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Human Metabolome Database Version 2.5

 

Showing metabocard for TG(16:0/16:0/16:0)[iso] (HMDB05356)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-12-06 15:50:25
Update Date 2010-04-25 00:07:46
Accession Number HMDB05356
Secondary Accession Numbers Not Available
Common Name TG(16:0/16:0/16:0)[iso]
Description TG(16:0/16:0/16:0) or Tripalmitin is a monoacid triglyceride. Triglycerides (TGs) are also known as triacylglycerols or triacylglycerides. TGs are fatty acid triesters of glycerol and may be divided into three general types with respect to their acyl substituents. They are simple or monoacid if they contain only one type of fatty acid, diacid if they contain two types of fatty acids and triacid if three different acyl groups. Chain lengths of the fatty acids in naturally occurring triglycerides can be of varying lengths and saturations but 16, 18 and 20 carbons are the most common. TGs are the main constituent of vegetable oil and animal fats. TGs are major components of very low density lipoprotein (VLDL) and chylomicrons, play an important role in metabolism as energy sources and transporters of dietary fat. They contain more than twice the energy (9 kcal/g) of carbohydrates and proteins. In the intestine, triglycerides are split into glycerol and fatty acids (this process is called lipolysis) (with the help of lipases and bile secretions), which can then move into blood vessels. The triglycerides are rebuilt in the blood from their fragments and become constituents of lipoproteins, which deliver the fatty acids to and from fat cells among other functions. Various tissues can release the free fatty acids and take them up as a source of energy. Fat cells can synthesize and store triglycerides. When the body requires fatty acids as an energy source, the hormone glucagon signals the breakdown of the triglycerides by hormone-sensitive lipase to release free fatty acids. As the brain cannot utilize fatty acids as an energy source, the glycerol component of triglycerides can be converted into glucose for brain fuel when it is broken down. (www.cyberlipid.org, www.wikipedia.org) TAGs can serve as fatty acid stores in all cells, but primarily in adipocytes of adipose tissue. The major building block for the synthesis of triacylglycerides, in non-adipose tissue, is glycerol. Adipocytes lack glycerol kinase and so must use another route to TAG synthesis. Specifically, dihydroxyacetone phosphate (DHAP), which is produced during glycolysis, is the precursor for TAG synthesis in adipose tissue. DHAP can also serve as a TAG precursor in non-adipose tissues, but does so to a much lesser extent than glycerol. The use of DHAP for the TAG backbone depends on whether the synthesis of the TAGs occurs in the mitochondria and ER or the ER and the peroxisomes. The ER/mitochondria pathway requires the action of glycerol-3-phosphate dehydrogenase to convert DHAP to glycerol-3-phosphate. Glycerol-3-phosphate acyltransferase then esterifies a fatty acid to glycerol-3-phosphate thereby generating lysophosphatidic acid. The ER/peroxisome reaction pathway uses the peroxisomal enzyme DHAP acyltransferase to acylate DHAP to acyl-DHAP which is then reduced by acyl-DHAP reductase. The fatty acids that are incorporated into TAGs are activated to acyl-CoAs through the action of acyl-CoA synthetases. Two molecules of acyl-CoA are esterified to glycerol-3-phosphate to yield 1,2-diacylglycerol phosphate (also known as phosphatidic acid). The phosphate is then removed by phosphatidic acid phosphatase (PAP1), to generate 1,2-diacylglycerol. This diacylglycerol serves as the substrate for addition of the third fatty acid to make TAG. Intestinal monoacylglycerols, derived from dietary fats, can also serve as substrates for the synthesis of 1,2-diacylglycerols.
Synonyms
  1. Tripalmitoylglycerol
  2. Tripalmitate
  3. Triglyceryl palmitate
  4. Triglyceride PPP
  5. Spezialfett 116
  6. Palmitic triglyceride
  7. Glyceryl tripalmitate
  8. Glyceryl trihexadecanoate
  9. Glycerol tripalmitate
  10. Glycerin tripalmitate
  11. Dynosan 114
  12. Dynasan 116
  13. Barolub LCD
  14. 1,2,3-trihexadecanoyl-sn-glycerol
  15. Tripalmitin
  16. Glyceryl trihexadecanoic acid
Chemical IUPAC Name 1,2,3-trihexadecanoyl-sn-glycerol
Chemical Formula C51H98O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Lipids
Class
  • Glycerolipids
Sub Class
  • Triacylglycerols
Family
  • Mammalian Metabolite
Species
  • carboxylic acid ester
Biofunction
  • Membrane component
Application
Source
  • Endogenous
Average Molecular Weight 807.320
Monoisotopic Molecular Weight 806.736328
Isomeric SMILES CCCCCCCCCCCCCCCC(=O)OCC(COC(=O)CCCCCCCCCCCCCCC)OC(=O)CCCCCCCCCCCCCCC
Canonical SMILES CCCCCCCCCCCCCCCC(=O)OCC(COC(=O)CCCCCCCCCCCCCCC)OC(=O)CCCCCCCCCCCCCCC
KEGG Compound ID Not Available
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB05356 Link Image
Metagene Link HMDB05356 Link Image
METLIN ID 3857 Link Image
PubChem Compound 11147 Link Image
PubChem Substance 10485765 Link Image
ChEBI ID Not Available
CAS Registry Number 555-44-2
InChI Identifier InChI=1/C51H98O6/c1-4-7-10-13-16-19-22-25-28-31-34-37-40-43-49(52)55-46-48(57-51(54)45-42-39-36-33-30-27-24-21-18-15-12-9-6-3)47-56-50(53)44-41-38-35-32-29-26-23-20-17-14-11-8-5-2/h48H,4-47H2,1-3H3
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.16e-05 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 10.59 [Predicted by ALOGPS]; 19.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
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 (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location
  • Blood
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 8.66 +/- 3.324 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal (Most Probable)
Comments Not Available
References
  • Psychogios N, Hau DD, Peng J, Guo AC, Mandal R, Bouatra S, Sinelnikov I, Krishnamurthy R, Eisner R, Gautam B, Young N, Xia J, Knox C, Dong E, Huang P, Hollander Z, Pedersen TL, Smith SR, Bamforth F, Greiner R, McManus B, Newman JW, Goodfriend T, Wishart DS: The human serum metabolome. PLoS One. 2011 Feb 16;6(2):e16957. [PubMed Link Image]
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Biofluid Blood
Value 123.344 +/- 31.645 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal (Upper Limit)
Comments Not Available
References
  • Psychogios N, Hau DD, Peng J, Guo AC, Mandal R, Bouatra S, Sinelnikov I, Krishnamurthy R, Eisner R, Gautam B, Young N, Xia J, Knox C, Dong E, Huang P, Hollander Z, Pedersen TL, Smith SR, Bamforth F, Greiner R, McManus B, Newman JW, Goodfriend T, Wishart DS: The human serum metabolome. PLoS One. 2011 Feb 16;6(2):e16957. [PubMed Link Image]
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Glycerolipid Metabolism SMP00039 Link Image map00561 Link Image
General References Not Available
Metabolic Enzymes
  1. Pancreatic triacylglycerol lipase
  2. Hepatic triacylglycerol lipase
  3. Pancreatic lipase-related protein 1
  4. Patatin-like phospholipase domain-containing protein 3
  5. Gastric triacylglycerol lipase
  6. Endothelial lipase
  7. Bile salt-activated lipase
  8. Diacylglycerol O-acyltransferase 1
  9. Pancreatic lipase-related protein 2
  10. Lipoprotein lipase
  11. Monoglyceride lipase
  12. Liver carboxylesterase 1
  13. Hormone-sensitive lipase
  14. Microsomal triglyceride transfer protein large subunit
  15. Protein disulfide-isomerase
  16. 2-acylglycerol O-acyltransferase 2
  17. Patatin-like phospholipase domain-containing protein 4
  18. Diacylglycerol O-acyltransferase 2
  19. 2-acylglycerol O-acyltransferase 1
  20. 2-acylglycerol O-acyltransferase 3
  21. Phospholipase B1, membrane-associated
  22. Glycerol-3-phosphate acyltransferase 3
  23. Patatin-like phospholipase domain-containing protein 2
  24. Pancreatic lipase-related protein 3
  25. Perilipin-4
  26. Apolipoprotein C-II
Enzyme 1 [top]
Enzyme 1 ID 5453
Enzyme 1 Name Pancreatic triacylglycerol lipase
Enzyme 1 Synonyms
  1. PL
  2. Pancreatic lipase
Enzyme 1 Gene Name PNLIP
Enzyme 1 Protein Sequence >Pancreatic triacylglycerol lipase
MLPLWTLSLLLGAVAGKEVCYERLGCFSDDSPWSGITERPLHILPWSPKDVNTRFLLYTN
ENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESVNCIC
VDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGR
RTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDGAPIVPNLGFGMSQVVGH
LDFFPNGGVEMPGCKKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGF
PCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNDVGQKFYLDTGDASNFARWRYKVS
VTLSGKKVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWY
NNVINPTLPRVGASKIIVETNVGKQFNFCSPETVREEVLLTLTPC
Enzyme 1 Number of Residues 465
Enzyme 1 Molecular Weight 51156.5
Enzyme 1 Theoretical pI 6.72
Enzyme 1 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 1 General Function Involved in catalytic activity
Enzyme 1 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-16
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID P16233 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name LIPP_HUMAN Link Image
Enzyme 1 PDB ID 1N8S Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1398 bp
ATGCTGCCACTTTGGACTCTTTCACTGCTGCTGGGAGCAGTAGCAGGAAAAGAAGTTTGC
TACGAAAGACTCGGCTGCTTCAGTGATGACTCCCCATGGTCAGGAATTACGGAAAGACCC
CTCCATATATTGCCTTGGTCTCCAAAAGATGTCAACACCCGCTTCCTCCTATATACTAAT
GAGAACCCAAACAACTTTCAAGAAGTTGCCGCAGATTCATCAAGCATCAGTGGCTCCAAT
TTCAAAACAAATAGAAAAACTCGCTTTATTATTCATGGATTCATAGACAAGGGAGAAGAA
AACTGGCTGGCCAATGTGTGCAAGAATCTGTTCAAGGTGGAAAGTGTGAACTGTATCTGT
GTGGACTGGAAAGGTGGCTCCCGAACTGGATACACACAAGCCTCGCAGAACATCAGGATC
GTGGGAGCAGAAGTGGCATATTTTGTTGAATTTCTTCAGTCGGCGTTCGGTTACTCACCT
TCCAACGTGCATGTCATTGGCCACAGCCTGGGTGCCCACGCTGCTGGGGAGGCTGGAAGG
AGAACCAATGGGACCATTGGACGCATCACAGGGTTGGACCCAGCAGAACCTTGCTTTCAG
GGCACACCTGAATTAGTCCGATTGGACCCCAGCGATGCCAAATTTGTGGATGTAATTCAC
ACGGATGGTGCCCCCATAGTCCCCAATTTGGGGTTTGGAATGAGCCAAGTCGTGGGCCAC
CTAGATTTCTTTCCAAATGGAGGAGTGGAAATGCCTGGATGTAAAAAGAACATTCTCTCT
CAGATTGTGGACATAGACGGAATCTGGGAAGGGACTCGAGACTTTGCGGCCTGTAATCAC
TTAAGAAGCTACAAATATTACACTGATAGCATCGTCAACCCTGATGGCTTTGCTGGATTC
CCCTGTGCCTCTTACAACGTCTTCACTGCAAACAAGTGTTTCCCTTGTCCAAGTGGAGGC
TGCCCACAGATGGGTCACTATGCTGATAGATATCCTGGGAAAACAAATGATGTGGGCCAG
AAATTTTATCTAGACACTGGTGATGCCAGTAATTTTGCACGTTGGAGGTATAAGGTATCT
GTCACACTGTCTGGAAAAAAGGTTACAGGACACATACTAGTTTCTTTGTTCGGAAATAAA
GGAAACTCTAAGCAGTATGAAATTTTCAAGGGCACTCTCAAACCAGATAGTACTCATTCC
AATGAATTTGACTCAGATGTGGATGTTGGGGACTTGCAGATGGTTAAATTTATTTGGTAT
AACAATGTGATCAACCCAACTTTACCTAGAGTGGGAGCATCCAAGATTATAGTGGAGACA
AATGTTGGAAAACAGTTCAACTTCTGTAGTCCAGAAACCGTCAGGGAGGAAGTTCTGCTC
ACCCTCACACCGTGTTAG
Enzyme 1 GenBank Gene ID J05125 Link Image
Enzyme 1 GeneCard ID PNLIP Link Image
Enzyme 1 GenAtlas ID PNLIP Link Image
Enzyme 1 HGNC ID HGNC:9155 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 10q26.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Lowe ME, Rosenblum JL, Strauss AW: Cloning and characterization of human pancreatic lipase cDNA. J Biol Chem. 1989 Nov 25;264(33):20042-8. [PubMed Link Image]
  2. Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [PubMed Link Image]
  3. Sims HF, Jennens ML, Lowe ME: The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family. Gene. 1993 Sep 15;131(2):281-5. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, 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]
  5. Winkler FK, D'Arcy A, Hunziker W: Structure of human pancreatic lipase. Nature. 1990 Feb 22;343(6260):771-4. [PubMed Link Image]
  6. van Tilbeurgh H, Sarda L, Verger R, Cambillau C: Structure of the pancreatic lipase-procolipase complex. Nature. 1992 Sep 10;359(6391):159-62. [PubMed Link Image]
  7. van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C: Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature. 1993 Apr 29;362(6423):814-20. [PubMed Link Image]
  8. Carriere F, Thirstrup K, Boel E, Verger R, Thim L: Structure-function relationships in naturally occurring mutants of pancreatic lipase. Protein Eng. 1994 Apr;7(4):563-9. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5458
Enzyme 2 Name Hepatic triacylglycerol lipase
Enzyme 2 Synonyms
  1. HL
  2. Hepatic lipase
  3. Lipase member C
Enzyme 2 Gene Name LIPC
Enzyme 2 Protein Sequence >Hepatic triacylglycerol lipase
MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQ
GCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLV
DWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSS
IGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGH
YDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAY
PCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQLKIQF
INQTETPIQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKW
ENSAVWANVWDTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQ
EKIFVKCEIKSKTSKRKIR
Enzyme 2 Number of Residues 499
Enzyme 2 Molecular Weight 55880.1
Enzyme 2 Theoretical pI 9.37
Enzyme 2 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 2 General Function Involved in catalytic activity
Enzyme 2 Specific Function Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin
Enzyme 2 Pathways
Enzyme 2 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-22
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 194097335 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P11150 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name LIPC_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1500 bp
ATGGACACAAGTCCCCTGTGTTTCTCCATTCTGTTGGTTTTATGCATCTTTATCCAATCA
AGTGCCCTTGGACAAAGCCTGAAACCAGAGCCATTTGGAAGAAGAGCTCAAGCTGTTGAA
ACAAACAAAACGCTGCATGAGATGAAGACCAGATTCCTGCTCTTTGGAGAAACCAATCAG
GGCTGTCAGATTCGAATCAATCATCCGGACACGTTACAGGAGTGCGGCTTCAACTCCTCC
CTGCCTCTGGTGATGATAATCCACGGGTGGTCGGTGGACGGCGTGCTAGAAAACTGGATC
TGGCAGATGGTGGCCGCGCTGAAGTCTCAGCCGGCCCAGCCAGTGAACGTGGGGCTGGTG
GACTGGATCACCCTGGCCCACGACCACTACACCATCGCCGTCCGCAACACCCGCCTTGTG
GGCAAGGAGGTCGCGGCTCTTCTCCGGTGGCTGGAGGAATCTGTGCAACTCTCTCGAAGC
CATGTTCACCTAATTGGGTACAGCCTGGGTGCACACGTGTCAGGATTTGCCGGCAGTTCC
ATCGGTGGAACGCACAAGATTGGGAGAATCACAGGGCTGGATGCCGCGGGACCTTTGTTT
GAGGGAAGTGCCCCCAGCAATCGTCTTTCTCCAGATGATGCCAATTTTGTGGATGCCATT
CATACCTTTACCCGGGAGCACATGGGCCTGAGCGTGGGCATCAAACAGCCCATAGGACAC
TATGACTTCTATCCCAACGGGGGCTCCTTCCAGCCTGGCTGCCACTTCCTAGAGCTCTAC
AGACATATTGCCCAGCACGGCTTCAATGCCATCACCCAGACCATAAAATGCTCCCACGAG
CGATCGGTGCACCTTTTCATCGACTCCTTGCTGCACGCCGGCACGCAGAGCATGGCCTAC
CCGTGTGGTGACATGAACAGCTTCAGCCAGGGCCTGTGCCTGAGCTGCAAGAAGGGCCGC
TGCAACACGCTGGGCTACCACGTCCGCCAGGAGCCGCGGAGCAAGAGCAAGAGGCTCTTC
CTCGTAACGCGAGCCCAGTCCCCCTTCAAAGTTTATCATTACCAGTTCAAGATCCAGTTC
ATCAACCAAACTGAGACACCAATACAAACAACTTTTACCATGTCACTACTCGGAACAAAA
GAGAAAATGCAGAAAATTCCCATCACTCTGGGCAAAGGAATTGCTAGTAATAAAACGTAT
TCCTTTCTTATCACGCTGGATGTGGATATCGGCGAGCTGATCATGATCAAGTTCAAGTGG
GAAAACAGTGCAGTGTGGGCCAATGTCTGGGACACGGTCCAGACCATCATCCCATGGAGC
ACAGGGCCGCGCCACTCAGGCCTCGTTCTGAAGACGATCAGAGTCAAAGCAGGAGAAACC
CAGCAAAGAATGACATTTTGTTCAGAAAACACAGATGACCTACTACTTCGCCCAACCCAG
GAAAAAATCTTCGTGAAATGTGAAATAAAGTCTAAAACATCAAAGCGAAAGATCAGATGA
Enzyme 2 GenBank Gene ID NM_000236.2 Link Image
Enzyme 2 GeneCard ID LIPC Link Image
Enzyme 2 GenAtlas ID LIPC Link Image
Enzyme 2 HGNC ID HGNC:6619 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 15q21-q23
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Martin GA, Busch SJ, Meredith GD, Cardin AD, Blankenship DT, Mao SJ, Rechtin AE, Woods CW, Racke MM, Schafer MP, et al.: Isolation and cDNA sequence of human postheparin plasma hepatic triglyceride lipase. J Biol Chem. 1988 Aug 5;263(22):10907-14. [PubMed Link Image]
  2. Stahnke G, Sprengel R, Augustin J, Will H: Human hepatic triglyceride lipase: cDNA cloning, amino acid sequence and expression in a cultured cell line. Differentiation. 1987;35(1):45-52. [PubMed Link Image]
  3. Datta S, Luo CC, Li WH, VanTuinen P, Ledbetter DH, Brown MA, Chen SH, Liu SW, Chan L: Human hepatic lipase. Cloned cDNA sequence, restriction fragment length polymorphisms, chromosomal localization, and evolutionary relationships with lipoprotein lipase and pancreatic lipase. J Biol Chem. 1988 Jan 25;263(3):1107-10. [PubMed Link Image]
  4. Cai SJ, Wong DM, Chen SH, Chan L: Structure of the human hepatic triglyceride lipase gene. Biochemistry. 1989 Nov 14;28(23):8966-71. [PubMed Link Image]
  5. Ameis D, Stahnke G, Kobayashi J, McLean J, Lee G, Buscher M, Schotz MC, Will H: Isolation and characterization of the human hepatic lipase gene. J Biol Chem. 1990 Apr 25;265(12):6552-5. [PubMed Link Image]
  6. 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]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, 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]
  8. Tiebel O, Gehrisch S, Pietzsch J, Gromeier S, Jaross W: 18 bp insertion/duplication with internal missense mutation in human hepatic lipase gene exon 3. Mutations in brief no. 181. Online. Hum Mutat. 1998;12(3):216. [PubMed Link Image]
  9. Takagi A, Ikeda Y, Mori A, Ashida Y, Yamamoto A: Identification of a BstNI polymorphism in exon 9 of the human hepatic triglyceride lipase gene. Mol Cell Probes. 1996 Aug;10(4):313-4. [PubMed Link Image]
  10. Todorova B, Kubaszek A, Pihlajamaki J, Lindstrom J, Eriksson J, Valle TT, Hamalainen H, Ilanne-Parikka P, Keinanen-Kiukaanniemi S, Tuomilehto J, Uusitupa M, Laakso M: The G-250A promoter polymorphism of the hepatic lipase gene predicts the conversion from impaired glucose tolerance to type 2 diabetes mellitus: the Finnish Diabetes Prevention Study. J Clin Endocrinol Metab. 2004 May;89(5):2019-23. [PubMed Link Image]
  11. Grarup N, Andreasen CH, Andersen MK, Albrechtsen A, Sandbaek A, Lauritzen T, Borch-Johnsen K, Jorgensen T, Schmitz O, Hansen T, Pedersen O: The -250G>A promoter variant in hepatic lipase associates with elevated fasting serum high-density lipoprotein cholesterol modulated by interaction with physical activity in a study of 16,156 Danish subjects. J Clin Endocrinol Metab. 2008 Jun;93(6):2294-9. Epub 2008 Mar 25. [PubMed Link Image]
  12. Hegele RA, Tu L, Connelly PW: Human hepatic lipase mutations and polymorphisms. Hum Mutat. 1992;1(4):320-4. [PubMed Link Image]
  13. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  14. Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5461
Enzyme 3 Name Pancreatic lipase-related protein 1
Enzyme 3 Synonyms
  1. PL-RP1
Enzyme 3 Gene Name PNLIPRP1
