Human Metabolome Database Version 2.5

Showing metabocard for PE(16:0/16:0) (HMDB08923)

Legend: metabolite field enzyme field

Version

2.5

Creation Date

2008-09-12 02:45:12

Update Date

2009-05-05 21:04:24

Accession Number

HMDB08923

Secondary Accession Numbers

HMDB05317

Common Name

PE(16:0/16:0)

Description

PE(16:0/16:0) is a phosphatidylethanolamine (PE or GPEtn). It is a glycerophospholipid in which a phosphorylethanolamine moiety occupies a glycerol substitution site. As is the case with diacylglycerols, glycerophosphoethanolamines can have many different combinations of fatty acids of varying lengths and saturation attached at the C-1 and C-2 positions. Fatty acids containing 16, 18 and 20 carbons are the most common. PE(16:0/16:0), in particular, consists of two chains of palmitic acid at the C-1 and C-2 positions. The palmitic acid moieties are derived from fish oils, milk fats, vegetable oils and animal fats. Phospholipids, are ubiquitous in nature and are key components of the lipid bilayer of cells, as well as being involved in metabolism and signaling. While most phospholipids have a saturated fatty acid on C-1 and an unsaturated fatty acid on C-2 of the glycerol backbone, the fatty acid distribution at the C-1 and C-2 positions of glycerol within phospholipids is continually in flux, owing to phospholipid degradation and the continuous phospholipid remodeling that occurs while these molecules are in membranes. PEs are neutral zwitterions at physiological pH. They mostly have palmitic or stearic acid on carbon 1 and a long chain unsaturated fatty acid (e.g. 18:2, 20:4 and 22:6) on carbon 2. PE synthesis can occur via two pathways. The first requires that ethanolamine be activated by phosphorylation and then coupled to CDP. The ethanolamine is then transferred from CDP-ethanolamine to phosphatidic acid to yield PE. The second involves the decarboxylation of PS.

Synonyms

GPEtn(16:0/16:0)
PE(32:0)
PE(16:0/16:0)
Phophatidylethanolamine(16:0/16:0)
1,2-dipalmitoyl-rac-glycero-3-phosphoethanolamine
GPEtn(32:0)
Phophatidylethanolamine(32:0)

Chemical IUPAC Name

1,2-dihexadecanoyl-rac-glycero-3-phosphoethanolamine

Chemical Formula

C₃₇H₇₄NO₈P

Chemical Structure

Chemical Taxonomy

Kingdom
Organic
Super Class
Lipids
Class
Phospholipids
Sub Class
Phosphatidylethanolamines
Family
Mammalian Metabolite
Species
primary amine primary aliphatic amine (alkylamine) carboxylic acid ester phosphoric acid ester
Biofunction
Membrane component Energy source Cell signaling
Application
—
Source
Endogenous

Average Molecular Weight

691.959

Monoisotopic Molecular Weight

691.515198

Isomeric SMILES

CCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(=O)OCCN)OC(=O)CCCCCCCCCCCCCCC

Canonical SMILES

CCCCCCCCCCCCCCCC(=O)OCC(COP(O)(=O)OCCN)OC(=O)CCCCCCCCCCCCCCC

KEGG Compound ID

C00350

BioCyc ID

L-1-PHOSPHATIDYL-ETHANOLAMINE Link Image

BiGG ID

Not Available

Wikipedia Link

Lecithin

NuGOwiki Link

HMDB08923

Metagene Link

HMDB08923

METLIN ID

Not Available

PubChem Compound

65109

PubChem Substance

10365992

ChEBI ID

Not Available

CAS Registry Number

Not Available

InChI Identifier

InChI=1/C37H74NO8P/c1-3-5-7-9-11-13-15-17-19-21-23-25-27-29-36(39)43-33-35(34-45-47(41,42)44-32-31-38)46-37(40)30-28-26-24-22-20-18-16-14-12-10-8-6-4-2/h35H,3-34,38H2,1-2H3,(H,41,42)/t35-/m1/s1

Synthesis Reference

Not Available

Melting Point (Experimental)

Not Available

Experimental Water Solubility

Not Available Source: PhysProp

Predicted Water Solubility

9.45e-05 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS

Physiological Charge

State

Solid

Experimental LogP/Hydrophobicity

Not Available Source: PhysProp

Predicted LogP/Hydrophobicity

8.08 [Predicted by ALOGPS] Calculated using ALOGPS

Material Safety Data Sheet (MSDS)

Not Available

MOL File

Show

SDF File

Show

PDB File

Show

2D Structure

3D Structure

Experimental PDB ID

Not Available

Experimental ¹H NMR Spectrum

Not Available

Experimental ¹³C NMR Spectrum

Not Available

Experimental ¹³C HSQC Spectrum

Not Available

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

Membrane

Biofluid Location

Blood

Tissue Location

Tissue	References
All Tissues	—
Brain	—

Concentrations (Normal)

Biofluid	Blood
Value	15.204 +/- 8.125 uM
Age	Adult:>18 yrs old
Sex	Both
Patient information	Normal (Upper Limit)
Comments	Not Available
References	Nikolaos Psychogios, David D. Hau, Jun Peng, An Chi Guo, Rupasri Mandal, Souhaila Bouatra, Igor Sinelnikov, Ramanarayan Krishnamurthy, Roman Eisner, Bijaya Gautam, Nelson Young, Jinaguo Xia, Craig Knox, Ying Wei Dong, Paul Huang, Janet McManus, Theresa Pedersen, Fiona Bamforth, Russ Greiner, Bruce McManus, John Newman, David S. Wishart, The Human Serum Metabolome, PLoS ONE (Submitted). 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 ]

Biofluid	Blood
Value	3.50225 +/- 2.1383 uM
Age	Adult:>18 yrs old
Sex	Both
Patient information	Normal (Most Probable)
Comments	Not Available
References	Nikolaos Psychogios, David D. Hau, Jun Peng, An Chi Guo, Rupasri Mandal, Souhaila Bouatra, Igor Sinelnikov, Ramanarayan Krishnamurthy, Roman Eisner, Bijaya Gautam, Nelson Young, Jinaguo Xia, Craig Knox, Ying Wei Dong, Paul Huang, Janet McManus, Theresa Pedersen, Fiona Bamforth, Russ Greiner, Bruce McManus, John Newman, David S. Wishart, The Human Serum Metabolome, PLoS ONE (Submitted). 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 ]

Concentrations (Abnormal)

Not Available

Associated Disorders

Not Available

OMIM ID

Not Available

Pathways

Name	SMPDB Link	KEGG Link
Phospholipid Biosynthesis	SMP00025	map00564

General References

Wikipedia

Metabolic Enzymes

Enzyme 1 [top]

Enzyme 1 ID

5287

Enzyme 1 Name

Calcium-dependent phospholipase A2 precursor

Enzyme 1 Synonyms

Phosphatidylcholine 2-acylhydrolase
PLA2-10
Group V phospholipase A2

Enzyme 1 Gene Name

PLA2G5

Enzyme 1 Protein Sequence

>Calcium-dependent phospholipase A2 precursor

MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS

Enzyme 1 Number of Residues

138

Enzyme 1 Molecular Weight

15674

Enzyme 1 Theoretical pI

8.48

Enzyme 1 GO Classification

Function
binding calcium ion binding carboxylic ester hydrolase activity catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding lipase activity phospholipase A2 activity phospholipase activity
Process
lipid catabolism lipid metabolism metabolism physiological process primary metabolism
Component
—

Enzyme 1 General Function

Not Available

Enzyme 1 Specific Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes more efficiently L-alpha-1-palmitoyl-2-oleoyl phosphatidylcholine than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L- alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine, or L- alpha-1-stearoyl-2-arachidonyl phosphatidylinositol. May be involved in the production of lung surfactant, the remodeling or regulation of cardiac muscle

Enzyme 1 Pathways

Arachidonic acid metabolism (map00590 )
Phospholipid Synthesis (map00564 )

Enzyme 1 Reactions

phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate

Enzyme 1 Pfam Domain Function

Phospholip_A2_1 (PF00068 )

Enzyme 1 Signals

1-20

Enzyme 1 Transmembrane Regions

Not Available

Enzyme 1 Essentiality

Not Available

Enzyme 1 GenBank ID Protein

460915

Enzyme 1 UniProtKB/Swiss-Prot ID

P39877

Enzyme 1 UniProtKB/Swiss-Prot Entry Name

PA2G5_HUMAN Link Image

Enzyme 1 PDB ID

Not Available

Enzyme 1 Cellular Location

Not Available

Enzyme 1 Gene Sequence

>417 bp

ATGAAAGGCCTCCTCCCACTGGCTTGGTTCCTGGCTTGTAGTGTGCCTGCTGTGCAAGGA
GGCTTGCTGGACCTAAAATCAATGATCGAGAAGGTGACAGGGAAGAACGCCCTGACAAAC
TACGGCTTCTACGGCTGTTACTGCGGCTGGGGCGGCCGAGGAACCCCCAAGGATGGCACC
GATTGGTGCTGTTGGGCGCATGACCACTGCTATGGGCGGCTGGAGGAGAAGGGCTGCAAC
ATTCGCACACAGTCCTACAAATACAGATTCGCGTGGGGCGTGGTCACCTGCGAGCCCGGG
CCCTTCTGCCATGTGAACCTCTGTGCCTGTGACCGGAAGCTCGTCTACTGCCTCAAGAGA
AACCTACGGAGCTACAACCCACAGTACCAATACTTTCCCAACATCCTCTGCTCCTAG

Enzyme 1 GenBank Gene ID

Enzyme 1 GeneCard ID

Enzyme 1 GenAtlas ID

Enzyme 1 HGNC ID

Enzyme 1 Chromosome Location

Enzyme 1 Locus

1p36-p34

Enzyme 1 SNPs

SNPJam Report Link Image

Enzyme 1 General References

Chen J, Engle SJ, Seilhamer JJ, Tischfield JA: Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2. J Biol Chem. 1994 Jan 28;269(4):2365-8. [PubMed ]

Enzyme 1 Metabolite References

Not Available

Enzyme 2 [top]

Enzyme 2 ID

5288

Enzyme 2 Name

Group IIF secretory phospholipase A2 precursor

Enzyme 2 Synonyms

Phosphatidylcholine 2-acylhydrolase GIIF
GIIF sPLA2
sPLA(2-IIF

Enzyme 2 Gene Name

PLA2G2F

Enzyme 2 Protein Sequence

>Group IIF secretory phospholipase A2 precursor

MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP

Enzyme 2 Number of Residues

168

Enzyme 2 Molecular Weight

18658

Enzyme 2 Theoretical pI

4.94

Enzyme 2 GO Classification

Function
binding calcium ion binding carboxylic ester hydrolase activity catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding lipase activity phospholipase A2 activity phospholipase activity
Process
lipid catabolism lipid metabolism metabolism physiological process primary metabolism
Component
—

Enzyme 2 General Function

Not Available

Enzyme 2 Specific Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference

Enzyme 2 Pathways

Arachidonic acid metabolism (map00590 )
Phospholipid Synthesis (map00564 )

Enzyme 2 Reactions

phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate

Enzyme 2 Pfam Domain Function

Phospholip_A2_1 (PF00068 )

Enzyme 2 Signals

1-20

Enzyme 2 Transmembrane Regions

Not Available

Enzyme 2 Essentiality

Not Available

Enzyme 2 GenBank ID Protein

12276060

Enzyme 2 UniProtKB/Swiss-Prot ID

Q9BZM2

Enzyme 2 UniProtKB/Swiss-Prot Entry Name

PA2GF_HUMAN Link Image

Enzyme 2 PDB ID

Not Available

Enzyme 2 Cellular Location

Not Available

Enzyme 2 Gene Sequence

>507 bp

ATGAAGAAGTTCTTCACCGTGGCCATCCTTGCTGGCAGCGTTCTGTCCACAGCTCACGGC
AGCCTGCTCAACCTGAAGGCCATGGTGGAGGCCGTCACAGGGAGGAGCGCCATCCTGTCC
TTCGTGGGCTACGGTTGCTACTGTGGGCTGGGGGGCCGTGGCCAGCCCAAGGATGAGGTG
GACTGGTGCTGCCACGCCCACGACTGCTGCTACCAGGAACTCTTTGACCAAGGCTGTCAC
CCCTATGTGGACCACTATGATCACACCATCGAGAACAACACTGAGATAGTCTGCAGTGAC
CTCAACAAGACAGAGTGTGACAAGCAGACATGCATGTGTGACAAGAACATGGTTCTGTGC
CTCATGAACCAGACGTACCGAGAGGAGTACCGTGGCTTCCTCAATGTCTACTGCCAGGGC
CCCACGCCCAACTGCAGCATCTATGAACCGCCCCCTGAGGAGGTCACCTGCAGTCACCAA
TCCCCAGCGCCCCCCGCCCCTCCCTAG

Enzyme 2 GenBank Gene ID

AF306566

Enzyme 2 GeneCard ID

PLA2G2F

Enzyme 2 GenAtlas ID

PLA2G2F

Enzyme 2 HGNC ID

HGNC:30040 Link Image

Enzyme 2 Chromosome Location

Enzyme 2 Locus

1p35

Enzyme 2 SNPs

SNPJam Report Link Image

Enzyme 2 General References

Valentin E, Singer AG, Ghomashchi F, Lazdunski M, Gelb MH, Lambeau G: Cloning and recombinant expression of human group IIF-secreted phospholipase A(2). Biochem Biophys Res Commun. 2000 Dec 9;279(1):223-8. [PubMed ]

Enzyme 2 Metabolite References

Not Available

Enzyme 3 [top]

Enzyme 3 ID

5289

Enzyme 3 Name

Cytosolic phospholipase A2

Enzyme 3 Synonyms

cPLA2
Phospholipase A2 group IVA[Includes: Phospholipase A2
Phosphatidylcholine 2- acylhydrolase
Lysophospholipase

Enzyme 3 Gene Name

PLA2G4A

Enzyme 3 Protein Sequence

>Cytosolic phospholipase A2

MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA

Enzyme 3 Number of Residues

749

Enzyme 3 Molecular Weight

85212

Enzyme 3 Theoretical pI

5.03

Enzyme 3 GO Classification

Function
carboxylic ester hydrolase activity catalytic activity hydrolase activity hydrolase activity, acting on ester bonds lipase activity phospholipase activity
Process
cellular lipid metabolism lipid metabolism membrane lipid metabolism metabolism phospholipid catabolism phospholipid metabolism physiological process primary metabolism
Component
—

Enzyme 3 General Function

Not Available

Enzyme 3 Specific Function

Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response

Enzyme 3 Pathways

Phospholipid Synthesis (map00564 )

Enzyme 3 Reactions

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate

Enzyme 3 Pfam Domain Function

C2 (PF00168 )
PLA2_B (PF01735 )

Enzyme 3 Signals

None

Enzyme 3 Transmembrane Regions

None

Enzyme 3 Essentiality

Not Available

Enzyme 3 GenBank ID Protein

190007

Enzyme 3 UniProtKB/Swiss-Prot ID

P47712

Enzyme 3 UniProtKB/Swiss-Prot Entry Name

PA24A_HUMAN Link Image

Enzyme 3 PDB ID

1CJY

Enzyme 3 PDB File

Show

Enzyme 3 3D Structure

Enzyme 3 Cellular Location

Not Available

Enzyme 3 Gene Sequence

>2250 bp

ATGTCATTTATAGATCCTTACCAGCACATTATAGTGGAGCACCAGTATTCCCACAAGTTT
ACGGTAGTGGTGTTACGTGCCACCAAAGTGACAAAGGGGGCCTTTGGTGACATGCTTGAT
ACTCCAGATCCCTATGTGGAACTTTTTATCTCTACAACCCCTGACAGCAGGAAGAGAACA
AGACATTTCAATAATGACATAAACCCTGTGTGGAATGAGACCTTTGAATTTATTTTGGAT
CCTAATCAGGAAAATGTTTTGGAGATTACGTTAATGGATGCCAATTATGTCATGGATGAA
ACTCTAGGGACAGCAACATTTACTGTATCTTCTATGAAGGTGGGAGAAAAGAAAGAAGTT
CCTTTTATTTTCAACCAAGTCACTGAAATGGTTCTAGAAATGTCTCTTGAAGTTTGCTCA
TGCCCAGACCTACGATTTAGTATGGCTCTGTGTGATCAGGAGAAGACTTTCAGACAACAG
AGAAAAGAACACATAAGGGAGAGCATGAAGAAACTCTTGGGTCCAAAGAATAGTGAAGGA
TTGCATTCTGCACGTGATGTGCCTGTGGTAGCCATATTGGGTTCAGGTGGGGGTTTCCGA
GCCATGGTGGGATTCTCTGGTGTGATGAAGGCATTATACGAATCAGGAATTCTGGATTGT
GCTACCTACGTTGCTGGTCTTTCTGGCTCCACCTGGTATATGTCAACCTTGTATTCTCAC
CCTGATTTTCCAGAGAAAGGGCCAGAGGAGATTAATGAAGAACTAATGAAAAATGTTAGC
CACAATCCCCTTTTACTTCTCACACCACAGAAAGTTAAAAGATATGTTGAGTCTTTATGG
AAGAAGAAAAGCTCTGGACAACCTGTCACCTTTACTGATATCTTTGGGATGTTAATAGGA
GAAACACTAATTCATAATAGAATGAATACTACTCTGAGCAGTTTGAAGGAAAAAGTTAAT
ACTGCACAATGCCCTTTACCTCTTTTCACCTGTCTTCATGTCAAACCTGACGTTTCAGAG
CTGATGTTTGCAGATTGGGTTGAATTTAGTCCATACGAAATTGGCATGGCTAAATATGGT
ACTTTTATGGCTCCCGACTTATTTGGAAGCAAATTTTTTATGGGAACAGTCGTTAAGAAG
TATGAAGAAAACCCCTTGCATTTCTTAATGGGTGTCTGGGGCAGTGCCTTTTCCATATTG
TTCAACAGAGTTTTGGGCGTTTCTGGTTCACAAAGCAGAGGCTCCACAATGGAGGAAGAA
TTAGAAAATATTACCACAAAGCATATTGTGAGTAATGATAGCTCGGACAGTGATGATGAA
TCACACGAACCCAAAGGCACTGAAAATGAAGATGCTGGAAGTGACTATCAAAGTGATAAT
CAAGCAAGTTGGATTCATCGTATGATAATGGCCTTGGTGAGTGATTCAGCTTTATTCAAT
ACCAGAGAAGGACGTGCTGGGAAGGTACACAACTTCATGCTGGGCTTGAATCTCAATACA
TCTTATCCACTGTCTCCTTTGAGTGACTTTGCCACACAGGACTCCTTTGATGATGATGAA
CTGGATGCAGCTGTAGCAGATCCTGATGAATTTGAGCGAATATATGAGCCTCTGGATGTC
AAAAGTAAAAAGATTCATGTAGTGGACAGTGGGCTCACATTTAACCTGCCGTATCCCTTG
ATACTGAGACCTCAGAGAGGGGTTGATCTCATAATCTCCTTTGACTTTTCTGCAAGGCCA
AGTGACTCTAGTCCTCCGTTCAAGGAACTTCTACTTGCAGAAAAGTGGGCTAAAATGAAC
AAGCTCCCCTTTCCAAAGATTGATCCTTATGTGTTTGATCGGGAAGGGCTGAAGGAGTGC
TATGTCTTTAAACCCAAGAATCCTGATATGGAGAAAGATTGCCCAACCATCATCCACTTT
GTTCTGGCCAACATCAACTTCAGAAAGTACAAGGCTCCAGGTGTTCCAAGGGAAACTGAG
GAAGAGAAAGAAATCGCTGACTTTGATATTTTTGATGACCCAGAATCACCATTTTCAACC
TTCAATTTTCAATATCCAAATCAAGCATTCAAAAGACTACATGATCTTATGCACTTCAAT
ACTCTGAACAACATTGATGTGATAAAAGAAGCCATGGTTGAAAGCATTGAATATAGAAGA
CAGAATCCATCTCGTTGCTCTGTTTCCCTTAGTAATGTTGAGGCAAGAAGATTTTTCAAC
AAGGAGTTTCTAAGTAAACCCAAAGCATAG

Enzyme 3 GenBank Gene ID

Enzyme 3 GeneCard ID

Enzyme 3 GenAtlas ID

Enzyme 3 HGNC ID

Enzyme 3 Chromosome Location

Enzyme 3 Locus

1q25

Enzyme 3 SNPs

SNPJam Report Link Image

Enzyme 3 General References

Clark JD, Lin LL, Kriz RW, Ramesha CS, Sultzman LA, Lin AY, Milona N, Knopf JL: A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. Cell. 1991 Jun 14;65(6):1043-51. [PubMed ]
Sharp JD, White DL, Chiou XG, Goodson T, Gamboa GC, McClure D, Burgett S, Hoskins J, Skatrud PL, Sportsman JR, et al.: Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2. J Biol Chem. 1991 Aug 15;266(23):14850-3. [PubMed ]
Lin LL, Wartmann M, Lin AY, Knopf JL, Seth A, Davis RJ: cPLA2 is phosphorylated and activated by MAP kinase. Cell. 1993 Jan 29;72(2):269-78. [PubMed ]
Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed ]
Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL: Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J Biol Chem. 1998 Jan 16;273(3):1596-604. [PubMed ]
Xu GY, McDonagh T, Yu HA, Nalefski EA, Clark JD, Cumming DA: Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2. J Mol Biol. 1998 Jul 17;280(3):485-500. [PubMed ]

Enzyme 3 Metabolite References

Not Available

Enzyme 4 [top]

Enzyme 4 ID

5290

Enzyme 4 Name

Phospholipase A2 precursor

Enzyme 4 Synonyms

Phosphatidylcholine 2- acylhydrolase
Group IB phospholipase A2

Enzyme 4 Gene Name

PLA2G1B

Enzyme 4 Protein Sequence

>Phospholipase A2 precursor

MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS

Enzyme 4 Number of Residues

148

Enzyme 4 Molecular Weight

16360

Enzyme 4 Theoretical pI

7.91

Enzyme 4 GO Classification

Function
binding calcium ion binding carboxylic ester hydrolase activity catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding lipase activity phospholipase A2 activity phospholipase activity
Process
lipid catabolism lipid metabolism metabolism physiological process primary metabolism
Component
—

Enzyme 4 General Function

Not Available

Enzyme 4 Specific Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides

Enzyme 4 Pathways

Arachidonic acid metabolism (map00590 )
Phospholipid Synthesis (map00564 )

Enzyme 4 Reactions

phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate

Enzyme 4 Pfam Domain Function

Phospholip_A2_1 (PF00068 )

Enzyme 4 Signals

1-15

Enzyme 4 Transmembrane Regions

Not Available

Enzyme 4 Essentiality

Not Available

Enzyme 4 GenBank ID Protein

387025

Enzyme 4 UniProtKB/Swiss-Prot ID

P04054

Enzyme 4 UniProtKB/Swiss-Prot Entry Name

PA21B_HUMAN Link Image

Enzyme 4 PDB ID

Not Available

Enzyme 4 Cellular Location

Not Available

Enzyme 4 Gene Sequence

>447 bp

ATGAAACTCCTTGTGCTAGCTGTGCTGCTCACAGTGGCCGCCGCCGACAGCGGCATCAGC
CCTCGGGCCGTGTGGCAGTTCCGCAAAATGATCAAGTGCGTGATCCCGGGGAGTGACCCC
TTCTTGGAATACAACAACTACGGCTGCTACTGTGGCTTGGGGGGCTCAGGCACCCCCGTG
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTACGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA

Enzyme 4 GenBank Gene ID

Enzyme 4 GeneCard ID

Enzyme 4 GenAtlas ID

Enzyme 4 HGNC ID

Enzyme 4 Chromosome Location

Enzyme 4 Locus

12q23-q24.1

Enzyme 4 SNPs

SNPJam Report Link Image

Enzyme 4 General References

Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK: Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. DNA. 1986 Dec;5(6):519-27. [PubMed ]
Grataroli R, Dijkman R, Dutilh CE, van der Ouderaa F, De Haas GH, Figarella C: Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region. Eur J Biochem. 1982 Feb;122(1):111-7. [PubMed ]
Verheij HM, Westerman J, Sternby B, De Haas GH: The complete primary structure of phospholipase A2 from human pancreas. Biochim Biophys Acta. 1983 Sep 14;747(1-2):93-9. [PubMed ]

Enzyme 4 Metabolite References

Not Available

Enzyme 5 [top]

Enzyme 5 ID

5291

Enzyme 5 Name

Group XIIB secretory phospholipase A2-like protein precursor

Enzyme 5 Synonyms

Group XIII secretory phospholipase A2-like protein
GXIII sPLA2-like
GXIIB

Enzyme 5 Gene Name

PLA2G12B

Enzyme 5 Protein Sequence

>Group XIIB secretory phospholipase A2-like protein precursor

MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGK
NGVCQYRCRYGKAPMPRPGYKPQEPNGCGSYFLGLKVPESMDLGIPAMTKCCNQLDVCYD
TCGANKYRCDAKFRWCLHSICSDLKRSLGFVSKVEAACDSLVDTVFNTVWTLGCRPFMNS
QRAACICAEEEKEEL

Enzyme 5 Number of Residues

195

Enzyme 5 Molecular Weight

21659

Enzyme 5 Theoretical pI

5.81

Enzyme 5 GO Classification

Function
binding calcium ion binding carboxylic ester hydrolase activity catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding lipase activity phospholipase A2 activity phospholipase activity
Process
lipid catabolism lipid metabolism metabolism physiological process primary metabolism
Component
extracellular region

Enzyme 5 General Function

Not Available

Enzyme 5 Specific Function

Not known; does not seem to have catalytic activity

Enzyme 5 Pathways

Not Available

Enzyme 5 Reactions

Not Available

Enzyme 5 Pfam Domain Function

PLA2G12 (PF06951 )

Enzyme 5 Signals

1-19

Enzyme 5 Transmembrane Regions

Not Available

Enzyme 5 Essentiality

Not Available

Enzyme 5 GenBank ID Protein

13560707

Enzyme 5 UniProtKB/Swiss-Prot ID

Q9BX93

Enzyme 5 UniProtKB/Swiss-Prot Entry Name

PG12B_HUMAN Link Image

Enzyme 5 PDB ID

Not Available

Enzyme 5 Cellular Location

Not Available

Enzyme 5 Gene Sequence

>585 bp

ATGAAGCTGGCCAGTGGCTTCTTGGTTTTGTGGCTCAGCCTTGGGGGTGGCCTGGCTCAG
AGCGACACGAGCCCTGACACGGAGGAGTCCTATTCAGACTGGGGCCTTCGGCACCTCCGG
GGAAGCTTTGAATCCGTCAATAGCTACTTCGATTCTTTTCTGGAGCTGCTGGGAGGGAAG
AATGGAGTCTGTCAGTACAGGTGCCGATATGGAAAGGCACCAATGCCCAGACCTGGCTAC
AAGCCCCAAGAGCCCAATGGCTGCGGCTCCTATTTCCTGGGTCTCAAGGTACCAGAAAGT
ATGGACTTGGGCATTCCAGCAATGACAAAGTGCTGCAACCAGCTGGATGTCTGTTATGAC
ACTTGCGGTGCCAACAAATATCGCTGTGATGCAAAATTCCGATGGTGTCTCCACTCGATC
TGCTCTGACCTTAAGCGGAGTCTGGGCTTTGTCTCCAAAGTGGAAGCCTGTGATTCCCTG
GTTGACACTGTGTTCAACACCGTGTGGACCTTGGGCTGCCGCCCCTTTATGAATAGTCAG
CGGGCAGCTTGCATCTGTGCAGAGGAGGAGAAGGAAGAGTTATGA

Enzyme 5 GenBank Gene ID

AF349540

Enzyme 5 GeneCard ID

PLA2G12B

Enzyme 5 GenAtlas ID

PLA2G12B

Enzyme 5 HGNC ID

HGNC:18555 Link Image

Enzyme 5 Chromosome Location

Enzyme 5 Locus

10q22.1

Enzyme 5 SNPs

SNPJam Report Link Image

Enzyme 5 General References

Rouault M, Bollinger JG, Lazdunski M, Gelb MH, Lambeau G: Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity. Biochemistry. 2003 Oct 7;42(39):11494-503. [PubMed ]

Enzyme 5 Metabolite References

Not Available

Enzyme 6 [top]

Enzyme 6 ID

5292

Enzyme 6 Name

Group 10 secretory phospholipase A2 precursor

Enzyme 6 Synonyms

Group X secretory phospholipase A2
Phosphatidylcholine 2-acylhydrolase GX
GX sPLA2
sPLA2-X

Enzyme 6 Gene Name

PLA2G10

Enzyme 6 Protein Sequence

>Group 10 secretory phospholipase A2 precursor

MLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPIAYMKYGCFCG
LGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGPAENKCQELLC
KCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD

Enzyme 6 Number of Residues

155

Enzyme 6 Molecular Weight

17132

Enzyme 6 Theoretical pI

6.46

Enzyme 6 GO Classification

Function
binding calcium ion binding carboxylic ester hydrolase activity catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding lipase activity phospholipase A2 activity phospholipase activity
Process
lipid catabolism lipid metabolism metabolism physiological process primary metabolism
Component
—

Enzyme 6 General Function

Not Available

Enzyme 6 Specific Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine

Enzyme 6 Pathways

Arachidonic acid metabolism (map00590 )
Phospholipid Synthesis (map00564 )

Enzyme 6 Reactions

phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate

Enzyme 6 Pfam Domain Function

Phospholip_A2_1 (PF00068 )

Enzyme 6 Signals

1-21

Enzyme 6 Transmembrane Regions

Not Available

Enzyme 6 Essentiality

Not Available

Enzyme 6 GenBank ID Protein

2289237

Enzyme 6 UniProtKB/Swiss-Prot ID

O15496

Enzyme 6 UniProtKB/Swiss-Prot Entry Name

PA2GX_HUMAN Link Image

Enzyme 6 PDB ID

Not Available

Enzyme 6 Cellular Location

Not Available

Enzyme 6 Gene Sequence

>498 bp

ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA

Enzyme 6 GenBank Gene ID

Enzyme 6 GeneCard ID

Enzyme 6 GenAtlas ID

Enzyme 6 HGNC ID

Enzyme 6 Chromosome Location

Enzyme 6 Locus

16p13.1-p12

Enzyme 6 SNPs

SNPJam Report Link Image

Enzyme 6 General References

Cupillard L, Koumanov K, Mattei MG, Lazdunski M, Lambeau G: Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. J Biol Chem. 1997 Jun 20;272(25):15745-52. [PubMed ]

Enzyme 6 Metabolite References

Not Available

Enzyme 7 [top]

Enzyme 7 ID

5294

Enzyme 7 Name

Group IIE secretory phospholipase A2 precursor

Enzyme 7 Synonyms

Phosphatidylcholine 2-acylhydrolase GIIE
GIIE sPLA2
sPLA(2-IIE

Enzyme 7 Gene Name

PLA2G2E

Enzyme 7 Protein Sequence

>Group IIE secretory phospholipase A2 precursor

MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC

Enzyme 7 Number of Residues

142

Enzyme 7 Molecular Weight

15989

Enzyme 7 Theoretical pI

8.28

Enzyme 7 GO Classification

Function
binding calcium ion binding carboxylic ester hydrolase activity catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding lipase activity phospholipase A2 activity phospholipase activity
Process
lipid catabolism lipid metabolism metabolism physiological process primary metabolism
Component
—

Enzyme 7 General Function

Not Available

Enzyme 7 Specific Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids

Enzyme 7 Pathways

Arachidonic acid metabolism (map00590 )
Phospholipid Synthesis (map00564 )

Enzyme 7 Reactions

phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate

Enzyme 7 Pfam Domain Function

Phospholip_A2_1 (PF00068 )

