We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for Glycerol 3-phosphate (HMDB00126)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:42
Accession Number HMDB00126
Secondary Accession Numbers HMDB02722
Common Name Glycerol 3-phosphate
Description Glycerol 3-phosphate is a chemical intermediate in the glycolysis metabolic pathway. It is commonly confused with the similarly named glycerate 3-phosphate or glyceraldehyde 3-phosphate. Glycerol 3-phosphate is produced from glycerol, the triose sugar backbone of triglycerides and glycerophospholipids, by the enzyme glycerol kinase. Glycerol 3-phospate may then be converted by dehydrogenation to dihydroxyacetone phosphate (DHAP) by the enzyme glycerol-3-phosphate dehydrogenase. DHAP can then be rearranged into glyceraldehyde 3-phosphate (GA3P) by triose phosphate isomerase (TIM), and feed into glycolysis. The glycerol 3-phosphate shuttle is used to rapidly regenerate NAD+ in brain and skeletal muscle cells of mammals (wikipedia).
Synonyms
  1. 1-(dihydrogen phosphate) Glycerol
  2. 1-Glycerophosphate
  3. 1-Glycerophosphorate
  4. 1-Glycerophosphoric acid
  5. 3-Glycerophosphate
  6. DL-Glycerol 1-phosphate
  7. DL-Glycerol 3-phosphate
  8. DL-a-Glycerol phosphate
  9. DL-a-Glycerophosphate
  10. DL-a-Glycerophosphorate
  11. DL-a-Glycerophosphoric acid
  12. DL-a-Glyceryl phosphate
  13. Glycerol 1-phosphate
  14. Glycerol a-phosphate
  15. Glycerol monophosphate
  16. Glycerophosphate
  17. Glycerophosphorate
  18. Glycerophosphoric acid
  19. Glycerophosphoric acid I
  20. Glyceryl phosphate
  21. Glyceryl phosphic acid
  22. a-Glycerophosphate
  23. a-Glycerophosphorate
  24. a-Glycerophosphoric acid
  25. a-Phosphoglycerol
  26. dihydrogen a-glycerophosphate
  27. DL-alpha-Glycerol phosphate
  28. DL-alpha-Glycerophosphate
  29. DL-alpha-Glycerophosphorate
  30. DL-alpha-Glycerophosphoric acid
  31. DL-alpha-Glyceryl phosphate
  32. alpha-Glycerophosphate
  33. alpha-Glycerophosphorate
  34. alpha-Glycerophosphoric acid
  35. alpha-Phosphoglycerol
  36. sn-Gro-1-P
  37. sn-glycerol 3-phosphate
Chemical IUPAC Name 1,2,3-Propanetriol, 1-(dihydrogen phosphate)
Chemical Formula C3H9O6P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellaneous
Class
  • Acyl Phosphates
Sub Class
  • Glycerophosphates
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • phosphoric acid ester
Biofunction
  • Component of Glycerolipid metabolism
  • Component of Glycerophospholipid metabolism
Application
Source
  • Endogenous
Average Molecular Weight 172.074
Monoisotopic Molecular Weight 172.013672
Isomeric SMILES OC[C@@H](O)COP(O)(O)=O
Canonical SMILES OCC(O)COP(O)(O)=O
KEGG Compound ID C00093 Link Image
BioCyc ID GLYCEROL-3P Link Image
BiGG ID 137383 Link Image
Wikipedia Link Glycerol 3-phosphate Link Image
NuGOwiki Link HMDB00126 Link Image
Metagene Link HMDB00126 Link Image
METLIN ID 5161 Link Image
PubChem Compound 439162 Link Image
PubChem Substance 830628 Link Image
ChEBI ID Not Available
CAS Registry Number 57-03-4
InChI Identifier InChI=1/C3H9O6P/c4-1-3(5)2-9-10(6,7)8/h3-5H,1-2H2,(H2,6,7,8)/t3-/m1/s1
Synthesis Reference Rios-Mercadillo, Victor M.; Whitesides, George M. Enzymic synthesis of sn-glycerol 3-phosphate. Journal of the American Chemical Society (1979), 101(19), 5828-9.
