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Protein

1-acyl-sn-glycerol-3-phosphate acyltransferase alpha

Gene

AGPAT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.1 Publication

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.1 Publication

Pathway:iCDP-diacylglycerol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase 2, mitochondrial (GPAT2), Glycerol-3-phosphate acyltransferase 4 (AGPAT6), Glycerol-3-phosphate acyltransferase 3 (AGPAT9), Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAM)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (AGPAT2), 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (AGPAT4), 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (AGPAT3), 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (AGPAT5), 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (AGPAT1), Lysocardiolipin acyltransferase 1 (LCLAT1)
  3. Phosphatidate cytidylyltransferase 1 (CDS1), Phosphatidate cytidylyltransferase 2 (CDS2), Phosphatidate cytidylyltransferase, mitochondrial (TAMM41), Phosphatidate cytidylyltransferase (CDS1), Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • 1-acylglycerol-3-phosphate O-acyltransferase activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS09762-MONOMER.
BRENDAi2.3.1.51. 2681.
ReactomeiREACT_1190. Triglyceride Biosynthesis.
REACT_120906. Synthesis of PA.
REACT_2122. ChREBP activates metabolic gene expression.
UniPathwayiUPA00557; UER00613.

Names & Taxonomyi

Protein namesi
Recommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (EC:2.3.1.51)
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 1
Short name:
1-AGP acyltransferase 1
Short name:
1-AGPAT 1
Lysophosphatidic acid acyltransferase alpha
Short name:
LPAAT-alpha
Protein G15
Gene namesi
Name:AGPAT1
Synonyms:G15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:324. AGPAT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei38 – 5821HelicalSequence AnalysisAdd
BLAST
Transmembranei128 – 14821HelicalSequence AnalysisAdd
BLAST
Transmembranei193 – 21321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: ProtInc
  • endoplasmic reticulum membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24621.

Polymorphism and mutation databases

BioMutaiAGPAT1.
DMDMi3914372.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 2832571-acyl-sn-glycerol-3-phosphate acyltransferase alphaPRO_0000208190Add
BLAST

Proteomic databases

MaxQBiQ99943.
PaxDbiQ99943.
PRIDEiQ99943.

PTM databases

PhosphoSiteiQ99943.

Expressioni

Tissue specificityi

Widely expressed. Expressed in adipose tissue and at high levels in testis and pancreas. Expressed at lower levels in tissues such as heart, brain, placenta, kidney, lung, spleen, thymus, prostate, ovary, intestine, colon, leukocyte and liver.1 Publication

Gene expression databases

BgeeiQ99943.
CleanExiHS_AGPAT1.
ExpressionAtlasiQ99943. baseline and differential.
GenevisibleiQ99943. HS.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MEOX2A4D1273EBI-3893468,EBI-10172134

Protein-protein interaction databases

BioGridi115805. 10 interactions.
IntActiQ99943. 3 interactions.
STRINGi9606.ENSP00000337463.

Structurei

3D structure databases

ProteinModelPortaliQ99943.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi104 – 1096HXXXXD motif
Motifi178 – 1814EGTR motif

Domaini

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0204.
GeneTreeiENSGT00390000008726.
HOGENOMiHOG000026375.
HOVERGENiHBG000676.
InParanoidiQ99943.
KOiK13509.
OMAiMLTIFRE.
PhylomeDBiQ99943.
TreeFamiTF314867.

Family and domain databases

InterProiIPR004552. AGP_acyltrans.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00530. AGP_acyltrn. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99943-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLWPGAWML LLLLFLLLLF LLPTLWFCSP SAKYFFKMAF YNGWILFLAV
60 70 80 90 100
LAIPVCAVRG RNVENMKILR LMLLHIKYLY GIRVEVRGAH HFPPSQPYVV
110 120 130 140 150
VSNHQSSLDL LGMMEVLPGR CVPIAKRELL WAGSAGLACW LAGVIFIDRK
160 170 180 190 200
RTGDAISVMS EVAQTLLTQD VRVWVFPEGT RNHNGSMLPF KRGAFHLAVQ
210 220 230 240 250
AQVPIVPIVM SSYQDFYCKK ERRFTSGQCQ VRVLPPVPTE GLTPDDVPAL
260 270 280
ADRVRHSMLT VFREISTDGR GGGDYLKKPG GGG
Length:283
Mass (Da):31,717
Last modified:January 1, 1998 - v2
Checksum:i71F3207259747C68
GO

