRAVTTQDAVNPIESLDTWTEFVEGKNKTVSKLVIQNANVSAMYKCVVSNKV
GQDERLIYFYVTTIPDGFTIESKPSEELLEGQPVLLSCQADSYKYEHLRWYRLNLSTLHD
AHGNPLLLDCKNVHLFATPLAASLEEVAPGARHATLSLSIPRVAPEHEGHYVCEVQDRRS
HDKHCHKKYLSVQALEAPRLTQNLTDLLVNVSDSLEMQCLVAGAHAPSIVWYKDERLLEE
KSGVDLADSNQKLSIQRVREEDAGRYLCSVCNAKGCVNSSASVAVEGSEDKGSMEIVILV
GTGVIAVFFWVLLLLIFCNMRRPAHADIKTGYLSIIMDPGEVPLEEQCEYLSYDASQWEF
PRERLHLGRVLGYGAFGKVVEASAFGIHKGSSCDTVAVKMLKEGATASEHRALMSELKIL
IHIGNHLNVVNLLGACTKPQGPLMVIVEFCKYGNLSNFLRAKRDAFSPCAEKSPEQRGRF
RAMVELARLDRRRPGSSDRVLFARFSKTEGGARRASPDQEAEDLWLSPLTMEDLVCYSFQ
VARGMEFLASRKCIHRDLAARNILLSESDVVKICDFGLARDIYKDPDYVRKGSARLPLKW
MAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCQRLRDGTRMRAPELA
TPAIRRIMLNCWSGDPKARPAFSELVEILGDLLQGRGLQEEEEVCMAPRSSQSSEEGSFS
QVSTMALHIAQADAEDSPPSLQRHSLAARYYNWVSFPGCLARGAETRGSSRMKTFEEFPM
TPTTYKGSVDNQTDSGMVLASEEFEQIESRHRQESGFR
|
| Enzyme 116 Number of Residues |
1298 |
| Enzyme 116 Molecular Weight |
145597.3 |
| Enzyme 116 Theoretical pI |
6.24 |
| Enzyme 116 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- growth factor binding
- kinase activity
- nucleoside binding
- protein binding
- protein kinase activity
- protein tyrosine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transmembrane receptor protein tyrosine kinase activity
- vascular endothelial growth factor receptor activity
|
| Process |
- biological regulation
- cell surface receptor linked signaling pathway
- cellular metabolic process
- enzyme linked receptor protein signaling pathway
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- positive regulation of cell proliferation
- protein amino acid phosphorylation
- regulation of biological process
- regulation of cell proliferation
- regulation of cellular process
- signaling
- signaling pathway
- transmembrane receptor protein tyrosine kinase signaling pathway
- vascular endothelial growth factor receptor signaling pathway
|
| Component |
- cell part
- integral to membrane
- integral to plasma membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 116 General Function |
Involved in protein kinase activity |
| Enzyme 116 Specific Function |
Receptor for VEGFC. Has a tyrosine-protein kinase activity |
| Enzyme 116 Pathways |
Not Available |
| Enzyme 116 Reactions |
- ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate [RN:R02584]
|
| Enzyme 116 Pfam Domain Function |
|
| Enzyme 116 Signals |
|
| Enzyme 116 Transmembrane Regions |
|
| Enzyme 116 Essentiality |
Not Available |
| Enzyme 116 GenBank ID Protein |
297050 |
| Enzyme 116 UniProtKB/Swiss-Prot ID |
P35916 |
| Enzyme 116 UniProtKB/Swiss-Prot Entry Name |
VGFR3_HUMAN |
| Enzyme 116 PDB ID |
Not Available |
| Enzyme 116 Cellular Location |
Not Available |
| Enzyme 116 Gene Sequence |
>3897 bp
ATGCAGCGGGGCGCCGCGCTGTGCCTGCGACTGTGGCTCTGCCTGGGACTCCTGGACGGC
CTGGTGAGTGACTACTCCATGACCCCCCCGACCTTGAACATCACGGAGGAGTCACACGTC
ATCGACACCGGTGACAGCCTGTCCATCTCCTGCAGGGGACAGCACCCCCTCGAGTGGGCT
TGGCCAGGAGCTCAGGAGGCGCCAGCCACCGGAGACAAGGACAGCGAGGACACGGGGGTG
GTGCGAGACTGCGAGGGCACAGACGCCAGGCCCTACTGCAAGGTGTTGCTGCTGCACGAG
GTACATGCCAACGACACAGGCAGCTACGTCTGCTACTACAAGTACATCAAGGCACGCATC
GAGGGCACCACGGCCGCCAGCTCCTACGTGTTCGTGAGAGACTTTGAGCAGCCATTCATC
AACAAGCCTGACACGCTCTTGGTCAACAGGAAGGACGCCATGTGGGTGCCCTGTCTGGTG
TCCATCCCCGGCCTCAATGTCACGCTGCGCTCGCAAAGCTCGGTGCTGTGGCCAGACGGG
CAGGAGGTGGTGTGGGATGACCGGCGGGGCATGCTCGTGTCCACGCCACTGCTGCACGAT
GCCCTGTACCTGCAGTGCGAGACCACCTGGGGAGACCAGGACTTCCTTTCCAACCCCTTC
CTGGTGCACATCACAGGCAACGAGCTCTATGACATCCAGCTGTTGCCCAGGAAGTCGCTG
GAGCTGCTGGTAGGGGAGAAGCTGGTCCTCAACTGCACCGTGTGGGCTGAGTTTAACTCA
GGTGTCACCTTTGACTGGGACTACCCAGGGAAGCAGGCAGAGCGGGGTAAGTGGGTGCCC
GAGCGACGCTCCCAACAGACCCACACAGAACTCTCCAGCATCCTGACCATCCACAACGTC
AGCCAGCACGACCTGGGCTCGTATGTGTGCAAGGCCAACAACGGCATCCAGCGATTTCGG
GAGAGCACCGAGGTCATTGTGCATGAAAATCCCTTCATCAGCGTCGAGTGGCTCAAAGGA
CCCATCCTGGAGGCCACGGCAGGAGACGAGCTGGTGAAGCTGCCCGTGAAGCTGGCAGCG
TACCCCCCGCCCGAGTTCCAGTGGTACAAGGATGGAAAGGCACTGTCCGGGCGCCACAGT
CCACATGCCCTGGTGCTCAAGGAGGTGACAGAGGCCAGCACAGGCACCTACACCCTCGCC
CTGTGGAACTCCGCTGCTGGCCTGAGGCGCAACATCAGCCTGGAGCTGGTGGTGAATGTG
CCCCCCCAGATACATGAGAAGGAGGCCTCCTCCCCCAGCATCTACTCGCGTCACAGCCGC
CAGGCCCTCACCTGCACGGCCTACGGGGTGCCCCTGCCTCTCAGCATCCAGTGGCACTGG
CGGCCCTGGACACCCTGCAAGATGTTTGCCCAGCGTAGTCTCCGGCGGCGGCAGCAGCAA
GACCTCATGCCACAGTGCCGTGACTGGAGGGCGGTGACCACGCAGGATGCCGTGAACCCC
ATCGAGAGCCTGGACACCTGGACCGAGTTTGTGGAGGGAAAGAATAAGACTGTGAGCAAG
CTGGTGATCCAGAATGCCAACGTGTCTGCCATGTACAAGTGTGTGGTCTCCAACAAGGTG
GGCCAGGATGAGCGGCTCATCTACTTCTATGTGACCACCATCCCCGACGGCTTCACCATC
GAATCCAAGCCATCCGAGGAGCTACTAGAGGGCCAGCCGGTGCTCCTGAGCTGCCAAGCC
GACAGCTACAAGTACGAGCATCTGCGCTGGTACCGCCTCAACCTGTCCACGCTGCACGAT
GCGCACGGGAACCCGCTTCTGCTCGACTGCAAGAACGTGCATCTGTTCGCCACCCCTCTG
GCCGCCAGCCTGGAGGAGGTGGCACCTGGGGCGCGCCACGCCACGCTCAGCCTGAGTATC
CCCCGCGTCGCGCCCGAGCACGAGGGCCACTATGTGTGCGAAGTGCAAGACCGGCGCAGC
CATGACAAGCACTGCCACAAGAAGTACCTGTCGGTGCAGGCCCTGGAAGCCCCTCGGCTC
ACGCAGAACTTGACCGACCTCCTGGTGAACGTGAGCGACTCGCTGGAGATGCAGTGCTTG
GTGGCCGGAGCGCACGCGCCCAGCATCGTGTGGTACAAAGACGAGAGGCTGCTGGAGGAA
AAGTCTGGAGTCGACTTGGCGGACTCCAACCAGAAGCTGAGCATCCAGCGCGTGCGCGAG
GAGGATGCGGGACCGTATCTGTGCAGCGTGTGCAGACCCAAGGGCTGCGTCAACTCCTCC
GCCAGCGTGGCCGTGGAAGGCTCCGAGGATAAGGGCAGCATGGAGATCGTGATCCTTGTC
GGTACCGGCGTCATCGCTGTCTTCTTCTGGGTCCTCCTCCTCCTCATCTTCTGTAACATG
AGGAGGCCGGCCCACGCAGACATCAAGACGGGCTACCTGTCCATCATCATGGACCCCGGG
GAGGTGCCTCTGGAGGAGCAATGCGAATACCTGTCCTACGATGCCAGCCAGTGGGAATTC
CCCCGAGAGCGGCTGCACCTGGGGAGAGTGCTCGGCTACGGCGCCTTCGGGAAGGTGGTG
GAAGCCTCCGCTTTCGGCATCCACAAGGGCAGCAGCTGTGACACCGTGGCCGTGAAAATG
CTGAAAGAGGGCGCCACGGCCAGCGAGCAGCGCGCGCTGATGTCGGAGCTCAAGATCCTC
ATTCACATCGGCAACCACCTCAACGTGGTCAACCTCCTCGGGGCGTGCACCAAGCCGCAG
GGCCCCCTCATGGTGATCGTGGAGTTCTGCAAGTACGGCAACCTCTCCAACTTCCTGCGC
GCCAAGCGGGACGCCTTCAGCCCCTGCGCGGAGAAGTCTCCCGAGCAGCGCGGACGCTTC
CGCGCCATGGTGGAGCTCGCCAGGCTGGATCGGAGGCGGCCGGGGAGCAGCGACAGGGTC
CTCTTCGCGCGGTTCTCGAAGACCGAGGGCGGAGCGAGGCGGGCTTCTCCAGACCAAGAA
GCTGAGGACCTGTGGCTGAGCCCGCTGACCATGGAAGATCTTGTCTGCTACAGCTTCCAG
GTGGCCAGAGGGATGGAGTTCCTGGCTTCCCGAAAGTGCATCCACAGAGACCTGGCTGCT
CGGAACATTCTGCTGTCGGAAAGCGACGTGGTGAAGATCTGTGACTTTGGCCTTGCCCGG
GACATCTACAAAGACCCCGACTACGTCCGCAAGGGCAGTGCCCGGCTGCCCCTGAAGTGG
ATGGCCCCTGAAAGCATCTTCGACAAGGTGTACACCACGCAGAGTGACGTGTGGTCCTTT
GGGGTGCTTCTCTGGGAGATCTTCTCTCTGGGGGCCTCCCCGTACCCTGGGGTGCAGATC
AATGAGGAGTTCTGCCAGCGCGTGAGAGACGGCACAAGGATGAGGGCCCCGGAGCTGGCC
ACTCCCGCCATACGCCACATCATGCTGAACTGCTGGTCCGGAGACCCCAAGGCGAGACCT
GCATTCTCGGACCTGGTGGAGATCCTGGGGGACCTGCTCCAGGGCAGGGGCCTGCAAGAG
GAAGAGGAGGTCTGCATGGCCCCGCGCAGCTCTCAGAGCTCAGAAGAGGGCAGCTTCTCG
CAGGTGTCCACCATGGCCCTACACATCGCCCAGGCTGACGCTGAGGACAGCCCGCCAAGC
CTGCAGCGCCACAGCCTGGCCGCCAGGTATTACAACTGGGTGTCCTTTCCCGGGTGCCTG
GCCAGAGGGGCTGAGACCCGTGGTTCCTCCAGGATGAAGACATTTGAGGAATTCCCCATG
ACCCCAACGACCTACAAAGGCTCTGTGGACAACCAGACAGACAGTGGGATGGTGCTGGCC
TCGGAGGAGTTTGAGCAGATAGAGAGCAGGCATAGACAAGAAAGCGGCTTCAGGTAG
|
| Enzyme 116 GenBank Gene ID |
X69878 |
| Enzyme 116 GeneCard ID |
FLT4 |
| Enzyme 116 GenAtlas ID |
FLT4 |
| Enzyme 116 HGNC ID |
HGNC:3767 |
| Enzyme 116 Chromosome Location |
5 |
| Enzyme 116 Locus |
5q35.3 |
| Enzyme 116 SNPs |
SNPJam Report |
| Enzyme 116 General References |
- Pajusola K, Aprelikova O, Korhonen J, Kaipainen A, Pertovaara L, Alitalo R, Alitalo K: FLT4 receptor tyrosine kinase contains seven immunoglobulin-like loops and is expressed in multiple human tissues and cell lines. Cancer Res. 1992 Oct 15;52(20):5738-43. [PubMed ]
- Galland F, Karamysheva A, Mattei MG, Rosnet O, Marchetto S, Birnbaum D: Chromosomal localization of FLT4, a novel receptor-type tyrosine kinase gene. Genomics. 1992 Jun;13(2):475-8. [PubMed ]
- Galland F, Karamysheva A, Pebusque MJ, Borg JP, Rottapel R, Dubreuil P, Rosnet O, Birnbaum D: The FLT4 gene encodes a transmembrane tyrosine kinase related to the vascular endothelial growth factor receptor. Oncogene. 1993 May;8(5):1233-40. [PubMed ]
- Lee J, Gray A, Yuan J, Luoh SM, Avraham H, Wood WI: Vascular endothelial growth factor-related protein: a ligand and specific activator of the tyrosine kinase receptor Flt4. Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):1988-92. [PubMed ]
- Aprelikova O, Pajusola K, Partanen J, Armstrong E, Alitalo R, Bailey SK, McMahon J, Wasmuth J, Huebner K, Alitalo K: FLT4, a novel class III receptor tyrosine kinase in chromosome 5q33-qter. Cancer Res. 1992 Feb 1;52(3):746-8. [PubMed ]
- Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed ]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Ferrell RE, Levinson KL, Esman JH, Kimak MA, Lawrence EC, Barmada MM, Finegold DN: Hereditary lymphedema: evidence for linkage and genetic heterogeneity. Hum Mol Genet. 1998 Dec;7(13):2073-8. [PubMed ]
- Irrthum A, Karkkainen MJ, Devriendt K, Alitalo K, Vikkula M: Congenital hereditary lymphedema caused by a mutation that inactivates VEGFR3 tyrosine kinase. Am J Hum Genet. 2000 Aug;67(2):295-301. Epub 2000 Jun 9. [PubMed ]
- Karkkainen MJ, Ferrell RE, Lawrence EC, Kimak MA, Levinson KL, McTigue MA, Alitalo K, Finegold DN: Missense mutations interfere with VEGFR-3 signalling in primary lymphoedema. Nat Genet. 2000 Jun;25(2):153-9. [PubMed ]
- Walter JW, North PE, Waner M, Mizeracki A, Blei F, Walker JW, Reinisch JF, Marchuk DA: Somatic mutation of vascular endothelial growth factor receptors in juvenile hemangioma. Genes Chromosomes Cancer. 2002 Mar;33(3):295-303. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 116 Metabolite References |
Not Available |
|
Enzyme 117
[top]
|
| Enzyme 117 ID |
6458 |
| Enzyme 117 Name |
Glycogen synthase kinase-3 beta |
| Enzyme 117 Synonyms |
- GSK-3 beta
|
| Enzyme 117 Gene Name |
GSK3B |
| Enzyme 117 Protein Sequence |
>Glycogen synthase kinase-3 beta
MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTK
VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSG
EKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR
DIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDV
WSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHP
WTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALF
NFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST
|
| Enzyme 117 Number of Residues |
420 |
| Enzyme 117 Molecular Weight |
46743.9 |
| Enzyme 117 Theoretical pI |
8.97 |
| Enzyme 117 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 117 General Function |
Involved in protein kinase activity |
| Enzyme 117 Specific Function |
Participates in the Wnt signaling pathway. Implicated in the hormonal control of several regulatory proteins including glycogen synthase, MYB and the transcription factor JUN. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates MUC1 in breast cancer cells, and decreases the interaction of MUC1 with CTNNB1/beta-catenin. Phosphorylates CTNNB1/beta-catenin. Phosphorylates SNAI1 |
| Enzyme 117 Pathways |
Not Available |
| Enzyme 117 Reactions |
- ATP + [tau-protein] = ADP + O-phospho-[tau-protein]
|
| Enzyme 117 Pfam Domain Function |
|
| Enzyme 117 Signals |
|
| Enzyme 117 Transmembrane Regions |
|
| Enzyme 117 Essentiality |
Not Available |
| Enzyme 117 GenBank ID Protein |
225903437 |
| Enzyme 117 UniProtKB/Swiss-Prot ID |
P49841 |
| Enzyme 117 UniProtKB/Swiss-Prot Entry Name |
GSK3B_HUMAN |
| Enzyme 117 PDB ID |
1J1C |
| Enzyme 117 PDB File |
Show |
| Enzyme 117 3D Structure |
|
| Enzyme 117 Cellular Location |
Not Available |
| Enzyme 117 Gene Sequence |
>1263 bp
ATGTCAGGGCGGCCCAGAACCACCTCCTTTGCGGAGAGCTGCAAGCCGGTGCAGCAGCCT
TCAGCTTTTGGCAGCATGAAAGTTAGCAGAGACAAGGACGGCAGCAAGGTGACAACAGTG
GTGGCAACTCCTGGGCAGGGTCCAGACAGGCCACAAGAAGTCAGCTATACAGACACTAAA
GTGATTGGAAATGGATCATTTGGTGTGGTATATCAAGCCAAACTTTGTGATTCAGGAGAA
CTGGTCGCCATCAAGAAAGTATTGCAGGACAAGAGATTTAAGAATCGAGAGCTCCAGATC
ATGAGAAAGCTAGATCACTGTAACATAGTCCGATTGCGTTATTTCTTCTACTCCAGTGGT
GAGAAGAAAGATGAGGTCTATCTTAATCTGGTGCTGGACTATGTTCCGGAAACAGTATAC
AGAGTTGCCAGACACTATAGTCGAGCCAAACAGACGCTCCCTGTGATTTATGTCAAGTTG
TATATGTATCAGCTGTTCCGAAGTTTAGCCTATATCCATTCCTTTGGAATCTGCCATCGG
GATATTAAACCGCAGAACCTCTTGTTGGATCCTGATACTGCTGTATTAAAACTCTGTGAC
TTTGGAAGTGCAAAGCAGCTGGTCCGAGGAGAACCCAATGTTTCGTATATCTGTTCTCGG
TACTATAGGGCACCAGAGTTGATCTTTGGAGCCACTGATTATACCTCTAGTATAGATGTA
TGGTCTGCTGGCTGTGTGTTGGCTGAGCTGTTACTAGGACAACCAATATTTCCAGGGGAT
AGTGGTGTGGATCAGTTGGTAGAAATAATCAAGGTCCTGGGAACTCCAACAAGGGAGCAA
ATCAGAGAAATGAACCCAAACTACACAGAATTTAAATTCCCTCAAATTAAGGCACATCCT
TGGACTAAGGTCTTCCGACCCCGAACTCCACCGGAGGCAATTGCACTGTGTAGCCGTCTG
CTGGAGTATACACCAACTGCCCGACTAACACCACTGGAAGCTTGTGCACATTCATTTTTT
GATGAATTACGGGACCCAAATGTCAAACTACCAAATGGGCGAGACACACCTGCACTCTTC
AACTTCACCACTCAAGAACTGTCAAGTAATCCACCTCTGGCTACCATCCTTATTCCTCCT
CATGCTCGGATTCAAGCAGCTGCTTCAACCCCCACAAATGCCACAGCAGCGTCAGATGCT
AATACTGGAGACCGTGGACAGACCAATAATGCTGCTTCTGCATCAGCTTCCAACTCCACC
TGA
|
| Enzyme 117 GenBank Gene ID |
NM_001146156.1 |
| Enzyme 117 GeneCard ID |
GSK3B |
| Enzyme 117 GenAtlas ID |
GSK3B |
| Enzyme 117 HGNC ID |
HGNC:4617 |
| Enzyme 117 Chromosome Location |
3 |
| Enzyme 117 Locus |
3q13.3 |
| Enzyme 117 SNPs |
SNPJam Report |
| Enzyme 117 General References |
- Stambolic V, Woodgett JR: Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation. Biochem J. 1994 Nov 1;303 ( Pt 3):701-4. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Rhoads AR, Karkera JD, Detera-Wadleigh SD: Radiation hybrid mapping of genes in the lithium-sensitive wnt signaling pathway. Mol Psychiatry. 1999 Sep;4(5):437-42. [PubMed ]
- Lau KF, Miller CC, Anderton BH, Shaw PC: Molecular cloning and characterization of the human glycogen synthase kinase-3beta promoter. Genomics. 1999 Sep 1;60(2):121-8. [PubMed ]
- Hong YR, Chen CH, Cheng DS, Howng SL, Chow CC: Human dynamin-like protein interacts with the glycogen synthase kinase 3beta. Biochem Biophys Res Commun. 1998 Aug 28;249(3):697-703. [PubMed ]
- Li Y, Bharti A, Chen D, Gong J, Kufe D: Interaction of glycogen synthase kinase 3beta with the DF3/MUC1 carcinoma-associated antigen and beta-catenin. Mol Cell Biol. 1998 Dec;18(12):7216-24. [PubMed ]
- Delcommenne M, Tan C, Gray V, Rue L, Woodgett J, Dedhar S: Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11211-6. [PubMed ]
- Hsu W, Zeng L, Costantini F: Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain. J Biol Chem. 1999 Feb 5;274(6):3439-45. [PubMed ]
- Hong YR, Chen CH, Chang JH, Wang S, Sy WD, Chou CK, Howng SL: Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta. Biochim Biophys Acta. 2000 Jul 24;1492(2-3):513-6. [PubMed ]
- Zhou BP, Deng J, Xia W, Xu J, Li YM, Gunduz M, Hung MC: Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition. Nat Cell Biol. 2004 Oct;6(10):931-40. Epub 2004 Sep 26. [PubMed ]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
- Hsu HC, Lee YL, Cheng TS, Howng SL, Chang LK, Lu PJ, Hong YR: Characterization of two non-testis-specific CABYR variants that bind to GSK3beta with a proline-rich extensin-like domain. Biochem Biophys Res Commun. 2005 Apr 15;329(3):1108-17. [PubMed ]
- Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed ]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
- Kobayashi T, Hino S, Oue N, Asahara T, Zollo M, Yasui W, Kikuchi A: Glycogen synthase kinase 3 and h-prune regulate cell migration by modulating focal adhesions. Mol Cell Biol. 2006 Feb;26(3):898-911. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Luo W, Peterson A, Garcia BA, Coombs G, Kofahl B, Heinrich R, Shabanowitz J, Hunt DF, Yost HJ, Virshup DM: Protein phosphatase 1 regulates assembly and function of the beta-catenin degradation complex. EMBO J. 2007 Mar 21;26(6):1511-21. Epub 2007 Feb 22. [PubMed ]
- Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed ]
- Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed ]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- 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 ]
- Kandasamy AD, Schulz R: Glycogen synthase kinase-3beta is activated by matrix metalloproteinase-2 mediated proteolysis in cardiomyoblasts. Cardiovasc Res. 2009 Sep 1;83(4):698-706. Epub 2009 Jun 3. [PubMed ]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Dajani R, Fraser E, Roe SM, Young N, Good V, Dale TC, Pearl LH: Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell. 2001 Jun 15;105(6):721-32. [PubMed ]
- Bax B, Carter PS, Lewis C, Guy AR, Bridges A, Tanner R, Pettman G, Mannix C, Culbert AA, Brown MJ, Smith DG, Reith AD: The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation. Structure. 2001 Dec;9(12):1143-52. [PubMed ]
- Dajani R, Fraser E, Roe SM, Yeo M, Good VM, Thompson V, Dale TC, Pearl LH: Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex. EMBO J. 2003 Feb 3;22(3):494-501. [PubMed ]
|
| Enzyme 117 Metabolite References |
Not Available |
|
Enzyme 118
[top]
|
| Enzyme 118 ID |
6460 |
| Enzyme 118 Name |
Katanin p60 ATPase-containing subunit A1 |
| Enzyme 118 Synonyms |
- Katanin p60 subunit A1
- p60 katanin
|
| Enzyme 118 Gene Name |
KATNA1 |
| Enzyme 118 Protein Sequence |
>Katanin p60 ATPase-containing subunit A1
MSLLMISENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTYLQQKWQQVWQEIN
VEAKHVKDIMKTLESFKLDSTPLKAAQHDLPASEGEVWSMPVPVERRPSPGPRKRQSSQY
SDPKSHGNRPSTTVRVHRSSAQNVHNDRGKAVRCREKKEQNKGREEKNKSPAAVTEPETN
KFDSTGYDKDLVEALERDIISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFKGIRR
PWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFY
SPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGTSENDDPSKMVMVLAATN
FPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGAD
ITNVCRDASLMAMRRRIEGLTPEEIRNLSKEEMHMPTTMEDFEMALKKVSKSVSAADIER
YEKWIFEFGSC
|
| Enzyme 118 Number of Residues |
491 |
| Enzyme 118 Molecular Weight |
55964.3 |
| Enzyme 118 Theoretical pI |
6.88 |
| Enzyme 118 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
- nucleoside binding
- nucleoside-triphosphatase activity
- nucleotide binding
- purine nucleoside binding
- pyrophosphatase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 118 General Function |
Involved in nucleotide binding |
| Enzyme 118 Specific Function |
Severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays, such as during disassembly of interphase microtubules at the G2-M transition. May also be required for microtubule release from the centrosome after nucleation. In mitotic spindles this could allow depolymerization of the microtubule end proximal to the centrosome, and subsequent poleward microtubule flux. In neurons, microtubule release within the cell body may allow their subsequent transport into neuronal processes by microtubule dependent motor proteins. This transport is required for axonal growth |