Melting Point (Experimental) 102-104oCC
Experimental Water Solubility 1000.0 mg/mL [MERCK INDEX (1996)] Source: PhysProp
Predicted Water Solubility 30.599998 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.84 [Predicted by ALOGPS]; -3.1 [Predicted by PubChem via XLOGP]; -1.93 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • mitochondria
Biofluid Location
  • Blood
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 30.0 +/- 3.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Glycerol Phosphate Shuttle SMP00124 Link Image
Glycerolipid Metabolism SMP00039 Link Image map00561 Link Image
Mitochondrial Electron Transport Chain SMP00355 Link Image map00190 Link Image
Phospholipid Biosynthesis SMP00025 Link Image map00564 Link Image
General References
  1. Slomiany BL, Piotrowski J, Mojtahed H, Slomiany A: Ebrotidine effect on the proteolytic and lipolytic activities of Helicobacter pylori. Gen Pharmacol. 1992 Mar;23(2):203-6. [PubMed Link Image]
  2. Guminski T: Some glycolytic enzymes in normal cerebrospinal fluid, brain tissue and blood plasma of infants. Clin Chim Acta. 1976 Aug 16;71(1):61-6. [PubMed Link Image]
  3. Wikipedia Link Image
Metabolic Enzymes
  1. Glycerol-3-phosphate dehydrogenase, mitochondrial
  2. Glycerol kinase 2
  3. Glycerol kinase
  4. Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic
  5. Glycerol-3-phosphate acyltransferase 1, mitochondrial
  6. Putative glycerol kinase 3
  7. CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
  8. Glycerol-3-phosphate dehydrogenase 1-like protein
  9. Putative uncharacterized protein DKFZp451B1115
  10. cDNA FLJ75492, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2
  11. N-acetyltransferase ESCO1 variant 1 (Establishment of cohesion 1 homolog 1 (S. cerevisiae), isoform CRA_b)
  12. Glycerophosphodiester phosphodiesterase 1
  13. Putative uncharacterized protein DKFZp451P0819
  14. cDNA, FLJ93716, Homo sapiens glycerol kinase (GK), mRNA
  15. Glycerol-3-phosphate acyltransferase 2, mitochondrial
  16. Putative glycerol kinase 5
  17. N-acetyltransferase ESCO1
Enzyme 1 [top]
Enzyme 1 ID 5429
Enzyme 1 Name Glycerol-3-phosphate dehydrogenase, mitochondrial
Enzyme 1 Synonyms
  1. GPD-M
  2. GPDH-M
  3. 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
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 285002233 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P43304 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GPDM_HUMAN Link Image
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 Link Image
Enzyme 1 GeneCard ID GPD2 Link Image
Enzyme 1 GenAtlas ID GPD2 Link Image
Enzyme 1 HGNC ID HGNC:4456 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q24.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6116
Enzyme 2 Name Glycerol kinase 2
Enzyme 2 Synonyms
  1. GK 2
  2. Glycerokinase 2
  3. ATP:glycerol 3-phosphotransferase 2
  4. 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
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 158257914 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q14410 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name GLPK2_HUMAN Link Image
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 Link Image
Enzyme 2 GeneCard ID GK2 Link Image
Enzyme 2 GenAtlas ID GK2 Link Image
Enzyme 2 HGNC ID HGNC:4291 Link Image
Enzyme 2 Chromosome Location 4
Enzyme 2 Locus 4q13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6117
Enzyme 3 Name Glycerol kinase
Enzyme 3 Synonyms
  1. GK
  2. Glycerokinase
  3. 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
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 5834428 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P32189 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GLPK_HUMAN Link Image
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 Link Image
Enzyme 3 GeneCard ID GK Link Image
Enzyme 3 GenAtlas ID GK Link Image
Enzyme 3 HGNC ID HGNC:4289 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
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
  1. GPD-C
  2. 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
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 21594877 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P21695 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GPDA_HUMAN Link Image
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 Link Image
Enzyme 4 GeneCard ID GPD1 Link Image
Enzyme 4 GenAtlas ID GPD1 Link Image
Enzyme 4 HGNC ID HGNC:4455 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 12q12-q13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
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
  1. 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
  • metabolic 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
  • None
Enzyme 5 Transmembrane Regions
  • 472-494 575-593
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 190358539 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9HCL2 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name GPAT1_HUMAN Link Image
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 Link Image
Enzyme 5 GeneCard ID GPAM Link Image
Enzyme 5 GenAtlas ID GPAM Link Image
Enzyme 5 HGNC ID HGNC:24865 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 10q25.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 8487
Enzyme 6 Name Putative glycerol kinase 3
Enzyme 6 Synonyms
  1. GK 3
  2. Glycerokinase 3
  3. ATP:glycerol 3-phosphotransferase 3
  4. 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
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 515029 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q14409 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name GLPK3_HUMAN Link Image
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 Link Image
Enzyme 6 GeneCard ID GK3P Link Image
Enzyme 6 GenAtlas ID GK3P Link Image
Enzyme 6 HGNC ID HGNC:4292 Link Image
Enzyme 6 Chromosome Location 4
Enzyme 6 Locus 4q32.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
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
  1. Phosphatidylglycerophosphate synthase 1
  2. 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
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID Q32NB8 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PGPS1_HUMAN Link Image
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 Link Image
Enzyme 7 GeneCard ID PGS1 Link Image
Enzyme 7 GenAtlas ID PGS1 Link Image
Enzyme 7 HGNC ID HGNC:30029 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 17q25.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
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
  1. 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
