|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5429 |
| Enzyme 1 Name |
Glycerol-3-phosphate dehydrogenase, mitochondrial |
| Enzyme 1 Synonyms |
- GPD-M
- GPDH-M
- mtGPD
|
| Enzyme 1 Gene Name |
GPD2 |
| Enzyme 1 Protein Sequence |
>Glycerol-3-phosphate dehydrogenase, mitochondrial
MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADCISEPVNREPPSREAQ
LLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVR
YLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLY
DLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYG
AATANYMEVVSLLKKTDPQTGKVRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKM
DDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTD
VTHHPIPSEEDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNH
VVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLY
IRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVGVRLVSEFPYIEAEVKYG
IKEYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFLY
YEMGYKSRSEQLTDRSEISLLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMD
ENTLHEILNEVDLNKNGQVELNEFLQLMSAIQKGRVSGSRLAILMKTAEENLDRRVPIPV
DRSCGGL
|
| Enzyme 1 Number of Residues |
727 |
| Enzyme 1 Molecular Weight |
80852.0 |
| Enzyme 1 Theoretical pI |
7.77 |
| Enzyme 1 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- glycerol-3-phosphate dehydrogenase activity
- ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor
|
| Process |
- alcohol metabolic process
- alditol metabolic process
- glycerol metabolic process
- glycerol-3-phosphate metabolic process
- metabolic process
- oxidation reduction
- polyol metabolic process
- small molecule metabolic process
|
| Component |
- glycerol-3-phosphate dehydrogenase complex
- macromolecular complex
- protein complex
|
|
| Enzyme 1 General Function |
Involved in calcium ion binding |
| Enzyme 1 Specific Function |
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol [RN:R00849]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
285002233  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P43304  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
GPDM_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>2184 bp
ATGGCATTTCAAAAGGCAGTGAAAGGGACGATTCTTGTTGGAGGAGGTGCTCTTGCAACT
GTTTTAGGACTTTCTCAGTTTGCTCATTACAGAAGGAAACAAATGAACCTGGCCTATGTT
AAAGCAGCAGACTGCATTTCAGAACCAGTTAACAGGGAGCCTCCTTCCAGAGAAGCTCAG
CTACTGACTTTGCAAAACACATCTGAATTTGATATCCTTGTTATTGGAGGAGGAGCAACA
GGAAGTGGCTGTGCGCTAGATGCTGTCACCAGAGGACTAAAAACAGCCCTTGTAGAAAGA
GATGATTTCTCATCAGGGACCAGCAGCAGAAGCACTAAATTGATCCATGGTGGTGTGAGA
TATCTGCAGAAGGCCATCATGAAGTTGGATATTGAGCAGTATAGGATGGTAAAAGAAGCC
CTTCATGAGCGTGCCAACCTGCTAGAAATTGCTCCCCATTTATCAGCTCCATTGCCTATA
ATGCTTCCAGTTTACAAGTGGTGGCAGTTACCTTACTACTGGGTAGGAATCAAGCTGTAT
GATTTGGTTGCAGGAAGCAATTGCCTAAAAAGCAGTTATGTCCTCAGCAAATCAAGAGCC
CTTGAACATTTCCCAATGCTCCAGAAGGACAAACTGGTAGGAGCAATTGTCTACTATGAC
GGACAACATAACGATGCACGGATGAACCTTGCCATTGCTCTGACTGCTGCCAGGTATGGG
GCTGCCACAGCCAATTACATGGAGGTAGTGAGCTTGCTCAAGAAGACAGACCCCCAGACA
GGGAAAGTGCGTGTGAGCGGCGCACGGTGCAAGGATGTCCTCACAGGGCAGGAATTTGAC
GTGAGAGCCAAATGTGTTATCAATGCCACGGGACCTTTCACGGACTCTGTGCGCAAAATG
GATGATAAAGACGCAGCAGCTATCTGCCAGCCAAGTGCTGGTGTCCATATTGTGATGCCT
GGTTATTACAGCCCAGAGAGCATGGGACTTCTTGACCCAGCGACCAGTGATGGGCGAGTT
ATTTTCTTCTTACCCTGGCAAAAGATGACGATCGCTGGCACTACTGATACTCCAACTGAT
GTTACACACCATCCAATTCCTTCAGAAGAAGATATCAACTTCATTTTGAATGAAGTGCGT
AATTACCTGAGTTGTGATGTTGAAGTGAGAAGAGGGGATGTCCTGGCAGCATGGAGTGGA
ATCCGTCCTCTTGTTACAGACCCCAAATCTGCAGATACTCAGTCTATCTCCCGAAATCAT
GTTGTTGATATCAGTGAGAGTGGCCTTATTACTATAGCAGGTGGAAAGTGGACAACTTAT
CGGTCTATGGCAGAAGATACCATAAATGCTGCTGTCAAAACTCATAATTTAAAAGCAGGA
CCAAGTAGAACAGTTGGGCTTTTCCTTCAAGGGGGTAAAGATTGGAGCCCCACACTCTAC
ATTAGGCTTGTGCAGGATTATGGACTTGAAAGCGAGGTGGCACAGCATCTTGCCGCCACC
TATGGTGATAAGGCCTTTGAGGTGGCCAAAATGGCAAGTGTGACTGGCAAAAGGTGGCCT
ATTGTTGGAGTACGTCTTGTGTCAGAATTTCCATATATTGAAGCAGAGGTGAAATATGGG
ATTAAGGAGTATGCCTGCACTGCTGTGGATATGATTTCACGTCGTACTCGCCTGGCCTTT
CTAAATGTCCAGGCAGCAGAGGAAGCCCTACCCAGGATTGTTGAACTGATGGGCAGGGAA
CTGAATTGGGATGATTATAAGAAGCAGGAACAACTTGAAACAGCCAGGAAGTTTCTATAT
TATGAAATGGGCTATAAATCTCGATCAGAACAGTTAACAGATCGCTCTGAAATTAGCCTA
CTGCCTTCAGACATTGACAGGTATAAGAAGAGATTTCATAAGTTTGATGCAGACCAGAAA
GGCTTTATTACCATTGTTGATGTTCAGCGTGTATTAGAGAGTATCAATGTCCAAATGGAT
GAAAATACACTCCATGAAATTCTAAATGAAGTTGATTTGAATAAAAATGGACAGGTTGAA
CTCAATGAATTTTTGCAGCTGATGAGTGCTATTCAAAAAGGAAGGGTATCTGGAAGCCGG
CTTGCTATACTAATGAAAACTGCAGAAGAGAACCTCGACAGAAGAGTTCCAATTCCAGTG
GACCGTAGTTGTGGAGGATTGTGA
|
| Enzyme 1 GenBank Gene ID |
NM_000408.4  |
| Enzyme 1 GeneCard ID |
GPD2  |
| Enzyme 1 GenAtlas ID |
GPD2  |
| Enzyme 1 HGNC ID |
HGNC:4456  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
2q24.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Lehn DA, Brown LJ, Simonson GD, Moran SM, MacDonald MJ: The sequence of a human mitochondrial glycerol-3-phosphate dehydrogenase-encoding cDNA. Gene. 1994 Dec 15;150(2):417-8. [PubMed
]
- Ferrer J, Aoki M, Behn P, Nestorowicz A, Riggs A, Permutt MA: Mitochondrial glycerol-3-phosphate dehydrogenase. Cloning of an alternatively spliced human islet-cell cDNA, tissue distribution, physical mapping, and identification of a polymorphic genetic marker. Diabetes. 1996 Feb;45(2):262-6. [PubMed
]
- Brown LJ, Stoffel M, Moran SM, Fernald AA, Lehn DA, LeBeau MM, MacDonald MJ: Structural organization and mapping of the human mitochondrial glycerol phosphate dehydrogenase-encoding gene and pseudogene. Gene. 1996 Jun 26;172(2):309-12. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [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 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6116 |
| Enzyme 2 Name |
Glycerol kinase 2 |
| Enzyme 2 Synonyms |
- GK 2
- Glycerokinase 2
- ATP:glycerol 3-phosphotransferase 2
- Glycerol kinase, testis specific 2
|
| Enzyme 2 Gene Name |
GK2 |
| Enzyme 2 Protein Sequence |
>Glycerol kinase 2
MAAPKTAAVGPLVGAVVQGTNSTRFLVFNSKTAELLSHHKVELTQEFPKEGWVEQDPKEI
LQSVYECIARTCEKLDELNIDISNIKAVGVSNQRETTVIWDKLTGEPLYNAVVWLDLRTQ
TTVEDLSKKIPGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVEEGRALFGTIDS
WLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIY
GLIKTGALEGVPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGL
LTTVAYKLGREKPAYYALEGSVAIAGAVIRWLRDNLGIIETSGDIERLAKEVGTSYGCYF
VPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEAMNRDCGIPLR
HLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTALGAAMAAGAAEGVSVWSLEPQALS
VLRMERFEPQIQATESEIRYATWKKAVMKSMGWVTSQSPEGGDPSIFSSLPLGFFIVSSM
VMLIGARYISGVP
|
| Enzyme 2 Number of Residues |
553 |
| Enzyme 2 Molecular Weight |
60593.3 |
| Enzyme 2 Theoretical pI |
5.53 |
| Enzyme 2 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 2 General Function |
Involved in phosphotransferase activity, alcohol group as acceptor |
| Enzyme 2 Specific Function |
Key enzyme in the regulation of glycerol uptake and metabolism |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ATP + glycerol = ADP + sn-glycerol 3-phosphate [RN:R00847]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
158257914  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q14410  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
GLPK2_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 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 2 GenBank Gene ID |
AK292241  |
| Enzyme 2 GeneCard ID |
GK2  |
| Enzyme 2 GenAtlas ID |
GK2  |
| Enzyme 2 HGNC ID |
HGNC:4291  |
| Enzyme 2 Chromosome Location |
4 |
| Enzyme 2 Locus |
4q13 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6117 |
| Enzyme 3 Name |
Glycerol kinase |
| Enzyme 3 Synonyms |
- GK
- Glycerokinase
- ATP:glycerol 3-phosphotransferase
|
| Enzyme 3 Gene Name |
GK |
| Enzyme 3 Protein Sequence |
>Glycerol kinase
MAASKKAVLGPLVGAVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEI
LHSVYECIEKTCEKLGQLNIDISNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQ
STVESLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDS
WLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIY
GLMKISHSVKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCV
FSDHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGT
SYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRD
CGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMAAGAAEGVGVWSL
EPEDLSAVTMERFEPQINAEESEIRYSTWKKAVMKSMGWVTTQSPESGDPSIFCSLPLGF
FIVSSMVMLIGARYISGIP
|
| Enzyme 3 Number of Residues |
559 |
| Enzyme 3 Molecular Weight |
61244.1 |
| Enzyme 3 Theoretical pI |
6.50 |
| Enzyme 3 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 3 General Function |
Involved in phosphotransferase activity, alcohol group as acceptor |
| Enzyme 3 Specific Function |
Key enzyme in the regulation of glycerol uptake and metabolism |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + glycerol = ADP + sn-glycerol 3-phosphate [RN:R00847]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
5834428  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P32189  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
GLPK_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 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 3 GenBank Gene ID |
AJ252550  |
| Enzyme 3 GeneCard ID |
GK  |
| Enzyme 3 GenAtlas ID |
GK  |
| Enzyme 3 HGNC ID |
HGNC:4289  |
| Enzyme 3 Chromosome Location |
Not Available |
| Enzyme 3 Locus |
Not Available |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6118 |
| Enzyme 4 Name |
Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic |
| Enzyme 4 Synonyms |
- GPD-C
- GPDH-C
|
| Enzyme 4 Gene Name |
GPD1 |
| Enzyme 4 Protein Sequence |
>Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic
MASKKVCIVGSGNWGSAIAKIVGGNAAQLAQFDPRVTMWVFEEDIGGKKLTEIINTQHEN
VKYLPGHKLPPNVVAVPDVVQAAEDADILIFVVPHQFIGKICDQLKGHLKANATGISLIK
GVDEGPNGLKLISEVIGERLGIPMSVLMGANIASEVADEKFCETTIGCKDPAQGQLLKEL
MQTPNFRITVVQEVDTVEICGALKNVVAVGAGFCDGLGFGDNTKAAVIRLGLMEMIAFAK
LFCSGPVSSATFLESCGVADLITTCYGGRNRKVAEAFARTGKSIEQLEKELLNGQKLQGP
ETARELYSILQHKGLVDKFPLFMAVYKVCYEGQPVGEFIHCLQNHPEHM
|
| Enzyme 4 Number of Residues |
349 |
| Enzyme 4 Molecular Weight |
37567.4 |
| Enzyme 4 Theoretical pI |
6.10 |
| Enzyme 4 GO Classification |
| Function |
- NAD or NADH binding
- binding
- catalytic activity
- coenzyme binding
- cofactor binding
- glycerol-3-phosphate dehydrogenase [NAD+] activity
- glycerol-3-phosphate dehydrogenase [NAD+] activity
- identical protein binding
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
- protein binding
- protein homodimerization activity
|
| Process |
- alcohol metabolic process
- alditol metabolic process
- carbohydrate metabolic process
- glycerol metabolic process
- glycerol-3-phosphate catabolic process
- glycerol-3-phosphate metabolic process
- metabolic process
- oxidation reduction
- polyol metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
- cell part
- cytoplasm
- glycerol-3-phosphate dehydrogenase complex
- intracellular part
- macromolecular complex
- protein complex
|
|
| Enzyme 4 General Function |
Involved in oxidoreductase activity |
| Enzyme 4 Specific Function |
sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+ [RN:R00842]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
21594877  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P21695  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
GPDA_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1050 bp
ATGGCTAGCAAGAAAGTCTGCATTGTAGGCTCCGGGAACTGGGGCTCAGCCATCGCCAAG
ATCGTGGGTGGCAATGCAGCCCAGCTGGCACAGTTTGACCCACGGGTGACCATGTGGGTA
TTTGAGGAAGACATTGGAGGCAAAAAGCTGACTGAGATCATCAACACGCAGCATGAGAAT
GTCAAATACCTGCCAGGGCACAAGTTGCCCCCAAATGTGGTGGCTGTCCCAGATGTGGTC
CAGGCTGCAGAGGATGCTGACATCCTGATCTTTGTGGTGCCCCATCAGTTCATCGGCAAG
ATCTGTGACCAGCTCAAGGGCCATCTGAAGGCAAACGCCACTGGCATATCTCTTATTAAG
GGGGTAGACGAGGGCCCCAATGGGCTGAAGCTCATCTCGGAAGTGATTGGGGAGCGCCTC
GGCATCCCCATGAGTGTGCTGATGGGGGCCAACATTGCCAGCGAGGTGGCTGATGAGAAG
TTCTGTGAGACAACCATTGGCTGCAAGGACCCGGCCCAGGGACAACTCCTGAAAGAGCTG
ATGCAGACACCAAACTTCCGTATCACAGTGGTGCAAGAGGTGGACACAGTAGAGATCTGT
GGAGCCTTAAAGAATGTAGTGGCCGTGGGGGCTGGCTTCTGTGATGGCCTGGGCTTTGGC
GACAACACCAAGGCGGCAGTGATCCGGCTGGGACTCATGGAGATGATAGCCTTCGCCAAG
CTCTTCTGCAGTGGCCCTGTGTCCTCTGCCACCTTCTTGGAGAGCTGTGGTGTTGCTGAC
CTGATCACTACCTGCTATGGAGGGCGGAACCGGAAAGTGGCTGAGGCCTTTGCGCGTACA
GGAAAGTCCATTGAGCAGCTGGAGAAAGAGTTGCTGAATGGGCAGAAACTGCAGGGGCCC
GAGACAGCCCGGGAGCTATACAGCATCCTCCAGCACAAGGGCCTGGTAGACAAGTTTCCC
TTGTTCATGGCTGTGTACAAGGTGTGCTACGAGGGCCAGCCAGTGGGTGAATTCATCCAC
TGCCTGCAGAATCATCCAGAACATATGTGA
|
| Enzyme 4 GenBank Gene ID |
BC032234  |
| Enzyme 4 GeneCard ID |
GPD1  |
| Enzyme 4 GenAtlas ID |
GPD1  |
| Enzyme 4 HGNC ID |
HGNC:4455  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
12q12-q13 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Menaya J, Gonzalez-Manchon C, Parrilla R, Ayuso MS: Molecular cloning, sequencing and expression of a cDNA encoding a human liver NAD-dependent alpha-glycerol-3-phosphate dehydrogenase. Biochim Biophys Acta. 1995 May 17;1262(1):91-4. [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
]
- Gwynn B, Lyford KA, Birkenmeier EH: Sequence conservation and structural organization of the glycerol-3-phosphate dehydrogenase promoter in mice and humans. Mol Cell Biol. 1990 Oct;10(10):5244-56. [PubMed
]
- Ou X, Ji C, Han X, Zhao X, Li X, Mao Y, Wong LL, Bartlam M, Rao Z: Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1). J Mol Biol. 2006 Mar 31;357(3):858-69. Epub 2006 Jan 18. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6119 |
| Enzyme 5 Name |
Glycerol-3-phosphate acyltransferase 1, mitochondrial |
| Enzyme 5 Synonyms |
- GPAT-1
|
| Enzyme 5 Gene Name |
GPAM |
| Enzyme 5 Protein Sequence |
>Glycerol-3-phosphate acyltransferase 1, mitochondrial
MDESALTLGTIDVSYLPHSSEYSVGRCKHTSEEWGECGFRPTIFRSATLKWKESLMSRKR
PFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDV
HKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKRILQEMVAT
VSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLLFLPVHRSHIDYLLLT
FILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDVLYRALLHGHI
VELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNVIPDILIIPVGISYDRII
EGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSA
LLSLEQALLPAILPSRPSDAADEGRDTSINESRNATDESLRRRLIANLAEHILFTASKSC
AIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLL
GNCVTITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLNKRGLG
GPTSTPPNLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQVCHETVGKFIQYGILTVAE
HDDQEDISPSLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITF
LQRLLGPLLEAYSSAAIFVHNFSGPVPEPEYLQKLHKYLITRTERNVAVYAESATYCLVK
NAVKMFKDIGVFKETKQKRVSVLELSSTFLPQCNRQKLLEYILSFVVL
|
| Enzyme 5 Number of Residues |
828 |
| Enzyme 5 Molecular Weight |
93793.9 |
| Enzyme 5 Theoretical pI |
7.78 |
| Enzyme 5 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in acyltransferase activity |
| Enzyme 5 Specific Function |
Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
190358539  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9HCL2  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
GPAT1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>2487 bp
ATGGATGAATCTGCACTGACCCTTGGTACAATAGATGTTTCTTATCTGCCACATTCATCA
GAATACAGTGTTGGTCGATGTAAGCACACAAGTGAGGAATGGGGTGAGTGTGGCTTTAGA
CCCACCATCTTCAGATCTGCAACTTTAAAATGGAAAGAAAGCCTAATGAGTCGGAAAAGG
CCATTTGTTGGAAGATGTTGTTACTCCTGCACTCCCCAGAGCTGGGACAAATTTTTCAAC
CCCAGTATCCCGTCTTTGGGTTTGCGGAATGTTATTTATATCAATGAAACTCACACAAGA
CACCGCGGATGGCTTGCAAGACGCCTTTCTTACGTTCTTTTTATTCAAGAGCGAGATGTG
CATAAGGGCATGTTTGCCACCAATGTGACTGAAAATGTGCTGAACAGCAGTAGAGTACAA
GAGGCAATTGCAGAAGTGGCTGCTGAATTAAACCCTGATGGTTCTGCCCAGCAGCAATCA
AAAGCCGTTAACAAAGTGAAAAAGAAAGCTAAAAGGATTCTTCAAGAAATGGTTGCCACT
GTCTCACCGGCAATGATCAGACTGACTGGGTGGGTGCTGCTAAAACTGTTCAACAGCTTC
TTTTGGAACATTCAAATTCACAAAGGTCAACTTGAGATGGTTAAAGCTGCAACTGAGACG
AATTTGCCGCTTCTGTTTCTACCAGTTCATAGATCCCATATTGACTATCTGCTGCTCACT
TTCATTCTCTTCTGCCATAACATCAAAGCACCATACATTGCTTCAGGCAATAATCTCAAC
ATCCCAATCTTCAGTACCTTGATCCATAAGCTTGGGGGCTTCTTCATACGACGAAGGCTC
GATGAAACACCAGATGGACGGAAAGATGTTCTCTATAGAGCTTTGCTCCATGGGCATATA
GTTGAATTACTTCGACAGCAGCAATTCTTGGAGATCTTCCTGGAAGGCACACGTTCTAGG
AGTGGAAAAACCTCTTGTGCTCGGGCAGGACTTTTGTCAGTTGTGGTAGATACTCTGTCT
ACCAATGTCATCCCAGACATCTTGATAATACCTGTTGGAATCTCCTATGATCGCATTATC
GAAGGTCACTACAATGGTGAACAACTGGGCAAACCTAAGAAGAATGAGAGCCTGTGGAGT
GTAGCAAGAGGTGTTATTAGAATGTTACGAAAAAACTATGGTTGTGTCCGAGTGGATTTT
GCACAGCCATTTTCCTTAAAGGAATATTTAGAAAGCCAAAGTCAGAAACCGGTGTCTGCT
CTACTTTCCCTGGAGCAAGCGTTGTTACCAGCTATACTTCCTTCAAGACCCAGTGATGCT
GCTGATGAAGGTAGAGACACGTCCATTAATGAGTCCAGAAATGCAACAGATGAATCCCTA
CGAAGGAGGTTGATTGCAAATCTGGCTGAGCATATTCTATTCACTGCTAGCAAGTCCTGT
GCCATTATGTCCACACACATTGTGGCTTGCCTGCTCCTCTACAGACACAGGCAGGGAATT
GATCTCTCCACATTGGTCGAAGACTTCTTTGTGATGAAAGAGGAAGTCCTGGCTCGTGAT
TTTGACCTGGGGTTCTCAGGAAATTCAGAAGATGTAGTAATGCATGCCATACAGCTGCTG
GGAAATTGTGTCACAATCACCCACACTAGCAGGAACGATGAGTTTTTTATCACCCCCAGC
ACAACTGTCCCATCAGTCTTCGAACTCAACTTCTACAGCAATGGGGTACTTCATGTCTTT
ATCATGGAGGCCATCATAGCTTGCAGCCTTTATGCAGTTCTGAACAAGAGGGGACTGGGG
GGTCCCACTAGCACCCCACCTAACCTGATCAGCCAGGAGCAGCTGGTGCGGAAGGCGGCC
AGCCTGTGCTACCTTCTCTCCAATGAAGGCACCATCTCACTGCCTTGCCAGACATTTTAC
CAAGTCTGCCATGAAACAGTAGGAAAGTTTATCCAGTATGGCATTCTTACAGTGGCAGAG
CACGATGACCAGGAAGATATCAGTCCTAGTCTTGCTGAGCAGCAGTGGGACAAGAAGCTT
CCAGAACCTTTGTCTTGGAGAAGTGATGAAGAAGATGAAGACAGTGACTTTGGGGAGGAA
CAGCGAGATTGCTACCTGAAGGTGAGCCAATCCAAGGAGCACCAGCAGTTTATCACCTTC
TTACAGAGACTCCTTGGGCCTTTGCTGGAGGCCTACAGCTCTGCTGCCATCTTTGTTCAC
AACTTCAGTGGTCCTGTTCCAGAACCTGAGTATCTGCAAAAGTTGCACAAATACCTAATA
ACCAGAACAGAAAGAAATGTTGCAGTATATGCTGAGAGTGCCACATATTGTCTTGTGAAG
AATGCTGTGAAAATGTTTAAGGATATTGGGGTTTTCAAGGAGACCAAACAAAAGAGAGTG
TCTGTTTTAGAACTGAGCAGCACTTTTCTACCTCAATGCAACCGACAAAAACTTCTAGAA
TATATTCTGAGTTTTGTGGTGCTGTAG
|
| Enzyme 5 GenBank Gene ID |
NM_020918.4  |
| Enzyme 5 GeneCard ID |
GPAM  |
| Enzyme 5 GenAtlas ID |
GPAM  |
| Enzyme 5 HGNC ID |
HGNC:24865  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
10q25.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- 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
]
- Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Aug 31;7(4):273-81. [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
]
- Chen YQ, Kuo MS, Li S, Bui HH, Peake DA, Sanders PE, Thibodeaux SJ, Chu S, Qian YW, Zhao Y, Bredt DS, Moller DE, Konrad RJ, Beigneux AP, Young SG, Cao G: AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase. J Biol Chem. 2008 Apr 11;283(15):10048-57. Epub 2008 Jan 31. [PubMed
]
- Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
8487 |
| Enzyme 6 Name |
Putative glycerol kinase 3 |
| Enzyme 6 Synonyms |
- GK 3
- Glycerokinase 3
- ATP:glycerol 3-phosphotransferase 3
- Glycerol kinase, testis specific 1
|
| Enzyme 6 Gene Name |
GK3P |
| Enzyme 6 Protein Sequence |
>Putative glycerol kinase 3
MAASKKAVLGPLVGAVDQGTSSTRFLVFNSRTAELLSHHQVEIKQEFPREGWVEQDPKEI
LHSVYECIEKTCEKLGQLNIGISNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQ
STVESLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDS
WLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPHVRSSSEIY
GLMKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGL
LTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYF
VPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLS
HLQVDGGMTSNKILMQLQADILYIPVVKPLMPETTALGAAMAAGAAEGVDVWSLEPEDLS
AVTMERFEPQINAEESEIRYSTWKKAVMKSMGWVTTQSPEGGDPSVFCSLPLGFFIVSSM
AMLIGARYISGIP
|
| Enzyme 6 Number of Residues |
553 |
| Enzyme 6 Molecular Weight |
60597.4 |
| Enzyme 6 Theoretical pI |
6.35 |
| Enzyme 6 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 6 General Function |
Involved in phosphotransferase activity, alcohol group as acceptor |
| Enzyme 6 Specific Function |
Key enzyme in the regulation of glycerol uptake and metabolism |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- ATP + glycerol = ADP + sn-glycerol 3-phosphate [RN:R00847]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
515029  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q14409  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
GLPK3_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1662 bp
ATGGCAGCCTCAAAGAAGGCAGTTTTGGGGCCATTGGTGGGGGCAGTGGACCAAGGCACC
AGTTCCACGCGCTTTTTGGTTTTCAATTCAAGAACAGCTGAACTACTTAGTCATCATCAA
GTGGAAATAAAACAAGAGTTCCCAAGAGAAGGATGGGTGGAACAGGACCCTAAGGAAATT
CTACATTCTGTCTATGAGTGTATAGAGAAAACATGTGAGAAACTTGGACAGCTCAATATT
GGTATTTCCAACATAAAAGCTATTGGTGTCAGCAACCAGAGGGAAACCACCGTAGCCTGG
GACAAGATAACTGGAGAGCCTCTCTACAATGCTGTAGTGTGGCTTGATCTAAGAACACAG
TCTACCGTTGAGAGTCTTAGTAAAAGAATTCCAGGAAATAATAACTTTGTCAAGTCCAAG
ACAGGCCTTCCACTTAGCACTTACTTCAGTGCAGTGAAACTTCGCTGGCTCCTCGACAAT
GTGAGAAAAGTTCAAAAGGCCGTTGAAGAAAAACGAGCTCTTTTTGGGACTATTGATTCA
TGGCTTATTTGGAGTTTGACAGGAGGCGTCAATGGAGGTGTCCACTGTACAGATGTAACA
AATGCAAGTAGGACTATGCTTTTCAACATTCATTCTTTGGAATGGGATAAACAACTCTGT
GAATTTTTTGGAATTCCAATGGAAATTCTTCCACATGTTCGGAGTTCTTCTGAGATCTAT
GGCCTAATGAAAGCGGGGGCCTTGGAAGGTGTGCCAATATCTGGGTGTTTAGGGGACCAG
TCTGCTGCACTGGTGGGACAAATGTGCTTCCAGATTGGACAAGCCAAAAATACGTATGGA
ACAGGATGTTTCTTACTATGTAATACAGGCCATAAGTGTGTATTTTCTGATCATGGCCTT
CTCACCACAGTGGCTTACAAACTTGGCAGAGACAAACCGGTATATTACGCTTTGGAAGGT
TCTGTAGCTATAGCTGGTGCTGTTATTCGCTGGCTAAGAGACAATCTTGGAATTATAAAG
ACCTCAGAAGAAATTGAAAAACTTGCTAAAGAAGTAGGTACTTCTTATGGCTGCTACTTC
GTCCCAGCATTTTCGGGGTTATATGCACCTTATTGGGAGCCCAGCGCAAGAGGGATAATC
TGTGGACTCACTCAATTCACGAATAAATGCCATATTGCTTTTGCTGCATTAGAAGCTGTT
TGTTTCCAAACTCGAGAGATTTTGGATGCCATGAATCGAGACTGTGGAATTCCACTCAGT
CATTTGCAGGTTGATGGAGGAATGACCAGCAACAAAATTCTTATGCAGCTACAAGCAGAC
ATTCTGTATATTCCAGTAGTGAAGCCCTTGATGCCCGAAACCACTGCACTGGGTGCTGCC
ATGGCGGCAGGGGCTGCAGAAGGAGTCGACGTATGGAGTCTTGAACCTGAGGATTTGTCC
GCCGTCACGATGGAGCGGTTTGAACCTCAGATTAATGCTGAGGAAAGTGAAATTCGTTAT
TCTACATGGAAGAAAGCTGTGATGAAGTCAATGGGTTGGGTTACAACTCAATCTCCAGAA
GGTGGTGACCCTAGTGTCTTCTGTAGTCTGCCCTTGGGCTTTTTTATAGTGAGTAGCATG
GCAATGTTAATCGGAGCAAGGTACATCTCAGGTATTCCATAA
|
| Enzyme 6 GenBank Gene ID |
X78711  |
| Enzyme 6 GeneCard ID |
GK3P  |
| Enzyme 6 GenAtlas ID |
GK3P  |
| Enzyme 6 HGNC ID |
HGNC:4292  |
| Enzyme 6 Chromosome Location |
4 |
| Enzyme 6 Locus |
4q32.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 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
]
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
8976 |
| Enzyme 7 Name |
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial |
| Enzyme 7 Synonyms |
- Phosphatidylglycerophosphate synthase 1
- PGP synthase 1
|
| Enzyme 7 Gene Name |
PGS1 |
| Enzyme 7 Protein Sequence |
>CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
MAVAAAAAAGPVFWRRLLGLLPGRPGLAALLGRLSDRLGRNRDRQRRRSPWLLLAPLLSP
AVPQVTSPPCCLCPEGVHRFQWIRNLVPEFGVSSSHVRVLSSPAEFFELMKGQIRVAKRR
VVMASLYLGTGPLEQELVDCLESTLEKSLQAKFPSNLKVSILLDFTRGSRGRKNSRTMLL
PLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDS
YFTNRQDRYVFLQDCAEIADFFTELVDAVGDVSLQLQGDDTVQVVDGMVHPYKGDRAEYC
KAANKRVMDVINSARTRQQMLHAQTFHSNSLLTQEDAAAAGDRRPAPDTWIYPLIQMKPF
EIQIDEIVTETLLTEAERGAKVYLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFG
AKGVAGAIPAAYVHIERQFFSEVCSLGQQERVQLQEYWRRGWTFHAKGLWLYLAGSSLPC
LTLIGSPNFGYRSVHRDLEAQIAIVTENQALQQQLHQEQEQLYLRSGVVSSATFEQPSRQ
VKLWVKMVTPLIKNFF
|
| Enzyme 7 Number of Residues |
556 |
| Enzyme 7 Molecular Weight |
62729.7 |
| Enzyme 7 Theoretical pI |
9.11 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- phosphotransferase activity, for other substituted phosphate groups
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in phosphotransferase activity, for other substituted phosphate groups |
| Enzyme 7 Specific Function |
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
- CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate [RN:R01801]
|
| Enzyme 7 Pfam Domain Function |
Not Available |
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
Not Available |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q32NB8  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PGPS1_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1671 bp
ATGGCGGTGGCGGCGGCAGCTGCGGCGGGACCCGTGTTCTGGAGGCGACTGCTGGGCCTC
CTGCCTGGCCGCCCAGGGCTGGCCGCGCTCCTGGGACGCCTGTCCGACCGCCTCGGCAGG
AACCGGGACCGCCAGCGCAGGAGGTCACCATGGCTGTTATTGGCTCCCTTGCTGTCCCCA
GCTGTTCCCCAGGTCACCTCCCCACCTTGCTGCCTGTGTCCAGAAGGCGTGCACCGGTTC
CAGTGGATCAGAAACCTGGTTCCAGAATTTGGAGTCTCCAGTTCTCACGTTAGGGTGCTT
TCTTCCCCGGCAGAGTTTTTCGAGCTCATGAAGGGGCAGATAAGAGTAGCCAAGAGGCGG
GTCGTGATGGCATCCCTCTACCTGGGGACAGGTCCTTTGGAACAGGAGCTGGTGGACTGC
CTGGAAAGTACTCTAGAAAAGTCACTCCAAGCAAAGTTTCCTTCAAATCTCAAGGTCTCC
ATTCTCTTAGACTTCACGCGGGGCTCACGAGGTCGGAAGAACTCCCGCACAATGCTGCTC
CCACTCCTGCGGAGGTTCCCAGAGCAGGTCCGAGTCTCCCTCTTTCACACGCCGCACCTC
CGTGGGCTGCTTCGGCTCCTCATCCCTGAGCGCTTCAACGAGACCATCGGCCTCCAGCAC
ATTAAGGTGTACCTCTTCGACAACAGCGTCATCTTGAGCGGTGCAAACCTGAGTGACTCC
TACTTCACCAACCGCCAGGACCGCTACGTGTTCCTGCAGGACTGTGCGGAGATTGCCGAC
TTCTTCACGGAGCTGGTGGACGCGGTGGGGGATGTGTCCCTGCAGCTGCAGGGGGACGAC
ACGGTGCAGGTGGTGGATGGGATGGTGCATCCTTACAAAGGGGACCGGGCCGAGTACTGC
AAGGCAGCCAATAAGAGGGTCATGGATGTGATCAACTCAGCCAGGACCCGCCAGCAGATG
CTGCATGCCCAGACCTTCCACAGCAACTCTCTTTTGACCCAGGAAGATGCAGCAGCTGCT
GGGGATCGCAGACCAGCCCCTGACACCTGGATTTATCCGCTGATTCAGATGAAGCCCTTC
GAGATTCAAATCGATGAGATTGTCACTGAGACCCTGTTGACTGAGGCGGAGCGCGGGGCA
AAGGTCTACCTCACCACTGGCTATTTCAACCTGACCCAGGCCTACATGGACCTGGTCTTG
GGCACTCGGGCTGAGTACCAGATCCTGCTGGCCTCACCAGAGGTGAATGGCTTCTTTGGG
GCCAAGGGGGTGGCCGGCGCCATCCCAGCGGCCTATGTGCACATCGAGCGACAGTTCTTC
AGTGAGGTGTGCAGCCTGGGACAGCAGGAGCGGGTCCAGCTTCAGGAGTACTGGCGGAGG
GGCTGGACGTTCCACGCCAAAGGCCTCTGGCTGTACCTGGCAGGGAGCAGCCTGCCCTGT
CTCACGCTGATTGGCTCTCCTAATTTTGGGTACAGGTCAGTTCACCGGGACCTGGAGGCC
CAGATTGCGATCGTGACGGAGAACCAGGCCCTGCAGCAGCAGCTTCACCAGGAGCAAGAG
CAGCTCTACCTGAGGTCAGGTGTGGTGTCCTCTGCCACCTTCGAGCAGCCGAGTCGCCAG
GTGAAGCTGTGGGTGAAGATGGTGACTCCACTGATCAAGAACTTCTTCTGA
|
| Enzyme 7 GenBank Gene ID |
AK316147  |
| Enzyme 7 GeneCard ID |
PGS1  |
| Enzyme 7 GenAtlas ID |
PGS1  |
| Enzyme 7 HGNC ID |
HGNC:30029  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
17q25.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 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
]
- 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 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
12879 |
| Enzyme 8 Name |
Glycerol-3-phosphate dehydrogenase 1-like protein |
| Enzyme 8 Synonyms |
- GPD1-L
|
| Enzyme 8 Gene Name |
GPD1L |
| Enzyme 8 Protein Sequence |
>Glycerol-3-phosphate dehydrogenase 1-like protein
MAAAPLKVCIVGSGNWGSAVAKIIGNNVKKLQKFASTVKMWVFEETVNGRKLTDIINNDH
ENVKYLPGHKLPENVVAMSNLSEAVQDADLLVFVIPHQFIHRICDEITGRVPKKALGITL
IKGIDEGPEGLKLISDIIREKMGIDISVLMGANIANEVAAEKFCETTIGSKVMENGLLFK
ELLQTPNFRITVVDDADTVELCGALKNIVAVGAGFCDGLRCGDNTKAAVIRLGLMEMIAF
ARIFCKGQVSTATFLESCGVADLITTCYGGRNRRVAEAFARTGKTIEELEKEMLNGQKLQ
GPQTSAEVYRILKQKGLLDKFPLFTAVYQICYESRPVQEMLSCLQSHPEHT
|
| Enzyme 8 Number of Residues |
351 |
| Enzyme 8 Molecular Weight |
38418.4 |
| Enzyme 8 Theoretical pI |
7.03 |
| Enzyme 8 GO Classification |
| Function |
- NAD or NADH binding
- binding
- catalytic activity
- coenzyme binding
- cofactor binding
- glycerol-3-phosphate dehydrogenase [NAD+] activity
- glycerol-3-phosphate dehydrogenase [NAD+] activity
- identical protein binding
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
- protein binding
- protein homodimerization activity
|
| Process |
- alcohol metabolic process
- alditol metabolic process
- carbohydrate metabolic process
- glycerol metabolic process
- glycerol-3-phosphate catabolic process
- glycerol-3-phosphate metabolic process
- metabolic process
- oxidation reduction
- polyol metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
- cell part
- cytoplasm
- glycerol-3-phosphate dehydrogenase complex
- intracellular part
- macromolecular complex
- protein complex
|
|
| Enzyme 8 General Function |
Involved in oxidoreductase activity |
| Enzyme 8 Specific Function |
Play a role in regulating cardiac sodium current; decreased enzymatic activity with resulting increased levels of glycerol 3-phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway, may ultimately lead to decreased sodium current; cardiac sodium current may also be reduced due to alterations of NAD(H) balance induced by DPD1L |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+ [RN:R00842]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
158259077  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q8N335  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
GPD1L_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1056 bp
ATGGCAGCGGCGCCCCTGAAAGTGTGCATCGTGGGCTCGGGGAACTGGGGTTCAGCTGTT
GCAAAAATAATTGGTAATAATGTCAAGAAACTTCAGAAATTTGCCTCCACAGTCAAGATG
TGGGTCTTTGAAGAAACAGTGAATGGCAGAAAACTGACAGACATCATAAATAATGACCAT
GAAAATGTAAAATATCTTCCTGGACACAAGCTGCCAGAAAATGTGGTTGCCATGTCAAAT
CTTAGCGAGGCTGTGCAGGATGCAGACCTGCTGGTGTTTGTCATTCCCCACCAGTTCATT
CACAGAATCTGTGATGAGATCACTGGGAGAGTGCCCAAGAAAGCGCTGGGAATCACCCTC
ATCAAGGGCATAGACGAGGGCCCCGAGGGGCTGAAGCTCATTTCTGACATCATCCGTGAG
AAGATGGGTATTGACATCAGTGTGCTGATGGGAGCCAACATTGCCAATGAGGTGGCTGCA
GAGAAGTTCTGTGAGACCACCATCGGCAGCAAAGTAATGGAGAACGGCCTTCTCTTCAAA
GAACTTCTGCAGACTCCAAATTTTCGAATTACCGTGGTTGATGATGCAGACACTGTTGAA
CTCTGTGGTGCGCTTAAGAACATCGTAGCTGTGGGAGCTGGGTTCTGCGACGGCCTCCGC
TGTGGAGACAACACCAAAGCGGCCGTCATCCGCCTGGGACTCATGGAAATGATTGCTTTT
GCCAGGATCTTCTGCAAAGGCCAAGTGTCTACAGCCACCTTCCTAGAGAGCTGCGGGGTG
GCCGACCTGATCACCACCTGTTACGGAGGGCGGAACCGCAGGGTGGCCGAGGCCTTCGCC
AGAACTGGGAAGACCATTGAAGAGTTGGAGAAGGAGATGCTGAATGGGCAAAAGCTCCAA
GGACCGCAGACTTCTGCTGAAGTGTACCGCATCCTCAAACAGAAGGGACTACTGGACAAG
TTTCCATTGTTTACTGCAGTGTATCAGATCTGCTACGAAAGCAGACCAGTTCAAGAGATG
TTGTCTTGTCTTCAGAGCCATCCAGAGCATACATAA
|
| Enzyme 8 GenBank Gene ID |
AK292808  |
| Enzyme 8 GeneCard ID |
GPD1L  |
| Enzyme 8 GenAtlas ID |
GPD1L  |
| Enzyme 8 HGNC ID |
HGNC:28956  |
| Enzyme 8 Chromosome Location |
3 |
| Enzyme 8 Locus |
3p22.3 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al.: Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995;2(1):37-43. [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
]
- Valdivia CR, Ueda K, Ackerman MJ, Makielski JC: GPD1L links redox state to cardiac excitability by PKC-dependent phosphorylation of the sodium channel SCN5A. Am J Physiol Heart Circ Physiol. 2009 Oct;297(4):H1446-52. Epub 2009 Aug 7. [PubMed
]
- Liu M, Sanyal S, Gao G, Gurung IS, Zhu X, Gaconnet G, Kerchner LJ, Shang LL, Huang CL, Grace A, London B, Dudley SC Jr: Cardiac Na+ current regulation by pyridine nucleotides. Circ Res. 2009 Oct 9;105(8):737-45. Epub 2009 Sep 10. [PubMed
]
- Van Norstrand DW, Valdivia CR, Tester DJ, Ueda K, London B, Makielski JC, Ackerman MJ: Molecular and functional characterization of novel glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L) mutations in sudden infant death syndrome. Circulation. 2007 Nov 13;116(20):2253-9. Epub 2007 Oct 29. [PubMed
]
- London B, Michalec M, Mehdi H, Zhu X, Kerchner L, Sanyal S, Viswanathan PC, Pfahnl AE, Shang LL, Madhusudanan M, Baty CJ, Lagana S, Aleong R, Gutmann R, Ackerman MJ, McNamara DM, Weiss R, Dudley SC Jr: Mutation in glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L) decreases cardiac Na+ current and causes inherited arrhythmias. Circulation. 2007 Nov 13;116(20):2260-8. Epub 2007 Oct 29. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
13045 |
| Enzyme 9 Name |
Putative uncharacterized protein DKFZp451B1115 |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
DKFZp451B1115 |
| Enzyme 9 Protein Sequence |
>Putative uncharacterized protein DKFZp451B1115
MDESALTLGTIDVSYLPHSSEYSVGRCKHTSEEWGECGFRPTVFRSATLKWKESLMSRKR
PFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDV
HKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKRILQEMVAT
VSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLLFLPVHRSHIDYLLLT
FILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDVLYRALLHGHI
VELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNVIPDILIIPVGISYGRII
EGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSA
LLSLEQALLPAILPSRPSDAADEGRDTSINESRNATDESLRRRLIANLAEHILFTASKSC
AIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLL
GNCVTITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLNKRGLG
GPTSTPPNLISQEQLVRKAASLCYLLSNEATISLPCQTFYQVCHETVGKFIQYGILTVAE
HDDQEDISPSLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITF
LQRLLGPLLEAYSSAAIFVHNFSGPVPEPEYLQKLHKYLITRTERNVAVYAESATYCLVK
NAVKMFKDIGVFKETKQKRVSVLELSSTFLPQCNRQKLLEYILSFVVL
|
| Enzyme 9 Number of Residues |
828 |
| Enzyme 9 Molecular Weight |
93735.9 |
| Enzyme 9 Theoretical pI |
7.89 |
| Enzyme 9 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in acyltransferase activity |
| Enzyme 9 Specific Function |
Not Available |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
30268347  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q86T70  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
Q86T70_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>2487 bp
ATGGATGAATCTGCACTGACCCTTGGTACAATAGATGTTTCTTATCTGCCACATTCATCA
GAATACAGTGTTGGTCGATGTAAGCACACAAGTGAGGAATGGGGTGAGTGTGGCTTTAGA
CCCACCGTCTTCAGATCTGCAACTTTAAAATGGAAAGAAAGCCTAATGAGTCGGAAAAGG
CCATTTGTTGGAAGATGTTGTTACTCCTGCACTCCCCAGAGCTGGGACAAATTTTTCAAC
CCCAGTATCCCGTCTTTGGGTTTGCGGAATGTTATTTATATCAATGAAACTCACACAAGA
CACCGCGGATGGCTTGCAAGACGCCTTTCTTACGTTCTTTTTATTCAAGAGCGAGATGTG
CATAAGGGCATGTTTGCCACCAATGTGACTGAAAATGTGCTGAACAGCAGTAGAGTACAA
GAGGCAATTGCAGAAGTGGCTGCTGAATTAAACCCTGATGGTTCTGCCCAGCAGCAATCA
AAAGCCGTTAACAAAGTGAAAAAGAAAGCTAAAAGGATTCTTCAAGAAATGGTTGCCACT
GTCTCACCGGCAATGATCAGACTGACTGGGTGGGTGCTGCTAAAACTGTTCAACAGCTTC
TTTTGGAACATTCAAATTCACAAAGGTCAACTTGAGATGGTTAAAGCTGCAACTGAGACG
AATTTGCCGCTTCTGTTTCTACCAGTTCATAGATCCCATATTGACTATCTGCTGCTCACT
TTCATTCTCTTCTGCCATAACATCAAAGCACCATACATTGCTTCAGGCAATAATCTCAAC
ATCCCAATCTTCAGTACCTTGATCCATAAGCTTGGGGGCTTCTTCATACGACGAAGGCTC
GATGAAACACCAGATGGACGGAAAGATGTTCTCTATAGAGCTTTGCTCCATGGGCATATA
GTTGAATTACTTCGACAGCAGCAATTCTTGGAGATCTTCCTGGAAGGCACACGTTCTAGG
AGTGGAAAAACCTCTTGTGCTCGGGCAGGACTTTTGTCAGTTGTGGTAGATACTCTGTCT
ACCAATGTCATCCCAGACATCTTGATAATACCTGTTGGAATCTCCTATGGTCGCATTATC
GAAGGTCACTACAATGGTGAACAACTGGGCAAACCTAAGAAGAATGAGAGCCTGTGGAGT
GTAGCAAGAGGTGTTATTAGAATGTTACGAAAAAACTATGGTTGTGTCCGAGTGGATTTT
GCACAGCCATTTTCCTTAAAGGAATATTTAGAAAGCCAAAGTCAGAAACCGGTGTCTGCT
CTACTTTCCCTGGAGCAAGCGTTGTTACCAGCTATACTTCCTTCAAGACCCAGTGATGCT
GCTGATGAGGGTAGAGACACGTCCATTAATGAGTCCAGAAATGCAACAGATGAATCCCTA
CGAAGGAGGTTGATTGCAAATCTGGCTGAGCATATTCTATTCACTGCTAGCAAGTCCTGT
GCCATTATGTCCACACACATTGTGGCTTGCCTGCTCCTCTACAGACACAGGCAGGGAATT
GATCTCTCCACATTGGTCGAAGACTTCTTTGTGATGAAAGAGGAAGTCCTGGCTCGTGAT
TTTGACCTGGGGTTCTCAGGAAATTCAGAAGATGTAGTAATGCATGCCATACAGCTGCTG
GGAAATTGTGTCACAATCACCCACACTAGCAGGAACGATGAGTTTTTTATCACCCCCAGC
ACAACTGTCCCATCAGTCTTCGAACTCAACTTCTACAGCAATGGGGTACTTCATGTCTTT
ATCATGGAGGCCATCATAGCTTGCAGCCTTTATGCAGTTCTGAACAAGAGGGGACTGGGG
GGTCCCACTAGCACCCCACCTAACCTGATCAGCCAGGAGCAGCTGGTGCGGAAGGCGGCC
AGCCTGTGCTACCTTCTCTCCAATGAAGCCACCATCTCACTGCCTTGCCAGACATTTTAC
CAAGTCTGCCATGAAACAGTAGGAAAGTTTATCCAGTATGGCATTCTTACAGTGGCAGAG
CACGATGACCAGGAAGATATCAGTCCTAGTCTTGCTGAGCAGCAGTGGGACAAGAAGCTT
CCTGAACCTTTGTCTTGGAGAAGTGATGAAGAAGATGAAGACAGTGACTTTGGGGAGGAA
CAGCGAGATTGCTACCTGAAGGTGAGCCAATCCAAGGAGCACCAGCAGTTTATCACCTTC
TTACAGAGACTCCTTGGGCCTTTGCTGGAGGCCTACAGCTCTGCTGCCATCTTTGTTCAC
AACTTCAGTGGTCCTGTTCCAGAACCTGAGTATCTGCAAAAGTTGCACAAATACCTAATA
ACCAGAACAGAAAGAAATGTTGCAGTATATGCTGAGAGTGCCACATATTGTCTTGTGAAG
AATGCTGTGAAAATGTTTAAGGATATTGGGGTTTTCAAGGAGACCAAACAAAAGAGAGTG
TCTGTTTTAGAACTGAGCAGCACTTTTCTACCTCAATGCAACCGACAAAAACTTCTAGAA
TATATTCTGAGTTTTGTGGTGCTGTAG
|
| Enzyme 9 GenBank Gene ID |
AL833061  |
| Enzyme 9 GeneCard ID |
DKFZp451B1115  |
| Enzyme 9 GenAtlas ID |
DKFZp451B1115  |
| Enzyme 9 HGNC ID |
HGNC:24865  |
| Enzyme 9 Chromosome Location |
Not Available |
| Enzyme 9 Locus |
Not Available |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
Not Available |
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
13047 |
| Enzyme 10 Name |
cDNA FLJ75492, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2 |
| Enzyme 10 Synonyms |
- mitochondrial
- GPD2, mRNA
- Glycerol-3-phosphate dehydrogenase 2
- Mitochondrial, isoform CRA_b
- cDNA FLJ78257, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2
- mitochondrial
- GPD2, mRNA
|
| Enzyme 10 Gene Name |
GPD2 |
| Enzyme 10 Protein Sequence |
>cDNA FLJ75492, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2
MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADCISEPVNREPPSREAQ
LLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVR
YLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLY
DLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYG
AATANYMEVVSLLKKTDPQTGKVHVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKM
DDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTD
VTHHPIPSEEDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNH
VVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLY
IRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVGVRLVSEFPYIEAEVKYG
IKEYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFLY
YEMGYKSRSEQLTDRSEISLLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMD
ENTLHEILNEVDLNKNGQVELNEFLQLMSAIQKGRVSGSRLAILMKTAEENLDRRVPIPV
DRSCGGL
|
| Enzyme 10 Number of Residues |
727 |
| Enzyme 10 Molecular Weight |
80835 |
| Enzyme 10 Theoretical pI |
7.58 |
| Enzyme 10 GO Classification |
Not Available |
| Enzyme 10 General Function |
Energy production and conversion |
| Enzyme 10 Specific Function |
Not Available |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
Not Available |
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
158255566  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
A8K4V0  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
A8K4V0_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
Not Available |
| Enzyme 10 GenBank Gene ID |
AK291065  |
| Enzyme 10 GeneCard ID |
A8K4V0  |
| Enzyme 10 GenAtlas ID |
Not Available |
| Enzyme 10 HGNC ID |
Not Available |
| Enzyme 10 Chromosome Location |
Not Available |
| Enzyme 10 Locus |
Not Available |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
Not Available |
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
13048 |
| Enzyme 11 Name |
N-acetyltransferase ESCO1 variant 1 (Establishment of cohesion 1 homolog 1 (S. cerevisiae), isoform CRA_b) |
| Enzyme 11 Synonyms |
Not Available |
| Enzyme 11 Gene Name |
ESCO1 |
| Enzyme 11 Protein Sequence |
>N-acetyltransferase ESCO1 variant 1 (Establishment of cohesion 1 homolog 1 (S. cerevisiae), isoform CRA_b)
MMSIQEKSKENSSKVTKKSDDKNSETEIQDSQKNLAKKSGPKETIKSQAKSSSESKINQP
ELETRMSTRSSKAASNDKATKSINKNTVTVRGYSQESTKKKLSQKKLVHENPKANEQLNR
RSQRLQQLTEVSRRSLRSREIQGQVQAVKQSLPPTKKEQCSSTQSKSNKTSQKHVKRKVL
EVKSDSKEDENLVINEVINSPKGKKRKVEHQTACACSSQCTQGSEKCPQKTTRRDETKPV
PVTSEVKRSKMATSVVPKKNEMKKSVHTQVNTNTTLPKSPQPSVPEQSDNELEQAGKSKR
GSILQLCEEIAGEIESDNVEVKKESSQMESVKEEKPTEIKLEETSVERQILHQKETNQDV
QCNRFFPSRKTKPVKCILNGINSSAKKNSNWTKIKLSKFNSVQHNKLDSQVSPKLGLLRT
SFSPPALEMHHPVTQSTFLGTKLHDRNITCQQEKMKEINSEEVKINDITVEINKTTERAP
ENCHLANEIKPSDPPLDNQMKHSFDSASNKNFSQCLESKLENSPVENVTAASTLLSQAKI
DTGENKFPGSAPQQHSILSNQTSKSSDNRETPRNHSLPKCNSHLEITIPKDLKLKEAEKT
DEKQLIIDAGQKRFGAVSCNVCGMLYTASNPEDETQHLLFHNQFISAVKYVGWKKERILA
EYPDGRIIMVLPEDPKYALKKVDEIREMVDNDLGFQQAPLMCYSRTKTLLFISNDKKVVG
CLIAEHIQWGYRVIEEKLPVIRSEEEKVRFERQKAWCCSTLPEPAICGISRIWVFSMMRR
KKIASRMIECLRSNFIYGSYLSKEEIAFSDPTPDGKLFATQYCGTGQFLVYNFINGQNST
|
| Enzyme 11 Number of Residues |
840 |
| Enzyme 11 Molecular Weight |
94983 |
| Enzyme 11 Theoretical pI |
Not Available |
| Enzyme 11 GO Classification |
Not Available |
| Enzyme 11 General Function |
Not Available |
| Enzyme 11 Specific Function |
Not Available |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
Not Available |
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
Not Available |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
B0YJ11  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
B0YJ11_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
Not Available |
| Enzyme 11 GenBank Gene ID |
Not Available |
| Enzyme 11 GeneCard ID |
B0YJ11  |
| Enzyme 11 GenAtlas ID |
Not Available |
| Enzyme 11 HGNC ID |
Not Available |
| Enzyme 11 Chromosome Location |
Not Available |
| Enzyme 11 Locus |
Not Available |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
Not Available |
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
13050 |