Enzyme 3 Protein Sequence >Pancreatic lipase-related protein 1
MLIFWTITLFLLGAAKGKEVCYEDLGCFSDTEPWGGTAIRPLKILPWSPEKIGTRFLLYT
NENPNNFQILLLSDPSTIEASNFQMDRKTRFIIHGFIDKGDESWVTDMCKKLFEVEEVNC
ICVDWKKGSQATYTQAANNVRVVGAQVAQMLDILLTEYSYPPSKVHLIGHSLGAHVAGEA
GSKTPGLSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPLIPFLGFGTNQQMG
HLDFFPNGGESMPGCKKNALSQIVDLDGIWAGTRDFVACNHLRSYKYYLESILNPDGFAA
YPCTSYKSFESDKCFPCPDQGCPQMGHYADKFAGRTSEEQQKFFLNTGEASNFARWRYGV
SITLSGRTATGQIKVALFGNKGNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLW
NNNVINPTLPKVGATKITVQKGEEKTVYNFCSEDTVREDTLLTLTPC
Enzyme 3 Number of Residues 467
Enzyme 3 Molecular Weight 51847.4
Enzyme 3 Theoretical pI 5.47
Enzyme 3 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 3 General Function Involved in catalytic activity
Enzyme 3 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-17
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 5453920 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P54315 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name LIPR1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1404 bp
ATGCTGATCTTCTGGACAATCACACTTTTCCTGCTGGGAGCAGCCAAAGGAAAAGAAGTT
TGCTATGAGGACCTCGGGTGCTTTTCTGACACTGAGCCCTGGGGCGGGACAGCAATCAGG
CCCCTGAAAATTCTCCCCTGGAGCCCTGAGAAGATCGGCACCCGCTTCCTGCTGTACACC
AATGAAAACCCAAACAACTTTCAAATTCTCCTCCTCTCTGATCCATCAACAATTGAGGCA
TCAAATTTTCAAATGGACAGAAAGACCCGGTTCATCATCCATGGCTTCATAGACAAAGGA
GATGAGAGCTGGGTGACAGACATGTGCAAGAAACTGTTCGAGGTGGAGGAGGTGAACTGC
ATCTGCGTGGACTGGAAGAAGGGCTCCCAAGCCACCTACACACAGGCTGCCAACAACGTG
CGAGTGGTGGGCGCCCAGGTGGCCCAGATGCTCGACATCCTCTTGACAGAGTATAGCTAC
CCCCCTTCCAAAGTTCACCTCATTGGCCACAGCCTGGGAGCCCACGTGGCTGGAGAGGCA
GGAAGCAAGACTCCAGGCCTGAGCAGGATTACAGGGTTGGATCCTGTAGAAGCAAGTTTC
GAGAGTACTCCTGAAGAGGTGCGACTTGATCCCTCTGATGCTGACTTTGTTGATGTGATT
CACACGGATGCAGCTCCCCTGATCCCATTCTTGGGTTTTGGAACGAACCAACAGATGGGT
CATCTTGACTTCTTCCCCAATGGAGGAGAGAGCATGCCGGGATGCAAGAAGAATGCCCTG
TCTCAGATCGTGGATCTAGATGGCATCTGGGCGGGAACCCGGGACTTTGTGGCTTGCAAT
CACCTAAGAAGCTACAAGTATTACTTGGAAAGCATCCTCAATCCCGATGGGTTTGCTGCA
TATCCCTGCACTTCCTACAAGTCCTTTGAGTCTGACAAGTGCTTCCCGTGTCCAGATCAA
GGATGCCCACAGATGGGTCACTATGCTGATAAATTTGCTGGCAGGACAAGTGAAGAGCAG
CAGAAATTCTTCTTGAACACAGGAGAGGCTAGCAATTTCGCTCGCTGGAGATATGGGGTT
TCCATCACACTGTCTGGAAGAACAGCCACTGGTCAGATCAAAGTTGCTTTGTTTGGAAAT
AAGGGAAACACTCACCAGTACAGCATCTTCAGGGGGATTCTCAAACCAGGCTCAACCCAT
TCCTATGAGTTTGATGCAAAGCTGGATGTTGGAACAATTGAGAAAGTCAAGTTTCTTTGG
AATAACAATGTGATAAATCCAACCCTCCCCAAAGTGGGTGCCACCAAGATCACTGTGCAA
AAGGGAGAAGAGAAGACAGTGTACAACTTCTGTAGCGAAGACACAGTGCGGGAAGACACG
CTGCTCACCCTCACGCCCTGCTAA
Enzyme 3 GenBank Gene ID NM_006229.2 Link Image
Enzyme 3 GeneCard ID PNLIPRP1 Link Image
Enzyme 3 GenAtlas ID PNLIPRP1 Link Image
Enzyme 3 HGNC ID HGNC:9156 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 10q25.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [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. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5464
Enzyme 4 Name Patatin-like phospholipase domain-containing protein 3
Enzyme 4 Synonyms
  1. Acylglycerol O-acyltransferase
  2. Adiponutrin
  3. Calcium-independent phospholipase A2-epsilon
  4. iPLA2-epsilon
Enzyme 4 Gene Name PNPLA3
Enzyme 4 Protein Sequence >Patatin-like phospholipase domain-containing protein 3
MYDAERGWSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGI
PLEQTLQVLSDLVRKARSRNIGIFHPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTR
VSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGGVSDNVPFIDAKT
TITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLR
GYLDAFRFLEEKGICNRPQPGLKSSSEGMDPEVAMPSWANMSLDSSPESAALAVRLEGDE
LLDHLRLSILPWDESILDTLSPRLATALSEEMKDKGGYMSKICNLLPIRIMSYVMLPCTL
PVESAIAIVQRLVTWLPDMPDDVLWLQWVTSQVFTRVLMCLLPASRSQMPVSSQQASPCT
PEQDWPCWTPCSPKGCPAETKAEATPRSILRSSLNFFLGNKVPAGAEGLSTFPSFSLEKS
L
Enzyme 4 Number of Residues 481
Enzyme 4 Molecular Weight 52864.6
Enzyme 4 Theoretical pI 6.68
Enzyme 4 GO Classification
Function
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 4 General Function Involved in metabolic process
Enzyme 4 Specific Function Multifunctional enzyme which has both triacylglycerol lipase and acylglycerol O-acyltransferase activities
Enzyme 4 Pathways
Enzyme 4 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 42-62
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 17059636 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9NST1 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PLPL3_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1446 bp
ATGTACGACGCAGAGCGCGGCTGGAGCTTGTCCTTCGCGGGCTGCGGCTTCCTGGGCTTC
TACCACGTCGGGGCGACCCGCTGCCTGAGCGAGCACGCCCCGCACCTCCTCCGCGACGCG
CGCATGTTGTTCGGCGCTTCGGCCGGGGCGTTGCACTGCGTCGGCGTCCTCTCCGGTATC
CCGCTGGAGCAGACTCTGCAGGTCCTCTCAGATCTTGTGCGGAAGGCCAGGAGTCGGAAC
ATTGGCATCTTCCATCCATCCTTCAACTTAAGCAAGTTCCTCCGACAGGGTCTCTGCAAA
TGCCTCCCGGCCAATGTCCACCAGCTCATCTCCGGCAAAATAGGCATCTCTCTTACCAGA
GTGTCTGATGGGGAAAACGTTCTGGTGTCTGACTTTCGGTCCAAAGACGAAGTCGTGGAT
GCCTTGGTATGTTCCTGCTTCATCCCCTTCTACAGTGGCCTTATCCCTCCTTCCTTCAGA
GGCGTGCGATATGTGGATGGAGGAGTGAGTGACAACGTACCCTTCATTGATGCCAAAACA
ACCATCACCGTGTCCCCCTTCTATGGGGAGTACGACATCTGCCCTAAAGTCAAGTCCACG
AACTTTCTTCATGTGGACATCACCAAGCTCAGTCTACGCCTCTGCACAGGGAACCTCTAC
CTTCTCTCGAGAGCTTTTGTCCCCCCGGATCTCAAGGTGCTGGGAGAGATATGCCTTCGA
GGATATTTGGATGCATTCAGGTTCTTGGAAGAGAAGGGCATCTGCAACAGGCCCCAGCCA
GGCCTGAAGTCATCCTCAGAAGGGATGGATCCTGAGGTCGCCATGCCCAGCTGGGCAAAC
ATGAGTCTGGATTCTTCCCCGGAGTCGGCTGCCTTGGCTGTGAGGCTGGAGGGAGATGAG
CTGCTAGACCACCTGCGTCTCAGCATCCTGCCCTGGGATGAGAGCATCCTGGACACCCTC
TCGCCCAGGCTCGCTACAGCACTGAGTGAAGAAATGAAAGACAAAGGTGGATACATGAGC
AAGATTTGCAACTTGCTACCCATTAGGATAATGTCTTATGTAATGCTGCCCTGTACCCTG
CCTGTGGAATCTGCCATTGCGATTGTCCAGAGACTGGTGACATGGCTTCCAGATATGCCC
GACGATGTCCTGTGGTTGCAGTGGGTGACCTCACAGGTGTTCACTCGAGTGCTGATGTGT
CTGCTCCCCGCCTCCAGGTCCCAAATGCCAGTGAGCAGCCAACAGGCCTCCCCATGCACA
CCTGAGCAGGACTGGCCCTGCTGGACTCCCTGCTCCCCCAAGGGCTGTCCAGCAGAGACC
AAAGCAGAGGCCACCCCGCGGTCCATCCTCAGGTCCAGCCTGAACTTCTTCTTGGGCAAT
AAAGTACCTGCTGGTGCTGAGGGGCTCTCCACCTTTCCCAGTTTTTCACTAGAGAAGAGT
CTGTGA
Enzyme 4 GenBank Gene ID AL138578 Link Image
Enzyme 4 GeneCard ID PNPLA3 Link Image
Enzyme 4 GenAtlas ID PNPLA3 Link Image
Enzyme 4 HGNC ID HGNC:18590 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 22q13.31
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Collins JE, Goward ME, Cole CG, Smink LJ, Huckle EJ, Knowles S, Bye JM, Beare DM, Dunham I: Reevaluating human gene annotation: a second-generation analysis of chromosome 22. Genome Res. 2003 Jan;13(1):27-36. [PubMed Link Image]
  2. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  3. 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]
  4. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed 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. Jenkins CM, Mancuso DJ, Yan W, Sims HF, Gibson B, Gross RW: Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem. 2004 Nov 19;279(47):48968-75. Epub 2004 Sep 10. [PubMed Link Image]
  7. Liu YM, Moldes M, Bastard JP, Bruckert E, Viguerie N, Hainque B, Basdevant A, Langin D, Pairault J, Clement K: Adiponutrin: A new gene regulated by energy balance in human adipose tissue. J Clin Endocrinol Metab. 2004 Jun;89(6):2684-9. [PubMed Link Image]
  8. Johansson LE, Lindblad U, Larsson CA, Rastam L, Ridderstrale M: Polymorphisms in the adiponutrin gene are associated with increased insulin secretion and obesity. Eur J Endocrinol. 2008 Nov;159(5):577-83. Epub 2008 Aug 26. [PubMed Link Image]
  9. Romeo S, Kozlitina J, Xing C, Pertsemlidis A, Cox D, Pennacchio LA, Boerwinkle E, Cohen JC, Hobbs HH: Genetic variation in PNPLA3 confers susceptibility to nonalcoholic fatty liver disease. Nat Genet. 2008 Dec;40(12):1461-5. Epub 2008 Sep 25. [PubMed Link Image]
  10. Kotronen A, Johansson LE, Johansson LM, Roos C, Westerbacka J, Hamsten A, Bergholm R, Arkkila P, Arola J, Kiviluoto T, Fisher RM, Ehrenborg E, Orho-Melander M, Ridderstrale M, Groop L, Yki-Jarvinen H: A common variant in PNPLA3, which encodes adiponutrin, is associated with liver fat content in humans. Diabetologia. 2009 Jun;52(6):1056-60. Epub 2009 Feb 18. [PubMed Link Image]
  11. He S, McPhaul C, Li JZ, Garuti R, Kinch L, Grishin NV, Cohen JC, Hobbs HH: A sequence variation (I148M) in PNPLA3 associated with nonalcoholic fatty liver disease disrupts triglyceride hydrolysis. J Biol Chem. 2010 Feb 26;285(9):6706-15. Epub 2009 Dec 23. [PubMed Link Image]
  12. Sookoian S, Castano GO, Burgueno AL, Gianotti TF, Rosselli MS, Pirola CJ: A nonsynonymous gene variant in the adiponutrin gene is associated with nonalcoholic fatty liver disease severity. J Lipid Res. 2009 Oct;50(10):2111-6. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5468
Enzyme 5 Name Gastric triacylglycerol lipase
Enzyme 5 Synonyms
  1. GL
  2. Gastric lipase
Enzyme 5 Gene Name LIPF
Enzyme 5 Protein Sequence >Gastric triacylglycerol lipase
MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILE
VNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRG
NTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFI
AFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQF
LATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKS
GKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPN
LIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK
Enzyme 5 Number of Residues 398
Enzyme 5 Molecular Weight 45237.4
Enzyme 5 Theoretical pI 7.37
Enzyme 5 GO Classification
Function
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 5 General Function Involved in lipid metabolic process
Enzyme 5 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 5 Pathways
Enzyme 5 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-19
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 758063 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P07098 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name LIPG_HUMAN Link Image
Enzyme 5 PDB ID 1HLG Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1197 bp
ATGTGGCTGCTTTTAACAATGGCAAGTTTGATATCTGTACTGGGGACTACACATGGTTTG
TTTGGAAAATTACATCCTGGAAGCCCTGAAGTGACTATGAACATTAGTCAGATGATTACT
TATTGGGGATACCCAAATGAAGAATATGAAGTTGTGACTGAAGATGGTTATATTCTTGAA
GTCAATAGAATTCCTTATGGGAAGAAAAATTCAGGGAATACAGGCCAGAGACCTGTTGTG
TTTTTGCAGCATGGTTTGCTTGCATCAGCCACAAACTGGATTTCCAACCTGCCGAACAAC
AGCCTTGCCTTCATTCTGGCAGATGCTGGTTATGATGTGTGGCTGGGCAACAGCAGAGGA
AACACCTGGGCCAGAAGAAACTTGTACTATTCACCAGATTCAGTTGAATTCTGGGCTTTC
AGCTTTGATGAAATGGCTAAATATGACCTTCCAGCCACAATCGACTTCATTGTAAAGAAA
ACTGGACAGAAGCAGCTACACTATGTTGGCCATTCCCAGGGCACCACCATTGGTTTTATT
GCCTTTTCCACCAATCCCAGCCTGGCTAAAAGAATCAAAACCTTCTATGCTCTAGCTCCT
GTTGCCACTGTGAAGTATACAAAAAGCCTTATAAACAAACTTAGATTTGTTCCTCAATCC
CTCTTCAAGTTTATATTTGGTGACAAAATATTCTACCCACACAACTTCTTTGATCAATTT
CTTGCTACTGAAGTGTGCTCCCGTGAGATGCTGAATCTCCTTTGCAGCAATGCCTTATTT
ATAATTTGTGGATTTGACAGTAAGAACTTTAACACGAGTCGCTTGGATGTGTATCTATCA
CATAATCCAGCAGGAACTTCTGTTCAAAACATGTTCCATTGGACCCAGGCTGTTAAGTCT
GGGAAATTCCAAGCTTATGACTGGGGAAGCCCAGTTCAGAATAGGATGCACTATGATCAG
TCCCAACCTCCCTACTACAATGTGACAGCCATGAATGTACCAATTGCAGTGTGGAACGGT
GGCAAGGACCTGTTGGCTGACCCCCAAGATGTTGGCCTTTTGCTTCCAAAACTCCCCAAT
CTTATTTACCACAAGGAGATTCCTTTTTACAATCACTTGGACTTTATCTGGGCAATGGAT
GCCCCTCAAGAAGTTTACAATGACATTGTTTCTATGATATCAGAAGATAAAAAGTAG
Enzyme 5 GenBank Gene ID X05997 Link Image
Enzyme 5 GeneCard ID LIPF Link Image
Enzyme 5 GenAtlas ID LIPF Link Image
Enzyme 5 HGNC ID HGNC:6622 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 10q23.31
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Bodmer MW, Angal S, Yarranton GT, Harris TJ, Lyons A, King DJ, Pieroni G, Riviere C, Verger R, Lowe PA: Molecular cloning of a human gastric lipase and expression of the enzyme in yeast. Biochim Biophys Acta. 1987 Aug 25;909(3):237-44. [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. Bernback S, Blackberg L: Human gastric lipase. The N-terminal tetrapeptide is essential for lipid binding and lipase activity. Eur J Biochem. 1989 Jul 1;182(3):495-9. [PubMed Link Image]
  4. Roussel A, Canaan S, Egloff MP, Riviere M, Dupuis L, Verger R, Cambillau C: Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. J Biol Chem. 1999 Jun 11;274(24):16995-7002. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5471
Enzyme 6 Name Endothelial lipase
Enzyme 6 Synonyms
  1. Endothelial cell-derived lipase
  2. EDL
  3. EL
Enzyme 6 Gene Name LIPG
Enzyme 6 Protein Sequence >Endothelial lipase
MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPE
HEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVV
VDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGN
FVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHID
IYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDS
NRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKN
MGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGAS
QSWYNLWKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWF
RKCRDGWRMKNETSPTVELP
Enzyme 6 Number of Residues 500
Enzyme 6 Molecular Weight 56794.3
Enzyme 6 Theoretical pI 8.00
Enzyme 6 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipoprotein lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 6 General Function Involved in catalytic activity
Enzyme 6 Specific Function Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin
Enzyme 6 Pathways
Enzyme 6 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-20
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 4836419 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9Y5X9 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name LIPE_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1503 bp
ATGAGCAACTCCGTTCCTCTGCTCTGTTTCTGGAGCCTCTGCTATTGCTTTGCTGCGGGG
AGCCCCGTACCTTTTGGTCCAGAGGGACGGCTGGAAGATAAGCTCCACAAACCCAAAGCT
ACACAGACTGAGGTCAAACCATCTGTGAGGTTTAACCTCCGCACCTCCAAGGACCCAGAG
CATGAAGGATGCTACCTCTCCGTCGGCCACAGCCAGCCCTTAGAAGACTGCAGTTTCAAC
ATGACAGCTAAAACCTTTTTCATCATTCACGGATGGACGATGAGCGGTATCTTTGAAAAC
TGGCTGCACAAACTCGTGTCAGCCCTGCACACAAGAGAGAAAGACGCCAATGTAGTTGTG
GTTGACTGGCTCCCCCTGGCCCACCAGCTTTACACGGATGCGGTCAATAATACCAGGGTG
GTGGGACACAGCATTGCCAGGATGCTCGACTGGCTGCAGGAGAAGGACGATTTTTCTCTC
GGGAATGTCCACTTGATCGGCTACAGCCTCGGAGCGCACGTGGCCGGGTATGCAGGCAAC
TTCGTGAAAGGAACGGTGGGCCGAATCACAGGTTTGGATCCTGCCGGGCCCATGTTTGAA
GGGGCCGACATCCACAAGAGGCTCTCTCCGGACGATGCAGATTTTGTGGATGTCCTCCAC
ACCTACACGCGTTCCTTCGGCTTGAGCATTGGTATTCAGATGCCTGTGGGCCACATTGAC
ATCTACCCCAATGGGGGTGACTTCCAGCCAGGCTGTGGACTCAACGATGTCTTGGGATCA
ATTGCATATGGAACAATCACAGAGGTGGTAAAATGTGAGCATGAGCGAGCCGTCCACCTC
TTTGTTGACTCTCTGGTGAATCAGGACAAGCCGAGTTTTGCCTTCCAGTGCACTGACTCC
AATCGCTTCAAAAAGGGGATCTGTCTGAGCTGCCGCAAGAACCGTTGTAATAGCATTGGC
TACAATGCCAAGAAAATGAGGAACAAGAGGAACAGCAAAATGTACCTAAAAACCCGGGCA
GGCATGCCTTTCAGAGTTTACCATTATCAGATGAAAATCCATGTCTTCAGTTACAAGAAC
ATGGGAGAAATTGAGCCCACCTTTTACGTCACCCTTTATGGCACTAATGCAGATTCCCAG
ACTCTGCCACTGGAAATAGTGGAGCGGATCGAGCAGAATGCCACCAACACCTTCCTGGTC
TACACCGAGGAGGACTTGGGAGACCTCTTGAAGATCCAGCTCACCTGGGAGGGGGCCTCT
CAGTCTTGGTACAACCTGTGGAAGGAGTTTCGCAGCTACCTGTCTCAACCCCGCAACCCC
GGACGGGAGCTGAATATCAGGCGCATCCGGGTGAAGTCTGGGGAAACCCAGCGGAAACTG
ACATTTTGTACAGAAGACCCTGAGAACACCAGCATATCCCCAGGCCGGGAGCTCTGGTTT
CGCAAGTGTCGGGATGGCTGGAGGATGAAAAACGAAACCAGTCCCACTGTGGAGCTTCCC
TGA
Enzyme 6 GenBank Gene ID AF118767 Link Image
Enzyme 6 GeneCard ID LIPG Link Image
Enzyme 6 GenAtlas ID LIPG Link Image
Enzyme 6 HGNC ID HGNC:6623 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 18q21.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Hirata K, Dichek HL, Cioffi JA, Choi SY, Leeper NJ, Quintana L, Kronmal GS, Cooper AD, Quertermous T: Cloning of a unique lipase from endothelial cells extends the lipase gene family. J Biol Chem. 1999 May 14;274(20):14170-5. [PubMed Link Image]
  2. Jaye M, Lynch KJ, Krawiec J, Marchadier D, Maugeais C, Doan K, South V, Amin D, Perrone M, Rader DJ: A novel endothelial-derived lipase that modulates HDL metabolism. Nat Genet. 1999 Apr;21(4):424-8. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, 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]
  5. McCoy MG, Sun GS, Marchadier D, Maugeais C, Glick JM, Rader DJ: Characterization of the lipolytic activity of endothelial lipase. J Lipid Res. 2002 Jun;43(6):921-9. [PubMed Link Image]
  6. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  7. Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5473
Enzyme 7 Name Bile salt-activated lipase
Enzyme 7 Synonyms
  1. BAL
  2. Bile salt-stimulated lipase
  3. BSSL
  4. Bucelipase
  5. Carboxyl ester lipase
  6. Cholesterol esterase
  7. Pancreatic lysophospholipase
  8. Sterol esterase
Enzyme 7 Gene Name CEL
Enzyme 7 Protein Sequence >Bile salt-activated lipase
MGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTK
ALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPV
MIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPG
NYGLRDQHMAIAWVKRNIAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQS
GVALSPWVIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGLEYP
MLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVT
EEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEIA
LAQHRANAKSAKTYAYLFSHPSRMPVYPKWVGADHADDIQYVFGKPFATPTGYRPQDRTV
SKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLR
YWTLTYLALPTVTDQEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSG
APPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVP
PTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDS
GAPPVPPTGDSEAAPVPPTDDSKEAQMPAVIRF
Enzyme 7 Number of Residues 753
Enzyme 7 Molecular Weight 79320.9
Enzyme 7 Theoretical pI 4.94
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Lipid transport and metabolism
Enzyme 7 Specific Function Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides
Enzyme 7 Pathways
Enzyme 7 Reactions
  • a steryl ester + H2O = a sterol + a fatty acid [RN:R02115]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-20
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 148536848 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P19835 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name CEL_HUMAN Link Image
Enzyme 7 PDB ID 1F6W Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2271 bp
ATGCTCACCATGGGGCGCCTGCAACTGGTTGTGTTGGGCCTCACCTGCTGCTGGGCAGTG
GCGAGTGCCGCGAAGCTGGGCGCCGTGTACACAGAAGGTGGGTTCGTGGAAGGCGTCAAT
AAGAAGCTCGGCCTCCTGGGTGACTCTGTGGACATCTTCAAGGGCATCCCCTTCGCAGCT
CCCACCAAGGCCCTGGAAAATCCTCAGCCACATCCTGGCTGGCAAGGGACCCTGAAGGCC
AAGAACTTCAAGAAGAGATGCCTGCAGGCCACCATCACCCAGGACAGCACCTACGGGGAT
GAAGACTGCCTGTACCTCAACATTTGGGTGCCCCAGGGCAGGAAGCAAGTCTCCCGGGAC