| Enzyme 118 Pathways |
Not Available |
| Enzyme 118 Reactions |
- ATP + H2O = ADP + phosphate [RN:R00086]
|
| Enzyme 118 Pfam Domain Function |
|
| Enzyme 118 Signals |
|
| Enzyme 118 Transmembrane Regions |
|
| Enzyme 118 Essentiality |
Not Available |
| Enzyme 118 GenBank ID Protein |
3283072 |
| Enzyme 118 UniProtKB/Swiss-Prot ID |
O75449 |
| Enzyme 118 UniProtKB/Swiss-Prot Entry Name |
KTNA1_HUMAN |
| Enzyme 118 PDB ID |
Not Available |
| Enzyme 118 Cellular Location |
Not Available |
| Enzyme 118 Gene Sequence |
>1476 bp
ATGAGTCTTCTTATGATTAGTGAGAATGTAAAATTGGCTCGTGAATATGCATTGCTGGGA
AACTATGACTCTGCGATGGTCTATTATCAGGGAGTTCTTGACCAAATGAACAAGTATCTG
TACTCAGTCAAAGATACATACCTCCAGCAGAAATGGCAACAGGTTTGGCAGGAAATAAAT
GTGGAAGCTAAACATGTTAAAGATATCATGAAAACACTAGAGAGCTTTAAACTGGACAGC
ACTCCCTTGAAAGCGGCACAGCATGACCTTCCAGCTTCTGAGGGAGAAGTCTGGTCCATG
CCTGTACCTGTTGAACGAAGACCCTCACCAGGACCTAGAAAACGCCAATCTTCTCAGTAC
AGTGACCCTAAATCACATGGTAATCGTCCAAGTACAACTGTCAGAGTTCACCGTTCATCT
GCACAGAATGTTCACAATGACAGAGGGAAAGCTGTTCGTTGTCGTGAAAAGAAAGAACAG
AATAAAGGAAGAGAGGAAAAGAACAAATCACCTGCTGCAGTAACAGAACCAGAGACAAAT
AAATTTGATAGTACCGGATATGATAAAGACTTAGTAGAAGCTTTGGAAAGAGATATAATT
TCCCAGAATCCCAATGTTCGATGGGATGATATCGCTGATTTAGTAGAAGCTAAAAAGTTG
CTTAAGGAAGCCGTAGTGTTACCAATGTGGATGCCCGAATTCTTTAAGGGCATTAGGAGA
CCATGGAAAGGAGTACTGATGGTCGGCCCACCTGGCACGGGGAAGACGCTCCTTGCTAAA
GCAGTAGCTACAGAATGCAAGACAACATTCTTCAATGTCTCTTCATCAACTTTGACTTCC
AAATACAGAGGAGAATCTGAGAAGCTTGTTCGTCTTCTGTTTGAAATGGCTCGATTTTAT
TCTCCAGCCACCATATTTATTGATGAGATAGACTCCATCTGTAGTCGCCGAGGGACTTCT
GAAGAACATGAAGCAAGCAGAAGGGTGAAAGCGGAGCTGCTGGTTCAGATGGATGGTGTT
GGAGGTACTTCTGAAAATGATGACCCTTCCAAAATGGTTATGGTTCTGGCAGCTACTAAT
TTTCCCTGGGATATAGATGAGGCTTTAAGACGACGCCTTGAGAAACGAATCTATATTCCT
TTGCCGTCAGCAAAAGGCAGGGAGGAGCTATTACGAATAAGTCTACGTGAGTTGGAATTG
GCTGATGATGTTGACCTTGCAAGTATAGCAGAAAACATGGAAGGTTATTCAGGTGCGGAC
ATTACCAACGTGTGCAGGGATGCGTCCTTGATGGCAATGAGAAGGCGCATTGAAGGTTTG
ACTCCAGAGGAAATCCGAAATCTTTCCAAAGAAGAAATGCACATGCCTACAACTATGGAG
GATTTCGAGATGGCTTTAAAAAAGGTTTCTAAGTCAGTGTCTGCTGCAGACATTGAAAGA
TACGAGAAATGGATATTTGAGTTTGGATCATGCTAA
|
| Enzyme 118 GenBank Gene ID |
AF056022 |
| Enzyme 118 GeneCard ID |
KATNA1 |
| Enzyme 118 GenAtlas ID |
KATNA1 |
| Enzyme 118 HGNC ID |
HGNC:6216 |
| Enzyme 118 Chromosome Location |
6 |
| Enzyme 118 Locus |
6q25.1 |
| Enzyme 118 SNPs |
SNPJam Report |
| Enzyme 118 General References |
- McNally FJ, Thomas S: Katanin is responsible for the M-phase microtubule-severing activity in Xenopus eggs. Mol Biol Cell. 1998 Jul;9(7):1847-61. [PubMed ]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- McNally KP, Bazirgan OA, McNally FJ: Two domains of p80 katanin regulate microtubule severing and spindle pole targeting by p60 katanin. J Cell Sci. 2000 May;113 ( Pt 9):1623-33. [PubMed ]
- Buster D, McNally K, McNally FJ: Katanin inhibition prevents the redistribution of gamma-tubulin at mitosis. J Cell Sci. 2002 Mar 1;115(Pt 5):1083-92. [PubMed ]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
|
| Enzyme 118 Metabolite References |
Not Available |
|
Enzyme 119
[top]
|
| Enzyme 119 ID |
6461 |
| Enzyme 119 Name |
Dual specificity protein kinase CLK4 |
| Enzyme 119 Synonyms |
- CDC-like kinase 4
|
| Enzyme 119 Gene Name |
CLK4 |
| Enzyme 119 Protein Sequence |
>Dual specificity protein kinase CLK4
MRHSKRTHCPDWDSRESWGHESYRGSHKRKRRSHSSTQENRHCKPHHQFKESDCHYLEAR
SLNERDYRDRRYVDEYRNDYCEGYVPRHYHRDIESGYRIHCSKSSVRSRRSSPKRKRNRH
CSSHQSRSKSHRRKRSRSIEDDEEGHLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHG
MDGMHVAVKIVKNVGRYREAARSEIQVLEHLNSTDPNSVFRCVQMLEWFDHHGHVCIVFE
LLGLSTYDFIKENSFLPFQIDHIRQMAYQICQSINFLHHNKLTHTDLKPENILFVKSDYV
VKYNSKMKRDERTLKNTDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDV
WSIGCILIEYYLGFTVFQTHDSKEHLAMMERILGPIPQHMIQKTRKRKYFHHNQLDWDEH
SSAGRYVRRRCKPLKEFMLCHDEEHEKLFDLVRRMLEYDPTQRITLDEALQHPFFDLLKK
K
|
| Enzyme 119 Number of Residues |
481 |
| Enzyme 119 Molecular Weight |
57491.5 |
| Enzyme 119 Theoretical pI |
8.82 |
| Enzyme 119 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 119 General Function |
Involved in protein kinase activity |
| Enzyme 119 Specific Function |
Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates serines, threonines and tyrosines. Required for the regulation of alternative splicing of MAPT/TAU |
| Enzyme 119 Pathways |
Not Available |
| Enzyme 119 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 119 Pfam Domain Function |
|
| Enzyme 119 Signals |
|
| Enzyme 119 Transmembrane Regions |
|
| Enzyme 119 Essentiality |
Not Available |
| Enzyme 119 GenBank ID Protein |
9965398 |
| Enzyme 119 UniProtKB/Swiss-Prot ID |
Q9HAZ1 |
| Enzyme 119 UniProtKB/Swiss-Prot Entry Name |
CLK4_HUMAN |
| Enzyme 119 PDB ID |
Not Available |
| Enzyme 119 Cellular Location |
Not Available |
| Enzyme 119 Gene Sequence |
>1446 bp
ATGCGGCATTCCAAAAGAACTCACTGTCCTGATTGGGATAGCAGAGAAAGCTGGGGACAT
GAAAGCTATCGTGGAAGTCACAAGCGGAAGAGGAGATCTCATAGTAGCACACAAGAGAAC
AGGCATTGTAAACCACATCACCAGTTTAAAGAATCTGATTGTCATTATTTAGAAGCAAGG
TCCTTGAATGAGCGAGATTATCGGGACCGGAGATACGTTGACGAATACAGGAATGACTAC
TGTGAAGGATATGTTCCTAGACATTATCACAGAGACATTGAAAGCGGGTATCGAATCCAC
TGCAGTAAATCTTCAGTCCGCAGCAGGAGAAGCAGTCCTAAAAGGAAGCGCAATAGACAC
TGTTCAAGTCATCAGTCACGTTCGAAGAGCCACCGAAGGAAAAGATCCAGGAGTATAGAG
GATGATGAGGAGGGTCACCTGATCTGTCAAAGTGGAGACGTTCTAAGAGCAAGATATGAA
ATCGTGGACACTTTGGGTGAAGGAGCCTTTGGCAAAGTTGTAGAGTGCATTGATCATGGC
ATGGATGGCATGCATGTAGCAGTGAAAATCGTAAAAAATGTAGGCCGTTACCGTGAAGCA
GCTCGTTCAGAAATCCAAGTATTAGAGCACTTAAATAGTACTGATCCCAATAGTGTCTTC
CGATGTGTCCAGATGCTAGAATGGTTTGATCATCATGGTCATGTTTGTATTGTGTTTGAA
CTACTGGGACTTAGTACTTACGATTTCATTAAAGAAAACAGCTTTCTGCCATTTCAAATT
GACCACATCAGGCAGATGGCGTATCAGATCTGCCAGTCAATAAATTTTTTACATCATAAT
AAATTAACCCATACAGATCTGAAGCCTGAAAATATTTTGTTTGTGAAGTCTGACTATGTA
GTCAAATATAATTCTAAAATGAAACGTGATGAACGCACACTGAAAAACACAGATATCAAA
GTTGTTGACTTTGGAAGTGCAACGTATGATGATGAACATCACAGTACTTTGGTGTCTACC
CGGCACTACAGAGCTCCCGAGGTCATTTTGGCTTTAGGTTGGTCTCAGCCTTGTGATGTT
TGGAGCATAGGTTGCATTCTTATTGAATATTACCTTGGTTTCACAGTCTTTCAGACTCAT
GATAGTAAAGAGCACCTGGCAATGATGGAACGAATATTAGGACCCATACCACAACACATG
ATTCAGAAAACAAGAAAACGCAAGTATTTTCACCATAACCAGCTAGATTGGGATGAACAC
AGTTCTGCTGGTAGATATGTTAGGAGACGCTGCAAACCGTTGAAGGAATTTATGCTTTGT
CATGATGAAGAACATGAGAAACTGTTTGACCTGGTTCGAAGAATGTTAGAATATGATCCA
ACTCAAAGAATTACCTTGGATGAAGCATTGCAGCATCCTTTCTTTGACTTATTAAAAAAG
AAATGA
|
| Enzyme 119 GenBank Gene ID |
AF294429 |
| Enzyme 119 GeneCard ID |
CLK4 |
| Enzyme 119 GenAtlas ID |
CLK4 |
| Enzyme 119 HGNC ID |
HGNC:13659 |
| Enzyme 119 Chromosome Location |
5 |
| Enzyme 119 Locus |
5q35 |
| Enzyme 119 SNPs |
SNPJam Report |
| Enzyme 119 General References |
- Schultz J, Jones T, Bork P, Sheer D, Blencke S, Steyrer S, Wellbrock U, Bevec D, Ullrich A, Wallasch C: Molecular characterization of a cDNA encoding functional human CLK4 kinase and localization to chromosome 5q35 [correction of 4q35]. Genomics. 2001 Feb 1;71(3):368-70. [PubMed ]
- McNally T, Huang Q, Janis RS, Liu Z, Olejniczak ET, Reilly RM: Structural analysis of UBL5, a novel ubiquitin-like modifier. Protein Sci. 2003 Jul;12(7):1562-6. [PubMed ]
- Kantham L, Kerr-Bayles L, Godde N, Quick M, Webb R, Sunderland T, Bond J, Walder K, Augert G, Collier G: Beacon interacts with cdc2/cdc28-like kinases. Biochem Biophys Res Commun. 2003 Apr 25;304(1):125-9. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 119 Metabolite References |
Not Available |
|
Enzyme 120
[top]
|
| Enzyme 120 ID |
6462 |
| Enzyme 120 Name |
V-type proton ATPase subunit G 3 |
| Enzyme 120 Synonyms |
- V-ATPase subunit G 3
- V-ATPase 13 kDa subunit 3
- Vacuolar proton pump subunit G 3
|
| Enzyme 120 Gene Name |
ATP6V1G3 |
| Enzyme 120 Protein Sequence |
>V-type proton ATPase subunit G 3
MTSQSQGIHQLLQAEKRAKDKLEEAKKRKGKRLKQAKEEAMVEIDQYRMQRDKEFRLKQS
KIMGSQNNLSDEIEEQTLGKIQELNGHYNKYMESVMNQLLSMVCDMKPEIHVNYRATN
|
| Enzyme 120 Number of Residues |
118 |
| Enzyme 120 Molecular Weight |
13916.9 |
| Enzyme 120 Theoretical pI |
9.67 |
| Enzyme 120 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
|
| Process |
- establishment of localization
- hydrogen transport
- proton transport
- transport
|
| Component |
- macromolecular complex
- protein complex
- proton-transporting V-type ATPase complex
- proton-transporting two-sector ATPase complex
- vacuolar proton-transporting V-type ATPase complex
|
|
| Enzyme 120 General Function |
Involved in hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances |
| Enzyme 120 Specific Function |
Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells |
| Enzyme 120 Pathways |
|
| Enzyme 120 Reactions |
Not Available |
| Enzyme 120 Pfam Domain Function |
|
| Enzyme 120 Signals |
|
| Enzyme 120 Transmembrane Regions |
|
| Enzyme 120 Essentiality |
Not Available |
| Enzyme 120 GenBank ID Protein |
55957706 |
| Enzyme 120 UniProtKB/Swiss-Prot ID |
Q96LB4 |
| Enzyme 120 UniProtKB/Swiss-Prot Entry Name |
VATG3_HUMAN |
| Enzyme 120 PDB ID |
Not Available |
| Enzyme 120 Cellular Location |
Not Available |
| Enzyme 120 Gene Sequence |
>357 bp
ATGACAAGCCAGTCTCAGGGGATCCACCAGCTTCTTCAGGCAGAAAAACGGGCCAAGGAC
AAGCTAGAGGAAGCCAAGAAGAGAAAAGGAAAGCGATTGAAGCAAGCCAAGGAGGAAGCA
ATGGTAGAAATTGACCAGTACAGAATGCAGAGAGATAAAGAGTTTCGACTAAAACAATCT
AAGATAATGGGCTCTCAGAATAATCTCTCAGATGAAATAGAAGAACAAACACTAGGGAAG
ATACAAGAACTTAATGGACACTACAATAAGTATATGGAAAGTGTGATGAACCAGCTCTTG
AGCATGGTCTGTGACATGAAACCAGAAATCCATGTGAACTACAGAGCCACCAACTAA
|
| Enzyme 120 GenBank Gene ID |
AL157402 |
| Enzyme 120 GeneCard ID |
ATP6V1G3 |
| Enzyme 120 GenAtlas ID |
ATP6V1G3 |
| Enzyme 120 HGNC ID |
HGNC:18265 |
| Enzyme 120 Chromosome Location |
1 |
| Enzyme 120 Locus |
1q31.3 |
| Enzyme 120 SNPs |
SNPJam Report |
| Enzyme 120 General References |
- Smith AN, Borthwick KJ, Karet FE: Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis. Gene. 2002 Sep 4;297(1-2):169-77. [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 120 Metabolite References |
Not Available |
|
Enzyme 121
[top]
|
| Enzyme 121 ID |
6463 |
| Enzyme 121 Name |
Receptor tyrosine-protein kinase erbB-3 |
| Enzyme 121 Synonyms |
- Proto-oncogene-like protein c-ErbB-3
- Tyrosine kinase-type cell surface receptor HER3
|
| Enzyme 121 Gene Name |
ERBB3 |
| Enzyme 121 Protein Sequence |
>Receptor tyrosine-protein kinase erbB-3
MRANDALQVLGLLFSLARGSEVGNSQAVCPGTLNGLSVTGDAENQYQTLYKLYERCEVVM
GNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSTLPLPNLRVVRGTQVYDGKFAIFVM
LNYNTNSSHALRQLRLTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRDRDAEIVVKDNG
RSCPPCHEVCKGRCWGPGSEDCQTLTKTICAPQCNGHCFGPNPNQCCHDECAGGCSGPQD
TDCFACRHFNDSGACVPRCPQPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTS
CVRACPPDKMEVDKNGLKMCEPCGGLCPKACEGTGSGSRFQTVDSSNIDGFVNCTKILGN
LDFLITGLNGDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGG
RSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRIYISANRQLCYHHSLNWTKVLRGPTEE
RLDIKHNRPRRDCVAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSRGGVCVTHCNFLNGEP
REFAHEAECFSCHPECQPMEGTATCNGSGSDTCAQCAHFRDGPHCVSSCPHGVLGAKGPI
YKYPDVQNECRPCHENCTQGCKGPELQDCLGQTLVLIGKTHLTMALTVIAGLVVIFMMLG
GTFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVF
GTVHKGVWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAIGSLDHAHIVRLLGLCPG
SSLQLVTQYLPLGSLLDHVRQHRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNV
LLKSPSQVQVADFGVADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVT
VWELMTFGAEPYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKE
LANEFTRMARDPPRYLVIKRESGPGIAPGPEPHGLTNKKLEEVELEPELDLDLDLEAEED
NLATTTLGSALSLPVGTLNRPRGSQSLLSPSSGYMPMNQGNLGESCQESAVSGSSERCPR
PVSLHPMPRGCLASESSEGHVTGSEAELQEKVSMCRSRSRSRSPRPRGDSAYHSQRHSLL
TPVTPLSPPGLEEEDVNGYVMPDTHLKGTPSSREGTLSSVGLSSVLGTEEEDEDEEYEYM
NRRRRHSPPHPPRPSSLEELGYEYMDVGSDLSASLGSTQSCPLHPVPIMPTAGTTPDEDY
EYMNRQRDGGGPGGDYAAMGACPASEQGYEEMRAFQGPGHQAPHVHYARLKTLRSLEATD
SAFDNPDYWHSRLFPKANAQRT
|
| Enzyme 121 Number of Residues |
1342 |
| Enzyme 121 Molecular Weight |
148097.1 |
| Enzyme 121 Theoretical pI |
6.53 |
| Enzyme 121 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein binding
- protein kinase activity
- protein tyrosine kinase activity
- purine nucleoside binding
- receptor signaling protein tyrosine kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transmembrane receptor protein tyrosine kinase activity
|
| Process |
- cell surface receptor linked signaling pathway
- cellular metabolic process
- enzyme linked receptor protein signaling pathway
- metabolic process
- peptidyl-tyrosine phosphorylation
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- signaling
- signaling pathway
- transmembrane receptor protein tyrosine kinase signaling pathway
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 121 General Function |
Involved in transmembrane receptor protein tyrosine kinase activity |
| Enzyme 121 Specific Function |
Binds and is activated by neuregulins and NTAK |
| Enzyme 121 Pathways |
Not Available |
| Enzyme 121 Reactions |
- ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate [RN:R02584]
|
| Enzyme 121 Pfam Domain Function |
|
| Enzyme 121 Signals |
|
| Enzyme 121 Transmembrane Regions |
|
| Enzyme 121 Essentiality |
Not Available |
| Enzyme 121 GenBank ID Protein |
52789419 |
| Enzyme 121 UniProtKB/Swiss-Prot ID |
P21860 |
| Enzyme 121 UniProtKB/Swiss-Prot Entry Name |
ERBB3_HUMAN |
| Enzyme 121 PDB ID |
1M6B |
| Enzyme 121 PDB File |
Show |
| Enzyme 121 3D Structure |
|
| Enzyme 121 Cellular Location |
Not Available |
| Enzyme 121 Gene Sequence |
>4029 bp
ATGAGGGCGAACGACGCTCTGCAGGTGCTGGGCTTGCTTTTCAGCCTGGCCCGGGGCTCC
GAGGTGGGCAACTCTCAGGCAGTGTGTCCTGGGACTCTGAATGGCCTGAGTGTGACCGGC
GATGCTGAGAACCAATACCAGACACTGTACAAGCTCTACGAGAGGTGTGAGGTGGTGATG
GGGAACCTTGAGATTGTGCTCACGGGACACAATGCCGACCTCTCCTTCCTGCAGTGGATT
CGAGAAGTGACAGGCTATGTCCTCGTGGCCATGAATGAATTCTCTACTCTACCATTGCCC
AACCTCCGCGTGGTGCGAGGGACCCAGGTCTACGATGGGAAGTTTGCCATCTTCGTCATG
TTGAACTATAACACCAACTCCAGCCACGCTCTGCGCCAGCTCCGCTTGACTCAGCTCACC
GAGATTCTGTCAGGGGGTGTTTATATTGAGAAGAACGATAAGCTTTGTCACATGGACACA
ATTGACTGGAGGGACATCGTGAGGGACCGAGATGCTGAGATAGTGGTGAAGGACAATGGC
AGAAGCTGTCCCCCCTGTCATGAGGTTTGCAAGGGGCGATGCTGGGGTCCTGGATCAGAA
GACTGCCAGACATTGACCAAGACCATCTGTGCTCCTCAGTGTAATGGTCACTGCTTTGGG
CCCAACCCCAACCAGTGCTGCCATGATGAGTGTGCCGGGGGCTGCTCAGGCCCTCAGGAC
ACAGACTGCTTTGCCTGCCGGCACTTCAATGACAGTGGAGCCTGTGTACCTCGCTGTCCA
CAGCCTCTTGTCTACAACAAGCTAACTTTCCAGCTGGAACCCAATCCCCACACCAAGTAT
CAGTATGGAGGAGTTTGTGTAGCCAGCTGTCCCCATAACTTTGTGGTGGATCAAACATCC
TGTGTCAGGGCCTGTCCTCCTGACAAGATGGAAGTAGATAAAAATGGGCTCAAGATGTGT
GAGCCTTGTGGGGGACTATGTCCCAAAGCCTGTGAGGGAACAGGCTCTGGGAGCCGCTTC
CAGACTGTGGACTCGAGCAACATTGATGGATTTGTGAACTGCACCAAGATCCTGGGCAAC
CTGGACTTTCTGATCACCGGCCTCAATGGAGACCCCTGGCACAAGATCCCTGCCCTGGAC
CCAGAGAAGCTCAATGTCTTCCGGACAGTACGGGAGATCACAGGTTACCTGAACATCCAG
TCCTGGCCGCCCCACATGCACAACTTCAGTGTTTTTTCCAATTTGACAACCATTGGAGGC
AGAAGCCTCTACAACCGGGGCTTCTCATTGTTGATCATGAAGAACTTGAATGTCACATCT
CTGGGCTTCCGATCCCTGAAGGAAATTAGTGCTGGGCGTATCTATATAAGTGCCAATAGG
CAGCTCTGCTACCACCACTCTTTGAACTGGACCAAGGTGCTTCGGGGGCCTACGGAAGAG
CGACTAGACATCAAGCATAATCGGCCGCGCAGAGACTGCGTGGCAGAGGGCAAAGTGTGT
GACCCACTGTGCTCCTCTGGGGGATGCTGGGGCCCAGGCCCTGGTCAGTGCTTGTCCTGT
CGAAATTATAGCCGAGGAGGTGTCTGTGTGACCCACTGCAACTTTCTGAATGGGGAGCCT
CGAGAATTTGCCCATGAGGCCGAATGCTTCTCCTGCCACCCGGAATGCCAACCCATGGAG
GGCACTGCCACATGCAATGGCTCGGGCTCTGATACTTGTGCTCAATGTGCCCATTTTCGA
GATGGGCCCCACTGTGTGAGCAGCTGCCCCCATGGAGTCCTAGGTGCCAAGGGCCCAATC
TACAAGTACCCAGATGTTCAGAATGAATGTCGGCCCTGCCATGAGAACTGCACCCAGGGG
TGTAAAGGACCAGAGCTTCAAGACTGTTTAGGACAAACACTGGTGCTGATCGGCAAAACC
CATCTGACAATGGCTTTGACAGTGATAGCAGGATTGGTAGTGATTTTCATGATGCTGGGC
GGCACTTTTCTCTACTGGCGTGGGCGCCGGATTCAGAATAAAAGGGCTATGAGGCGATAC
TTGGAACGGGGTGAGAGCATAGAGCCTCTGGACCCCAGTGAGAAGGCTAACAAAGTCTTG
GCCAGAATCTTCAAAGAGACAGAGCTAAGGAAGCTTAAAGTGCTTGGCTCGGGTGTCTTT
GGAACTGTGCACAAAGGAGTGTGGATCCCTGAGGGTGAATCAATCAAGATTCCAGTCTGC
ATTAAAGTCATTGAGGACAAGAGTGGACGGCAGAGTTTTCAAGCTGTGACAGATCATATG
CTGGCCATTGGCAGCCTGGACCATGCCCACATTGTAAGGCTGCTGGGACTATGCCCAGGG
TCATCTCTGCAGCTTGTCACTCAATATTTGCCTCTGGGTTCTCTGCTGGATCATGTGAGA
CAACACCGGGGGGCACTGGGGCCACAGCTGCTGCTCAACTGGGGAGTACAAATTGCCAAG
GGAATGTACTACCTTGAGGAACATGGTATGGTGCATAGAAACCTGGCTGCCCGAAACGTG
CTACTCAAGTCACCCAGTCAGGTTCAGGTGGCAGATTTTGGTGTGGCTGACCTGCTGCCT
CCTGATGATAAGCAGCTGCTATACAGTGAGGCCAAGACTCCAATTAAGTGGATGGCCCTT
GAGAGTATCCACTTTGGGAAATACACACACCAGAGTGATGTCTGGAGCTATGGTGTGACA
GTTTGGGAGTTGATGACCTTCGGGGCAGAGCCCTATGCAGGGCTACGATTGGCTGAAGTA
CCAGACCTGCTAGAGAAGGGGGAGCGGTTGGCACAGCCCCAGATCTGCACAATTGATGTC
TACATGGTGATGGTCAAGTGTTGGATGATTGATGAGAACATTCGCCCAACCTTTAAAGAA
CTAGCCAATGAGTTCACCAGGATGGCCCGAGACCCACCACGGTATCTGGTCATAAAGAGA
GAGAGTGGGCCTGGAATAGCCCCTGGGCCAGAGCCCCATGGTCTGACAAACAAGAAGCTA
GAGGAAGTAGAGCTGGAGCCAGAACTAGACCTAGACCTAGACTTGGAAGCAGAGGAGGAC
AACCTGGCAACCACCACACTGGGCTCCGCCCTCAGCCTACCAGTTGGAACACTTAATCGG
CCACGTGGGAGCCAGAGCCTTTTAAGTCCATCATCTGGATACATGCCCATGAACCAGGGT
AATCTTGGGGAGTCTTGCCAGGAGTCTGCAGTTTCTGGGAGCAGTGAACGGTGCCCCCGT
CCAGTCTCTCTACACCCAATGCCACGGGGATGCCTGGCATCAGAGTCATCAGAGGGGCAT
GTAACAGGCTCTGAGGCTGAGCTCCAGGAGAAAGTGTCAATGTGTAGGAGCCGGAGCAGG
AGCCGGAGCCCACGGCCACGCGGAGATAGCGCCTACCATTCCCAGCGCCACAGTCTGCTG
ACTCCTGTTACCCCACTCTCCCCACCCGGGTTAGAGGAAGAGGATGTCAACGGTTATGTC
ATGCCAGATACACACCTCAAAGGTACTCCCTCCTCCCGGGAAGGCACCCTTTCTTCAGTG
GGTCTCAGTTCTGTCCTGGGTACTGAAGAAGAAGATGAAGATGAGGAGTATGAATACATG
AACCGGAGGAGAAGGCACAGTCCACCTCATCCCCCTAGGCCAAGTTCCCTTGAGGAGCTG
GGTTATGAGTACATGGATGTGGGGTCAGACCTCAGTGCCTCTCTGGGCAGCACACAGAGT
TGCCCACTCCACCCTGTACCCATCATGCCCACTGCAGGCACAACTCCAGATGAAGACTAT
GAATATATGAATCGGCAACGAGATGGAGGTGGTCCTGGGGGTGATTATGCAGCCATGGGG
GCCTGCCCAGCATCTGAGCAAGGGTATGAAGAGATGAGAGCTTTTCAGGGGCCTGGACAT
CAGGCCCCCCATGTCCATTATGCCCGCCTAAAAACTCTACGTAGCTTAGAGGCTACAGAC
TCTGCCTTTGATAACCCTGATTACTGGCATAGCAGGCTTTTCCCCAAGGCTAATGCCCAG
AGAACGTAA
|
| Enzyme 121 GenBank Gene ID |
BC082992 |
| Enzyme 121 GeneCard ID |
ERBB3 |
| Enzyme 121 GenAtlas ID |
ERBB3 |
| Enzyme 121 HGNC ID |
HGNC:3431 |
| Enzyme 121 Chromosome Location |
1 |
| Enzyme 121 Locus |
12q13 |
| Enzyme 121 SNPs |
SNPJam Report |
| Enzyme 121 General References |
- Kraus MH, Issing W, Miki T, Popescu NC, Aaronson SA: Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: evidence for overexpression in a subset of human mammary tumors. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9193-7. [PubMed ]
- Plowman GD, Whitney GS, Neubauer MG, Green JM, McDonald VL, Todaro GJ, Shoyab M: Molecular cloning and expression of an additional epidermal growth factor receptor-related gene. Proc Natl Acad Sci U S A. 1990 Jul;87(13):4905-9. [PubMed ]