Enzyme 7 Signals

1-19

Enzyme 7 Transmembrane Regions

Not Available

Enzyme 7 Essentiality

Not Available

Enzyme 7 GenBank ID Protein

7108923

Enzyme 7 UniProtKB/Swiss-Prot ID

Q9NZK7

Enzyme 7 UniProtKB/Swiss-Prot Entry Name

PA2GE_HUMAN Link Image

Enzyme 7 PDB ID

Not Available

Enzyme 7 Cellular Location

Not Available

Enzyme 7 Gene Sequence

>429 bp

ATGAAATCTCCCCACGTGCTGGTGTTCCTTTGCCTCCTGGTGGCTCTGGTCACCGGGAAC
CTGGTTCAGTTTGGGGTGATGATCGAGAAGATGACAGGCAAGTCCGCCCTGCAGTACAAC
GACTATGGCTGTTACTGCGGCATCGGTGGCTCCCACTGGCCGGTGGACCAGACTGACTGG
TGCTGCCACGCCCACGACTGCTGCTACGGGCGTCTGGAGAAGCTGGGCTGTGAGCCCAAA
CTGGAAAAGTATCTTTTCTCTGTCAGCGAACGTGGCATTTTCTGCGCCGGCAGGACCACC
TGCCAGCGGCTGACCTGCGAGTGTGACAAGAGGGCTGCCCTCTGCTTTCGCCGCAACCTG
GGCACCTACAACCGCAAATATGCCCATTATCCCAACAAGCTGTGCACCGGGCCCACCCCG
CCCTGCTGA

Enzyme 7 GenBank Gene ID

AF189279

Enzyme 7 GeneCard ID

PLA2G2E

Enzyme 7 GenAtlas ID

PLA2G2E

Enzyme 7 HGNC ID

HGNC:13414 Link Image

Enzyme 7 Chromosome Location

Enzyme 7 Locus

1p36.13

Enzyme 7 SNPs

SNPJam Report Link Image

Enzyme 7 General References

Suzuki N, Ishizaki J, Yokota Y, Higashino K, Ono T, Ikeda M, Fujii N, Kawamoto K, Hanasaki K: Structures, enzymatic properties, and expression of novel human and mouse secretory phospholipase A(2)s. J Biol Chem. 2000 Feb 25;275(8):5785-93. [PubMed ]

Enzyme 7 Metabolite References

Not Available

Enzyme 8 [top]

Enzyme 8 ID

5302

Enzyme 8 Name

Group IID secretory phospholipase A2 precursor

Enzyme 8 Synonyms

Phosphatidylcholine 2-acylhydrolase GIID
GIID sPLA2
PLA2IID
sPLA(2-IID
Secretory-type PLA, stroma-associated homolog

Enzyme 8 Gene Name

PLA2G2D

Enzyme 8 Protein Sequence

>Group IID secretory phospholipase A2 precursor

MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC

Enzyme 8 Number of Residues

145

Enzyme 8 Molecular Weight

16546

Enzyme 8 Theoretical pI

8.28

Enzyme 8 GO Classification

Function
binding calcium ion binding carboxylic ester hydrolase activity catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding lipase activity phospholipase A2 activity phospholipase activity
Process
lipid catabolism lipid metabolism metabolism physiological process primary metabolism
Component
—

Enzyme 8 General Function

Not Available

Enzyme 8 Specific Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined

Enzyme 8 Pathways

Arachidonic acid metabolism (map00590 )
Phospholipid Synthesis (map00564 )

Enzyme 8 Reactions

phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate

Enzyme 8 Pfam Domain Function

Phospholip_A2_1 (PF00068 )

Enzyme 8 Signals

1-20

Enzyme 8 Transmembrane Regions

Not Available

Enzyme 8 Essentiality

Not Available

Enzyme 8 GenBank ID Protein

5771420

Enzyme 8 UniProtKB/Swiss-Prot ID

Q9UNK4

Enzyme 8 UniProtKB/Swiss-Prot Entry Name

PA2GD_HUMAN Link Image

Enzyme 8 PDB ID

Not Available

Enzyme 8 Cellular Location

Not Available

Enzyme 8 Gene Sequence

>438 bp

ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG

Enzyme 8 GenBank Gene ID

Enzyme 8 GeneCard ID

Enzyme 8 GenAtlas ID

Enzyme 8 HGNC ID

Enzyme 8 Chromosome Location

Enzyme 8 Locus

1p36.12

Enzyme 8 SNPs

SNPJam Report Link Image

Enzyme 8 General References

Ishizaki J, Suzuki N, Higashino K, Yokota Y, Ono T, Kawamoto K, Fujii N, Arita H, Hanasaki K: Cloning and characterization of novel mouse and human secretory phospholipase A(2)s. J Biol Chem. 1999 Aug 27;274(35):24973-9. [PubMed ]
Shakhov AN, Rubtsov AV, Lyakhov IG, Tumanov AV, Nedospasov SA: SPLASH (PLA2IID), a novel member of phospholipase A2 family, is associated with lymphotoxin deficiency. Genes Immun. 2000 Feb;1(3):191-9. [PubMed ]

Enzyme 8 Metabolite References

Not Available

Enzyme 9 [top]

Enzyme 9 ID

5309

Enzyme 9 Name

Phospholipase D2

Enzyme 9 Synonyms

PLD 2
Choline phosphatase 2
Phosphatidylcholine-hydrolyzing phospholipase D2
PLD1C
hPLD2

Enzyme 9 Gene Name

PLD2

Enzyme 9 Protein Sequence

>Phospholipase D2

MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFA
PGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVL
MSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYR
NYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVV
KDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQAR
WWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIF
ITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRAL
MLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSE
SAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPW
RDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQ
CTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDE
IVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHR
LKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLL
GKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICD
DFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQ
GHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT

Enzyme 9 Number of Residues

933

Enzyme 9 Molecular Weight

105988

Enzyme 9 Theoretical pI

7.68

Enzyme 9 GO Classification

Function
catalytic activity
Process
cell communication cellular process intracellular signaling cascade metabolism physiological process signal transduction
Component
—

Enzyme 9 General Function

Lipid transport and metabolism

Enzyme 9 Specific Function

May have a role in signal-induced cytoskeletal regulation and/or endocytosis

Enzyme 9 Pathways

Phospholipid Synthesis (map00564 )

Enzyme 9 Reactions

A phosphatidylcholine + H2O = choline + a phosphatidate

Enzyme 9 Pfam Domain Function

PH (PF00169 )
PLDc (PF00614 )
PX (PF00787 )

Enzyme 9 Signals

None

Enzyme 9 Transmembrane Regions

None

Enzyme 9 Essentiality

Not Available

Enzyme 9 GenBank ID Protein

2645858

Enzyme 9 UniProtKB/Swiss-Prot ID

O14939

Enzyme 9 UniProtKB/Swiss-Prot Entry Name

PLD2_HUMAN Link Image

Enzyme 9 PDB ID

Not Available

Enzyme 9 Cellular Location

Not Available

Enzyme 9 Gene Sequence

>2802 bp

ATGACGGCGACCCCTGAGAGCCTCTTCCCCACTGGGGACGAACTGGACTCCAGCCAGCTC
CAGATGGAGTCCGATGAGGTGGACACCCTGAAGGAGGGAGAGGACCCAGCCGACCGGATG
CACCCGTTTCTGGCCATCTATGAGCTTCAGTCTCTGAAAGTGCACCCCTTGGTGTTCGCA
CCTGGGGTCCCTGTCACAGCCCAGGTGGTGGGCACCGAAAGATATACCAGCGGATCCAAG
GTGGGAACCTGCACTCTGTATTCTGTCCGCTTGACTCACGGCGACTTTTCCTGGACAACC
AAGAAGAAATACCGTCATTTTCAGGAGCTGCATCGGGACCTCCTGAGACACAAAGTCTTG
ATGAGTCTGCTCCCTCTGGCTCGATTTGCCGTTGCCTATTCTCCAGCCCGAGATGCAGGC
AACAGAGAGATGCCCTCTCTACCCCGGGCAGGTCCTGAGGGCTCCACCAGACATGCAGCC
AGCAAACAGAAATACCTGGAGAATTACCTCAACTGTCTCTTGACCATGTCTTTCTATCGC
AACTACCATGCCATGACAGAGTTCCTGGAAGTCAGTCAGCTGTCCTTTATCCCGGACTTG
GGCCGCAAAGGACTGGAGGGGATGATCCGGAAGCGCTCAGGTGGCCACCGTGTTCCTGGC
CTCACCTGCTGTGGCCGAGACCAAGTTTGTTATCGCTGGTCCAAGAGGTGGCTGGTGGTG
AAGGACTCCTTCCTGCTGTACATGTGCCTCGAGACAGGTGCCATCTCATTTGTTCAGCTC
TTTGACCCTGGCTTTGAGGTGCAAGTGGGGAAAAGGAGCACGGAGGCACGGCACGGCGTG
CGGATCGATACCTCCCACAGGTCCTTGATTCTCAAGTGCAGCAGCTACCGGCAGGCACGG
TGGTGGGCCCAAGAGATCACTGAGCTGGCACAGGGCCCAGGCAGAGACTTCCTACAGCTG
CACCGGCATGACAGCTACGCCCCACCCCGGCCTGGGACCTTGGCCCGGTGGTTTGTGAAT
GGGGCAGGTTACTTTGCTGCTGTGGCAGATGCCATCCTTCGAGCTCAAGAGGAGATTTTC
ATCACAGACTGGTGGTTGAGTCCTGAGGTTTACCTGAAGCGTCCGGCCCATTCAGATGAC
TGGAGACTGGACATTATGCTCAAGAGGAAGGCGGAGGAAGGTGTCCGTGTGTCTATTCTG
CTGTTTAAAGAAGTGGAATTGGCCTTGGGCATCAACAGTGGCTATAGCAAGAGGGCGCTG
ATGCTGCTGCACCCCAACATAAAGGTGATGCGTCACCCAGACCAAGTGACGTTGTGGGCC
CATCATGAGAAGCTCCTGGTGGTGGACCAAGTGGTAGCATTCCTGGGGGGACTGGACCTT
GCCTATGGCCGCTGGGATGACCTGCACTACCGACTGACTGACCTTGGAGACTCCTCTGAA
TCAGCTGCCTCCCAGCCTCCCACCCCGCGCCCAGACTCACCAGCCACCCCAGACCTCTCT
CACAACCAATTCTTCTGGCTGGGCAAGGACTACAGCAATCTTATCACCAAGGACTGGGTG
CAGCTGGACCGGCCTTTCGAAGATTTCATTGACAGGGAGACGACCCCTCGGATGCCATGG
CGGGACGTTGGGGTGGTCGTCCATGGCCTACCGGCCCGGGACCTTGCCCGGCACTTCATC
CAGCGCTGGAACTTCACCAAGACCACCAAGGCCAAGTACAAGACTCCCACATACCCCTAC
CTGCTTCCCAAGTCTACCAGCACGGCCAATCAGCTCCCCTTCACACTTCCAGGAGGGCAG
TGCACCACCGTACAGGTCTTGCGATCAGTGGACCGCTGGTCAGCAGGGACTCTGGAGAAC
TCCATCCTCAATGCCTACCTGCACACCATCAGGGAGAGCCAGCACTTCCTCTACATTGAG
AATCAGTTCTTCATTAGCTGCTCAGATGGGCGGACGGTTCTGAACAAGGTGGGCGATGAG
ATTGTGGACAGAATCCTGAAGGCCCACAAACAGGGGTGGTGTTACCGAGTCTACGTGCTT
TTGCCCTTACTCCCTGGCTTCGAGGGTGACATCTCCACGGGCGGTGGCAACTCCATCCAG
GCCATTCTGCACTTTACTTACAGGACCCTGTGTCGTGGGGAGTATTCAATCCTGCATCGC
CTTAAAGCAGCCATGGGGACAGCATGGCGGGACTATATTTCCATCTGCGGGCTTCGTACA
CACGGAGAGCTGGGCGGGCACCCCGTCTCGGAGCTCATCTACATCCACAGCAAGGTGCTC
ATCGCAGATGACCGGACAGTCATCATTGGTTCTGCAAACATCAATGACCGGAGCTTGCTG
GGGAAGCGGGACAGTGAGCTGGCCGTGCTGATCGAGGACACAGAGACGGAACCATCCCTC
ATGAATGGGGCAGAGTATCAGGCGGGCAGGTTTGCCTTGAGTCTGCGGAAGCACTGCTTC
GGTGTGATTCTTGGAGCAAATACCCGGCCAGACTTGGATCTCCGAGACCCCATCTGTGAT
GACTTCTTCCAGTTGTGGCAAGACATGGCTGAGAGCAACGCCAATATCTATGAGCAGATC
TTCCGCTGCCTGCCATCCAATGCCACGCGTTCCCTGCGGACTCTCCGGGAGTACGTGGCC
GTGGAGCCCTTGGCCACGGTCAGTCCCCCCTTGGCTCGGTCTGAGCTCACCCAGGTCCAG
GGCCACCTGGTCCACTTCCCCCTCAAGTTCCTAGAGGATGAGTCTTTGCTGCCCCCGCTG
GGTAGCAAGGAGGGCATGATCCCCCTAGAAGTGTGGACATAG

Enzyme 9 GenBank Gene ID

Enzyme 9 GeneCard ID

Enzyme 9 GenAtlas ID

Enzyme 9 HGNC ID

Enzyme 9 Chromosome Location

Enzyme 9 Locus

17p13.1

Enzyme 9 SNPs

SNPJam Report Link Image

Enzyme 9 General References

Steed PM, Clark KL, Boyar WC, Lasala DJ: Characterization of human PLD2 and the analysis of PLD isoform splice variants. FASEB J. 1998 Oct;12(13):1309-17. [PubMed ]
Lopez I, Arnold RS, Lambeth JD: Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J Biol Chem. 1998 May 22;273(21):12846-52. [PubMed ]

Enzyme 9 Metabolite References

Not Available

Enzyme 10 [top]

Enzyme 10 ID

5310

Enzyme 10 Name

Phosphatidylethanolamine N-methyltransferase

Enzyme 10 Synonyms

PEAMT
PEMT
PEMT2

Enzyme 10 Gene Name

PEMT

Enzyme 10 Protein Sequence

>Phosphatidylethanolamine N-methyltransferase

MTRLLGYVDPLDPSFVAAVITITFNPLYWNVVARWEHKTRKLSRAFGSPYLACYSLSVTI
LLLNFLRSHCFTQAMLSQPRMESLDTPAAYSLGLALLGLGVVLVLSSFFALGFAGTFLGD
YFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIMALLYE
EPFTAEIYRQKASGSHKRS

Enzyme 10 Number of Residues

199

Enzyme 10 Molecular Weight

22166

Enzyme 10 Theoretical pI

8.96

Enzyme 10 GO Classification

Function
N-methyltransferase activity catalytic activity methyltransferase activity transferase activity transferase activity, transferring one-carbon groups
Process
cellular lipid metabolism lipid metabolism membrane lipid metabolism metabolism phospholipid metabolism physiological process primary metabolism
Component
—

Enzyme 10 General Function

Not Available

Enzyme 10 Specific Function

Catalyzes three sequential methylation of phosphatidylethanolamine (PE) by AdoMet, thus producing phosphatidylcholine (PC)

Enzyme 10 Pathways

Phospholipid Synthesis (map00564 )
Glycine, Serine and Threonine Metabolism (map00260 )

Enzyme 10 Reactions

S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine

Enzyme 10 Pfam Domain Function

PEMT (PF04191 )

Enzyme 10 Signals

None

Enzyme 10 Transmembrane Regions

13-33 46-66 94-114 158-178

Enzyme 10 Essentiality

Not Available

Enzyme 10 GenBank ID Protein

5825555

Enzyme 10 UniProtKB/Swiss-Prot ID

Q9UBM1

Enzyme 10 UniProtKB/Swiss-Prot Entry Name

PEMT_HUMAN Link Image

Enzyme 10 PDB ID

Not Available

Enzyme 10 Cellular Location

Not Available

Enzyme 10 Gene Sequence

>600 bp

ATGACCCGGCTGCTGGGCTACGTGGACCCCCTGGATCCCAGCTTTGTGGCTGCCGTCATC
ACCATCACCTTCAATCCGCTCTACTGGAATGTGGTTGCACGATGGGAACACAAGACCCGC
AAGCTGAGCAGGGCCTTCGGATCCCCCTACCTGGCCTGCTACTCTCTAAGCGTCACCATC
CTGCTCCTGAACTTCCTGCGCTCGCACTGCTTCACGCAGGCCATGCTGAGCCAGCCCAGG
ATGGAGAGCCTGGACACCCCCGCGGCCTACAGCCTGGGCCTCGCGCTCCTGGGACTGGGC
GTCGTGCTCGTGCTCTCCAGCTTCTTTGCACTGGGGTTCGCTGGAACTTTCCTAGGTGAT
TACTTCGGGATCCTCAAGGAGGCGAGAGTGACCGTGTTCCCCTTCAACATCCTGGACAAC
CCCATGTACTGGGGAAGCACAGCCAACTACTTGGGCTGGGCCATCATGCACGCCAGCCCC
ACGGGCCTGCTCCTGACGGTGCTGGTGGCCCTCACCTACATAATGGCTCTCCTATACGAA
GAGCCCTTCACCGCTGAGATCTACCGGCAGAAAGCCTCCGGGTCCCACAAGAGGAGCTGA

Enzyme 10 GenBank Gene ID

AF176807

Enzyme 10 GeneCard ID

PEMT

Enzyme 10 GenAtlas ID

PEMT

Enzyme 10 HGNC ID

HGNC:8830

Enzyme 10 Chromosome Location

Enzyme 10 Locus

17p11.2

Enzyme 10 SNPs

SNPJam Report Link Image

Enzyme 10 General References

Walkey CJ, Shields DJ, Vance DE: Identification of three novel cDNAs for human phosphatidylethanolamine N-methyltransferase and localization of the human gene on chromosome 17p11.2. Biochim Biophys Acta. 1999 Jan 4;1436(3):405-12. [PubMed ]
Shields DJ, Agellon LB, Vance DE: Structure, expression profile and alternative processing of the human phosphatidylethanolamine N-methyltransferase (PEMT) gene. Biochim Biophys Acta. 2001 May 31;1532(1-2):105-14. [PubMed ]
Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed ]

Enzyme 10 Metabolite References

Not Available

Enzyme 11 [top]

Enzyme 11 ID

5311

Enzyme 11 Name

Phospholipase D1

Enzyme 11 Synonyms

PLD 1
Choline phosphatase 1
Phosphatidylcholine-hydrolyzing phospholipase D1
hPLD1

Enzyme 11 Gene Name

PLD1

Enzyme 11 Protein Sequence

>Phospholipase D1

MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSA
IYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKF
KHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREMPSLPRSSENMIREEQFLGRR
KQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNC
CGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRID
NLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKG
YFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLY
KEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGI
DLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKS
IDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGL
KPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQL
DKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLL
PKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIE
NQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQ
AIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLL
IADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCF
RVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFI
NKPVLAKEDPIRAEEELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT

Enzyme 11 Number of Residues

1074

Enzyme 11 Molecular Weight

124186

Enzyme 11 Theoretical pI

9.07

Enzyme 11 GO Classification

Function
catalytic activity
Process
cell communication cellular process intracellular signaling cascade metabolism physiological process signal transduction
Component
—

Enzyme 11 General Function

Lipid transport and metabolism

Enzyme 11 Specific Function

Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic

Enzyme 11 Pathways

Phospholipid Synthesis (map00564 )

Enzyme 11 Reactions

A phosphatidylcholine + H2O = choline + a phosphatidate

Enzyme 11 Pfam Domain Function

PH (PF00169 )
PLDc (PF00614 )
PX (PF00787 )

Enzyme 11 Signals

None

Enzyme 11 Transmembrane Regions

None

Enzyme 11 Essentiality

Not Available

Enzyme 11 GenBank ID Protein

1185463

Enzyme 11 UniProtKB/Swiss-Prot ID

Q13393

Enzyme 11 UniProtKB/Swiss-Prot Entry Name

PLD1_HUMAN Link Image

Enzyme 11 PDB ID

Not Available

Enzyme 11 Cellular Location

Not Available

Enzyme 11 Gene Sequence

>3225 bp

ATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAATTGCTGCTGAC
ATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGGGAGAGGAGGTA
GACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCCCTTTCTCTGCT
ATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCTCCGGCTGTCCA
ATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGGTACCAAGTATT
AATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTAAGAGGAAATTC
AAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTATCCGCATCCCC
ATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGCCTCGAGAGATG
CCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCCTTGGTAGAAGA
AAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATAGAAACTATCAT
GCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATTTGGGACCAAAG
GGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAGGCTTGAATTGC
TGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAGTGAAAGATTCC
TTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGCTGGTAGACAAA
GAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAATCCGAATTGAT
AATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTCGGTGGTGGGGA
GGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAGATCATCGATTT
GGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTAATGCCAAAGGA
TATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTTTTATCACAGAC
TGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAAATCGTTGGAGG
TTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCATAATGCTCTAC
AAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGACTTTGATGCGT
CTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCACCGTCTATTTG
TGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTGTGGGAGGGATT
GACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACGTGGGCAGTGTG
AAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAATGGAGTCTATG
GAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCATCCAGAAGAGT
ATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGTTCTCCAAATTT
AGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCATCAGCAGCATT
GACAGCACCTCCAGTTATTTTAATCACTATAGAAGTCATCACAATTTAATCCATGGTTTA
AAACCCCACTTCAAACTCTTTCACCCGTCCAGTGAGTCTGAGCAAGGACTCACTAGACCT
CATGCTGATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGGGAGAGCTGCATGGGGAA
ACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCAAAGACTGGGTTCAACTT
GATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCCGGATGCCCTGGCATGAC
ATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCACGTCACTTCATCCAGCGC
TGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTTCTTATCCTTTTCTGCTT
CCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGCCTGGGTCTGTCCATGCT
AACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTATAAAGTACCATGAAGAG
TCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGCACTATATCTATATCGAA
AACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCAACAAGATAGGCGATGCC
ATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAATACCGGGTATATGTCGTG
ATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCGGAGGAAATGCTCTACAG
GCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAAATTCCATCCTTGGACAG
TTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCATTCTGTGGTCTTAGAACA
CATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATGTCCACAGCAAGTTGTTA
ATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAAATGACCGCAGCATGCTG
GGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAGAGACTGTTCCTTCAGTA
ATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGACTTCGGCTACAGTGCTTT
AGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTCAGGATCCAGTGAGTGAC
AAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATGCTACAATTTATGACAAG
GTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTCAGCTGAGAGACTTTATA
AACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGGAGGAACTGAAGAAGATC
CGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAGAAAGCCTACTGCCTTCT
GTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTTAA

Enzyme 11 GenBank Gene ID

U38545

Enzyme 11 GeneCard ID

PLD1

Enzyme 11 GenAtlas ID

PLD1

Enzyme 11 HGNC ID

HGNC:9067

Enzyme 11 Chromosome Location

Enzyme 11 Locus

3q26

Enzyme 11 SNPs

SNPJam Report Link Image

Enzyme 11 General References

Hammond SM, Altshuller YM, Sung TC, Rudge SA, Rose K, Engebrecht J, Morris AJ, Frohman MA: Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J Biol Chem. 1995 Dec 15;270(50):29640-3. [PubMed ]
Hammond SM, Jenco JM, Nakashima S, Cadwallader K, Gu Q, Cook S, Nozawa Y, Prestwich GD, Frohman MA, Morris AJ: Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha. J Biol Chem. 1997 Feb 7;272(6):3860-8. [PubMed ]
Steed PM, Clark KL, Boyar WC, Lasala DJ: Characterization of human PLD2 and the analysis of PLD isoform splice variants. FASEB J. 1998 Oct;12(13):1309-17. [PubMed ]
Lopez I, Arnold RS, Lambeth JD: Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J Biol Chem. 1998 May 22;273(21):12846-52. [PubMed ]

Enzyme 11 Metabolite References

Not Available

Enzyme 12 [top]

Enzyme 12 ID

5783

Enzyme 12 Name

Group 3 secretory phospholipase A2 precursor

Enzyme 12 Synonyms

Group III secretory phospholipase A2
Phosphatidylcholine 2-acylhydrolase GIII
GIII sPLA2

Enzyme 12 Gene Name

PLA2G3

Enzyme 12 Protein Sequence

>Group 3 secretory phospholipase A2 precursor

MGVQAGLFGMLGFLGVALGGSPALRWYRTSCHLTKAVPGNPLGYLSFLAKDAQGLALIHA
RWDAHRRLQACSWEDEPELTAAYGALCAHETAWGSFIHTPGPELQRALATLQSQWEACRA
LEESPAGARKKRAAGQSGVPGGGHQREKRGWTMPGTLWCGVGDSAGNSSELGVFQGPDLC
CREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDIVGVAFFNVL
EIPCFVLEEQEACVAWYWWGGCRMYGTVPLARLQPRTFYNASWSSRATSPTPSSRSPAPP
KPRQKQHLRKGPPHQKGSKRPSKANTTALQDPMVSPRLDVAPTGLQGPQGGLKPQGARWV
CRSFRRHLDQCEHQIGPREIEFQLLNSAQEPLFHCNCTRRLARFLRLHSPPEVTNMLWEL
LGTTCFKLAPPLDCVEGKNCSRDPRAIRVSARHLRRLQQRRHQLQDKGTDERQPWPSEPL
RGPMSFYNQCLQLTQAARRPDRQQKSWSQ

Enzyme 12 Number of Residues

509

Enzyme 12 Molecular Weight

57152

Enzyme 12 Theoretical pI

9.23

Enzyme 12 GO Classification

Function
binding calcium ion binding carboxylic ester hydrolase activity catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding lipase activity phospholipase A2 activity phospholipase activity
Process
cellular lipid metabolism lipid catabolism lipid metabolism membrane lipid metabolism metabolism phospholipid metabolism physiological process primary metabolism
Component
extracellular region

Enzyme 12 General Function

Not Available

Enzyme 12 Specific Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Shows an 11-fold preference for phosphatidylglycerol over phosphatidylcholine

Enzyme 12 Pathways

Arachidonic acid metabolism (map00590 )
Phospholipid Synthesis (map00564 )

Enzyme 12 Reactions

phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate

Enzyme 12 Pfam Domain Function

Phospholip_A2_2 (PF05826 )

Enzyme 12 Signals

1-19

Enzyme 12 Transmembrane Regions

Not Available

Enzyme 12 Essentiality

Not Available

Enzyme 12 GenBank ID Protein

7274380

Enzyme 12 UniProtKB/Swiss-Prot ID

Q9NZ20

Enzyme 12 UniProtKB/Swiss-Prot Entry Name

PA2G3_HUMAN Link Image

Enzyme 12 PDB ID

Not Available

Enzyme 12 Cellular Location

Not Available

Enzyme 12 Gene Sequence

>1530 bp

ATGGGGGTTCAGGCAGGGCTGTTTGGGATGCTGGGCTTCCTGGGGGTGGCCCTGGGGGGC
TCCCCTGCCCTCCGCTGGTACAGGACCTCCTGCCACTTGACCAAGGCCGTCCCTGGCAAC
CCACTGGGGTACCTGAGCTTCCTGGCCAAGGATGCTCAGGGACTGGCCCTGATCCATGCC
CGCTGGGATGCGCATAGGAGGCTGCAGGCATGTAGCTGGGAGGATGAGCCGGAGCTCACC
GCAGCCTACGGTGCTCTCTGTGCTCATGAGACTGCCTGGGGCTCCTTCATCCACACCCCC
GGACCCGAGCTGCAGAGAGCACTGGCCACTCTTCAGAGTCAGTGGGAGGCATGCCGAGCG
CTTGAGGAGAGTCCAGCAGGGGCCAGGAAGAAGCGAGCAGCAGGGCAGAGTGGAGTCCCT
GGTGGAGGGCACCAGCGAGAGAAGAGAGGATGGACCATGCCTGGCACACTGTGGTGTGGA
GTTGGAGATTCTGCTGGGAACTCCTCGGAGCTGGGGGTCTTCCAGGGACCTGATCTCTGT
TGCCGGGAACATGACCGCTGCCCACAGAACATCTCACCCTTGCAGTACAACTATGGCATC
CGAAACTACCGATTCCACACCATCTCCCACTGTGACTGTGACACCAGGTTTCAGCAATGC
CTACAGAATCAGCACGACTCCATCTCGGACATCGTGGGCGTGGCCTTCTTCAACGTGCTG
GAGATCCCCTGCTTTGTGCTGGAGGAGCAGGAGGCGTGTGTGGCGTGGTACTGGTGGGGC
GGGTGTAGGATGTACGGCACAGTGCCCCTCGCTCGCCTGCAGCCCAGGACCTTCTACAAT
GCCTCCTGGAGCTCCCGGGCCACCTCCCCAACTCCCAGCTCCCGGAGCCCAGCCCCTCCC
AAGCCTCGACAGAAGCAGCACCTTCGGAAGGGGCCACCACATCAGAAAGGGTCCAAGCGC
CCCAGCAAAGCCAACACCACAGCCCTCCAGGACCCTATGGTCTCTCCCAGGCTTGATGTG
GCCCCCACAGGCCTCCAGGGCCCACAGGGTGGCCTAAAACCTCAGGGTGCCCGCTGGGTC
TGCCGCAGCTTCCGCCGCCACCTGGACCAGTGTGAGCACCAGATTGGGCCCCGGGAAATC
GAGTTCCAGCTGCTCAACAGCGCCCAAGAGCCCCTCTTCCACTGCAACTGCACGCGCCGT
CTGGCACGCTTCCTGAGGCTCCACAGCCCACCCGAGGTTACCAACATGCTTTGGGAGCTG
CTGGGCACAACCTGCTTCAAGCTGGCCCCTCCACTGGACTGTGTGGAAGGCAAAAACTGT
TCCAGAGACCCTAGGGCCATCAGGGTGTCAGCCCGGCACTTGCGGAGGCTTCAGCAGAGG
CGACACCAGCTCCAGGATAAAGGCACAGATGAGAGGCAGCCATGGCCTTCAGAGCCCCTG
AGAGGCCCCATGTCATTCTACAACCAGTGCCTGCAGCTAACCCAGGCAGCCAGGAGACCC
GACAGGCAGCAGAAGTCCTGGAGCCAGTGA

Enzyme 12 GenBank Gene ID

AF220490

Enzyme 12 GeneCard ID

PLA2G3

Enzyme 12 GenAtlas ID

PLA2G3

Enzyme 12 HGNC ID

HGNC:17934 Link Image

Enzyme 12 Chromosome Location

Enzyme 12 Locus

22q11.2-q13.2

Enzyme 12 SNPs

SNPJam Report Link Image

Enzyme 12 General References

Valentin E, Ghomashchi F, Gelb MH, Lazdunski M, Lambeau G: Novel human secreted phospholipase A(2) with homology to the group III bee venom enzyme. J Biol Chem. 2000 Mar 17;275(11):7492-6. [PubMed ]
Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]

Enzyme 12 Metabolite References

Not Available

Enzyme 13 [top]