CTGCCCGTTATGATCTGGATCTATGGAGGCGCCTTCCTCATGGGGTCCGGCCATGGGGCC
AACTTCCTCAACAACTACCTGTATGACGGCGAGGAGATCGCCACACGCGGAAACGTCATC
GTGGTCACCTTCAACTACCGTGTCGGCCCCCTTGGGTTCCTCAGCACTGGGGACGCCAAT
CTGCCAGGTAACTATGGCCTTCGGGATCAGCACATGGCCATTGCTTGGGTGAAGAGGAAT
ATCGCGGCCTTCGGGGGGGACCCCAACAACATCACGCTCTTCGGGGAGTCTGCTGGAGGT
GCCAGCGTCTCTCTGCAGACCCTCTCCCCCTACAACAAGGGCCTCATCCGGCGAGCCATC
AGCCAGAGCGGCGTGGCCCTGAGTCCCTGGGTCATCCAGAAAAACCCACTCTTCTGGGCC
AAAAAGGTGGCTGAGAAGGTGGGTTGCCCTGTGGGTGATGCCGCCAGGATGGCCCAGTGT
CTGAAGGTTACTGATCCCCGAGCCCTGACGCTGGCCTATAAGGTGCCGCTGGCAGGCCTG
GAGTACCCCATGCTGCACTATGTGGGCTTCGTCCCTGTCATTGATGGAGACTTCATCCCC
GCTGACCCGATCAACCTGTACGCCAACGCCGCCGACATCGACTATATAGCAGGCACCAAC
AACATGGACGGCCACATCTTCGCCAGCATCGACATGCCTGCCATCAACAAGGGCAACAAG
AAAGTCACGGAGGAGGACTTCTACAAGCTGGTCAGTGAGTTCACAATCACCAAGGGGCTC
AGAGGCGCCAAGACGACCTTTGATGTCTACACCGAGTCCTGGGCCCAGGACCCATCCCAG
GAGAATAAGAAGAAGACTGTGGTGGACTTTGAGACCGATGTCCTCTTCCTGGTGCCCACC
GAGATTGCCCTAGCCCAGCACAGAGCCAATGCCAAGAGTGCCAAGACCTACGCCTACCTG
TTTTCCCATCCCTCTCGGATGCCCGTCTACCCCAAATGGGTGGGGGCCGACCATGCAGAT
GACATTCAGTACGTTTTCGGGAAGCCCTTCGCCACCCCCACGGGCTACCGGCCCCAAGAC
AGGACAGTCTCTAAGGCCATGATCGCCTACTGGACCAACTTTGCCAAAACAGGGGACCCC
AACATGGGCGACTCGGCTGTGCCCACACACTGGGAACCCTACACTACGGAAAACAGCGGC
TACCTGGAGATCACCAAGAAGATGGGCAGCAGCTCCATGAAGCGGAGCCTGAGAACCAAC
TTCCTGCGCTACTGGACCCTCACCTATCTGGCGCTGCCCACAGTGACCGACCAGGAGGCC
ACCCCTGTGCCCCCCACAGGGGACTCCGAGGCCACTCCCGTGCCCCCCACGGGTGACTCC
GAGACCGCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGT
GACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCC
ACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTG
CCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCC
CCCGTGCCGCCCACGGGTGACTCCGGCGCCCCCCCCGTGCCGCCCACGGGTGACGCCGGG
CCCCCCCCCGTGCCGCCCACGGGTGACTCCGGCGCCCCCCCCGTGCCGCCCACGGGTGAC
TCCGGGGCCCCCCCCGTGACCCCCACGGGTGACTCCGAGACCGCCCCCGTGCCGCCCACG
GGTGACTCCGGGGCCCCCCCTGTGCCCCCCACGGGTGACTCTGAGGCTGCCCCTGTGCCC
CCCACAGATGACTCCAAGGAAGCTCAGATGCCTGCAGTCATTAGGTTTTAG
Enzyme 7 GenBank Gene ID Not Available
Enzyme 7 GeneCard ID CEL Link Image
Enzyme 7 GenAtlas ID CEL Link Image
Enzyme 7 HGNC ID HGNC:1848 Link Image
Enzyme 7 Chromosome Location 9
Enzyme 7 Locus 9q34.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Nilsson J, Blackberg L, Carlsson P, Enerback S, Hernell O, Bjursell G: cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. Eur J Biochem. 1990 Sep 11;192(2):543-50. [PubMed Link Image]
  2. Hui DY, Kissel JA: Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase. FEBS Lett. 1990 Dec 10;276(1-2):131-4. [PubMed Link Image]
  3. Baba T, Downs D, Jackson KW, Tang J, Wang CS: Structure of human milk bile salt activated lipase. Biochemistry. 1991 Jan 15;30(2):500-10. [PubMed Link Image]
  4. Lidberg U, Nilsson J, Stromberg K, Stenman G, Sahlin P, Enerback S, Bjursell G: Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene. Genomics. 1992 Jul;13(3):630-40. [PubMed Link Image]
  5. Roudani S, Miralles F, Margotat A, Escribano MJ, Lombardo D: Bile salt-dependent lipase transcripts in human fetal tissues. Biochim Biophys Acta. 1995 Oct 17;1264(1):141-50. [PubMed Link Image]
  6. Madeyski K, Lidberg U, Bjursell G, Nilsson J: Structure and organization of the human carboxyl ester lipase locus. Mamm Genome. 1998 Apr;9(4):334-8. [PubMed Link Image]
  7. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  8. Hui DY, Hayakawa K, Oizumi J: Lipoamidase activity in normal and mutagenized pancreatic cholesterol esterase (bile salt-stimulated lipase). Biochem J. 1993 Apr 1;291 ( Pt 1):65-9. [PubMed Link Image]
  9. Christie DL, Cleverly DR, O'Connor CJ: Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases. FEBS Lett. 1991 Jan 28;278(2):190-4. [PubMed Link Image]
  10. Wang CS, Dashti A, Jackson KW, Yeh JC, Cummings RD, Tang J: Isolation and characterization of human milk bile salt-activated lipase C-tail fragment. Biochemistry. 1995 Aug 22;34(33):10639-44. [PubMed Link Image]
  11. Mechref Y, Chen P, Novotny MV: Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk. Glycobiology. 1999 Mar;9(3):227-34. [PubMed Link Image]
  12. Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC: Crystal structure of the catalytic domain of human bile salt activated lipase. Protein Sci. 2000 Sep;9(9):1783-90. [PubMed Link Image]
  13. Raeder H, Johansson S, Holm PI, Haldorsen IS, Mas E, Sbarra V, Nermoen I, Eide SA, Grevle L, Bjorkhaug L, Sagen JV, Aksnes L, Sovik O, Lombardo D, Molven A, Njolstad PR: Mutations in the CEL VNTR cause a syndrome of diabetes and pancreatic exocrine dysfunction. Nat Genet. 2006 Jan;38(1):54-62. Epub 2005 Dec 20. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5475
Enzyme 8 Name Diacylglycerol O-acyltransferase 1
Enzyme 8 Synonyms
  1. ACAT-related gene product 1
  2. Diglyceride acyltransferase
Enzyme 8 Gene Name DGAT1
Enzyme 8 Protein Sequence >Diacylglycerol O-acyltransferase 1
MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVG
SGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQV
VSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPA
AVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHT
VSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWM
VPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREF
YRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVS
VPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLN
YEAPAAEA
Enzyme 8 Number of Residues 488
Enzyme 8 Molecular Weight 55277.7
Enzyme 8 Theoretical pI 9.60
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Involved in diacylglycerol O-acyltransferase activity
Enzyme 8 Specific Function Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly
Enzyme 8 Pathways
Enzyme 8 Reactions
  • acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol [RN:R02251]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 104-124 130-150 166-186 189-209 282-302 332-352 406-426 428-448 453-473
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 29170487 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O75907 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name DGAT1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1467 bp
ATGGGCGACCGCGGCAGCTCCCGGCGCCGGAGGACAGGGTCGCGGCCCTCGAGCCACGGC
GGCGGCGGGCCTGCGGCGGCGGAAGAGGAGGTGCGGGACGCCGCTGCGGGCCCCGACGTG
GGAGCCGCGGGGGACGCGCCAGCCCCGGCCCCCAACAAGGACGGAGACGCCGGCGTGGGC
AGCGGCCACTGGGAGCTGAGGTGCCATCGCCTGCAGGATTCTTTATTCAGCTCTGACAGT
GGCTTCAGCAACTACCGTGGCATCCTGAACTGGTGTGTGGTGATGCTGATCTTGAGCAAT
GCCCGGTTATTTCTGGAGAACCTCATCAAGTATGGCATCCTGGTGGACCCCATCCAGGTG
GTTTCTCTGTTCCTGAAGGATCCCTATAGCTGGCCCGCCCCATGCCTGGTTATTGCGGCC
AATGTCTTTGCTGTGGCTGCATTCCAGGTTGAGAAGCGCCTGGCGGTGGGTGCCCTGACG
GAGCAGGCGGGACTGCTGCTGCACGTGGCCAACCTGGCCACCATTCTGTGTTTCCCAGCG
GCTGTGGTCTTACTGGTTGAGTCTATCACTCCAGTGGGCTCCCTGCTGGCGCTGATGGCG
CACACCATCCTCTTCCTCAAGCTCTTCTCCTACCGCGACGTCAACTCATGGTGCCGCAGG
GCCAGGGCCAAGGCTGCCTCTGCAGGGAAGAAGGCCAGCAGTGCTGCTGCCCCGCACACC
GTGAGCTACCCGGACAATCTGACCTACCGCGATCTCTACTACTTCCTCTTCGCCCCCACC
TTGTGCTACGAGCTCAACTTTCCCCGCTCTCCCCGCATCCGGAAGCGCTTTCTGCTGCGA
CGGATCCTTGAGATGCTGTTCTTCACCCAGCTCCAGGTGGGGCTGATCCAGCAGTGGATG
GTCCCCACCATCCAGAACTCCATGAAGCCCTTCAAGGACATGGACTACTCACGCATCATC
GAGCGCCTCCTGAAGCTGGCGGTCCCCAATCACCTCATCTGGCTCATCTTCTTCTACTGG
CTCTTCCACTCCTGCCTGAATGCCGTGGCTGAGCTCATGCAGTTTGGAGACCGGGAGTTC
TACCGGGACTGGTGGAACTCCGAGTCTGTCACCTACTTCTGGCAGAACTGGAACATCCCT
GTGCACAAGTGGTGCATCAGACACTTCTACAAGCCCATGCTTCGACGGGGCAGCAGCAAG
TGGATGGCCAGGACAGGGGTGTTCCTGGCCTCGGCCTTCTTCCACGAGTACCTGGTGAGC
GTCCCTCTGCGAATGTTCCGCCTCTGGGCGTTCACGGGCATGATGGCTCAGATCCCACTG
GCCTGGTTCGTGGGCCGCTTTTTCCAGGGCAACTATGGCAACGCAGCTGTGTGGCTGTCG
CTCATCATCGGACAGCCAATAGCCGTCCTCATGTACGTCCACGACTACTACGTGCTCAAC
TATGAGGCCCCAGCGGCAGAGGCCTGA
Enzyme 8 GenBank Gene ID AB057815 Link Image
Enzyme 8 GeneCard ID DGAT1 Link Image
Enzyme 8 GenAtlas ID DGAT1 Link Image
Enzyme 8 HGNC ID HGNC:2843 Link Image
Enzyme 8 Chromosome Location 8
Enzyme 8 Locus 8q24.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Oelkers P, Behari A, Cromley D, Billheimer JT, Sturley SL: Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes. J Biol Chem. 1998 Oct 9;273(41):26765-71. [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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5477
Enzyme 9 Name Pancreatic lipase-related protein 2
Enzyme 9 Synonyms
  1. PL-RP2
Enzyme 9 Gene Name PNLIPRP2
Enzyme 9 Protein Sequence >Pancreatic lipase-related protein 2
MLPPWTLGLLLLATVRGKEVCYGQLGCFSDEKPWAGTLQRPVKLLPWSPEDIDTRFLLYT
NENPNNFQLITGTEPDTIEASNFQLDRKTRFIIHGFLDKAEDSWPSDMCKKMFEVEKVNC
ICVDWRHGSRAMYTQAVQNIRVVGAETAFLIQALSTQLGYSLEDVHVIGHSLGAHTAAEA
GRRLGGRVGRITGLDPAGPCFQDEPEEVRLDPSDAVFVDVIHTDSSPIVPSLGFGMSQKV
GHLDFFPNGGKEMPGCKKNVLSTITDIDGIWEGIGGFVSCNHLRSFEYYSSSVLNPDGFL
GYPCASYDEFQESKCFPCPAEGCPKMGHYADQFKGKTSAVEQTFFLNTGESGNFTSWRYK
VSVTLSGKEKVNGYIRIALYGSNENSKQYEIFKGSLKPDASHTCAIDVDFNVGKIQKVKF
LWNKRGINLSEPKLGASQITVQSGEDGTEYNFCSSDTVEENVLQSLYPC
Enzyme 9 Number of Residues 469
Enzyme 9 Molecular Weight 51946.3
Enzyme 9 Theoretical pI 5.11
Enzyme 9 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 9 General Function Involved in catalytic activity
Enzyme 9 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 9 Pathways
Enzyme 9 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-17
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID P54317 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name LIPR2_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1410 bp
ATGCTGCCCCCTTGGACCCTCGGCCTTCTCCTGCTGGCCACAGTCAGAGGAAAAGAGGTC
TGCTACGGACAACTTGGCTGCTTTTCTGATGAAAAACCATGGGCAGGAACCCTTCAGCGA
CCTGTAAAATTACTTCCCTGGTCCCCCGAGGACATTGACACCCGCTTTCTTCTGTACACA
AATGAAAATCCAAACAACTTCCAACTAATCACTGGCACGGAACCAGACACCATTGAGGCT
TCAAACTTCCAACTGGACCGCAAGACACGCTTCATCATCCATGGCTTCTTAGACAAGGCG
GAGGACAGCTGGCCATCGGACATGTGCAAGAAAATGTTTGAAGTGGAGAAGGTGAACTGC
ATCTGTGTGGACTGGAGGCACGGGTCCCGGGCAATGTACACCCAAGCCGTGCAAAACATT
CGGGTTGTTGGGGCGGAGACAGCTTTCTTAATACAAGCACTGTCGACGCAGCTAGGGTAC
AGCCTTGAGGACGTGCATGTCATCGGCCACAGCCTGGGCGCGCACACGGCCGCGGAGGCG
GGCAGGAGGCTGGGGGGCCGCGTGGGCAGGATCACAGGGCTGGATCCAGCAGGGCCGTGC
TTCCAGGATGAACCTGAGGAGGTTCGGTTGGATCCATCTGACGCCGTGTTTGTGGATGTG
ATTCACACAGATTCTTCTCCCATAGTTCCTTCCCTAGGTTTCGGAATGAGCCAAAAGGTG
GGCCATCTGGATTTCTTTCCAAATGGAGGAAAGGAAATGCCCGGATGTAAGAAAAATGTC
CTTTCAACCATTACTGATATTGATGGAATATGGGAAGGAATTGGTGGCTTTGTGTCTTGC
AATCACCTAAGAAGCTTCGAGTATTACTCAAGCAGCGTCCTCAACCCTGATGGCTTCCTG
GGCTATCCCTGTGCCTCCTACGATGAGTTTCAGGAGAGTAAGTGTTTCCCTTGTCCAGCT
GAAGGATGCCCCAAAATGGGGCACTATGCTGACCAATTTAAGGGGAAAACAAGTGCTGTG
GAACAAACCTTTTTCCTGAACACAGGAGAGAGTGGTAACTTTACTAGTTGGAGATATAAG
GTATCAGTCACACTTTCTGGAAAAGAGAAAGTGAATGGGTACATCAGGATTGCTTTGTAT
GGAAGTAATGAAAACTCGAAACAATATGAGATTTTCAAAGGATCCCTCAAACCAGATGCA
AGTCACACGTGTGCTATTGATGTGGATTTTAATGTTGGAAAAATACAGAAAGTTAAATTC
CTCTGGAACAAACGTGGGATAAATCTATCTGAGCCCAAACTGGGGGCTTCCCAAATCACA
GTGCAAAGTGGTGAAGATGGGACTGAGTATAATTTTTGTAGCAGCGACACTGTGGAAGAA
AACGTCTTGCAATCTCTTTACCCTTGTTAA
Enzyme 9 GenBank Gene ID M93284 Link Image
Enzyme 9 GeneCard ID PNLIPRP2 Link Image
Enzyme 9 GenAtlas ID PNLIPRP2 Link Image
Enzyme 9 HGNC ID HGNC:9157 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 10q25.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [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. Eydoux C, Spinelli S, Davis TL, Walker JR, Seitova A, Dhe-Paganon S, De Caro A, Cambillau C, Carriere F: Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation. Biochemistry. 2008 Sep 9;47(36):9553-64. Epub 2008 Aug 15. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5545
Enzyme 10 Name Lipoprotein lipase
Enzyme 10 Synonyms
  1. LPL
Enzyme 10 Gene Name LPL
Enzyme 10 Protein Sequence >Lipoprotein lipase
MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGV
AESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEH
YPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRIT
GLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQ
PGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKG
LCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQ
AFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDW
WSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG
Enzyme 10 Number of Residues 475
Enzyme 10 Molecular Weight 53162.1
Enzyme 10 Theoretical pI 8.26
Enzyme 10 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipoprotein lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 10 General Function Involved in catalytic activity
Enzyme 10 Specific Function The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium
Enzyme 10 Pathways
Enzyme 10 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-27
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 189065397 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P06858 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name LIPL_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1428 bp
ATGGAGAGCAAAGCCCTGCTCGTGCTGACTCTGGCCGTGTGGCTCCAGAGTCTGACCGCC
TCCCGCGGAGGGGTGGCCGCCGCCGACCAAAGAAGAGATTTTATCGACATCGAAAGTAAA
TTTGCCCTAAGGACCCCTGAAGACACAGCTGAGGACACTTGCCACCTCATTCCCGGAGTA
GCAGAGTCCGTGGCTACCTGTCATTTCAATCACAGCAGCAAAACCTTCATGGTGATCCAT
GGCTGGACGGTAACAGGAATGTATGAGAGTTGGGTGCCAAAACTTGTGGCCGCCCTGTAC
AAGAGAGAACCAGACTCCAATGTCATTGTGGTGGACTGGCTGTCACGGGCTCAGGAGCAT
TACCCAGTGTCCGCGGGCTACACCAAACTGGTGGGACAGGATGTGGCCCGGTTTATCAAC
TGGATGGAGGAGGAGTTTAACTACCCTCTGGACAATGTCCATCTCTTGGGATACAGCCTT
GGAGCCCATGCTGCTGGCATTGCAGGAAGTCTGACCAATAAGAAAGTCAACAGAATTACT
GGCCTCGATCCAGCTGGACCTAACTTTGAGTATGCAGAAGCCCCGAGTCGTCTTTCTCCT
GATGATGCAGATTTTGTAGACGTCTTACACACATTCACCAGAGGGTCCCCTGGTCGAAGC
ATTGGAATCCAGAAACCAGTTGGGCATGTTGACATTTACCCGAATGGAGGTACTTTTCAG
CCAGGATGTAACATTGGAGAAGCTATCCGCGTGATTGCAGAGAGAGGACTTGGAGATGTG
GACCAGCTAGTGAAGTGCTCCCACGAGCGCTCCATTCATCTCTTCATCGACTCTCTGTTG
AATGAAGAAAATCCAAGTAAGGCCTACAGGTGCAGTTCCAAGGAAGCCTTTGAGAAAGGG
CTCTGCTTGAGTTGTAGAAAGAACCGCTGCAACAATCTGGGCTATGAGATCAATAAAGTC
AGAGCCAAAAGAAGCAGCAAAATGTACCTGAAGACTCGTTCTCAGATGCCCTACAAAGTC
TTCCATTACCAAGTAAAGATTCATTTTTCTGGGACTGAGAGTGAAACCCATACCAATCAG
GCCTTTGAGATTTCTCTGTATGGCACCGTGGCCGAGAGTGAGAACATCCCATTCACTCTG
CCTGAAGTTTCCACAAATAAGACCTACTCCTTCCTAATTTACACAGAGGTAGATATTGGA
GAACTACTCATGTTGAAGCTCAAATGGAAGAGTGATTCATACTTTAGCTGGTCAGACTGG
TGGAGCAGTCCCGGCTTCGCCATTCAGAAGATCAGAGTAAAAGCAGGAGAGACTCAGAAA
AAGGTGATCTTCTGTTCTAGGGAGAAAGTGTCTCATTTGCAGAAAGGAAAGGCACCTGCG
GTATTTGTGAAATGCCATGACAAGTCTCTGAATAAGAAGTCAGGCTGA
Enzyme 10 GenBank Gene ID AK312311 Link Image
Enzyme 10 GeneCard ID LPL Link Image
Enzyme 10 GenAtlas ID LPL Link Image
Enzyme 10 HGNC ID HGNC:6677 Link Image
Enzyme 10 Chromosome Location 8
Enzyme 10 Locus 8p22
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Wion KL, Kirchgessner TG, Lusis AJ, Schotz MC, Lawn RM: Human lipoprotein lipase complementary DNA sequence. Science. 1987 Mar 27;235(4796):1638-41. [PubMed Link Image]
  2. Gotoda T, Senda M, Gamou T, Furuichi Y, Oka K: Nucleotide sequence of human cDNA coding for a lipoprotein lipase (LPL) cloned from placental cDNA library. Nucleic Acids Res. 1989 Mar 25;17(6):2351. [PubMed Link Image]
  3. Takagi A, Ikeda Y, Yamamoto A: DNA sequence of lipoprotein lipase cDNA cloned from human monocytic leukemia THP-1 cells. Nucleic Acids Res. 1990 Nov 11;18(21):6436. [PubMed Link Image]
  4. Chuat JC, Raisonnier A, Etienne J, Galibert F: The lipoprotein lipase-encoding human gene: sequence from intron-6 to intron-9 and presence in intron-7 of a 40-million-year-old Alu sequence. Gene. 1992 Jan 15;110(2):257-61. [PubMed Link Image]
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  26. Ma YH, Bruin T, Tuzgol S, Wilson BI, Roederer G, Liu MS, Davignon J, Kastelein JJ, Brunzell JD, Hayden MR: Two naturally occurring mutations at the first and second bases of codon aspartic acid 156 in the proposed catalytic triad of human lipoprotein lipase. In vivo evidence that aspartic acid 156 is essential for catalysis. J Biol Chem. 1992 Jan 25;267(3):1918-23. [PubMed Link Image]
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  29. Ishimura-Oka K, Semenkovich CF, Faustinella F, Goldberg IJ, Shachter N, Smith LC, Coleman T, Hide WA, Brown WV, Oka K, et al.: A missense (Asp250----Asn) mutation in the lipoprotein lipase gene in two unrelated families with familial lipoprotein lipase deficiency. J Lipid Res. 1992 May;33(5):745-54. [PubMed Link Image]
  30. Reina M, Brunzell JD, Deeb SS: Molecular basis of familial chylomicronemia: mutations in the lipoprotein lipase and apolipoprotein C-II genes. J Lipid Res. 1992 Dec;33(12):1823-32. [PubMed Link Image]
  31. Kobayashi J, Sasaki N, Tashiro J, Inadera H, Saito Y, Yoshida S: A missense mutation (Ala334-->Thr) in exon 7 of the lipoprotein lipase gene in a case with type I hyperlipidemia. Biochem Biophys Res Commun. 1993 Mar 31;191(3):1046-54. [PubMed Link Image]
  32. Haubenwallner S, Horl G, Shachter NS, Presta E, Fried SK, Hofler G, Kostner GM, Breslow JL, Zechner R: A novel missense mutation in the gene for lipoprotein lipase resulting in a highly conservative amino acid substitution (Asp180-->Glu) causes familial chylomicronemia (type I hyperlipoproteinemia). Genomics. 1993 Nov;18(2):392-6. [PubMed Link Image]
  33. Ma Y, Liu MS, Ginzinger D, Frohlich J, Brunzell JD, Hayden MR: Gene-environment interaction in the conversion of a mild-to-severe phenotype in a patient homozygous for a Ser172-->Cys mutation in the lipoprotein lipase gene. J Clin Invest. 1993 May;91(5):1953-8. [PubMed Link Image]
  34. Wilson DE, Hata A, Kwong LK, Lingam A, Shuhua J, Ridinger DN, Yeager C, Kaltenborn KC, Iverius PH, Lalouel JM: Mutations in exon 3 of the lipoprotein lipase gene segregating in a family with hypertriglyceridemia, pancreatitis, and non-insulin-dependent diabetes. J Clin Invest. 1993 Jul;92(1):203-11. [PubMed Link Image]
  35. Bruin T, Tuzgol S, van Diermen DE, Hoogerbrugge-van der Linden N, Brunzell JD, Hayden MR, Kastelein JJ: Recurrent pancreatitis and chylomicronemia in an extended Dutch kindred is caused by a Gly154-->Ser substitution in lipoprotein lipase. J Lipid Res. 1993 Dec;34(12):2109-19. [PubMed Link Image]
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  37. Kobayashi J, Inadera H, Fujita Y, Talley G, Morisaki N, Yoshida S, Saito Y, Fojo SS, Brewer HB Jr: A naturally occurring mutation at the second base of codon asparagine 43 in the proposed N-linked glycosylation site of human lipoprotein lipase: in vivo evidence that asparagine 43 is essential for catalysis and secretion. Biochem Biophys Res Commun. 1994 Nov 30;205(1):506-15. [PubMed Link Image]
