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Q9HCL2 (GPAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol-3-phosphate acyltransferase 1, mitochondrial

Short name=GPAT-1
EC=2.3.1.15
Gene names
Name:GPAM
Synonyms:GPAT1, KIAA1560
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length828 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Ref.5

Catalytic activity

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.

Subcellular location

Mitochondrion outer membrane; Multi-pass membrane protein By similarity.

Domain

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 similarities

Belongs to the GPAT/DAPAT family.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Phospholipid biosynthesis
Phospholipid metabolism
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityPolymorphism
   DomainTransit peptide
Transmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCDP-diacylglycerol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

acyl-CoA metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular lipid metabolic process

Traceable author statement. Source: Reactome

defense response to virus

Inferred from electronic annotation. Source: Ensembl

fatty acid homeostasis

Inferred from electronic annotation. Source: Ensembl

fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

interleukin-2 secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of activation-induced cell death of T cells

Inferred from electronic annotation. Source: Ensembl

phosphatidic acid biosynthetic process

Traceable author statement. Source: Reactome

phospholipid homeostasis

Inferred from electronic annotation. Source: Ensembl

phospholipid metabolic process

Traceable author statement. Source: Reactome

positive regulation of activated T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

regulation of cytokine secretion

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride biosynthetic process

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Traceable author statement. Source: Reactome

plasma membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionglycerol-3-phosphate O-acyltransferase activity

Inferred from mutant phenotype Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 828Glycerol-3-phosphate acyltransferase 1, mitochondrialPRO_0000024690

Regions

Topological domain? – 471Mitochondrial intermembrane Potential
Transmembrane472 – 49423Helical; Potential
Topological domain495 – 57480Cytoplasmic Potential
Transmembrane575 – 59319Helical; Potential
Topological domain594 – 828235Mitochondrial intermembrane Potential
Motif230 – 2356HXXXXD motif

Amino acid modifications

Modified residue3801Phosphoserine By similarity
Modified residue6881Phosphoserine By similarity
Modified residue6951Phosphoserine Ref.6
Modified residue7801N6-acetyllysine By similarity
Modified residue7841N6-acetyllysine By similarity

Natural variations

Natural variant41S → Y.
Corresponds to variant rs11549703 [ dbSNP | Ensembl ].
VAR_050585
Natural variant431I → V.
Corresponds to variant rs2792751 [ dbSNP | Ensembl ].
VAR_050586
Natural variant1311E → G.
Corresponds to variant rs10787428 [ dbSNP | Ensembl ].
VAR_050587
Natural variant3861I → T.
Corresponds to variant rs35019520 [ dbSNP | Ensembl ].
VAR_050588

Experimental info

Sequence conflict2041I → F in CAD89932. Ref.1
Sequence conflict6521Q → R in CAD89932. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9HCL2 [UniParc].

Last modified February 15, 2005. Version 3.
Checksum: 7AADD21BC8684693

FASTA82893,795
        10         20         30         40         50         60 
MDESALTLGT IDVSYLPHSS EYSVGRCKHT SEEWGECGFR PTIFRSATLK WKESLMSRKR 

        70         80         90        100        110        120 
PFVGRCCYSC TPQSWDKFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YVLFIQERDV 

       130        140        150        160        170        180 
HKGMFATNVT ENVLNSSRVQ EAIAEVAAEL NPDGSAQQQS KAVNKVKKKA KRILQEMVAT 

       190        200        210        220        230        240 
VSPAMIRLTG WVLLKLFNSF FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT 

       250        260        270        280        290        300 
FILFCHNIKA PYIASGNNLN IPIFSTLIHK LGGFFIRRRL DETPDGRKDV LYRALLHGHI 

       310        320        330        340        350        360 
VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS TNVIPDILII PVGISYDRII 

       370        380        390        400        410        420 
EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGCVRVDF AQPFSLKEYL ESQSQKPVSA 

       430        440        450        460        470        480 
LLSLEQALLP AILPSRPSDA ADEGRDTSIN ESRNATDESL RRRLIANLAE HILFTASKSC 

       490        500        510        520        530        540 
AIMSTHIVAC LLLYRHRQGI DLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL 

       550        560        570        580        590        600 
GNCVTITHTS RNDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSL YAVLNKRGLG 

       610        620        630        640        650        660 
GPTSTPPNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCHETVGKF IQYGILTVAE 

       670        680        690        700        710        720 
HDDQEDISPS LAEQQWDKKL PEPLSWRSDE EDEDSDFGEE QRDCYLKVSQ SKEHQQFITF 

       730        740        750        760        770        780 
LQRLLGPLLE AYSSAAIFVH NFSGPVPEPE YLQKLHKYLI TRTERNVAVY AESATYCLVK 

       790        800        810        820 
NAVKMFKDIG VFKETKQKRV SVLELSSTFL PQCNRQKLLE YILSFVVL 

« Hide

References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Spinal cord.
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-828.
Tissue: Brain.
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase."
Chen Y.Q., Kuo M.-S., Li S., Bui H.H., Peake D.A., Sanders P.E., Thibodeaux S.J., Chu S., Qian Y.-W., Zhao Y., Bredt D.S., Moller D.E., Konrad R.J., Beigneux A.P., Young S.G., Cao G.
J. Biol. Chem. 283:10048-10057(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL833093 mRNA. Translation: CAD89932.1.
AL391986 Genomic DNA. Translation: CAH73716.1.
AB046780 mRNA. Translation: BAB13386.1.
RefSeqNP_001231878.1. NM_001244949.1.
NP_065969.3. NM_020918.5.
XP_005270055.1. XM_005269998.1.
UniGeneHs.42586.

3D structure databases

ProteinModelPortalQ9HCL2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121707. 2 interactions.
IntActQ9HCL2. 1 interaction.
STRING9606.ENSP00000265276.

PTM databases

PhosphoSiteQ9HCL2.

Polymorphism databases

DMDM59803040.

Proteomic databases

PaxDbQ9HCL2.
PRIDEQ9HCL2.

Protocols and materials databases

DNASU57678.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000348367; ENSP00000265276; ENSG00000119927.
ENST00000423155; ENSP00000409242; ENSG00000119927.
GeneID57678.
KEGGhsa:57678.
UCSCuc001kzp.3. human.

Organism-specific databases

CTD57678.
GeneCardsGC10M113899.
HGNCHGNC:24865. GPAM.
HPAHPA046339.
MIM602395. gene.
neXtProtNX_Q9HCL2.
PharmGKBPA134983031.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2937.
HOGENOMHOG000112780.
HOVERGENHBG000102.
InParanoidQ9HCL2.
KOK00629.
OMAKKNESLW.
OrthoDBEOG74R1PZ.
PhylomeDBQ9HCL2.
TreeFamTF313360.

Enzyme and pathway databases

BioCycMetaCyc:57678-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00557; UER00612.

Gene expression databases

ArrayExpressQ9HCL2.
BgeeQ9HCL2.
CleanExHS_GPAM.
GenevestigatorQ9HCL2.

Family and domain databases

InterProIPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERPTHR12563. PTHR12563. 1 hit.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFPIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGPAM. human.
GeneWikiGPAM.
GenomeRNAi57678.
NextBio64486.
PROQ9HCL2.
SOURCESearch...

Entry information

Entry nameGPAT1_HUMAN
AccessionPrimary (citable) accession number: Q9HCL2
Secondary accession number(s): Q5VW51, Q86TA3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM