GPAM
entrez
57678
canonical
uniprot
Q9HCL2
canonical
ensembl
ENSG00000119927
resolver
ensp
ENSP00000265276
resolver
ensp
ENSP00000571894
resolver
ensp
ENSP00000571895
resolver
ensp
ENSP00000571896
resolver
ensp
ENSP00000571897
resolver
ensp
ENSP00000571898
resolver
ensp
ENSP00000571899
resolver
ensp
ENSP00000571900
resolver
ensp
ENSP00000571901
resolver
ensp
ENSP00000571902
resolver
ensp
ENSP00000571903
resolver
enst
ENST00000348367
resolver
enst
ENST00000901835
resolver
enst
ENST00000901836
resolver
enst
ENST00000901837
resolver
enst
ENST00000901838
resolver
enst
ENST00000901839
resolver
enst
ENST00000901840
resolver
enst
ENST00000901841
resolver
enst
ENST00000901842
resolver
enst
ENST00000901843
resolver
enst
ENST00000901844
resolver
genesymbol
GPAM
resolver
genesymbol_syn
GPAT1
resolver
genesymbol_syn
KIAA1560
resolver
hgnc
HGNC:24865
resolver
uniprot
Q5VW51
resolver
uniprot
Q86TA3
resolver
uniprot
Q8N1G6
resolver
uniprot_entry
GPAT1_HUMAN
resolver
uniprot_entry
Q8N1G6_HUMAN
resolver
uniprot_sec
Q5VW51
resolver
uniprot_sec
Q86TA3
resolver
amino_acid_sequence
MDESALTLGTIDVSYLPHSSEYSVGRCKHTSEEWGECGFRPTIFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKRILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLLFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDVLYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNVIPDILIIPVGISYDRIIEGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSALLSLEQALLPAILPSRPSDAADEGRDTSINESRNATDESLRRRLIANLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLLGNCVTITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLNKRGLGGPTSTPPNLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQVCHETVGKFIQYGILTVAEHDDQEDISPSLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAIFVHNFSGPVPEPEYLQKLHKYLITRTERNVAVYAESATYCLVKNAVKMFKDIGVFKETKQKRVSVLELSSTFLPQCNRQKLLEYILSFVVL
uniprot
proteins
ec_number
2.3.1.15
uniprot
proteins
function
FUNCTION: Mitochondrial membrane protein that catalyzes the essential first step of biosynthesis of glycerolipids such as triglycerides, phosphatidic acids and lysophosphatidic acids (PubMed:18238778, PubMed:19075029, PubMed:36522428). Esterifies acyl-group from acyl-coenzyme A (acyl-CoA) to the sn-1 position of glycerol-3-phosphate, to produce lysophosphatidic acid (PubMed:18238778). Has a narrow hydrophobic binding cleft that selects for a linear acyl chain (PubMed:36522428). Catalytic activity is higher for substrates with a 16-carbon acyl chain (PubMed:36522428). {ECO:0000269|PubMed:18238778, ECO:0000269|PubMed:19075029, ECO:0000269|PubMed:36522428}.
uniprot
proteins
mass_dalton
93795
uniprot
proteins
mutagenesis
MUTAGEN 89; /note="R->E: Abrogates mitochondrial localization; when associated with E-98, E-100, E-101, E-102, E-107, E-108 and E-118."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 98; /note="H->E: Abrogates mitochondrial localization; when associated with E-89, E-100, E-101, E-102, E-107, E-108 and E-118."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 100; /note="R->E: Abrogates mitochondrial localization; when associated with E-89, E-98, E-101, E-102, E-107, E-108 and E-118."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 101; /note="H->E: Abrogates mitochondrial localization; when associated with E-89, E-98, E-100, E-102, E-107, E-108 and E-118."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 102; /note="R->E: Abrogates mitochondrial localization; when associated with E-89, E-98, E-100, E-101, E-107, E-108 and E-118."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 107; /note="R->E: Abrogates mitochondrial localization; when associated with E-89, E-98, E-100, E-101, E-102, E-108 and E-118."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 108; /note="R->E: Abrogates mitochondrial localization; when associated with E-89, E-98, E-100, E-101, E-102, E-107 and E-118."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 118; /note="R->E: Abrogates mitochondrial localization; when associated with E-89, E-98, E-100, E-101, E-102, E-107 and E-108."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 230; /note="H->A: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 233; /note="H->W: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 273; /note="G->L: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 278; /note="R->A: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 313; /note="F->A: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 318; /note="R->A: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:36522428"; MUTAGEN 388; /note="M->W: Impairs catalytic activity."; /evidence="ECO:0000269|PubMed:36522428
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. {ECO:0000269|PubMed:18238778}.
uniprot
proteins
protein_family
GPAT/DAPAT family
uniprot
proteins
pubmed
10997877
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18238778
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
19075029
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
36522428
uniprot
proteins
sequence_length
828
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:36522428}; Peripheral membrane protein {ECO:0000269|PubMed:36522428}. Note=Associated with the mitochondrion outer membrane of hepatic cells via a patch of basic residues. {ECO:0000269|PubMed:36522428}.
uniprot
proteins