  38. Ma Y, Liu MS, Chitayat D, Bruin T, Beisiegel U, Benlian P, Foubert L, De Gennes JL, Funke H, Forsythe I, et al.: Recurrent missense mutations at the first and second base of codon Arg243 in human lipoprotein lipase in patients of different ancestries. Hum Mutat. 1994;3(1):52-8. [PubMed Link Image]
  39. Bruin T, Tuzgol S, Mulder WJ, van den Ende AE, Jansen H, Hayden MR, Kastelein JJ: A compound heterozygote for lipoprotein lipase deficiency, Val69-->Leu and Gly188-->Glu: correlation between in vitro LPL activity and clinical expression. J Lipid Res. 1994 Mar;35(3):438-45. [PubMed Link Image]
  40. Ma Y, Ooi TC, Liu MS, Zhang H, McPherson R, Edwards AL, Forsythe IJ, Frohlich J, Brunzell JD, Hayden MR: High frequency of mutations in the human lipoprotein lipase gene in pregnancy-induced chylomicronemia: possible association with apolipoprotein E2 isoform. J Lipid Res. 1994 Jun;35(6):1066-75. [PubMed Link Image]
  41. Previato L, Guardamagna O, Dugi KA, Ronan R, Talley GD, Santamarina-Fojo S, Brewer HB Jr: A novel missense mutation in the C-terminal domain of lipoprotein lipase (Glu410-->Val) leads to enzyme inactivation and familial chylomicronemia. J Lipid Res. 1994 Sep;35(9):1552-60. [PubMed Link Image]
  42. Reymer PW, Gagne E, Groenemeyer BE, Zhang H, Forsyth I, Jansen H, Seidell JC, Kromhout D, Lie KE, Kastelein J, et al.: A lipoprotein lipase mutation (Asn291Ser) is associated with reduced HDL cholesterol levels in premature atherosclerosis. Nat Genet. 1995 May;10(1):28-34. [PubMed Link Image]
  43. Henderson HE, Hassan F, Marais D, Hayden MR: A new mutation destroying disulphide bridging in the C-terminal domain of lipoprotein lipase. Biochem Biophys Res Commun. 1996 Oct 3;227(1):189-94. [PubMed Link Image]
  44. de Bruin TW, Mailly F, van Barlingen HH, Fisher R, Castro Cabezas M, Talmud P, Dallinga-Thie GM, Humphries SE: Lipoprotein lipase gene mutations D9N and N291S in four pedigrees with familial combined hyperlipidaemia. Eur J Clin Invest. 1996 Aug;26(8):631-9. [PubMed Link Image]
  45. Wiebusch H, Funke H, Bruin T, Bucher H, von Eckardstein A, Kastelein JJ, Assmann G: Compound heterozygosity for a known (D250N) and a novel (E410K) missense mutation in the C-terminal domain of lipoprotein lipase causes familial chylomicronemia. Hum Mutat. 1996;8(4):381-3. [PubMed Link Image]
  46. Wiebusch H, Funke H, Santer R, Richter W, Assmann G: A novel missense (E163G) mutation in the catalytic subunit of lipoprotein lipase causes familial chylomicronemia. Hum Mutat. 1996;8(4):392. [PubMed Link Image]
  47. Rouis M, Lohse P, Dugi KA, Lohse P, Beg OU, Ronan R, Talley GD, Brunzell JD, Santamarina-Fojo S: Homozygosity for two point mutations in the lipoprotein lipase (LPL) gene in a patient with familial LPL deficiency: LPL(Asp9-->Asn, Tyr262-->His). J Lipid Res. 1996 Mar;37(3):651-61. [PubMed Link Image]
  48. Benlian P, De Gennes JL, Foubert L, Zhang H, Gagne SE, Hayden M: Premature atherosclerosis in patients with familial chylomicronemia caused by mutations in the lipoprotein lipase gene. N Engl J Med. 1996 Sep 19;335(12):848-54. [PubMed Link Image]
  49. Foubert L, Bruin T, De Gennes JL, Ehrenborg E, Furioli J, Kastelein J, Benlian P, Hayden M: A single Ser259Arg mutation in the gene for lipoprotein lipase causes chylomicronemia in Moroccans of Berber ancestry. Hum Mutat. 1997;10(3):179-85. [PubMed Link Image]
  50. Mailly F, Palmen J, Muller DP, Gibbs T, Lloyd J, Brunzell J, Durrington P, Mitropoulos K, Betteridge J, Watts G, Lithell H, Angelico F, Humphries SE, Talmud PJ: Familial lipoprotein lipase (LPL) deficiency: a catalogue of LPL gene mutations identified in 20 patients from the UK, Sweden, and Italy. Hum Mutat. 1997;10(6):465-73. [PubMed Link Image]
  51. Foubert L, De Gennes JL, Lagarde JP, Ehrenborg E, Raisonnier A, Girardet JP, Hayden MR, Benlian P: Assessment of French patients with LPL deficiency for French Canadian mutations. J Med Genet. 1997 Aug;34(8):672-5. [PubMed Link Image]
  52. Henderson HE, Bijvoet SM, Mannens MA, Bruin T, Erkelens DW, Hayden MR, Kastelein JJ: Ile225Thr loop mutation in the lipoprotein lipase (LPL) gene is a de novo event. Am J Med Genet. 1998 Jul 24;78(4):313-6. [PubMed Link Image]
  53. Henderson H, Leisegang F, Hassan F, Hayden M, Marais D: A novel Glu421Lys substitution in the lipoprotein lipase gene in pregnancy-induced hypertriglyceridemic pancreatitis. Clin Chim Acta. 1998 Jan 12;269(1):1-12. [PubMed Link Image]
  54. Evans D, Wendt D, Ahle S, Guerra A, Beisiegel U: Compound heterozygosity for a new (S259G) and a previously described (G188E) mutation in lipoprotein lipase (LpL) as a cause of chylomicronemia. Mutations in brief no. 183. Online. Hum Mutat. 1998;12(3):217. [PubMed Link Image]
  55. Zhang Q, Liu Y, Liu BW, Fan P, Cavanna J, Galton DJ: Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII that relate to coronary artery disease: a study in Chinese and European subjects. Mol Genet Metab. 1998 Jul;64(3):177-83. [PubMed Link Image]
  56. Nickerson DA, Taylor SL, Weiss KM, Clark AG, Hutchinson RG, Stengard J, Salomaa V, Vartiainen E, Boerwinkle E, Sing CF: DNA sequence diversity in a 9.7-kb region of the human lipoprotein lipase gene. Nat Genet. 1998 Jul;19(3):233-40. [PubMed Link Image]
  57. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  58. Takagi A, Ikeda Y, Takeda E, Yamamoto A: A newly identified lipoprotein lipase (LPL) gene mutation (F270L) in a Japanese patient with familial LPL deficiency. Biochim Biophys Acta. 2000 Nov 15;1502(3):433-46. [PubMed Link Image]
  59. Ikeda Y, Goji K, Takagi A: A compound heterozygote for a novel missense mutation (G105R) in exon 3 and a missense mutation (D204E) in exon 5 of the lipoprotein lipase gene in a Japanese infant with hyperchylomicronaemia. Clin Sci (Lond). 2000 Dec;99(6):569-78. [PubMed Link Image]
  60. Hoffmann MM, Jacob S, Luft D, Schmulling RM, Rett K, Marz W, Haring HU, Matthaei S: Type I hyperlipoproteinemia due to a novel loss of function mutation of lipoprotein lipase, Cys(239)-->Trp, associated with recurrent severe pancreatitis. J Clin Endocrinol Metab. 2000 Dec;85(12):4795-8. [PubMed Link Image]
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Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5549
Enzyme 11 Name Monoglyceride lipase
Enzyme 11 Synonyms
  1. MGL
  2. HU-K5
  3. Lysophospholipase homolog
  4. Lysophospholipase-like
Enzyme 11 Gene Name MGLL
Enzyme 11 Protein Sequence >Monoglyceride lipase
MPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEE
LARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG
HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPID
SSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADR
LCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTA
SPP
Enzyme 11 Number of Residues 303
Enzyme 11 Molecular Weight 33261.1
Enzyme 11 Theoretical pI 7.00
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Lipid transport and metabolism
Enzyme 11 Specific Function Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes 2-arachidonoylglycerol, a putative endocannabinoid
Enzyme 11 Pathways
Enzyme 11 Reactions
  • Hydrolyses glycerol monoesters of long-chain fatty acids ALL_REAC (other) R01351 R01352 REFERENCE 1 [PMID:6776896] AUTHORS Mentlein R, Heiland S, Heymann E. TITLE Simultaneous purification and comparative characterization of six serine hydrolases from rat liver microsomes. JOURNAL Arch. Biochem. Biophys. 200 (1980) 547-59. ORGANISM Rattus norvegicus [GN:rno] REFERENCE 2 [PMID:5916497] AUTHORS Pope JL, McPherson JC, Tidwell HC. TITLE A study of a monoglyceride-hydrolyzing enzyme of intestinal mucosa. JOURNAL J. Biol. Chem. 241 (1966) 2306-10. ORGANISM Rattus norvegicus [GN:rno]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 14594904 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q99685 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name MGLL_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >912 bp
ATGCCAGAGGAAAGTTCCCCCAGGCGGACCCCGCAGAGCATTCCCTACCAGGACCTCCCT
CACCTGGTCAATGCAGACGGACAGTACCTCTTCTGCAGGTACTGGAAACCCACAGGCACA
CCCAAGGCCCTCATCTTTGTGTCCCATGGAGCCGGAGAGCACAGTGGCCGCTATGAAGAG
CTGGCTCGGATGCTGATGGGGCTGGACCTGCTGGTGTTCGCCCACGACCATGTTGGCCAC
GGACAGAGCGAAGGGGAGAGGATGGTAGTGTCTGACTTCCACGTTTTCGTCAGGGATGTG
TTGCAGCATGTGGATTCCATGCAGAAAGACTACCCTGGGCTTCCTGTCTTCCTTCTGGGC
CACTCCATGGGAGGCGCCATCGCCATCCTCACGGCCGCAGAGAGGCCGGGCCACTTCGCC
GGCATGGTACTCATTTCGCCTCTGGTTCTTGCCAATCCTGAATCTGCAACAACTTTCAAG
GTCCTTGCTGCGAAAGTGCTCAACCTTGTGCTGCCAAACTTGTCCCTCGGGCCCATCGAC
TCCAGCGTGCTCTCTCGGAATAAGACAGAGGTCGACATTTATAACTCAGACCCCCTGATC
TGCCGGGCAGGGCTGAAGGTGTGCTTCGGCATCCAACTGCTGAATGCCGTCTCACGGGTG
GAGCGCGCCCTCCCCAAGCTGACTGTGCCCTTCCTGCTGCTCCAGGGCTCTGCCGATCGC
CTATGTGACAGCAAAGGGGCCTACCTGCTCATGGAGTTAGCCAAGAGCCAGGACAAGACT
CTCAAGATTTATGAAGGTGCCTACCATGTTCTCCACAAGGAGCTTCCTGAAGTCACCAAC
TCCGTCTTCCATGAAATAAACATGTGGGTCTCTCAAAGGACAGCCACGGCAGGAACTGCG
TCCCCACCCTGA
Enzyme 11 GenBank Gene ID AJ270950 Link Image
Enzyme 11 GeneCard ID MGLL Link Image
Enzyme 11 GenAtlas ID MGLL Link Image
Enzyme 11 HGNC ID HGNC:17038 Link Image
Enzyme 11 Chromosome Location 3
Enzyme 11 Locus 3q21.3
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Wall EM, Cao J, Chen N, Buller RM, Upton C: A novel poxvirus gene and its human homolog are similar to an E. coli lysophospholipase. Virus Res. 1997 Dec;52(2):157-67. [PubMed Link Image]
  2. Karlsson M, Reue K, Xia YR, Lusis AJ, Langin D, Tornqvist H, Holm C: Exon-intron organization and chromosomal localization of the mouse monoglyceride lipase gene. Gene. 2001 Jul 11;272(1-2):11-8. [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. 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5744
Enzyme 12 Name Liver carboxylesterase 1
Enzyme 12 Synonyms
  1. Acyl-coenzyme A:cholesterol acyltransferase
  2. ACAT
  3. Brain carboxylesterase hBr1
  4. Cocaine carboxylesterase
  5. Egasyn
  6. HMSE
  7. Monocyte/macrophage serine esterase
  8. Retinyl ester hydrolase
  9. REH
  10. Serine esterase 1
  11. Triacylglycerol hydrolase
  12. TGH
Enzyme 12 Gene Name CES1
Enzyme 12 Protein Sequence >Liver carboxylesterase 1
MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPL
GPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLN
IYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST
GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLF
HRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLK
MKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIP
MQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDL
IADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPF
LKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLK
DKEVAFWTNLFAKKAVEKPPQTEHIEL
Enzyme 12 Number of Residues 567
Enzyme 12 Molecular Weight 62520.6
Enzyme 12 Theoretical pI 6.58
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Lipid transport and metabolism
Enzyme 12 Specific Function Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine. Catalyzes the transesterification of cocaine to form cocaethylene. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate
Enzyme 12 Pathways
Enzyme 12 Reactions
  • a carboxylic ester + H2O = an alcohol + a carboxylate [RN:R00630]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-17
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID P23141 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name EST1_HUMAN Link Image
Enzyme 12 PDB ID 1MX1 Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1704 bp
ATGTGGCTCCGTGCCTTTATCCTGGCCACTCTCTCTGCTTCCGCGGCTTGGGGGCATCCG
TCCTCGCCACCTGTGGTGGACACCGTGCATGGCAAAGTGCTGGGGAAGTTCGTCAGCTTA
GAAGGATTTGCACAGCCTGTGGCCATTTTCCTGGGAATCCCTTTTGCCAAGCCGCCTCTT
GGACCCCTGAGGTTTACTCCACCGCAGCCTGCAGAACCATGGAGCTTTGTGAAGAATGCC
ACCTCGTACCCTCCTATGTGCACCCAAGATCCCAAGGCGGGGCAGTTACTCTCAGAGCTA
TTTACAAACCGAAAGGAGAACATTCCTCTCAAGCTTTCTGAAGACTGTCTTTACCTCAAT
ATTTACACTCCTGCTGACTTGACCAAGAAAAACAGGCTGCCGGTGATGGTGTGGATCCAC
GGAGGGGGGCTGATGGTGGGTGCGGCATCAACCTATGATGGGCTGGCCCTTGCTGCCCAT
GAAAACGTGGTGGTGGTGACCATTCAATATCGCCTGGGCATCTGGGGATTCTTCAGCACA
GGGGATGAACACAGCCGGGGGAACTGGGGTCACCTGGACCAGGTGGCTGCCCTGCGCTGG
GTCCAGGACAACATTGCCAGCTTTGGAGGGAACCCAGGCTCTGTGACCATCTTTGGAGAG
TCAGCGGGAGGAGAAAGTGTCTCTGTTCTTGTTTTGTCTCCATTGGCCAAGAACCTCTTC
CACCGGGCCATTTCTGAGAGTGGCGTGGCCCTCACTTCTGTTCTGGTGAAGAAAGGTGAT
GTCAAGCCCTTGGCTGAGCAAATTGCTATCACTGCTGGGTGCAAAACCACCACCTCTGCT
GTCATGGTTCACTGCCTGCGACAGAAGACGGAAGAGGAGCTCTTGGAGACGACATTGAAA
ATGAAATTCTTATCTCTGGACTTACAGGGAGACCCCAGAGAGAGTCAACCCCTTCTGGGC
ACTGTGATTGATGGGATGCTGCTGCTGAAAACACCTGAAGAGCTTCAAGCTGAAAGGAAT
TTCCACACTGTCCCCTACATGGTCGGAATTAACAAGCAGGAGTTTGGCTGGTTGATTCCA
ATGCAGTTGATGAGCTATCCACTCTCCGAAGGGCAACTGGACCAGAAGACAGCCATGTCA
CTCCTGTGGAAGTCCTATCCCCTTGTTTGCATTGCTAAGGAACTGATTCCAGAAGCCACT
GAGAAATACTTAGGAGGAACAGACGACACTGTCAAAAAGAAAGACCTGTTCCTGGACTTG
ATAGCAGATGTGATGTTTGGTGTCCCATCTGTGATTGTGGCCCGGAACCACAGAGATGCT
GGAGCACCCACCTACATGTATGAGTTTCAGTACCGTCCAAGCTTCTCATCAGACATGAAA
CCCAAGACGGTGATAGGAGACCACGGGGATGAGCTCTTCTCCGTCTTTGGGGCCCCATTT
TTAAAAGAGGGTGCCTCAGAAGAGGAGATCAGACTTAGCAAGATGGTGATGAAATTCTGG
GCCAACTTTGCTCGCAATGGAAACCCCAATGGGGAAGGGCTGCCCCACTGGCCAGAGTAC
AACCAGAAGGAAGGGTATCTGCAGATTGGTGCCAACACCCAGGCGGCCCAGAAGCTGAAG
GACAAAGAAGTAGCTTTCTGGACCAACCTCTTTGCCAAGAAGGCAGTGGAGAAGCCACCC
CAGACAGAACACATAGAGCTGTGA
Enzyme 12 GenBank Gene ID M73499 Link Image
Enzyme 12 GeneCard ID CES1 Link Image
Enzyme 12 GenAtlas ID CES1 Link Image
Enzyme 12 HGNC ID HGNC:1863 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 16q22.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Munger JS, Shi GP, Mark EA, Chin DT, Gerard C, Chapman HA: A serine esterase released by human alveolar macrophages is closely related to liver microsomal carboxylesterases. J Biol Chem. 1991 Oct 5;266(28):18832-8. [PubMed Link Image]
  2. Kroetz DL, McBride OW, Gonzalez FJ: Glycosylation-dependent activity of baculovirus-expressed human liver carboxylesterases: cDNA cloning and characterization of two highly similar enzyme forms. Biochemistry. 1993 Nov 2;32(43):11606-17. [PubMed Link Image]
  3. Shibata F, Takagi Y, Kitajima M, Kuroda T, Omura T: Molecular cloning and characterization of a human carboxylesterase gene. Genomics. 1993 Jul;17(1):76-82. [PubMed Link Image]
  4. Becker A, Bottcher A, Lackner KJ, Fehringer P, Notka F, Aslanidis C, Schmitz G: Purification, cloning, and expression of a human enzyme with acyl coenzyme A: cholesterol acyltransferase activity, which is identical to liver carboxylesterase. Arterioscler Thromb. 1994 Aug;14(8):1346-55. [PubMed Link Image]
  5. Islam MR, Waheed A, Shah GN, Tomatsu S, Sly WS: Human egasyn binds beta-glucuronidase but neither the esterase active site of egasyn nor the C terminus of beta-glucuronidase is involved in their interaction. Arch Biochem Biophys. 1999 Dec 1;372(1):53-61. [PubMed Link Image]
  6. Ghosh S: Cholesteryl ester hydrolase in human monocyte/macrophage: cloning, sequencing, and expression of full-length cDNA. Physiol Genomics. 2000 Jan 24;2(1):1-8. [PubMed Link Image]
  7. Alam M, Ho S, Vance DE, Lehner R: Heterologous expression, purification, and characterization of human triacylglycerol hydrolase. Protein Expr Purif. 2002 Feb;24(1):33-42. [PubMed Link Image]
  8. 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]
  9. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  10. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, 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]
  11. Mori M, Hosokawa M, Ogasawara Y, Tsukada E, Chiba K: cDNA cloning, characterization and stable expression of novel human brain carboxylesterase. FEBS Lett. 1999 Sep 10;458(1):17-22. [PubMed Link Image]
  12. Brzezinski MR, Abraham TL, Stone CL, Dean RA, Bosron WF: Purification and characterization of a human liver cocaine carboxylesterase that catalyzes the production of benzoylecgonine and the formation of cocaethylene from alcohol and cocaine. Biochem Pharmacol. 1994 Nov 1;48(9):1747-55. [PubMed Link Image]
  13. Schindler R, Mentlein R, Feldheim W: Purification and characterization of retinyl ester hydrolase as a member of the non-specific carboxylesterase supergene family. Eur J Biochem. 1998 Feb 1;251(3):863-73. [PubMed Link Image]
  14. Satoh T, Hosokawa M: Molecular aspects of carboxylesterase isoforms in comparison with other esterases. Toxicol Lett. 1995 Dec;82-83:439-45. [PubMed Link Image]
  15. Alam M, Vance DE, Lehner R: Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: identification of the catalytic triad and a glycosylation site. Biochemistry. 2002 May 28;41(21):6679-87. [PubMed Link Image]
  16. Long RM, Calabrese MR, Martin BM, Pohl LR: Cloning and sequencing of a human liver carboxylesterase isoenzyme. Life Sci. 1991;48(11):PL43-9. [PubMed Link Image]
  17. Zschunke F, Salmassi A, Kreipe H, Buck F, Parwaresch MR, Radzun HJ: cDNA cloning and characterization of human monocyte/macrophage serine esterase-1. Blood. 1991 Jul 15;78(2):506-12. [PubMed Link Image]
  18. Riddles PW, Richards LJ, Bowles MR, Pond SM: Cloning and analysis of a cDNA encoding a human liver carboxylesterase. Gene. 1991 Dec 15;108(2):289-92. [PubMed Link Image]
  19. Zhu HJ, Patrick KS, Yuan HJ, Wang JS, Donovan JL, DeVane CL, Malcolm R, Johnson JA, Youngblood GL, Sweet DH, Langaee TY, Markowitz JS: Two CES1 gene mutations lead to dysfunctional carboxylesterase 1 activity in man: clinical significance and molecular basis. Am J Hum Genet. 2008 Jun;82(6):1241-8. Epub 2008 May 15. [PubMed Link Image]
  20. Bencharit S, Morton CL, Hyatt JL, Kuhn P, Danks MK, Potter PM, Redinbo MR: Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine: from binding promiscuity to selective inhibition. Chem Biol. 2003 Apr;10(4):341-9. [PubMed Link Image]
  21. Bencharit S, Morton CL, Xue Y, Potter PM, Redinbo MR: Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme. Nat Struct Biol. 2003 May;10(5):349-56. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5781
Enzyme 13 Name Hormone-sensitive lipase
Enzyme 13 Synonyms
  1. HSL
Enzyme 13 Gene Name LIPE
Enzyme 13 Protein Sequence >Hormone-sensitive lipase
MEPGSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPLTQ
QETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLG
KESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQET
PEQSDKQTTPVQGAKSKQGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVGS
SSDTDSPATMGGMVAQGVKLGFKGKSGYKVMSGYSGTSPHEKTSARNHRHYQDTASRLIH
NMDLRTMTQSLVTLAEDNIAFFSSQGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAH
LFDLDPETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALT
QLRALVYYAQRLLVTNRPGVLFFEGDEGLTADFLREYVTLHKGCFYGRCLGFQFTPAIRP
FLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWK
AFWNITEMEVLSSLANMASATVRVSRLLSLPPEAFEMPLTADPTLTVTISPPLAHTGPGP
VLVRLISYDLREGQDSEELSSLIKSNGQRSLELWPRPQQAPRSRSLIVHFHGGGFVAQTS
RSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERIC
LAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLQPAASPSRLLSLMDPLLPLSVL
SKCVSAYAGAKTEDHSNSDQKALGMMGLVRRDTALLLRDFRLGASSWLNSFLELSGRKSQ
KMSEPIAEPMRRSVSEAALAQPQGPLGTDSLKNLTLRDLSLRGNSETSSDTPEMSLSAET
LSPSTPSDVNFLLPPEDAGEEAEAKNELSPMDRGLGVRAAFPEGFHPRRSSQGATQMPLY
SSPIVKNPFMSPLLAPDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVE
DLPHGFLTLAALCRETRQAAELCVERIRLVLTPPAGAGPSGETGAAGVDGGCGGRH
Enzyme 13 Number of Residues 1076
Enzyme 13 Molecular Weight 116596.7
Enzyme 13 Theoretical pI 6.68
Enzyme 13 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
Process
  • alcohol metabolic process
  • cholesterol metabolic process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • small molecule metabolic process
  • sterol metabolic process
Component
Enzyme 13 General Function Involved in hydrolase activity
Enzyme 13 Specific Function In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • (1) diacylglycerol + H2O = monoacylglycerol + a carboxylate [RN:R05209]
  • (2) triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
  • (3) monoacylglycerol + H2O = glycerol + a carboxylate [RN:R07293]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 47124456 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q05469 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name LIPS_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >3231 bp
ATGGAGCCAGGTTCTAAGTCAGTGTCTAGGTCAGACTGGCAACCTGAACCACACCAGAGG
CCTATAACCCCGCTAGAGCCTGGGCCAGAAAAGACACCCATAGCCCAGCCAGAATCGAAG
ACTCTGCAGGGATCCAATACCCAACAGAAGCCTGCTTCAAACCAAAGACCCCTCACCCAG
CAGGAGACCCCTGCACAACATGATGCTGAATCCCAGAAGGAACCTAGAGCCCAACAAAAA
TCTGCTTCACAAGAGGAATTTCTTGCCCCACAGAAGCCCGCACCACAGCAATCACCTTAC
ATCCAAAGGGTGCTGCTCACTCAACAGGAAGCTGCCTCCCAGCAGGGACCTGGGCTAGGA
AAAGAATCTATAACTCAACAGGAGCCAGCATTGAGACAAAGACATGTAGCCCAGCCAGGG
CCTGGGCCAGGAGAGCCACCTCCAGCTCAACAAGAAGCTGAATCAACACCTGCGGCCCAG
GCTAAACCTGGAGCCAAAAGGGAGCCATCTGCCCCGACTGAATCTACGTCCCAAGAGACA
CCTGAACAGTCAGACAAGCAAACAACGCCAGTCCAGGGAGCCAAATCCAAGCAGGGATCT
TTGACAGAGCTGGGATTTCTAACAAAACTTCAGGAACTATCCATACAGCGATCAGCCCTA
GAGTGGAAGGCACTTTCTGAGTGGGTCACAGATTCTGAGTCAGAATCAGATGTGGGATCA
TCTTCAGACACAGATTCTCCAGCCACGATGGGTGGAATGGTGGCCCAGGGAGTGAAGCTA
GGCTTCAAAGGAAAATCTGGTTATAAAGTGATGTCAGGATACAGTGGGACGTCGCCACAT
GAGAAAACCAGTGCTCGGAATCACAGACACTACCAGGATACAGCCTCAAGGCTCATCCAC
AACATGGACCTGCGCACAATGACACAGTCGCTGGTGACTCTGGCGGAGGACAACATAGCC
TTCTTCTCGAGCCAGGGTCCTGGGGAAACGGCCCAGCGGCTGTCAGGCGTTTTTGCCGGT
GTACGGGAGCAGGCGCTGGGGCTGGAGCCGGCCCTGGGCCGCCTGCTGGGTGTGGCGCAC
CTCTTTGACCTGGACCCAGAGACACCGGCCAACGGGTACCGCAGCCTAGTGCACACAGCC
CGCTGCTGCCTGGCGCACCTCCTGCACAAATCCCGCTATGTGGCCTCCAACCGCCGCAGC
ATCTTCTTCCGCACCAGCCACAACCTGGCCGAGCTGGAGGCCTACCTGGCTGCCCTCACC
CAGCTCCGCGCTCTGGTCTACTACGCCCAGCGCCTGCTGGTTACCAATCGGCCGGGGGTA
CTCTTCTTTGAGGGCGACGAGGGGCTCACCGCCGACTTCCTCCGGGAGTATGTCACGCTG
CATAAGGGATGCTTCTATGGCCGCTGCCTGGGCTTCCAGTTCACGCCTGCCATCCGGCCA
TTCCTGCAGACCATCTACATTGGGCTGGTGTCCTTCGGGGAGCACTACAAACGCAACGAG
ACAGGCCTCAGTGTGGCCGCCAGCTCTCTCTTCACCAGCGGCCGCTTTGCCATCGACCCC
GAGCTGCGTGGGGCTGAGTTTGAGCGGATCACACAGAACCTGGACGTGCACTTCTGGAAA
GCCTTCTGGAACATCACCGAGATGGAAGTGCTATCGTCTCTGGCCAACATGGCATCGGCC
ACCGTGAGGGTAAGCCGCCTGCTCAGCCTGCCACCCGAAGCCTTTGAGATGCCACTGACT
GCCGACCCCACGCTCACGGTCACCATCTCACCCCCACTGGCCCACACAGGCCCTGGGCCC
GTCCTCGTCAGGCTCATCTCCTGTGACCTGCGTGAAGGACAGGACAGTGAGGAGCTCAGC
AGCCTGATAAAGTCCAACGGCCAACGGAGCCTGGAGCTGTGGCCGCGCCCCCAGCAGGCA
CCCCGCTCGCGGTCCCTGATAGTGCACTTCCACGGCGGTGGCTTTGTGGCCCAGACCTCC
AGATCCCACGAGCCCTACCTCAAGAGCTGGGCCCAGGAGCTGGGCGCCCCCATCATCTCC
ATCGACTACTCCCTGGCCCCTGAGGCCCCCTTCCCCCGTGCGCTGGAGGAGTGCTTCTTC
GCCTACTGCTGGGCCATCAAGCACTGCGCCCTCCTTGGCTCAACAGGGGAACGAATCTGC
CTTGCGGGGGACAGTGCAGGCGGGAACCTCTGCTTCACCGTGGCTCTTCGGGCAGCAGCC
TACGGGGTGCGGGTGCCAGATGGCATCATGGCAGCCTACCCGGCCACAATGCTGCAGCCT
GCCGCCTCTCCCTCCCGCCTGCTGAGCCTCATGGACCCCTTGCTGCCCCTCAGTGTGCTC
TCCAAGTGTGTCAGCGCCTATGCTGGTGCAAAGACGGAGGACCACTCCAACTCAGACCAG
AAAGCCCTCGGCATGATGGGGCTGGTGCGGCGGGACACAGCCCTGCTCCTCCGAGACTTC
CGCCTGGGTGCCTCCTCATGGCTCAACTCCTTCCTGGAGTTAAGTGGGCGCAAGTCCCAG
AAGATGTCGGAGCCCATAGCAGAGCCGATGCGCCGCAGTGTGTCTGAAGCAGCACTGGCC
CAGCCCCAGGGCCCACTGGGCACGGATTCCCTCAAGAACCTGACCCTGAGGGACTTGAGC
CTGAGGGGAAACTCCGAGACGTCGTCGGACACCCCCGAGATGTCGCTGTCAGCTGAGACA
CTTAGCCCCTCCACACCCTCCGATGTCAACTTCTTATTACCACCTGAGGATGCAGGGGAA
GAGGCTGAGGCCAAAAATGAGCTGAGCCCCATGGACAGAGGCCTGGGCGTCCGTGCCGCC
TTCCCCGAGGGTTTCCACCCCCGACGCTCCAGCCAGGGTGCCACACAGATGCCCCTCTAC
TCCTCACCCATAGTCAAGAACCCCTTCATGTCGCCGCTGCTGGCACCCGACAGCATGCTC
AAGAGCCTGCCACCTGTGCACATCGTGGCGTGCGCGCTGGACCCCATGCTGGACGACTCG
GTCATGCTCGCGCGGCGACTGCGCAACCTGGGCCAGCCGGTGACGCTGCGCGTGGTGGAG
GACCTGCCGCACGGCTTCCTGACCCTAGCGGCGCTGTGCCGCGAGACGCGCCAGGCCGCA
GAGCTGTGCGTGGAGCGCATCCGCCTCGTCCTCACTCCTCCCGCCGGAGCCGGGCCGAGC
GGGGAGACGGGGGCTGCGGGGGTAGACGGGGGCTGCGGGGGGCGACACTAA
Enzyme 13 GenBank Gene ID BC070041 Link Image
Enzyme 13 GeneCard ID LIPE Link Image
Enzyme 13 GenAtlas ID LIPE Link Image
Enzyme 13 HGNC ID HGNC:6621 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 19q13.2
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Langin D, Laurell H, Holst LS, Belfrage P, Holm C: Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4897-901. [PubMed Link Image]
  2. Holst LS, Langin D, Mulder H, Laurell H, Grober J, Bergh A, Mohrenweiser HW, Edgren G, Holm C: Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase. Genomics. 1996 Aug 1;35(3):441-7. [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. Aboulaich N, Ortegren U, Vener AV, Stralfors P: Association and insulin regulated translocation of hormone-sensitive lipase with PTRF. Biochem Biophys Res Commun. 2006 Nov 24;350(3):657-61. Epub 2006 Sep 28. [PubMed Link Image]
  5. Ortegren U, Yin L, Ost A, Karlsson H, Nystrom FH, Stralfors P: Separation and characterization of caveolae subclasses in the plasma membrane of primary adipocytes; segregation of specific proteins and functions. FEBS J. 2006 Jul;273(14):3381-92. Epub 2006 Jun 26. [PubMed Link Image]
  6. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  7. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6942
Enzyme 14 Name Microsomal triglyceride transfer protein large subunit
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name MTTP
Enzyme 14 Protein Sequence >Microsomal triglyceride transfer protein large subunit
MILLAVLFLCFISSYSASVKGHTTGLSLNNDRLYKLTYSTEVLLDRGKGKLQDSVGYRIS
SNVDVALLWRNPDGDDDQLIQITMKDVNVENVNQQRGEKSIFKGKSPSKIMGKENLEALQ
RPTLLHLIHGKVKEFYSYQNEAVAIENIKRGLASLFQTQLSSGTTNEVDISGNCKVTYQA
HQDKVIKIKALDSCKIARSGFTTPNQVLGVSSKATSVTTYKIEDSFVIAVLAEETHNFGL
NFLQTIKGKIVSKQKLELKTTEAGPRLMSGKQAAAIIKAVDSKYTAIPIVGQVFQSHCKG
CPSLSELWRSTRKYLQPDNLSKAEAVRNFLAFIQHLRTAKKEEILQILKMENKEVLPQLV
DAVTSAQTSDSLEAILDFLDFKSDSSIILQERFLYACGFASHPNEELLRALISKFKGSIG
SSDIRETVMIITGTLVRKLCQNEGCKLKAVVEAKKLILGGLEKAEKKEDTRMYLLALKNA
LLPEGIPSLLKYAEAGEGPISHLATTALQRYDLPFITDEVKKTLNRIYHQNRKVHEKTVR
TAAAAIILNNNPSYMDVKNILLSIGELPQEMNKYMLAIVQDILRFEMPASKIVRRVLKEM
VAHNYDRFSRSGSSSAYTGYIERSPRSASTYSLDILYSGSGILRRSNLNIFQYIGKAGLH
GSQVVIEAQGLEALIAATPDEGEENLDSYAGMSAILFDVQLRPVTFFNGYSDLMSKMLSA
SGDPISVVKGLILLIDHSQELQLQSGLKANIEVQGGLAIDISGAMEFSLWYRESKTRVKN
RVTVVITTDITVDSSFVKAGLETSTETEAGLEFISTVQFSQYPFLVCMQMDKDEAPFRQF
EKKYERLSTGRGYVSQKRKESVLAGCEFPLHQENSEMCKVVFAPQPDSTSSGWF
Enzyme 14 Number of Residues 894
Enzyme 14 Molecular Weight 99350.3
Enzyme 14 Theoretical pI 8.62
Enzyme 14 GO Classification
Function
  • lipid transporter activity
  • substrate-specific transporter activity
  • transporter activity
Process
  • establishment of localization
  • lipid transport
  • transport
Component
Enzyme 14 General Function Involved in lipid transporter activity
Enzyme 14 Specific Function Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces. Required for the secretion of plasma lipoproteins that contain apolipoprotein B
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-18
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 414669 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P55157 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name MTP_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2685 bp
ATGATTCTTCTTGCTGTGCTTTTTCTCTGCTTCATTTCCTCATATTCAGCTTCTGTTAAA
GGTCACACAACTGGTCTCTCATTAAATAATGACCGGCTGTACAAGCTCACGTACTCCACT
GAAGTTCTTCTTGATCGGGGCAAAGGAAAACTGCAAGACAGCGTGGGCTACCGCATTTCC
TCCAACGTGGATGTGGCCTTACTATGGAGGAATCCTGATGGTGATGATGACCAGTTGATC
CAAATAACGATGAAGGATGTAAATGTTGAAAATGTGAATCAGCAGAGAGGAGAGAAGAGC
ATCTTCAAAGGAAAAAGCCCATCTAAAATAATGGGAAAGGAAAACTTGGAAGCTCTGCAA
AGACCTACGCTCCTTCATCTAATCCATGGAAAGGTCAAAGAGTTCTACTCATATCAAAAT
GAGGCAGTGGCCATAGAAAATATCAAGAGAGGTCTGGCTAGCCTATTTCAGACACAGTTA
AGCTCTGGAACCACCAATGAGGTAGATATCTCTGGAAATTGTAAAGTGACCTACCAGGCT
CATCAAGACAAAGTGATCAAAATTAAGGCCTTGGATTCATGCAAAATAGCGAGGTCTGGA
TTTACGACCCCAAATCAGGTCTTGGGTGTCAGTTCAAAAGCTACATCTGTCACCACCTAT
AAGATAGAAGACAGCTTTGTTATAGCTGTGCTTGCTGAAGAAACACACAATTTTGGACTG
AATTTCCTACAAACCATTAAGGGGAAAATAGTATCGAAGCAGAAATTAGAGCTGAAGACA
ACCGAAGCAGGCCCAAGATTGATGTCTGGAAAGCAGGCTGCAGCCATAATCAAAGCAGTT
GATTCAAAGTACACGGCCATTCCCATTGTGGGGCAGGTCTTCCAGAGCCACTGTAAAGGA
TGTCCTTCTCTCTCGGAGCTCTGGCGGTCCACCAGGAAATACCTGCAGCCTGACAACCTT
TCCAAGGCTGAGGCTGTCAGAAACTTCCTGGCCTTCATTCAGCACCTCAGGACTGCGAAG
AAAGAAGAGATCCTTCAAATACTAAAGATGGAAAATAAGGAAGTATTACCTCAGCTGGTG
GATGCTGTCACCTCTGCTCAGACCTCAGACTCATTAGAAGCCATTTTGGACTTTTTGGAT
TTCAAAAGTGACAGCAGCATTATCCTCCAGGAGAGGTTTCTCTATGCCTGTGGATTTGCT
TCTCATCCCAATGAAGAACTCCTGAGAGCCCTCATTAGTAAGTTCAAAGGTTCTATTGGT
AGCAGTGACATCAGAGAAACTGTTATGATCATCACTGGGACACTTGTCAGAAAGTTGTGT
CAGAATGAAGGCTGCAAACTCAAAGCAGTAGTGGAAGCTAAGAAGTTAATCCTGGGAGGA
CTTGAAAAAGCAGAGAAAAAAGAGGACACCAGGATGTATCTGCTGGCTTTGAAGAATGCC
CTGCTTCCAGAAGGCATCCCAAGTCTTCTGAAGTATGCAGAAGCAGGAGAAGGGCCCATC
AGCCACCTGGCTACCACTGCTCTCCAGAGATATGATCTCCCTTTCATAACTGATGAGGTG
AAGAAGACCTTAAACAGAATATACCACCAAAACCGTAAAGTTCATGAAAAGACTGTGCGC
ACTGCTGCAGCTGCTATCATTTTAAATAACAATCCATCCTACATGGACGTCAAGAACATC
CTGCTGTCTATTGGGGAGCTTCCCCAAGAAATGAATAAATACATGCTCGCCATTGTTCAA
GACATCCTACGTTTTGAAATGCCTGCAAGCAAAATTGTCCGTCGAGTTCTGAAGGAAATG
GTCGCTCACAATTATGACCGTTTCTCCAGGAGTGGATCTTCTTCTGCCTACACTGGCTAC
ATAGAACGTAGTCCCCGTTCGGCATCTACTTACAGCCTAGACATTCTCTACTCGGGTTCT
GGCATTCTAAGGAGAAGTAACCTGAACATCTTTCAGTACATTGGGAAGGCTGGTCTTCAC
GGTAGCCAGGTGGTTATTGAAGCCCAAGGACTGGAAGCCTTAATCGCAGCCACCCCTGAC
GAGGGGGAGGAGAACCTTGACTCCTATGCTGGTATGTCAGCCATCCTCTTTGATGTTCAG
CTCAGACCTGTCACCTTTTTCAACGGATACAGTGATTTGATGTCCAAAATGCTGTCAGCA
TCTGGCGACCCTATCAGTGTGGTGAAAGGACTTATTCTGCTAATAGATCATTCTCAGGAA
CTTCAGTTACAATCTGGACTAAAAGCCAATATAGAGGTCCAGGGTGGTCTAGCTATTGAT
ATTTCAGGTGCAATGGAGTTTAGCTTGTGGTATCGTGAGTCTAAAACCCGAGTGAAAAAT
AGGGTGACTGTGGTAATAACCACTGACATCACAGTGGACTCCTCTTTTGTGAAAGCTGGC
CTGGAAACCAGTACAGAAACAGAAGCAGGCTTGGAGTTTATCTCCACAGTGCAGTTTTCT
CAGTACCCATTCTTAGTTTGCATGCAGATGGACAAGGATGAAGCTCCATTCAGGCAATTT
GAGAAAAAGTACGAAAGGCTGTCCACAGGCAGAGGTTATGTCTCTCAGAAAAGAAAAGAA
AGCGTATTAGCAGGATGTGAATTCCCGCTCCATCAAGAGAACTCAGAGATGTGCAAAGTG
GTGTTTGCCCCTCAGCCGGATAGTACTTCCAGCGGATGGTTTTGA
Enzyme 14 GenBank Gene ID X75500 Link Image
Enzyme 14 GeneCard ID MTTP Link Image
Enzyme 14 GenAtlas ID MTTP Link Image
Enzyme 14 HGNC ID HGNC:7467 Link Image
Enzyme 14 Chromosome Location 4
Enzyme 14 Locus 4q24
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Shoulders CC, Brett DJ, Bayliss JD, Narcisi TM, Jarmuz A, Grantham TT, Leoni PR, Bhattacharya S, Pease RJ, Cullen PM, et al.: Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein. Hum Mol Genet. 1993 Dec;2(12):2109-16. [PubMed Link Image]
  2. Sharp D, Blinderman L, Combs KA, Kienzle B, Ricci B, Wager-Smith K, Gil CM, Turck CW, Bouma ME, Rader DJ, et al.: Cloning and gene defects in microsomal triglyceride transfer protein associated with abetalipoproteinaemia. Nature. 1993 Sep 2;365(6441):65-9. [PubMed Link Image]
  3. Sharp D, Ricci B, Kienzle B, Lin MC, Wetterau JR: Human microsomal triglyceride transfer protein large subunit gene structure. Biochemistry. 1994 Aug 9;33(31):9057-61. [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. Hagan DL, Kienzle B, Jamil H, Hariharan N: Transcriptional regulation of human and hamster microsomal triglyceride transfer protein genes. Cell type-specific expression and response to metabolic regulators. J Biol Chem. 1994 Nov 18;269(46):28737-44. [PubMed Link Image]
  7. Shoulders CC, Narcisi TM, Read J, Chester A, Brett DJ, Scott J, Anderson TA, Levitt DG, Banaszak LJ: The abetalipoproteinemia gene is a member of the vitellogenin family and encodes an alpha-helical domain. Nat Struct Biol. 1994 May;1(5):285-6. [PubMed Link Image]
  8. Narcisi TM, Shoulders CC, Chester SA, Read J, Brett DJ, Harrison GB, Grantham TT, Fox MF, Povey S, de Bruin TW, et al.: Mutations of the microsomal triglyceride-transfer-protein gene in abetalipoproteinemia. Am J Hum Genet. 1995 Dec;57(6):1298-310. [PubMed Link Image]
  9. Rehberg EF, Samson-Bouma ME, Kienzle B, Blinderman L, Jamil H, Wetterau JR, Aggerbeck LP, Gordon DA: A novel abetalipoproteinemia genotype. Identification of a missense mutation in the 97-kDa subunit of the microsomal triglyceride transfer protein that prevents complex formation with protein disulfide isomerase. J Biol Chem. 1996 Nov 22;271(47):29945-52. [PubMed Link Image]
  10. Wang J, Hegele RA: Microsomal triglyceride transfer protein (MTP) gene mutations in Canadian subjects with abetalipoproteinemia. Hum Mutat. 2000 Mar;15(3):294-5. [PubMed Link Image]
  11. Ohashi K, Ishibashi S, Osuga J, Tozawa R, Harada K, Yahagi N, Shionoiri F, Iizuka Y, Tamura Y, Nagai R, Illingworth DR, Gotoda T, Yamada N: Novel mutations in the microsomal triglyceride transfer protein gene causing abetalipoproteinemia. J Lipid Res. 2000 Aug;41(8):1199-204. [PubMed Link Image]
  12. Ledmyr H, Karpe F, Lundahl B, McKinnon M, Skoglund-Andersson C, Ehrenborg E: Variants of the microsomal triglyceride transfer protein gene are associated with plasma cholesterol levels and body mass index. J Lipid Res. 2002 Jan;43(1):51-8. [PubMed Link Image]
  13. Lancellotti S, Di Leo E, Penacchioni JY, Balli F, Viola L, Bertolini S, Calandra S, Tarugi P: Hypobetalipoproteinemia with an apparently recessive inheritance due to a "de novo" mutation of apolipoprotein B. Biochim Biophys Acta. 2004 Jan 20;1688(1):61-7. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 8308
Enzyme 15 Name Protein disulfide-isomerase
Enzyme 15 Synonyms
  1. PDI
  2. Cellular thyroid hormone-binding protein
  3. Prolyl 4-hydroxylase subunit beta
  4. p55
Enzyme 15 Gene Name P4HB
Enzyme 15 Protein Sequence >Protein disulfide-isomerase
MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALA
PEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGR
EADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAID
DIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEF
TEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQR
ILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQEL
PEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENI
VIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGD
DDDLEDLEEAEEPDMEEDDDQKAVKDEL
Enzyme 15 Number of Residues 508
Enzyme 15 Molecular Weight 57115.8
Enzyme 15 Theoretical pI 4.49
Enzyme 15 GO Classification
Function
  • catalytic activity
  • isomerase activity
Process
  • cell redox homeostasis
  • cellular homeostasis
  • cellular process
Component
  • endoplasmic reticulum
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • organelle
Enzyme 15 General Function Involved in isomerase activity
Enzyme 15 Specific Function This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions
  • Catalyses the rearrangement of -S-S- bonds in proteins
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-17
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 35655 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P07237 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PDIA1_HUMAN Link Image
Enzyme 15 PDB ID 1MEK Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1527 bp
ATGCTGCGCCGCGCTCTGCTGTGCCTGCCGTGGNCCGCCCTGGTGCGCGCCGACGCCCCC
GAGGAGGAGGACCACGTCTTGGTGCTGCGGAAAAGCAACTTCGCGGAGGCGCTGGCGGCC
CACAAGTACCCGCCGGTGGAGTTCCATGCCCCCTGGTGTGGCCACTGCAAGGCTCTGGCC
CCTGAGTATGCCAAAGCCGCTGGGAAGCTGAAGGCAGAAGGTTCCGAGATCAGGTTGGCC
AAGGTGGACGCCACGGAGGAGTCTGACCTAGCCCAGCAGTACGGCGTGCGCGGCTATCCC
ACCATCAAGTTCTTCAGGAATGGAGACACGGCTTCCCCCAAGGAATATACAGCTGGCAGA
GAGGCTGATGACATCGTGAACTGGCTGAAGAAGCGCACGGGCCCGGCTGCCACCACCCTG
CCTGACGGCGCAGCTGCAGAGTCCTTGGTGGAGTCCAGCGAGGTGGCCGTCATCGGCTTC
TTCAAGGACGTGGAGTCGGACTCTGCCAAGCAGTTTTTGCAGGCAGCAGAGGCCATCGAT
GACATACCATTTGGGATCACTTCCAACAGTGACGTGTTCTCCAAATACCAGCTCGACAAA
GATGGGGTTGTCCTCTTTAAGAAGTTTGATGAAGGCCGGAACAACTTTGAAGGGGAGGTC
ACCAAGGAGAACCTGCTGGACTTTATCAAACACAACCAGCTGCCCCTTGTCATCGAGTTC
ACCGAGCAGACAGCCCCGAAGATTTTTGGAGGTGAAATCAAGACTCACATCCTGCTGTTC
TTGCCCAAGAGTGTGTCTGACTATGACGGCAAACTGAGCAACTTCAAAACAGCAGCCGAG
AGCTTCAAGGGCAAGATCCTGTTCATCTTCATCGACAGCGACCACACCGACAACCAGCGC
ATCCTCGAGTTCTTTGGCCTGAAGAAGGAAGAGTGCCCGGCCGTGCGCCTCATCACCTTG
GAGGAGGAGATGACCAAGTACAAGCCCGAATCGGAGGAGCTGACGGCAGAGAGGATCACA
GAGTTCTGCCACCGCTTCCTGGAGGGCAAAATCAAGCCCCACCTGATGAGCCAGGAGCTG
CCGGAGGACTGGGACAAGCAGCCTGTCAAGGTGCTTGTTGGGAAGAACTTTGAAGACGTG
GCTTTTGATGAGAAAAAAAACGTCTTTGTGGAGTTCTATGCCCCATGGTGTGGTCACTGC
AAACAGTTGGCTCCCATTTGGGATAAACTGGGAGAGACGTACAAGGACCATGAGAACATC
GTCATCGCCAAGATGGACTCGACTGCCAACGAGGTGGAGGCCGTCAAAGTGCACGGCTTC
CCCACACTCGGGTTCTTTCCTGCCAGTGCCGACAGGACGGTCATTGATTACAACGGGGAA
CGCACGCTGGATGGTTTTAAGAAATTCCTAGAGAGCGGTGGCCAAGATGGGGCAGGGGAT
GTTGACGACCTCGAGGACCTCGAAGAAGCAGAGGAGCCAGACATGGAGGAAGACGATGAC
CAGAAAGCTGTGAAAGATGAACTGTAA
Enzyme 15 GenBank Gene ID X05130 Link Image
Enzyme 15 GeneCard ID P4HB Link Image
Enzyme 15 GenAtlas ID P4HB Link Image
Enzyme 15 HGNC ID HGNC:8548 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 17q25
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Pihlajaniemi T, Helaakoski T, Tasanen K, Myllyla R, Huhtala ML, Koivu J, Kivirikko KI: Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J. 1987 Mar;6(3):643-9. [PubMed Link Image]
  2. Cheng SY, Gong QH, Parkison C, Robinson EA, Appella E, Merlino GT, Pastan I: The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum. J Biol Chem. 1987 Aug 15;262(23):11221-7. [PubMed Link Image]