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 158259077 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q8N335 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name GPD1L_HUMAN Link Image
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 Link Image
Enzyme 8 GeneCard ID GPD1L Link Image
Enzyme 8 GenAtlas ID GPD1L Link Image
Enzyme 8 HGNC ID HGNC:28956 Link Image
Enzyme 8 Chromosome Location 3
Enzyme 8 Locus 3p22.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
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
  • metabolic 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
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 30268347 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q86T70 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q86T70_HUMAN Link Image
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 Link Image
Enzyme 9 GeneCard ID DKFZp451B1115 Link Image
Enzyme 9 GenAtlas ID DKFZp451B1115 Link Image
Enzyme 9 HGNC ID HGNC:24865 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
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
  1. mitochondrial
  2. GPD2, mRNA
  3. Glycerol-3-phosphate dehydrogenase 2
  4. Mitochondrial, isoform CRA_b
  5. cDNA FLJ78257, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2
  6. mitochondrial
  7. 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
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 158255566 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID A8K4V0 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name A8K4V0_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AK291065 Link Image
Enzyme 10 GeneCard ID A8K4V0 Link Image
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 Link Image
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
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID B0YJ11 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B0YJ11_HUMAN Link Image
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 Link Image
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 Link Image
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
  1. Membrane-interacting protein of RGS16
  2. 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
  • None
Enzyme 12 Transmembrane Regions
  • 4-24 248-268
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 7637877 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9NZC3 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name GDE1_HUMAN Link Image
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 Link Image
Enzyme 12 GeneCard ID GDE1 Link Image
Enzyme 12 GenAtlas ID GDE1 Link Image
Enzyme 12 HGNC ID HGNC:29644 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 16p12-p11.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
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
  • cell
  • membrane
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
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 30268383 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q86TA3 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name Q86TA3_HUMAN Link Image
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 Link Image
Enzyme 13 GeneCard ID Q86TA3 Link Image
Enzyme 13 GenAtlas ID DKFZp451P0819 Link Image
Enzyme 13 HGNC ID HGNC:24865 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
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
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID B2R833 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name B2R833_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID AK313215 Link Image
Enzyme 14 GeneCard ID B2R833 Link Image
Enzyme 14 GenAtlas ID GK Link Image
Enzyme 14 HGNC ID HGNC:4289 Link Image
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
  1. GPAT-2
  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
  • metabolic 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
  • None
Enzyme 15 Transmembrane Regions
  • 159-179 452-472
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 116812614 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q6NUI2 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name GPAT2_HUMAN Link Image
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 Link Image
Enzyme 15 GeneCard ID GPAT2 Link Image
Enzyme 15 GenAtlas ID GPAT2 Link Image
Enzyme 15 HGNC ID HGNC:27168 Link Image
Enzyme 15 Chromosome Location 2
Enzyme 15 Locus 2q11.1
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 16857
Enzyme 16 Name Putative glycerol kinase 5
Enzyme 16 Synonyms
  1. GK 5
  2. Glycerokinase 5
  3. 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
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 88196792 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q6ZS86 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name GLPK5_HUMAN Link Image
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 Link Image
Enzyme 16 GeneCard ID GK5 Link Image
Enzyme 16 GenAtlas ID GK5 Link Image
Enzyme 16 HGNC ID HGNC:28635 Link Image
Enzyme 16 Chromosome Location 3
Enzyme 16 Locus 3q23
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 21018
Enzyme 17 Name N-acetyltransferase ESCO1
Enzyme 17 Synonyms
  1. CTF7 homolog 1
  2. Establishment factor-like protein 1
  3. EFO1p
  4. hEFO1
  5. Establishment of cohesion 1 homolog 1
  6. ECO1 homolog 1
  7. 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
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 116235478 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q5FWF5 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name ESCO1_HUMAN Link Image
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 Link Image
Enzyme 17 GeneCard ID ESCO1 Link Image
Enzyme 17 GenAtlas ID ESCO1 Link Image
Enzyme 17 HGNC ID HGNC:24645 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 18q11.2
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. Bellows AM, Kenna MA, Cassimeris L, Skibbens RV: Human EFO1p exhibits acetyltransferase activity and is a unique combination of linker histone and Ctf7p/Eco1p chromatid cohesion establishment domains. Nucleic Acids Res. 2003 Nov 1;31(21):6334-43. [PubMed Link Image]
  6. Hou F, Zou H: Two human orthologues of Eco1/Ctf7 acetyltransferases are both required for proper sister-chromatid cohesion. Mol Biol Cell. 2005 Aug;16(8):3908-18. Epub 2005 Jun 15. [PubMed Link Image]
  7. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  9. Zhang J, Shi X, Li Y, Kim BJ, Jia J, Huang Z, Yang T, Fu X, Jung SY, Wang Y, Zhang P, Kim ST, Pan X, Qin J: Acetylation of Smc3 by Eco1 is required for S phase sister chromatid cohesion in both human and yeast. Mol Cell. 2008 Jul 11;31(1):143-51. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available