Enzyme 13 ID

6427

Enzyme 13 Name

Probable phospholipid-transporting ATPase IG

Enzyme 13 Synonyms

ATPase class I type 11C
ATPase IG
ATPase IQ
ATPase class VI type 11C

Enzyme 13 Gene Name

ATP11C

Enzyme 13 Protein Sequence

>Probable phospholipid-transporting ATPase IG

MQMVPSLPPASECAGEEKRVGTRTVFVGNHPVSETEAYIAQRFCDNRIVSSKYTLWNFLP
KNLFEQFRRIANFYFLIIFLVQVTVDTPTSPVTSGLPLFFVITVTAIKQGYEDCLRHRAD
NEVNKSTVYIIENAKRVRKESEKIKVGDVVEVQADETFPCDLILLSSCTTDGTCYVTTAS
LDGESNCKTHYAVRDTIALCTAESIDTLRAAIECEQPQPDLYKFVGRINIYSNSLEAVAR
SLGPENLLLKGATLKNTEKIYGVAVYTGMETKMALNYQGKSQKRSAVEKSINAFLIVYLF
ILLTKAAVCTTLKYVWQSTPYNDEPWYNQKTQKERETLKVLKMFTDFLSFMVLFNFIIPV
SMYVTVEMQKFLGSFFISWDKDFYDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTEN
SMEFIECCIDGHKYKGVTQEVDGLSQTDGTLTYFDKVDKNREELFLRALCLCHTVEIKTN
DAVDGATESAELTYISSSPDEIALVKGAKRYGFTFLGNRNGYMRVENQRKEIEEYELLHT
LNFDAVRRRMSVIVKTQEGDILLFCKGADSAVFPRVQNHEIELTKVHVERNAMDGYRTLC
VAFKEIAPDDYERINRQLIEAKMALQDREEKMEKVFDDIETNMNLIGATAVEDKLQDQAA
ETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHE
LLIEYRKKLLHEFPKSTRSFKKAWTEHQEYGLIIDGSTLSLILNSSQDSSSNNYKSIFLQ
ICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKE
GRQAARNSDYSVPKFKHLKKLLLAHGHLYYVRIAHLVQYFFYKNLCFILPQFLYQFFCGF
SQQPLYDAAYLTMYNICFTSLPILAYSLLEQHINIDTLTSDPRLYMKISGNAMLQLGPFL
YWTFLAAFEGTVFFFGTYFLFQTASLEENGKVYGNWTFGTIVFTVLVFTVTLKLALDTRF
WTWINHFVIWGSLAFYVFFSFFWGGIIWPFLKQQRMYFVFAQMLSSVSTWLAIILLIFIS
LFPEILLIVLKNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNVL

Enzyme 13 Number of Residues

1132

Enzyme 13 Molecular Weight

129479

Enzyme 13 Theoretical pI

6.63

Enzyme 13 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport metabolism physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 13 General Function

Inorganic ion transport and metabolism

Enzyme 13 Specific Function

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)

Enzyme 13 Pathways

Not Available

Enzyme 13 Reactions

ATP + H2O = ADP + phosphate

Enzyme 13 Pfam Domain Function

Hydrolase (PF00702 )

Enzyme 13 Signals

None

Enzyme 13 Transmembrane Regions

67-85 87-107 291-311 347-367 880-900 909-929 956-976 996-1016 1027-1047 1070-1090

Enzyme 13 Essentiality

Not Available

Enzyme 13 GenBank ID Protein

39573513

Enzyme 13 UniProtKB/Swiss-Prot ID

Q8NB49

Enzyme 13 UniProtKB/Swiss-Prot Entry Name

AT11C_HUMAN Link Image

Enzyme 13 PDB ID

Not Available

Enzyme 13 Cellular Location

Not Available

Enzyme 13 Gene Sequence

>3399 bp

ATGCAGATGGTCCCATCTCTCCCTCCAGCCTCTGAGTGTGCTGGAGAAGAGAAACGAGTT
GGCACACGCACAGTGTTTGTTGGCAATCATCCAGTTTCGGAAACAGAAGCTTACATTGCA
CAAAGATTTTGTGATAATAGAATAGTCTCATCTAAGTATACACTTTGGAATTTTCTCCCA
AAGAATCTGTTTGAACAGTTTAGAAGAATTGCAAATTTTTATTTTCTCATAATCTTCCTT
GTACAGGTCACAGTAGACACACCAACTAGCCCAGTTACCAGTGGACTTCCACTTTTCTTT
GTTATAACTGTTACAGCCATCAAGCAGGGATATGAGGATTGGCTGAGACACAGAGCTGAC
AATGAAGTCAACAAAAGCACTGTTTACATTATTGAAAATGCAAAGCGAGTGAGAAAAGAA
AGTGAAAAAATCAAGGTTGGTGATGTAGTAGAAGTACAGGCAGATGAAACCTTTCCCTGT
GATCTTATTCTTCTATCATCTTGCACCACTGATGGAACCTGTTATGTCACTACAGCCAGT
CTTGATGGGGAATCCAATTGCAAGACACATTATGCAGTACGTGATACCATTGCACTGTGT
ACAGCAGAATCCATCGATACCCTCCGAGCAGCAATTGAATGTGAACAGCCTCAACCTGAC
CTCTACAAATTTGTTGGGCGAATCAATATCTACAGTAATAGTCTTGAGGCTGTTGCCAGG
TCTTTGGGACCTGAAAATCTCTTGCTGAAAGGAGCTACGCTAAAAAATACCGAGAAGATA
TATGGAGTTGCTGTTTACACTGGAATGGAAACCAAAATGGCTTTGAACTACCAAGGGAAA
TCTCAGAAACGTTCTGCTGTTGAAAAATCTATTAATGCTTTCCTGATTGTATATTTATTT
ATCTTACTGACCAAAGCTGCAGTATGCACTACTCTAAAGTATGTTTGGCAAAGTACCCCA
TACAATGATGAACCTTGGTATAACCAAAAGACTCAGAAAGAGCGAGAGACCTTGAAGGTT
TTAAAAATGTTCACCGACTTCCTATCATTTATGGTTCTATTCAACTTTATCATTCCTGTC
TCCATGTACGTCACAGTAGAAATGCAGAAATTCTTGGGCTCCTTCTTCATCTCATGGGAT
AAGGACTTTTATGATGAAGAAATTAATGAAGGAGCCCTGGTTAACACATCAGACCTTAAT
GAAGAACTTGGTCAGGTGGATTATGTATTTACAGATAAGACTGGAACACTCACTGAAAAC
AGCATGGAATTCATTGAATGCTGCATAGATGGCCACAAATATAAAGGTGTAACTCAAGAG
GTTGATGGATTATCTCAAACTGATGGAACTTTAACATATTTTGACAAAGTAGATAAGAAT
CGAGAAGAGCTGTTTCTACGTGCCTTGTGTTTATGTCATACTGTAGAAATCAAAACAAAC
GATGCTGTTGATGGAGCTACAGAATCAGCTGAATTAACCTATATCTCCTCTTCACCAGAT
GAAATAGCTTTGGTGAAAGGAGCTAAAAGGTACGGGTTCACATTTTTAGGAAATCGAAAT
GGATATATGAGAGTAGAGAACCAAAGAAAAGAAATAGAAGAATATGAACTTCTTCACACC
TTAAACTTTGATGCTGTCCGGCGACGTATGAGTGTAATTGTGAAGACTCAAGAAGGAGAC
ATACTTCTCTTTTGTAAAGGAGCAGACTCGGCAGTTTTTCCCAGAGTGCAAAATCATGAA
ATTGAGTTAACTAAAGTCCATGTGGAACGTAATGCAATGGATGGGTATCGGACACTCTGT
GTAGCCTTCAAAGAAATTGCTCCAGATGATTATGAAAGAATTAACAGACAGCTCATAGAG
GCAAAAATGGCCTTACAAGACAGAGAAGAAAAAATGGAAAAAGTTTTCGATGATATTGAG
ACAAACATGAATTTAATTGGAGCCACTGCAGTTGAAGACAAGCTACAAGATCAAGCTGCA
GAGACCATTGAAGCTCTGCATGCAGCAGGCCTGAAAGTCTGGGTGCTCACTGGGGACAAG
ATGGAGACAGCTAAATCCACATGCTATGCCTGCCGCCTTTTCCAGACCAACACTGAGCTC
TTAGAACTAACCACAAAAACCATTGAAGAAAGTGAAAGGAAAGAAGATCGATTACATGAA
TTATTGATAGAATATCGCAAGAAATTGCTGCATGAGTTTCCTAAAAGTACTAGAAGCTTT
AAAAAAGCATGGACAGAACATCAGGAATATGGATTAATCATAGATGGCTCCACATTGTCA
CTCATACTAAATTCTAGTCAAGACTCTAGTTCAAACAATTACAAAAGCATTTTCCTACAA
ATATGTATGAAGTGTACTGCAGTGCTCTGCTGTCGGATGGCACCATTACAGAAAGCCCAG
ATTGTCAGAATGGTGAAGAATTTAAAAGGCAGCCCAATAACTCTGTCGATAGGTGATGGT
GCCAATGATGTTAGTATGATCTTGGAATCCCATGTGGGAATAGGTATTAAAGGCAAAGAA
GGTCGCCAAGCAGCTAGGAATAGCGATTATTCTGTTCCAAAGTTTAAACACTTAAAGAAA
CTGCTGTTGGCTCATGGACATCTATATTATGTGAGAATAGCACACCTTGTACAGTACTTC
TTCTATAAGAACCTTTGTTTCATTTTGCCACAGTTTTTGTACCAGTTCTTCTGTGGATTC
TCACAACAGCCACTGTATGATGCTGCTTACCTTACAATGTACAATATCTGCTTCACATCC
TTGCCCATCCTGGCCTATAGTCTACTGGAACAGCACATCAACATTGACACTCTGACCTCA
GATCCCCGATTGTATATGAAAATTTCTGGCAATGCCATGCTACAGTTGGGCCCCTTCTTA
TATTGGACATTTCTGGCTGCCTTTGAAGGGACAGTGTTCTTCTTTGGGACTTACTTTCTT
TTTCAGACTGCATCCCTAGAAGAAAATGGAAAGGTATACGGAAACTGGACTTTTGGAACC
ATTGTTTTTACAGTCTTAGTATTCACTGTAACCCTGAAGCTTGCCTTGGATACCCGATTC
TGGACGTGGATAAATCACTTTGTGATTTGGGGTTCTTTAGCCTTCTATGTATTTTTCTCA
TTCTTCTGGGGAGGAATTATTTGGCCTTTTCTCAAGCAACAGAGAATGTATTTTGTATTT
GCCCAAATGCTGTCTTCTGTATCCACATGGTTGGCTATAATTCTTCTAATATTTATCAGC
CTGTTCCCTGAGATTCTTCTGATAGTATTAAAGAATGTAAGAAGAAGAAGTGCCAGGAGA
AATCTGAGCTGTAGAAGGGCATCTGACTCATTATCCGCCAGACCTTCAGTCAGACCTCTT
CTTTTACGAACATTCTCAGACGAATCTAATGTATTGTAA

Enzyme 13 GenBank Gene ID

AJ580093

Enzyme 13 GeneCard ID

ATP11C

Enzyme 13 GenAtlas ID

ATP11C

Enzyme 13 HGNC ID

HGNC:13554 Link Image

Enzyme 13 Chromosome Location

Enzyme 13 Locus

Xq27.1

Enzyme 13 SNPs

SNPJam Report Link Image

Enzyme 13 General References

Not Available

Enzyme 13 Metabolite References

Not Available

Enzyme 14 [top]

Enzyme 14 ID

6428

Enzyme 14 Name

Probable phospholipid-transporting ATPase IH

Enzyme 14 Synonyms

ATPase class I type 11A
ATPase IS

Enzyme 14 Gene Name

ATP11A

Enzyme 14 Protein Sequence

>Probable phospholipid-transporting ATPase IH

MDCSLVRTLVHRYCAGEENWVDSRTIYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNF
IPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHK
ADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTT
ASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPV
VRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVY
LCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYII
PVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLT
ENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHT
VQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNREN
HIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVER
NAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATA
VEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEE
QSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNY
RELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGI
GVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLY
QFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALL
RWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKL
ALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIV
LLVTISLLPDVLKKVLCRQLWPTATERVQTKSQCLSVEQSTIFMLSQTSSSLSF

Enzyme 14 Number of Residues

1134

Enzyme 14 Molecular Weight

129757

Enzyme 14 Theoretical pI

6.58

Enzyme 14 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport metabolism physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 14 General Function

Inorganic ion transport and metabolism

Enzyme 14 Specific Function

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)

Enzyme 14 Pathways

Not Available

Enzyme 14 Reactions

ATP + H2O = ADP + phosphate

Enzyme 14 Pfam Domain Function

Hydrolase (PF00702 )

Enzyme 14 Signals

None

Enzyme 14 Transmembrane Regions

62-82 89-110 297-318 350-372 882-902 915-934 965-986 1001-1023 1030-1050 1069-1093

Enzyme 14 Essentiality

Not Available

Enzyme 14 GenBank ID Protein

55664449

Enzyme 14 UniProtKB/Swiss-Prot ID

P98196

Enzyme 14 UniProtKB/Swiss-Prot Entry Name

AT11A_HUMAN Link Image

Enzyme 14 PDB ID

Not Available

Enzyme 14 Cellular Location

Not Available

Enzyme 14 Gene Sequence

>414 bp

ATATTTGGAAACTGGACGTTTGGAACGCTGGTATTCACCGTGATGGTGTTCACAGTTACA
CTAAAGCTTGCATTGGACACACACTACTGGACTTGGATCAACCATTTTGTCATCTGGGGG
TCGCTGCTGTTCTACGTTGTCTTTTCGCTTCTCTGGGGAGGAGTGATCTGGCCGTTCCTC
AACTACCAGAGGATGTACTACGTGTTCATCCAGATGCTGTCCAGCGGGCCCGCCTGGCTG
GCCATCGTGCTGCTGGTGACCATCAGCCTCCTTCCCGACGTCCTCAAGAAAGTCCTGTGC
CGGCAGCTGTGGCCAACAGCAACAGAGAGAGTCCAGACTAAGAGCCAGTGCCTTTCTGTC
GAGCAGTCAACCATCTTTATGCTTTCTCAGACTTCCAGCAGCCTGAGTTTCTGA

Enzyme 14 GenBank Gene ID

AL356740

Enzyme 14 GeneCard ID

ATP11A

Enzyme 14 GenAtlas ID

ATP11A

Enzyme 14 HGNC ID

HGNC:13552 Link Image

Enzyme 14 Chromosome Location

Enzyme 14 Locus

13q34

Enzyme 14 SNPs

SNPJam Report Link Image

Enzyme 14 General References

Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed ]

Enzyme 14 Metabolite References

Not Available

Enzyme 15 [top]

Enzyme 15 ID

6465

Enzyme 15 Name

Probable phospholipid-transporting ATPase VA

Enzyme 15 Synonyms

ATPVA
Aminophospholipid translocase VA

Enzyme 15 Gene Name

ATP10A

Enzyme 15 Protein Sequence

>Probable phospholipid-transporting ATPase VA

MEREPAGTEEPGPPGRRRRREGRTRTVRSNLLPPPGAEDPAAGAAKGERRRRRGCAQHLA
DNRLKTTKYTLLSFLPKNLFEQFHRPANVYFVFIALLNFVPAVNAFQPGLALAPVLFILA
ITAFRDLWEDYSRHRSDHKINHLGCLVFSREEKKYVNRFWKEIHVGDFVRLRCNEIFPAD
ILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDL
SRFRGCIIHDNGKKAGLYKENLLLRGCTLRNTDAVVGIVIYAGHETKALLNNSGPRYKRS
KLERQMNCDVLWCVLLLVCMSLFSAVGHGLWIWRYQEKKSLFYVPKSDGSSLSPVTAAVY
SFLTMIIVLQVLIPISLYVSIEIVKACQVYFINQDMQLYDEETDSQLQCRALNITEDLGQ
IQYIFSDKTGTLTENKMVFRRCTVSGVEYSHDANAQRLARYQEADSEEEEVVPRGGSVSQ
RGSIGSHQSVRVVHRTQSTKSHRRTGSRAEAKRASMLSKHTAFSSPMEKDITPDPKLLEK
VSECDKSLAVARHQEHLLAHLSPELSDVFDFFIALTICNTVVVTSPDQPRTKVRVRFELK
SPVKTIEDFLRRFTPSCLTSGCSSIGSLAANKSSHKLGSSFPSTPSSDGMLLRLEERLGQ
PTSAIASNGYSSQADNWASELAQEQESERELRYEAESPDEAALVYAARAYNCVLVERLHD
QVSVELPHLGRLTFELLHTLGFDSVRKRMSVVIRHPLTDEINVYTKGADSVVMDLLQPCS
SVDARGRHQKKIRSKTQNYLNVYAAEGLRTLCIAKRVLSKEEYACWLQSHLEAESSLENS
EELLFQSAIRLETNLHLLGATGIEDRLQDGVPETISKLRQAGLQIWVLTGDKQETAVNIA
YACKLLDHDEEVITLNATSQEACAALLDQCLCYVQSRGLQRAPEKTKGKVSMRFSSLCPP
STSTASGRRPSLVIDGRSLAYALEKNLEDKFLFLAKQCRSVLCCRSTPLQKSMVVKLVRS
KLKAMTLAIGDGANDVSMIQVADVGVGISGQEGMQAVMASDFAVPKFRYLERLLILHGHW
CYSRLANMVLYFFYKNTMFVGLLFWFQFFCGFSASTMIDQWYLIFFNLLFSSLPPLVTGV
LDRDVPANVLLTNPQLYKSGQNMEEYRPRTFWFNMADAAFQSLVCFSIPYLAYYDSNVDL
FTWGTPIVTIALLTFLLHLGIETKTWTWLNWITCGFSVLLFFTVALIYNASCATCYPPSN
PYWTMQALLGDPVFYLTCLMTPVAALLPRLFFRSLQGRVFPTQLQLARQLTRKSPRRCSA
PKETFAQGRLPKDSGTEHSSGRTVKTSVPLSQPSWHTQQPVCSLEASGEPSTVDMSMPVR
EHTLLEGLSAPAPMSSAPGEAVLRSPGGCPEESKVRAASTGRVTPLSSLFSLPTFSLLNW
ISSWSLVSRLGSVLQFSRTEQLADGQAGRGLPVQPHSGRSGLQGPDHRLLIGASSRRSQ

Enzyme 15 Number of Residues

1499

Enzyme 15 Molecular Weight

167690

Enzyme 15 Theoretical pI

8.43

Enzyme 15 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 15 General Function

Inorganic ion transport and metabolism

Enzyme 15 Specific Function

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)

Enzyme 15 Pathways

Not Available

Enzyme 15 Reactions

ATP + H2O = ADP + phosphate

Enzyme 15 Pfam Domain Function

Hydrolase_3 (PF08282 )

Enzyme 15 Signals

None

Enzyme 15 Transmembrane Regions

87-106 111-128 310-332 363-384 1088-1108 1120-1140 1171-1192 1200-1222 1229-1249 1268-1292

Enzyme 15 Essentiality

Not Available

Enzyme 15 GenBank ID Protein

14009443

Enzyme 15 UniProtKB/Swiss-Prot ID

O60312

Enzyme 15 UniProtKB/Swiss-Prot Entry Name

AT10A_HUMAN Link Image

Enzyme 15 PDB ID

Not Available

Enzyme 15 Cellular Location

Not Available

Enzyme 15 Gene Sequence

>4500 bp

ATGGAGCGGGAGCCGGCGGGGACCGAGGAGCCCGGGCCTCCGGGACGGCGGAGGCGCCGA
GAGGGCAGGACGCGCACGGTGCGCTCCAACCTGCTGCCGCCCCCGGGCGCCGAGGACCCT
GCGGCTGGCGCGGCCAAGGGCGAGCGGCGACGGCGGCGCGGGTGTGCCCAGCACCTGGCC
GACAACCGGCTCAAGACTACCAAGTACACGCTGCTGTCCTTCCTGCCCAAGAACCTGTTC
GAGCAGTTCCACCGCCCGGCCAACGTGTACTTTGTCTTCATCGCGCTGCTCAACTTCGTG
CCGGCGGTGAACGCCTTCCAGCCCGGCCTGGCACTGGCGCCGGTGCTCTTCATCCTGGCC
ATCACGGCCTTCAGGGACCTGTGGGAGGACTACAGCCGCCACCGCTCCGACCACAAGATC
AACCACCTGGGCTGCCTGGTCTTCAGCAGGGAAGAAAAGAAATACGTGAACCGATTCTGG
AAAGAAATCCACGTGGGAGACTTTGTGCGTCTTCGCTGCAACGAAATCTTCCCTGCGGAC
ATTCTGCTGCTCTCCTCCAGTGACCCCGACGGGCTATGCCACATCGAGACCGCCAACCTG
GATGGAGAGACCAACCTGAAGCGGCGGCAGGTGGTCCGCGGCTTCTCGGAGCTTGTCTCC
GAATTCAATCCTTTGACGTTCACCAGCGTGATCGAATGCGAGAAGCCAAACAACGACCTG
AGTAGGTTTCGCGGCTGCATCATACATGACAACGGGAAAAAGGCCGGGCTGTATAAAGAA
AACCTGCTGCTGAGGGGCTGCACCCTTAGGAACACGGACGCAGTCGTCGGCATTGTCATC
TACGCAGGACATGAAACCAAGGCTCTGCTGAACAACAGTGGGCCCCGCTACAAGCGCAGC
AAGCTGGAGAGGCAGATGAACTGCGACGTGCTCTGGTGTGTCCTGCTCCTTGTTTGCATG
TCTCTGTTTTCAGCAGTCGGACATGGACTGTGGATATGGCGGTATCAAGAGAAGAAGTCA
TTATTTTATGTCCCCAAGTCTGATGGAAGCTCCTTATCCCCAGTCACAGCTGCAGTTTAC
TCATTTTTAACAATGATAATAGTTCTGCAGGTTTTGATCCCAATTTCCTTATACGTTTCC
ATTGAAATTGTTAAAGCATGCCAAGTGTACTTCATTAACCAGGACATGCAGTTGTATGAC
GAAGAAACAGACTCGCAGCTGCAGTGCCGAGCTCTGAACATCACGGAAGACTTAGGACAG
ATACAGTACATTTTCTCAGATAAAACTGGCACTTTGACAGAGAATAAGATGGTTTTCCGA
AGATGCACTGTGTCTGGTGTAGAATATTCTCATGATGCAAATGCGCAGCGTCTGGCCAGG
TACCAAGAGGCAGACTCGGAGGAGGAGGAGGTGGTGCCCAGAGGGGGCTCGGTGTCCCAG
CGCGGCAGCATCGGCAGCCACCAGAGTGTCCGGGTGGTGCACAGAACCCAGAGCACCAAG
TCCCACCGGCGCACGGGCAGCCGGGCCGAGGCCAAGAGGGCCAGCATGCTGTCCAAGCAC
ACGGCCTTCAGCAGCCCCATGGAGAAGGATATCACGCCCGACCCAAAGCTGCTGGAGAAG
GTGAGTGAGTGTGACAAGAGCCTAGCCGTGGCGAGGCATCAGGAGCACCTGCTGGCCCAC
CTCTCGCCCGAGCTGTCTGACGTCTTTGATTTCTTCATCGCACTCACCATCTGCAACACA
GTCGTCGTCACGTCCCCGGATCAGCCACGAACAAAGGTGAGGGTGAGGTTTGAGCTGAAG
TCCCCGGTGAAGACGATAGAAGACTTCCTGCGGAGGTTCACACCCAGCTGCCTGACCTCA
GGCTGCAGCAGCATCGGGAGCCTGGCCGCCAACAAGTCCAGCCACAAGTTGGGCTCCAGC
TTCCCGTCCACCCCGTCCAGCGACGGCATGCTTCTCAGGCTGGAGGAGAGGCTGGGCCAG
CCCACCTCGGCCATCGCCAGCAACGGCTACAGCAGCCAGGCGGACAACTGGGCCTCGGAG
CTTGCTCAGGAGCAGGAGTCAGAGCGCGAGCTGCGGTACGAGGCGGAGAGCCCGGATGAG
GCCGCACTGGTGTATGCGGCCAGAGCCTACAACTGCGTGCTTGTGGAGCGGCTGCACGAC
CAAGTGTCAGTGGAGCTGCCCCACCTGGGCAGGCTCACCTTCGAGCTCCTGCACACACTG
GGTTTCGATTCCGTCCGCAAGAGGATGTCAGTGGTGATCCGGCACCCGCTTACCGATGAG
ATCAACGTCTACACCAAGGGGGCCGACTCAGTGGTCATGGATCTCCTGCAGCCCTGCTCT
TCAGTTGACGCCAGAGGGAGGCATCAAAAAAAGATTCGGAGCAAAACTCAGAATTACCTC
AACGTGTATGCGGCGGAAGGCCTGCGCACCTTGTGCATCGCCAAGAGAGTTCTGAGTAAA
GAAGAGTATGCCTGCTGGTTGCAAAGCCACCTAGAAGCCGAATCCTCCCTGGAAAACAGC
GAGGAGCTCCTCTTCCAGTCTGCCATTCGCCTGGAGACCAACCTGCACTTGTTAGGTGCC
ACTGGGATTGAAGACCGCCTGCAGGACGGAGTCCCTGAAACTATTTCTAAATTGCGTCAA
GCGGGCCTGCAGATTTGGGTTCTCACTGGTGACAAACAAGAAACAGCTGTCAACATTGCA
TATGCCTGCAAACTGCTGGACCACGACGAGGAGGTCATCACCCTGAATGCCACCTCCCAG
GAGGCGTGTGCAGCCCTGCTAGACCAGTGCCTATGCTACGTGCAGTCCAGAGGCCTCCAG
AGAGCCCCTGAGAAGACCAAGGGCAAAGTGAGCATGAGGTTCTCCTCTCTCTGCCCACCC
TCCACGTCCACTGCCTCTGGCCGCAGACCCAGCCTCGTGATCGATGGGAGAAGCCTGGCC
TACGCTCTCGAGAAAAACCTGGAGGACAAATTCCTCTTCCTTGCCAAGCAGTGCCGCTCC
GTCCTCTGCTGTCGGTCGACGCCTCTGCAGAAGAGCATGGTGGTGAAGCTGGTGCGGAGC
AAGCTCAAGGCCATGACCCTGGCCATAGGTGATGGAGCCAATGATGTCAGCATGATCCAG
GTGGCAGATGTGGGTGTGGGAATCTCCGGCCAGGAGGGTATGCAGGCAGTGATGGCCAGC
GACTTTGCAGTGCCGAAATTCCGATACCTGGAGAGGCTCTTGATTCTTCACGGGCATTGG
TGCTACTCCCGACTTGCCAACATGGTGCTGTACTTCTTCTACAAAAACACAATGTTCGTG
GGCCTCCTGTTTTGGTTCCAGTTTTTCTGTGGCTTCTCTGCATCTACCATGATTGACCAG
TGGTATCTAATCTTCTTTAATCTGCTCTTCTCGTCACTTCCCCCGCTCGTGACTGGGGTG
CTGGACAGGGATGTGCCAGCCAATGTGCTGCTGACCAACCCGCAGCTCTACAAGAGTGGC
CAGAACATGGAGGAATACCGGCCACGAACGTTCTGGTTTAACATGGCCGACGCCGCCTTC
CAGAGCCTGGTTTGCTTTTCCATTCCTTACCTGGCCTACTATGACTCGAACGTGGACCTG
TTTACCTGGGGGACCCCTATTGTGACAATCGCGCTGCTCACTTTCCTGCTCCACCTGGGC
ATTGAAACCAAAACCTGGACCTGGCTCAACTGGATAACGTGTGGCTTCAGTGTCCTTTTG
TTTTTCACCGTGGCTTTGATTTACAATGCGTCTTGTGCCACGTGCTATCCTCCGTCCAAC
CCTTACTGGACTATGCAAGCCTTACTGGGTGACCCAGTGTTTTACTTGACTTGCCTGATG
ACGCCTGTCGCTGCACTGCTGCCCAGATTGTTTTTCAGATCCCTCCAGGGGAGGGTTTTC
CCCACACAACTTCAGCTGGCACGTCAGTTGACCAGGAAGTCCCCCAGGAGATGCAGTGCT
CCCAAAGAGACCTTTGCTCAGGGACGCCTCCCGAAGGACTCGGGAACCGAGCACTCATCA
GGGAGGACAGTCAAGACCTCTGTGCCCCTGTCCCAGCCTTCTTGGCACACACAGCAGCCG
GTCTGCTCCCTGGAGGCCAGCGGGGAGCCCAGCACAGTGGACATGAGCATGCCAGTGAGG
GAGCACACCCTGCTGGAGGGGCTGAGCGCACCGGCCCCCATGTCCTCTGCGCCAGGGGAG
GCTGTCCTGAGGAGTCCAGGAGGGTGTCCTGAGGAGTCCAAGGTGAGAGCTGCCAGCACC
GGCAGGGTGACCCCCCTGTCTTCCCTCTTCAGCCTGCCTACCTTCAGCTTACTCAACTGG
ATTTCCTCCTGGTCGCTGGTCAGCAGGCTGGGGAGTGTCTTACAGTTCTCCCGGACGGAG
CAGCTTGCAGATGGACAAGCGGGACGTGGACTTCCTGTCCAGCCCCACTCAGGCCGATCA
GGACTTCAAGGGCCAGACCACAGACTACTTATAGGAGCATCTTCAAGGCGGTCACAGTGA

Enzyme 15 GenBank Gene ID

AB051358

Enzyme 15 GeneCard ID

ATP10A

Enzyme 15 GenAtlas ID

ATP10A

Enzyme 15 HGNC ID

HGNC:13542 Link Image

Enzyme 15 Chromosome Location

Enzyme 15 Locus

15q11.2

Enzyme 15 SNPs

SNPJam Report Link Image

Enzyme 15 General References

Meguro M, Kashiwagi A, Mitsuya K, Nakao M, Kondo I, Saitoh S, Oshimura M: A novel maternally expressed gene, ATP10C, encodes a putative aminophospholipid translocase associated with Angelman syndrome. Nat Genet. 2001 May;28(1):19-20. [PubMed ]
Herzing LB, Kim SJ, Cook EH Jr, Ledbetter DH: The human aminophospholipid-transporting ATPase gene ATP10C maps adjacent to UBE3A and exhibits similar imprinted expression. Am J Hum Genet. 2001 Jun;68(6):1501-5. Epub 2001 May 11. [PubMed ]
Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed ]

Enzyme 15 Metabolite References

Not Available

Enzyme 16 [top]

Enzyme 16 ID

6488

Enzyme 16 Name

Probable phospholipid-transporting ATPase IC

Enzyme 16 Synonyms

Familial intrahepatic cholestasis type 1
ATPase class I type 8B member 1

Enzyme 16 Gene Name

ATP8B1

Enzyme 16 Protein Sequence

>Probable phospholipid-transporting ATPase IC

MSTERDSETTFDEDSQPNDEVVPYSDDETEDELDDQGSAVEPEQNRVNREAEENREPFRK
ECTWQVKANDRKYHEQPHFMNTKFLCIKESKYANNAIKTYKYNAFTFIPMNLFEQFKRAA
NLYFLALLILQAVPQISTLAWYTTLVPLLVVLGVTAIKDLVDDVARHKMDKEINNRTCEV
IKDGRFKVAKWKEIQVGDVIRLKKNDFVPADILLLSSSEPNSLCYVETAELDGETNLKFK
MSLEITDQYLQREDTLATFDGFIECEEPNNRLDKFTGTLFWRNTSFPLDADKILLRGCVI
RNTDFCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIFVVLILLSAGLAIGHA
YWEAQVGNSSWYLYDGEDDTPSYRGFLIFWGYIIVLNTMVPISLYVSVEVIRLGQSHFIN
WDLQMYYAEKDTPAKARTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGQIYGDHR
DASQHNHNKIEQVDFSWNTYADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLAVCHTVMVD
RTDGQLNYQAASPDEGALVNAARNFGFAFLARTQNTITISELGTERTYNVLAILDFNSDR
KRMSIIVRTPEGNIKLYCKGADTVIYERLHRMNPTKQETQDALDIFANETLRTLCLCYKE
IEEKEFTEWNKKFMAASVASTNRDEALDKVYEEIEKDLILLGATAIEDKLQDGVPETISK
LAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHARMENQRNRGGVYA
KFAPPVQESFFPPGGNRALIITGSWLNEILLEKKTKRNKILKLKFPRTEEERRMRTQSKR
RLEAKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNM
IKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFA
FTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYTSLPVLLMGLLDQDVSDKLSLRFPGLYI
VGQRDLLFNYKRFFVSLLHGVLTSMILFFIPLGAYLQTVGQDGEAPSDYQSFAVTIASAL
VITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNAL
RQPYIWLTIILTVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWQRRQQVFRR
GVSTRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIVADGTAEYRRTGDS

Enzyme 16 Number of Residues

1251

Enzyme 16 Molecular Weight

143727

Enzyme 16 Theoretical pI

7.16

Enzyme 16 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 16 General Function

Inorganic ion transport and metabolism

Enzyme 16 Specific Function

May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids in the canicular membrane. May have a role in transport of bile acids into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both

Enzyme 16 Pathways

Not Available

Enzyme 16 Reactions

ATP + H2O = ADP + phosphate

Enzyme 16 Pfam Domain Function

Not Available

Enzyme 16 Signals

None

Enzyme 16 Transmembrane Regions

109-130 137-156 341-362 390-411 950-970 983-1002 1033-1054 1069-1091 1098-1118 1139-1163

Enzyme 16 Essentiality

Not Available

Enzyme 16 GenBank ID Protein

3628757

Enzyme 16 UniProtKB/Swiss-Prot ID

O43520

Enzyme 16 UniProtKB/Swiss-Prot Entry Name

AT8B1_HUMAN Link Image

Enzyme 16 PDB ID

Not Available

Enzyme 16 Cellular Location

Not Available

Enzyme 16 Gene Sequence

>3756 bp

ATGAGTACAGAAAGAGACTCAGAAACGACATTTGACGAGGATTCTCAGCCTAATGACGAA
GTGGTTCCCTACAGTGATGATGAAACAGAAGATGAACTTGATGACCAGGGGTCTGCTGTT
GAACCAGAACAAAACCGAGTCAACAGGGAAGCAGAGGAGAACCGGGAGCCATTCAGAAAA
GAATGTACATGGCAAGTCAAAGCAAACGATCGCAAGTACCACGAACAACCTCACTTTATG
AACACAAAATTCTTGTGTATTAAGGAGAGTAAATATGCGAATAATGCAATTAAAACATAC
AAGTACAACGCATTTACCTTTATACCAATGAATCTGTTTGAGCAGTTTAAGAGAGCAGCC
AATTTATATTTCCTGGCTCTTCTTATCTTACAGGCAGTTCCTCAAATCTCTACCCTGGCT
TGGTACACCACACTAGTGCCCCTGCTTGTGGTGCTGGGCGTCACTGCAATCAAAGACCTG
GTGGACGATGTGGCTCGCCATAAAATGGATAAGGAAATCAACAATAGGACGTGTGAAGTC
ATTAAGGATGGCAGGTTCAAAGTTGCTAAGTGGAAAGAAATTCAAGTTGGAGACGTCATT
CGTCTGAAAAAAAATGATTTTGTTCCAGCTGACATTCTCCTGCTGTCTAGCTCTGAGCCT
AACAGCCTCTGCTATGTGGAAACAGCAGAACTGGACGGAGAAACCAATTTAAAATTTAAG
ATGTCACTTGAAATCACAGACCAGTACCTCCAAAGAGAAGATACATTGGCTACATTTGAT
GGTTTTATTGAATGTGAAGAACCCAATAACCGACTAGATAAGTTTACAGGAACACTATTT
TGGAGAAACACAAGTTTTCCTTTGGATGCTGATAAAATTTTGTTACGTGGCTGTGTAATT
AGGAACACCGATTTCTGCCACGGCTTAGTCATTTTTGCAGGTGCTGACACTAAAATAATG
AAGAATAGTGGGAAAACCAGATTTAAAAGAACTAAAATTGATTACTTGATGAACTACATG
GTTTACACGATCTTTGTTGTTCTTATTCTGCTTTCTGCTGGTCTTGCCATCGGCCATGCT
TATTGGGAAGCACAGGTGGGCAATTCCTCTTGGTACCTCTATGATGGAGAAGACGATACA
CCCTCCTACCGTGGATTCCTCATTTTCTGGGGCTATATCATTGTTCTCAACACCATGGTA
CCCATCTCTCTCTATGTCAGCGTGGAAGTGATTCGTCTTGGACAGAGTCACTTCATCAAC
TGGGACCTGCAAATGTACTATGCTGAGAAGGACACACCCGCAAAAGCTAGAACCACCACA
CTCAATGAACAGCTCGGGCAGATCCATTATATCTTCTCTGATAAGACGGGGACACTCACA
CAAAATATCATGACCTTTAAAAAGTGCTGTATCAACGGGCAGATATATGGGGACCATCGG
GATGCCTCTCAACACAACCACAACAAAATAGAGCAAGTTGATTTTAGCTGGAATACATAT
GCTGATGGGAAGCTTGCATTTTATGACCACTATCTTATTGAGCAAATCCAGTCAGGGAAA
GAGCCAGAAGTACGACAGTTCTTCTTCTTGCTCGCAGTTTGCCACACAGTCATGGTGGAT
AGGACTGATGGTCAGCTCAACTACCAGGCAGCCTCTCCCGATGAAGGTGCCCTGGTAAAC
GCTGCCAGGAACTTTGGCTTTGCCTTCCTCGCCAGGACCCAGAACACCATCACCATCAGT
GAACTGGGCACTGAAAGGACTTACAATGTTCTTGCCATTTTGGACTTCAACAGTGACCGG
AAGCGAATGTCTATCATTGTAAGAACCCCAGAAGGCAATATCAAGCTTTACTGTAAAGGT
GCTGACACTGTTATTTATGAACGGTTACATCGAATGAATCCTACTAAGCAAGAAACACAG
GATGCCCTGGATATCTTTGCAAATGAAACTCTTAGAACCCTATGCCTTTGCTACAAGGAA
ATTGAAGAAAAAGAATTTACAGAATGGAATAAAAAGTTTATGGCTGCCAGTGTGGCCTCC
ACCAACCGGGACGAAGCTCTGGATAAAGTATATGAGGAGATTGAAAAAGACTTAATTCTC
CTGGGAGCTACAGCTATTGAAGACAAGCTACAGGATGGAGTTCCAGAAACCATTTCAAAA
CTTGCAAAAGCTGACATTAAGATCTGGGTGCTTACTGGAGACAAAAAGGAAACTGCTGAA
AATATAGGATTTGCTTGTGAACTTCTGACTGAAGACACCACCATCTGCTATGGGGAGGAT
ATTAATTCTCTTCTTCATGCAAGGATGGAAAACCAGAGGAATAGAGGTGGCGTCTACGCA
AAGTTTGCACCTCCTGTGCAGGAATCTTTTTTTCCACCCGGTGGAAACCGTGCCTTAATC
ATCACTGGTTCTTGGTTGAATGAAATTCTTCTCGAGAAAAAGACCAAGAGAAATAAGATT
CTGAAGCTGAAGTTCCCAAGAACAGAAGAAGAAAGACGGATGCGGACCCAAAGTAAAAGG
AGGCTAGAAGCTAAGAAAGAGCAGCGGCAGAAAAACTTTGTGGACCTGGCCTGCGAGTGC
AGCGCAGTCATCTGCTGCCGCGTCACCCCCAAGCAGAAGGCCATGGTGGTGGACCTGGTG
AAGAGGTACAAGAAAGCCATCACGCTGGCCATCGGAGATGGGGCCAATGACGTGAACATG
ATCAAAACTGCCCACATTGGCGTTGGAATAAGTGGACAAGAAGGAATGCAAGCTGTCATG
TCGAGTGACTATTCCTTTGCTCAGTTCCGATATCTGCAGAGGCTACTGCTGGTGCATGGC
CGATGGTCTTACATAAGGATGTGCAAGTTCCTACGATACTTCTTTTACAAAAACTTTGCC
TTTACTTTGGTTCATTTCTGGTACTCCTTCTTCAATGGCTACTCTGCGCAGACTGCATAC
GAGGATTGGTTCATCACCCTCTACAACGTGCTGTACACCAGCCTGCCCGTGCTCCTCATG
GGGCTGCTCGACCAGGATGTGAGTGACAAACTGAGCCTCCGATTCCCTGGGTTATACATA
GTGGGACAAAGAGACTTACTATTCAACTATAAGAGATTCTTTGTAAGCTTGTTGCATGGG
GTCCTAACATCGATGATCCTCTTCTTCATACCTCTTGGAGCTTATCTGCAAACCGTAGGG
CAGGATGGAGAGGCACCTTCCGACTACCAGTCTTTTGCCGTCACCATTGCCTCTGCTCTT
GTAATAACAGTCAATTTCCAGATTGGCTTGGATACTTCTTATTGGACTTTTGTGAATGCT
TTTTCAATTTTTGGAAGCATTGCACTTTATTTTGGCATCATGTTTGACTTTCATAGTGCT
GGAATACATGTTCTCTTTCCATCTGCATTTCAATTTACAGGCACAGCTTCAAACGCTCTG
AGACAGCCATACATTTGGTTAACTATCATCCTGACTGTTGCTGTGTGCTTACTACCCGTC
GTTGCCATTCGATTCCTGTCAATGACCATCTGGCCATCAGAAAGTGATAAGATCCAGAAG
CATCGCAAGCGGTTGAAGGCGGAGGAGCAGTGGCAGCGACGGCAGCAGGTGTTCCGCCGG
GGCGTGTCAACGCGGCGCTCGGCCTACGCCTTCTCGCACCAGCGGGGCTACGCGGACCTC
ATCTCCTCCGGGCGCAGCATCCGCAAGAAGCGCTCGCCGCTTGATGCCATCGTGGCGGAT
GGCACCGCGGAGTACAGGCGCACCGGGGACAGCTGA

Enzyme 16 GenBank Gene ID

AF038007

Enzyme 16 GeneCard ID

ATP8B1

Enzyme 16 GenAtlas ID

ATP8B1

Enzyme 16 HGNC ID

HGNC:3706

Enzyme 16 Chromosome Location

Enzyme 16 Locus

18q21-q22|18q21.31

Enzyme 16 SNPs

SNPJam Report Link Image

Enzyme 16 General References

Bull LN, van Eijk MJ, Pawlikowska L, DeYoung JA, Juijn JA, Liao M, Klomp LW, Lomri N, Berger R, Scharschmidt BF, Knisely AS, Houwen RH, Freimer NB: A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis. Nat Genet. 1998 Mar;18(3):219-24. [PubMed ]
Halleck MS, Pradhan D, Blackman C, Berkes C, Williamson P, Schlegel RA: Multiple members of a third subfamily of P-type ATPases identified by genomic sequences and ESTs. Genome Res. 1998 Apr;8(4):354-61. [PubMed ]
Tygstrup N, Steig BA, Juijn JA, Bull LN, Houwen RH: Recurrent familial intrahepatic cholestasis in the Faeroe Islands. Phenotypic heterogeneity but genetic homogeneity. Hepatology. 1999 Feb;29(2):506-8. [PubMed ]
Klomp LW, Bull LN, Knisely AS, van Der Doelen MA, Juijn JA, Berger R, Forget S, Nielsen IM, Eiberg H, Houwen RH: A missense mutation in FIC1 is associated with greenland familial cholestasis. Hepatology. 2000 Dec;32(6):1337-41. [PubMed ]

Enzyme 16 Metabolite References

Not Available

Enzyme 17 [top]

Enzyme 17 ID

6516

Enzyme 17 Name

Probable phospholipid-transporting ATPase IIA

Enzyme 17 Synonyms

ATPase class II type 9A
ATPase IIA

Enzyme 17 Gene Name

ATP9A

Enzyme 17 Protein Sequence

>Probable phospholipid-transporting ATPase IIA

MTDNIPLQPVRQKKRMDSRPRAGCCEWLRCCGGGEARPRTVWLGHPEKRDQRYPRNVINN
QKYNFFTFLPGVLFNQFKYFFNLYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTVIRE
AVEEIRCYVRDKEVNSQVYSRLTARGTVKVKSSNIQVGDLIIVEKNQRVPADMIFLRTSE
KNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFVGTFT
REDSDPPISESLSIENTLWAGTVVASGTVVGVVLYTGRELRSVMNTSNPRSKIGLFDLEV
NCLTKILFGALVVVSLVMVALQHFAGRWYLQIIRFLLLFSNIIPISLRVNLDMGKIVYSW
VIRRDSKIPGTVVRSSTIPEQLGRISYLLTDKTGTLTQNEMIFKRLHLGTVAYGLDSMDE
VQSHIFSIYTQQSQDPPAQKGPTLTTKVRRTMSSRVHEAVKAIALCHNVTPVYESNGVTD
QAEAEKQYEDSCRVYQASSPDEVALVQWTESVGLTLVGRDQSSMQLRTPGDQILNFTILQ
IFPFTYESKRMGIIVRDESTGEITFYMKGADVVMAGIVQYNDWLEEECGNMAREGLRVLV
VAKKSLAEEQYQDFEARYVQAKLSVHDRSLKVATVIESLEMEMELLCLTGVEDQLQADVR
PTLETLRNAGIKVWMLTGDKLETATCTAKNAHLVTRNQDIHVFRLVTNRGEAHLELNAFR
RKHDCALVISGDSLEVCLKYYEYEFMELACQCPAVVCCRCAPTQKAQIVRLLQERTGKLT
CAVGDGGNDVSMIQESDCGVGVEGKEGKQASLAADFSITQFKHLGRLLMVHGRNSYKRSA
ALSQFVIHRSLCISTMQAVFSSVFYFASVPLYQGFLIIGYSTIYTMFPVFSLVLDKDVKS
EVAMLYPELYKDLLKGRPLSYKTFLIWVLISIYQGSTIMYGALLLFESEFVHIVAISFTS
LILTELLMVALTIQTWHWLMTVAELLSLACYIASLVFLHEFIDVYFIATLSFLWKVSVIT
LVSCLPLYVLKYLRRRFSPPSYSKLTS

Enzyme 17 Number of Residues

1047

Enzyme 17 Molecular Weight

118584

Enzyme 17 Theoretical pI

7.81

Enzyme 17 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport metabolism physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 17 General Function

Inorganic ion transport and metabolism

Enzyme 17 Specific Function

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)

Enzyme 17 Pathways

Not Available

Enzyme 17 Reactions

ATP + H2O = ADP + phosphate

Enzyme 17 Pfam Domain Function

Hydrolase (PF00702 )

Enzyme 17 Signals

None

Enzyme 17 Transmembrane Regions

70-91 97-119 304-325 333-354 842-862 875-893 924-942 950-972 979-999 1007-1030

Enzyme 17 Essentiality

Not Available

Enzyme 17 GenBank ID Protein

56205769

Enzyme 17 UniProtKB/Swiss-Prot ID

O75110

Enzyme 17 UniProtKB/Swiss-Prot Entry Name

ATP9A_HUMAN Link Image

Enzyme 17 PDB ID

Not Available

Enzyme 17 Cellular Location

Not Available

Enzyme 17 Gene Sequence

>68 bp

ATGACGGACAACATCCCGCTGCAGCCGGTGCGCCAGAAGAAGCGGATGGACAGCAGGCCC
CGCGCCGG

Enzyme 17 GenBank Gene ID

AL353799

Enzyme 17 GeneCard ID

ATP9A

Enzyme 17 GenAtlas ID

ATP9A

Enzyme 17 HGNC ID

HGNC:13540 Link Image

Enzyme 17 Chromosome Location

Enzyme 17 Locus

20q13.2

Enzyme 17 SNPs

SNPJam Report Link Image

Enzyme 17 General References

Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [PubMed ]

Enzyme 17 Metabolite References

Not Available

Enzyme 18 [top]

Enzyme 18 ID

6535

Enzyme 18 Name

Probable phospholipid-transporting ATPase VD

Enzyme 18 Synonyms

ATPVD

Enzyme 18 Gene Name

ATP10D

Enzyme 18 Protein Sequence

>Probable phospholipid-transporting ATPase VD

MTEALQWARYHWRRLIRGATRDDDSGPYNYSSLLACGRKSSQTPKLSGRHRIVVPHIQPF
KDEYEKFSGAYVNNRIRTTKYTLLNFVPRNLFEQFHRAANLYFLFLVVLNWVPLVEAFQK
EITMLPLVVVLTIIAIKDGLEGYRKYKIDKQINNLITKVYSRKEKKYIDRCWKDVTVGDF
IRLSCNEVIPADMVLLFSTDPDGICHIETSGLDGESNLKQRQVVRGYAEQDSEVDPEKFS
SRIECESPNNDLSRFRGFLEHSNKERVGLSKENLLLRGCTIRNTEAVVGIVVYAGHETKA
MLNNSGPRYKRSKLERRANTDVLWCVMLLVIMCLTGAVGHGIWLSRYEKMHFFNVPEPDG
HIISPLLAGFYMFWTMIILLQVLIPISLYVSIEIVKLGQIYFIQSDVDFYNEKMDSIVQC
RALNIAEDLGQIQYLFSDKTGTLTENKMVFRRCSVAGFDYCHEENARRLESYQEAVSEDE
DFIDTVSGSLSNMAKPRAPSCRTVHNGPLGNKPSNHLAGSSFTLGSGEGASEVPHSRQAA
FSSPIETDVVPDTRLLDKFSQITPRLFMPLDETIQNPPMETLYIIDFFIALAICNTVVVS
APNQPRQKIRHPSLGGLPIKSLEEIKSLFQRWSVRRSSSPSLNSGKEPSSGVPNAFVSRL
PLFSRMKPASPVEEEVSQVCESPQCSSSSACCTETEKQHGDAGLLNGKAESLPGQPLACN
LCYEAESPDEAALVYAARAYQCTLRSRTPEQVMVDFAALGPLTFQLLHILPFDSVRKRMS
VVVRHPLSNQVVVYTKGADSVIMELLSVASPDGASLEKQQMIVREKTQKHLDDYAKQGLR
TLCIAKKVMSDTEYAEWLRNHFLAETSIDNREELLLESAMRLENKLTLLGATGIEDRLQE
GVPESIEALHKAGIKIWMLTGDKQETAVNIAYACKLLEPDDKLFILNTQSKDACGMLMST
ILKELQKKTQALPEQVSLSEDLLQPPVPRDSGLRAGLIITGRTLEFALQESLQKQFLELT
SWCQAVVCCRATPLQKSEVVKLVRSHLQVMTLAIGDGANDVSMIQVADIGIGVSGQEGMQ
AVMASDFAVYQFKHLSKLLLVHGHWCYTRLSNMILYFFYKNVAYVNLLFWYQFFCGFSGT
SMTDYWVLIFFNLLFTSAPPVIYGVLEKDVSAETLMQLPELYRSGQKSEAYLPHTFWITL
LDAFYQSLVCFFVPYFTYQGSDTDIFAFGNPLNTAALFIVLLHLVIESKSLTWIHLLVII
GSILSYFLFAIVFGAMCVTCNPPSNPYWIMQEHMLDPVFYLVCILTTSIALLPRFVYRVL
QGSLFPSPILRAKHFDRLTPEERTKALKKWRGAGKMNQVTSKYANQSAGKSGRRPMPGPS
AVFAMKSASSCAIEQGNLSLCETALDQGYSETKAFEMAGPSKGKES

Enzyme 18 Number of Residues

1426

Enzyme 18 Molecular Weight

160322

Enzyme 18 Theoretical pI

7.23

Enzyme 18 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 18 General Function

Inorganic ion transport and metabolism

Enzyme 18 Specific Function

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)

Enzyme 18 Pathways

Not Available

Enzyme 18 Reactions

ATP + H2O = ADP + phosphate

Enzyme 18 Pfam Domain Function

Hydrolase_3 (PF08282 )

Enzyme 18 Signals

None

Enzyme 18 Transmembrane Regions

98-118 122-142 322-342 366-386 1114-1134 1146-1166 1196-1216 1225-1245 1253-1273 1293-1313

Enzyme 18 Essentiality

Not Available

Enzyme 18 GenBank ID Protein

28193030

Enzyme 18 UniProtKB/Swiss-Prot ID

Q9P241

Enzyme 18 UniProtKB/Swiss-Prot Entry Name

AT10D_HUMAN Link Image

Enzyme 18 PDB ID

Not Available

Enzyme 18 Cellular Location

Not Available

Enzyme 18 Gene Sequence

>4281 bp

ATGACTGAGGCTCTCCAATGGGCCAGATATCACTGGCGACGGCTGATCAGAGGTGCAACC
AGGGATGATGATTCAGGGCCATACAACTATTCCTCGTTGCTCGCCTGTGGGCGCAAGTCC
TCTCAGACCCCTAAACTGTCAGGAAGGCACCGGATTGTTGTTCCCCACATCCAGCCCTTC
AAGGATGAGTATGAGAAGTTCTCCGGAGCCTATGTGAACAATCGAATACGAACAACAAAG
TACACACTTCTGAATTTTGTGCCAAGAAATTTATTTGAACAATTTCACAGAGCTGCCAAT
TTATATTTCCTGTTCCTAGTTGTCCTGAACTGGGTACCTTTGGTAGAAGCCTTCCAAAAG
GAAATCACCATGTTGCCTCTGGTGGTGGTCCTTACAATTATCGCAATTAAAGATGGCCTG
GAAGGTTATCGGAAATACAAAATTGACAAACAGATCAATAATTTAATAACTAAAGTTTAT
AGTAGGAAAGAGAAAAAATACATTGACCGATGCTGGAAAGACGTTACTGTTGGGGACTTT
ATTCGCCTCTCCTGCAACGAGGTCATCCCTGCAGACATGGTACTACTCTTTTCCACTGAT
CCAGATGGAATCTGTCACATTGAGACTTCTGGTCTTGATGGAGAGAGCAATTTAAAACAG
AGGCAGGTGGTTCGGGGATATGCAGAACAGGACTCTGAAGTTGATCCTGAGAAGTTTTCC
AGTAGGATAGAATGTGAAAGCCCAAACAATGACCTCAGCAGATTCCGAGGCTTCCTAGAA
CATTCCAACAAAGAACGCGTGGGTCTCAGTAAAGAAAATTTGTTGCTTAGAGGATGCACC
ATTAGAAACACAGAGGCTGTTGTGGGCATTGTGGTTTATGCAGGCCATGAAACCAAAGCA
ATGCTGAACAACAGTGGGCCACGGTATAAGCGCAGCAAATTAGAAAGAAGAGCAAACACA
GATGTCCTCTGGTGTGTCATGCTTCTGGTCATAATGTGCTTAACTGGCGCAGTAGGTCAT
GGAATCTGGCTGAGCAGGTATGAAAAGATGCATTTTTTCAATGTTCCCGAGCCTGATGGA
CATATCATATCACCACTGTTGGCAGGATTTTATATGTTTTGGACCATGATCATTTTGTTA
CAGGTCTTGATTCCTATTTCTCTCTATGTTTCCATCGAAATTGTGAAGCTTGGACAAATA
TATTTCATTCAAAGTGATGTGGATTTCTACAATGAAAAAATGGATTCTATTGTTCAGTGC
CGAGCCCTGAACATCGCCGAGGATCTGGGACAGATTCAGTACCTCTTTTCCGATAAGACA
GGAACCCTCACTGAGAATAAGATGGTTTTTCGAAGATGTAGTGTGGCAGGATTTGATTAC
TGCCATGAAGAAAATGCCAGGAGGTTGGAGTCCTATCAGGAAGCTGTCTCTGAAGATGAA
GATTTTATAGACACAGTCAGTGGTTCCCTCAGCAATATGGCAAAACCGAGAGCCCCCAGC
TGCAGGACAGTTCATAATGGGCCTTTGGGAAATAAGCCCTCAAATCATCTTGCTGGGAGC
TCTTTTACTCTAGGAAGTGGAGAAGGAGCCAGTGAAGTGCCTCATTCCAGACAGGCTGCT
TTCAGTAGCCCCATTGAAACAGACGTGGTACCAGACACCAGGCTTTTAGACAAATTTAGT
CAGATTACACCTCGGCTCTTTATGCCACTAGATGAGACCATCCAAAATCCACCAATGGAA
ACTTTGTACATTATCGACTTTTTCATTGCATTGGCAATTTGCAACACAGTAGTGGTTTCT
GCTCCTAACCAACCCCGACAAAAGATCAGACACCCTTCACTGGGGGGGTTGCCCATTAAG
TCTTTGGAAGAGATTAAAAGTCTTTTCCAGAGATGGTCTGTCCGAAGATCAAGTTCTCCA
TCGCTTAACAGTGGGAAAGAGCCATCTTCTGGAGTTCCAAACGCCTTTGTGAGCAGACTC
CCTCTCTTTAGTCGAATGAAACCAGCTTCACCTGTGGAGGAAGAGGTCTCCCAGGTGTGT
GAGAGCCCCCAGTGCTCCAGTAGCTCAGCTTGCTGCACAGAAACAGAGAAACAACACGGT
GATGCAGGCCTCCTGAATGGCAAGGCAGAGTCCCTCCCTGGACAGCCATTGGCCTGCAAC
CTGTGTTATGAGGCCGAGAGCCCAGACGAAGCGGCCTTAGTGTATGCCGCCAGGGCTTAC
CAATGCACTTTACGGTCTCGGACACCAGAGCAGGTCATGGTGGACTTTGCTGCTTTGGGA
CCATTAACATTTCAACTCCTACACATCCTGCCCTTTGACTCAGTAAGAAAAAGAATGTCT
GTTGTGGTCCGACACCCTCTTTCCAATCAAGTTGTGGTGTATACGAAAGGCGCTGATTCT
GTGATCATGGAGTTACTGTCGGTGGCTTCCCCAGATGGAGCAAGTCTGGAGAAACAACAG
ATGATAGTAAGGGAGAAAACCCAGAAGCACTTGGATGACTATGCCAAACAAGGCCTTCGT
ACTTTATGTATAGCAAAGAAGGTCATGAGTGACACTGAATATGCAGAGTGGCTGAGGAAT
CATTTTTTAGCTGAAACCAGCATTGACAACAGGGAAGAATTACTACTTGAATCTGCCATG
AGGTTGGAGAACAAACTTACATTACTTGGTGCTACTGGCATTGAAGACCGTCTGCAGGAG
GGAGTCCCTGAATCTATAGAAGCTCTTCACAAAGCGGGCATCAAGATCTGGATGCTGACA
GGGGACAAGCAGGAGACAGCTGTCAACATAGCTTATGCATGCAAACTACTGGAGCCAGAT
GACAAGCTTTTTATCCTCAATACCCAAAGTAAAGATGCCTGTGGGATGCTGATGAGCACA
ATTTTGAAAGAACTTCAGAAGAAAACTCAAGCCCTGCCAGAGCAAGTGTCATTAAGTGAA
GATTTACTTCAGCCTCCTGTCCCCCGGGACTCAGGGTTACGAGCTGGACTCATTATCACT
GGGAGGACCCTGGAGTTTGCCCTGCAAGAAAGTCTGCAAAAGCAGTTCCTGGAACTGACA
TCTTGGTGTCAAGCTGTGGTCTGCTGCCGAGCCACACCGCTGCAGAAAAGTGAAGTGGTG
AAATTGGTCCGCAGCCATCTCCAGGTGATGACCCTTGCTATTGGTGATGGTGCCAATGAT
GTTAGCATGATACAAGTGGCAGACATTGGGATAGGGGTCTCAGGTCAAGAAGGCATGCAG
GCTGTGATGGCCAGTGACTTTGCCGTTTATCAGTTCAAACATCTCAGCAAGCTCCTTCTT
GTCCATGGACACTGGTGTTATACACGGCTTTCCAACATGATTCTCTATTTTTTCTATAAG
AATGTGGCCTATGTGAACCTCCTTTTCTGGTACCAGTTCTTTTGTGGATTTTCAGGGACA
TCCATGACTGATTACTGGGTTTTGATCTTCTTCAACCTCCTCTTCACATCTGCCCCTCCT
GTCATTTATGGTGTTTTGGAGAAAGATGTGTCTGCAGAGACCCTCATGCAACTGCCTGAA
CTTTACAGAAGTGGTCAGAAATCAGAGGCATACTTACCCCATACCTTCTGGATCACCTTA
TTGGATGCTTTTTATCAAAGCCTGGTCTGCTTCTTTGTGCCTTATTTTACCTACCAGGGC
TCAGATACTGACATCTTTGCATTTGGAAACCCCCTGAACACAGCCGCTCTGTTCATCGTT
CTCCTCCATCTGGTCATTGAAAGCAAGAGTTTGACTTGGATTCACTTGCTGGTCATCATT
GGTAGCATCTTGTCTTATTTTTTATTTGCCATAGTTTTTGGAGCCATGTGTGTAACTTGC
AACCCACCATCCAACCCTTACTGGATTATGCAGGAGCACATGCTGGATCCAGTATTCTAC
TTAGTTTGTATCCTCACGACGTCCATTGCTCTTCTGCCCAGGTTTGTATACAGAGTTCTT
CAGGGATCCCTGTTTCCATCTCCAATTCTGAGAGCTAAGCACTTTGACAGACTAACTCCA
GAGGAGAGGACTAAAGCTCTCAAGAAGTGGAGAGGGGCTGGAAAGATGAATCAAGTGACA
TCAAAGTATGCTAACCAATCAGCTGGCAAGTCAGGAAGAAGACCCATGCCTGGCCCTTCT
GCTGTATTTGCAATGAAGTCAGCAAGTTCCTGTGCTATTGAGCAAGGAAACTTATCTCTG
TGTGAGACTGCTTTAGATCAAGGCTACTCTGAAACTAAGGCCTTTGAGATGGCTGGACCC
TCCAAAGGTAAAGAAAGCTAG

Enzyme 18 GenBank Gene ID

AJ441078

Enzyme 18 GeneCard ID

ATP10D

Enzyme 18 GenAtlas ID

ATP10D

Enzyme 18 HGNC ID

HGNC:13549 Link Image

Enzyme 18 Chromosome Location

Enzyme 18 Locus

4p12

Enzyme 18 SNPs

SNPJam Report Link Image

Enzyme 18 General References

Flamant S, Pescher P, Lemercier B, Clement-Ziza M, Kepes F, Fellous M, Milon G, Marchal G, Besmond C: Characterization of a putative type IV aminophospholipid transporter P-type ATPase. Mamm Genome. 2003 Jan;14(1):21-30. [PubMed ]
Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed ]

Enzyme 18 Metabolite References

Not Available

Enzyme 19 [top]

Enzyme 19 ID

6543

Enzyme 19 Name

Probable phospholipid-transporting ATPase IB

Enzyme 19 Synonyms

ATPase class I type 8A member 2
ML-1

Enzyme 19 Gene Name

ATP8A2

Enzyme 19 Protein Sequence

>Probable phospholipid-transporting ATPase IB

MSRATSVGDQLEAPARTIYLNQPHLNKFRDNQISTAKYSVLTFLPRFLYEQIRRAANAFF
LFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNG
MWHTIMWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLS
HTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSLVALGPDQILLRGTQLRNTQ
WVFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSAGALYWNR
SHGEKNWYIKKMDTTSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMY
YIGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELAREP
SSDDFCRMPPPCSDSCDFDDPRLLKNIEDRHPTAPCIQEFLTLLAVCHTVVPEKDGDNII
YQASSPDEAALVKGAKKLGFVFTARTPFSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIV
RTPSGRLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSENEYE
EWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIK
IWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCTDLGNLLGKENDV
ALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIG
DGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCIL
YCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCTQESM
LRFPQLYKITQNGEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLTSGHATDYLFV
GNIVYTYVVVTVCLKAGLETTAWTKFSHLAVWGSMLTWLVFFGIYSTIWPTIPIAPDMRG
QATMVLSSAHFWLGLFLVPTACLIEDVAWRAAKHTCKKTLLEEVQELETKSRVLGKAVLR
DSNGKRLNERDRLIKRLGRKTPPTLFRGSSLQQGVPHGYAFSQEEHGAVSQEEVIRAYDT
TKKKSRKK

