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Q9HCL2

- GPAT1_HUMAN

UniProt

Q9HCL2 - GPAT1_HUMAN

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Protein

Glycerol-3-phosphate acyltransferase 1, mitochondrial

Gene

GPAM

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

Functioni

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

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. glycerol-3-phosphate O-acyltransferase activity Source: UniProtKB

GO - Biological processi

  1. acyl-CoA metabolic process Source: Ensembl
  2. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  3. cellular lipid metabolic process Source: Reactome
  4. defense response to virus Source: Ensembl
  5. fatty acid homeostasis Source: Ensembl
  6. fatty acid metabolic process Source: Ensembl
  7. glycerophospholipid biosynthetic process Source: Reactome
  8. interleukin-2 secretion Source: Ensembl
  9. negative regulation of activation-induced cell death of T cells Source: Ensembl
  10. phosphatidic acid biosynthetic process Source: Reactome
  11. phospholipid homeostasis Source: Ensembl
  12. phospholipid metabolic process Source: Reactome
  13. positive regulation of activated T cell proliferation Source: Ensembl
  14. positive regulation of multicellular organism growth Source: Ensembl
  15. regulation of cytokine secretion Source: Ensembl
  16. response to glucose Source: Ensembl
  17. small molecule metabolic process Source: Reactome
  18. triglyceride biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:57678-MONOMER.
ReactomeiREACT_1190. Triglyceride Biosynthesis.
REACT_120906. Synthesis of PA.
REACT_147904. Activation of gene expression by SREBF (SREBP).
UniPathwayiUPA00557; UER00612.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 1, mitochondrial (EC:2.3.1.15)
Short name:
GPAT-1
Gene namesi
Name:GPAM
Synonyms:GPAT1, KIAA1560
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:24865. GPAM.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrial outer membrane Source: Reactome
  4. plasma membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134983031.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 828Glycerol-3-phosphate acyltransferase 1, mitochondrialPRO_0000024690
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei380 – 3801PhosphoserineBy similarity
Modified residuei688 – 6881PhosphoserineBy similarity
Modified residuei695 – 6951Phosphoserine1 Publication
Modified residuei780 – 7801N6-acetyllysineBy similarity
Modified residuei784 – 7841N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9HCL2.
PaxDbiQ9HCL2.
PRIDEiQ9HCL2.

PTM databases

PhosphoSiteiQ9HCL2.

Expressioni

Gene expression databases

BgeeiQ9HCL2.
CleanExiHS_GPAM.
ExpressionAtlasiQ9HCL2. baseline and differential.
GenevestigatoriQ9HCL2.

Organism-specific databases

HPAiHPA046339.

Interactioni

Protein-protein interaction databases

BioGridi121707. 3 interactions.
IntActiQ9HCL2. 1 interaction.
STRINGi9606.ENSP00000265276.

Structurei

3D structure databases

ProteinModelPortaliQ9HCL2.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini? – 471Mitochondrial intermembraneSequence Analysis
Topological domaini495 – 57480CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini594 – 828235Mitochondrial intermembraneSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei472 – 49423HelicalSequence AnalysisAdd
BLAST
Transmembranei575 – 59319HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi230 – 2356HXXXXD 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

Belongs to the GPAT/DAPAT family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2937.
GeneTreeiENSGT00520000055570.
HOGENOMiHOG000112780.
HOVERGENiHBG000102.
InParanoidiQ9HCL2.
KOiK00629.
OMAiKKNESLW.
OrthoDBiEOG74R1PZ.
PhylomeDBiQ9HCL2.
TreeFamiTF313360.

Family and domain databases

InterProiIPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9HCL2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDESALTLGT IDVSYLPHSS EYSVGRCKHT SEEWGECGFR PTIFRSATLK
60 70 80 90 100
WKESLMSRKR PFVGRCCYSC TPQSWDKFFN PSIPSLGLRN VIYINETHTR
110 120 130 140 150
HRGWLARRLS YVLFIQERDV HKGMFATNVT ENVLNSSRVQ EAIAEVAAEL
160 170 180 190 200
NPDGSAQQQS KAVNKVKKKA KRILQEMVAT VSPAMIRLTG WVLLKLFNSF
210 220 230 240 250
FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT FILFCHNIKA
260 270 280 290 300
PYIASGNNLN IPIFSTLIHK LGGFFIRRRL DETPDGRKDV LYRALLHGHI
310 320 330 340 350
VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS TNVIPDILII
360 370 380 390 400
PVGISYDRII EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGCVRVDF
410 420 430 440 450
AQPFSLKEYL ESQSQKPVSA LLSLEQALLP AILPSRPSDA ADEGRDTSIN
460 470 480 490 500
ESRNATDESL RRRLIANLAE HILFTASKSC AIMSTHIVAC LLLYRHRQGI
510 520 530 540 550
DLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL GNCVTITHTS
560 570 580 590 600
RNDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSL YAVLNKRGLG
610 620 630 640 650
GPTSTPPNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCHETVGKF
660 670 680 690 700
IQYGILTVAE HDDQEDISPS LAEQQWDKKL PEPLSWRSDE EDEDSDFGEE
710 720 730 740 750
QRDCYLKVSQ SKEHQQFITF LQRLLGPLLE AYSSAAIFVH NFSGPVPEPE
760 770 780 790 800
YLQKLHKYLI TRTERNVAVY AESATYCLVK NAVKMFKDIG VFKETKQKRV
810 820
SVLELSSTFL PQCNRQKLLE YILSFVVL
Length:828
Mass (Da):93,795
Last modified:February 15, 2005 - v3
Checksum:i7AADD21BC8684693
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041I → F in CAD89932. (PubMed:17974005)Curated
Sequence conflicti652 – 6521Q → R in CAD89932. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41S → Y.
Corresponds to variant rs11549703 [ dbSNP | Ensembl ].
VAR_050585
Natural varianti43 – 431I → V.
Corresponds to variant rs2792751 [ dbSNP | Ensembl ].
VAR_050586
Natural varianti131 – 1311E → G.
Corresponds to variant rs10787428 [ dbSNP | Ensembl ].
VAR_050587
Natural varianti386 – 3861I → T.
Corresponds to variant rs35019520 [ dbSNP | Ensembl ].
VAR_050588

