SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q99943

- PLCA_HUMAN

UniProt

Q99943 - PLCA_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
Gene
AGPAT1, G15
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Pathwayi

GO - Molecular functioni

  1. 1-acylglycerol-3-phosphate O-acyltransferase activity Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  1. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  2. cellular lipid metabolic process Source: Reactome
  3. energy reserve metabolic process Source: Reactome
  4. glycerophospholipid biosynthetic process Source: Reactome
  5. phosphatidic acid biosynthetic process Source: BHF-UCL
  6. phospholipid metabolic process Source: Reactome
  7. positive regulation of cellular metabolic process Source: Reactome
  8. positive regulation of cytokine production Source: BHF-UCL
  9. positive regulation of cytokine-mediated signaling pathway Source: BHF-UCL
  10. small molecule metabolic process Source: Reactome
  11. triglyceride biosynthetic process Source: Reactome
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: Chromosome 6

Organism-specific databases

HGNCiHGNC:324. AGPAT1.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei38 – 5821Helical; Reviewed prediction
Add
BLAST
Transmembranei128 – 14821Helical; Reviewed prediction
Add
BLAST
Transmembranei193 – 21321Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24621.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626 Reviewed prediction
Add
BLAST
Chaini27 – 2832571-acyl-sn-glycerol-3-phosphate acyltransferase alpha
PRO_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

ArrayExpressiQ99943.
BgeeiQ99943.
CleanExiHS_AGPAT1.
GenevestigatoriQ99943.

Interactioni

Protein-protein interaction databases

BioGridi115805. 6 interactions.
IntActiQ99943. 2 interactions.
STRINGi9606.ENSP00000401287.

Structurei

3D structure databases

ProteinModelPortaliQ99943.

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.
HOGENOMiHOG000026375.
HOVERGENiHBG000676.
InParanoidiQ99943.
KOiK13509.
OMAiCALRGRN.
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

MDLWPGAWML LLLLFLLLLF LLPTLWFCSP SAKYFFKMAF YNGWILFLAV    50
LAIPVCAVRG RNVENMKILR LMLLHIKYLY GIRVEVRGAH HFPPSQPYVV 100
VSNHQSSLDL LGMMEVLPGR CVPIAKRELL WAGSAGLACW LAGVIFIDRK 150
RTGDAISVMS EVAQTLLTQD VRVWVFPEGT RNHNGSMLPF KRGAFHLAVQ 200
AQVPIVPIVM SSYQDFYCKK ERRFTSGQCQ VRVLPPVPTE GLTPDDVPAL 250
ADRVRHSMLT VFREISTDGR GGGDYLKKPG GGG 283
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.

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:
EMBL
GenBank
DDBJ
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.
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.

Polymorphism databases

DMDMi3914372.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4744.1.
RefSeqi NP_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.
UniGenei Hs.409230.

3D structure databases

ProteinModelPortali Q99943.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115805. 6 interactions.
IntActi Q99943. 2 interactions.
STRINGi 9606.ENSP00000401287.

Chemistry

ChEMBLi CHEMBL3583.

PTM databases

PhosphoSitei Q99943.

Polymorphism databases

DMDMi 3914372.

Proteomic databases

MaxQBi Q99943.
PaxDbi Q99943.
PRIDEi Q99943.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336984 ; 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 .
GeneIDi 10554.
KEGGi hsa:10554.
UCSCi uc003oae.3. human.

Organism-specific databases

CTDi 10554.
GeneCardsi GC06M032135.
GC06Mi32147.
GC06Mj32084.
GC06Ml32175.
GC06Mm32212.
GC06Mn32093.
GC06Mo32142.
HGNCi HGNC:324. AGPAT1.
MIMi 603099. gene.
neXtProti NX_Q99943.
PharmGKBi PA24621.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0204.
HOGENOMi HOG000026375.
HOVERGENi HBG000676.
InParanoidi Q99943.
KOi K13509.
OMAi CALRGRN.
PhylomeDBi Q99943.
TreeFami TF314867.

Enzyme and pathway databases

UniPathwayi UPA00557 ; UER00613 .
BioCyci MetaCyc:HS09762-MONOMER.
BRENDAi 2.3.1.51. 2681.
Reactomei REACT_1190. Triglyceride Biosynthesis.
REACT_120906. Synthesis of PA.
REACT_2122. ChREBP activates metabolic gene expression.

Miscellaneous databases

GeneWikii AGPAT1.
GenomeRNAii 10554.
NextBioi 40041.
PROi Q99943.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99943.
Bgeei Q99943.
CleanExi HS_AGPAT1.
Genevestigatori Q99943.

Family and domain databases

InterProi IPR004552. AGP_acyltrans.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view ]
Pfami PF01553. Acyltransferase. 1 hit.
[Graphical view ]
SMARTi SM00563. PlsC. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00530. AGP_acyltrn. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 131 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