Enzyme 19 Number of Residues

1148

Enzyme 19 Molecular Weight

129243

Enzyme 19 Theoretical pI

7.84

Enzyme 19 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 19 General Function

Inorganic ion transport and metabolism

Enzyme 19 Specific Function

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)

Enzyme 19 Pathways

Not Available

Enzyme 19 Reactions

ATP + H2O = ADP + phosphate

Enzyme 19 Pfam Domain Function

E1-E2_ATPase (PF00122 )

Enzyme 19 Signals

None

Enzyme 19 Transmembrane Regions

45-66 72-94 277-298 324-345 838-858 871-890 921-942 957-979 986-1006 1025-1049

Enzyme 19 Essentiality

Not Available

Enzyme 19 GenBank ID Protein

27820152

Enzyme 19 UniProtKB/Swiss-Prot ID

Q9NTI2

Enzyme 19 UniProtKB/Swiss-Prot Entry Name

AT8A2_HUMAN Link Image

Enzyme 19 PDB ID

Not Available

Enzyme 19 Cellular Location

Not Available

Enzyme 19 Gene Sequence

>2985 bp

ATGTCCCGGGCCACGTCTGTTGGAGACCAGCTGGAGGCACCCGCCCGCACCATTTACCTC
AACCAACCGCATCTCAACAAATTCCGCGACAACCAGATCAGTACGGCCAAGTACAGCGTG
TTGACATTTCTACCTCGATTCTTGTATGAGCAGATTAGAAGAGCTGCTAATGCCTTCTTT
CTCTTCATTGCCTTATTACAGCAAATTCCAGATGTATCTCCAACAGGAAGATATACCACC
CTGGTGCCATTGATCATTATTTTAACAATTGCAGGCATCAAAGAGATTGTAGAAGATTTT
AAGCGACACAAGGCAGACAATGCAGTTAACAAAAAGAAAACAATAGTGTTAAGAAATGGT
ATGTGGCATACCATTATGTGGAAAGAGGTGGCAGTGGGAGACATTGTGAAGGTCGTCAAT
GGGCAGTATCTTCCAGCAGATGTGGTCCTGCTGTCATCCAGTGAACCTCAGGCAATGTGT
TATGTTGAAACAGCTAATCTGGATGGGGAGACGAACCTTAAAATACGTCAGGGTTTGAGT
CACACTGCTGACATGCAAACACGTGAAGTTCTGATGAAGTTATCTGGAACTATAGAGTGT
GAAGGGCCCAACCGCCACCTCTATGACTTCACTGGAAACTTGAACTTAGATGGGAAAAGC
CTTGTTGCCCTTGGGCCTGACCAGATCTTATTAAGAGGTACACAGCTTAGAAATACTCAG
TGGGTCTTTGGCATAGTTGTTTATACTGGACACGACACCAAACTCATGCAGAATTCAACC
AAAGCGCCTCTCAAGAGATCAAATGTTGAGAAGGTGACTAACGTGCAGATCCTGGTGTTG
TTTGGCATCCTCTTGGTCATGGCCTTGGTGAGCTCGGCGGGGGCCCTGTACTGGAACAGG
TCTCATGGTGAAAAGAACTGGTACATCAAGAAGATGGACACCACCTCAGATAATTTTGGA
TACAACCTACTGACGTTCATCATCTTATACAACAATCTTATTCCCATCAGTCTGTTGGTG
ACTCTTGAGGTTGTGAAGTATACTCAAGCCCTTTTCATAAACTGGGACACAGATATGTAT
TATATAGGAAATGACACTCCTGCCATGGCCAGGACATCAAACCTTAATGAAGAGCTTGGG
CAGGTGAAATATCTCTTTTCTGACAAGACTGGAACGCTTACATGCAATATCATGAACTTT
AAGAAGTGCAGCATTGCCGGAGTAACCTATGGTCACTTCCCAGAATTGGCAAGAGAGCCG
TCTTCAGATGACTTCTGTCGGATGCCTCCTCCCTGTAGTGATTCCTGTGACTTTGATGAC
CCCAGGCTGTTGAAGAACATTGAGGATCGCCATCCCACAGCCCCTTGCATTCAGGAGTTC
CTCACCCTTCTGGCCGTGTGCCACACGGTTGTTCCTGAGAAGGATGGAGATAACATCATC
TACCAGGCCTCTTCCCCAGATGAAGCTGCTTTGGTGAAAGGAGCTAAAAAGCTGGGCTTT
GTCTTCACAGCCAGAACACCATTCTCAGTCATCATAGAAGCGGTGAGTAACATGCGTGTG
CATTTCAGATCACCTGCTTTTGTGAAGATTGTGTGTGTGAAATGGCATGTCTATTGTAAA
TATGATCAGGCCACAAGGGCAGCCATTACTCAGCACTGCACTGACCTTGGGAATTTGCTG
GGCAAGGAAAATGACGTGGCCCTCATCATCGATGGCCACACCCTGAAGTACGCGCTCTCC
TTCGAAGTCCGGAGGAGTTTCCTGGATTTGGCACTCTCGTGCAAAGCGGTCATATGCTGC
AGAGTGTCTCCTCTGCAGAAGTCTGAGATAGTGGATGTGGTGAAGAAGCGGGTGAAGGCC
ATCACCCTCGCCATCGGAGACGGCGCCAACGATGTCGGGATGATCCAGACAGCCCACGTG
GGTGTGGGAATCAGTGGGAATGAAGGCATGCAGGCCACCAACAACTCGGATTACGCCATC
GCACAGTTTTCCTACTTAGAGAAGCTTCTGTTGGTTCATGGAGCCTGGAGCTACAACCGG
GTGACCAAGTGCATCTTGTACTGCTTCTATAAGAACGTGGTCCTGTATATTATTGAGCTT
TGGTTCGCCTTTGTTAATGGATTTTCTGGGCAGATTTTATTTGAACGTTGGTGCATCGGC
CTGTACAATGTGATTTTCACCGCTTTGCCGCCCTTCACTCTGGGAATCTTTGAGAGGTCT
TGCACTCAGGAGAGCATGCTCAGGTTTCCCCAGCTCTACAAAATCACCCAGAATGGCGAA
GGCTTCAACACAAAGGTTTTCTGGGGTCACTGCATCAACGCCTTGGTCCACTCCCTCATC
CTCTTCTGGTTTCCCATGAAAGCTCTGGAGCATGATACTGTGTTTGACAGTGGTCATGCT
ACCGACTATTTATTTGTTGGAAATATTGTTTACACATATGTTGTTGTTACTGTTTGTCTG
AAAGCTGGTTTGGAGACCACAGCTTGGACTAAATTCAGTCATCTGGCTGTCTGGGGAAGC
ATGCTGACCTGGCTGGTGTTTTTTGGCATCTACTCGACCATCTGGCCCACCATTCCCATT
GCTCCAGATATGAGAGGACAGGCAACTATGGTCCTGAGCTCCGCACACTTCTGGTTGGGA
TTATTTCTGGTTCCTACTGCCTGTTTGATTGAAGATGTGGCATGGAGAGCAGCCAAGCAC
ACCTGCAAAAAGACATTGCTGGAGGAGGTGCAGGAGCTGGAAACCAAGTCTCGAGTCCTG
GGAAAAGCGGTGCTGCGGGATAGCAATGGAAAGAGGCTGAACGAGCGCGACCGCCTGATC
AAGAGGCTGGGCCGGAAGACGCCCCCGACGCTGTTCCGGGGCAGCTCCCTGCAGCAGGGC
GTCCCGCATGGGTATGCTTTTTCTCAAGAAGAACACGGAGCTGTTAGTCAGGAAGAAGTC
ATCCGTGCTTATGACACCACCAAAAAGAAATCCAGGAAGAAATAA

Enzyme 19 GenBank Gene ID

AF236871

Enzyme 19 GeneCard ID

ATP8A2

Enzyme 19 GenAtlas ID

ATP8A2

Enzyme 19 HGNC ID

HGNC:13533 Link Image

Enzyme 19 Chromosome Location

Enzyme 19 Locus

13q12-13

Enzyme 19 SNPs

SNPJam Report Link Image

Enzyme 19 General References

Sun XL, Li D, Fang J, Noyes I, Casto B, Theil K, Shuler C, Milo GE: Changes in levels of normal ML-1 gene transcripts associated with the conversion of human nontumorigenic to tumorigenic phenotypes. Gene Expr. 1999;8(2):129-39. [PubMed ]

Enzyme 19 Metabolite References

Not Available

Enzyme 20 [top]

Enzyme 20 ID

6655

Enzyme 20 Name

Probable phospholipid-transporting ATPase IA

Enzyme 20 Synonyms

Chromaffin granule ATPase II
ATPase class I type 8A member 1

Enzyme 20 Gene Name

ATP8A1

Enzyme 20 Protein Sequence

>Probable phospholipid-transporting ATPase IA

MPTMRRTVSEIRSRAEGYEKTDDVSEKTSLADQEEVRTIFINQPQLTKFCNNHVSTAKYN
IITFLPRFLYSQFRRAANSFFLFIALLQQIPDVSPTGRYTTLVPLLFILAVAAIKEIIED
IKRHKADNAVNKKQTQVLRNGAWEIVHWEKVAVGEIVKVTNGEHLPADLISLSSSEPQAM
CYIETSNLDGETNLKIRQGLPATSDIKDVDSLMRISGRIECESPNRHLYDFVGNIRLDGH
GTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILI
LFCILIAMSLVCSVGSAIWNRRHSGKDWYLNLNYGGASNFGLNFLTFIILFNNLIPISLL
VTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQ
FKKCTIAGVAYGHVPEPEDYGCSPDEWQNSQFGDEKTFSDSSLLENLQNNHPTAPIICEF
LTMMAVCHTAVPEREGDKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEER
YELLNVLEFTSARKRMSVIVRTPSGKLRLYCKGADTVIYDRLAETSKYKEITLKHLEQFA
TEGLRTLCFAVAEISESDFQEWRAVYQRASTSVQNRLLKLEESYELIEKNLQLLGATAIE
DKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCKLLKKNMGMIVINEGSLDGTR
ETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQ
KSEVVEMVKKQVKVVTLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYL
KNLLMIHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMF
TAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPL
KALQYGTAFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVV
FFGIYSSLWPAIPMAPDMSGEAAMLFSSGVFWMGLLFIPVASLLLDVVYKVIKRTAFKTL
VDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQD
ENGIVSQSEVIRAYDTTKQRPDEW

Enzyme 20 Number of Residues

1164

Enzyme 20 Molecular Weight

131371

Enzyme 20 Theoretical pI

6.83

Enzyme 20 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport metabolism physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 20 General Function

Inorganic ion transport and metabolism

Enzyme 20 Specific Function

May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids, mainly in secretory vesicles

Enzyme 20 Pathways

Not Available

Enzyme 20 Reactions

ATP + H2O = ADP + phosphate

Enzyme 20 Pfam Domain Function

E1-E2_ATPase (PF00122 )
Hydrolase (PF00702 )

Enzyme 20 Signals

None

Enzyme 20 Transmembrane Regions

66-86 93-115 298-319 345-366 858-878 891-910 941-962 977-999 1006-1026 1045-1070

Enzyme 20 Essentiality

Not Available

Enzyme 20 GenBank ID Protein

4972583

Enzyme 20 UniProtKB/Swiss-Prot ID

Q9Y2Q0

Enzyme 20 UniProtKB/Swiss-Prot Entry Name

AT8A1_HUMAN Link Image

Enzyme 20 PDB ID

Not Available

Enzyme 20 Cellular Location

Not Available

Enzyme 20 Gene Sequence

>3492 bp

ATGCCCACCATGCGGAGGACCGTGTCGGAGATCCGCTCGCGCGCCGAAGGTTATGAGAAG
ACAGATGATGTTTCAGAGAAGACCTCACTGGCTGACCAGGAGGAAGTAAGGACTATTTTC
ATCAACCAGCCCCAGCTGACAAAATTCTGCAATAACCATGTCAGCACTGCAAAATACAAC
ATAATCACATTCCTTCCAAGATTTCTCTACTCTCAGTTCAGAAGAGCTGCTAATTCATTT
TTTCTCTTTATTGCACTGCTGCAGCAAATACCTGATGTGTCACCAACAGGTCGTTATACA
ACACTGGTTCCTCTCTTATTTATTTTAGCTGTGGCAGCTATCAAAGAGATAATAGAAGAT
ATTAAACGACATAAAGCTGATAATGCAGTGAACAAGAAACAAACGCAAGTTTTGAGAAAT
GGTGCTTGGGAAATTGTCCACTGGGAAAAGGTGGCAGTAGGGGAGATAGTGAAAGTGACC
AATGGGGAACATCTCCCAGCAGATCTCATCAGTCTGTCCTCAAGTGAGCCCCAAGCCATG
TGCTACATTGAAACATCCAACTTAGATGGTGAAACAAACTTGAAAATTAGACAGGGCTTA
CCAGCAACATCAGATATCAAAGACGTTGACAGTTTGATGAGGATTTCTGGCAGAATTGAG
TGTGAAAGTCCAAACAGACATCTCTACGATTTTGTTGGAAACATAAGGCTTGATGGACAT
GGCACCGTTCCACTGGGAGCAGATCAGATTCTTCTTCGAGGAGCTCAGTTGAGAAATACA
CAGTGGGTTCATGGAATAGTTGTCTACACTGGACATGACACCAAGCTGATGCAGAATTCA
ACAAGTCCACCACTTAAGCTCTCAAATGTGGAACGGATTACAAATGTACAAATTTTGATT
TTATTTTGTATCTTAATTGCCATGTCTCTTGTCTGTTCTGTGGGCTCAGCCATTTGGAAT
CGAAGGCATTCTGGAAAAGACTGGTATCTCAATCTAAACTATGGTGGCGCTAGTAATTTT
GGACTGAATTTCTTGACCTTCATCATCCTTTTCAACAATCTCATTCCTATCAGCTTATTG
GTTACATTAGAAGTTGTGAAATTTACCCAGGCATACTTCATAAATTGGGATCTTGACATG
CACTATGAACCCACAGACACTGCTGCTATGGCTCGAACATCTAATCTGAATGAGGAACTT
GGCCAGGTTAAATACATATTTTCTGACAAAACTGGTACTCTGACATGCAATGTAATGCAG
TTTAAGAAGTGCACCATAGCGGGAGTTGCTTATGGCCATGTCCCTGAACCTGAGGATTAT
GGCTGCTCTCCTGATGAATGGCAGAACTCACAGTTTGGAGATGAAAAAACATTTAGTGAT
TCATCATTGCTGGAAAATCTCCAAAATAATCATCCAACTGCACCTATAATATGTGAATTT
CTTACAATGATGGCAGTCTGTCACACAGCAGTGCCAGAGCGAGAAGGTGACAAGATTATT
TATCAAGCAGCATCTCCAGATGAGGGAGCATTGGTCAGAGCAGCCAAGCAATTGAATTTT
GTTTTCACTGGAAGAACACCCGACTCGGTGATTATAGATTCACTGGGGCAGGAAGAAAGA
TATGAATTGCTCAATGTCTTGGAGTTTACCAGTGCTAGGAAAAGAATGTCAGTGATTGTT
CGCACTCCATCTGGAAAGTTACGACTCTACTGCAAAGGAGCTGACACTGTAATTTATGAT
CGACTGGCAGAGACGTCAAAATACAAAGAAATTACCCTAAAACATTTAGAGCAGTTTGCT
ACAGAAGGGTTAAGAACTTTATGTTTTGCTGTGGCTGAGATTTCAGAGAGCGACTTTCAG
GAGTGGCGAGCAGTCTATCAGCGAGCATCTACATCTGTGCAGAACAGGCTACTCAAACTC
GAAGAGAGTTATGAGTTGATTGAAAAGAATCTTCAGCTACTTGGAGCAACAGCCATTGAG
GATAAATTACAAGATCAAGTGCCTGAAACCATAGAAACGCTAATGAAAGCAGACATCAAA
ATCTGGATCCTTACAGGGGACAAGCAAGAAACTGCCATTAACATCGGACACTCCTGCAAA
CTGTTGAAGAAGAACATGGGAATGATTGTTATAAATGAAGGCTCTCTTGATGGAACAAGG
GAAACTCTCAGTCGTCACTGTACTACCCTTGGTGATGCTCTCCGGAAAGAGAATGATTTT
GCTCTTATAATTGATGGGAAAACCCTCAAATATGCCTTAACCTTTGGAGTACGACAGTAT
TTCCTGGACTTAGCTTTGTCATGCAAAGCTGTCATTTGCTGTCGGGTTTCTCCTCTTCAA
AAATCTGAAGTTGTTGAGATGGTTAAGAAACAAGTCAAAGTCGTAACGCTTGCAATCGGT
GATGGAGCAAATGATGTCAGCATGATACAGACAGCGCACGTTGGTGTTGGTATCAGTGGC
AATGAAGGCCTGCAGGCAGCTAATTCCTCTGACTACTCCATAGCTCAGTTCAAATATTTG
AAGAATTTACTGATGATTCATGGTGCCTGGAACTATAACAGAGTCTCCAAGTGCATCTTA
TACTGCTTCTACAAGAATATAGTGCTCTATATTATCGAGATCTGGTTTGCCTTTGTTAAT
GGCTTTTCTGGACAGATCCTCTTTGAAAGATGGTGTATAGGTCTCTATAACGTGATGTTT
ACAGCAATGCCTCCTTTAACTCTTGGAATATTTGAGAGATCATGCAGAAAAGAGAACATG
TTGAAGTACCCTGAATTATACAAAACATCTCAGAATGCCCTGGACTTCAACACCAAGGTT
TTCTGGGTTCATTGTTTAAATGGCCTCTTCCACTCAGTTATTCTGTTTTGGTTTCCACTA
AAAGCCCTTCAGTATGGTACTGCATTTGGAAATGGGAAAACCTCGGATTATCTGCTACTG
GGAAACTTTGTGTACACTTTTGTGGTGATAACTGTGTGTTTGAAAGCTGGATTGGAGACA
TCATATTGGACATGGTTCAGCCACATAGCGATATGGGGGAGCATCGCACTCTGGGTGGTG
TTTTTTGGAATCTACTCATCTCTGTGGCCTGCCATTCCGATGGCCCCTGATATGTCAGGA
GAGGCAGCCATGTTGTTCAGTTCTGGAGTCTTTTGGATGGGCTTGTTATTCATCCCTGTG
GCATCTCTGCTCCTTGATGTGGTGTACAAGGTTATCAAGAGGACTGCTTTTAAAACATTG
GTCGATGAAGTTCAGGAGCTGGAGGCAAAATCTCAAGACCCAGGAGCAGTTGTACTTGGA
AAAAGCCTGACCGAGAGGGCGCAACTGCTCAAGAACGTCTTTAAGAAGAACCACGTGAAC
TTGTACCGCTCTGAATCCTTGCAACAAAATCTGCTCCATGGGTATGCGTTCTCTCAAGAT
GAAAATGGAATCGTTTCACAGTCTGAAGTGATAAGAGCATATGATACCACGAAACAGAGG
CCCGACGAATGG

Enzyme 20 GenBank Gene ID

AF067820

Enzyme 20 GeneCard ID

ATP8A1

Enzyme 20 GenAtlas ID

ATP8A1

Enzyme 20 HGNC ID

HGNC:13531 Link Image

Enzyme 20 Chromosome Location

Enzyme 20 Locus

4p14-p12

Enzyme 20 SNPs

SNPJam Report Link Image

Enzyme 20 General References

Mouro I, Halleck MS, Schlegel RA, Mattei MG, Williamson P, Zachowski A, Devaux P, Cartron JP, Colin Y: Cloning, expression, and chromosomal mapping of a human ATPase II gene, member of the third subfamily of P-type ATPases and orthologous to the presumed bovine and murine aminophospholipid translocase. Biochem Biophys Res Commun. 1999 Apr 13;257(2):333-9. [PubMed ]

Enzyme 20 Metabolite References

Not Available

Enzyme 21 [top]

Enzyme 21 ID

6759

Enzyme 21 Name

Probable phospholipid-transporting ATPase IM

Enzyme 21 Synonyms

ATPase class I type 8B member 4

Enzyme 21 Gene Name

ATP8B4

Enzyme 21 Protein Sequence

>Probable phospholipid-transporting ATPase IM

MFCSEKKLREVERIVKANDREYNEKFQYADNRIHTSKYNILTFLPINLFEQFQRVANAYF
LCLLILQLIPEISSLTWFTTIVPLVLVITMTAVKDATDDYFRHKSDNQVNNRQSEVLINS
KLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRHALS
VTSELGADISRLAGFDGIVVCEVPNNKLDKFMGILSWKDSKHSLNNEKIILRGCILRNTS
WCFGMVIFAGPDTKLMQNSGKTKFKRTSIDRLMNTLVLWIFGFLICLGIILAIGNSIWES
QTGDQFRTFLFWNEGEKSSVFSGFLTFWSYIIILNTVVPISLYVSVEVIRLGHSYFINWD
RKMYYSRKAIPAVARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKRCSINGRIYGEVHDD
LDQKTEITQEKEPVDFSVKSQADREFQFFDHHLMESIKMGDPKVHEFLRLLALCHTVMSE
ENSAGELIYQVQSPDEGALVTAARNFGFIFKSRTPETITIEELGTLVTYQLLAFLDFNNT
RKRMSVIVRNPEGQIKLYSKGADTILFEKLHPSNEVLLSLTSDHLSEFAGEGLRTLAIAY
RDLDDKYFKEWHKMLEDANAATEERDERIAELYEEIERDLMLLGATAVEDKLQEGVIETV
TSLSLANIKIWVLTGDKQETAINIGYACNMLTDDMNDVFVIAGNNAVEVREELRKAKQNL
FGQNRNFSNGHVVCEKKQQLELDSIVEETITGDYALIINGHSLAHALESDVKNDLLELAC
MCKTVICCRVTPLQKAQVVELVKKYRNAVTLAIGDGANDVSMIKSAHIGVGISGQEGLQA
VLASDYSFAQFRYLQRLLLVHGRWSYFRMCKFLCYFFYKNFAFTLVHFWFGFFCGFSAQT
VYDQWFITLFNIVYTSLPVLAMGIFDQDVSDQNSVDCPQLYKPGQLNLLFNKRKFFICVL
HGIYTSLVLFFIPYGAFYNVAGEDGQHIADYQSFAVTMATSLVIVVSVQIALDTSYWTFI
NHVFIWGSIAIYFSILFTMHSNGIFGIFPNQFPFVGNARHSLTQKCIWLVILLTTVASVM
PVVAFRFLKVDLYPTLSDQIRRWQKAQKKARPPSSRRPRTRRSSSRRSGYAFAHQEGYGE
LITSGKNMRAKNPPPTSGLEKTHYNSTSWIENLCKKTTDTVSSFSQDKTVKL

Enzyme 21 Number of Residues

1192

Enzyme 21 Molecular Weight

135942

Enzyme 21 Theoretical pI

6.92

Enzyme 21 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 21 General Function

Inorganic ion transport and metabolism

Enzyme 21 Specific Function

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)

Enzyme 21 Pathways

Not Available

Enzyme 21 Reactions

ATP + H2O = ADP + phosphate

Enzyme 21 Pfam Domain Function

Hydrolase_3 (PF08282 )

Enzyme 21 Signals

None

Enzyme 21 Transmembrane Regions

45-66 73-92 277-298 328-349 872-892 905-924 955-976 991-1013 1020-1040 1061-1085

Enzyme 21 Essentiality

Not Available

Enzyme 21 GenBank ID Protein

18916718

Enzyme 21 UniProtKB/Swiss-Prot ID

Q8TF62

Enzyme 21 UniProtKB/Swiss-Prot Entry Name

AT8B4_HUMAN Link Image

Enzyme 21 PDB ID

Not Available

Enzyme 21 Cellular Location

Not Available

Enzyme 21 Gene Sequence

>3249 bp

GGAAGAAGATTTATCCTGGTCCTGAGAAAAATACTGCAGAATGAAAAATGGATGAATGTC
AAAGTGGGAGACATCATTAAATTAGAAAATAACCAATTTGTTGCTGCTGATTTACTTCTC
CTATCAAGTAGTGAGCCACATGGTCTCTGTTATGTTGAAACTGCTGAGCTTGATGGGGAA
ACGAACCTAAAAGTCCGCCATGCACTATCAGTTACTTCAGAACTTGGAGCAGATATCAGC
AGACTTGCAGGGTTTGATGGGATTGTTGTCTGTGAGGTGCCTAACAACAAGTTAGATAAA
TTCATGGGAATCCTTTCTTGGAAAGACAGCAAGCATTCCCTCAACAATGAGAAGATAATC
CTGAGAGGCTGCATCCTGAGAAATACCAGCTGGTGTTTTGGAATGGTTATTTTTGCAGGT
CCTGACACTAAACTAATGCAGAATAGTGGTAAGACAAAGTTTAAAAGGACAAGCATTGAT
AGATTGATGAATACTCTAGTACTATGGATTTTTGGGTTTCTGATATGCTTGGGAATTATT
CTTGCAATAGGAAATTCAATCTGGGAGAGTCAAACTGGGGACCAATTCAGAACTTTCCTC
TTTTGGAATGAAGGAGAGAAGAGCTCTGTGTTCTCCGGATTCTTAACATTCTGGTCATAT
ATTATTATTCTCAATACAGTTGTACCCATTTCCTTATATGTGAGTGTGGAAGTAATTCGT
CTAGGACACAGTTATTTTATAAACTGGGACCGGAAGATGTATTATTCTCGAAAAGCAATA
CCTGCAGTGGCTCGAACGACCACGCTCAATGAGGAACTGGGGCAGATTGAGTACATTTTC
TCCGACAAAACGGGTACCCTCACTCAAAACATCATGACCTTTAAAAGATGTTCCATTAAT
GGGAGAATCTATGGTGAAGTACATGATGACCTGGATCAGAAGACAGAAATAACTCAGGAA
AAAGAGCCTGTGGATTTCTCAGTCAAATCTCAAGCGGATAGAGAATTTCAGTTCTTTGAC
CACCATCTGATGGAATCCATTAAAATGGGTGATCCCAAAGTTCATGAATTCCTTAGGTTA
CTTGCTCTCTGCCACACTGTAATGTCAGAAGAGAATAGCGCAGGAGAGCTGATTTACCAA
GTTCAGTCACCTGATGAAGGGGCTCTAGTGACTGCCGCTAGAAATTTTGGGTTCATTTTT
AAATCCCGGACCCCAGAGACCATAACAATAGAAGAATTGGGAACACTAGTTACTTATCAA
TTACTTGCCTTTTTGGATTTCAACAACACCAGAAAAAGGATGTCTGTCATAGTTCGAAAC
CCAGAAGGACAGATAAAGCTTTATTCCAAAGGAGCAGATACTATTCTGTTTGAAAAACTT
CATCCTTCCAATGAAGTCCTTTTGTCTTTGACGTCAGACCACCTCAGTGAATTTGCAGGG
GAAGGCCTTCGGACCTTGGCCATCGCATACAGAGACCTGGATGACAAGTACTTTAAAGAG
TGGCATAAGATGCTTGAAGATGCGAATGCTGCCACAGAAGAGAGGGATGAACGAATAGCT
GAGCTATATGAAGAAATTGAAAGAGATTTGATGCTACTAGGTGCCACTGCTGTAGAAGAT
AAGTTACAGGAGGGTGTTATTGAAACAGTTACAAGTTTATCACTAGCCAATATTAAGATC
TGGGTCCTAACAGGAGACAAACAAGAAACTGCCATCAACATCGGTTATGCCTGCAACATG
CTGACTGACGACATGAATGATGTGTTTGTGATAGCAGGGAATAATGCTGTGGAAGTGAGA
GAAGAACTCAGGAAAGCAAAACAAAATTTGTTTGGACAAAACAGAAATTTTTCCAATGGC
CATGTAGTTTGTGAAAAAAAGCAGCAGCTGGAGTTGGATTCTATTGTAGAAGAAACCATA
ACAGGAGATTATGCCTTAATCATAAATGGCCACAGTTTGGCTCATGCCCTAGAAAGTGAT
GTCAAGAATGATCTCCTAGAACTTGCTTGCATGTGTAAGACTGTAATTTGCTGCAGGGTC
ACTCCACTCCAGAAAGCCCAAGTGGTAGAGCTGGTGAAGAAGTACAGAAATGCTGTTACT
TTGGCCATTGGTGATGGAGCCAATGATGTCAGCATGATTAAAAGTGCTCACATTGGTGTT
GGCATCAGCGGCCAGGAAGGATTGCAAGCAGTCTTAGCCAGCGACTATTCATTTGCACAG
TTTAGATATCTCCAAAGGCTTCTCCTTGTTCATGGAAGGTGGTCTTATTTCCGAATGTGC
AAATTCTTATGCTATTTCTTCTATAAGAATTTTGCATTTACACTTGTGCATTTCTGGTTT
GGTTTCTTCTGTGGTTTCTCAGCCCAGACTGTTTATGACCAGTGGTTCATCACCCTTTTT
AACATTGTTTACACATCACTGCCTGTTTTAGCCATGGGGATTTTTGACCAGGATGTGAGT
GACCAGAACAGCGTGGACTGTCCCCAGCTCTACAAACCAGGACAGCTGAATCTGCTTTTT
AACAAGCGTAAATTTTTCATTTGCGTGTTGCATGGAATCTACACCTCATTAGTCCTTTTC
TTCATCCCCTATGGGGCCTTTTACAACGTGGCTGGAGAAGATGGGCAACATATTGCTGAC
TACCAGTCCTTTGCAGTTACCATGGCCACATCTTTGGTCATTGTGGTCAGTGTGCAGATA
GCCTTGGATACCAGTTACTGGACTTTCATTAATCACGTCTTCATCTGGGGGAGCATTGCC
ATTTATTTCTCCATTTTATTTACAATGCACAGTAATGGCATCTTTGGCATCTTCCCAAAC
CAGTTTCCATTTGTTGGTAATGCACGACATTCCCTGACCCAGAAGTGCATCTGGCTTGTA
ATTCTCTTAACAACAGTGGCTTCAGTTATGCCAGTGGTGGCATTCAGATTTTTGAAGGTG
GATTTATACCCAACCCTGAGTGATCAGATCCGCCGGTGGCAGAAGGCTCAAAAGAAGGCA
AGGCCTCCAAGTAGCCGAAGGCCTCGGACCCGCAGGTCAAGCTCAAGAAGGTCTGGATAT
GCTTTTGCTCACCAAGAAGGCTATGGAGAGCTTATCACATCTGGAAAAAATATGCGAGCT
AAAAATCCACCCCCAACATCAGGGCTGGAAAAGACACATTATAATAGCACTAGCTGGATT
GAAAATTTATGTAAGAAAACCACAGACACCGTGAGCAGCTTTAGCCAGGATAAAACAGTG
AAACTGTGA

Enzyme 21 GenBank Gene ID

AB075819

Enzyme 21 GeneCard ID

ATP8B4

Enzyme 21 GenAtlas ID

ATP8B4

Enzyme 21 HGNC ID

HGNC:13536 Link Image

Enzyme 21 Chromosome Location

Enzyme 21 Locus

15q21.2

Enzyme 21 SNPs

SNPJam Report Link Image

Enzyme 21 General References

Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed ]

Enzyme 21 Metabolite References

Not Available

Enzyme 22 [top]