- Katoh M, Yazaki Y, Sugimura T, Terada M: c-erbB3 gene encodes secreted as well as transmembrane receptor tyrosine kinase. Biochem Biophys Res Commun. 1993 May 14;192(3):1189-97. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Lessor TJ, Hamburger AW: Regulation of the ErbB3 binding protein Ebp1 by protein kinase C. Mol Cell Endocrinol. 2001 Apr 25;175(1-2):185-91. [PubMed ]
- Li Y, Yu WH, Ren J, Chen W, Huang L, Kharbanda S, Loda M, Kufe D: Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein. Mol Cancer Res. 2003 Aug;1(10):765-75. [PubMed ]
- Kinugasa Y, Ishiguro H, Tokita Y, Oohira A, Ohmoto H, Higashiyama S: Neuroglycan C, a novel member of the neuregulin family. Biochem Biophys Res Commun. 2004 Sep 3;321(4):1045-9. [PubMed ]
- Narkis G, Ofir R, Manor E, Landau D, Elbedour K, Birk OS: Lethal congenital contractural syndrome type 2 (LCCS2) is caused by a mutation in ERBB3 (Her3), a modulator of the phosphatidylinositol-3-kinase/Akt pathway. Am J Hum Genet. 2007 Sep;81(3):589-95. Epub 2007 Jul 24. [PubMed ]
- Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Cho HS, Leahy DJ: Structure of the extracellular region of HER3 reveals an interdomain tether. Science. 2002 Aug 23;297(5585):1330-3. Epub 2002 Aug 1. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 121 Metabolite References |
Not Available |
|
Enzyme 122
[top]
|
| Enzyme 122 ID |
6464 |
| Enzyme 122 Name |
Ephrin type-A receptor 5 |
| Enzyme 122 Synonyms |
- EPH homology kinase 1
- EHK-1
- EPH-like kinase 7
- EK7
- hEK7
|
| Enzyme 122 Gene Name |
EPHA5 |
| Enzyme 122 Protein Sequence |
>Ephrin type-A receptor 5
MRGSGPRGAGRRRPPSGGGDTPITPASLAGCYSAPRRAPLWTCLLLCAALRTLLASPSNE
VNLLDSRTVMGDLGWIAFPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISN
EGASRIFIELKFTLRDCNSLPGGLGTCKETFNMYYFESDDQNGRNIKENQYIKIDTIAAD
ESFTELDLGDRVMKLNTEVRDVGPLSKKGFYLAFQDVGACIALVSVRVYYKKCPSVVRHL
AVFPDTITGADSSQLLEVSGSCVNHSVTDEPPKMHCSAEGEWLVPIGKCMCKAGYEEKNG
TCQVCRPGFFKASPHIQSCGKCPPHSYTHEEASTSCVCEKDYFRRESDPPTMACTRPPSA
PRNAISNVNETSVFLEWIPPADTGGRKDVSYYIACKKCNSHAGVCEECGGHVRYLPRQSG
LKNTSVMMVDLLAHTNYTFEIEAVNGVSDLSPGARQYVSVNVTTNQAAPSPVTNVKKGKI
AKNSISLSWQEPDRPNGIILEYEIKYFEKDQETSYTIIKSKETTITAEGLKPASVYVFQI
RARTAAGYGVFSRRFEFETTPVFAASSDQSQIPVIAVSVTVGVILLAVVIGVLLSGSCCE
CGCGRASSLCAVAHPSLIWRCGYSKAKQDPEEEKMHFHNGHIKLPGVRTYIDPHTYEDPN
QAVHEFAKEIEASCITIERVIGAGEFGEVCSGRLKLPGKRELPVAIKTLKVGYTEKQRRD
FLGEASIMGQFDHPNIIHLEGVVTKSKPVMIVTEYMENGSLDTFLKKNDGQFTVIQLVGM
LRGISAGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKI
PIRWTAPEAIAFRKFTSASDVWSYGIVMWEVVSYGERPYWEMTNQDVIKAVEEGYRLPSP
MDCPAALYQLMLDCWQKERNSRPKFDEIVNMLDKLIRNPSSLKTLVNASCRVSNLLAEHS
PLGSGAYRSVGEWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIM
NSLQEMKVQLVNGMVPL
|
| Enzyme 122 Number of Residues |
1037 |
| Enzyme 122 Molecular Weight |
114802.3 |
| Enzyme 122 Theoretical pI |
6.92 |
| Enzyme 122 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ephrin receptor activity
- kinase activity
- nucleoside binding
- protein binding
- protein kinase activity
- protein tyrosine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transmembrane receptor protein tyrosine kinase activity
|
| Process |
- cell surface receptor linked signaling pathway
- cellular metabolic process
- enzyme linked receptor protein signaling pathway
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- signaling
- signaling pathway
- transmembrane receptor protein tyrosine kinase signaling pathway
|
| Component |
- cell part
- integral to membrane
- integral to plasma membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 122 General Function |
Involved in ephrin receptor activity |
| Enzyme 122 Specific Function |
Receptor for members of the ephrin-A family. Binds to ephrin-A1, -A2, -A3, -A4 and -A5 |
| Enzyme 122 Pathways |
Not Available |
| Enzyme 122 Reactions |
- ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate [RN:R02584]
|
| Enzyme 122 Pfam Domain Function |
|
| Enzyme 122 Signals |
|
| Enzyme 122 Transmembrane Regions |
|
| Enzyme 122 Essentiality |
Not Available |
| Enzyme 122 GenBank ID Protein |
221625401 |
| Enzyme 122 UniProtKB/Swiss-Prot ID |
P54756 |
| Enzyme 122 UniProtKB/Swiss-Prot Entry Name |
EPHA5_HUMAN |
| Enzyme 122 PDB ID |
Not Available |
| Enzyme 122 Cellular Location |
Not Available |
| Enzyme 122 Gene Sequence |
>3114 bp
ATGCGGGGCTCGGGGCCCCGGGGTGCGGGACGCCGGCGGCCCCCAAGCGGCGGCGGCGAC
ACCCCCATCACCCCAGCGTCCCTGGCCGGCTGCTACTCTGCACCTCGACGGGCTCCCCTC
TGGACGTGCCTTCTCCTGTGCGCCGCACTCCGGACCCTCCTGGCCAGCCCCAGCAACGAA
GTGAATTTATTGGATTCACGCACTGTCATGGGGGACCTGGGATGGATTGCTTTTCCAAAA
AATGGGTGGGAAGAGATTGGTGAAGTGGATGAAAATTATGCCCCTATCCACACATACCAA
GTATGCAAAGTGATGGAACAGAATCAGAATAACTGGCTTTTGACCAGTTGGATCTCCAAT
GAAGGTGCTTCCAGAATCTTCATAGAACTCAAATTTACCCTGCGGGACTGCAACAGCCTT
CCTGGAGGACTGGGGACCTGTAAGGAAACCTTTAATATGTATTACTTTGAGTCAGATGAT
CAGAATGGGAGAAACATCAAGGAAAACCAATACATCAAAATTGATACCATTGCTGCCGAT
GAAAGCTTTACAGAACTTGATCTTGGTGACCGTGTTATGAAACTGAATACAGAGGTCAGA
GATGTAGGACCTCTAAGCAAAAAGGGATTTTATCTTGCTTTTCAAGATGTTGGTGCTTGC
ATTGCTCTGGTTTCTGTGCGTGTATACTATAAAAAATGCCCTTCTGTGGTACGACACTTG
GCTGTCTTCCCTGACACCATCACTGGAGCTGATTCTTCCCAATTGCTCGAAGTGTCAGGC
TCCTGTGTCAACCATTCTGTGACCGATGAACCTCCCAAAATGCACTGCAGCGCCGAAGGG
GAGTGGCTGGTGCCCATCGGGAAATGCATGTGCAAGGCAGGATATGAAGAGAAAAATGGC
ACCTGTCAAGTGTGCAGACCTGGGTTCTTCAAAGCCTCACCTCACATCCAGAGCTGCGGC
AAATGTCCACCTCACAGTTATACCCATGAGGAAGCTTCAACCTCTTGTGTCTGTGAAAAG
GATTATTTCAGGAGAGAGTCTGATCCACCCACAATGGCATGCACAAGACCCCCCTCTGCT
CCTCGGAATGCCATCTCAAATGTTAATGAAACTAGTGTCTTTCTGGAATGGATTCCGCCT
GCTGACACTGGTGGAAGGAAAGACGTGTCATATTATATTGCATGCAAGAAGTGCAACTCC
CATGCAGGTGTGTGTGAGGAGTGTGGCGGTCATGTCAGGTACCTTCCCCGGCAAAGCGGC
CTGAAAAACACCTCTGTCATGATGGTGGATCTACTCGCTCACACAAACTATACCTTTGAG
ATTGAGGCAGTGAATGGAGTGTCCGACTTGAGCCCAGGAGCCCGGCAGTATGTGTCTGTA
AATGTAACCACAAATCAAGCAGCTCCATCTCCAGTCACCAATGTGAAAAAAGGGAAAATT
GCAAAAAACAGCATCTCTTTGTCTTGGCAAGAACCAGATCGTCCCAATGGAATCATCCTA
GAGTATGAAATCAAGTATTTTGAAAAGGACCAAGAGACCAGCTACACGATTATCAAATCT
AAAGAGACAACTATTACTGCAGAGGGCTTGAAACCAGCTTCAGTTTATGTCTTCCAAATT
CGAGCACGTACAGCAGCAGGCTATGGTGTCTTCAGTCGAAGATTTGAGTTTGAAACCACC
CCAGTGTTTGCAGCATCCAGCGATCAAAGCCAGATTCCTGTAATTGCTGTGTCTGTGACA
GTGGGAGTCATTTTGTTGGCAGTGGTTATCGGCGTCCTCCTCAGTGGAAGTTGCTGCGAA
TGTGGCTGTGGGAGGGCTTCTTCCCTGTGCGCTGTTGCCCATCCAAGCCTAATATGGCGG
TGTGGCTACAGCAAAGCAAAACAAGATCCAGAAGAGGAAAAGATGCATTTTCATAATGGG
CACATTAAACTGCCAGGAGTAAGAACTTACATTGATCCACATACCTATGAGGATCCCAAT
CAAGCTGTCCACGAATTTGCTAAGGAGATAGAAGCATCATGTATCACCATTGAGAGAGTT
ATTGGAGCAGGTGAATTTGGTGAAGTTTGTAGTGGACGTTTGAAACTACCAGGAAAAAGA
GAATTACCTGTGGCTATCAAAACCCTTAAAGTAGGCTATACTGAAAAGCAACGCAGAGAT
TTCCTAGGTGAAGCAAGTATCATGGGACAGTTTGATCATCCTAACATCATCCATTTAGAA
GGTGTGGTGACCAAAAGTAAACCAGTGATGATCGTGACAGAGTATATGGAGAATGGCTCT
TTAGATACATTTTTGAAGAAAAACGATGGGCAGTTCACTGTGATTCAGCTTGTTGGCATG
CTGAGAGGTATCTCTGCAGGAATGAAGTACCTTTCTGACATGGGCTATGTGCATAGAGAT
CTTGCTGCCAGAAACATCTTAATCAACAGTAACCTTGTGTGCAAAGTGTCTGACTTTGGA
CTTTCCCGGGTACTGGAAGATGATCCCGAGGCAGCCTACACCACAAGGGGAGGAAAAATT
CCAATCAGATGGACTGCCCCAGAAGCAATAGCTTTCCGAAAGTTTACTTCTGCCAGTGAT
GTCTGGAGTTATGGAATAGTAATGTGGGAAGTTGTGTCTTATGGAGAGAGACCCTACTGG
GAGATGACCAATCAAGATGTGATTAAAGCGGTAGAGGAAGGCTATCGTCTGCCAAGCCCC
ATGGATTGTCCTGCTGCTCTCTATCAGTTAATGCTGGATTGCTGGCAGAAAGAGCGAAAT
AGCAGGCCCAAGTTTGATGAAATAGTCAACATGTTGGACAAGCTGATACGTAACCCAAGT
AGTCTGAAGACGCTGGTTAATGCATCCTGCAGAGTATCTAATTTATTGGCAGAACATAGC
CCACTAGGATCTGGGGCCTACAGATCAGTAGGTGAATGGCTAGAGGCAATCAAGATGGGC
CGGTATACAGAGATTTTCATGGAAAATGGATACAGTTCAATGGACGCTGTGGCTCAGGTG
ACCTTGGAGGATTTGAGACGGCTTGGAGTGACTCTTGTCGGTCACCAGAAGAAGATCATG
AACAGCCTTCAAGAAATGAAGGTGCAGCTGGTAAACGGAATGGTGCCATTGTAA
|
| Enzyme 122 GenBank Gene ID |
NM_004439.5 |
| Enzyme 122 GeneCard ID |
EPHA5 |
| Enzyme 122 GenAtlas ID |
EPHA5 |
| Enzyme 122 HGNC ID |
HGNC:3389 |
| Enzyme 122 Chromosome Location |
4 |
| Enzyme 122 Locus |
4q13.1 |
| Enzyme 122 SNPs |
SNPJam Report |
| Enzyme 122 General References |
- Miescher GC, Taylor V, Olivieri G, Mindermann T, Schrock E, Steck AJ: Extensive splice variation and localization of the EHK-1 receptor tyrosine kinase in adult human brain and glial tumors. Brain Res Mol Brain Res. 1997 Jun;46(1-2):17-24. [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 ]
- 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 ]
- Fox GM, Holst PL, Chute HT, Lindberg RA, Janssen AM, Basu R, Welcher AA: cDNA cloning and tissue distribution of five human EPH-like receptor protein-tyrosine kinases. Oncogene. 1995 Mar 2;10(5):897-905. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 122 Metabolite References |
Not Available |
|
Enzyme 123
[top]
|
| Enzyme 123 ID |
6465 |
| Enzyme 123 Name |
Probable phospholipid-transporting ATPase VA |
| Enzyme 123 Synonyms |
- ATPase class V type 10A
- Aminophospholipid translocase VA
|
| Enzyme 123 Gene Name |
ATP10A |
| Enzyme 123 Protein Sequence |
>Probable phospholipid-transporting ATPase VA
MEREPAGTEEPGPPGRRRRREGRTRTVRSNLLPPPGAEDPAAGAAKGERRRRRGCAQHLA
DNRLKTTKYTLLSFLPKNLFEQFHRPANVYFVFIALLNFVPAVNAFQPGLALAPVLFILA
ITAFRDLWEDYSRHRSDHKINHLGCLVFSREEKKYVNRFWKEIHVGDFVRLRCNEIFPAD
ILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDL
SRFRGCIIHDNGKKAGLYKENLLLRGCTLRNTDAVVGIVIYAGHETKALLNNSGPRYKRS
KLERQMNCDVLWCVLLLVCMSLFSAVGHGLWIWRYQEKKSLFYVPKSDGSSLSPVTAAVY
SFLTMIIVLQVLIPISLYVSIEIVKACQVYFINQDMQLYDEETDSQLQCRALNITEDLGQ