| Enzyme 12 Name |
Glycerophosphodiester phosphodiesterase 1 |
| Enzyme 12 Synonyms |
- Membrane-interacting protein of RGS16
- RGS16-interacting membrane protein
|
| Enzyme 12 Gene Name |
GDE1 |
| Enzyme 12 Protein Sequence |
>Glycerophosphodiester phosphodiesterase 1
MWLWEDQGGLLGPFSFLLLVLLLVTRSPVNACLLTGSLFVLLRVFSFEPVPSCRALQVLK
PRDRISAIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGIPVLMHDNTVDRTT
DGTGRLCDLTFEQIRKLNPAANHRLRNDFPDEKIPTLREAVAECLNHNLTIFFDVKGHAH
KATEALKKMYMEFPQLYNNSVVCSFLPEVIYKMRQTDRDVITALTHRPWSLSHTGDGKPR
YDTFWKHFIFVMMDILLDWSMHNILWYLCGISAFLMQKDFVSPAYLKKWSAKGIQVVGWT
VNTFDEKSYYESHLGSSYITDSMVEDCEPHF
|
| Enzyme 12 Number of Residues |
331 |
| Enzyme 12 Molecular Weight |
37718.0 |
| Enzyme 12 Theoretical pI |
6.70 |
| Enzyme 12 GO Classification |
| Function |
- catalytic activity
- glycerophosphodiester phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- alcohol metabolic process
- alditol metabolic process
- glycerol metabolic process
- lipid metabolic process
- metabolic process
- polyol metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in glycerophosphodiester phosphodiesterase activity |
| Enzyme 12 Specific Function |
Has glycerophosphoinositol phosphodiesterase activity. Has little or no activity towards glycerophosphocholine. GDE1 activity can be modulated by G-protein signaling pathways |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
- 1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O = myo-inositol + sn-glycerol 3-phosphate [RN:R01193]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
7637877  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9NZC3  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
GDE1_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>996 bp
ATGTGGCTGTGGGAGGACCAGGGCGGCCTCCTGGGCCCTTTCTCCTTCCTGCTGCTAGTG
CTGCTGCTGGTGACGCGGAGCCCGGTCAATGCCTGCCTCCTCACCGGCAGCCTCTTCGTT
CTACTGCGCGTCTTCAGCTTTGAGCCGGTGCCCTCTTGCAGGGCCCTGCAGGTGCTCAAG
CCCCGGGACCGCATTTCTGCCATCGCCCACCGTGGCGGCAGCCACGACGCGCCCGAGAAC
ACGCTGGCGGCCATTCGGCAGGCAGCTAAGAATGGAGCAACAGGCGTGGAGTTGGACATT
GAGTTTACTTCTGACGGGATTCCTGTCTTAATGCACGATAACACAGTAGATAGGACGACT
GATGGGACTGGGCGATTGTGTGATTTGACATTTGAACAAATTAGGAAGCTGAATCCTGCA
GCAAACCACAGACTCAGGAATGATTTCCCTGATGAAAAGATCCCTACCCTAAGGGAAGCT
GTTGCAGAGTGCCTAAACCATAACCTCACAATCTTCTTTGATGTCAAAGGCCATGCACAC
AAGGCTACTGAGGCTCTAAAGAAAATGTATATGGAATTTCCTCAACTGTATAATAATAGT
GTGGTCTGTTCTTTCTTGCCAGAAGTTATCTACAAGATGAGACAAACAGATCGGGATGTA
ATAACAGCATTAACTCACAGACCTTGGAGCCTAAGCCATACAGGAGATGGGAAACCACGC
TATGATACTTTCTGGAAACATTTTATATTTGTTATGATGGACATTTTGCTCGATTGGAGC
ATGCATAATATCTTGTGGTACCTGTGTGGAATTTCAGCTTTCCTCATGCAAAAGGATTTT
GTATCCCCGGCCTACTTGAAGAAGTGGTCAGCTAAAGGAATCCAGGTTGTTGGTTGGACT
GTTAATACCTTTGATGAAAAGAGTTACTACGAATCCCATCTTGGTTCCAGCTATATCACT
GACAGCATGGTAGAAGACTGCGAACCTCACTTCTAG
|
| Enzyme 12 GenBank Gene ID |
AF212862  |
| Enzyme 12 GeneCard ID |
GDE1  |
| Enzyme 12 GenAtlas ID |
GDE1  |
| Enzyme 12 HGNC ID |
HGNC:29644  |
| Enzyme 12 Chromosome Location |
1 |
| Enzyme 12 Locus |
16p12-p11.2 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Zheng B, Chen D, Farquhar MG: MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16. Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):3999-4004. [PubMed
]
- Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [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
]
- Bachmann AS, Duennebier FF, Mocz G: Genomic organization, characterization, and molecular 3D model of GDE1, a novel mammalian glycerophosphoinositol phosphodiesterase. Gene. 2006 Apr 12;371(1):144-53. Epub 2006 Feb 9. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
15215 |
| Enzyme 13 Name |
Putative uncharacterized protein DKFZp451P0819 |
| Enzyme 13 Synonyms |
Not Available |
| Enzyme 13 Gene Name |
DKFZp451P0819 |
| Enzyme 13 Protein Sequence |
>Putative uncharacterized protein DKFZp451P0819
MDESALTLGTIDVSYLPHSSEYSVGRCKHTSEEWGECGFRPTIFRSATLKWKESLMSRKR
PFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDV
HKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKRILQEMVAT
VSPAMIRLTGWVLLKLFNSFFWNFQIHKGQLEMVKAATETNLPLLFLPVHRSHIDYLLLT
FILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDVLYRALLHGHI
VELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNVIPDILIIPVGISYDRII
EGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSA
LLSLEQALLPAILPSRPSDAADEGRDTSINESRNATDESLRRRLIANLAEHILFTASKSC
AIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLL
GNCVTITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLNKRGLG
GPTSTPPNLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQVCHETVGKFIRYGILTVAE
HDDQEDISPSLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITF
LQRLLGPLLEAYSSAAIFVHNFSGPVPEPEYLQKLHKYLITRTERNVAVYAESATYCLVK
NAVKMFKDIGVFKETKQKRVSVLELSSTFLPQCNRQKLLEYILSFVVL
|
| Enzyme 13 Number of Residues |
828 |
| Enzyme 13 Molecular Weight |
93858 |
| Enzyme 13 Theoretical pI |
7.89 |
| Enzyme 13 GO Classification |
| Function |
- O-acyltransferase activity
- acyltransferase activity
- catalytic activity
- glycerol-3-phosphate O-acyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
- cellular lipid metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- phospholipid biosynthesis
- phospholipid metabolism
- physiological process
- primary metabolism
|
| Component |
|
|
| Enzyme 13 General Function |
Lipid transport and metabolism |
| Enzyme 13 Specific Function |
Not Available |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
30268383  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q86TA3  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
Q86TA3_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>2487 bp
ATGGATGAATCTGCACTGACCCTTGGTACAATAGATGTTTCTTATCTGCCACATTCATCA
GAATACAGTGTTGGTCGATGTAAGCACACAAGTGAGGAATGGGGTGAGTGTGGCTTTAGA
CCCACCATCTTCAGATCTGCAACTTTAAAATGGAAAGAAAGCCTAATGAGTCGGAAAAGG
CCATTTGTTGGAAGATGTTGTTACTCCTGCACTCCCCAGAGCTGGGACAAATTTTTCAAC
CCCAGTATCCCGTCTTTGGGTTTGCGGAATGTTATTTATATCAATGAAACTCACACAAGA
CACCGCGGATGGCTTGCAAGACGCCTTTCTTACGTTCTTTTTATTCAAGAGCGAGATGTG
CATAAGGGCATGTTTGCCACCAATGTGACTGAAAATGTGCTGAACAGCAGTAGAGTACAA
GAGGCAATTGCAGAAGTGGCTGCTGAATTAAACCCTGATGGTTCTGCCCAGCAGCAATCA
AAAGCCGTTAACAAAGTGAAAAAGAAAGCTAAAAGGATTCTTCAAGAAATGGTTGCCACT
GTCTCACCGGCAATGATCAGACTGACTGGGTGGGTGCTGCTAAAACTGTTCAACAGCTTC
TTTTGGAACTTTCAAATTCACAAAGGTCAACTTGAGATGGTTAAAGCTGCAACTGAGACG
AATTTGCCGCTTCTGTTTCTACCAGTTCATAGATCCCATATTGACTATCTGCTGCTCACT
TTCATTCTCTTCTGCCATAACATCAAAGCACCATACATTGCTTCAGGCAATAATCTCAAC
ATCCCAATCTTCAGTACCTTGATCCATAAGCTTGGGGGCTTCTTCATACGACGAAGGCTC
GATGAAACACCAGATGGACGGAAAGATGTTCTCTATAGAGCTTTGCTCCATGGGCATATA
GTTGAATTACTTCGACAGCAGCAATTCTTGGAGATCTTCCTGGAAGGCACACGTTCTAGG
AGTGGAAAAACCTCTTGTGCTCGGGCAGGACTTTTGTCAGTTGTGGTAGATACTCTGTCT
ACCAATGTCATCCCAGACATCTTGATAATACCTGTTGGAATCTCCTATGATCGCATTATC
GAAGGTCACTACAATGGTGAACAACTGGGCAAACCTAAGAAGAATGAGAGCCTGTGGAGT
GTAGCAAGAGGTGTTATTAGAATGTTACGAAAAAACTATGGTTGTGTCCGAGTGGATTTT
GCACAGCCATTTTCCTTAAAGGAATATTTAGAAAGCCAAAGTCAGAAACCGGTGTCTGCT
CTACTTTCCCTGGAGCAAGCGTTGTTACCAGCTATACTTCCTTCAAGACCCAGTGATGCT
GCTGATGAAGGTAGAGACACGTCCATTAATGAGTCCAGAAATGCAACAGATGAATCCCTA
CGAAGGAGGTTGATTGCAAATCTGGCTGAGCATATTCTATTCACTGCTAGCAAGTCCTGT
GCCATTATGTCCACACACATTGTGGCTTGCCTGCTCCTCTACAGACACAGGCAGGGAATT
GATCTCTCCACATTGGTCGAAGACTTCTTTGTGATGAAAGAGGAAGTCCTGGCTCGTGAT
TTTGACCTGGGGTTCTCAGGAAATTCAGAAGATGTAGTAATGCATGCCATACAGCTGCTG
GGAAATTGTGTCACAATCACCCACACTAGCAGGAACGATGAGTTTTTTATCACCCCCAGC
ACAACTGTCCCATCAGTCTTCGAACTCAACTTCTACAGCAATGGGGTACTTCATGTCTTT
ATCATGGAGGCCATCATAGCTTGCAGCCTTTATGCAGTTCTGAACAAGAGGGGACTGGGG
GGTCCCACTAGCACCCCACCTAACCTGATCAGCCAGGAGCAGCTGGTGCGGAAGGCGGCC
AGCCTGTGCTACCTTCTCTCCAATGAAGGCACCATCTCACTGCCTTGCCAGACATTTTAC
CAAGTCTGCCATGAAACAGTAGGAAAGTTTATCCGGTATGGCATTCTTACAGTGGCAGAG
CACGATGACCAGGAAGATATCAGTCCTAGTCTTGCTGAGCAGCAGTGGGACAAGAAGCTT
CCAGAACCTTTGTCTTGGAGAAGTGATGAAGAAGATGAAGACAGTGACTTTGGGGAGGAA
CAGCGAGATTGCTACCTGAAGGTGAGCCAATCCAAGGAGCACCAGCAGTTTATCACCTTC
TTACAGAGACTCCTTGGGCCTTTGCTGGAGGCCTACAGCTCTGCTGCCATCTTTGTTCAC
AACTTCAGTGGTCCTGTTCCAGAACCTGAGTATCTGCAAAAGTTGCACAAATACCTAATA