Enzyme 22 ID

6781

Enzyme 22 Name

Probable phospholipid-transporting ATPase IF

Enzyme 22 Synonyms

ATPase class I type 11B
ATPase IR

Enzyme 22 Gene Name

ATP11B

Enzyme 22 Protein Sequence

>Probable phospholipid-transporting ATPase IF

MWRWIRQQLGFDPPHQSDTRTIYVANRFPQNGLYTPQKFIDNRIISSKYTVWNFVPKNLF
EQFRRVANFYFLIIFLVQLMIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHNSDNEVN
GAPVYVVRSGGLVKTRSKNIRVGDIVRIAKDEIFPADLVLLSSDRLDGSCHVTTASLDGE
TNLKTHVAVPETALLQTVANLDTLVAVIECQQPEADLYRFMGRMIITQQMEEIVRPLGPE
SLLLRGARLKNTKEIFGVAVYTGMETKMALNYKSKSQKRSAVEKSMNTFLIIYLVILISE
AVISTILKYTWQAEEKWDEPWYNQKTEHQRNSSKILRFISDFLAFLVLYNFIIPISLYVT
VEMQKFLGSFFIGWDLDLYHEESDQKAQVNTSDLNEELGQVEYVFTDKTGTLTENEMQFR
ECSINGMKYQEINGRLVPEGPTPDSSEGNLSYLSSLSHLNNLSHLTTSSSFRTSPENETE
LIKEHDLFFKAVSLCHTVQISNVQTDCTGDGPWQSNLAPSQLEYYASSPDEKALVEAAAR
IGIVFIGNSEETMEVKTLGKLERYKLLHILEFDSDRRRMSVIVQAPSGEKLLFAKGAESS
ILPKCIGGEIEKTRIHVDEFALKGLRTLCIAYRKFTSKEYEEIDKRIFEARTALQQREEK
LAAVFQFIEKDLILLGATAVEDRLQDKVRETIEALRMAGIKVWVLTGDKHETAVSVSLSC
GHFHRTMNILELINQKSDSECAEQLRQLARRITEDHVIQHGLVVDGTSLSLALREHEKLF
MEVCRNCSAVLCCRMAPLQKAKVIRLIKISPEKPITLAVGDGANDVSMIQEAHVGIGIMG
KEGRQAARNSDYAIARFKFLSKLLFVHGHFYYIRIATLVQYFFYKNVCFITPQFLYQFYC
LFSQQTLYDSVYLTLYNICFTSLPILIYSLLEQHVDPHVLQNKPTLYRDISKNRLLSIKT
FLYWTILGFSHAFIFFFGSYLLIGKDTSLLGNGQMFGNWTFGTLVFTVMVITVTVKMALE
THFWTWINHLVTWGSIIFYFVFSLFYGGILWPFLGSQNMYFVFIQLLSSGSAWFAIILMV
VTCLFLDIIKKVFDRHLHPTSTEKAQLTETNAGIKCLDSMCCFPEGEAACASVGRMLERV
IGRCSPTHISRSWSASDPFYTNDRSILTLSTMDSSTC

Enzyme 22 Number of Residues

1177

Enzyme 22 Molecular Weight

134191

Enzyme 22 Theoretical pI

6.95

Enzyme 22 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport metabolism physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 22 General Function

Inorganic ion transport and metabolism

Enzyme 22 Specific Function

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)

Enzyme 22 Pathways

Not Available

Enzyme 22 Reactions

ATP + H2O = ADP + phosphate

Enzyme 22 Pfam Domain Function

Hydrolase (PF00702 )

Enzyme 22 Signals

None

Enzyme 22 Transmembrane Regions

56-77 83-104 290-311 342-359 877-898 911-930 961-982 998-1020 1026-1047 1066-1090

Enzyme 22 Essentiality

Not Available

Enzyme 22 GenBank ID Protein

6457268

Enzyme 22 UniProtKB/Swiss-Prot ID

Q9Y2G3

Enzyme 22 UniProtKB/Swiss-Prot Entry Name

AT11B_HUMAN Link Image

Enzyme 22 PDB ID

Not Available

Enzyme 22 Cellular Location

Not Available

Enzyme 22 Gene Sequence

>744 bp

ATGTGGCGCTGGATCCGGCAGCAGCTGGGTTTTGACCCACCACATCAGAGTGACACAAGA
ACCATCTACGTAGCCAACAGGTTTCCTCAGAATGGCCTTTACACACCTCAGAAATTTATA
GATAACAGGATCATTTCATCTAAGTACACTGTGTGGAATTTTGTTCCAAAAAATTTATTT
GAACAGTTCAGAAGAGTGGCAAACTTTTATTTTCTTATTATATTTTTGGTTCAGCTTATG
ATTGATACACCTACCAGTCCAGTTACCAGTGGACTTCCATTATTCTTTGTGATAACAGTA
ACTGCCATAAAGCAGGGATATGAAGATTGGTTACGGCATAANTCAGATAATGAAGTAAAT
GGAGCTCCTGTTTATGTTGTTCGAAGTGGTGGCCTTGTAAAAACTAGATCAAAAAACATT
CGGGTGGGTGATATTGTTCGAATAGCCAAAGATGAAATTTTTCCTGCAGACTTGGTGCTT
CTGTCCTCAGATCGACTGGATGGTTCCTGTCACGTTACAACTGCTAGTTTGGACGGAGAA
ACTAACCTGAAGACACATGTGGCAGTTCCAGAAACAGCATTATTACAAACAGTTGCCAAT
TTGGACACTCTAGTAGCTGTAATAGAATGCCAGCAACCAGAAGCAGACTTATACAGATTC
ATGGGACGAATGATCATAACCCAACAAATGGAAGAAATTGTAAGACCTCTGGGGCCGGAG
AGTCTCCTGCTTCGTGGAGCCAGA

Enzyme 22 GenBank Gene ID

AF156548

Enzyme 22 GeneCard ID

ATP11B

Enzyme 22 GenAtlas ID

ATP11B

Enzyme 22 HGNC ID

HGNC:13553 Link Image

Enzyme 22 Chromosome Location

Enzyme 22 Locus

3q27

Enzyme 22 SNPs

SNPJam Report Link Image

Enzyme 22 General References

Halleck MS, Lawler JF JR, Blackshaw S, Gao L, Nagarajan P, Hacker C, Pyle S, Newman JT, Nakanishi Y, Ando H, Weinstock D, Williamson P, Schlegel RA: Differential expression of putative transbilayer amphipath transporters. Physiol Genomics. 1999 Nov 11;1(3):139-50. [PubMed ]
Halleck MS, Schlegel RA, Williamson PL: Reanalysis of ATP11B, a type IV P-type ATPase. J Biol Chem. 2002 Mar 22;277(12):9736-40. Epub 2002 Jan 14. [PubMed ]
Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed ]

Enzyme 22 Metabolite References

Not Available

Enzyme 23 [top]

Enzyme 23 ID

6785

Enzyme 23 Name

Probable phospholipid-transporting ATPase IK

Enzyme 23 Synonyms

ATPase class I type 8B member 3

Enzyme 23 Gene Name

ATP8B3

Enzyme 23 Protein Sequence

>Probable phospholipid-transporting ATPase IK

MGTGPAQTPRSTRAGPEPSPAPPGPGDTGDSDVTQEGSGPAGIRGGETVIRAGMGDSPGR
GAPERRHKAQPGRARKYEWRPEGPTSMGSLGQREDLQDEDRNSAFTWKVQANNRAYNGQF
KEKVILCWQRKKYKTNVIRTAKYNFYSFLPLNLYEQFHRVSNLFFLIIIILQSIPDISTL
PWFSLSTPMVCLLFIRATRDLVDDMGRHKSDRAINNRPCQILMGKSFKQKKWQDLCVGDV
VCLRKDNIVPADMLLLASTEPSSLCYVETVDIDGETNLKFRQALMVTHKELATIKKMASF
QGTVTCEAPNSRMHHFVGCLEWNDKKYSLDIGNLLLRGCRIRNTDTCYGLVIYAGFDTKI
MKNCGKIHLKRTKLDLLMNKLVVVIFISVVLVCLVLAFGFGFSVKEFKDHHYYLSGVHGS
SVAAESFFVFWSFLILLSVTIPMSMFILSEFIYLGNSVFIDWDVQMYYKPQDVPAKARST
SLNDHLGQVEYIFSDKTGTLTQNILTFNKCCISGRVYGPDSEATTRPKENPYLWNKFADG
KLLFHNAALLHLVRTNGDEAVREFWRLLAICHTVMVRESPRERPDQLLYQAASPDEGALV
TAARNFGYVFLSRTQDTVTIMELGEERVYQVLAIMDFNSTRKRMSVLVRKPEGAICLYTK
GADTVIFERLHRRGAMEFATEEALAAFAQETLRTLCLAYREVAEDIYEDWQQRHQEASLL
LQNRAQALQQVYNEMEQDLRLLGATAIEDRLQDGVPETIKCLKKSNIKIWVLTGDKQETA
VNIGFACELLSENMLILEEKEISRILETYWENSNNLLTRESLSQVKLALVINGDFLDKLL
VSLRKEPRALAQNVNMDEAWQELGQSRRDFLYARRLSLLCRRFGLPLAAPPAQDSRARRS
SEVLQERAFVDLASKCQAVICCRVTPKQKALIVALVKKYHQVVTLAIGDGANDINMIKTA
DVGVGLAGQEGMQAVQNSDFVLGQFCFLQRLLLVHGRWSYVRICKFLRYFFYKSMASMMV
QVWFACYNGFTGQPLYEGWFLALFNLLYSTLPVLYIGLFEQDVSAEQSLEKPELYVVGQK
DELFNYWVFVQAIAHGVTTSLVNFFMTLWISRDTAGPASFSDHQSFAVVVALSCLLSITM
EVILIIKYWTALCVATILLSLGFYAIMTTTTQSFWLFRVSPTTFPFLYADLSVMSSPSIL
LVVLLSVSINTFPVLALRVIFPALKELRAKEEKVEEGPSEEIFTMEPLPHVHRESRARRS
SYAFSHREGYANLITQGTILRRGPGVSSDIASESLDPSDEEAASSPKESQ

Enzyme 23 Number of Residues

1310

Enzyme 23 Molecular Weight

148032

Enzyme 23 Theoretical pI

7.80

Enzyme 23 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 23 General Function

Inorganic ion transport and metabolism

Enzyme 23 Specific Function

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)

Enzyme 23 Pathways

Not Available

Enzyme 23 Reactions

ATP + H2O = ADP + phosphate

Enzyme 23 Pfam Domain Function

Hydrolase_3 (PF08282 )

Enzyme 23 Signals

None

Enzyme 23 Transmembrane Regions

150-171 178-197 382-403 431-452 1006-1026 1039-1058 1089-1110 1123-1145 1152-1172 1193-1217

Enzyme 23 Essentiality

Not Available

Enzyme 23 GenBank ID Protein

Not Available

Enzyme 23 UniProtKB/Swiss-Prot ID

O60423

Enzyme 23 UniProtKB/Swiss-Prot Entry Name

AT8B3_HUMAN Link Image

Enzyme 23 PDB ID

Not Available

Enzyme 23 Cellular Location

Not Available

Enzyme 23 Gene Sequence

Not Available

Enzyme 23 GenBank Gene ID

AC004755

Enzyme 23 GeneCard ID

ATP8B3

Enzyme 23 GenAtlas ID

ATP8B3

Enzyme 23 HGNC ID

HGNC:13535 Link Image

Enzyme 23 Chromosome Location

Enzyme 23 Locus

19p13.3

Enzyme 23 SNPs

SNPJam Report Link Image

Enzyme 23 General References

Not Available

Enzyme 23 Metabolite References

Not Available

Enzyme 24 [top]

Enzyme 24 ID

7395

Enzyme 24 Name

Phospholipid scramblase 1

Enzyme 24 Synonyms

PL scramblase 1
Ca(2+-dependent phospholipid scramblase 1
Erythrocyte phospholipid scramblase
MmTRA1b

Enzyme 24 Gene Name

PLSCR1

Enzyme 24 Protein Sequence

>Phospholipid scramblase 1

MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAG
FPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVL
TGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLR
CSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCC
GDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLI
DFMFFESTGSQEQKSGVW

Enzyme 24 Number of Residues

318

Enzyme 24 Molecular Weight

35049

Enzyme 24 Theoretical pI

4.57

Enzyme 24 GO Classification

Not Available

Enzyme 24 General Function

Not Available

Enzyme 24 Specific Function

May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation

Enzyme 24 Pathways

Not Available

Enzyme 24 Reactions

Not Available

Enzyme 24 Pfam Domain Function

Scramblase (PF03803 )

Enzyme 24 Signals

None

Enzyme 24 Transmembrane Regions

289-305

Enzyme 24 Essentiality

Not Available

Enzyme 24 GenBank ID Protein

4092081

Enzyme 24 UniProtKB/Swiss-Prot ID

O15162

Enzyme 24 UniProtKB/Swiss-Prot Entry Name

PLS1_HUMAN Link Image

Enzyme 24 PDB ID

Not Available

Enzyme 24 Cellular Location

Not Available

Enzyme 24 Gene Sequence

>957 bp

ATGGACAAACAAAACTCACAGATGAATGCTTCTCACCCGGAAACAAACTTGCCAGTTGGG
TATCCTCCTCAGTATCCACCGACAGCATTCCAAGGACCTCCAGGATATAGTGGCTACCCT
GGGCCCCAGGTCAGCTACCCACCCCCACCAGCCGGCCATTCAGGTCCTGGCCCAGCTGGC
TTTCCTGTCCCAAATCAGCCAGTGTATAATCAGCCAGTATATAATCAGCCAGTTGGAGCT
GCAGGGGTACCATGGATGCCAGCGCCACAGCCTCCATTAAACTGTCCACCTGGATTAGAA
TATTTAAGTCAGATAGATCAGATACTGATTCATCAGCAAATTGAACTTCTGGAAGTTTTA
ACAGGTTTTGAAACTAATAACAAATATGAAATTAAGAACAGCTTTGGACAGAGGGTTTAC
TTTGCAGCGGAAGATACTGATTGCTGTACCCGAAATTGCTGTGGGCCATCTAGACCTTTT
ACCTTGAGGATTATTGATAATATGGGTCAAGAAGTCATAACTCTGGAGAGACCACTAAGA
TGTAGCAGCTGTTGTTGTCCCTGCTGCCTTCAGGAGATAGAAATCCAAGCTCCTCCTGGT
GTACCAATAGGTTATGTTATTCAGACTTGGCACCCATGTCTACCAAAGTTTACAATTCAA
AATGAGAAAAGAGAGGATGTACTAAAAATAAGTGGTCCATGTGTTGTGTGCAGCTGTTGT
GGAGATGTTGATTTTGAGATTAAATCTCTTGATGAACAGTGTGTGGTTGGCAAAATTTCC
AAGCACTGGACTGGAATTTTGAGAGAGGCATTTACAGACGCTGATAACTTTGGAATCCAG
TTCCCTTTAGACCTTGATGTTAAAATGAAAGCTGTAATGATTGGTGCCTGTTTCCTCATT
GACTTCATGTTTTTTGAAAGCACTGGCAGCCAGGAACAAAAATCAGGAGTGTGGTAG

Enzyme 24 GenBank Gene ID

AF098642

Enzyme 24 GeneCard ID

PLSCR1

Enzyme 24 GenAtlas ID

PLSCR1

Enzyme 24 HGNC ID

HGNC:9092

Enzyme 24 Chromosome Location

Enzyme 24 Locus

3q23

Enzyme 24 SNPs

SNPJam Report Link Image

Enzyme 24 General References

Zhou Q, Zhao J, Stout JG, Luhm RA, Wiedmer T, Sims PJ: Molecular cloning of human plasma membrane phospholipid scramblase. A protein mediating transbilayer movement of plasma membrane phospholipids. J Biol Chem. 1997 Jul 18;272(29):18240-4. [PubMed ]
Kasukabe T, Kobayashi H, Kaneko Y, Okabe-Kado J, Honma Y: Identity of human normal counterpart (MmTRA1b) of mouse leukemogenesis-associated gene (MmTRA1a) product as plasma membrane phospholipid scramblase and chromosome mapping of the human MmTRA1b/phospholipid scramblase gene. Biochem Biophys Res Commun. 1998 Aug 19;249(2):449-55. [PubMed ]
Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed ]
Basse F, Stout JG, Sims PJ, Wiedmer T: Isolation of an erythrocyte membrane protein that mediates Ca2+-dependent transbilayer movement of phospholipid. J Biol Chem. 1996 Jul 19;271(29):17205-10. [PubMed ]
Frasch SC, Henson PM, Kailey JM, Richter DA, Janes MS, Fadok VA, Bratton DL: Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta. J Biol Chem. 2000 Jul 28;275(30):23065-73. [PubMed ]
Sun J, Zhao J, Schwartz MA, Wang JY, Wiedmer T, Sims PJ: c-Abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1. J Biol Chem. 2001 Aug 3;276(31):28984-90. Epub 2001 Jun 4. [PubMed ]
Zhao J, Zhou Q, Wiedmer T, Sims PJ: Palmitoylation of phospholipid scramblase is required for normal function in promoting Ca2+-activated transbilayer movement of membrane phospholipids. Biochemistry. 1998 May 5;37(18):6361-6. [PubMed ]
Zhou Q, Sims PJ, Wiedmer T: Identity of a conserved motif in phospholipid scramblase that is required for Ca2+-accelerated transbilayer movement of membrane phospholipids. Biochemistry. 1998 Feb 24;37(8):2356-60. [PubMed ]

Enzyme 24 Metabolite References

Not Available

Enzyme 25 [top]

Enzyme 25 ID

7740

Enzyme 25 Name

Phosphatidylserine decarboxylase proenzyme

Enzyme 25 Synonyms

Not Available

Enzyme 25 Gene Name

PISD

Enzyme 25 Protein Sequence

>Phosphatidylserine decarboxylase proenzyme

MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPART
MFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLS
RAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPV
CGLHSISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKN
QLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCH
NERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNRE
GVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL

Enzyme 25 Number of Residues

408

Enzyme 25 Molecular Weight

46573

Enzyme 25 Theoretical pI

9.80

Enzyme 25 GO Classification

Function
carbon-carbon lyase activity carboxy-lyase activity catalytic activity lyase activity phosphatidylserine decarboxylase activity
Process
cellular lipid metabolism lipid metabolism membrane lipid metabolism metabolism phospholipid biosynthesis phospholipid metabolism physiological process primary metabolism
Component
—

Enzyme 25 General Function

Lipid transport and metabolism

Enzyme 25 Specific Function

Phosphatidyl-L-serine = phosphatidylethanolamine + CO(2)

Enzyme 25 Pathways

Phospholipid Synthesis (map00564 )
Glycine, Serine and Threonine Metabolism (map00260 )

Enzyme 25 Reactions

phosphatidyl-L-serine = phosphatidylethanolamine + CO2

Enzyme 25 Pfam Domain Function

PS_Dcarbxylase (PF02666 )

Enzyme 25 Signals

None

Enzyme 25 Transmembrane Regions

None

Enzyme 25 Essentiality

Not Available

Enzyme 25 GenBank ID Protein

57997016

Enzyme 25 UniProtKB/Swiss-Prot ID

Q9UG56

Enzyme 25 UniProtKB/Swiss-Prot Entry Name

PISD_HUMAN Link Image

Enzyme 25 PDB ID

Not Available

Enzyme 25 Cellular Location

Not Available

Enzyme 25 Gene Sequence

>1227 bp

ATGGCGACGTCCGTGGGGCACCGATGTCTGGGATTACTGCACGGGGTCGCGCCGTGGCGG
AGCAGCCTCCATCCCTGTGAGATCACTGCCCTGAGCCAATCCCTACAGCCCTTACGGAAG
CTGCCTTTTAGAGCCTTTCGCACAGATGCCAGAAAAATCCACACTGCCCCTGCCCGAACC
ATGTTCCTGCTGCGTCCCCTGCCCATTCTGTTGGTGACAGGCGGCGGGTATGCAGGGTAC
CGGCAGTATGAGAAGTACAGGGAGCGAGAGCTGGAGAAGCTGGGATTGGAGATTCCACCC
AAACTTGCTGGTCACTGGGAGGTGGCTTTGTACAAGTCAGTGCCAACGCGCTTGCTGTCA
CGGGCCTGGGGTCGCCTCAATCAGGTGGAGCTGCCACACTGGCTGCGCAGGCCCGTCTAC
AGCCTGTACATCTGGACGTTTGGGGTGAACATGAAAGAGGCCGCTGTGGAGGACCTGCAT
CACTACCGCAACCTCAGCGAGTTCTTCCGGCGCAAGCTGAAGCCGCAGGCCCGGCCTGTC
TGTGGCCTGCACAGCATTAGCCCATCGGATGGAAGGATCCTCAACTTTGGGCAGGTGAAG
AACTGTGAGGTGGAGCAGGTAAAGGGGGTCACCTACTCCCTGGAGTCGTTCCTGGGCCCG
CGTATGTGCACAGAGGACCTGCCCTTCCCACCAGCCGCGTCGTGTGACTCCTTCAAGAAC
CAGCTGGTCACCCGGGAAGGGAATGAGCTCTATCACTGTGTCATCTACCTGGCCCCTGGG
GACTACCACTGCTTCCACTCCCCCACCGACTGGACTGTGTCCCACCGGCGCCACTTCCCA
GGCTCCCTGATGTCAGTGAACCCTGGCATGGCTCGCTGGATCAAAGAGCTCTTCTGCCAT
AACGAGCGGGTGGTCCTGACGGGGGACTGGAAACATGGCTTCTTCTCACTGACAGCTGTG
GGGGCCACCAACGTGGGCTCCATTCGCATCTACTTTGACCGGGACCTGCACACAAACAGC
CCAAGGCACAGCAAGGGCTCCTACAATGACTTCAGCTTCGTGACGCACACCAATAGAGAG
GGCGTCCCCATGCGTAAGGGCGAGCACCTGGGCGAGTTCAACCTGGGCTCCACCATCGTG
CTCATCTTCGAGGCCCCCAAGGACTTCAATTTCCAGCTGAAAACAGGACAGAAAATCCGC
TTTGGGGAAGCCCTGGGCTCGCTCTAG

Enzyme 25 GenBank Gene ID

AL050371

Enzyme 25 GeneCard ID

PISD

Enzyme 25 GenAtlas ID

PISD

Enzyme 25 HGNC ID

HGNC:8999

Enzyme 25 Chromosome Location

Enzyme 25 Locus

22q12.2

Enzyme 25 SNPs

SNPJam Report Link Image

Enzyme 25 General References

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 ]

Enzyme 25 Metabolite References

Not Available

Enzyme 26 [top]

Enzyme 26 ID

8048

Enzyme 26 Name

Phospholipid transfer protein precursor

Enzyme 26 Synonyms

Lipid transfer protein II

Enzyme 26 Gene Name

PLTP

Enzyme 26 Protein Sequence

>Phospholipid transfer protein precursor

MALFGALFLALLAGAHAEFPGCKIRVTSKALELVKQEGLRFLEQELETITIPDLRGKEGH
FYYNISEVKVTELQLTSSELDFQPQQELMLQITNASLGLRFRRQLLYWFFYDGGYINASA
EGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTFKKVYDFLSTFITSGMRFLL
NQQICPVLYHAGTVLLNSLLDTVPVRSSVDELVGIDYSLMKDPVASTSNLDMDFRGAFFP
LTERNWSLPNRAVEPQLQEEERMVYVAFSEFFFDSAMESYFRAGALQLLLVGDKVPHDLD
MLLRATYFGSIVLLSPAVIDSPLKLELRVLAPPRCTIKPSGTTISVTASVTIALVPPDQP
EVQLSSMTMDARLSAKMALRGKALRTQLDLRRFRIYSNHSALESLALIPLQAPLKTMLQI
GVMPMLNERTWRGVQIPLPEGINFVHEVVTNHAGFLTIGADLHFAKGLREVIEKNRPADV
RASTAPTPSTAAV

Enzyme 26 Number of Residues

493

Enzyme 26 Molecular Weight

54740

Enzyme 26 Theoretical pI

7.01

Enzyme 26 GO Classification

Function
binding lipid binding
Process
—
Component
—

Enzyme 26 General Function

Not Available

Enzyme 26 Specific Function

Converts HDL into larger and smaller particles. May play a key role in extracellular phospholipid transport and modulation of hdl particles

Enzyme 26 Pathways

Not Available

Enzyme 26 Reactions

Not Available

Enzyme 26 Pfam Domain Function

LBP_BPI_CETP (PF01273 )
LBP_BPI_CETP_C (PF02886 )

Enzyme 26 Signals

1-17

Enzyme 26 Transmembrane Regions

Not Available

Enzyme 26 Essentiality

Not Available

Enzyme 26 GenBank ID Protein

468326

Enzyme 26 UniProtKB/Swiss-Prot ID

P55058

Enzyme 26 UniProtKB/Swiss-Prot Entry Name

PLTP_HUMAN Link Image

Enzyme 26 PDB ID

Not Available

Enzyme 26 Cellular Location

Not Available

Enzyme 26 Gene Sequence

>1482 bp

ATGGCCCTCTTCGGGGCCCTCTTCCTAGCGCTGCTGGCAGGCGCACATGCAGAGTTCCCA
GGCTGCAAGATCCGCGTCACCTCCAAGGCGCTGGAGCTGGTGAAGCAGGAGGGGCTGCGC
TTTCTGGAGCAAGAGCTGGAGACTATCACCATTCCGGACCTGCGGGGCAAAGAAGGCCAC
TTCTACTACAACATCTCTGAGGTGAAGGTCACAGAGCTGCAACTGACATCTTCCGAGCTC
GATTTCCAGCCACAGCAGGAGCTGATGCTTCAAATCACCAATGCCTCCTTGGGGCTGCGC
TTCCGGAGACAGCTGCTCTACTGGTTCTTCTATGATGGGGGCTACATCAACGCCTCAGCT
GAGGGTGTGTCCATCCGCACTGGTCTGGAGCTCTCCCGGGATCCCGCTGGACGGATGAAA
GTGTCCAATGTCTCCTGCCAGGCCTCTGTCTCCAGAATGCACGCGGCCTTCGGGGGAACC
TTCAAGAAGGTGTATGATTTTCTCTCCACGTTCATCACCTCAGGGATGCGCTTCCTCCTC
AACCAGCAGATCTGCCCTGTCCTCTACCACGCAGGGACGGTCCTGCTCAACTCCCTCCTG
GACACCGTGCCTGTGCGCAGTTCTGTGGACGAGCTTGTTGGCATTGACTATTCCCTCATG
AAGGATCCTGTGGCTTCCACCAGCAACCTGGACATGGACTTCCGGGGGGCCTTCTTCCCC
CTGACTGAGAGGAACTGGAGCCTCCCCAACCGGGCAGTGGAGCCCCAGCTGCAGGAGGAA
GAGCGGATGGTGTATGTGGCCTTCTCTGAGTTCTTCTTCGACTCTGCCATGGAGAGCTAC
TTCCGGGCGGGGGCCCTGCAGCTGTTGCTGGTGGGGGACAAGGTGCCCCACGACCTGGAC
ATGCTGCTGAGGGCCACCTACTTTGGGAGCATTGTCCTGCTGAGCCCAGCAGTGATTGAC
TCCCCATTGAAGCTGGAGCTGCGGGTCCTGGCCCCACCGCGCTGCACCATCAAGCCCTCT
GGCACCACCATCTCTGTCACTGCTAGCGTCACCATTGCCCTGGTCCCACCAGACCAGCCT
GAGGTCCAGCTGTCCAGCATGACTATGGACGCCCGTCTCAGCGCCAAGATGGCTCTCCGG
GGGAAGGCCCTGCGCACGCAGCTGGACCTGCGCAGGTTCCGAATCTATTCCAACCATTCT
GCACTGGAGTCGCTGGCTCTGATCCCATTACAGGCCCCTCTGAAGACCATGCTGCAGATT
GGGGTGATGCCCATGCTCAATGAGCGGACCTGGCGTGGGGTGCAGATCCCACTACCTGAG
GGCATCAACTTTGTGCATGAGGTGGTGACGAACCATGCGGGATTCCTCACCATCGGGGCT
GATCTCCACTTTGCCAAAGGGCTGCGAGAGGTGATTGAGAAGAACCGGCCTGCTGATGTC
AGGGCGTCCACTGCCCCCACACCGTCCACAGCAGCTGTCTGA

Enzyme 26 GenBank Gene ID

L26232

Enzyme 26 GeneCard ID

PLTP

Enzyme 26 GenAtlas ID

PLTP

Enzyme 26 HGNC ID

HGNC:9093

Enzyme 26 Chromosome Location

Enzyme 26 Locus

20q12-q13.1

Enzyme 26 SNPs

SNPJam Report Link Image

Enzyme 26 General References

Day JR, Albers JJ, Lofton-Day CE, Gilbert TL, Ching AF, Grant FJ, O'Hara PJ, Marcovina SM, Adolphson JL: Complete cDNA encoding human phospholipid transfer protein from human endothelial cells. J Biol Chem. 1994 Mar 25;269(12):9388-91. [PubMed ]
Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
Qu SJ, Fan HZ, Kilinc C, Pownall HJ: Role of cysteine residues in human plasma phospholipid transfer protein. J Protein Chem. 1999 Feb;18(2):193-8. [PubMed ]
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 ]

Enzyme 26 Metabolite References

Not Available

Enzyme 27 [top]

Enzyme 27 ID

8755

Enzyme 27 Name

CDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2

Enzyme 27 Synonyms

Not Available

Enzyme 27 Gene Name

Not Available

Enzyme 27 Protein Sequence

>CDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2

MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGED
GLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKS
KNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACR
CHYEEKTDL

Enzyme 27 Number of Residues

189

Enzyme 27 Molecular Weight

21067

Enzyme 27 Theoretical pI

7.27

Enzyme 27 GO Classification

Function
binding calcium ion binding carboxylic ester hydrolase activity catalytic activity cation binding hydrolase activity hydrolase activity, acting on ester bonds ion binding lipase activity phospholipase A2 activity phospholipase activity
Process
lipid catabolism lipid metabolism metabolism physiological process primary metabolism
Component
extracellular region

Enzyme 27 General Function

Not Available

Enzyme 27 Specific Function

Not Available

Enzyme 27 Pathways

Arachidonic acid metabolism (map00590 )
Phospholipid Synthesis (map00564 )

Enzyme 27 Reactions

phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate

Enzyme 27 Pfam Domain Function

PLA2G12 (PF06951 )

Enzyme 27 Signals

1-22

Enzyme 27 Transmembrane Regions

Not Available

Enzyme 27 Essentiality

Not Available

Enzyme 27 GenBank ID Protein

22761446

Enzyme 27 UniProtKB/Swiss-Prot ID

Q542Y6

Enzyme 27 UniProtKB/Swiss-Prot Entry Name

Q542Y6_HUMAN Link Image

Enzyme 27 PDB ID

Not Available

Enzyme 27 Cellular Location

Not Available

Enzyme 27 Gene Sequence

>570 bp

ATGGCCCTGCTCTCGCGCCCCGCGCTCACCCTCCTGCTCCTCCTCATGGCCGCTGTTGTC
AGGTGCCAGGAGCAGGCCCAGACCACCGACTGGAGAGCCACCCTGAAGACCATCCGGAAC
GGCGTTCATAAGATAGACACGTACCTGAACGCCGCCTTGGACCTCCTAGGAGGCGAGGAC
GGTCTCTGCCAGTATAAATGCAGTGACGGATCTAAGCCTTTCCCACGTTATGGTTATAAA
CCCTCCCCACCGAATGGATGTGGCTCTCCACTGTTTGGTGTTCATCTTAACATTGGTATC
CCTTCCCTGACAAAGTGTTGCAACCAACACGACAGGTGCTATGAGACCTGTGGCAAAAGC
AAGAATGACTGTGATGAAGAATTCCAGTATTGCCTCTCCAAGATCTGCCGAGATGTACAG
AAAACACTAGGACTAACTCAGCATGTTCAGGCATGTGAAACAACAGTGGAGCTCTTGTTT
GACAGTGTTATACATTTAGGTTGTAAACCATATCTGGACAGCCAACGAGCCGCATGCAGG
TGTCATTATGAAGAAAAAACTGATCTTTAA