IQYIFSDKTGTLTENKMVFRRCTVSGVEYSHDANAQRLARYQEADSEEEEVVPRGGSVSQ
RGSIGSHQSVRVVHRTQSTKSHRRTGSRAEAKRASMLSKHTAFSSPMEKDITPDPKLLEK
VSECDKSLAVARHQEHLLAHLSPELSDVFDFFIALTICNTVVVTSPDQPRTKVRVRFELK
SPVKTIEDFLRRFTPSCLTSGCSSIGSLAANKSSHKLGSSFPSTPSSDGMLLRLEERLGQ
PTSAIASNGYSSQADNWASELAQEQESERELRYEAESPDEAALVYAARAYNCVLVERLHD
QVSVELPHLGRLTFELLHTLGFDSVRKRMSVVIRHPLTDEINVYTKGADSVVMDLLQPCS
SVDARGRHQKKIRSKTQNYLNVYAAEGLRTLCIAKRVLSKEEYACWLQSHLEAESSLENS
EELLFQSAIRLETNLHLLGATGIEDRLQDGVPETISKLRQAGLQIWVLTGDKQETAVNIA
YACKLLDHDEEVITLNATSQEACAALLDQCLCYVQSRGLQRAPEKTKGKVSMRFSSLCPP
STSTASGRRPSLVIDGRSLAYALEKNLEDKFLFLAKQCRSVLCCRSTPLQKSMVVKLVRS
KLKAMTLAIGDGANDVSMIQVADVGVGISGQEGMQAVMASDFAVPKFRYLERLLILHGHW
CYSRLANMVLYFFYKNTMFVGLLFWFQFFCGFSASTMIDQWYLIFFNLLFSSLPPLVTGV
LDRDVPANVLLTNPQLYKSGQNMEEYRPRTFWFNMADAAFQSLVCFSIPYLAYYDSNVDL
FTWGTPIVTIALLTFLLHLGIETKTWTWLNWITCGFSVLLFFTVALIYNASCATCYPPSN
PYWTMQALLGDPVFYLTCLMTPVAALLPRLFFRSLQGRVFPTQLQLARQLTRKSPRRCSA
PKETFAQGRLPKDSGTEHSSGRTVKTSVPLSQPSWHTQQPVCSLEASGEPSTVDMSMPVR
EHTLLEGLSAPAPMSSAPGEAVLRSPGGCPEESKVRAASTGRVTPLSSLFSLPTFSLLNW
ISSWSLVSRLGSVLQFSRTEQLADGQAGRGLPVQPHSGRSGLQGPDHRLLIGASSRRSQ
|
| Enzyme 123 Number of Residues |
1499 |
| Enzyme 123 Molecular Weight |
167686.6 |
| Enzyme 123 Theoretical pI |
8.43 |
| Enzyme 123 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 123 General Function |
Involved in ATP binding |
| Enzyme 123 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 123 Pathways |
Not Available |
| Enzyme 123 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 123 Pfam Domain Function |
|
| Enzyme 123 Signals |
|
| Enzyme 123 Transmembrane Regions |
- 87-106
111-128
310-332
363-384
1088-1108
1120-1140
1171-1192
1200-1222
1229-1249
1268-1292
|
| Enzyme 123 Essentiality |
Not Available |
| Enzyme 123 GenBank ID Protein |
14424433 |
| Enzyme 123 UniProtKB/Swiss-Prot ID |
O60312 |
| Enzyme 123 UniProtKB/Swiss-Prot Entry Name |
AT10A_HUMAN |
| Enzyme 123 PDB ID |
Not Available |
| Enzyme 123 Cellular Location |
Not Available |
| Enzyme 123 Gene Sequence |
>4500 bp
ATGGAGCGGGAGCCGGCGGGGACCGAGGAGCCCGGGCCTCCGGGACGGCGGAGGCGCCGA
GAGGGCAGGACGCGCACGGTGCGCTCCAACCTGCTGCCGCCCCCGGGCGCCGAGGACCCT
GCGGCTGGCGCGGCCAAGGGCGAGCGGCGACGGCGGCGCGGGTGTGCCCAGCACCTGGCC
GACAACCGGCTCAAGACTACCAAGTACACGCTGCTGTCCTTCCTGCCCAAGAACCTGTTC
GAGCAGTTCCACCGCCCGGCCAACGTGTACTTTGTCTTCATCGCGCTGCTCAACTTCGTG
CCGGCGGTGAACGCCTTCCAGCCCGGCCTGGCACTGGCGCCGGTGCTCTTCATCCTGGCC
ATCACGGCCTTCAGGGACCTGTGGGAGGACTACAGCCGCCACCGCTCCGACCACAAGATC
AACCACCTGGGCTGCCTGGTCTTCAGCAGGGAAGAAAAGAAATACGTGAACCGATTCTGG
AAAGAAATCCACGTGGGAGACTTTGTGCGTCTTCGCTGCAACGAAATCTTCCCTGCGGAC
ATTCTGCTGCTCTCCTCCAGTGACCCCGACGGGCTATGCCACATCGAGACCGCCAACCTG
GATGGAGAGACCAACCTGAAGCGGCGGCAGGTGGTCCGCGGCTTCTCGGAGCTTGTCTCC
GAATTCAATCCTTTGACGTTCACCAGCGTGATCGAATGCGAGAAGCCAAACAACGACCTG
AGTAGGTTTCGCGGCTGCATCATACATGACAACGGGAAAAAGGCCGGGCTGTATAAAGAA
AACCTGCTGCTGAGGGGCTGCACCCTTAGGAACACGGACGCAGTCGTCGGCATTGTCATC
TACGCAGGACATGAAACCAAGGCTCTGCTGAACAACAGTGGGCCCCGCTACAAGCGCAGC
AAGCTGGAGAGGCAGATGAACTGCGACGTGCTCTGGTGTGTCCTGCTCCTTGTTTGCATG
TCTCTGTTTTCAGCAGTCGGACATGGACTGTGGATATGGCGGTATCAAGAGAAGAAGTCA
TTATTTTATGTCCCCAAGTCTGATGGAAGCTCCTTATCCCCAGTCACAGCTGCAGTTTAC
TCATTTTTAACAATGATAATAGTTCTGCAGGTTTTGATCCCAATTTCCTTATACGTTTCC
ATTGAAATTGTTAAAGCATGCCAAGTGTACTTCATTAACCAGGACATGCAGTTGTATGAC
GAAGAAACAGACTCGCAGCTGCAGTGCCGAGCTCTGAACATCACGGAAGACTTAGGACAG
ATACAGTACATTTTCTCAGATAAAACTGGCACTTTGACAGAGAATAAGATGGTTTTCCGA
AGATGCACTGTGTCTGGTGTAGAATATTCTCATGATGCAAATGCGCAGCGTCTGGCCAGG
TACCAAGAGGCAGACTCGGAGGAGGAGGAGGTGGTGCCCAGAGGGGGCTCGGTGTCCCAG
CGCGGCAGCATCGGCAGCCACCAGAGTGTCCGGGTGGTGCACAGAACCCAGAGCACCAAG
TCCCACCGGCGCACGGGCAGCCGGGCCGAGGCCAAGAGGGCCAGCATGCTGTCCAAGCAC
ACGGCCTTCAGCAGCCCCATGGAGAAGGATATCACGCCCGACCCAAAGCTGCTGGAGAAG
GTGAGTGAGTGTGACAAGAGCCTAGCCGTGGCGAGGCATCAGGAGCACCTGCTGGCCCAC
CTCTCGCCTGAGCTGTCTGACGTCTTTGATTTCTTCATCGCACTCACCATCTGCAACACA
GTCGTCGTCACGTCCCCGGATCAGCCACGAACAAAGGTGAGGGTGAGGTTTGAGCTGAAG
TCCCCGGTGAAGACGATAGAAGACTTCCTGCGGAGGTTCACACCCAGCTGCCTGACCTCA
GGCTGCAGCAGCATCGGGAGCCTGGCCGCCAACAAGTCCAGCCACAAGTTGGGCTCCAGC
TTCCCGTCCACCCCGTCCAGCGACGGCATGCTTCTCAGGCTGGAGGAGAGGCTGGGCCAG
CCCACCTCGGCCATCGCCAGCAACGGCTACAGCAGCCAGGCGGACAACTGGGCCTCGGAG
CTTGCTCAGGAGCAGGAGTCAGAGCGCGAGCTGCGGTACGAGGCGGAGAGCCCGGATGAG
GCCGCACTGGTGTATGCGGCCAGAGCCTACAACTGCGTGCTTGTGGAGCGGCTGCACGAC
CAAGTGTCAGTGGAGCTGCCCCACCTGGGCAGGCTCACCTTCGAGCTCCTGCACACACTG
GGTTTCGATTCCGTCCGCAAGAGGATGTCAGTGGTGATCCGGCACCCGCTTACCGATGAG
ATCAACGTCTACACCAAGGGGGCCGACTCAGTGGTCATGGATCTCCTGCAGCCCTGCTCT
TCAGTTGACGCCAGAGGGAGGCATCAAAAAAAGATTCGGAGCAAAACTCAGAATTACCTC
AACGTGTATGCGGCGGAAGGCCTGCGCACCTTGTGCATCGCCAAGAGAGTTCTGAGTAAA
GAAGAGTATGCCTGCTGGTTGCAAAGCCACCTAGAAGCCGAATCCTCCCTGGAAAACAGC
GAGGAGCTCCTCTTCCAGTCTGCCATTCGCCTGGAGACCAACCTGCACTTGTTAGGTGCC
ACTGGGATTGAAGACCGCCTGCAGGACGGAGTCCCTGAAACTATTTCTAAATTGCGTCAA
GCGGGCCTGCAGATTTGGGTTCTCACTGGTGACAAACAAGAAACAGCTGTCAACATTGCA
TATGCCTGCAAACTGCTGGACCACGACGAGGAGGTCATCACCCTGAATGCCACCTCCCAG
GAGGCGTGTGCAGCCCTGCTAGACCAGTGCCTATGCTACGTGCAGTCCAGAGGCCTCCAG
AGAGCCCCTGAGAAGACCAAGGGCAAAGTGAGCATGAGGTTCTCCTCTCTCTGCCCACCC
TCCACGTCCACTGCCTCTGGCCGCAGACCCAGCCTCGTGATCGATGGGAGAAGCCTGGCC
TACGCTCTCGAGAAAAACCTGGAGGACAAATTCCTCTTCCTTGCCAAGCAGTGCCGCTCC
GTCCTCTGCTGTCGGTCGACGCCTCTGCAGAAGAGCATGGTGGTGAAGCTGGTGCGGAGC
AAGCTCAAGGCCATGACCCTGGCCATAGGTGATGGAGCCAATGATGTCAGCATGATCCAG
GTGGCAGATGTGGGTGTGGGAATCTCCGGCCAGGAGGGTATGCAGGCAGTGATGGCCAGC
GACTTTGCAGTGCCGAAATTCCGATACCTGGAGAGGCTCTTGATTCTTCACGGGCATTGG
TGCTACTCCCGACTTGCCAACATGGTGCTGTACTTCTTCTACAAAAACACAATGTTCGTG
GGCCTCCTGTTTTGGTTCCAGTTTTTCTGTGGCTTCTCTGCATCTACCATGATTGACCAG
TGGTATCTAATCTTCTTTAATCTGCTCTTCTCGTCACTTCCCCCGCTCGTGACTGGGGTG
CTGGACAGGGATGTGCCAGCCAATGTGCTGCTGACCAACCCGCAGCTCTACAAGAGTGGC
CAGAACATGGAGGAATACCGGCCACGAACGTTCTGGTTTAACATGGCCGACGCCGCCTTC
CAGAGCCTGGTTTGCTTTTCCATTCCTTACCTGGCCTACTATGACTCGAACGTGGACCTG
TTTACCTGGGGGACCCCTATTGTGACAATCGCGCTGCTCACTTTCCTGCTCCACCTGGGC
ATTGAAACCAAAACCTGGACCTGGCTCAACTGGATAACGTGTGGCTTCAGTGTCCTTTTG
TTTTTCACCGTGGCTTTGATTTACAATGCGTCTTGTGCCACGTGCTATCCTCCGTCCAAC
CCTTACTGGACTATGCAAGCCTTACTGGGTGACCCAGTGTTTTACTTGACTTGCCTGATG
ACGCCTGTCGCTGCACTGCTGCCCAGATTGTTTTTCAGATCCCTCCAGGGGAGGGTTTTC
CCCACACAACTTCAGCTGGCACGTCAGTTGACCAGGAAGTCCCCCAGGAGATGCAGTGCT
CCCAAAGAGACCTTTGCTCAGGGACGCCTCCCGAAGGACTCGGGAACCGAGCACTCATCA
GGGAGGACAGTCAAGACCTCTGTGCCCCTGTCCCAGCCTTCTTGGCACACACAGCAGCCG
GTCTGCTCCCTGGAGGCCAGCGGGGAGCCCAGCACAGTGGACATGAGCATGCCAGTGAGG
GAGCACACCCTGCTGGAGGGGCTGAGCGCACCGGCCCCCATGTCCTCTGCGCCAGGGGAG
GCTGTCCTGAGGAGTCCAGGAGGGTGTCCTGAGGAGTCCAAGGTGAGAGCTGCCAGCACC
GGCAGGGTGACCCCCCTGTCTTCCCTCTTCAGCCTGCCTACCTTCAGCTTACTCAACTGG
ATTTCCTCCTGGTCGCTGGTCAGCAGGCTGGGGAGTGTCTTACAGTTCTCCCGGACGGAG
CAGCTTGCAGATGGACAAGCGGGACGTGGACTTCCTGTCCAGCCCCACTCAGGCCGATCA
GGACTTCAAGGGCCAGACCACAGACTACTTATAGGAGCATCTTCAAGGCGGTCACAGTGA
|
| Enzyme 123 GenBank Gene ID |
NM_024490.3 |
| Enzyme 123 GeneCard ID |
ATP10A |
| Enzyme 123 GenAtlas ID |
ATP10A |
| Enzyme 123 HGNC ID |
HGNC:13542 |
| Enzyme 123 Chromosome Location |
1 |
| Enzyme 123 Locus |
15q11.2 |
| Enzyme 123 SNPs |
SNPJam Report |
| Enzyme 123 General References |
- Meguro M, Kashiwagi A, Mitsuya K, Nakao M, Kondo I, Saitoh S, Oshimura M: A novel maternally expressed gene, ATP10C, encodes a putative aminophospholipid translocase associated with Angelman syndrome. Nat Genet. 2001 May;28(1):19-20. [PubMed ]
- Herzing LB, Kim SJ, Cook EH Jr, Ledbetter DH: The human aminophospholipid-transporting ATPase gene ATP10C maps adjacent to UBE3A and exhibits similar imprinted expression. Am J Hum Genet. 2001 Jun;68(6):1501-5. Epub 2001 May 11. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed ]
|
| Enzyme 123 Metabolite References |
Not Available |
|
Enzyme 124
[top]
|
| Enzyme 124 ID |
6468 |
| Enzyme 124 Name |
[Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial |
| Enzyme 124 Synonyms |
- Pyruvate dehydrogenase kinase isoform 1
|
| Enzyme 124 Gene Name |
PDK1 |
| Enzyme 124 Protein Sequence |
>[Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial
MRLARLLRGAALAGPGPGLRAAGFSRSFSSDSGSSPASERGVPGQVDFYARFSPSPLSMK
QFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQE
LLDFKDKSAEDAKAIYDFTDTVIRIRNRHNDVIPTMAQGVIEYKESFGVDPVTSQNVQYF
LDRFYMSRISIRMLLNQHSLLFGGKGKGSPSHRKHIGSINPNCNVLEVIKDGYENARRLC
DLYYINSPELELEELNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHANRGVYPP
IQVHVTLGNEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAVPLAGFGYGLP
ISRLYAQYFQGDLKLYSLEGYGTDAVIYIKALSTDSIERLPVYNKAAWKHYNTNHEADDW
CVPSREPKDMTTFRSA
|
| Enzyme 124 Number of Residues |
436 |
| Enzyme 124 Molecular Weight |
49243.8 |
| Enzyme 124 Theoretical pI |
9.05 |
| Enzyme 124 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein histidine kinase activity
- protein kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- two-component sensor activity
|
| Process |
- biological regulation
- cellular metabolic process
- metabolic process
- peptidyl-histidine phosphorylation
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- regulation of biological process
- regulation of cellular process
- signal transduction
|
| Component |
| — |
|
| Enzyme 124 General Function |
Involved in ATP binding |
| Enzyme 124 Specific Function |
Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism |
| Enzyme 124 Pathways |
Not Available |
| Enzyme 124 Reactions |
- ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate [RN:R03449]
|
| Enzyme 124 Pfam Domain Function |
|
| Enzyme 124 Signals |
|
| Enzyme 124 Transmembrane Regions |
|
| Enzyme 124 Essentiality |
Not Available |
| Enzyme 124 GenBank ID Protein |
1088281 |
| Enzyme 124 UniProtKB/Swiss-Prot ID |
Q15118 |
| Enzyme 124 UniProtKB/Swiss-Prot Entry Name |
PDK1_HUMAN |
| Enzyme 124 PDB ID |
Not Available |
| Enzyme 124 Cellular Location |
Not Available |
| Enzyme 124 Gene Sequence |
>1311 bp
ATGAGGCTGGCGCGGCTGCTTCGCGGAGCCGCCTTGGCCGGCCCGGGCCCGGGGCTGCGC
GCCGCCGGCTTCAGCCGCAGCTTCAGCTCGGACTCGGGCTCCAGCCCGGCGTCCGAGCGC
GGCGTTCCGGGCCAGGTGGACTTCTACGCGCGCTTCTCGCCGTCCCCGCTCTCCATGAAG
CAGTTCCTGGACTTCGGATCAGTGAATGCTTGTGAAAAGACCTCATTTATGTTTCTGCGG
CAAGAGTTGCCTGTCAGACTGGCAAATATAATGAAAGAAATAAGTCTCCTTCCAGATAAT
CTTCTCAGGACACCATCCGTTCAATTGGTACAAAGCTGGTATATCCAGAGTCTTCAGGAG
CTTCTTGATTTTAAGGACAAAAGTGCTGAGGATGCTAAAGCTATTTATGACTTTACAGAT
ACTGTGATACGGATCAGAAACCGACACAATGATGTCATTCCCACAATGGCCCAGGGTGTG
ATTGAATACAAGGAGAGCTTTGGGGTGGATCCTGTCACCAGCCAGAATGTTCAGTACTTT
TTGGATCGATTCTACATGAGTCGCATTTCAATTAGAATGTTACTCAATCAGCACTCTTTA
TTGTTTGGTGGAAAAGGCAAAGGAAGTCCATCTCATCGAAAACACATTGGAAGCATAAAT
CCAAACTGCAATGTACTTGAAGTTATTAAAGATGGCTATGAAAATGCTAGGCGTCTGTGT
GATTTGTATTATATTAACTCTCCCGAACTAGAACTTGAAGAACTAAATGCAAAATCACCA
GGACAGCCAATACAAGTGGTTTATGTACCATCCCATCTCTATCACATGGTGTTTGAACTT
TTCAAGAATGCAATGAGAGCCACTATGGAACACCATGCCAACAGAGGTGTTTACCCCCCT
ATTCAAGTTCATGTCACGCTGGGTAATGAGGATTTGACTGTGAAGATGAGTGACCGAGGA
GGTGGCGTTCCTTTGAGGAAAATTGACAGACTTTTCAACTACATGTATTCAACTGCACCA
AGACCTCGTGTTGAGACCTCCCGCGCAGTGCCTCTGGCTGGTTTTGGTTATGGATTGCCC
ATATCACGTCTTTACGCACAATACTTCCAAGGAGACCTGAAGCTGTATTCCCTAGAGGGT
TACGGGACAGATGCAGTTATCTACATTAAGGCTCTGTCAACAGACTCAATAGAAAGACTC
CCAGTGTATAACAAAGCTGCCTGGAAGCATTACAACACCAACCACGAGGCTGATGACTGG
TGCGTCCCCAGCAGAGAACCCAAAGACATGACGACGTTCCGCAGTGCCTAG
|
| Enzyme 124 GenBank Gene ID |
L42450 |
| Enzyme 124 GeneCard ID |
PDK1 |
| Enzyme 124 GenAtlas ID |
PDK1 |
| Enzyme 124 HGNC ID |
HGNC:8809 |
| Enzyme 124 Chromosome Location |
2 |
| Enzyme 124 Locus |
2q31.1 |
| Enzyme 124 SNPs |
SNPJam Report |
| Enzyme 124 General References |
- Gudi R, Bowker-Kinley MM, Kedishvili NY, Zhao Y, Popov KM: Diversity of the pyruvate dehydrogenase kinase gene family in humans. J Biol Chem. 1995 Dec 1;270(48):28989-94. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Kato M, Li J, Chuang JL, Chuang DT: Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol. Structure. 2007 Aug;15(8):992-1004. Epub 2007 Aug 2. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 124 Metabolite References |
Not Available |
|
Enzyme 125
[top]
|
| Enzyme 125 ID |
6469 |
| Enzyme 125 Name |
Cell division protein kinase 10 |
| Enzyme 125 Synonyms |
- Serine/threonine-protein kinase PISSLRE
|
| Enzyme 125 Gene Name |
CDK10 |
| Enzyme 125 Protein Sequence |
>Cell division protein kinase 10
MAEPDLECEQIRLKCIRKEGFFTVPPEHRLGRCRSVKEFEKLNRIGEGTYGIVYRARDTQ
TDEIVALKKVRMDKEKDGIPISSLREITLLLRLRHPNIVELKEVVVGNHLESIFLVMGYC
EQDLASLLENMPTPFSEAQVKCIVLQVLRGLQYLHRNFIIHRDLKVSNLLMTDKGCVKTA
DFGLARAYGVPVKPMTPKVVTLWYRAPELLLGTTTQTTSIDMWAVGCILAELLAHRPLLP
GTSEIHQIDLIVQLLGTPSENIWPGFSKLPLVGQYSLRKQPYNNLKHKFPWLSEAGLRLL
HFLFMYDPKKRATAGDCLESSYFKEKPLPCEPELMPTFPHHRNKRAAPATSEGQSKRCKP
|
| Enzyme 125 Number of Residues |
360 |
| Enzyme 125 Molecular Weight |
41037.7 |
| Enzyme 125 Theoretical pI |
9.08 |
| Enzyme 125 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 125 General Function |
Involved in protein kinase activity |
| Enzyme 125 Specific Function |
ATP + a protein = ADP + a phosphoprotein |
| Enzyme 125 Pathways |
Not Available |
| Enzyme 125 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 125 Pfam Domain Function |
|
| Enzyme 125 Signals |
|
| Enzyme 125 Transmembrane Regions |
|
| Enzyme 125 Essentiality |
Not Available |
| Enzyme 125 GenBank ID Protein |
148596926 |
| Enzyme 125 UniProtKB/Swiss-Prot ID |
Q15131 |
| Enzyme 125 UniProtKB/Swiss-Prot Entry Name |
CDK10_HUMAN |
| Enzyme 125 PDB ID |
Not Available |
| Enzyme 125 Cellular Location |
Not Available |
| Enzyme 125 Gene Sequence |
>1083 bp
ATGGCGGAGCCAGATCTGGAGTGCGAGCAGATCCGTCTGAAGTGTATTCGTAAGGAGGGC
TTCTTCACGGTGCCTCCGGAACACAGGCTGGGACGATGCCGGAGTGTGAAGGAGTTTGAG
AAGCTGAACCGCATTGGAGAGGGTACCTACGGCATTGTGTATCGGGCCCGGGACACCCAG
ACAGATGAGATTGTCGCACTGAAGAAGGTGCGGATGGACAAGGAGAAGGATGGCATCCCC
ATCAGCAGCTTGCGGGAGATCACGCTGCTGCTCCGCCTGCGTCATCCGAACATCGTGGAG
CTGAAGGAGGTGGTTGTGGGGAACCACCTGGAGAGCATCTTCCTGGTGATGGGTTACTGT
GAGCAGGACCTGGCCAGCCTCCTGGAGAATATGCCAACACCCTTCTCGGAGGCTCAGGTC
AAGTGCATCGTGCTGCAGGTGCTCCGGGGCCTCCAGTATCTGCACAGGAACTTCATTATC
CACAGGGACCTGAAGGTTTCCAACTTGCTCATGACCGACAAGGGTTGTGTGAAGACAGCG
GATTTCGGCCTGGCCCGGGCCTATGGTGTCCCAGTAAAGCCAATGACCCCCAAGGTGGTC
ACTCTCTGGTACCGAGCCCCTGAACTGCTGTTGGGAACCACCACGCAGACCACCAGCATC
GACATGTGGGCTGTGGGCTGCATACTGGCCGAGCTGCTGGCGCACAGGCCTCTTCTCCCC
GGCACTTCCGAGATCCACCAGATCGACTTGATCGTGCAGCTGCTGGGCACGCCCAGTGAG
AACATCTGGCCGGGCTTTTCCAAGCTGCCACTGGTCGGCCAGTACAGCCTCCGGAAGCAG
CCCTACAACAACCTGAAGCACAAGTTCCCATGGCTGTCGGAGGCCGGGCTGCGCCTGCTG
CACTTCCTGTTCATGTACGACCCTAAGAAAAGGGCGACGGCCGGGGACTGCCTGGAGAGC
TCCTATTTCAAGGAGAAGCCCCTACCCTGTGAGCCGGAGCTCATGCCGACCTTTCCCCAC
CACCGCAACAAGCGGGCCGCCCCAGCCACCTCCGAGGGCCAGAGCAAGCGCTGTAAACCC
TGA
|
| Enzyme 125 GenBank Gene ID |
NM_052988.4 |
| Enzyme 125 GeneCard ID |
CDK10 |
| Enzyme 125 GenAtlas ID |
CDK10 |
| Enzyme 125 HGNC ID |
HGNC:1770 |
| Enzyme 125 Chromosome Location |
1 |
| Enzyme 125 Locus |
16q24 |
| Enzyme 125 SNPs |
SNPJam Report |
| Enzyme 125 General References |
- Grana X, Claudio PP, De Luca A, Sang N, Giordano A: PISSLRE, a human novel CDC2-related protein kinase. Oncogene. 1994 Jul;9(7):2097-103. [PubMed ]
- Brambilla R, Draetta G: Molecular cloning of PISSLRE, a novel putative member of the cdk family of protein serine/threonine kinases. Oncogene. 1994 Oct;9(10):3037-41. [PubMed ]
- Crawford J, Ianzano L, Savino M, Whitmore S, Cleton-Jansen AM, Settasatian C, d'apolito M, Seshadri R, Pronk JC, Auerbach AD, Verlander PC, Mathew CG, Tipping AJ, Doggett NA, Zelante L, Callen DF, Savoia A: The PISSLRE gene: structure, exon skipping, and exclusion as tumor suppressor in breast cancer. Genomics. 1999 Feb 15;56(1):90-7. [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 ]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 125 Metabolite References |
Not Available |
|
Enzyme 126
[top]
|
| Enzyme 126 ID |
6470 |
| Enzyme 126 Name |
Serine/threonine-protein kinase Nek1 |
| Enzyme 126 Synonyms |
- Never in mitosis A-related kinase 1
- NimA-related protein kinase 1
- Renal carcinoma antigen NY-REN-55
|
| Enzyme 126 Gene Name |
NEK1 |
| Enzyme 126 Protein Sequence |
>Serine/threonine-protein kinase Nek1
MEKYVRLQKIGEGSFGKAILVKSTEDGRQYVIKEINISRMSSKEREESRREVAVLANMKH
PNIVQYRESFEENGSLYIVMDYCEGGDLFKRINAQKGVLFQEDQILDWFVQICLALKHVH
DRKILHRDIKSQNIFLTKDGTVQLGDFGIARVLNSTVELARTCIGTPYYLSPEICENKPY
NNKSDIWALGCVLYELCTLKHAFEAGSMKNLVLKIISGSFPPVSLHYSYDLRSLVSQLFK
RNPRDRPSVNSILEKGFIAKRIEKFLSPQLIAEEFCLKTFSKFGSQPIPAKRPASGQNSI
SVMPAQKITKPAAKYGIPLAYKKYGDKKLHEKKPLQKHKQAHQTPEKRVNTGEERRKISE
EAARKRRLEFIEKEKKQKDQIISLMKAEQMKRQEKERLERINRAREQGWRNVLSAGGSGE
VKAPFLGSGGTIAPSSFSSRGQYEHYHAIFDQMQQQRAEDNEAKWKREIYGRGLPERGIL
PGVRPGFPYGAAGHHHFPDADDIRKTLKRLKAVSKQANANRQKGQLAVERAKQVEEFLQR
KREAMQNKARAEGHMVYLARLRQIRLQNFNERQQIKAKLRGEKKEANHSEGQEGSEEADM
RRKKIESLKAHANARAAVLKEQLERKRKEAYEREKKVWEEHLVAKGVKSSDVSPPLGQHE
TGGSPSKQQMRSVISVTSALKEVGVDSSLTDTRETSEEMQKTNNAISSKREILRRLNENL
KAQEDEKGKQNLSDTFEINVHEDAKEHEKEKSVSSDRKKWEAGGQLVIPLDELTLDTSFS
TTERHTVGEVIKLGPNGSPRRAWGKSPTDSVLKILGEAELQLQTELLENTTIRSEISPEG
EKYKPLITGEKKVQCISHEINPSAIVDSPVETKSPEFSEASPQMSLKLEGNLEEPDDLET
EILQEPSGTNKDESLPCTITDVWISEEKETKETQSADRITIQENEVSEDGVSSTVDQLSD
IHIEPGTNDSQHSKCDVDKSVQPEPFFHKVVHSEHLNLVPQVQSVQCSPEESFAFRSHSH
LPPKNKNKNSLLIGLSTGLFDANNPKMLRTCSLPDLSKLFRTLMDVPTVGDVRQDNLEID
EIEDENIKEGPSDSEDIVFEETDTDLQELQASMEQLLREQPGEEYSEEEESVLKNSDVEP
TANGTDVADEDDNPSSESALNEEWHSDNSDGEIASECECDSVFNHLEELRLHLEQEMGFE
KFFEVYEKIKAIHEDEDENIEICSKIVQNILGNEHQHLYAKILHLVMADGAYQEDNDE
|
| Enzyme 126 Number of Residues |
1258 |
| Enzyme 126 Molecular Weight |
142827.3 |
| Enzyme 126 Theoretical pI |
5.78 |
| Enzyme 126 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 126 General Function |
Involved in protein kinase activity |
| Enzyme 126 Specific Function |
Phosphorylates serines and threonines, but also appears to possess tyrosine kinase activity. Implicated in the control of meiosis |
| Enzyme 126 Pathways |
Not Available |
| Enzyme 126 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 126 Pfam Domain Function |
|
| Enzyme 126 Signals |
|
| Enzyme 126 Transmembrane Regions |
|
| Enzyme 126 Essentiality |
Not Available |
| Enzyme 126 GenBank ID Protein |
41872673 |
| Enzyme 126 UniProtKB/Swiss-Prot ID |
Q96PY6 |
| Enzyme 126 UniProtKB/Swiss-Prot Entry Name |
NEK1_HUMAN |
| Enzyme 126 PDB ID |
Not Available |
| Enzyme 126 Cellular Location |
Not Available |
| Enzyme 126 Gene Sequence |
>3777 bp
ATGGAGAAGTATGTTAGACTACAGAAGATTGGAGAAGGTTCATTTGGAAAAGCCATTCTT
GTTAAATCTACAGAAGATGGCAGACAGTATGTTATCAAGGAAATTAACATCTCAAGAATG
TCCAGTAAAGAAAGAGAAGAATCAAGGAGAGAAGTTGCAGTATTGGCAAACATGAAGCAT
CCAAATATTGTCCAGTATAGAGAATCATTTGAAGAAAATGGCTCTCTCTACATAGTAATG