Sequence cautioni

The sequence AAB47493.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti30 – 301P → S.
Corresponds to variant rs11964847 [ dbSNP | Ensembl ].
VAR_050593

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56417 mRNA. Translation: AAB58775.1.
U75971 mRNA. Translation: AAB96378.1.
Y09565 mRNA. Translation: CAA70758.1.
U89336 Genomic DNA. Translation: AAB47493.1. Different initiation.
AL662884 Genomic DNA. Translation: CAI18347.1.
AL662828 Genomic DNA. Translation: CAI17430.1.
AL845464 Genomic DNA. Translation: CAI41807.1.
BX284686 Genomic DNA. Translation: CAM26221.1.
BX927239 Genomic DNA. Translation: CAQ06593.1.
CR933878 Genomic DNA. Translation: CAQ09622.1.
CR812478 Genomic DNA. Translation: CAQ10697.1.
CH471081 Genomic DNA. Translation: EAX03600.1.
BC002402 mRNA. Translation: AAH02402.1.
BC003007 mRNA. Translation: AAH03007.1.
BC004310 mRNA. Translation: AAH04310.1.
BC090849 mRNA. Translation: AAH90849.1.
CCDSiCCDS4744.1.
RefSeqiNP_006402.1. NM_006411.3.
NP_116130.2. NM_032741.4.
XP_005248863.1. XM_005248806.1.
XP_005272819.1. XM_005272762.1.
XP_005274887.1. XM_005274830.1.
XP_005275131.1. XM_005275074.1.
XP_005275261.1. XM_005275204.1.
XP_005275395.1. XM_005275338.1.
XP_005275562.1. XM_005275505.1.
XP_011512536.1. XM_011514234.1.
XP_011544583.1. XM_011546281.1.
XP_011545473.1. XM_011547171.1.
XP_011546127.1. XM_011547825.1.
XP_011546307.1. XM_011548005.1.
XP_011546484.1. XM_011548182.1.
XP_011546679.1. XM_011548377.1.
UniGeneiHs.409230.