ACCAGAACAGAAAGAAATGTTGCAGTATATGCTGAGAGTGCCACATATTGTCTTGTGAAG
AATGCTGTGAAAATGTTTAAGGATATTGGGGTTTTCAAGGAGACCAAACAAAAGAGAGTG
TCTGTTTTAGAACTGAGCAGCACTTTTCTACCTCAATGCAACCGACAAAAACTTCTAGAA
TATATTCTGAGTTTTGTGGTGCTGTAG
|
| Enzyme 13 GenBank Gene ID |
AL833093  |
| Enzyme 13 GeneCard ID |
Q86TA3  |
| Enzyme 13 GenAtlas ID |
DKFZp451P0819  |
| Enzyme 13 HGNC ID |
HGNC:24865  |
| Enzyme 13 Chromosome Location |
Not Available |
| Enzyme 13 Locus |
Not Available |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
Not Available |
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
16495 |
| Enzyme 14 Name |
cDNA, FLJ93716, Homo sapiens glycerol kinase (GK), mRNA |
| Enzyme 14 Synonyms |
Not Available |
| Enzyme 14 Gene Name |
Not Available |
| Enzyme 14 Protein Sequence |
>cDNA, FLJ93716, Homo sapiens glycerol kinase (GK), mRNA
MAASKKAVLGPLVGAVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEI
LHSVYECIEKTCEKLGQLNIDISNIKAIGVSNQRETTVVWDKITGEPLYNAVVWLDLRTQ
STVESLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVRKVQKAVEEKRALFGTIDS
WLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKQLCEFFGIPMEILPNVRSSSEIY
GLMKAGALEGVPISGCLGDQSAALVGQMCFQIGQAKNTYGTGCFLLCNTGHKCVFSDHGL
LTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKTSEEIEKLAKEVGTSYGCYF
VPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLS
HLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMAAGAAEGVGVWSLEPEDLS
AVTMERFEPQINAEESEIRYSTWKKAVMKSMGWVTTQSPESGIP
|
| Enzyme 14 Number of Residues |
524 |
| Enzyme 14 Molecular Weight |
57490 |
| Enzyme 14 Theoretical pI |
6.25 |
| Enzyme 14 GO Classification |
| Function |
- catalytic activity
- glycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- carbohydrate metabolism
- cellular metabolism
- glycerol metabolism
- glycerol-3-phosphate metabolism
- macromolecule metabolism
- metabolism
- physiological process
- polyol metabolism
|
| Component |
| — |
|
| Enzyme 14 General Function |
Energy production and conversion |
| Enzyme 14 Specific Function |
Not Available |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
Not Available |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
B2R833  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
B2R833_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
Not Available |
| Enzyme 14 GenBank Gene ID |
AK313215  |
| Enzyme 14 GeneCard ID |
B2R833  |
| Enzyme 14 GenAtlas ID |
GK  |
| Enzyme 14 HGNC ID |
HGNC:4289  |
| Enzyme 14 Chromosome Location |
Not Available |
| Enzyme 14 Locus |
Not Available |
| Enzyme 14 SNPs |
Not Available |
| Enzyme 14 General References |
Not Available |
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
16856 |
| Enzyme 15 Name |
Glycerol-3-phosphate acyltransferase 2, mitochondrial |
| Enzyme 15 Synonyms |
- GPAT-2
- xGPAT1
|
| Enzyme 15 Gene Name |
GPAT2 |
| Enzyme 15 Protein Sequence |
>Glycerol-3-phosphate acyltransferase 2, mitochondrial
MATMLEGRCQTQPRSSPSGREASLWSSGFGMKLEAVTPFLGKYRPFVGRCCQTCTPKSWE
SLFHRSITDLGFCNVILVKEENTRFRGWLVRRLCYFLWSLEQHIPPCQDVPQKIMESTGV
QNLLSGRVPGGTGEGQVPDLVKKEVQRILGHIQAPPRPFLVRLFSWALLRFLNCLFLNVQ
LHKGQMKMVQKAAQAGLPLVLLSTHKTLLDGILLPFMLLSQGLGVLRVAWDSRACSPALR
ALLRKLGGLFLPPEASLSLDSSEGLLARAVVQAVIEQLLVSGQPLLIFLEEPPGALGPRL
SALGQAWVGFVVQAVQVGIVPDALLVPVAVTYDLVPDAPCDIDHASAPLGLWTGALAVLR
SLWSRWGCSHRICSRVHLAQPFSLQEYIVSARSCWGGRQTLEQLLQPIVLGQCTAVPDTE
KEQEWTPITGPLLALKEEDQLLVRRLSCHVLSASVGSSAVMSTAIMATLLLFKHQKLLGE
FSWLTEEILLRGFDVGFSGQLRSLLQHSLSLLRAHVALLRIRQGDLLVVPQPGPGLTHLA
QLSAELLPVFLSEAVGACAVRGLLAGRVPPQGPWELQGILLLSQNELYRQILLLMHLLPQ
DLLLLKPCQSSYCYCQEVLDRLIQCGLLVAEETPGSRPACDTGRQRLSRKLLWKPSGDFT
DSDSDDFGEADGRYFRLSQQSHCPDFFLFLCRLLSPLLKAFAQAAAFLRQGQLPDTELGY
TEQLFQFLQATAQEEGIFECADPKLAISAVWTFRDLGVLQQTPSPAGPRLHLSPTFASLD
NQEKLEQFIRQFICS
|
| Enzyme 15 Number of Residues |
795 |
| Enzyme 15 Molecular Weight |
87834.5 |
| Enzyme 15 Theoretical pI |
7.63 |
| Enzyme 15 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in acyltransferase activity |
| Enzyme 15 Specific Function |
Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
- acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
|
| Enzyme 15 Pfam Domain Function |
Not Available |
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
116812614  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q6NUI2  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
GPAT2_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>2388 bp
ATGGCCACCATGTTGGAAGGCAGATGCCAAACTCAGCCAAGGAGCAGCCCCAGTGGCCGA
GAGGCTAGCCTGTGGTCGTCAGGCTTTGGGATGAAGCTGGAGGCTGTCACTCCATTCCTG
GGGAAGTATCGCCCCTTTGTGGGTCGCTGTTGCCAGACCTGCACCCCCAAGAGCTGGGAG
TCCCTCTTCCACAGAAGCATAACGGACCTAGGCTTCTGCAATGTGATCCTGGTGAAGGAG
GAGAACACAAGGTTTCGGGGCTGGCTGGTTCGGAGGCTCTGCTATTTCCTGTGGTCCCTG
GAGCAGCACATCCCCCCCTGCCAGGATGTCCCACAGAAGATCATGGAAAGCACCGGGGTG
CAGAACCTCCTCTCAGGGAGGGTCCCAGGAGGCACTGGGGAAGGCCAGGTGCCTGACCTT
GTGAAGAAGGAGGTACAGCGCATCCTGGGTCACATCCAGGCCCCACCCCGTCCCTTCCTG
GTCAGGCTGTTCAGCTGGGCGCTGCTGAGGTTCCTGAACTGCCTGTTCCTGAATGTGCAG
CTCCACAAGGGTCAGATGAAGATGGTCCAGAAGGCCGCCCAGGCAGGCTTGCCGCTTGTC
CTCCTCTCTACTCACAAAACCCTCCTGGATGGGATCCTGCTGCCCTTTATGCTGCTCTCC
CAGGGCCTGGGTGTGCTTCGTGTGGCCTGGGACTCCCGCGCCTGCTCCCCTGCCCTCAGA
GCTCTGCTGAGGAAGCTTGGGGGGCTTTTCCTGCCCCCAGAGGCCAGCCTCTCCCTGGAC
AGCTCTGAGGGGCTCCTTGCCAGGGCTGTGGTCCAGGCGGTCATAGAGCAGCTGCTGGTT
AGTGGGCAGCCCCTGCTCATCTTCCTGGAGGAACCTCCTGGGGCTCTGGGGCCACGGCTG
TCAGCCCTGGGCCAGGCTTGGGTGGGGTTTGTGGTGCAGGCAGTCCAGGTGGGCATCGTC
CCAGATGCTCTGCTGGTACCAGTGGCCGTCACCTATGACCTGGTTCCGGATGCACCGTGT
GACATAGACCATGCCTCGGCCCCCCTGGGGCTGTGGACAGGAGCTCTGGCTGTCCTACGT
AGCTTGTGGAGCCGCTGGGGCTGCAGCCACCGGATCTGCTCCCGGGTGCACCTAGCTCAG
CCCTTTTCCCTGCAGGAATACATCGTCAGTGCCAGAAGCTGCTGGGGCGGCAGACAGACC
CTGGAGCAGCTACTGCAGCCCATCGTGCTGGGCCAATGTACTGCTGTCCCAGACACTGAG
AAGGAGCAGGAGTGGACCCCCATAACTGGGCCTCTCCTGGCCCTCAAGGAAGAGGACCAG
CTCCTGGTCAGGAGACTGAGCTGTCATGTCCTGAGTGCCAGTGTAGGGAGCTCTGCGGTG
ATGAGCACGGCCATTATGGCAACGCTGCTGCTCTTCAAGCATCAGAAGCTCCTGGGGGAG
TTCTCCTGGCTGACGGAGGAGATACTGTTGCGTGGCTTTGATGTAGGCTTCTCTGGGCAG
CTGCGGAGCCTGCTGCAGCACTCACTGAGCCTGCTGCGGGCGCACGTGGCCCTGCTGCGC
ATCCGTCAGGGTGACTTGCTGGTGGTGCCGCAGCCTGGCCCAGGCCTCACACACCTGGCA
CAACTGAGTGCTGAGCTGCTGCCCGTCTTCCTGAGCGAGGCTGTGGGCGCCTGTGCAGTG
CGGGGGCTGCTGGCAGGCAGAGTGCCGCCCCAGGGGCCCTGGGAGCTGCAGGGCATATTG
CTGCTGAGCCAGAATGAGCTGTACCGCCAGATCCTGCTGCTGATGCACCTGCTGCCGCAA
GACCTGCTGCTGCTAAAGCCCTGCCAGTCTTCCTACTGCTACTGTCAGGAGGTGCTGGAC
CGGCTCATCCAATGCGGGCTCCTGGTTGCTGAGGAGACCCCAGGCTCCCGGCCAGCCTGT
GACACAGGGCGACAGCGATTGAGCAGAAAGCTGCTGTGGAAACCGAGTGGGGACTTTACT
GATAGTGACAGTGATGACTTCGGAGAGGCTGACGGCCGGTACTTCAGGCTCAGCCAGCAG
TCACACTGCCCAGATTTCTTTCTTTTCCTCTGCCGCCTGCTCAGCCCGCTGCTCAAGGCC
TTTGCACAGGCTGCCGCCTTCCTCCGCCAGGGCCAGCTGCCCGATACTGAGTTGGGCTAC
ACAGAGCAGCTGTTCCAGTTCCTGCAGGCCACCGCCCAGGAAGAAGGGATCTTCGAGTGT
GCGGACCCAAAGCTCGCCATCAGTGCTGTCTGGACCTTCAGAGACCTAGGGGTTCTGCAG
CAGACGCCGAGCCCTGCAGGCCCCAGGCTCCACCTGTCCCCTACTTTTGCCAGCCTGGAC
AATCAGGAAAAACTAGAACAGTTCATCCGGCAGTTCATTTGTAGCTAG
|
| Enzyme 15 GenBank Gene ID |
NM_207328.2  |
| Enzyme 15 GeneCard ID |
GPAT2  |
| Enzyme 15 GenAtlas ID |
GPAT2  |
| Enzyme 15 HGNC ID |
HGNC:27168  |
| Enzyme 15 Chromosome Location |
2 |
| Enzyme 15 Locus |
2q11.1 |
| 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
]
- 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 |
16857 |
| Enzyme 16 Name |
Putative glycerol kinase 5 |
| Enzyme 16 Synonyms |
- GK 5
- Glycerokinase 5
- ATP:glycerol 3-phosphotransferase 5
|
| Enzyme 16 Gene Name |
GK5 |
| Enzyme 16 Protein Sequence |
>Putative glycerol kinase 5
MSGLLTDPEQRAQEPRYPGFVLGLDVGSSVIRCHVYDRAARVCGSSVQKVENLYPQIGWV
EIDPDVLWIQFVAVIKEAVKAAGIQMNQIVGLGISTQRATFITWNKKTGNHFHNFISWQD
LRAVELVKSWNNSLLMKIFHSSCRVLHFFTRSKRLFTASLFTFTTQQTSLRLVWILQNLT
EVQKAVEEENCCFGTIDTWLLYKLTKGSVYATDFSNASTTGLFDPYKMCWSGMITSLISI
PLSLLPPVRDTSHNFGSVDEEIFGVPIPIVALVADQQSAMFGECCFQTGDVKLTMGTGTF
LDINTGNSLQQTTGGFYPLIGWKIGQEVVCLAESNAGDIGTAIKWAQQLDLFTDAAETEK
MAKSLEDSEGVCFVPSFSGLQAPLNDPWACASFMGLKPSTSKYHLVRAILESIAFRNKQL
YEMMKKEIHIPVRKIRADGGVCKNGFVMQMTSDLINENIDRPADIDMSCLGAASLAGLAV
GFWTDKEELKKLRQSEVVFKPQKKCQEYEMSLENWAKAVKRSMNWYNKT
|