GATTACTGTGAGGGAGGGGATCTGTTTAAGCGAATAAATGCTCAGAAAGGCGTTTTGTTT
CAAGAGGATCAGATTTTGGACTGGTTTGTACAGATATGTTTGGCCCTGAAACATGTACAT
GATAGAAAAATTCTTCATCGAGACATTAAATCTCAGAACATATTTTTAACTAAAGATGGA
ACAGTACAACTTGGAGATTTTGGAATTGCTAGAGTTCTTAATAGTACTGTAGAGCTGGCT
CGAACTTGCATAGGGACCCCATACTACTTGTCACCTGAAATCTGTGAAAACAAACCTTAC
AATAATAAAAGTGACATTTGGGCTCTGGGGTGTGTCCTTTATGAGCTGTGTACACTTAAA
CATGCTTTTGAAGCTGGCAGTATGAAAAACCTGGTACTGAAGATAATATCTGGATCTTTT
CCACCTGTGTCTTTGCATTATTCCTATGATCTCCGCAGTTTGGTGTCTCAGTTATTTAAA
AGAAATCCTAGGGATAGACCATCAGTCAACTCCATATTGGAGAAAGGTTTTATAGCCAAA
CGCATTGAAAAGTTTCTCTCTCCTCAGCTTATTGCAGAAGAATTTTGTCTAAAAACATTT
TCGAAGTTTGGATCACAGCCTATACCAGCTAAAAGACCAGCTTCAGGACAAAACTCGATT
TCTGTTATGCCTGCTCAGAAAATTACAAAGCCTGCCGCTAAATATGGAATACCTTTAGCA
TATAAGAAATATGGAGATAAAAAATTACACGAAAAGAAACCACTGCAAAAACATAAACAG
GCCCATCAAACTCCAGAGAAGAGAGTGAATACTGGAGAAGAAAGGAGGAAAATATCTGAG
GAAGCAGCAAGAAAGAGAAGGCTGGAATTTATTGAAAAAGAAAAGAAACAAAAGGATCAG
ATTATTAGTTTAATGAAGGCTGAACAAATGAAAAGGCAAGAAAAGGAAAGGTTGGAAAGA
ATAAATAGGGCCAGGGAACAAGGATGGAGAAATGTGCTAAGTGCTGGTGGAAGTGGTGAA
GTAAAGGCTCCTTTTCTGGGCAGTGGAGGGACTATAGCTCCATCATCTTTTTCTTCTCGA
GGACAGTATGAACATTACCATGCCATTTTTGACCAAATGCAGCAACAAAGAGCAGAAGAT
AATGAAGCTAAATGGAAAAGAGAAATATATGGTCGAGGTCTTCCAGAAAGAGGAATTCTG
CCTGGAGTTCGTCCAGGATTTCCTTATGGGGCTGCAGGTCATCACCATTTTCCTGATGCT
GATGATATTAGAAAAACTTTGAAAAGATTGAAGGCGGTGTCTAAACAAGCCAATGCAAAC
AGGCAAAAAGGGCAGCTAGCTGTAGAAAGAGCTAAACAAGTAGAAGAGTTCCTGCAGCGA
AAACGGGAAGCTATGCAGAATAAAGCTCGAGCCGAAGGACATATGGTTTATCTGGCAAGA
CTGAGGCAAATAAGACTACAGAATTTCAATGAGCGCCAACAGATTAAAGCCAAACTTCGT
GGTGAAAAGAAAGAAGCTAATCATTCTGAAGGACAAGAAGGAAGTGAAGAGGCTGACATG
AGGCGCAAAAAAATCGAATCACTGAAGGCCCATGCAAATGCACGTGCTGCTGTACTAAAA
GAACAACTAGAACGAAAGAGAAAGGAGGCTTATGAGAGAGAAAAAAAAGTGTGGGAAGAG
CATTTGGTGGCTAAAGGAGTTAAGAGTTCTGATGTTTCTCCACCTTTGGGACAGCATGAA
ACAGGTGGCTCTCCATCAAAGCAACAGATGAGATCTGTTATTTCTGTAACTTCAGCTTTG
AAAGAAGTTGGCGTGGACAGTAGTTTAACTGATACCCGGGAAACTTCAGAAGAGATGCAA
AAGACCAACAATGCTATTTCAAGTAAGCGAGAAATACTTCGTAGATTAAATGAAAATCTT
AAAGCTCAAGAAGATGAAAAAGGAAAGCAGAATCTCTCTGATACTTTTGAGATAAATGTT
CATGAAGATGCCAAAGAGCATGAAAAAGAAAAATCAGTTTCATCTGATCGCAAGAAGTGG
GAGGCAGGAGGTCAACTTGTGATTCCTCTGGATGAGTTAACACTAGATACATCCTTCTCT
ACAACTGAAAGACATACAGTGGGAGAAGTTATTAAATTAGGTCCTAATGGATCTCCAAGA
AGAGCCTGGGGGAAAAGTCCGACAGATTCTGTTCTAAAGATACTTGGAGAAGCTGAACTA
CAACTTCAGACAGAACTATTAGAAAATACAACTATTAGAAGTGAGATTTCTCCCGAAGGG
GAAAAGTACAAACCCTTAATTACTGGAGAAAAAAAAGTACAATGTATTTCACATGAAATA
AACCCATCAGCTATTGTTGATTCTCCTGTTGAGACAAAAAGTCCCGAGTTCAGTGAGGCA
TCTCCACAGATGTCATTGAAACTGGAAGGAAATTTAGAAGAACCTGATGATTTGGAAACA
GAAATTCTACAAGAGCCAAGTGGAACAAACAAAGATGAGAGCTTGCCATGCACTATTACT
GATGTGTGGATTAGTGAGGAAAAAGAAACAAAGGAAACTCAGTCGGCAGATAGGATCACC
ATTCAGGAAAATGAAGTTTCTGAAGATGGAGTCTCGAGTACTGTGGACCAACTTAGTGAC
ATTCATATAGAGCCTGGAACCAATGATTCTCAGCACTCTAAATGTGATGTAGATAAGTCT
GTGCAACCGGAACCATTTTTCCATAAGGTGGTTCATTCTGAACACTTGAACTTAGTCCCT
CAAGTTCAATCAGTTCAGTGTTCACCAGAAGAATCCTTTGCATTTCGATCTCACTCGCAT
TTACCACCAAAAAATAAAAACAAGAATTCCTTGCTGATTGGACTTTCAACTGGTCTGTTT
GATGCAAACAACCCAAAGATGTTAAGGACATGTTCACTTCCAGATCTCTCAAAGCTGTTC
AGAACCCTTATGGATGTTCCCACCGTAGGAGATGTTCGTCAAGACAATCTTGAAATAGAT
GAAATTGAAGATGAAAACATTAAAGAAGGACCTTCTGATTCTGAAGACATTGTGTTTGAA
GAAACTGACACAGATTTACAAGAGCTGCAGGCCTCGATGGAACAGTTACTTAGGGAACAA
CCTGGTGAAGAATACAGTGAAGAAGAAGAGTCAGTCTTGAAGAACAGTGATGTGGAGCCA
ACTGCAAATGGGACAGATGTGGCAGATGAAGATGACAATCCCAGCAGTGAAAGTGCCCTG
AACGAAGAATGGCACTCAGATAACAGTGATGGTGAAATTGCTAGTGAATGTGAATGCGAT
AGTGTCTTTAACCATTTAGAGGAACTGAGACTTCATCTGGAGCAGGAAATGGGCTTTGAA
AAATTCTTTGAGGTTTATGAGAAAATAAAGGCTATTCATGAAGATGAAGATGAAAATATT
GAAATTTGTTCAAAAATAGTTCAAAATATTTTGGGAAATGAACATCAGCATCTTTATGCC
AAGATTCTTCATTTAGTCATGGCAGATGGAGCCTACCAAGAAGATAATGATGAATAA
|
| Enzyme 126 GenBank Gene ID |
NM_012224.1 |
| Enzyme 126 GeneCard ID |
NEK1 |
| Enzyme 126 GenAtlas ID |
NEK1 |
| Enzyme 126 HGNC ID |
HGNC:7744 |
| Enzyme 126 Chromosome Location |
4 |
| Enzyme 126 Locus |
4q33 |
| Enzyme 126 SNPs |
SNPJam Report |
| Enzyme 126 General References |
- Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins. DNA Res. 2001 Aug 31;8(4):179-87. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- 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 ]
- Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed ]
- 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 ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed ]
|
| Enzyme 126 Metabolite References |
Not Available |
|
Enzyme 127
[top]
|
| Enzyme 127 ID |
6471 |
| Enzyme 127 Name |
Activin receptor type-1 |
| Enzyme 127 Synonyms |
- Activin receptor type I
- ACTR-I
- Activin receptor-like kinase 2
- ALK-2
- Serine/threonine-protein kinase receptor R1
- SKR1
- TGF-B superfamily receptor type I
- TSR-I
|
| Enzyme 127 Gene Name |
ACVR1 |
| Enzyme 127 Protein Sequence |
>Activin receptor type-1
MVDGVMILPVLIMIALPSPSMEDEKPKVNPKLYMCVCEGLSCGNEDHCEGQQCFSSLSIN
DGFHVYQKGCFQVYEQGKMTCKTPPSPGQAVECCQGDWCNRNITAQLPTKGKSFPGTQNF
HLEVGLIILSVVFAVCLLACLLGVALRKFKRRNQERLNPRDVEYGTIEGLITTNVGDSTL
ADLLDHSCTSGSGSGLPFLVQRTVARQITLLECVGKGRYGEVWRGSWQGENVAVKIFSSR
DEKSWFRETELYNTVMLRHENILGFIASDMTSRHSSTQLWLITHYHEMGSLYDYLQLTTL
DTVSCLRIVLSIASGLAHLHIEIFGTQGKPAIAHRDLKSKNILVKKNGQCCIADLGLAVM
HSQSTNQLDVGNNPRVGTKRYMAPEVLDETIQVDCFDSYKRVDIWAFGLVLWEVARRMVS
NGIVEDYKPPFYDVVPNDPSFEDMRKVVCVDQQRPNIPNRWFSDPTLTSLAKLMKECWYQ
NPSARLTALRIKKTLTKIDNSLDKLKTDC
|
| Enzyme 127 Number of Residues |
509 |
| Enzyme 127 Molecular Weight |
57152.4 |
| Enzyme 127 Theoretical pI |
7.36 |
| Enzyme 127 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- receptor signaling protein serine/threonine kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transforming growth factor beta receptor activity
- transmembrane receptor protein serine/threonine kinase activity
|
| Process |
- cell surface receptor linked signaling pathway
- cellular metabolic process
- enzyme linked receptor protein signaling pathway
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- signaling
- signaling pathway
- transmembrane receptor protein serine/threonine kinase signaling pathway
|
| Component |
|
|
| Enzyme 127 General Function |
Involved in receptor signaling protein serine/threonine kinase activity |
| Enzyme 127 Specific Function |
On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis |
| Enzyme 127 Pathways |
Not Available |
| Enzyme 127 Reactions |
- ATP + [receptor-protein] = ADP + [receptor-protein] phosphate
|
| Enzyme 127 Pfam Domain Function |
|
| Enzyme 127 Signals |
|
| Enzyme 127 Transmembrane Regions |
|
| Enzyme 127 Essentiality |
Not Available |
| Enzyme 127 GenBank ID Protein |
Not Available |
| Enzyme 127 UniProtKB/Swiss-Prot ID |
Q04771 |
| Enzyme 127 UniProtKB/Swiss-Prot Entry Name |
ACVR1_HUMAN |
| Enzyme 127 PDB ID |
Not Available |
| Enzyme 127 Cellular Location |
Not Available |
| Enzyme 127 Gene Sequence |
>1530 bp
ATGGTAGATGGAGTGATGATTCTTCCTGTGCTTATCATGATTGCTCTCCCCTCCCCTAGT
ATGGAAGATGAGAAGCCCAAGGTCAACCCCAAACTCTACATGTGTGTGTGTGAAGGTCTC
TCCTGCGGTAATGAGGACCACTGTGAAGGCCAGCAGTGCTTTTCCTCACTGAGCATCAAC
GATGGCTTCCACGTCTACCAGAAAGGCTGCTTCCAGGTTTATGAGCAGGGAAAGATGACC
TGTAAGACCCCGCCGTCCCCTGGCCAAGCCGTGGAGTGCTGCCAAGGGGACTGGTGTAAC
AGGAACATCACGGCCCAGCTGCCCACTAAAGGAAAATCCTTCCCTGGAACACAGAATTTC
CACTTGGAGGTTGGCCTCATTATTCTCTCTGTAGTGTTCGCAGTATGTCTTTTAGCCTGC
CTGCTGGGAGTTGCTCTCCGAAAATTTAAAAGGCGCAACCAAGAACGCCTCAATCCCCGA
GACGTGGAGTATGGCACTATCGAAGGGCTCATCACCACCAATGTTGGAGACAGCACTTTA
GCAGATTTATTGGATCATTCGTGTACATCAGGAAGTGGCTCTGGTCTTCCTTTTCTGGTA
CAAAGAACAGTGGCTCGCCAGATTACACTGTTGGAGTGTGTCGGGAAAGGCAGGTATGGT
GAGGTGTGGAGGGGCAGCTGGCAAGGGGAAAATGTTGCCGTGAAGATCTTCTCCTCCCGT
GATGAGAAGTCATGGTTCAGGGAAACGGAATTGTACAACACTGTGATGCTGAGGCATGAA
AATATCTTAGGTTTCATTGCTTCAGACATGACATCAAGACACTCCAGTACCCAGCTGTGG
TTAATTACACATTATCATGAAATGGGATCGTTGTACGACTATCTTCAGCTTACTACTCTG
GATACAGTTAGCTGCCTTCGAATAGTGCTGTCCATAGCTAGTGGTCTTGCACATTTGCAC
ATAGAGATATTTGGGACCCAAGGGAAACCAGCCATTGCCCATCGAGATTTAAAGAGCAAA
AATATTCTGGTTAAGAAGAATGGACAGTGTTGCATAGCAGATTTGGGCCTGGCAGTCATG
CATTCCCAGAGCACCAATCAGCTTGATGTGGGGAACAATCCCCGTGTGGGCACCAAGCGC
TACATGGCCCCCGAAGTTCTAGATGAAACCATCCAGGTGGATTGTTTCGATTCTTATAAA
AGGGTCGATATTTGGGCCTTTGGACTTGTTTTGTGGGAAGTGGCCAGGCGGATGGTGAGC
AATGGTATAGTGGAGGATTACAAGCCACCGTTCTACGATGTGGTTCCCAATGACCCAAGT
TTTGAAGATATGAGGAAGGTAGTCTGTGTGGATCAACAAAGGCCAAACATACCCAACAGA
TGGTTCTCAGACCCGACATTAACCTCTCTGGCCAAGCTAATGAAAGAATGCTGGTATCAA
AATCCATCCGCAAGACTCACAGCACTGCGTATCAAAAAGACTTTGACCAAAATTGATAAT
TCCCTCGACAAATTGAAAACTGACTGTTGA
|
| Enzyme 127 GenBank Gene ID |
L02911 |
| Enzyme 127 GeneCard ID |
ACVR1 |
| Enzyme 127 GenAtlas ID |
ACVR1 |
| Enzyme 127 HGNC ID |
HGNC:171 |
| Enzyme 127 Chromosome Location |
2 |
| Enzyme 127 Locus |
2q23-q24 |
| Enzyme 127 SNPs |
SNPJam Report |
| Enzyme 127 General References |
- Matsuzaki K, Xu J, Wang F, McKeehan WL, Krummen L, Kan M: A widely expressed transmembrane serine/threonine kinase that does not bind activin, inhibin, transforming growth factor beta, or bone morphogenic factor. J Biol Chem. 1993 Jun 15;268(17):12719-23. [PubMed ]
- ten Dijke P, Ichijo H, Franzen P, Schulz P, Saras J, Toyoshima H, Heldin CH, Miyazono K: Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity. Oncogene. 1993 Oct;8(10):2879-87. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
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