  3. Tasanen K, Parkkonen T, Chow LT, Kivirikko KI, Pihlajaniemi T: Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase. J Biol Chem. 1988 Nov 5;263(31):16218-24. [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. Tasanen K, Oikarinen J, Kivirikko KI, Pihlajaniemi T: Promoter of the gene for the multifunctional protein disulfide isomerase polypeptide. Functional significance of the six CCAAT boxes and other promoter elements. J Biol Chem. 1992 Jun 5;267(16):11513-9. [PubMed Link Image]
  7. Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed Link Image]
  8. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  9. Ward LD, Hong J, Whitehead RH, Simpson RJ: Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis. Electrophoresis. 1990 Oct;11(10):883-91. [PubMed Link Image]
  10. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  11. Urade R, Oda T, Ito H, Moriyama T, Utsumi S, Kito M: Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease. J Biochem (Tokyo). 1997 Oct;122(4):834-42. [PubMed Link Image]
  12. Morris JI, Varandani PT: Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase). Biochim Biophys Acta. 1988 Feb 28;949(2):169-80. [PubMed Link Image]
  13. Bauw G, Rasmussen HH, van den Bulcke M, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes. Electrophoresis. 1990 Jul;11(7):528-36. [PubMed Link Image]
  14. Mezghrani A, Courageot J, Mani JC, Pugniere M, Bastiani P, Miquelis R: Protein-disulfide isomerase (PDI) in FRTL5 cells. pH-dependent thyroglobulin/PDI interactions determine a novel PDI function in the post-endoplasmic reticulum of thyrocytes. J Biol Chem. 2000 Jan 21;275(3):1920-9. [PubMed Link Image]
  15. Fenouillet E, Barbouche R, Courageot J, Miquelis R: The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding. J Infect Dis. 2001 Mar 1;183(5):744-52. Epub 2001 Jan 25. [PubMed Link Image]
  16. Lumb RA, Bulleid NJ: Is protein disulfide isomerase a redox-dependent molecular chaperone? EMBO J. 2002 Dec 16;21(24):6763-70. [PubMed Link Image]
  17. Ko HS, Uehara T, Nomura Y: Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death. J Biol Chem. 2002 Sep 20;277(38):35386-92. Epub 2002 Jul 2. [PubMed Link Image]
  18. Gallina A, Hanley TM, Mandel R, Trahey M, Broder CC, Viglianti GA, Ryser HJ: Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry. J Biol Chem. 2002 Dec 27;277(52):50579-88. Epub 2002 Sep 5. [PubMed Link Image]
  19. Barbouche R, Miquelis R, Jones IM, Fenouillet E: Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion. J Biol Chem. 2003 Jan 31;278(5):3131-6. Epub 2002 Sep 5. [PubMed Link Image]
  20. Basrur V, Yang F, Kushimoto T, Higashimoto Y, Yasumoto K, Valencia J, Muller J, Vieira WD, Watabe H, Shabanowitz J, Hearing VJ, Hunt DF, Appella E: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J Proteome Res. 2003 Jan-Feb;2(1):69-79. [PubMed Link Image]
  21. Wilkinson B, Gilbert HF: Protein disulfide isomerase. Biochim Biophys Acta. 2004 Jun 1;1699(1-2):35-44. [PubMed Link Image]
  22. Markovic I, Stantchev TS, Fields KH, Tiffany LJ, Tomic M, Weiss CD, Broder CC, Strebel K, Clouse KA: Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1 envelope-mediated T-cell fusion during viral entry. Blood. 2004 Mar 1;103(5):1586-94. Epub 2003 Oct 30. [PubMed Link Image]
  23. Barbouche R, Lortat-Jacob H, Jones IM, Fenouillet E: Glycosaminoglycans and protein disulfide isomerase-mediated reduction of HIV Env. Mol Pharmacol. 2005 Apr;67(4):1111-8. Epub 2005 Jan 11. [PubMed Link Image]
  24. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  25. Kemmink J, Darby NJ, Dijkstra K, Scheek RM, Creighton TE: Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase. Protein Sci. 1995 Dec;4(12):2587-93. [PubMed Link Image]
  26. Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE: Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry. 1996 Jun 18;35(24):7684-91. [PubMed Link Image]
  27. Kemmink J, Dijkstra K, Mariani M, Scheek RM, Penka E, Nilges M, Darby NJ: The structure in solution of the b domain of protein disulfide isomerase. J Biomol NMR. 1999 Apr;13(4):357-68. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 8626
Enzyme 16 Name 2-acylglycerol O-acyltransferase 2
Enzyme 16 Synonyms
  1. Acyl-CoA:monoacylglycerol acyltransferase 2
  2. MGAT2
  3. hMGAT2
  4. Diacylglycerol O-acyltransferase candidate 5
  5. hDC5
  6. Diacylglycerol acyltransferase 2-like protein 5
  7. Monoacylglycerol O-acyltransferase 2
Enzyme 16 Gene Name MOGAT2
Enzyme 16 Protein Sequence >2-acylglycerol O-acyltransferase 2
MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLD
RDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFAN
LCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNL
LGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSG
SWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEE
VNQLHQRYIKELCNLFEAHKLKFNIPADQHLEFC
Enzyme 16 Number of Residues 334
Enzyme 16 Molecular Weight 38195.3
Enzyme 16 Theoretical pI 9.77
Enzyme 16 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 16 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 16 Specific Function Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity
Enzyme 16 Pathways
Enzyme 16 Reactions
  • acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • 23-37 38-59 103-123
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 37537527 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q3SYC2 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name MOGT2_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1005 bp
ATGGTAGAGTTCGCGCCCTTGTTTATGCCGTGGGAGCGCAGGCTGCAGACACTTGCTGTC
CTACAGTTTGTCTTCTCCTTCTTGGCACTGGCCGAGATCTGCACTGTGGGCTTCATAGCC
CTCCTGTTTACAAGATTCTGGCTCCTCACTGTCCTGTATGCGGCCTGGTGGTATCTGGAC
CGAGACAAGCCACGGCAGGGGGGCCGGCACATCCAGGCCATCAGGTGCTGGACTATATGG
AAGTACATGAAGGACTATTTCCCCATCTCGCTGGTCAAGACTGCTGAGCTGGACCCCTCT
CGGAACTACATTGCGGGCTTCCACCCCCATGGAGTCCTGGCAGTCGGAGCCTTTGCCAAC
CTGTGCACTGAGAGCACAGGCTTCTCTTCGATCTTCCCCGGTATCCGCCCCCATCTGATG
ATGCTGACCTTGTGGTTCCGGGCCCCCTTCTTCAGAGATTACATCATGTCTGCAGGGTTG
GTCACATCAGAAAAGGAGAGTGCTGCTCACATTCTGAACAGGAAGGGTGGCGGAAACTTG
CTGGGCATCATTGTAGGGGGTGCCCAGGAGGCCCTGGATGCCAGGCCTGGATCCTTCACG
CTGTTACTGCGGAACCGAAAGGGCTTCGTCAGGCTCGCCCTGACACACGGGGCACCCCTG
GTGCCAATCTTCTCCTTCGGGGAGAATGACCTATTTGACCAGATTCCCAACTCTTCTGGC
TCCTGGTTACGCTATATCCAGAATCGGTTGCAGAAGATCATGGGCATCTCCCTCCCACTC
TTTCATGGCCGTGGTGTCTTCCAGTACAGCTTTGGTTTAATACCCTACCGCCGGCCCATC
ACCACTGTGGTGGGGAAGCCCATCGAGGTACAGAAGACGCTGCATCCCTCGGAGGAGGAG
GTGAACCAGCTGCACCAGCGTTATATCAAAGAGCTGTGCAACCTCTTCGAGGCCCACAAA
CTTAAGTTCAACATCCCTGCTGACCAGCACTTGGAGTTCTGCTGA
Enzyme 16 GenBank Gene ID NM_025098.2 Link Image
Enzyme 16 GeneCard ID MOGAT2 Link Image
Enzyme 16 GenAtlas ID MOGAT2 Link Image
Enzyme 16 HGNC ID HGNC:23248 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 11q13.5
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Yen CL, Farese RV Jr: MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine. J Biol Chem. 2003 May 16;278(20):18532-7. Epub 2003 Mar 5. [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. Lockwood JF, Cao J, Burn P, Shi Y: Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity. Am J Physiol Endocrinol Metab. 2003 Nov;285(5):E927-37. Epub 2003 Jun 24. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 8715
Enzyme 17 Name Patatin-like phospholipase domain-containing protein 4
Enzyme 17 Synonyms
  1. Protein GS2
Enzyme 17 Gene Name PNPLA4
Enzyme 17 Protein Sequence >Patatin-like phospholipase domain-containing protein 4
MKHINLSFAACGFLGIYHLGAASALCRHGKKLVKDVKAFAGASAGSLVASVLLTAPEKIE
ECNQFTYKFAEEIRRQSFGAVTPGYDFMARLRSGMESILPPSAHELAQNRLHVSITNAKT
RENHLVSTFSSREDLIKVLLASSFVPIYAGLKLVEYKGQKWVDGGLTNALPILPVGRTVT
ISPFSGRLDISPQDKGQLDLYVNIAKQDIMLSLANLVRLNQALFPPSKRKMESLYQCGFD
DTVKFLLKENWFE
Enzyme 17 Number of Residues 253
Enzyme 17 Molecular Weight 27980.2
Enzyme 17 Theoretical pI 9.54
Enzyme 17 GO Classification
Function
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 17 General Function Involved in metabolic process
Enzyme 17 Specific Function Lipid hydrolase
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 158260799 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P41247 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PLPL4_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >762 bp
ATGAAGCACATCAACCTATCATTTGCAGCGTGTGGATTTCTGGGCATTTACCACTTGGGG
GCAGCATCTGCACTTTGCAGACATGGCAAAAAACTTGTGAAGGATGTCAAAGCCTTCGCT
GGGGCGTCTGCGGGATCGTTGGTTGCTTCTGTTCTGCTAACAGCACCAGAAAAAATAGAG
GAATGTAACCAATTTACCTACAAGTTTGCCGAAGAAATCAGAAGGCAGTCTTTCGGGGCA
GTAACGCCCGGTTATGACTTCATGGCCCGACTAAGAAGTGGGATGGAGTCGATTCTTCCT
CCCAGCGCTCACGAGCTGGCCCAGAACCGACTGCACGTATCCATCACCAACGCCAAAACC
AGAGAAAATCACTTAGTCTCCACTTTTTCCTCCAGGGAGGACCTCATTAAGGTCCTCCTA
GCCAGCAGTTTTGTGCCCATTTATGCAGGACTGAAGCTAGTGGAATACAAAGGGCAGAAG
TGGGTGGACGGAGGCCTCACCAACGCTCTTCCCATCCTGCCCGTCGGCCGGACAGTAACC
ATCTCCCCCTTCAGTGGACGACTGGACATCTCCCCGCAGGACAAAGGGCAGCTAGATCTG
TATGTTAATATCGCCAAGCAGGATATCATGTTGTCCCTGGCAAACCTGGTGAGACTCAAC
CAAGCCCTTTTTCCCCCAAGCAAGAGGAAAATGGAATCTTTGTATCAGTGTGGTTTTGAT
GACACTGTTAAGTTTTTACTTAAAGAAAATTGGTTTGAATAA
Enzyme 17 GenBank Gene ID AK289888 Link Image
Enzyme 17 GeneCard ID PNPLA4 Link Image
Enzyme 17 GenAtlas ID PNPLA4 Link Image
Enzyme 17 HGNC ID HGNC:24887 Link Image
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Lee WC, Salido E, Yen PH: Isolation of a new gene GS2 (DXS1283E) from a CpG island between STS and KAL1 on Xp22.3. Genomics. 1994 Jul 15;22(2):372-6. [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. Jenkins CM, Mancuso DJ, Yan W, Sims HF, Gibson B, Gross RW: Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem. 2004 Nov 19;279(47):48968-75. Epub 2004 Sep 10. [PubMed Link Image]
  5. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 10076
Enzyme 18 Name Diacylglycerol O-acyltransferase 2
Enzyme 18 Synonyms
  1. Diglyceride acyltransferase 2
Enzyme 18 Gene Name DGAT2
Enzyme 18 Protein Sequence >Diacylglycerol O-acyltransferase 2
MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLN
RSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKG
GRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATE
VSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGG
AAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQ
KKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHT
MYMEALVKLFDKHKTKFGLPETEVLEVN
Enzyme 18 Number of Residues 388
Enzyme 18 Molecular Weight 43830.5
Enzyme 18 Theoretical pI 9.80
Enzyme 18 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 18 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 18 Specific Function Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation
Enzyme 18 Pathways
Enzyme 18 Reactions
  • acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol [RN:R02251]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • 76-96 98-117
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 22506631 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q96PD7 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name DGAT2_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1167 bp
ATGAAGACCCTCATAGCCGCCTACTCCGGGGTCCTGCGCGGCGAGCGTCAGGCCGAGGCT
GACCGGAGCCAGCGCTCTCACGGAGGACCTGCGCTGTCGCGCGAGGGGTCTGGGAGATGG
GGCACTGGATCCAGCATCCTCTCCGCCCTCCAGGACCTCTTCTCTGTCACCTGGCTCAAT
AGGTCCAAGGTGGAAAAGCAGCTACAGGTCATCTCAGTGCTCCAGTGGGTCCTGTCCTTC
CTTGTACTGGGAGTGGCCTGCAGTGCCATCCTCATGTACATATTCTGCACTGATTGCTGG
CTCATCGCTGTGCTCTACTTCACTTGGCTGGTGTTTGACTGGAACACACCCAAGAAAGGT
GGCAGGAGGTCACAGTGGGTCCGAAACTGGGCTGTGTGGCGCTACTTTCGAGACTACTTT
CCCATCCAGCTGGTGAAGACACACAACCTGCTGACCACCAGGAACTATATCTTTGGATAC
CACCCCCATGGTATCATGGGCCTGGGTGCCTTCTGCAACTTCAGCACAGAGGCCACAGAA
GTGAGCAAGAAGTTCCCAGGCATACGGCCTTACCTGGCTACACTGGCAGGCAACTTCCGA
ATGCCTGTGTTGAGGGAGTACCTGATGTCTGGAGGTATCTGCCCTGTCAGCCGGGACACC
ATAGACTATTTGCTTTCAAAGAATGGGAGTGGCAATGCTATCATCATCGTGGTCGGGGGT
GCGGCTGAGTCTCTGAGCTCCATGCCTGGCAAGAATGCAGTCACCCTGCGGAACCGCAAG
GGCTTTGTGAAACTGGCCCTGCGTCATGGAGCTGACCTGGTTCCCATCTACTCCTTTGGA
GAGAATGAAGTGTACAAGCAGGTGATCTTCGAGGAGGGCTCCTGGGGCCGATGGGTCCAG
AAGAAGTTCCAGAAATACATTGGTTTCGCCCCATGCATCTTCCATGGTCGAGGCCTCTTC
TCCTCCGACACCTGGGGGCTGGTGCCCTACTCCAAGCCCATCACCACTGTTGTGGGAGAG
CCCATCACCATCCCCAAGCTGGAGCACCCAACCCAGCAAGACATCGACCTGTACCACACC
ATGTACATGGAGGCCCTGGTGAAGCTCTTCGACAAGCACAAGACCAAGTTCGGCCTCCCG
GAGACTGAGGTCCTGGAGGTGAACTGA
Enzyme 18 GenBank Gene ID AB048286 Link Image
Enzyme 18 GeneCard ID DGAT2 Link Image
Enzyme 18 GenAtlas ID DGAT2 Link Image
Enzyme 18 HGNC ID HGNC:16940 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 11q13.5
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Cases S, Stone SJ, Zhou P, Yen E, Tow B, Lardizabal KD, Voelker T, Farese RV Jr: Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J Biol Chem. 2001 Oct 19;276(42):38870-6. Epub 2001 Jul 31. [PubMed Link Image]
  2. Wakimoto K, Chiba H, Michibata H, Seishima M, Kawasaki S, Okubo K, Mitsui H, Torii H, Imai Y: A novel diacylglycerol acyltransferase (DGAT2) is decreased in human psoriatic skin and increased in diabetic mice. Biochem Biophys Res Commun. 2003 Oct 17;310(2):296-302. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. 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]
  5. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, 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]
  7. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 10239
Enzyme 19 Name 2-acylglycerol O-acyltransferase 1
Enzyme 19 Synonyms
  1. Acyl-CoA:monoacylglycerol acyltransferase 1
  2. MGAT1
  3. Diacylglycerol O-acyltransferase candidate 2
  4. hDC2
  5. Diacylglycerol acyltransferase 2-like protein 1
  6. Monoacylglycerol O-acyltransferase 1
Enzyme 19 Gene Name MOGAT1
Enzyme 19 Protein Sequence >2-acylglycerol O-acyltransferase 1
MKVEFAPLNIQLARRLQTVAVLQWVLKYLLLGPMSIGITVMLIIHNYLFLYIPYLMWLYF
DWHTPERGGRRSSWIKNWTLWKHFKDYFPIHLIKTQDLDPSHNYIFGFHPHGIMAVGAFG
NFSVNYSDFKDLFPGFTSYLHVLPLWFWCPVFREYVMSVGLVSVSKKSVSYMVSKEGGGN
ISVIVLGGAKESLDAHPGKFTLFIRQRKGFVKIALTHGASLVPVVSFGENELFKQTDNPE
GSWIRTVQNKLQKIMGFALPLFHARGVFQYNFGLMTYRKAIHTVVGRPIPVRQTLNPTQE
QIEELHQTYMEELRKLFEEHKGKYGIPEHETLVLK
Enzyme 19 Number of Residues 335
Enzyme 19 Molecular Weight 38812.2
Enzyme 19 Theoretical pI 9.96
Enzyme 19 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 19 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 19 Specific Function Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Probably not involved in absorption of dietary fat in the small intestine
Enzyme 19 Pathways
Enzyme 19 Reactions
  • acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 18-38 40-60 132-152
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 148746191 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q96PD6 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name MOGT1_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1008 bp
ATGAAGGTAGAGTTTGCACCGCTCAACATCCAGCTGGCGCGGCGGCTGCAGACGGTGGCC
GTGCTGCAGTGGGTCCTGAAATACCTGCTGCTCGGGCCGATGTCCATTGGAATCACTGTG
ATGCTGATCATACACAACTATTTGTTCCTTTACATCCCTTATTTGATGTGGCTTTACTTT
GACTGGCATACCCCAGAGCGAGGAGGCAGGAGATCCAGCTGGATCAAAAATTGGACTCTT
TGGAAACACTTTAAGGACTATTTTCCAATTCATCTTATCAAAACTCAAGATTTGGATCCA
AGTCACAACTATATATTTGGGTTTCACCCCCATGGAATAATGGCAGTTGGAGCCTTTGGG
AATTTTTCTGTAAATTATTCTGACTTCAAGGACCTGTTTCCTGGCTTTACTTCATATCTT
CACGTGCTGCCACTTTGGTTCTGGTGTCCTGTCTTTCGAGAATATGTGATGAGTGTTGGG
CTGGTTTCAGTTTCCAAGAAAAGTGTGTCCTACATGGTAAGCAAGGAGGGAGGTGGAAAC
ATCTCTGTCATTGTCCTTGGGGGTGCAAAAGAATCACTGGATGCTCATCCTGGAAAGTTC
ACTCTGTTCATCCGCCAGCGGAAAGGATTTGTTAAAATTGCTTTGACCCATGGCGCCTCT
CTGGTCCCAGTGGTTTCTTTTGGTGAAAATGAACTGTTTAAACAAACTGACAACCCTGAA
GGATCATGGATTAGAACTGTTCAGAATAAACTGCAGAAGATCATGGGGTTTGCTTTGCCC
CTGTTTCATGCCAGGGGAGTTTTTCAGTACAATTTTGGCCTAATGACCTATAGGAAAGCC
ATCCACACTGTTGTTGGCCGCCCGATCCCTGTTCGTCAGACTCTGAACCCGACCCAGGAG
CAGATTGAGGAGTTACATCAGACCTATATGGAGGAACTTAGGAAATTGTTTGAGGAACAC
AAAGGAAAGTATGGCATTCCAGAGCACGAGACTCTTGTTTTAAAATGA
Enzyme 19 GenBank Gene ID NM_058165.2 Link Image
Enzyme 19 GeneCard ID MOGAT1 Link Image
Enzyme 19 GenAtlas ID MOGAT1 Link Image
Enzyme 19 HGNC ID HGNC:18210 Link Image
Enzyme 19 Chromosome Location 2
Enzyme 19 Locus 2q36.1
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Cases S, Stone SJ, Zhou P, Yen E, Tow B, Lardizabal KD, Voelker T, Farese RV Jr: Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J Biol Chem. 2001 Oct 19;276(42):38870-6. Epub 2001 Jul 31. [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. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 12903
Enzyme 20 Name 2-acylglycerol O-acyltransferase 3
Enzyme 20 Synonyms
  1. Acyl-CoA:monoacylglycerol acyltransferase 3
  2. MGAT3
  3. Diacylglycerol O-acyltransferase candidate 7
  4. hDC7
  5. Diacylglycerol acyltransferase 2-like protein 7
  6. Monoacylglycerol O-acyltransferase 3
Enzyme 20 Gene Name MOGAT3
Enzyme 20 Protein Sequence >2-acylglycerol O-acyltransferase 3
MGVATTLQPPTTSKTLQKQHLEAVGAYQYVLTFLFMGPFFSLLVFVLLFTSLWPFSVFYL
VWLYVDWDTPNQGGRRSEWIRNRAIWRQLRDYYPVKLVKTAELPPDRNYVLGAHPHGIMC
TGFLCNFSTESNGFSQLFPGLRPWLAVLAGLFYLPVYRDYIMSFGLCPVSRQSLDFILSQ
PQLGQAVVIMVGGAHEALYSVPGEHCLTLQKRKGFVRLALRHGASLVPVYSFGENDIFRL
KAFATGSWQHWCQLTFKKLMGFSPCIFWGRGLFSATSWGLLPFAVPITTVVGRPIPVPQR
LHPTEEEVNHYHALYMTALEQLFEEHKESCGVPASTCLTFI
Enzyme 20 Number of Residues 341
Enzyme 20 Molecular Weight 38729.8
Enzyme 20 Theoretical pI 8.70
Enzyme 20 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 20 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 20 Specific Function Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Also able to catalyze the terminal step in triacylglycerol synthesis by using diacylglycerol and fatty acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and oleoyl-CoA. May be involved in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes
Enzyme 20 Pathways
Enzyme 20 Reactions
  • acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 29-49 50-70 137-157
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 29124967 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q86VF5 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name MOGT3_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1026 bp
ATGGGAGTTGCCACAACCCTGCAGCCCCCAACCACTTCCAAAACCTTGCAGAAGCAGCAT
CTAGAAGCAGTGGGCGCCTACCAATATGTGCTCACTTTCCTCTTCATGGGCCCTTTCTTC
TCCCTTCTTGTCTTTGTCCTCCTCTTCACGTCACTCTGGCCCTTCTCTGTTTTTTACTTG
