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Protein

Glycerol-3-phosphate acyltransferase 1, mitochondrial

Gene

GPAM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.By similarity1 Publication

Catalytic activityi

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

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 1 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 1, mitochondrial (GPAM), Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAM), Glycerol-3-phosphate acyltransferase 4 (GPAT4), Glycerol-3-phosphate acyltransferase 3 (GPAT3), Glycerol-3-phosphate acyltransferase 1, mitochondrial, Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAM), Glycerol-3-phosphate acyltransferase 1, mitochondrial (DKFZp451B1115)
  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

  • glycerol-3-phosphate O-acyltransferase activity Source: UniProtKB
  • sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity Source: UniProtKB-EC

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:57678-MONOMER
ReactomeiR-HSA-1483166 Synthesis of PA
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
R-HSA-75109 Triglyceride biosynthesis
R-HSA-8931987 RUNX1 regulates estrogen receptor mediated transcription
UniPathwayiUPA00557; UER00612

Chemistry databases

SwissLipidsiSLP:000000094

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
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000119927.13
HGNCiHGNC:24865 GPAM
MIMi602395 gene
neXtProtiNX_Q9HCL2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini? – 471Mitochondrial intermembraneSequence analysis
Transmembranei472 – 494HelicalSequence analysisAdd BLAST23
Topological domaini495 – 574CytoplasmicSequence analysisAdd BLAST80
Transmembranei575 – 593HelicalSequence analysisAdd BLAST19
Topological domaini594 – 828Mitochondrial intermembraneSequence analysisAdd BLAST235

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi57678
OpenTargetsiENSG00000119927
PharmGKBiPA134983031

Chemistry databases

ChEMBLiCHEMBL3734642

Polymorphism and mutation databases

BioMutaiGPAM
DMDMi59803040

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000024690? – 828Glycerol-3-phosphate acyltransferase 1, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei380PhosphoserineBy similarity1
Modified residuei688PhosphoserineBy similarity1
Modified residuei695PhosphoserineCombined sources1
Modified residuei780N6-acetyllysineBy similarity1
Modified residuei784N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9HCL2
MaxQBiQ9HCL2
PaxDbiQ9HCL2
PeptideAtlasiQ9HCL2
PRIDEiQ9HCL2

PTM databases

iPTMnetiQ9HCL2
PhosphoSitePlusiQ9HCL2

Expressioni

Gene expression databases

BgeeiENSG00000119927
CleanExiHS_GPAM
ExpressionAtlasiQ9HCL2 baseline and differential
GenevisibleiQ9HCL2 HS

Organism-specific databases

HPAiHPA046339
HPA060090

Interactioni

Protein-protein interaction databases

BioGridi121707, 13 interactors
IntActiQ9HCL2, 1 interactor
MINTiQ9HCL2
STRINGi9606.ENSP00000265276

Structurei

3D structure databases

ProteinModelPortaliQ9HCL2
SMRiQ9HCL2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi230 – 235HXXXXD motif6

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

eggNOGiKOG3729 Eukaryota
COG2937 LUCA
GeneTreeiENSGT00520000055570
HOGENOMiHOG000112780
HOVERGENiHBG000102
InParanoidiQ9HCL2
KOiK00629
OMAiKKNESLW
OrthoDBiEOG091G0IKA
PhylomeDBiQ9HCL2
TreeFamiTF313360

Family and domain databases

InterProiView protein in InterPro
IPR022284 GPAT/DHAPAT
IPR028354 GPAT_PlsB
IPR002123 Plipid/glycerol_acylTrfase
PANTHERiPTHR12563 PTHR12563, 1 hit
PfamiView protein in Pfam
PF01553 Acyltransferase, 1 hit
PIRSFiPIRSF500064 GPAT, 1 hit
PIRSF000437 GPAT_DHAPAT, 1 hit
SMARTiView protein in SMART
SM00563 PlsC, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti204I → F in CAD89932 (PubMed:17974005).Curated1
Sequence conflicti652Q → R in CAD89932 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0505854S → Y. Corresponds to variant dbSNP:rs11549703Ensembl.1
Natural variantiVAR_05058643I → V. Corresponds to variant dbSNP:rs2792751Ensembl.1
Natural variantiVAR_050587131E → G. Corresponds to variant dbSNP:rs10787428Ensembl.1
Natural variantiVAR_050588386I → T. Corresponds to variant dbSNP:rs35019520Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL833093 mRNA Translation: CAD89932.1
AL391986 Genomic DNA No translation available.
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.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiGPAT1_HUMAN
AccessioniPrimary (citable) accession number: Q9HCL2
Secondary accession number(s): Q5VW51, Q86TA3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: February 15, 2005
Last modified: April 25, 2018
This is version 147 of the entry and version 3 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health