Enzyme 27 GenBank Gene ID

AK075389

Enzyme 27 GeneCard ID

Not Available

Enzyme 27 GenAtlas ID

Not Available

Enzyme 27 HGNC ID

HGNC:18554 Link Image

Enzyme 27 Chromosome Location

Not Available

Enzyme 27 Locus

Not Available

Enzyme 27 SNPs

Not Available

Enzyme 27 General References

Not Available

Enzyme 27 Metabolite References

Not Available

Enzyme 28 [top]

Enzyme 28 ID

8937

Enzyme 28 Name

Choline/ethanolaminephosphotransferase 1

Enzyme 28 Synonyms

hCEPT1

Enzyme 28 Gene Name

CEPT1

Enzyme 28 Protein Sequence

>Choline/ethanolaminephosphotransferase 1

MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAG
RSLLEPLMQGYWEWLVRRVPSWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYI
ACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPD
WMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIP
VLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLA
AMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLD
QYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH

Enzyme 28 Number of Residues

416

Enzyme 28 Molecular Weight

46554

Enzyme 28 Theoretical pI

Not Available

Enzyme 28 GO Classification

Function
—
Process
cellular lipid metabolism lipid metabolism membrane lipid metabolism metabolism phospholipid biosynthesis phospholipid metabolism physiological process primary metabolism
Component
—

Enzyme 28 General Function

Not Available

Enzyme 28 Specific Function

Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity

Enzyme 28 Pathways

Aminophosphonate metabolism (map00440 )
Ether lipid metabolism (map00565 )
Phospholipid Synthesis (map00564 )

Enzyme 28 Reactions

CDPcholine + diacylglycerol (homo sapiens) --> CMP + H+ + Phosphatidylcholine (homo sapiens)

Enzyme 28 Pfam Domain Function

CDP-OH_P_transf (PF01066 )

Enzyme 28 Signals

None

Enzyme 28 Transmembrane Regions

87-107 115-135 186-206 209-229 239-259 283-303 317-337 365-385

Enzyme 28 Essentiality

Not Available

Enzyme 28 GenBank ID Protein

4584877

Enzyme 28 UniProtKB/Swiss-Prot ID

Q9Y6K0

Enzyme 28 UniProtKB/Swiss-Prot Entry Name

CEPT1_HUMAN Link Image

Enzyme 28 PDB ID

Not Available

Enzyme 28 Cellular Location

Not Available

Enzyme 28 Gene Sequence

Not Available

Enzyme 28 GenBank Gene ID

AF068302

Enzyme 28 GeneCard ID

Not Available

Enzyme 28 GenAtlas ID

CEPT1

Enzyme 28 HGNC ID

HGNC:24289 Link Image

Enzyme 28 Chromosome Location

Not Available

Enzyme 28 Locus

Not Available

Enzyme 28 SNPs

SNPJam Report Link Image

Enzyme 28 General References

Henneberry AL, McMaster CR: Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine. Biochem J. 1999 Apr 15;339 ( Pt 2):291-8. [PubMed ]
Henneberry AL, Wistow G, McMaster CR: Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J Biol Chem. 2000 Sep 22;275(38):29808-15. [PubMed ]

Enzyme 28 Metabolite References

Not Available

Enzyme 29 [top]

Enzyme 29 ID

12911

Enzyme 29 Name

Phospholipase D3

Enzyme 29 Synonyms

PLD 3
Choline phosphatase 3
Phosphatidylcholine-hydrolyzing phospholipase D3
HindIII K4L homolog
Hu-K4

Enzyme 29 Gene Name

PLD3

Enzyme 29 Protein Sequence

>Phospholipase D3

MKPKLMYQELKVPAEEPANELPMNEIEAWKAAEKKARWVLLVLILAVVGFGALMTQLFLW
EYGDLHLFGPNQRPAPCYDPCEAVLVESIPEGLDFPNASTGNPSTSQAWLGLLAGAHSSL
DIASFYWTLTNNDTHTQEPSAQQGEEVLRQLQTLAPKGVNVRIAVSKPSGPQPQADLQAL
LQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCL
ARDLTKIFEAYWFLGQAGSSIPSTWPRFYDTRYNQETPMEICLNGTPALAYLASAPPPLC
PSGRTPDLKALLNVVDNARSFIYVAVMNYLPTLEFSHPHRFWPAIDDGLRRATYERGVKV
RLLISCWGHSEPSMRAFLLSLAALRDNHTHSDIQVKLFVVPADEAQARIPYARVNHNKYM
VTERATYIGTSNWSGNYFTETAGTSLLVTQNGRGGLRSQLEAIFLRDWDSPYSHDLDTSA
DSVGNACRLL

Enzyme 29 Number of Residues

490

Enzyme 29 Molecular Weight

54706

Enzyme 29 Theoretical pI

6.45

Enzyme 29 GO Classification

Function
catalytic activity
Process
metabolism physiological process
Component
—

Enzyme 29 General Function

Not Available

Enzyme 29 Specific Function

A phosphatidylcholine + H(2)O = choline + a phosphatidate

Enzyme 29 Pathways

Ether lipid metabolism (map00565 )
Phospholipid Synthesis (map00564 )
GnRH signaling pathway (map04912 )

Enzyme 29 Reactions

a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310] ALL_REAC R01310
(other) R02051 R07385

Enzyme 29 Pfam Domain Function

PLD_envelope (PF08371 )
PLDc (PF00614 )

Enzyme 29 Signals

None

Enzyme 29 Transmembrane Regions

39-59

Enzyme 29 Essentiality

Not Available

Enzyme 29 GenBank ID Protein

1575347

Enzyme 29 UniProtKB/Swiss-Prot ID

Q8IV08

Enzyme 29 UniProtKB/Swiss-Prot Entry Name

PLD3_HUMAN Link Image

Enzyme 29 PDB ID

Not Available

Enzyme 29 Cellular Location

Not Available

Enzyme 29 Gene Sequence

Not Available

Enzyme 29 GenBank Gene ID

U60644

Enzyme 29 GeneCard ID

Q8IV08

Enzyme 29 GenAtlas ID

PLD3

Enzyme 29 HGNC ID

HGNC:17158 Link Image

Enzyme 29 Chromosome Location

Not Available

Enzyme 29 Locus

Not Available

Enzyme 29 SNPs

SNPJam Report Link Image

Enzyme 29 General References

Not Available

Enzyme 29 Metabolite References

Not Available

Enzyme 30 [top]

Enzyme 30 ID

12912

Enzyme 30 Name

Phospholipase D4

Enzyme 30 Synonyms

PLD 4
Choline phosphatase 4
Phosphatidylcholine-hydrolyzing phospholipase D4

Enzyme 30 Gene Name

PLD4

Enzyme 30 Protein Sequence

>Phospholipase D4

MLKPLWKAAVAPTWPCSMPPRRPWDREAGTLQVLGALAVLWLGSVALICLLWQVPRPPTW
GQVQPKDVPRSWEHGSSPAWEPLEAEARQQRDSCQLVLVESIPQDLPSAAGSPSAQPLGQ
AWLQLLDTAQESVHVASYYWSLTGPDIGVNDSSSQLGEALLQKLQQLLGRNISLAVATSS
PTLARTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQV
KELGAVIYNCSHLAQDLEKTFQTYWVLGVPKAVLPKTWPQNFSSHFNRFQPFHGLFDGVP
TTAYFSASPPALCPQGRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDN
ALRAAAFGKGVRVRLLVGCGLNTDPTMFPYLRSLQALSNPAANVSVDVKVFIVPVGNHSN
IPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQSPGAQPAGATVQEQLRQL
FERDWSSRYAVGLDGQAPGQDCVWQG

Enzyme 30 Number of Residues

506

Enzyme 30 Molecular Weight

55627

Enzyme 30 Theoretical pI

8.46

Enzyme 30 GO Classification

Function
catalytic activity
Process
metabolism physiological process
Component
—

Enzyme 30 General Function

Not Available

Enzyme 30 Specific Function

A phosphatidylcholine + H(2)O = choline + a phosphatidate

Enzyme 30 Pathways

Ether lipid metabolism (map00565 )
Phospholipid Synthesis (map00564 )
GnRH signaling pathway (map04912 )

Enzyme 30 Reactions

a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310] ALL_REAC R01310
(other) R02051 R07385

Enzyme 30 Pfam Domain Function

PLD_envelope (PF08371 )
PLDc (PF00614 )

Enzyme 30 Signals

None

Enzyme 30 Transmembrane Regions

31-51

Enzyme 30 Essentiality

Not Available

Enzyme 30 GenBank ID Protein

37182804

Enzyme 30 UniProtKB/Swiss-Prot ID

Q96BZ4

Enzyme 30 UniProtKB/Swiss-Prot Entry Name

PLD4_HUMAN Link Image

Enzyme 30 PDB ID

Not Available

Enzyme 30 Cellular Location

Not Available

Enzyme 30 Gene Sequence

Not Available

Enzyme 30 GenBank Gene ID

AY358843

Enzyme 30 GeneCard ID

Q96BZ4

Enzyme 30 GenAtlas ID

PLD4

Enzyme 30 HGNC ID

HGNC:23792 Link Image

Enzyme 30 Chromosome Location

Not Available

Enzyme 30 Locus

Not Available

Enzyme 30 SNPs

SNPJam Report Link Image

Enzyme 30 General References

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 ]

Enzyme 30 Metabolite References

Not Available

Enzyme 31 [top]

Enzyme 31 ID

12915

Enzyme 31 Name

Phospholipid scramblase 2

Enzyme 31 Synonyms

PL scramblase 2
Ca(2+-dependent phospholipid scramblase 2

Enzyme 31 Gene Name

PLSCR2

Enzyme 31 Protein Sequence

>Phospholipid scramblase 2

MPAPPPPLNCPPGLEYLSQIDMILIHQQIELLEVLFSFESSNMYEIKNSFGQRIYFAAED
TNFCIRNCCGRSRPFTLRITDNVGREVITLERPLRCNCCCCPCCLQEIEIQAPPGVPVGY
VTQTWHPCLTKFTIKNQKREDVLKISGPCIVCSCIAGVDFEITSLDEQIVVGRISKHWSG
FLREAFTDADNFGIQFPRDLDVKMKAVMIGACFLIDYMFFERTR

Enzyme 31 Number of Residues

224

Enzyme 31 Molecular Weight

25523

Enzyme 31 Theoretical pI

5.34

Enzyme 31 GO Classification

Not Available

Enzyme 31 General Function

Not Available

Enzyme 31 Specific Function

May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system

Enzyme 31 Pathways

Not Available

Enzyme 31 Reactions

Not Available

Enzyme 31 Pfam Domain Function

Scramblase (PF03803 )

Enzyme 31 Signals

None

Enzyme 31 Transmembrane Regions

204-220

Enzyme 31 Essentiality

Not Available

Enzyme 31 GenBank ID Protein

9651165

Enzyme 31 UniProtKB/Swiss-Prot ID

Q9NRY7

Enzyme 31 UniProtKB/Swiss-Prot Entry Name

PLS2_HUMAN Link Image

Enzyme 31 PDB ID

Not Available

Enzyme 31 Cellular Location

Not Available

Enzyme 31 Gene Sequence

Not Available

Enzyme 31 GenBank Gene ID

AF159441

Enzyme 31 GeneCard ID

Q9NRY7

Enzyme 31 GenAtlas ID

PLSCR2

Enzyme 31 HGNC ID

HGNC:16494 Link Image

Enzyme 31 Chromosome Location

Not Available

Enzyme 31 Locus

Not Available

Enzyme 31 SNPs

SNPJam Report Link Image

Enzyme 31 General References

Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed ]

Enzyme 31 Metabolite References

Not Available

Enzyme 32 [top]

Enzyme 32 ID

12916

Enzyme 32 Name

Phospholipid scramblase 3

Enzyme 32 Synonyms

PL scramblase 3
Ca(2+-dependent phospholipid scramblase 3

Enzyme 32 Gene Name

PLSCR3

Enzyme 32 Protein Sequence

>Phospholipid scramblase 3

MAGYLPPKGYAPSPPPPYPVTPGYPEPALHPGPGQAPVPAQVPAPAPGFALFPSPGPVAL
GSAAPFLPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGAGQPLGQAA
EESNCCARLCCGARRPLRVRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTI
GHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQW
GGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAITS

Enzyme 32 Number of Residues

295

Enzyme 32 Molecular Weight

31663

Enzyme 32 Theoretical pI

6.63

Enzyme 32 GO Classification

Not Available

Enzyme 32 General Function

Not Available

Enzyme 32 Specific Function

Enzyme 32 Pathways

Not Available

Enzyme 32 Reactions

Not Available

Enzyme 32 Pfam Domain Function

Scramblase (PF03803 )

Enzyme 32 Signals

None

Enzyme 32 Transmembrane Regions

266-282

Enzyme 32 Essentiality

Not Available

Enzyme 32 GenBank ID Protein

9651167

Enzyme 32 UniProtKB/Swiss-Prot ID

Q9NRY6

Enzyme 32 UniProtKB/Swiss-Prot Entry Name

PLS3_HUMAN Link Image

Enzyme 32 PDB ID

Not Available

Enzyme 32 Cellular Location

Not Available

Enzyme 32 Gene Sequence

Not Available

Enzyme 32 GenBank Gene ID

AF159442

Enzyme 32 GeneCard ID

Q9NRY6

Enzyme 32 GenAtlas ID

PLSCR3

Enzyme 32 HGNC ID

HGNC:16495 Link Image

Enzyme 32 Chromosome Location

Not Available

Enzyme 32 Locus

Not Available

Enzyme 32 SNPs

SNPJam Report Link Image

Enzyme 32 General References

Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed ]

Enzyme 32 Metabolite References

Not Available

Enzyme 33 [top]

Enzyme 33 ID

12917

Enzyme 33 Name

Phospholipid scramblase 4

Enzyme 33 Synonyms

PL scramblase 4
Ca(2+-dependent phospholipid scramblase 4
TRA1
Cell growth-inhibiting gene 43 protein

Enzyme 33 Gene Name

PLSCR4

Enzyme 33 Protein Sequence

>Phospholipid scramblase 4

MSGVVPTAPEQPAGEMENQTKPPDPRPDAPPEYSSHFLPGPPGTAVPPPTGYPGGLPMGY
YSPQQPSTFPLYQPVGGIHPVRYQPGKYPMPNQSVPITWMPGPTPMANCPPGLEYLVQLD
NIHVLQHFEPLEMMTCFETNNRYDIKNNSDQMVYVVTEDTDDFTRNAYRTLRPFVLRVTD
CMGREIMTMQRPFRCTCCCFCCPSARQELEVQCPPGVTIGFVAEHWNLCRAVYSIQNEKK
ENVMRVRGPCSTYGCGSDSVFEVKSLDGISNIGSIIRKWNGLLSAMADADHFDIHFPLDL
DVKMKAMIFGACFLIDFMYFERSPPQRSR

Enzyme 33 Number of Residues

329

Enzyme 33 Molecular Weight

36965

Enzyme 33 Theoretical pI

5.62

Enzyme 33 GO Classification

Not Available

Enzyme 33 General Function

Not Available

Enzyme 33 Specific Function

Enzyme 33 Pathways

Not Available

Enzyme 33 Reactions

Not Available

Enzyme 33 Pfam Domain Function

Scramblase (PF03803 )

Enzyme 33 Signals

None

Enzyme 33 Transmembrane Regions

304-320

Enzyme 33 Essentiality

Not Available

Enzyme 33 GenBank ID Protein

9622872

Enzyme 33 UniProtKB/Swiss-Prot ID

Q9NRQ2

Enzyme 33 UniProtKB/Swiss-Prot Entry Name

PLS4_HUMAN Link Image

Enzyme 33 PDB ID

Not Available

Enzyme 33 Cellular Location

Not Available

Enzyme 33 Gene Sequence

Not Available

Enzyme 33 GenBank Gene ID

AF199023

Enzyme 33 GeneCard ID

Q9NRQ2

Enzyme 33 GenAtlas ID

PLSCR4

Enzyme 33 HGNC ID

HGNC:16497 Link Image

Enzyme 33 Chromosome Location

Not Available

Enzyme 33 Locus

Not Available

Enzyme 33 SNPs

SNPJam Report Link Image

Enzyme 33 General References

Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed ]

Enzyme 33 Metabolite References

Not Available

Enzyme 34 [top]

Enzyme 34 ID

12918

Enzyme 34 Name

Phospholipid scramblase family memmber 5

Enzyme 34 Synonyms

Not Available

Enzyme 34 Gene Name

PLSCR5

Enzyme 34 Protein Sequence

>Phospholipid scramblase family memmber 5

MASKDAQNQRRGLPGFLPGAPDPDQSLPASSNPGNQAWQLSLPLPSSFLPTVSLPPGLEY
LSQLDLIIIHQQVELLGMILGAETSNKYEIKNSLGQRIYFAVEESICFNRTFCSTLRSCT
LRITDNSGREVITVNRPLRCNSCWCPCYLQELEIQAPPGTIVGYVTQKWDPFLPKFTIQN
ANKEDILKIVGPCVTCGCFGDVDFEVKTINEKLTIGKISKYWSGFVNDVFTNADNFGIHV
PADLDVTVKAAMIGACFLFDFMFFEHSLAGL

Enzyme 34 Number of Residues

271

Enzyme 34 Molecular Weight

29997

Enzyme 34 Theoretical pI

4.90

Enzyme 34 GO Classification

Not Available

Enzyme 34 General Function

Not Available

Enzyme 34 Specific Function

Not Available

Enzyme 34 Pathways

Not Available

Enzyme 34 Reactions

Not Available

Enzyme 34 Pfam Domain Function

Scramblase (PF03803 )

Enzyme 34 Signals

None

Enzyme 34 Transmembrane Regions

None

Enzyme 34 Essentiality

Not Available

Enzyme 34 GenBank ID Protein

41323046

Enzyme 34 UniProtKB/Swiss-Prot ID

A0PG75

Enzyme 34 UniProtKB/Swiss-Prot Entry Name

PLS5_HUMAN Link Image

Enzyme 34 PDB ID

Not Available

Enzyme 34 Cellular Location

Not Available

Enzyme 34 Gene Sequence

Not Available

Enzyme 34 GenBank Gene ID

AY436642

Enzyme 34 GeneCard ID

A0PG75

Enzyme 34 GenAtlas ID

PLSCR5

Enzyme 34 HGNC ID

HGNC:19952 Link Image

Enzyme 34 Chromosome Location

Not Available

Enzyme 34 Locus

Not Available

Enzyme 34 SNPs

SNPJam Report Link Image

Enzyme 34 General References

Not Available

Enzyme 34 Metabolite References

Not Available

Enzyme 35 [top]

Enzyme 35 ID

12919

Enzyme 35 Name

Probable phospholipid-transporting ATPase VB

Enzyme 35 Synonyms

Not Available

Enzyme 35 Gene Name

ATP10B

Enzyme 35 Protein Sequence

>Probable phospholipid-transporting ATPase VB

MALSVDSSWHRWQWRVRDGFPHCPSETTPLLSPEKGRQSYNLTQQRVVFPNNSIFHQDWE
EVSRRYPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITML
PLAIVLFVIMIKDGMEDFKRHRFDKAINCSNIRIYERKEQTYVQKCWKDVRVGDFIQMKC
NEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEVQFEPELFHNTIVC
EKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNS
GPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSFLPS
ALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNI
AEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENAKRLETPKELDSDGEEWTQY
QCLSFSARWAQDPATMRSQKGAQPLRRSQSARVPIQGHYRQRSMGHRESSQPPVAFSSSI
EKDVTPDKNLLTKVRDAALWLETLSDSRPAKASLSTTSSIADFFLALTICNSVMVSTTTE
PRQRVTIKPSSKALGTSLEKIQQLFQKLKLLSLSQSFSSTAPSDTDLGESLGANVATTDS
DERDDASVCSGGDSTDDGGYRSSMWDQGDILESGSGTSLEEALEAPATDLARPEFCYEAE
SPDEAALVHAAHAYSFTLVSRTPEQVTVRLPQGTCLTFSLLCTLGFDSVRKRMSVVVRHP
LTGEIVVYTKGADSVIMDLLEDPACVPDINMEKKLRKIRARTQKHLDLYARDGLRTLCIA
KKVVSEEDFRRWASFRREAEASLDNRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDT
IATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTINTENQETCESILNCALEEL
KQFRELQKPDRKLFGFRLPSKTPSITSEAVVPEAGLVIDGKTLNAIFQGKLEKKFLELTQ
YCRSVLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQA
VMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSST
MIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMV
DAFYQSLICFFIPYLAYKGSDIDVFTFGTPINTISLTTILLHQAMEMKTWTIFHGVVLLG
SFLMYFLVSLLYNATCVICNSPTNPYWVMEGQLSNPTFYLVCFLTPVVALLPRYFFLSLQ
GTCGKSLISKAQKIDKLPPDKRNLEIQSWRSRQRPAPVPEVARPTHHPVSSITGQDFSAS
TPKSSNPPKRKHVEESVLHEQRCGTECMRDDSCSGDSSAQLSSGEHLLGPNRIMAYSRGQ
TDMCRCSKRSSHRRSQSSLTI

Enzyme 35 Number of Residues

1461

Enzyme 35 Molecular Weight

165392

Enzyme 35 Theoretical pI

6.87

Enzyme 35 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 35 General Function

Inorganic ion transport and metabolism

Enzyme 35 Specific Function

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)

Enzyme 35 Pathways

Not Available

Enzyme 35 Reactions

ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086] ALL_REAC R00086

Enzyme 35 Pfam Domain Function

Hydrolase_3 (PF08282 )

Enzyme 35 Signals

None

Enzyme 35 Transmembrane Regions

83-104 111-132 317-338 369-390 1112-1132 1145-1164 1195-1216 1224-1246 1253-1273 1292-1316

Enzyme 35 Essentiality

Not Available

Enzyme 35 GenBank ID Protein

58257664

Enzyme 35 UniProtKB/Swiss-Prot ID

O94823

Enzyme 35 UniProtKB/Swiss-Prot Entry Name

AT10B_HUMAN Link Image

Enzyme 35 PDB ID

Not Available

Enzyme 35 Cellular Location

Not Available

Enzyme 35 Gene Sequence

Not Available

Enzyme 35 GenBank Gene ID

AB018258

Enzyme 35 GeneCard ID

O94823

Enzyme 35 GenAtlas ID

ATP10B

Enzyme 35 HGNC ID

HGNC:13543 Link Image

Enzyme 35 Chromosome Location

Not Available

Enzyme 35 Locus

Not Available

Enzyme 35 SNPs

SNPJam Report Link Image

Enzyme 35 General References

Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed ]

Enzyme 35 Metabolite References

Not Available

Enzyme 36 [top]

Enzyme 36 ID

12920

Enzyme 36 Name

Probable phospholipid-transporting ATPase ID

Enzyme 36 Synonyms

ATPase class I type 8B member 2

Enzyme 36 Gene Name

ATP8B2

Enzyme 36 Protein Sequence

>Probable phospholipid-transporting ATPase ID

MTVPKEMPEKWARAQAPPSWSRKKPSWGTEEERRARANDREYNEKFQYASNCIKTSKYNI
LTFLPVNLFEQFQEVANTYFLFLLILQLIPQISSLSWFTTIVPLVLVLTITAVKDATDDY
FRHKSDNQVNNRQSQVLINGILQQEQWMNVCVGDIIKLENNQFVAADLLLLSSSEPHGLC
YIETAELDGETNMKVRQAIPVTSELGDISKLAKFDGEVICEPPNNKLDKFSGTLYWKENK
FPLSNQNMLLRGCVLRNTEWCFGLVIFAGPDTKLMQNSGRTKFKRTSIDRLMNTLVLWIF
GFLVCMGVILAIGNAIWEHEVGMRFQVYLPWDEAVDSAFFSGFLSFWSYIIILNTVVPIS
LYVSVEVIRLGHSYFINWDKKMFCMKKRTPAEARTTTLNEELGQVEYIFSDKTGTLTQNI
MVFNKCSINGHSYGDVFDVLGHKAELGERPEPVDFSFNPLADKKFLFWDPSLLEAVKIGD
PHTHEFFRLLSLCHTVMSEEKNEGELYYKAQSPDEGALVTAARNFGFVFRSRTPKTITVH
EMGTAITYQLLAILDFNNIRKRMSVIVRNPEGKIRLYCKGADTILLDRLHHSTQELLNTT
MDHLNEYAGEGLRTLVLAYKDLDEEYYEEWAERRLQASLAQDSREDRLASIYEEVENNMM
LLGATAIEDKLQQGVPETIALLTLANIKIWVLTGDKQETAVNIGYSCKMLTDDMTEVFIV
TGHTVLEVREELRKAREKMMDSSRSVGNGFTYQDKLSSSKLTSVLEAVAGEYALVINGHS
LAHALEADMELEFLETACACKAVICCRVTPLQKAQVVELVKKYKKAVTLAIGDGANDVSM
IKTAHIGVGISGQEGIQAVLASDYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFA
FTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGVFDQDVPEQRSMEYPKLYE
PGQLNLLFNKREFFICIAQGIYTSVLMFFIPYGVFADATRDDGTQLADYQSFAVTVATSL
VIVVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSNGLFDMFPNQFRFVGNAQNTL
AQPTVWLTIVLTTVVCIMPVVAFRFLRLNLKPDLSDTVRYTQLVRKKQKAQHRCMRRVGR
TGSRRSGYAFSHQEGFGELIMSGKNMRLSSLALSSFTTRSSSSWIESLRRKKSDSASSPS
GGADKPLKG

Enzyme 36 Number of Residues

1209

Enzyme 36 Molecular Weight

137442

Enzyme 36 Theoretical pI

6.99

Enzyme 36 GO Classification

Function
ATP binding ATPase activity ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism adenyl nucleotide binding binding catalytic activity cation transporter activity hydrolase activity hydrolase activity, acting on acid anhydrides hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides ion transporter activity nucleoside-triphosphatase activity nucleotide binding purine nucleotide binding pyrophosphatase activity transporter activity
Process
cation transport cellular physiological process ion transport metabolism physiological process transport
Component
cell integral to membrane intrinsic to membrane membrane

Enzyme 36 General Function

Inorganic ion transport and metabolism

Enzyme 36 Specific Function

ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out)

Enzyme 36 Pathways

Not Available

Enzyme 36 Reactions

ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086] ALL_REAC R00086

Enzyme 36 Pfam Domain Function

Hydrolase (PF00702 )

Enzyme 36 Signals

None

Enzyme 36 Transmembrane Regions

65-86 93-112 296-317 347-368 890-910 923-942 973-994 1009-1031 1038-1058 1079-1103

Enzyme 36 Essentiality

Not Available

Enzyme 36 GenBank ID Protein

16549511

Enzyme 36 UniProtKB/Swiss-Prot ID

P98198

Enzyme 36 UniProtKB/Swiss-Prot Entry Name

AT8B2_HUMAN Link Image

Enzyme 36 PDB ID

Not Available

Enzyme 36 Cellular Location

Not Available

Enzyme 36 Gene Sequence

Not Available

Enzyme 36 GenBank Gene ID

AK054886

Enzyme 36 GeneCard ID

P98198

Enzyme 36 GenAtlas ID

ATP8B2

Enzyme 36 HGNC ID

HGNC:13534 Link Image

Enzyme 36 Chromosome Location

Not Available

Enzyme 36 Locus

Not Available

Enzyme 36 SNPs

SNPJam Report Link Image

Enzyme 36 General References

Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O: Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. DNA Res. 1999 Oct 29;6(5):329-36. [PubMed ]

Enzyme 36 Metabolite References

Not Available

Enzyme 37 [top]

Enzyme 37 ID

12924

Enzyme 37 Name

Abhydrolase domain-containing protein 4

Enzyme 37 Synonyms

Lyso-N- acylphosphatidylethanolamine lipase
Alpha/beta-hydrolase 4

Enzyme 37 Gene Name

ABHD4

Enzyme 37 Protein Sequence

>Abhydrolase domain-containing protein 4

MADDLEQQSQGWLSSWLPTWRPTSMSQLKNVEARILQCLQNKFLARYVSLPNQNKIWTVT
VSPEQNDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGA
EDEFVTSIETWRETMGIPSMILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTN
PSEIRAPPAWVKAVASVLGRSNPLAVLRVAGPWGPGLVQRFRPDFKRKFADFFEDDTISE
YIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRKDVPITMIYGSDTWIDTSTGKK
VKMQRPDSYVRDMEIKGASHHVYADQPHIFNAVVEEICDSVD

Enzyme 37 Number of Residues

342

Enzyme 37 Molecular Weight

38795

Enzyme 37 Theoretical pI

7.69

Enzyme 37 GO Classification

Function
aminopeptidase activity catalytic activity exopeptidase activity hydrolase activity peptidase activity
Process
aromatic compound metabolism cellular metabolism cellular protein metabolism macromolecule metabolism metabolism physiological process protein metabolism proteolysis
Component
—

Enzyme 37 General Function

Not Available

Enzyme 37 Specific Function

Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains. Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine

Enzyme 37 Pathways

Not Available

Enzyme 37 Reactions

Not Available

Enzyme 37 Pfam Domain Function

Abhydrolase_1 (PF00561 )

Enzyme 37 Signals

None

Enzyme 37 Transmembrane Regions

None

Enzyme 37 Essentiality

Not Available

Enzyme 37 GenBank ID Protein

10434528

Enzyme 37 UniProtKB/Swiss-Prot ID

Q8TB40

Enzyme 37 UniProtKB/Swiss-Prot Entry Name

ABHD4_HUMAN Link Image

Enzyme 37 PDB ID

Not Available

Enzyme 37 Cellular Location

Not Available

Enzyme 37 Gene Sequence

Not Available

Enzyme 37 GenBank Gene ID

AK022878

Enzyme 37 GeneCard ID

Q8TB40

Enzyme 37 GenAtlas ID

ABHD4

Enzyme 37 HGNC ID

HGNC:20154 Link Image

Enzyme 37 Chromosome Location

Not Available

Enzyme 37 Locus

Not Available

Enzyme 37 SNPs

SNPJam Report Link Image

Enzyme 37 General References

Not Available

Enzyme 37 Metabolite References

Not Available

Enzyme 38 [top]

Enzyme 38 ID

12925

Enzyme 38 Name

N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D

Enzyme 38 Synonyms

N-acyl- phosphatidylethanolamine-hydrolyzing phospholipase D, isoform CRA_a

Enzyme 38 Gene Name

NAPE-PLD

Enzyme 38 Protein Sequence

>N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D

MDENESNQSLMTSSQYPKEAVRKRQNSARNSGASDSSRFSRKSFKLDYRLEEDVTKSKKG
KDGRFVNPWPTWKNPSIPNVLRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGV
REAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDA
VLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPG
HDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGP
FDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEHYLEPPVK
LNEALERYGLNAEDFFVLKHGESRYLNNNDENF

Enzyme 38 Number of Residues

393

Enzyme 38 Molecular Weight

45595

Enzyme 38 Theoretical pI

6.10

Enzyme 38 GO Classification

Not Available

Enzyme 38 General Function

Not Available

Enzyme 38 Specific Function

Not Available

Enzyme 38 Pathways

Not Available

Enzyme 38 Reactions

Not Available

Enzyme 38 Pfam Domain Function

Not Available

Enzyme 38 Signals

None

Enzyme 38 Transmembrane Regions

None

Enzyme 38 Essentiality

Not Available

Enzyme 38 GenBank ID Protein

47938140

Enzyme 38 UniProtKB/Swiss-Prot ID

Q6IQ20

Enzyme 38 UniProtKB/Swiss-Prot Entry Name

Q6IQ20_HUMAN Link Image

Enzyme 38 PDB ID

Not Available

Enzyme 38 Cellular Location

Not Available

Enzyme 38 Gene Sequence

Not Available

Enzyme 38 GenBank Gene ID

BC071604

Enzyme 38 GeneCard ID

Q6IQ20

Enzyme 38 GenAtlas ID

NAPEPLD

Enzyme 38 HGNC ID

HGNC:21683 Link Image

Enzyme 38 Chromosome Location

Not Available

Enzyme 38 Locus

Not Available

Enzyme 38 SNPs

SNPJam Report Link Image

Enzyme 38 General References

Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed ]