GTGTGGCTCTATGTGGACTGGGACACACCCAACCAAGGTGGAAGGCGTTCGGAGTGGATA
AGGAACCGGGCAATTTGGAGACAACTAAGGGATTATTATCCTGTCAAGCTGGTGAAAACA
GCAGAGCTGCCCCCGGATCGGAACTACGTGCTGGGCGCCCACCCTCATGGGATCATGTGT
ACAGGCTTCCTCTGTAATTTCTCCACCGAGAGCAATGGCTTCTCCCAGCTCTTCCCGGGG
CTCCGGCCCTGGTTAGCCGTGCTGGCTGGCCTCTTCTACCTCCCGGTCTATCGCGACTAC
ATCATGTCCTTTGGACTCTGTCCGGTGAGCCGCCAGAGCCTGGACTTCATCCTGTCCCAG
CCCCAGCTCGGGCAGGCCGTGGTCATCATGGTGGGGGGTGCGCACGAGGCCCTGTATTCA
GTCCCCGGGGAGCACTGCCTTACGCTCCAGAAGCGCAAAGGCTTCGTGCGCCTGGCGCTG
AGGCACGGGGCGTCCCTGGTGCCCGTGTACTCCTTTGGGGAGAATGACATCTTTAGACTT
AAGGCTTTTGCCACAGGCTCCTGGCAGCATTGGTGCCAGCTCACCTTCAAGAAGCTCATG
GGCTTCTCTCCTTGCATCTTCTGGGGTCGCGGTCTCTTCTCAGCCACCTCCTGGGGCCTG
CTGCCCTTTGCTGTGCCCATCACCACTGTGGTGGGCCGCCCCATCCCCGTCCCCCAGCGC
CTCCACCCCACCGAGGAGGAAGTCAATCACTATCACGCCCTCTACATGACGGCCCTGGAG
CAGCTCTTCGAGGAGCACAAGGAAAGCTGTGGGGTCCCCGCTTCCACCTGCCTCACCTTC
ATCTAG
Enzyme 20 GenBank Gene ID AY229854 Link Image
Enzyme 20 GeneCard ID MOGAT3 Link Image
Enzyme 20 GenAtlas ID MOGAT3 Link Image
Enzyme 20 HGNC ID HGNC:23249 Link Image
Enzyme 20 Chromosome Location 7
Enzyme 20 Locus 7q22.1
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Cheng D, Nelson TC, Chen J, Walker SG, Wardwell-Swanson J, Meegalla R, Taub R, Billheimer JT, Ramaker M, Feder JN: Identification of acyl coenzyme A:monoacylglycerol acyltransferase 3, an intestinal specific enzyme implicated in dietary fat absorption. J Biol Chem. 2003 Apr 18;278(16):13611-4. Epub 2003 Mar 3. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, 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 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 12922
Enzyme 21 Name Phospholipase B1, membrane-associated
Enzyme 21 Synonyms
  1. Phospholipase B
  2. hPLB
  3. Phospholipase B/lipase
  4. PLB/LIP
  5. Phospholipase A2
  6. Lysophospholipase
Enzyme 21 Gene Name PLB1
Enzyme 21 Protein Sequence >Phospholipase B1, membrane-associated
MGLRPGIFLLELLLLLGQGTPQIHTSPRKSTLEGQLWPETLKNSPFPCNPNKLGVNMPSK
SVHSLKPSDIKFVAAIGNLEIPPDPGTGDLEKQDWTERPQQVCMGVMTVLSDIIRYFSPS
VPMPVCHTGKRVIPHDGAEDLWIQAQELVRNMKENLQLDFQFDWKLINVFFSNASQCYLC
PSAQQNGLAAGGVDELMGVLDYLQQEVPRAFVNLVDLSEVAEVSRQYHGTWLSPAPEPCN
CSEETTRLAKVVMQWSYQEAWNSLLASSRYSEQESFTVVFQPFFYETTPSLHSEDPRLQD
STTLAWHLWNRMMEPAGEKDEPLSVKHGRPMKCPSQESPYLFSYRNSNYLTRLQKPQDKL
EVREGAEIRCPDKDPSDTVPTSVHRLKPADINVIGALGDSLTAGNGAGSTPGNVLDVLTQ
YRGLSWSVGGDENIGTVTTLANILREFNPSLKGFSVGTGKETSPNAFLNQAVAGGRAEDL
PVQARRLVDLMKNDTRIHFQEDWKIITLFIGGNDLCDFCNDLVHYSPQNFTDNIGKALDI
LHAEVPRAFVNLVTVLEIVNLRELYQEKKVYCPRMILRSLCPCVLKFDDNSTELATLIEF
NKKFQEKTHQLIESGRYDTREDFTVVVQPFFENVDMPKTSEGLPDNSFFAPDCFHFSSKS
HSRAASALWNNMLEPVGQKTTRHKFENKINITCPNQVQPFLRTYKNSMQGHGTWLPCRDR
APSALHPTSVHALRPADIQVVAALGDSLTAGNGIGSKPDDLPDVTTQYRGLSYSAGGDGS
LENVTTLPNILREFNRNLTGYAVGTGDANDTNAFLNQAVPGAKAEDLMSQVQTLMQKMKD
DHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSAANFVHHLRNALDVLHREVPRVLVNLV
DFLNPTIMRQVFLGNPDKCPVQQASVLCNCVLTLRENSQELARLEAFSRAYRSSMRELVG
SGRYDTQEDFSVVLQPFFQNIQLPVLADGLPDTSFFAPDCIHPNQKFHSQLARALWTNML
EPLGSKTETLDLRAEMPITCPTQNEPFLRTPRNSNYTYPIKPAIENWGSDFLCTEWKASN
SVPTSVHQLRPADIKVVAALGDSLTTAVGARPNNSSDLPTSWRGLSWSIGGDGNLETHTT
LPNILKKFNPYLLGFSTSTWEGTAGLNVAAEGARARDMPAQAWDLVERMKNSPDINLEKD
WKLVTLFIGVNDLCHYCENPEAHLATEYVQHIQQALDILSEELPRAFVNVVEVMELASLY
QGQGGKCAMLAAQNNCTCLRHSQSSLEKQELKKVNWNLQHGISSFSYWHQYTQREDFAVV
VQPFFQNTLTPLNERGDTDLTFFSEDCFHFSDRGHAEMAIALWNNMLEPVGRKTTSNNFT
HSRAKLKCPSPESPYLYTLRNSRLLPDQAEEAPEVLYWAVPVAAGVGLVVGIIGTVVWRC
RRGGRREDPPMSLRTVAL
Enzyme 21 Number of Residues 1458
Enzyme 21 Molecular Weight 163079.3
Enzyme 21 Theoretical pI 5.72
Enzyme 21 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 21 General Function Involved in hydrolase activity
Enzyme 21 Specific Function Membrane-associated phospholipase. Exhibits a calcium- independent broad substrate specificity including phospholipase A2/lysophospholipase activity. Preferential hydrolysis at the sn-2 position of diacylphospholipids and diacyglycerol, whereas it shows no positional specificity toward triacylglycerol. Exhibits also esterase activity toward p-nitrophenyl. May act on the brush border membrane to facilitate the absorption of digested lipids
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-21
Enzyme 21 Transmembrane Regions
  • 1418-1438
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 283436112 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q6P1J6 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name PLB1_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >4377 bp
ATGGGGCTGCGGCCAGGCATTTTCCTCCTGGAGCTGCTGCTGCTTCTGGGGCAAGGGACC
CCTCAGATCCATACCTCTCCTAGAAAGAGTACATTGGAAGGGCAGCTATGGCCAGAGACC
CTGAAGAATTCTCCATTCCCATGCAACCCAAATAAATTAGGAGTGAATATGCCTTCTAAA
TCAGTTCACTCTCTGAAGCCTTCTGATATTAAATTTGTGGCAGCCATTGGCAATCTGGAA
ATTCCTCCAGACCCAGGGACGGGCGATCTGGAGAAGCAAGACTGGACTGAAAGGCCACAG
CAGGTGTGCATGGGAGTGATGACAGTCCTTTCAGACATCATCAGATATTTCAGTCCTTCT
GTTCCAATGCCTGTGTGCCACACTGGAAAGAGAGTCATACCCCACGATGGTGCTGAAGAC
TTGTGGATTCAGGCTCAAGAACTGGTGAGAAACATGAAAGAGAACCTGCAACTTGACTTT
CAATTTGACTGGAAGCTCATCAATGTGTTCTTCAGTAATGCAAGCCAGTGTTACCTGTGC
CCCTCTGCTCAACAGAATGGGCTTGCGGCGGGCGGCGTGGATGAGCTGATGGGGGTGCTG
GACTACCTGCAGCAGGAGGTCCCCAGAGCATTTGTAAACCTGGTGGACCTCTCTGAGGTT
GCAGAGGTCTCTCGTCAGTATCACGGCACTTGGCTCAGCCCTGCACCAGAGCCCTGTAAT
TGCTCAGAGGAGACCACCCGGCTGGCCAAGGTGGTGATGCAGTGGTCTTATCAGGAAGCC
TGGAACAGCCTCCTGGCCTCCAGCAGGTACAGTGAGCAGGAGTCCTTCACCGTGGTTTTC
CAGCCTTTCTTCTATGAGACCACCCCATCTCTACACTCGGAGGACCCCCGACTCCAGGAT
TCTACCACGCTGGCCTGGCATCTCTGGAATAGGATGATGGAGCCAGCAGGAGAGAAAGAT
GAGCCATTGAGTGTAAAACACGGGAGGCCAATGAAGTGTCCCTCTCAGGAGAGCCCCTAT
CTGTTCAGCTACAGAAACAGCAACTACCTGACCAGACTGCAGAAACCCCAAGACAAGCTT
GAGGTAAGAGAAGGAGCGGAAATCAGATGTCCTGACAAAGACCCCTCCGATACGGTTCCC
ACCTCAGTTCATAGGCTGAAGCCGGCTGACATCAACGTAATTGGAGCCCTGGGTGACTCT
CTCACGGCAGGCAATGGGGCCGGGTCCACACCTGGGAACGTCTTGGACGTCTTGACTCAG
TACCGAGGCCTGTCCTGGAGCGTCGGCGGAGATGAGAACATCGGCACCGTTACCACCCTG
GCGAACATCCTCCGGGAATTCAACCCTTCCCTGAAGGGCTTCTCTGTTGGCACTGGGAAA
GAAACCAGTCCTAATGCCTTCTTAAACCAGGCTGTGGCAGGAGGCCGAGCTGAGGATCTA
CCTGTCCAGGCCAGGAGGCTGGTGGACCTGATGAAGAATGACACGAGGATACACTTTCAG
GAAGACTGGAAGATAATAACCCTGTTTATAGGCGGCAATGACCTCTGTGATTTCTGCAAT
GATCTGGTCCACTATTCTCCCCAGAACTTCACAGACAACATTGGAAAGGCCCTGGACATC
CTCCATGCTGAGGTTCCTCGGGCATTTGTGAACCTGGTGACGGTGCTTGAGATCGTCAAC
CTGAGGGAGCTGTACCAGGAGAAAAAAGTCTACTGCCCAAGGATGATCCTCAGGTCTCTG
TGTCCCTGTGTCCTGAAGTTTGATGATAACTCAACAGAACTTGCTACCCTCATCGAATTC
AACAAGAAGTTTCAGGAGAAGACCCACCAACTGATTGAGAGTGGGCGATATGACACAAGG
GAAGATTTTACTGTGGTTGTGCAGCCGTTCTTTGAAAACGTGGACATGCCAAAGACCTCG
GAAGGATTGCCTGACAACTCTTTCTTCGCTCCTGACTGTTTCCACTTCAGCAGCAAGTCT
CACTCCCGAGCAGCCAGTGCTCTCTGGAACAATATGCTGGAGCCTGTTGGCCAGAAGACG
ACTCGTCATAAGTTTGAAAACAAGATCAATATCACATGTCCGAACCAGGTCCAGCCGTTT
CTGAGGACCTACAAGAACAGCATGCAGGGTCATGGGACCTGGCTGCCATGCAGGGACAGA
GCCCCTTCTGCCTTGCACCCTACCTCAGTGCATGCCCTGAGACCTGCAGACATCCAAGTT
GTGGCTGCTCTGGGGGATTCTCTGACCGCTGGCAATGGAATTGGCTCCAAACCAGACGAC
CTCCCCGATGTCACCACACAGTATCGGGGACTGTCATACAGTGCAGGAGGGGACGGCTCC
CTGGAGAATGTGACCACCTTACCTAATATCCTTCGGGAGTTTAACAGAAACCTCACAGGC
TACGCCGTGGGCACGGGTGATGCCAATGACACGAATGCATTCCTCAATCAAGCTGTTCCC
GGAGCAAAGGCTGAGGATCTTATGAGCCAAGTCCAAACTCTGATGCAGAAGATGAAAGAT
GATCATAGAGTAAATTTCCATGAAGACTGGAAGGTCATCACAGTGCTGATCGGAGGCAGC
GATTTATGTGACTACTGCACAGATTCGAATCTGTATTCTGCAGCCAACTTTGTTCACCAT
CTCCGCAATGCCTTGGACGTCCTGCATAGAGAGGTGCCCAGAGTCCTGGTCAACCTCGTG
GACTTCCTGAACCCCACTATCATGCGGCAGGTGTTCCTGGGAAACCCAGACAAGTGCCCA
GTGCAGCAGGCCAGCGTTTTGTGTAACTGCGTTCTGACCCTGCGGGAGAACTCCCAAGAG
CTAGCCAGGCTGGAGGCCTTCAGCCGAGCCTACCGGAGCAGCATGCGCGAGCTGGTGGGG
TCAGGCCGCTATGACACGCAGGAGGACTTCTCTGTGGTGCTGCAGCCCTTCTTCCAGAAC
ATCCAGCTCCCTGTCCTGGCGGATGGGCTCCCAGATACGTCCTTCTTTGCCCCAGACTGC
ATCCACCCAAATCAGAAATTCCACTCCCAGCTGGCCAGAGCCCTTTGGACCAATATGCTT
GAACCACTTGGAAGCAAAACAGAGACCCTGGACCTGAGAGCAGAGATGCCCATCACCTGT
CCCACTCAGAATGAGCCCTTCCTGAGAACCCCTCGGAATAGTAACTACACGTACCCCATC
AAGCCAGCCATTGAGAACTGGGGCAGTGACTTCCTGTGTACAGAGTGGAAGGCTTCCAAT
AGTGTTCCAACCTCTGTCCACCAGCTCCGACCAGCAGACATCAAAGTGGTGGCCGCCCTG
GGTGACTCTCTGACTACAGCAGTGGGAGCTCGACCAAACAACTCCAGTGACCTACCCACA
TCTTGGAGGGGACTCTCTTGGAGCATTGGAGGGGATGGGAACTTGGAGACTCACACCACA
CTGCCCAACATTCTGAAGAAGTTCAACCCTTACCTCCTTGGCTTCTCTACCAGCACCTGG
GAGGGGACAGCAGGACTAAATGTGGCAGCGGAAGGGGCCAGAGCTAGGGACATGCCAGCC
CAGGCCTGGGACCTGGTAGAGCGAATGAAAAACAGCCCCGACATCAACCTGGAGAAAGAC
TGGAAGCTGGTCACACTCTTCATTGGGGTCAACGACTTGTGTCATTACTGTGAGAATCCG
GAGGCCCACTTGGCCACGGAATATGTTCAGCACATCCAACAGGCCCTGGACATCCTCTCT
GAGGAGCTCCCAAGGGCTTTCGTCAACGTGGTGGAGGTCATGGAGCTGGCTAGCCTGTAC
CAGGGCCAAGGCGGGAAATGTGCCATGCTGGCAGCTCAGAACAACTGCACTTGCCTCAGA
CACTCGCAAAGCTCCCTGGAGAAGCAAGAACTGAAGAAAGTGAACTGGAACCTCCAGCAT
GGCATCTCCAGTTTCTCCTACTGGCACCAATACACACAGCGTGAGGACTTTGCGGTTGTG
GTGCAGCCTTTCTTCCAAAACACACTCACCCCACTGAACGAGAGAGGGGACACTGACCTC
ACCTTCTTCTCCGAGGACTGTTTTCACTTCTCAGACCGCGGGCATGCCGAGATGGCCATC
GCACTCTGGAACAACATGCTGGAACCAGTGGGCCGCAAGACTACCTCCAACAACTTCACC
CACAGCCGAGCCAAACTCAAGTGCCCCTCTCCTGAGAGCCCTTACCTCTACACCCTGCGG
AACAGCCGATTGCTCCCAGACCAGGCTGAAGAAGCCCCCGAGGTGCTCTACTGGGCTGTC
CCAGTGGCAGCGGGAGTCGGCCTTGTGGTGGGCATCATCGGGACAGTGGTCTGGAGGTGC
AGGAGAGGTGGCCGGAGGGAAGATCCTCCAATGAGCCTGCGCACTGTGGCCCTCTAG
Enzyme 21 GenBank Gene ID NM_153021.4 Link Image
Enzyme 21 GeneCard ID PLB1 Link Image
Enzyme 21 GenAtlas ID PLB1 Link Image
Enzyme 21 HGNC ID HGNC:30041 Link Image
Enzyme 21 Chromosome Location 2
Enzyme 21 Locus 2p23.2
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. 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]
  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. 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]
  4. Maury E, Prevost MC, Nauze M, Redoules D, Tarroux R, Charveron M, Salles JP, Perret B, Chap H, Gassama-Diagne A: Human epidermis is a novel site of phospholipase B expression. Biochem Biophys Res Commun. 2002 Jul 12;295(2):362-9. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 12936
Enzyme 22 Name Glycerol-3-phosphate acyltransferase 3
Enzyme 22 Synonyms
  1. GPAT-3
  2. 1-acylglycerol-3-phosphate O-acyltransferase 9
  3. 1-AGP acyltransferase 9
  4. 1-AGPAT 9
  5. Acyl-CoA:glycerol-3-phosphate acyltransferase 3
  6. hGPAT3
  7. Lung cancer metastasis-associated protein 1
  8. Lysophosphatidic acid acyltransferase theta
  9. LPAAT-theta
  10. MAG-1
Enzyme 22 Gene Name AGPAT9
Enzyme 22 Protein Sequence >Glycerol-3-phosphate acyltransferase 3
MEGAELAGKILSTWLTLVLGFILLPSVFGVSLGISEIYMKILVKTLEWATIRIEKGTPKE
SILKNSASVGIIQRDESPMEKGLSGLRGRDFELSDVFYFSKKGLEAIVEDEVTQRFSSEE
LVSWNLLTRTNVNFQYISLRLTMVWVLGVIVRYCVLLPLRVTLAFIGISLLVIGTTLVGQ
LPDSSLKNWLSELVHLTCCRICVRALSGTIHYHNKQYRPQKGGICVANHTSPIDVLILTT
DGCYAMVGQVHGGLMGIIQRAMVKACPHVWFERSEMKDRHLVTKRLKEHIADKKKLPILI
FPEGTCINNTSVMMFKKGSFEIGGTIHPVAIKYNPQFGDAFWNSSKYNMVSYLLRMMTSW
AIVCDVWYMPPMTREEGEDAVQFANRVKSAIAIQGGLTELPWDGGLKRAKVKDIFKEEQQ
KNYSKMIVGNGSLS
Enzyme 22 Number of Residues 434
Enzyme 22 Molecular Weight 48704.8
Enzyme 22 Theoretical pI 9.15
Enzyme 22 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 22 General Function Involved in acyltransferase activity
Enzyme 22 Specific Function Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Overexpression activates the mTOR pathway
Enzyme 22 Pathways
Enzyme 22 Reactions
  • acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 14-34 137-157 161-181
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 21362092 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q53EU6 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name GPAT3_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1305 bp
ATGGAGGGCGCAGAGCTGGCCGGGAAGATCCTTTCCACCTGGCTGACGCTGGTTCTCGGC
TTCATCCTTTTACCTTCGGTCTTCGGAGTGTCTCTGGGCATCTCCGAGATCTACATGAAG
ATCCTAGTGAAAACTTTAGAGTGGGCCACAATACGAATTGAAAAAGGAACCCCAAAGGAG
TCGATTCTTAAAAACTCTGCTTCTGTTGGTATTATCCAAAGAGATGAGTCACCCATGGAA
AAAGGGCTCTCTGGTCTACGAGGAAGGGACTTTGAGCTGTCTGACGTGTTTTATTTCTCC
AAGAAGGGATTGGAAGCCATTGTAGAAGATGAAGTGACCCAGAGGTTTTCCTCAGAGGAG
CTAGTGTCATGGAATCTCCTCACAAGAACCAATGTAAATTTCCAGTACATCAGTCTGCGG
CTCACTATGGTGTGGGTGCTGGGCGTCATAGTGCGCTATTGTGTCCTACTGCCTCTGAGG
GTTACCTTGGCTTTCATTGGGATCAGTTTGCTGGTTATAGGAACTACACTGGTTGGGCAG
CTGCCAGACAGCAGCCTCAAAAACTGGCTGAGTGAACTGGTCCATCTGACTTGCTGCCGG
ATCTGTGTGCGAGCCCTCTCTGGTACCATTCATTATCATAACAAGCAGTACAGACCCCAG
AAGGGAGGCATTTGTGTTGCCAACCATACTTCCCCCATTGATGTTTTAATCTTGACAACG
GATGGATGTTATGCTATGGTTGGCCAGGTTCATGGCGGCTTGATGGGAATTATTCAGAGA
GCTATGGTCAAGGCTTGTCCTCATGTCTGGTTTGAACGCTCAGAAATGAAGGATCGACAC
CTGGTTACTAAGAGACTAAAAGAACATATTGCTGATAAGAAGAAACTACCCATACTAATT
TTTCCTGAAGGAACTTGCATCAACAATACTTCAGTCATGATGTTTAAAAAGGGGAGCTTT
GAAATTGGAGGAACCATACATCCAGTTGCAATTAAGTATAACCCTCAGTTCGGTGATGCA
TTTTGGAACAGTAGTAAATACAACATGGTGAGCTACCTGCTTCGAATGATGACCAGCTGG
GCCATCGTCTGTGACGTGTGGTACATGCCCCCCATGACCAGAGAGGAAGGAGAAGATGCA
GTCCAGTTTGCTAACAGGGTTAAGTCTGCTATTGCTATACAAGGAGGCCTGACTGAACTT
CCCTGGGATGGAGGACTAAAGAGAGCAAAGGTGAAGGACATCTTTAAGGAAGAGCAGCAG
AAAAATTACAGCAAGATGATTGTGGGCAATGGATCTCTCAGCTAA
Enzyme 22 GenBank Gene ID NM_032717.3 Link Image
Enzyme 22 GeneCard ID AGPAT9 Link Image
Enzyme 22 GenAtlas ID AGPAT9 Link Image
Enzyme 22 HGNC ID HGNC:28157 Link Image
Enzyme 22 Chromosome Location 4
Enzyme 22 Locus 4q21.23
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Tang W, Yuan J, Chen X, Gu X, Luo K, Li J, Wan B, Wang Y, Yu L: Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway. J Biochem Mol Biol. 2006 Sep 30;39(5):626-35. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, 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]
  5. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed Link Image]
  6. Cao J, Li JL, Li D, Tobin JF, Gimeno RE: Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis. Proc Natl Acad Sci U S A. 2006 Dec 26;103(52):19695-700. Epub 2006 Dec 14. [PubMed Link Image]
  7. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed 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]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 12969
Enzyme 23 Name Patatin-like phospholipase domain-containing protein 2
Enzyme 23 Synonyms
  1. Adipose triglyceride lipase
  2. Calcium-independent phospholipase A2
  3. Desnutrin
  4. IPLA2-zeta
  5. Pigment epithelium-derived factor
  6. TTS2.2
  7. Transport-secretion protein 2
  8. TTS2
Enzyme 23 Gene Name PNPLA2
Enzyme 23 Protein Sequence >Patatin-like phospholipase domain-containing protein 2
MFPREKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGV
CLGEAGAKFIEVSKEARKRFLGPLHPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTR
VSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRYVDGGISDNLPLYELKN
TITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYRLSKALFPPEPLVLREMCKQ
GYRDGLRFLQRNGLLNRPNPLLALPPARPHGPEDKDQAVESAQAEDYSQLPGEDHILEHL
PARLNEALLEACVEPTDLLTTLSNMLPVRLATAMMVPYTLPLESALSFTIRLLEWLPDVP
EDIRWMKEQTGSICQYLVMRAKRKLGRHLPSRLPEQVELRRVQSLPSVPLSCAAYREALP
GWMRNNLSLGDALAKWEECQRQLLLGLFCTNVAFPPEALRMRAPADPAPAPADPASPQHQ
LAGPAPLLSTPAPEARPVIGALGL
Enzyme 23 Number of Residues 504
Enzyme 23 Molecular Weight 55315.2
Enzyme 23 Theoretical pI 7.09
Enzyme 23 GO Classification
Function
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 23 General Function Involved in metabolic process
Enzyme 23 Specific Function Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion
Enzyme 23 Pathways
Enzyme 23 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 9-29
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 32698724 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q96AD5 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PLPL2_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1515 bp
ATGTTTCCCCGCGAGAAGACGTGGAACATCTCGTTCGCGGGCTGCGGCTTCCTCGGCGTC
TACTACGTCGGCGTGGCCTCCTGCCTCCGCGAGCACGCGCCCTTCCTGGTGGCCAACGCC
ACGCACATCTACGGCGCCTCGGCCGGGGCGCTCACGGCCACGGCGCTGGTCACCGGGGTC
TGCCTGGGTGAGGCTGGTGCCAAGTTCATTGAGGTATCTAAAGAGGCCCGGAAGCGGTTC
CTGGGCCCCCTGCACCCCTCCTTCAACCTGGTAAAGATCATCCGCAGTTTCCTGCTGAAG
GTCCTGCCTGCTGATAGCCATGAGCATGCCAGTGGGCGCCTGGGCATCTCCCTGACCCGC
GTGTCAGACGGCGAGAATGTCATTATATCCCACTTCAACTCCAAGGACGAGCTCATCCAG
GCCAATGTCTGCAGCGGTTTCATCCCCGTGTACTGTGGGCTCATCCCTCCCTCCCTCCAG
GGGGTGCGCTACGTGGATGGTGGCATTTCAGACAACCTGCCACTCTATGAGCTTAAGAAC
ACCATCACAGTGTCCCCCTTCTCGGGCGAGAGTGACATCTGTCCGCAGGACAGCTCCACC
AACATCCACGAGCTGCGGGTCACCAACACCAGCATCCAGTTCAACCTGCGCAACCTCTAC
CGCCTCTCCAAGGCCCTCTTCCCGCCGGAGCCCCTGGTGCTGCGAGAGATGTGCAAGCAG
GGATACCGGGATGGCCTGCGCTTTCTGCAGCGGAACGGCCTCCTGAACCGGCCCAACCCC
TTGCTGGCGTTGCCCCCCGCCCGCCCCCACGGCCCAGAGGACAAGGACCAGGCAGTGGAG
AGCGCCCAAGCGGAGGATTACTCGCAGCTGCCCGGAGAAGATCACATCCTGGAGCACCTG
CCCGCCCGGCTCAATGAGGCCCTGCTGGAGGCCTGCGTGGAGCCCACGGACCTGCTGACC
ACCCTCTCCAACATGCTGCCTGTGCGTCTGGCCACGGCCATGATGGTGCCCTACACGCTG
CCGCTGGAGAGCGCTCTGTCCTTCACCATCCGCTTGCTGGAGTGGCTGCCCGACGTTCCC
GAGGACATCCGGTGGATGAAGGAGCAGACGGGCAGCATCTGCCAGTACCTGGTGATGCGC
GCCAAGAGGAAGCTGGGCAGGCACCTGCCCTCCAGGCTGCCGGAGCAGGTGGAGCTGCGC
CGCGTCCAGTCGCTGCCGTCCGTGCCGCTGTCCTGCGCCGCCTACAGAGAGGCACTGCCC
GGCTGGATGCGCAACAACCTCTCGCTGGGGGACGCGCTGGCCAAGTGGGAGGAGTGCCAG
CGCCAGCTGCTGCTCGGCCTCTTCTGCACCAACGTGGCCTTCCCGCCCGAAGCTCTGCGC
ATGCGCGCACCCGCCGACCCGGCTCCCGCCCCCGCGGACCCAGCATCCCCGCAGCACCAG
CTGGCCGGGCCTGCCCCCTTGCTGAGCACCCCTGCTCCCGAGGCCCGGCCCGTGATCGGG
GCCCTGGGGCTGTGA
Enzyme 23 GenBank Gene ID NM_020376.3 Link Image
Enzyme 23 GeneCard ID PNPLA2 Link Image
Enzyme 23 GenAtlas ID PNPLA2 Link Image
Enzyme 23 HGNC ID HGNC:30802 Link Image
Enzyme 23 Chromosome Location 1
Enzyme 23 Locus 11p15.5
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Zimmermann R, Strauss JG, Haemmerle G, Schoiswohl G, Birner-Gruenberger R, Riederer M, Lass A, Neuberger G, Eisenhaber F, Hermetter A, Zechner R: Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase. Science. 2004 Nov 19;306(5700):1383-6. [PubMed Link Image]
  2. Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J: Large-scale cDNA transfection screening for genes related to cancer development and progression. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15724-9. Epub 2004 Oct 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. Jenkins CM, Mancuso DJ, Yan W, Sims HF, Gibson B, Gross RW: Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem. 2004 Nov 19;279(47):48968-75. Epub 2004 Sep 10. [PubMed Link Image]
  5. Langin D, Dicker A, Tavernier G, Hoffstedt J, Mairal A, Ryden M, Arner E, Sicard A, Jenkins CM, Viguerie N, van Harmelen V, Gross RW, Holm C, Arner P: Adipocyte lipases and defect of lipolysis in human obesity. Diabetes. 2005 Nov;54(11):3190-7. [PubMed Link Image]
  6. Lake AC, Sun Y, Li JL, Kim JE, Johnson JW, Li D, Revett T, Shih HH, Liu W, Paulsen JE, Gimeno RE: Expression, regulation, and triglyceride hydrolase activity of Adiponutrin family members. J Lipid Res. 2005 Nov;46(11):2477-87. Epub 2005 Sep 8. [PubMed Link Image]