Genome annotation databases

EnsembliENST00000336984; ENSP00000337463; ENSG00000204310.
ENST00000375104; ENSP00000364245; ENSG00000204310.
ENST00000375107; ENSP00000364248; ENSG00000204310.
ENST00000383294; ENSP00000372782; ENSG00000206324.
ENST00000395496; ENSP00000378874; ENSG00000204310.
ENST00000395497; ENSP00000378875; ENSG00000204310.
ENST00000395499; ENSP00000378877; ENSG00000204310.
ENST00000399825; ENSP00000382721; ENSG00000206324.
ENST00000399827; ENSP00000382723; ENSG00000206324.
ENST00000399829; ENSP00000382725; ENSG00000206324.
ENST00000399830; ENSP00000382726; ENSG00000206324.
ENST00000399833; ENSP00000382728; ENSG00000206324.
ENST00000414520; ENSP00000406615; ENSG00000227642.
ENST00000414933; ENSP00000388870; ENSG00000227642.
ENST00000415173; ENSP00000412805; ENSG00000228892.
ENST00000416363; ENSP00000407189; ENSG00000236873.
ENST00000417388; ENSP00000415015; ENSG00000228892.
ENST00000424030; ENSP00000397765; ENSG00000236873.
ENST00000425204; ENSP00000388253; ENSG00000226467.
ENST00000425572; ENSP00000394919; ENSG00000235758.
ENST00000427763; ENSP00000401410; ENSG00000226467.
ENST00000430226; ENSP00000412304; ENSG00000235758.
ENST00000430777; ENSP00000392820; ENSG00000236873.
ENST00000433376; ENSP00000387810; ENSG00000228892.
ENST00000433896; ENSP00000408842; ENSG00000236873.
ENST00000434614; ENSP00000401287; ENSG00000235758.
ENST00000436149; ENSP00000388090; ENSG00000235758.
ENST00000439774; ENSP00000398016; ENSG00000236873.
ENST00000440840; ENSP00000395863; ENSG00000236873.
ENST00000444369; ENSP00000408032; ENSG00000227642.
ENST00000446323; ENSP00000392083; ENSG00000226467.
ENST00000446463; ENSP00000405864; ENSG00000226467.
ENST00000448196; ENSP00000404106; ENSG00000235758.
ENST00000449776; ENSP00000410831; ENSG00000226467.
ENST00000451833; ENSP00000406582; ENSG00000228892.
ENST00000452393; ENSP00000406614; ENSG00000228892.
ENST00000452427; ENSP00000387738; ENSG00000235758.
ENST00000454929; ENSP00000390988; ENSG00000227642.
ENST00000455898; ENSP00000395613; ENSG00000228892.
ENST00000456421; ENSP00000389516; ENSG00000227642.
ENST00000456679; ENSP00000388815; ENSG00000227642.
ENST00000457923; ENSP00000405565; ENSG00000226467.
GeneIDi10554.
KEGGihsa:10554.
UCSCiuc003oae.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56417 mRNA. Translation: AAB58775.1.
U75971 mRNA. Translation: AAB96378.1.
Y09565 mRNA. Translation: CAA70758.1.
U89336 Genomic DNA. Translation: AAB47493.1. Different initiation.
AL662884 Genomic DNA. Translation: CAI18347.1.
AL662828 Genomic DNA. Translation: CAI17430.1.
AL845464 Genomic DNA. Translation: CAI41807.1.
BX284686 Genomic DNA. Translation: CAM26221.1.
BX927239 Genomic DNA. Translation: CAQ06593.1.
CR933878 Genomic DNA. Translation: CAQ09622.1.
CR812478 Genomic DNA. Translation: CAQ10697.1.
CH471081 Genomic DNA. Translation: EAX03600.1.
BC002402 mRNA. Translation: AAH02402.1.
BC003007 mRNA. Translation: AAH03007.1.
BC004310 mRNA. Translation: AAH04310.1.
BC090849 mRNA. Translation: AAH90849.1.
CCDSiCCDS4744.1.
RefSeqiNP_006402.1. NM_006411.3.
NP_116130.2. NM_032741.4.
XP_005248863.1. XM_005248806.1.
XP_005272819.1. XM_005272762.1.
XP_005274887.1. XM_005274830.1.
XP_005275131.1. XM_005275074.1.
XP_005275261.1. XM_005275204.1.
XP_005275395.1. XM_005275338.1.
XP_005275562.1. XM_005275505.1.
XP_011512536.1. XM_011514234.1.
XP_011544583.1. XM_011546281.1.
XP_011545473.1. XM_011547171.1.
XP_011546127.1. XM_011547825.1.
XP_011546307.1. XM_011548005.1.
XP_011546484.1. XM_011548182.1.
XP_011546679.1. XM_011548377.1.
UniGeneiHs.409230.

3D structure databases

ProteinModelPortaliQ99943.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115805. 10 interactions.
IntActiQ99943. 3 interactions.
STRINGi9606.ENSP00000337463.

Chemistry

ChEMBLiCHEMBL3583.

PTM databases

PhosphoSiteiQ99943.

Polymorphism and mutation databases

BioMutaiAGPAT1.
DMDMi3914372.