Enzyme 38 Metabolite References

Not Available

Enzyme 39 [top]

Enzyme 39 ID

12926

Enzyme 39 Name

Phosphatidylethanolamine-binding protein 1

Enzyme 39 Synonyms

PEBP-1
Prostatic-binding protein
HCNPpp
Neuropolypeptide h3
Raf kinase inhibitor protein
RKIP[Contains: Hippocampal cholinergic neurostimulating peptide
HCNP]

Enzyme 39 Gene Name

PEBP1

Enzyme 39 Protein Sequence

>Phosphatidylethanolamine-binding protein 1

MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDS
GKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSGTVLSDYVGSGPPKGTGLHRY
VWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKL
YEQLSGK

Enzyme 39 Number of Residues

187

Enzyme 39 Molecular Weight

21057

Enzyme 39 Theoretical pI

7.65

Enzyme 39 GO Classification

Not Available

Enzyme 39 General Function

Not Available

Enzyme 39 Specific Function

HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor

Enzyme 39 Pathways

Not Available

Enzyme 39 Reactions

Not Available

Enzyme 39 Pfam Domain Function

PBP (PF01161 )

Enzyme 39 Signals

None

Enzyme 39 Transmembrane Regions

None

Enzyme 39 Essentiality

Not Available

Enzyme 39 GenBank ID Protein

435638

Enzyme 39 UniProtKB/Swiss-Prot ID

P30086

Enzyme 39 UniProtKB/Swiss-Prot Entry Name

PEBP1_HUMAN Link Image

Enzyme 39 PDB ID

1BEH

Enzyme 39 PDB File

Show

Enzyme 39 3D Structure

Enzyme 39 Cellular Location

Not Available

Enzyme 39 Gene Sequence

Not Available

Enzyme 39 GenBank Gene ID

D16111

Enzyme 39 GeneCard ID

P30086

Enzyme 39 GenAtlas ID

PEBP1

Enzyme 39 HGNC ID

HGNC:8630

Enzyme 39 Chromosome Location

Not Available

Enzyme 39 Locus

Not Available

Enzyme 39 SNPs

SNPJam Report Link Image

Enzyme 39 General References

Hori N, Chae KS, Murakawa K, Matoba R, Fukushima A, Okubo K, Matsubara K: A human cDNA sequence homologue of bovine phosphatidylethanolamine-binding protein. Gene. 1994 Mar 25;140(2):293-4. [PubMed ]
Tohdoh N, Tojo S, Agui H, Ojika K: Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein. Brain Res Mol Brain Res. 1995 Jun;30(2):381-4. [PubMed ]
Seddiqi N, Bollengier F, Alliel PM, Perin JP, Bonnet F, Bucquoy S, Jolles P, Schoentgen F: Amino acid sequence of the Homo sapiens brain 21-23-kDa protein (neuropolypeptide h3), comparison with its counterparts from Rattus norvegicus and Bos taurus species, and expression of its mRNA in different tissues. J Mol Evol. 1994 Dec;39(6):655-60. [PubMed ]
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 ]
Ojika K, Mitake S, Tohdoh N, Appel SH, Otsuka Y, Katada E, Matsukawa N: Hippocampal cholinergic neurostimulating peptides (HCNP). Prog Neurobiol. 2000 Jan;60(1):37-83. [PubMed ]
Yeung K, Seitz T, Li S, Janosch P, McFerran B, Kaiser C, Fee F, Katsanakis KD, Rose DW, Mischak H, Sedivy JM, Kolch W: Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP. Nature. 1999 Sep 9;401(6749):173-7. [PubMed ]
Banfield MJ, Barker JJ, Perry AC, Brady RL: Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure. 1998 Oct 15;6(10):1245-54. [PubMed ]

Enzyme 39 Metabolite References

Not Available

Enzyme 40 [top]

Enzyme 40 ID

12927

Enzyme 40 Name

PEBP family protein precursor

Enzyme 40 Synonyms

Not Available

Enzyme 40 Gene Name

Not Available

Enzyme 40 Protein Sequence

>PEBP family protein precursor

MGWTMRLVTAALLLGLMMVVTGDEDENSPCAHEALLDEDTLFCQGLEVFYPELGNIGCKV
VPDCNNYRQKITSWMEPIVKFPGAVDGATYILVMVDPDAPSRAEPRQRFWRHWLVTDIKG
ADLKKGKIQGQELSAYQAPSPPAHSGFHRYQFFVYLQEGKVISLLPKENKTRGSWKMDRF
LNRFHLGEPEASTQFMTQNYQDSPTLQAPRERASEPKHKNQAEIAAC

Enzyme 40 Number of Residues

227

Enzyme 40 Molecular Weight

25734

Enzyme 40 Theoretical pI

6.51

Enzyme 40 GO Classification

Not Available

Enzyme 40 General Function

Not Available

Enzyme 40 Specific Function

Not Available

Enzyme 40 Pathways

Not Available

Enzyme 40 Reactions

Not Available

Enzyme 40 Pfam Domain Function

PBP (PF01161 )

Enzyme 40 Signals

1-22

Enzyme 40 Transmembrane Regions

None

Enzyme 40 Essentiality

Not Available

Enzyme 40 GenBank ID Protein

14585855

Enzyme 40 UniProtKB/Swiss-Prot ID

Q96S96

Enzyme 40 UniProtKB/Swiss-Prot Entry Name

PEBPL_HUMAN Link Image

Enzyme 40 PDB ID

Not Available

Enzyme 40 Cellular Location

Not Available

Enzyme 40 Gene Sequence

Not Available

Enzyme 40 GenBank Gene ID

AY037148

Enzyme 40 GeneCard ID

Q96S96

Enzyme 40 GenAtlas ID

Not Available

Enzyme 40 HGNC ID

Not Available

Enzyme 40 Chromosome Location

Not Available

Enzyme 40 Locus

Not Available

Enzyme 40 SNPs

Not Available

Enzyme 40 General References

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 ]

Enzyme 40 Metabolite References

Not Available

Enzyme 41 [top]

Enzyme 41 ID

12928

Enzyme 41 Name

Ethanolaminephosphotransferase 1

Enzyme 41 Synonyms

hEPT1
Selenoprotein I

Enzyme 41 Gene Name

SELI

Enzyme 41 Protein Sequence

>Ethanolaminephosphotransferase 1

MAGYEYVSPEQLAGFDKYKYSAVDTNPLSLYVMHPFWNTIVKVFPTWLAPNLITFSGFLL
VVFNFLLMAYFDPDFYASAPGHKHVPDWVWIVVGILNFVAYTLDGVDGKQARRTNSSTPL
GELFDHGLDSWSCVYFVVTVYSIFGRGSTGVSVFVLYLLLWVVLFSFILSHWEKYNTGIL
FLPWGYDISQVTISFVYIVTAVVGVEAWYEPFLFNFLYRDLFTAMIIGCALCVTLPMSLL
NFFRSYKNNTLKLNSVYEAMVPLFSPCLLFILSTAWILWSPSDILELHPRVFYFMVGTAF
ANSTCQLIVCQMSSTRCPTLNWLLVPLFLVVLVVNLGVASYVESILLYTLTTAFTLAHIH
YGVRVVKQLSSHFQIYPFSLRKPNSDCLGMEEKNIGL

Enzyme 41 Number of Residues

397

Enzyme 41 Molecular Weight

45182

Enzyme 41 Theoretical pI

6.59

Enzyme 41 GO Classification

Function
—
Process
cellular lipid metabolism lipid metabolism membrane lipid metabolism metabolism phospholipid biosynthesis phospholipid metabolism physiological process primary metabolism
Component
—

Enzyme 41 General Function

Not Available

Enzyme 41 Specific Function

Catalyzes phosphatidylethanolamine biosynthesis from CDP-ethanolamine. It thereby plays a central role in the formation and maintenance of vesicular membranes. Involved in the foramtion of phosphatidylethanolamine via 'Kennedy' pathway

Enzyme 41 Pathways

Aminophosphonate metabolism (map00440 )
Ether lipid metabolism (map00565 )
Phospholipid Synthesis (map00564 )

Enzyme 41 Reactions

CDP-ethanolamine + 1,2-diacylglycerol = CMP + a phosphatidylethanolamine [RN:R02057] ALL_REAC R02057
(other) R04920 R06364 R07384

Enzyme 41 Pfam Domain Function

CDP-OH_P_transf (PF01066 )

Enzyme 41 Signals

None

Enzyme 41 Transmembrane Regions

47-69 84-103 123-145 150-172 179-201 221-243 256-278 291-310 317-339 344-366

Enzyme 41 Essentiality

Not Available

Enzyme 41 GenBank ID Protein

52078126

Enzyme 41 UniProtKB/Swiss-Prot ID

Q9C0D9

Enzyme 41 UniProtKB/Swiss-Prot Entry Name

SELI_HUMAN Link Image

Enzyme 41 PDB ID

Not Available

Enzyme 41 Cellular Location

Not Available

Enzyme 41 Gene Sequence

Not Available

Enzyme 41 GenBank Gene ID

BK001426

Enzyme 41 GeneCard ID

Q9C0D9

Enzyme 41 GenAtlas ID

Not Available

Enzyme 41 HGNC ID

Not Available

Enzyme 41 Chromosome Location

Not Available

Enzyme 41 Locus

Not Available

Enzyme 41 SNPs

SNPJam Report Link Image

Enzyme 41 General References

Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R, Gladyshev VN: Characterization of mammalian selenoproteomes. Science. 2003 May 30;300(5624):1439-43. [PubMed ]
Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed ]

Enzyme 41 Metabolite References

Not Available

Enzyme 42 [top]

Enzyme 42 ID

13054

Enzyme 42 Name

Phosphatidylserine decarboxylase (Phosphatidylserine decarboxylase, isoform CRA_a)

Enzyme 42 Synonyms

Not Available

Enzyme 42 Gene Name

PISD

Enzyme 42 Protein Sequence

>Phosphatidylserine decarboxylase (Phosphatidylserine decarboxylase, isoform CRA_a)

MMCQSEARQGPELRAAKWLHFPQLALRRRLGQLSCMSRPALKLRSWPLTVLYYLLPFGAL
RPLSRVGWRPVSRVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEA
AVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYS
LESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTV
SHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFD
RDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQL
KTGQKIRFGEALGSL

Enzyme 42 Number of Residues

375

Enzyme 42 Molecular Weight

43047

Enzyme 42 Theoretical pI

Not Available

Enzyme 42 GO Classification

Not Available

Enzyme 42 General Function

Not Available

Enzyme 42 Specific Function

Not Available

Enzyme 42 Pathways

Not Available

Enzyme 42 Reactions

Not Available

Enzyme 42 Pfam Domain Function

PS_Dcarbxylase (PF02666 )

Enzyme 42 Signals

None

Enzyme 42 Transmembrane Regions

None

Enzyme 42 Essentiality

Not Available

Enzyme 42 GenBank ID Protein

Not Available

Enzyme 42 UniProtKB/Swiss-Prot ID

B1AKM7

Enzyme 42 UniProtKB/Swiss-Prot Entry Name

B1AKM7_HUMAN Link Image

Enzyme 42 PDB ID

Not Available

Enzyme 42 Cellular Location

Not Available

Enzyme 42 Gene Sequence

Not Available

Enzyme 42 GenBank Gene ID

Not Available

Enzyme 42 GeneCard ID

B1AKM7

Enzyme 42 GenAtlas ID

Not Available

Enzyme 42 HGNC ID

Not Available

Enzyme 42 Chromosome Location

Not Available

Enzyme 42 Locus

Not Available

Enzyme 42 SNPs

SNPJam Report Link Image

Enzyme 42 General References

Not Available

Enzyme 42 Metabolite References

Not Available

Enzyme 43 [top]

Enzyme 43 ID

14866

Enzyme 43 Name

Cytosolic phospholipase A2 beta

Enzyme 43 Synonyms

Not Available

Enzyme 43 Gene Name

PLA2G4B

Enzyme 43 Protein Sequence

>MEKAEVSRTCLLTVRVLQAHRLPSKDLVTPSDCYVTLWLPTACSHRLQTRTVKNSSSPVWNQSFHFRIHR

QLKNVMELKVFDQDLVTGDDPVLSVLFDAGTLRAGEFRRESFSLSPQGEGRLEVEFRLQS
LADRGEWLVSNGVLVARELSCLHVQLEETGDQKSSEHRVQLVVPGSCEGPQEASVGTGTF
RFHCPACWEQELSIRLQDAPEEQLKAPLSALPSGQVVRLVFPTSQEPLMRVELKKEAGLR
ELAVRLGFGPCAEEQAFLSRRKQVVAAALRQALQLDGDLQEDEIPVVAIMATGGGIRAMT
SLYGQLAGLKELGLLDCVSYITGASGSTWALANLYEDPEWSQKDLAGPTELLKTQVTKNK
LGVLAPSQLQRYRQELAERARLGYPSCFTNLWALINEALLHDEPHDHKLSDQREALSHGQ
NPLPIYCALNTKGQSLTTFEFGEWCEFSPYEVGFPKYGAFIPSELFGSEFFMGQLMKRLP
ESRICFLEGIWSNLYAANLQDSLYWASEPSQFWDRWVRNQANLDKEQVPLLKIEEPPSTA
GRIAEFFTDLLTWRPLAQATHNFLRGLHFHKDYFQHPHFSTWKATTLDGLPNQLTPSEPH
LCLLDVGYLINTSCLPLLQPTRDVDLILSLDYNLHGAFQQLQLLGRFCQEQGIPFPPISP
SPEEQLQPRECHTFSDPTCPGAPAVLHFPLVSDSFREYSAPGVRRTPEEAAAGEVNLSSS
DSPYHYTKVTYSQEDVDKLLHLTHYNVCNNQEQLLEALRQAVQRRRQRRPH

Enzyme 43 Number of Residues

781

Enzyme 43 Molecular Weight

88066

Enzyme 43 Theoretical pI

5.85

Enzyme 43 GO Classification

Function
carboxylic ester hydrolase activity catalytic activity hydrolase activity hydrolase activity, acting on ester bonds lipase activity phospholipase activity
Process
cellular lipid metabolism lipid metabolism membrane lipid metabolism metabolism phospholipid catabolism phospholipid metabolism physiological process primary metabolism
Component
—

Enzyme 43 General Function

Not Available

Enzyme 43 Specific Function

Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position with a preference for arachidonoyl phospholipids. Has a much weaker activity than PLA2G4A. Isoform 3 has calcium-dependent activity against palmitoyl-arachidonyl-phosphatidylethanolamine and low level lysophospholipase activity but no activity against phosphatidylcholine

Enzyme 43 Pathways

Not Available

Enzyme 43 Reactions

Not Available

Enzyme 43 Pfam Domain Function

C2 (PF00168 )
PLA2_B (PF01735 )

Enzyme 43 Signals

None

Enzyme 43 Transmembrane Regions

None

Enzyme 43 Essentiality

Not Available

Enzyme 43 GenBank ID Protein

3811347

Enzyme 43 UniProtKB/Swiss-Prot ID

P0C869

Enzyme 43 UniProtKB/Swiss-Prot Entry Name

PA24B_HUMAN Link Image

Enzyme 43 PDB ID

Not Available

Enzyme 43 Cellular Location

Not Available

Enzyme 43 Gene Sequence

>3039 bp

ATGGCGGAGGCGGCTTTGGAAGCCGTGCGGAGCGAGTTACGAGAATTCCCGGCCGCTGCA
AGGGAGCTCTGCGTGCCTCTTGCTGTGCCCTACCTGGACAAACCCCCAACTCCGCTCCAC
TTCTACCGGGACTGGGTCTGCCCCAACAGGCCGTGCATTATCCGCAACGCTCTGCAGCAC
TGGCCGGCCCTCCAGAAGTGGTCCCTCCCCTATTTCAGAGCCACAGTGGGCTCCACAGAG
GTGAGTGTGGCCGTGACCCCAGATGGTTACGCGGATGCCGTGAGAGGGGATCGCTTCATG
ATGCCAGCTGAGCGCCGCCTGCCCCTGAGCTTCGTGCTGGATGTGCTGGAGGGCCGGGCC
CAGCACCCTGGAGTCCTCTATGTGCAGAAGCAGTGCTCCAACCTGCCCAGCGAGCTGCCC
CAGCTGCTGCCTGATCTGGAATCCCATGTGCCCTGGGCCTCCGAAGCCCTGGGAAAGATG
CCCGATGCTGTGAACTTCTGGCTGGGGGAGGCGGCTGCAGTGACTTCTTTGCACAAGGAC
CACTATGAGAACCTCTACTGCGTGGTCTCAGGAGAGAAGCATTTCCTGTTCCATCCGCCC
AGCGACCGGCCCTTCATCCCCTATGAGCTGTACACGCCGGCAACCTACCAGCTAACTGAA
GAGGGCACCTTTAAGGTGGTGGATGAAGAGGCCATGGAGAAGGCAGAGGTGTCCAGGACC
TGCCTGCTCACGGTTCGTGTCCTGCAGGCCCATCGCCTACCCTCTAAGGACCTAGTGACC
CCCTCTGACTGCTACGTGACTCTCTGGCTGCCCACGGCCTGCAGCCACAGGCTCCAGACA
CGCACGGTCAAGAACAGCAGTAGCCCTGTCTGGAACCAGAGCTTTCACTTCAGGATCCAC
AGGCAGCTCAAGAATGTCATGGAACTGAAAGTCTTTGACCAGGACCTGGTGACCGGAGAT
GACCCTGTGTTGTCAGTACTGTTTGATGCGGGGACTCTGCGGGCTGGGGAGTTCCGGCGC
GAGAGCTTCTCACTGAGCCCTCAGGGTGAGGGGCGCCTGGAAGTTGAATTTCGCCTGCAG
AGTCTGGCTGACCGTGGCGAGTGGCTCGTCAGCAATGGCGTTCTGGTGGCCCGGGAGCTC
TCCTGCTTGCACGTTCAACTGGAGGAGACAGGAGACCAGAAGTCCTCAGAGCACAGAGTT
CAGCTTGTGGTTCCTGGGTCCTGTGAGGGTCCGCAGGAGGCCTCTGTGGGCACTGGCACC
TTCCGCTTCCACTGCCCAGCCTGCTGGGAGCAGGAGCTGAGTATTCGCCTGCAGGATGCC
CCCGAGGAGCAACTAAAGGCGCCACTGAGTGCCCTGCCCTCTGGTCAAGTGGTGAGGCTT
GTCTTCCCCACGTCCCAGGAGCCCCTGATGAGAGTGGAGCTGAAAAAAGAAGCAGGACTG
AGGGAGCTGGCCGTGCGACTGGGCTTCGGGCCCTGTGCAGAGGAGCAGGCCTTCCTGAGC
AGGAGGAAGCAGGTGGTGGCCGCGGCCTTGAGGCAGGCCCTGCAGCTGGATGGAGACCTG
CAGGAGGATGAGATCCCAGTGGTAGCTATTATGGCCACTGGTGGTGGGATCCGGGCAATG
ACTTCCCTGTATGGGCAGCTGGCTGGCCTGAAGGAGCTGGGCCTCTTGGATTGCGTCTCC
TACATCACCGGGGCCTCGGGCTCCACCTGGGCCTTGGCCAACCTTTATGAGGACCCAGAG
TGGTCTCAGAAGGACCTGGCAGGGCCCACTGAGTTGCTGAAGACCCAGGTGACCAAGAAC
AAGCTGGGTGTGCTGGCCCCCAGCCAGCTGCAGCGGTACCGGCAGGAGCTGGCCGAGCGT
GCCCGCTTGGGCTACCCAAGCTGCTTCACCAACCTGTGGGCCCTCATCAACGAGGCGCTG
CTGCATGATGAGCCCCATGATCACAAGCTCTCAGATCAACGGGAGGCCCTGAGTCATGGC
CAGAACCCTCTGCCCATCTACTGTGCCCTCAACACCAAAGGGCAGAGCCTGACCACTTTT
GAATTTGGGGAGTGGTGCGAGTTCTCTCCCTACGAGGTCGGCTTCCCCAAGTACGGGGCC
TTCATCCCCTCTGAGCTCTTTGGCTCCGAGTTCTTTATGGGGCAGCTGATGAAGAGGCTT
CCTGAGTCCCGCATCTGCTTCTTAGAAGGTATCTGGAGCAACCTGTATGCAGCCAACCTC
CAGGACAGCTTATACTGGGCCTCAGAGCCCAGCCAGTTCTGGGACCGCTGGGTCAGGAAC
CAGGCCAACCTGGACAAGGAGCAGGTCCCCCTTCTGAAGATAGAAGAACCACCCTCAACA
GCCGGCAGRATAGCTGAGTTTTTCACCGATCTTCTGACGTGGCGTCCACTGGCCCAGGCC
ACACATAATTTCCTGCGTGGCCTCCATTTCCACAAAGACTACTTTCAGCATCCTCACTTC
TCCACATGGAAAGCTACCACTCTGGATGGGCTCCCCAACCAGCTGACACCCTCGGAGCCC
CACCTGTGCCTGCTGGATGTTGGCTACCTCATCAATACCAGCTGCCTGCCCCTCCTGCAG
CCCACTCGGGACGTGGACCTCATCCTGTCATTGGACTACAACCTCCACGGAGCCTTCCAG
CAGTTGCAGCTCCTGGGCCGGTTCTGCCAGGAGCAGGGGATCCCGTTCCCACCCATCTCG
CCCAGCCCCGAAGAGCAGCTCCAGCCTCGGGAGTGCCACACCTTCTCCGACCCCACCTGC
CCCGGAGCCCCTGCGGTGCTGCACTTTCCTCTGGTCAGCGACTCCTTCCGGGAGTACTCG
GCCCCTGGGGTCCGGCGGACACCCGAGGAGGCGGCAGCTGGGGAGGTGAACCTGTCTTCA
TCGGACTCTCCCTACCACTACACGAAGGTGACCTACAGCCAGGAGGACGTGGACAAGCTG
CTGCACCTGACACATTACAATGTCTGCAACAACCAGGAGCAGCTGCTGGAGGCTCTGCGC
CAGGCAGTGCAGCGGAGGCGGCAGCGCAGGCCCCACTGA

Enzyme 43 GenBank Gene ID

AF065215

Enzyme 43 GeneCard ID

P0C869

Enzyme 43 GenAtlas ID

PLA2G4B

Enzyme 43 HGNC ID

HGNC:9036

Enzyme 43 Chromosome Location

Enzyme 43 Locus

15q11.2-q21.3

Enzyme 43 SNPs

SNPJam Report Link Image

Enzyme 43 General References

Pickard RT, Strifler BA, Kramer RM, Sharp JD: Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1999 Mar 26;274(13):8823-31. [PubMed ]
Song C, Chang XJ, Bean KM, Proia MS, Knopf JL, Kriz RW: Molecular characterization of cytosolic phospholipase A2-beta. J Biol Chem. 1999 Jun 11;274(24):17063-7. [PubMed ]

Enzyme 43 Metabolite References

Not Available

Enzyme 44 [top]

Enzyme 44 ID

15207

Enzyme 44 Name

Phospholipase D1 variant (Fragment)

Enzyme 44 Synonyms

Not Available

Enzyme 44 Gene Name

Not Available

Enzyme 44 Protein Sequence

>Phospholipase D1 variant (Fragment)

ANAQVLAAPSPCSPFAFTLSKVNMSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEG
EEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRV
PSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEP
REMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDL
GPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLL
VDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKD
HRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGN
RWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSST
VYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAM
ESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSI
SSIDSTSNTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPR
MPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVP
GSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFN
KIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGEN
SILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANIN
DRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQ
DPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEE
ELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT

Enzyme 44 Number of Residues

1059

Enzyme 44 Molecular Weight

122010

Enzyme 44 Theoretical pI

9.03

Enzyme 44 GO Classification

Function
catalytic activity
Process
cell communication cellular process intracellular signaling cascade metabolism physiological process signal transduction
Component
—

Enzyme 44 General Function

Lipid transport and metabolism

Enzyme 44 Specific Function

Not Available

Enzyme 44 Pathways

Not Available

Enzyme 44 Reactions

Not Available

Enzyme 44 Pfam Domain Function

PH (PF00169 )
PLDc (PF00614 )
PX (PF00787 )

Enzyme 44 Signals

None

Enzyme 44 Transmembrane Regions

None

Enzyme 44 Essentiality

Not Available

Enzyme 44 GenBank ID Protein

62089400

Enzyme 44 UniProtKB/Swiss-Prot ID

Q59EA4

Enzyme 44 UniProtKB/Swiss-Prot Entry Name

Q59EA4_HUMAN Link Image

Enzyme 44 PDB ID

Not Available

Enzyme 44 Cellular Location

Not Available

Enzyme 44 Gene Sequence

>3182 bp

CCGCCAACGCGCAGGTGCTAGCGGCCCCTTCGCCCTGCAGCCCCTTTGCTTTTACTCTGT
CCAAAGTTAACATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAA
TTGCTGCTGACATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGG
GAGAGGAGGTAGACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCC
CTTTCTCTGCTATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCT
CCGGCTGTCCAATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGG
TACCAAGTATTAATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTA
AGAGGAAATTCAAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTA
TCCGCATCCCCATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGC
CTCGAGAGATGCCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCC
TTGGTAGAAGAAAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATA
GAAACTATCATGCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATT
TGGGACCAAAGGGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAG
GCTTGAATTGCTGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAG
TGAAAGATTCCTTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGC
TGGTAGACAAAGAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAA
TCCGAATTGATAATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTC
GGTGGTGGGGAGGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAG
ATCATCGATTTGGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTA
ATGCCAAAGGATATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTT
TTATCACAGACTGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAA
ATCGTTGGAGGTTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCA
TAATGCTCTACAAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGA
CTTTGATGCGTCTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCA
CCGTCTATTTGTGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTG
TGGGAGGGATTGACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACG
TGGGCAGTGTGAAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAA
TGGAGTCTATGGAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCA
TCCAGAAGAGTATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGT
TCTCCAAATTTAGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCA
TCAGCAGCATTGACAGCACCTCCAATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGG
GAGAGCTGCATGGGGAAACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCA
AAGACTGGGTTCAACTTGATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCC
GGATGCCCTGGCATGACATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCAC
GTCACTTCATCCAGCGCTGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTT
CTTATCCTTTTCTGCTTCCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGC
CTGGGTCTGTCCATGCTAACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTA
TAAAGTACCATGAAGAGTCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGC
ACTATATCTATATCGAAAACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCA
ACAAGATAGGCGATGCCATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAAT
ACCGGGTATATGTCGTGATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCG
GAGGAAATGCTCTACAGGCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAA
ATTCCATCCTTGGACAGTTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCAT
TCTGTGGTCTTAGAACACATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATG
TCCACAGCAAGTTGTTAATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAA
ATGACCGCAGCATGCTGGGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAG
AGACTGTTCCTTCAGTAATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGAC
TTCGGCTACAGTGCTTTAGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTC
AGGATCCAGTGAGTGACAAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATG
CTACAATTTATGACAAGGTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTC
AGCTGAGAGACTTTATAAACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGG
AGGAACTGAAGAAGATCCGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAG
AAAGCCTACTGCCTTCTGTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTT
AA

Enzyme 44 GenBank Gene ID

AB209907

Enzyme 44 GeneCard ID

Q59EA4

Enzyme 44 GenAtlas ID

Not Available

Enzyme 44 HGNC ID

HGNC:9067

Enzyme 44 Chromosome Location

Not Available

Enzyme 44 Locus

Not Available

Enzyme 44 SNPs

Not Available

Enzyme 44 General References

Not Available

Enzyme 44 Metabolite References

Not Available

Enzyme 45 [top]

Enzyme 45 ID

15299

Enzyme 45 Name

cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a)

Enzyme 45 Synonyms

Not Available

Enzyme 45 Gene Name

PLA2G2A

Enzyme 45 Protein Sequence

>cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a)

MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC

Enzyme 45 Number of Residues

144

Enzyme 45 Molecular Weight

16083

Enzyme 45 Theoretical pI

9.51

Enzyme 45 GO Classification

Not Available

Enzyme 45 General Function

Not Available

Enzyme 45 Specific Function

Not Available

Enzyme 45 Pathways

Not Available

Enzyme 45 Reactions

Not Available

Enzyme 45 Pfam Domain Function

Not Available

Enzyme 45 Signals

None

Enzyme 45 Transmembrane Regions

None

Enzyme 45 Essentiality

Not Available

Enzyme 45 GenBank ID Protein

158256040

Enzyme 45 UniProtKB/Swiss-Prot ID

A8K5I7

Enzyme 45 UniProtKB/Swiss-Prot Entry Name

A8K5I7_HUMAN Link Image

Enzyme 45 PDB ID

1DB4

Enzyme 45 PDB File

Show

Enzyme 45 3D Structure

Enzyme 45 Cellular Location

Not Available

Enzyme 45 Gene Sequence

>435 bp

ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA

Enzyme 45 GenBank Gene ID

AK291302

Enzyme 45 GeneCard ID

A8K5I7

Enzyme 45 GenAtlas ID

Not Available

Enzyme 45 HGNC ID

Not Available

Enzyme 45 Chromosome Location

Not Available

Enzyme 45 Locus

Not Available

Enzyme 45 SNPs

SNPJam Report Link Image

Enzyme 45 General References

Not Available

Enzyme 45 Metabolite References

Not Available

Enzyme 46 [top]

Enzyme 46 ID

16561

Enzyme 46 Name

Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)

Enzyme 46 Synonyms

Not Available

Enzyme 46 Gene Name

PLA2G6

Enzyme 46 Protein Sequence

>Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)

MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRQLQDLMHISRARKPAFILGSMRDEK
RTHDHLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSM
AYMRGMYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPA
ELHLFRNYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGG
LLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNP
WELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVS
DTVLVNALWETEVYIYEHREEFQKLIQLLLSP

Enzyme 46 Number of Residues

752

Enzyme 46 Molecular Weight

84094

Enzyme 46 Theoretical pI

7.24

Enzyme 46 GO Classification

Function
—
Process
lipid metabolism metabolism physiological process primary metabolism
Component
—

Enzyme 46 General Function

Not Available

Enzyme 46 Specific Function

Not Available

Enzyme 46 Pathways

Not Available

Enzyme 46 Reactions

Not Available

Enzyme 46 Pfam Domain Function

Ank (PF00023 )
Patatin (PF01734 )

Enzyme 46 Signals

None

Enzyme 46 Transmembrane Regions

None

Enzyme 46 Essentiality

Not Available

Enzyme 46 GenBank ID Protein

Not Available

Enzyme 46 UniProtKB/Swiss-Prot ID

B0QYE8

Enzyme 46 UniProtKB/Swiss-Prot Entry Name

B0QYE8_HUMAN Link Image

Enzyme 46 PDB ID

Not Available

Enzyme 46 Cellular Location

Not Available

Enzyme 46 Gene Sequence

Not Available

Enzyme 46 GenBank Gene ID

AL022322

Enzyme 46 GeneCard ID

B0QYE8

Enzyme 46 GenAtlas ID

Not Available

Enzyme 46 HGNC ID

Not Available

Enzyme 46 Chromosome Location

Enzyme 46 Locus

22q13.1

Enzyme 46 SNPs

SNPJam Report Link Image

Enzyme 46 General References

Not Available

Enzyme 46 Metabolite References

Not Available

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Human Metabolome Database Version 2.5

Showing metabocard for PE(16:0/16:0) (HMDB08923)