  7. Kim JY, Tillison K, Lee JH, Rearick DA, Smas CM: The adipose tissue triglyceride lipase ATGL/PNPLA2 is downregulated by insulin and TNF-alpha in 3T3-L1 adipocytes and is a target for transactivation by PPARgamma. Am J Physiol Endocrinol Metab. 2006 Jul;291(1):E115-27. Epub 2006 May 16. [PubMed Link Image]
  8. Smirnova E, Goldberg EB, Makarova KS, Lin L, Brown WJ, Jackson CL: ATGL has a key role in lipid droplet/adiposome degradation in mammalian cells. EMBO Rep. 2006 Jan;7(1):106-13. [PubMed Link Image]
  9. Notari L, Baladron V, Aroca-Aguilar JD, Balko N, Heredia R, Meyer C, Notario PM, Saravanamuthu S, Nueda ML, Sanchez-Sanchez F, Escribano J, Laborda J, Becerra SP: Identification of a lipase-linked cell membrane receptor for pigment epithelium-derived factor. J Biol Chem. 2006 Dec 8;281(49):38022-37. Epub 2006 Oct 10. [PubMed Link Image]
  10. 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]
  11. Schoenborn V, Heid IM, Vollmert C, Lingenhel A, Adams TD, Hopkins PN, Illig T, Zimmermann R, Zechner R, Hunt SC, Kronenberg F: The ATGL gene is associated with free fatty acids, triglycerides, and type 2 diabetes. Diabetes. 2006 May;55(5):1270-5. [PubMed Link Image]
  12. Fischer J, Lefevre C, Morava E, Mussini JM, Laforet P, Negre-Salvayre A, Lathrop M, Salvayre R: The gene encoding adipose triglyceride lipase (PNPLA2) is mutated in neutral lipid storage disease with myopathy. Nat Genet. 2007 Jan;39(1):28-30. Epub 2006 Dec 24. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 17240
Enzyme 24 Name Pancreatic lipase-related protein 3
Enzyme 24 Synonyms
  1. PL-RP3
Enzyme 24 Gene Name PNLIPRP3
Enzyme 24 Protein Sequence >Pancreatic lipase-related protein 3
MLGIWIVAFLFFGTSRGKEVCYERLGCFKDGLPWTRTFSTELVGLPWSPEKINTRFLLYT
IHNPNAYQEISAVNSSTIQASYFGTDKITRINIAGWKTDGKWQRDMCNVLLQLEDINCIN
LDWINGSREYIHAVNNLRVVGAEVAYFIDVLMKKFEYSPSKVHLIGHSLGAHLAGEAGSR
IPGLGRITGLDPAGPFFHNTPKEVRLDPSDANFVDVIHTNAARILFELGVGTIDACGHLD
FYPNGGKHMPGCEDLITPLLKFNFNAYKKEMASFFDCNHARSYQFYAESILNPDAFIAYP
CRSYTSFKAGNCFFCSKEGCPTMGHFADRFHFKNMKTNGSHYFLNTGSLSPFARWRHKLS
VKLSGSEVTQGTVFLRVGGAVRKTGEFAIVSGKLEPGMTYTKLIDADVNVGNITSVQFIW
KKHLFEDSQNKLGAEMVINTSGKYGYKSTFCSQDIMGPNILQNLKPC
Enzyme 24 Number of Residues 467
Enzyme 24 Molecular Weight 52253.4
Enzyme 24 Theoretical pI 8.36
Enzyme 24 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 24 General Function Involved in catalytic activity
Enzyme 24 Specific Function Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • 1-17
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 190341077 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q17RR3 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name LIPR3_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1404 bp
ATGCTTGGAATTTGGATTGTTGCATTCTTGTTCTTTGGCACATCAAGAGGAAAAGAAGTT
TGCTATGAAAGGTTAGGGTGTTTCAAAGATGGTTTACCATGGACCAGGACTTTCTCAACA
GAGTTGGTAGGTTTACCCTGGTCTCCAGAGAAGATAAACACTCGTTTCCTGCTCTACACT
ATACACAATCCCAATGCCTATCAGGAGATCAGTGCGGTTAATTCTTCAACTATCCAAGCC
TCATATTTTGGAACAGACAAGATCACCCGTATCAACATAGCTGGATGGAAAACAGATGGC
AAATGGCAGAGAGACATGTGCAATGTGTTGCTACAGCTGGAAGATATAAATTGCATTAAT
TTAGATTGGATCAACGGTTCACGGGAATACATCCATGCTGTAAACAATCTCCGTGTTGTT
GGTGCTGAGGTGGCTTATTTTATTGATGTTCTCATGAAAAAATTTGAATATTCCCCTTCT
AAAGTGCACTTGATTGGCCACAGCTTGGGAGCACACCTGGCTGGGGAAGCTGGGTCAAGG
ATACCAGGCCTTGGAAGAATAACTGGGTTGGACCCAGCTGGGCCATTTTTCCACAACACT
CCAAAGGAAGTCAGGCTAGACCCCTCGGATGCCAACTTTGTTGACGTTATTCATACAAAT
GCAGCTCGCATCCTCTTTGAGCTTGGTGTTGGAACCATTGATGCTTGTGGTCATCTTGAC
TTTTACCCAAATGGAGGGAAGCACATGCCAGGATGTGAAGACTTAATTACACCTTTACTG
AAATTTAACTTCAATGCTTACAAAAAAGAAATGGCTTCCTTCTTTGACTGTAACCATGCC
CGAAGTTATCAATTTTATGCTGAAAGCATTCTTAATCCTGATGCATTTATTGCTTATCCT
TGTAGATCCTACACATCTTTTAAAGCAGGAAATTGCTTCTTTTGTTCCAAAGAAGGTTGC
CCAACAATGGGTCATTTTGCTGATAGATTTCACTTCAAAAATATGAAGACTAATGGATCA
CATTATTTTTTAAACACAGGGTCCCTTTCCCCATTTGCCCGTTGGAGGCACAAATTGTCT
GTTAAACTCAGTGGAAGCGAAGTCACTCAAGGAACTGTCTTTCTTCGTGTAGGCGGGGCA
GTTAGGAAAACTGGGGAGTTTGCCATTGTCAGTGGAAAACTTGAGCCAGGCATGACTTAC
ACAAAATTAATCGATGCAGATGTTAACGTTGGAAACATTACAAGTGTTCAGTTCATCTGG
AAAAAACATTTGTTTGAAGATTCTCAGAATAAGTTGGGAGCAGAAATGGTGATAAATACA
TCTGGGAAATATGGATATAAATCTACCTTCTGTAGCCAAGACATTATGGGACCTAATATT
CTCCAGAACCTGAAACCATGCTAA
Enzyme 24 GenBank Gene ID NM_001011709.2 Link Image
Enzyme 24 GeneCard ID PNLIPRP3 Link Image
Enzyme 24 GenAtlas ID PNLIPRP3 Link Image
Enzyme 24 HGNC ID HGNC:23492 Link Image
Enzyme 24 Chromosome Location 1
Enzyme 24 Locus 10q25.3
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. 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]
  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. Saelee P, Wongkham S, Puapairoj A, Khuntikeo N, Petmitr S, Chariyalertsak S, Sumethchotimaytha W, Karalak A: Novel PNLIPRP3 and DOCK8 gene expression and prognostic implications of DNA loss on chromosome 10q25.3 in hepatocellular carcinoma. Asian Pac J Cancer Prev. 2009 Jul-Sep;10(3):501-6. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 17302
Enzyme 25 Name Perilipin-4
Enzyme 25 Synonyms
  1. Adipocyte protein S3-12
Enzyme 25 Gene Name PLIN4
Enzyme 25 Protein Sequence >Perilipin-4
MQTLGSFFGSLPGFSSARNLVANAHSSARARPAADPTGAPAAEAAQPQAQVAAHPEQTAP
WTEKELQPSEKQMVSGAKDLVCSKMSRAKDAVSSGVASVVDVAKGVVQGGLDTTRSALTG
TKEVVSSGVTGAMDMAKGAVQGGLDTSKAVLTGTKDTVSTGLTGAVNVAKGTVQAGVDTT
KTVLTGTKDTVTTGVMGAVNLAKGTVQTGVETSKAVLTGTKDAVSTGLTGAVNVARGSIQ
TGVDTSKTVLTGTKDTVCSGVTGAMNVAKGTIQTGVDTSKTVLTGTKDTVCSGVTGAMNV
AKGTIQTGVDTSKTVLTGTKDTVCSGVTGAMNVAKGTIQTGVDTTKTVLTGTKNTVCSGV
TGAVNLAKEAIQGGLDTTKSMVMGTKDTMSTGLTGAANVAKGAMQTGLNTTQNIATGTKD
TVCSGVTGAMNLARGTIQTGVDTTKIVLTGTKDTVCSGVTGAANVAKGAVQGGLDTTKSV
LTGTKDAVSTGLTGAVNVAKGTVQTGVDTTKTVLTGTKDTVCSGVTSAVNVAKGAVQGGL
DTTKSVVIGTKDTMSTGLTGAANVAKGAVQTGVDTAKTVLTGTKDTVTTGLVGAVNVAKG
TVQTGMDTTKTVLTGTKDTIYSGVTSAVNVAKGAVQTGLKTTQNIATGTKNTFGSGVTSA
VNVAKGAAQTGVDTAKTVLTGTKDTVTTGLMGAVNVAKGTVQTSVDTTKTVLTGTKDTVC
SGVTGAANVAKGAIQGGLDTTKSVLTGTKDAVSTGLTGAVKLAKGTVQTGMDTTKTVLTG
TKDAVCSGVTGAANVAKGAVQMGVDTAKTVLTGTKDTVCSGVTGAANVAKGAVQTGLKTT
QNIATGTKNTLGSGVTGAAKVAKGAVQGGLDTTKSVLTGTKDAVSTGLTGAVNLAKGTVQ
TGVDTSKTVLTGTKDTVCSGVTGAVNVAKGTVQTGVDTAKTVLSGAKDAVTTGVTGAVNV
AKGTVQTGVDASKAVLMGTKDTVFSGVTGAMSMAKGAVQGGLDTTKTVLTGTKDAVSAGL
MGSGNVATGATHTGLSTFQNWLPSTPATSWGGLTSSRTTDNGGEQTALSPQEAPFSGIST
PPDVLSVGPEPAWEAAATTKGLATDVATFTQGAAPGREDTGLLATTHGPEEAPRLAMLQN
ELEGLGDIFHPMNAEEQAQLAASQPGPKVLSAEQGSYFVRLGDLGPSFRQRAFEHAVSHL
QHGQFQARDTLAQLQDCFRLIEKAQQAPEGQPRLDQGSGASAEDAAVQEERDAGVLSRVC
GLLRQLHTAYSGLVSSLQGLPAELQQPVGRARHSLCELYGIVASAGSVEELPAERLVQSR
EGVHQAWQGLEQLLEGLQHNPPLSWLVGPFALPAGGQ
Enzyme 25 Number of Residues 1357
Enzyme 25 Molecular Weight 134431.0
Enzyme 25 Theoretical pI 9.11
Enzyme 25 GO Classification Not Available
Enzyme 25 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 25 Specific Function May play a role in triacylglycerol packaging into adipocytes. May function as a coat protein involved in the biogenesis of lipid droplets
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 122937195 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q96Q06 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PLIN4_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >4074 bp
ATGCAGACCCTGGGCAGCTTCTTTGGGTCCCTGCCTGGCTTCAGCTCTGCCCGGAACCTG
GTGGCCAACGCACATAGCTCGGCGAGAGCCCGGCCGGCCGCTGACCCCACAGGAGCGCCT
GCTGCCGAGGCTGCCCAACCACAGGCTCAGGTGGCTGCCCACCCAGAGCAGACGGCCCCA
TGGACGGAGAAGGAGCTGCAACCTTCGGAAAAGCAGATGGTGTCCGGGGCCAAAGACCTG
GTGTGTTCCAAGATGTCCAGGGCCAAGGATGCCGTGTCCTCCGGGGTGGCCAGCGTGGTG
GACGTGGCTAAGGGAGTGGTCCAGGGAGGCCTGGACACCACTCGGTCTGCACTTACGGGC
ACCAAGGAGGTGGTGTCCAGCGGGGTCACAGGGGCCATGGACATGGCTAAGGGGGCCGTC
CAAGGGGGTCTGGACACCTCGAAGGCTGTCCTCACCGGCACCAAGGACACGGTGTCCACT
GGGCTCACGGGGGCAGTGAATGTGGCCAAAGGGACCGTACAGGCCGGTGTGGACACCACC
AAGACTGTGCTGACCGGCACCAAAGACACAGTGACTACTGGGGTCATGGGGGCAGTGAAC
TTGGCCAAAGGGACTGTCCAGACTGGCGTGGAAACCTCCAAGGCTGTGCTGACCGGCACC
AAAGATGCTGTGTCCACTGGGCTCACAGGGGCAGTGAATGTGGCCAGAGGAAGCATTCAG
ACCGGTGTGGACACCAGTAAGACTGTCCTAACAGGTACCAAGGACACCGTCTGTAGTGGG
GTGACTGGTGCCATGAATGTGGCCAAAGGAACCATCCAGACCGGCGTGGACACCAGTAAG
ACTGTCCTAACAGGTACCAAGGACACCGTCTGTAGTGGGGTGACTGGTGCCATGAATGTG
GCCAAAGGAACCATCCAGACCGGCGTGGACACCAGTAAGACTGTCCTAACAGGTACCAAG
GACACCGTCTGTAGTGGGGTGACTGGTGCCATGAATGTGGCCAAAGGAACCATCCAGACC
GGCGTGGACACCACCAAGACTGTCCTAACTGGCACCAAGAACACTGTCTGCAGTGGGGTG
ACCGGTGCCGTGAACTTGGCCAAAGAGGCCATCCAGGGGGGCCTGGATACCACCAAGTCT
ATGGTCATGGGTACGAAAGACACGATGTCCACTGGGCTCACAGGGGCAGCGAATGTGGCC
AAGGGGGCCATGCAAACTGGGCTGAACACAACCCAAAATATCGCAACAGGTACAAAGGAC
ACCGTCTGCAGTGGGGTGACTGGTGCCATGAATTTGGCCAGAGGAACCATCCAGACAGGC
GTGGACACCACCAAGATCGTTCTAACTGGTACCAAGGACACTGTCTGCAGTGGGGTCACC
GGTGCTGCGAATGTGGCCAAAGGGGCCGTCCAGGGCGGCCTGGACACTACAAAGTCTGTC
CTGACTGGCACTAAAGATGCTGTGTCCACTGGGCTCACAGGGGCTGTGAACGTGGCCAAA
GGGACCGTCCAGACCGGCGTAGACACCACCAAGACTGTCCTAACCGGCACCAAGGACACC
GTCTGCAGTGGGGTGACCAGTGCTGTGAACGTGGCCAAAGGGGCCGTCCAGGGGGGCCTG
GACACCACCAAGTCTGTGGTCATAGGTACAAAAGACACGATGTCCACTGGGCTCACGGGG
GCAGCGAATGTGGCCAAGGGGGCTGTCCAGACAGGTGTAGACACAGCCAAGACCGTGCTG
ACCGGCACCAAGGACACAGTGACTACTGGGCTCGTGGGGGCAGTGAATGTCGCCAAAGGG
ACCGTCCAGACAGGCATGGACACCACCAAAACTGTCCTAACCGGTACCAAGGACACCATC
TACAGTGGGGTCACCAGTGCCGTGAACGTGGCCAAGGGGGCTGTGCAAACTGGGCTGAAA
ACGACCCAAAATATCGCGACAGGTACAAAGAACACCTTTGGCAGTGGGGTGACCAGTGCT
GTGAATGTGGCCAAAGGGGCTGCCCAGACAGGTGTAGACACGGCCAAGACCGTGCTGACC
GGCACCAAGGACACAGTCACTACTGGGCTCATGGGGGCAGTGAATGTCGCCAAAGGGACT
GTCCAGACCAGTGTGGACACCACCAAGACTGTCCTAACTGGTACCAAGGACACCGTCTGC
AGTGGGGTGACCGGTGCTGCGAATGTGGCCAAAGGGGCCATCCAAGGGGGCCTGGACACT
ACAAAGTCTGTCCTGACTGGCACTAAAGATGCTGTGTCCACTGGGCTCACAGGGGCTGTG
AAGTTGGCCAAAGGGACTGTCCAGACCGGCATGGACACCACCAAGACTGTGTTAACTGGT
ACCAAGGATGCTGTGTGCAGTGGGGTGACCGGTGCTGCGAATGTGGCCAAGGGGGCCGTC
CAGATGGGTGTAGACACGGCCAAGACCGTGCTGACCGGTACCAAGGACACTGTCTGCAGT
GGGGTCACCGGTGCTGCGAACGTGGCCAAGGGTGCTGTGCAAACTGGGCTGAAAACGACC
CAAAATATCGCAACAGGTACAAAGAACACCCTTGGCAGTGGGGTGACCGGTGCTGCGAAA
GTGGCCAAAGGGGCCGTCCAGGGGGGCCTGGACACTACAAAGTCTGTCCTGACTGGCACT
AAAGATGCCGTGTCCACTGGGCTCACAGGGGCTGTGAACTTGGCCAAAGGGACTGTCCAG
ACCGGCGTGGACACCAGCAAGACTGTCCTGACCGGTACCAAGGACACCGTCTGCAGTGGA
GTCACTGGTGCCGTAAATGTGGCCAAAGGGACCGTCCAGACAGGTGTGGACACAGCCAAG
ACGGTGCTGAGTGGCGCTAAGGATGCAGTGACTACTGGAGTCACGGGGGCAGTGAATGTG
GCCAAAGGAACCGTGCAGACCGGCGTGGACGCCTCCAAGGCTGTGCTTATGGGTACCAAG
GACACTGTCTTCAGTGGGGTTACCGGTGCCATGAGCATGGCCAAAGGGGCCGTCCAGGGG
GGCCTGGACACCACCAAGACAGTGCTGACCGGAACCAAAGACGCAGTGTCCGCTGGGCTC
ATGGGGTCAGGGAACGTGGCGACAGGGGCCACCCACACTGGCCTCAGCACCTTCCAGAAC
TGGTTACCTAGTACCCCCGCCACCTCCTGGGGTGGACTCACCAGTTCCAGGACCACAGAC
AATGGTGGGGAGCAGACTGCCCTGAGCCCCCAAGAGGCCCCGTTCTCTGGCATCTCCACG
CCCCCGGATGTGCTCAGTGTAGGCCCGGAGCCTGCCTGGGAAGCCGCAGCCACTACCAAG
GGCCTTGCGACTGACGTGGCGACGTTCACCCAAGGGGCCGCCCCAGGCAGGGAGGACACG
GGGCTTTTGGCCACCACACACGGCCCCGAAGAAGCCCCACGCTTGGCAATGCTGCAGAAT
GAGTTGGAGGGGCTGGGGGACATCTTCCACCCCATGAATGCGGAGGAGCAAGCTCAGCTG
GCTGCCTCCCAGCCTGGGCCAAAGGTGCTGTCGGCGGAACAGGGGAGCTACTTCGTTCGT
TTAGGTGACCTGGGTCCCAGCTTCCGCCAGCGGGCATTTGAACACGCGGTGAGCCACCTG
CAGCACGGCCAGTTCCAAGCCAGGGACACTCTGGCCCAGCTCCAGGACTGCTTCAGGCTG
ATTGAAAAGGCCCAGCAGGCTCCAGAAGGGCAGCCACGTCTGGACCAGGGCTCAGGTGCC
AGTGCGGAGGACGCTGCTGTCCAGGAGGAGCGGGATGCCGGGGTTCTGTCCAGGGTCTGC
GGCCTTCTCCGGCAGCTGCACACGGCCTACAGTGGCCTGGTCTCCAGCCTCCAGGGCCTG
CCCGCCGAGCTCCAGCAGCCAGTGGGGCGGGCGCGGCACAGCCTCTGTGAGCTCTATGGC
ATCGTGGCCTCAGCTGGCTCTGTAGAGGAGCTGCCCGCAGAGCGGCTGGTGCAGAGCCGC
GAGGGTGTGCACCAGGCTTGGCAGGGGTTAGAGCAGCTGCTGGAGGGCCTACAGCACAAT
CCCCCGCTCAGCTGGCTGGTAGGGCCCTTCGCCTTGCCCGCTGGCGGGCAGTAG
Enzyme 25 GenBank Gene ID NM_001080400.1 Link Image
Enzyme 25 GeneCard ID PLIN4 Link Image
Enzyme 25 GenAtlas ID PLIN4 Link Image
Enzyme 25 HGNC ID HGNC:29393 Link Image
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 19p13.3
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  2. 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]
  3. Dalen KT, Schoonjans K, Ulven SM, Weedon-Fekjaer MS, Bentzen TG, Koutnikova H, Auwerx J, Nebb HI: Adipose tissue expression of the lipid droplet-associating proteins S3-12 and perilipin is controlled by peroxisome proliferator-activated receptor-gamma. Diabetes. 2004 May;53(5):1243-52. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 17303
Enzyme 26 Name Apolipoprotein C-II
Enzyme 26 Synonyms
  1. Apo-CII
  2. ApoC-II
  3. Apolipoprotein C2
Enzyme 26 Gene Name APOC2
Enzyme 26 Protein Sequence >Apolipoprotein C-II
MGTRLLPALFLVLLVLGFEVQGTQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYE
KTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE
Enzyme 26 Number of Residues 101
Enzyme 26 Molecular Weight 11283.8
Enzyme 26 Theoretical pI 4.36
Enzyme 26 GO Classification
Function
  • enzyme activator activity
  • enzyme regulator activity
Process
  • establishment of localization
  • lipid metabolic process
  • lipid transport
  • metabolic process
  • primary metabolic process
  • transport
Component
  • chylomicron
  • macromolecular complex
  • plasma lipoprotein particle
  • protein-lipid complex
Enzyme 26 General Function Involved in enzyme activator activity
Enzyme 26 Specific Function Component of the very low density lipoprotein (VLDL) fraction in plasma, and is an activator of several triacylglycerol lipases. The association of APOC2 with plasma chylomicrons, VLDL, and HDL is reversible, a function of the secretion and catabolism of triglyceride-rich lipoproteins, and changes rapidly
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • 1-22
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 32130518 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P02655 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name APOC2_HUMAN Link Image
Enzyme 26 PDB ID 1SOH Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >306 bp
ATGGGCACACGACTCCTCCCAGCTCTGTTTCTTGTCCTCCTGGTATTGGGATTTGAGGTC
CAGGGGACCCAACAGCCCCAGCAAGATGAGATGCCTAGCCCGACCTTCCTCACCCAGGTG
AAGGAATCTCTCTCCAGTTACTGGGAGTCAGCAAAGACAGCCGCCCAGAACCTGTACGAG
AAGACATACCTGCCCGCTGTAGATGAGAAACTCAGGGACTTGTACAGCAAAAGCACAGCA
GCCATGAGCACTTACACAGGCATTTTTACTGACCAAGTTCTTTCTGTGCTGAAGGGAGAG
GAGTAA
Enzyme 26 GenBank Gene ID NM_000483.3 Link Image
Enzyme 26 GeneCard ID APOC2 Link Image
Enzyme 26 GenAtlas ID APOC2 Link Image
Enzyme 26 HGNC ID HGNC:609 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 19q13.2
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Fojo SS, Law SW, Brewer HB Jr: The human preproapolipoprotein C-II gene. Complete nucleic acid sequence and genomic organization. FEBS Lett. 1987 Mar 9;213(1):221-6. [PubMed Link Image]
  2. Fojo SS, Law SW, Brewer HB Jr: Human apolipoprotein C-II: complete nucleic acid sequence of preapolipoprotein C-II. Proc Natl Acad Sci U S A. 1984 Oct;81(20):6354-7. [PubMed Link Image]
  3. Sharpe CR, Sidoli A, Shelley CS, Lucero MA, Shoulders CC, Baralle FE: Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA abundance. Nucleic Acids Res. 1984 May 11;12(9):3917-32. [PubMed Link Image]
  4. Das HK, Jackson CL, Miller DA, Leff T, Breslow JL: The human apolipoprotein C-II gene sequence contains a novel chromosome 19-specific minisatellite in its third intron. J Biol Chem. 1987 Apr 5;262(10):4787-93. [PubMed Link Image]
  5. Wei CF, Tsao YK, Robberson DL, Gotto AM Jr, Brown K, Chan L: The structure of the human apolipoprotein C-II gene. Electron microscopic analysis of RNA:DNA hybrids, complete nucleotide sequence, and identification of 5' homologous sequences among apolipoprotein genes. J Biol Chem. 1985 Dec 5;260(28):15211-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, 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]
  7. Myklebost O, Williamson B, Markham AF, Myklebost SR, Rogers J, Woods DE, Humphries SE: The isolation and characterization of cDNA clones for human apolipoprotein CII. J Biol Chem. 1984 Apr 10;259(7):4401-4. [PubMed Link Image]
  8. Jackson CL, Bruns GA, Breslow JL: Isolation of cDNA and genomic clones for apolipoprotein C-II. Methods Enzymol. 1986;128:788-800. [PubMed Link Image]
  9. Hospattankar AV, Fairwell T, Ronan R, Brewer HB Jr: Amino acid sequence of human plasma apolipoprotein C-II from normal and hyperlipoproteinemic subjects. J Biol Chem. 1984 Jan 10;259(1):318-22. [PubMed Link Image]
  10. Jackson RL, Baker HN, Gilliam EB, Gotto AM Jr: Primary structure of very low density apolipoprotein C-II of human plasma. Proc Natl Acad Sci U S A. 1977 May;74(5):1942-5. [PubMed Link Image]
  11. Chun EM, Park YJ, Kang HS, Cho HM, Jun DY, Kim YH: Expression of the apolipoprotein C-II gene during myelomonocytic differentiation of human leukemic cells. J Leukoc Biol. 2001 Apr;69(4):645-50. [PubMed Link Image]
  12. Lycksell PO, Ohman A, Bengtsson-Olivecrona G, Johansson LB, Wijmenga SS, Wernic D, Graslund A: Sequence specific 1H-NMR assignments and secondary structure of a carboxy-terminal functional fragment of apolipoprotein CII. Eur J Biochem. 1992 Apr 1;205(1):223-31. [PubMed Link Image]
  13. Ohman A, Lycksell PO, Graslund A: A refined three-dimensional solution structure of a carboxy terminal fragment of apolipoprotein CII. Eur Biophys J. 1993;22(5):351-7. [PubMed Link Image]
  14. Menzel HJ, Kane JP, Malloy MJ, Havel RJ: A variant primary structure of apolipoprotein C-II in individuals of African descent. J Clin Invest. 1986 Feb;77(2):595-601. [PubMed Link Image]
  15. Pullinger CR, Zysow BR, Hennessy LK, Frost PH, Malloy MJ, Kane JP: Molecular cloning and characteristics of a new apolipoprotein C-II mutant identified in three unrelated individuals with hypercholesterolemia and hypertriglyceridemia. Hum Mol Genet. 1993 Jan;2(1):69-74. [PubMed Link Image]
  16. Hegele RA, Connelly PW, Maguire GF, Huff MW, Leiter L, Wolfe BM, Evans AJ, Little JA: An apolipoprotein CII mutation, CIILys19----Thr' identified in patients with hyperlipidemia. Dis Markers. 1991 Mar-Apr;9(2):73-80. [PubMed Link Image]
  17. Zysow BR, Pullinger CR, Hennessy LK, Farese RV Jr, Ghassemzadeh M, Kane JP: The apolipoprotein C-II variant apoC-IILys19-->Thr is not associated with dyslipidemia in an affected kindred. Clin Genet. 1994 Jun;45(6):292-7. [PubMed Link Image]
  18. Inadera H, Hibino A, Kobayashi J, Kanzaki T, Shirai K, Yukawa S, Saito Y, Yoshida S: A missense mutation (Trp 26-->Arg) in exon 3 of the apolipoprotein CII gene in a patient with apolipoprotein CII deficiency (apo CII-Wakayama). Biochem Biophys Res Commun. 1993 Jun 30;193(3):1174-83. [PubMed Link Image]
  19. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available