Proteomic databases

MaxQBiQ99943.
PaxDbiQ99943.
PRIDEiQ99943.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336984; ENSP00000337463; ENSG00000204310.
ENST00000375104; ENSP00000364245; ENSG00000204310.
ENST00000375107; ENSP00000364248; ENSG00000204310.
ENST00000383294; ENSP00000372782; ENSG00000206324.
ENST00000395496; ENSP00000378874; ENSG00000204310.
ENST00000395497; ENSP00000378875; ENSG00000204310.
ENST00000395499; ENSP00000378877; ENSG00000204310.
ENST00000399825; ENSP00000382721; ENSG00000206324.
ENST00000399827; ENSP00000382723; ENSG00000206324.
ENST00000399829; ENSP00000382725; ENSG00000206324.
ENST00000399830; ENSP00000382726; ENSG00000206324.
ENST00000399833; ENSP00000382728; ENSG00000206324.
ENST00000414520; ENSP00000406615; ENSG00000227642.
ENST00000414933; ENSP00000388870; ENSG00000227642.
ENST00000415173; ENSP00000412805; ENSG00000228892.
ENST00000416363; ENSP00000407189; ENSG00000236873.
ENST00000417388; ENSP00000415015; ENSG00000228892.
ENST00000424030; ENSP00000397765; ENSG00000236873.
ENST00000425204; ENSP00000388253; ENSG00000226467.
ENST00000425572; ENSP00000394919; ENSG00000235758.
ENST00000427763; ENSP00000401410; ENSG00000226467.
ENST00000430226; ENSP00000412304; ENSG00000235758.
ENST00000430777; ENSP00000392820; ENSG00000236873.
ENST00000433376; ENSP00000387810; ENSG00000228892.
ENST00000433896; ENSP00000408842; ENSG00000236873.
ENST00000434614; ENSP00000401287; ENSG00000235758.
ENST00000436149; ENSP00000388090; ENSG00000235758.
ENST00000439774; ENSP00000398016; ENSG00000236873.
ENST00000440840; ENSP00000395863; ENSG00000236873.
ENST00000444369; ENSP00000408032; ENSG00000227642.
ENST00000446323; ENSP00000392083; ENSG00000226467.
ENST00000446463; ENSP00000405864; ENSG00000226467.
ENST00000448196; ENSP00000404106; ENSG00000235758.
ENST00000449776; ENSP00000410831; ENSG00000226467.
ENST00000451833; ENSP00000406582; ENSG00000228892.
ENST00000452393; ENSP00000406614; ENSG00000228892.
ENST00000452427; ENSP00000387738; ENSG00000235758.
ENST00000454929; ENSP00000390988; ENSG00000227642.
ENST00000455898; ENSP00000395613; ENSG00000228892.
ENST00000456421; ENSP00000389516; ENSG00000227642.
ENST00000456679; ENSP00000388815; ENSG00000227642.
ENST00000457923; ENSP00000405565; ENSG00000226467.
GeneIDi10554.
KEGGihsa:10554.
UCSCiuc003oae.3. human.

Organism-specific databases

CTDi10554.
GeneCardsiGC06M032135.
GC06Mi32147.
GC06Mj32084.
GC06Ml32175.
GC06Mm32212.
GC06Mn32093.
GC06Mo32142.
HGNCiHGNC:324. AGPAT1.
MIMi603099. gene.
neXtProtiNX_Q99943.
PharmGKBiPA24621.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0204.
GeneTreeiENSGT00390000008726.
HOGENOMiHOG000026375.
HOVERGENiHBG000676.
InParanoidiQ99943.
KOiK13509.
OMAiMLTIFRE.
PhylomeDBiQ99943.
TreeFamiTF314867.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00613.
BioCyciMetaCyc:HS09762-MONOMER.
BRENDAi2.3.1.51. 2681.
ReactomeiREACT_1190. Triglyceride Biosynthesis.
REACT_120906. Synthesis of PA.
REACT_2122. ChREBP activates metabolic gene expression.

Miscellaneous databases

GeneWikiiAGPAT1.
GenomeRNAii10554.
NextBioi40041.
PROiQ99943.
SOURCEiSearch...

Gene expression databases

BgeeiQ99943.
CleanExiHS_AGPAT1.
ExpressionAtlasiQ99943. baseline and differential.
GenevisibleiQ99943. HS.

Family and domain databases

InterProiIPR004552. AGP_acyltrans.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00530. AGP_acyltrn. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells."
    West J., Tompkins C.K., Balantac N., Nudelman E., Meengs B., White T., Bursten S., Coleman J., Kumar A., Singer J.W., Leung D.W.
    DNA Cell Biol. 16:691-701(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases."
    Stamps A.C., Elmore M.A., Hill M.E., Kelly K., Makda A.A., Finnen M.J.
    Biochem. J. 326:455-461(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex."
    Aguado B., Campbell R.D.
    J. Biol. Chem. 273:4096-4105(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
    Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
    Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain, Lung and Skin.
  8. "Human 1-acylglycerol-3-phosphate O-acyltransferase isoforms 1 and 2: biochemical characterization and inability to rescue hepatic steatosis in Agpat2(-/-) gene lipodystrophic mice."
    Agarwal A.K., Sukumaran S., Cortes V.A., Tunison K., Mizrachi D., Sankella S., Gerard R.D., Horton J.D., Garg A.
    J. Biol. Chem. 286:37676-37691(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPLCA_HUMAN
AccessioniPrimary (citable) accession number: Q99943
Secondary accession number(s): A2BFI5, Q5BL03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: July 22, 2015
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.