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL833093 mRNA. Translation: CAD89932.1.
AL391986 Genomic DNA. Translation: CAH73716.1.
AB046780 mRNA. Translation: BAB13386.1.
CCDSiCCDS7570.1.
RefSeqiNP_001231878.1. NM_001244949.1.
NP_065969.3. NM_020918.5.
XP_005270055.1. XM_005269998.1.
UniGeneiHs.42586.

Genome annotation databases

EnsembliENST00000348367; ENSP00000265276; ENSG00000119927.
GeneIDi57678.
KEGGihsa:57678.
UCSCiuc001kzp.3. human.

Polymorphism databases

DMDMi59803040.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL833093 mRNA. Translation: CAD89932.1 .
AL391986 Genomic DNA. Translation: CAH73716.1 .
AB046780 mRNA. Translation: BAB13386.1 .
CCDSi CCDS7570.1.
RefSeqi NP_001231878.1. NM_001244949.1.
NP_065969.3. NM_020918.5.
XP_005270055.1. XM_005269998.1.
UniGenei Hs.42586.

3D structure databases

ProteinModelPortali Q9HCL2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121707. 3 interactions.
IntActi Q9HCL2. 1 interaction.
STRINGi 9606.ENSP00000265276.

PTM databases

PhosphoSitei Q9HCL2.

Polymorphism databases

DMDMi 59803040.

Proteomic databases

MaxQBi Q9HCL2.
PaxDbi Q9HCL2.
PRIDEi Q9HCL2.

Protocols and materials databases

DNASUi 57678.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000348367 ; ENSP00000265276 ; ENSG00000119927 .
GeneIDi 57678.
KEGGi hsa:57678.
UCSCi uc001kzp.3. human.

Organism-specific databases

CTDi 57678.
GeneCardsi GC10M113899.
HGNCi HGNC:24865. GPAM.
HPAi HPA046339.
MIMi 602395. gene.
neXtProti NX_Q9HCL2.
PharmGKBi PA134983031.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2937.
GeneTreei ENSGT00520000055570.
HOGENOMi HOG000112780.
HOVERGENi HBG000102.
InParanoidi Q9HCL2.
KOi K00629.
OMAi KKNESLW.
OrthoDBi EOG74R1PZ.
PhylomeDBi Q9HCL2.
TreeFami TF313360.

Enzyme and pathway databases

UniPathwayi UPA00557 ; UER00612 .
BioCyci MetaCyc:57678-MONOMER.
Reactomei REACT_1190. Triglyceride Biosynthesis.
REACT_120906. Synthesis of PA.
REACT_147904. Activation of gene expression by SREBF (SREBP).

Miscellaneous databases

ChiTaRSi GPAM. human.
GeneWikii GPAM.
GenomeRNAii 57678.
NextBioi 64486.
PROi Q9HCL2.
SOURCEi Search...

Gene expression databases

Bgeei Q9HCL2.
CleanExi HS_GPAM.
ExpressionAtlasi Q9HCL2. baseline and differential.
Genevestigatori Q9HCL2.

Family and domain databases

InterProi IPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view ]
PANTHERi PTHR12563. PTHR12563. 1 hit.
Pfami PF01553. Acyltransferase. 1 hit.
[Graphical view ]
PIRSFi PIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTi SM00563. PlsC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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.

Entry informationi

Entry nameiGPAT1_HUMAN
AccessioniPrimary (citable) accession number: Q9HCL2
Secondary accession number(s): Q5VW51, Q86TA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: February 15, 2005
Last modified: October 29, 2014
This is version 120 of the entry and version 3 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 10
    Human chromosome 10: 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