| Enzyme 16 Number of Residues |
529 |
| Enzyme 16 Molecular Weight |
59167.7 |
| Enzyme 16 Theoretical pI |
6.90 |
| Enzyme 16 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 16 General Function |
Involved in phosphotransferase activity, alcohol group as acceptor |
| Enzyme 16 Specific Function |
ATP + glycerol = ADP + sn-glycerol 3- phosphate |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
- ATP + glycerol = ADP + sn-glycerol 3-phosphate [RN:R00847]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
88196792  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q6ZS86  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
GLPK5_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1590 bp
ATGTCGGGGCTGCTCACGGACCCGGAGCAGAGAGCGCAGGAGCCGCGGTACCCCGGCTTC
GTGCTGGGGCTGGATGTGGGCAGTTCTGTGATCCGCTGCCACGTCTATGACCGGGCGGCG
CGGGTCTGCGGCTCCAGCGTGCAGAAGGTAGAAAATCTTTATCCTCAAATTGGCTGGGTA
GAAATTGATCCTGATGTTCTTTGGATTCAATTTGTTGCCGTAATAAAAGAAGCAGTCAAA
GCTGCAGGAATACAGATGAATCAAATTGTTGGTCTTGGCATTTCAACACAGAGAGCAACT
TTTATTACGTGGAACAAGAAAACAGGAAATCATTTTCACAACTTTATAAGTTGGCAAGAC
TTAAGAGCTGTTGAACTTGTAAAATCTTGGAATAATTCTCTTCTTATGAAGATATTTCAC
AGTTCTTGCCGAGTGCTTCACTTTTTCACTAGAAGTAAACGACTTTTTACAGCCAGTTTG
TTCACTTTCACAACCCAGCAGACTTCTTTGAGATTGGTCTGGATTTTACAGAACTTGACT
GAGGTGCAAAAGGCAGTTGAAGAAGAAAATTGCTGCTTTGGGACTATTGATACCTGGTTG
TTATATAAGCTCACAAAAGGTTCTGTATATGCCACAGATTTTTCAAATGCTAGTACAACT
GGACTTTTTGACCCATATAAGATGTGTTGGAGTGGGATGATTACCTCTCTAATTTCGATA
CCACTTTCTCTCCTACCTCCTGTGAGGGACACAAGCCACAATTTTGGATCAGTGGATGAA
GAGATATTTGGTGTGCCTATACCAATAGTTGCCTTGGTTGCTGACCAGCAATCAGCCATG
TTTGGAGAGTGCTGCTTCCAGACAGGTGATGTGAAATTAACCATGGGAACTGGGACATTT
TTGGATATTAACACTGGAAATAGCCTTCAACAGACTACTGGAGGCTTTTATCCATTAATT
GGGTGGAAGATTGGGCAAGAAGTCGTATGCTTAGCTGAAAGCAATGCAGGAGACACTGGT
ACTGCCATAAAATGGGCTCAGCAGTTAGACCTTTTCACAGATGCTGCTGAGACTGAAAAA
ATGGCCAAAAGTTTGGAGGATTCTGAAGGAGTTTGTTTTGTTCCATCTTTTAGTGGATTA
CAGGCTCCATTAAATGACCCCTGGGCATGTGCCTCTTTTATGGGTTTGAAGCCTTCTACC
AGTAAATACCATCTTGTACGAGCAATATTGGAGTCAATAGCTTTCAGAAACAAACAGTTA
TATGAGATGATGAAGAAAGAGATTCATATTCCTGTAAGAAAAATCCGGGCAGATGGAGGA
GTTTGTAAGAATGGTTTTGTCATGCAGATGACTTCAGACCTGATTAATGAGAATATAGAC
AGACCTGCCGACATTGACATGTCATGCCTGGGTGCAGCTTCTCTAGCTGGCCTTGCTGTT
GGGTTTTGGACTGACAAGGAGGAACTAAAGAAACTGAGACAAAGTGAAGTGGTTTTCAAG
CCACAGAAGAAATGTCAAGAATATGAAATGAGTCTGGAAAACTGGGCCAAAGCAGTGAAA
CGCTCCATGAATTGGTATAACAAGACATAA
|
| Enzyme 16 GenBank Gene ID |
NM_001039547.2  |
| Enzyme 16 GeneCard ID |
GK5  |
| Enzyme 16 GenAtlas ID |
GK5  |
| Enzyme 16 HGNC ID |
HGNC:28635  |
| Enzyme 16 Chromosome Location |
3 |
| Enzyme 16 Locus |
3q23 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 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
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
21018 |
| Enzyme 17 Name |
N-acetyltransferase ESCO1 |
| Enzyme 17 Synonyms |
- CTF7 homolog 1
- Establishment factor-like protein 1
- EFO1p
- hEFO1
- Establishment of cohesion 1 homolog 1
- ECO1 homolog 1
- ESO1 homolog 1
|
| Enzyme 17 Gene Name |
ESCO1 |
| Enzyme 17 Protein Sequence |
>N-acetyltransferase ESCO1
MMSIQEKSKENSSKVTKKSDDKNSETEIQDSQKNLAKKSGPKETIKSQAKSSSESKINQP
ELETRMSTRSSKAASNDKATKSINKNTVTVRGYSQESTKKKLSQKKLVHENPKANEQLNR
RSQRLQQLTEVSRRSLRSREIQGQVQAVKQSLPPTKKEQCSSTQSKSNKTSQKHVKRKVL
EVKSDSKEDENLVINEVINSPKGKKRKVEHQTACACSSQCTQGSEKCPQKTTRRDETKPV
PVTSEVKRSKMATSVVPKKNEMKKSVHTQVNTNTTLPKSPQPSVPEQSDNELEQAGKSKR
GSILQLCEEIAGEIESDNVEVKKESSQMESVKEEKPTEIKLEETSVERQILHQKETNQDV
QCNRFFPSRKTKPVKCILNGINSSAKKNSNWTKIKLSKFNSVQHNKLDSQVSPKLGLLRT
SFSPPALEMHHPVTQSTFLGTKLHDRNITCQQEKMKEINSEEVKINDITVEINKTTERAP
ENCHLANEIKPSDPPLDNQMKHSFDSASNKNFSQCLESKLENSPVENVTAASTLLSQAKI
DTGENKFPGSAPQQHSILSNQTSKSSDNRETPRNHSLPKCNSHLEITIPKDLKLKEAEKT
DEKQLIIDAGQKRFGAVSCNVCGMLYTASNPEDETQHLLFHNQFISAVKYVGWKKERILA
EYPDGRIIMVLPEDPKYALKKVDEIREMVDNDLGFQQAPLMCYSRTKTLLFISNDKKVVG
CLIAEHIQWGYRVIEEKLPVIRSEEEKVRFERQKAWCCSTLPEPAICGISRIWVFSMMRR
KKIASRMIECLRSNFIYGSYLSKEEIAFSDPTPDGKLFATQYCGTGQFLVYNFINGQNST
|
| Enzyme 17 Number of Residues |
840 |
| Enzyme 17 Molecular Weight |
94982.2 |
| Enzyme 17 Theoretical pI |
9.73 |
| Enzyme 17 GO Classification |
| Function |
- DNA binding
- DNA polymerase activity
- DNA-directed DNA polymerase activity
- binding
- catalytic activity
- damaged DNA binding
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- DNA metabolic process
- DNA repair
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Involved in damaged DNA binding |
| Enzyme 17 Specific Function |
Acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. Acts by mediating the acetylation of cohesin component SMC3 |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
Not Available |
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
116235478  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q5FWF5  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
ESCO1_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>2523 bp
ATGATGTCCATTCAGGAGAAATCAAAAGAGAATTCCTCCAAAGTTACTAAAAAAAGTGAC
GATAAGAATTCAGAAACAGAAATTCAGGATTCTCAAAAGAATCTAGCAAAAAAATCAGGT
CCAAAGGAGACTATAAAATCACAGGCTAAATCTTCCAGTGAAAGTAAAATAAATCAGCCA
GAATTGGAAACACGCATGAGTACAAGGTCATCAAAGGCAGCATCTAATGATAAAGCTACT
AAATCCATTAATAAAAATACGGTGACTGTGAGGGGATATTCACAAGAATCTACAAAAAAG
AAATTATCTCAGAAAAAATTAGTACATGAAAACCCTAAAGCAAATGAACAGCTTAACCGG
AGATCACAAAGGCTACAACAATTAACAGAGGTTTCAAGAAGGTCGTTACGCAGTAGAGAA
ATTCAGGGTCAAGTTCAAGCAGTTAAACAGAGTTTGCCACCAACTAAAAAAGAGCAGTGT
AGCAGTACTCAGAGTAAATCTAATAAAACAAGTCAAAAACATGTGAAGAGAAAAGTACTG
GAAGTAAAGTCTGACTCTAAAGAAGATGAAAATCTAGTAATTAATGAAGTAATAAATTCT
CCCAAAGGGAAAAAACGCAAGGTAGAACATCAGACAGCTTGTGCTTGTAGTTCTCAATGC
ACGCAAGGATCTGAAAAGTGTCCTCAGAAGACTACTAGAAGAGACGAAACGAAACCTGTG
CCTGTAACTTCTGAGGTGAAAAGATCAAAAATGGCTACTTCAGTGGTCCCGAAAAAGAAT
GAGATGAAGAAGTCGGTTCATACACAAGTGAATACTAACACAACACTCCCAAAAAGTCCA
CAGCCATCAGTGCCTGAACAAAGTGATAATGAGCTGGAGCAAGCAGGAAAGAGCAAACGA
GGTAGTATTCTCCAGCTCTGTGAAGAAATTGCTGGTGAAATTGAGTCAGATAATGTAGAG
GTAAAAAAGGAATCTTCACAAATGGAAAGTGTAAAGGAAGAAAAGCCCACAGAAATAAAA
TTGGAAGAGACCAGTGTTGAAAGACAAATACTTCATCAGAAGGAAACAAATCAGGATGTG
CAATGTAATCGTTTTTTCCCAAGTAGAAAAACAAAGCCTGTGAAATGTATACTAAATGGA
ATAAACAGCTCAGCCAAGAAGAACTCCAACTGGACTAAAATTAAACTCTCAAAATTTAAC
TCTGTGCAGCACAATAAGTTGGACTCTCAAGTTTCCCCTAAATTAGGCTTATTACGAACC
AGTTTTTCACCACCAGCTTTAGAAATGCATCATCCAGTGACTCAAAGTACGTTTTTAGGG
ACAAAGCTACATGATAGAAATATAACTTGCCAGCAGGAAAAAATGAAAGAAATTAATTCT
GAAGAAGTGAAAATTAATGATATTACAGTAGAAATTAATAAAACCACAGAAAGGGCTCCT
GAAAATTGTCATTTGGCCAATGAGATAAAACCTTCTGACCCACCATTGGATAATCAGATG
AAACATTCTTTTGATTCAGCATCAAATAAGAATTTCAGCCAATGTTTGGAATCCAAGCTA
GAAAACAGTCCAGTGGAAAATGTTACTGCTGCTTCGACTCTGCTCAGTCAAGCAAAAATT
GATACAGGAGAGAATAAATTTCCAGGTTCAGCTCCCCAACAGCATAGTATTCTCAGTAAC
CAGACATCTAAAAGCAGTGATAACAGGGAGACACCACGAAATCATTCTTTGCCTAAGTGT
AATTCCCATTTGGAGATAACAATTCCAAAGGACTTGAAACTAAAAGAAGCAGAGAAAACT
GATGAAAAACAGTTGATTATAGATGCAGGACAAAAAAGATTTGGAGCAGTTTCTTGTAAT
GTTTGTGGAATGCTGTATACAGCTTCAAATCCAGAAGATGAAACACAGCATCTGCTTTTC
CACAACCAGTTTATAAGTGCTGTTAAATATGTGGGCTGGAAGAAAGAAAGAATTCTGGCT
GAATACCCTGATGGCAGGATAATAATGGTTCTTCCTGAAGACCCAAAGTATGCCCTGAAA
AAGGTTGACGAGATTAGAGAGATGGTTGACAATGATTTAGGTTTTCAACAGGCTCCACTA
ATGTGCTATTCCAGAACTAAAACACTTCTCTTCATTTCCAATGACAAAAAAGTAGTTGGC
TGCCTAATTGCGGAACATATCCAATGGGGCTACAGAGTTATAGAAGAGAAACTTCCAGTT
ATCAGGTCAGAAGAAGAAAAAGTCAGATTTGAAAGGCAAAAAGCCTGGTGCTGCTCAACA
TTACCAGAGCCTGCAATCTGCGGGATCAGTCGAATATGGGTATTCAGCATGATGCGTCGG
AAGAAAATTGCTTCTCGCATGATTGAATGCCTAAGGAGTAACTTTATATATGGCTCATAT
TTGAGCAAAGAAGAAATTGCTTTCTCAGATCCCACTCCTGATGGAAAGCTGTTTGCAACA
CAGTACTGTGGCACTGGTCAATTTCTGGTATATAATTTTATTAATGGACAGAATAGCACG
TAA
|
| Enzyme 17 GenBank Gene ID |
NM_052911.2  |
| Enzyme 17 GeneCard ID |
ESCO1  |
| Enzyme 17 GenAtlas ID |
ESCO1  |
| Enzyme 17 HGNC ID |
HGNC:24645  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
18q11.2 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 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
]
- 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
]
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| Enzyme 17 Metabolite References |
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