AGK
entrez
55750
canonical
uniprot
Q53H12
canonical
ensembl
ENSG00000006530
resolver
ensembl
ENSG00000262327
resolver
ensp
ENSP00000458417
resolver
ensp
ENSP00000496789
resolver
ensp
ENSP00000497280
resolver
ensp
ENSP00000497457
resolver
ensp
ENSP00000579165
resolver
ensp
ENSP00000665916
resolver
enst
ENST00000575872
resolver
enst
ENST00000650006
resolver
genesymbol
AGK
resolver
genesymbol_syn
MULK
resolver
hgnc
HGNC:21869
resolver
uniprot
A0A3B3ISZ0
resolver
uniprot
Q75KN1
resolver
uniprot
Q96GC3
resolver
uniprot
Q9NP48
resolver
uniprot_entry
A0A3B3ISZ0_HUMAN
resolver
uniprot_entry
AGK_HUMAN
resolver
uniprot_sec
Q75KN1
resolver
uniprot_sec
Q96GC3
resolver
uniprot_sec
Q9NP48
resolver
amino_acid_sequence
MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPTQ
uniprot
proteins
disease_involvement
DISEASE: Mitochondrial DNA depletion syndrome 10 (MTDPS10) [MIM:212350]: An autosomal recessive mitochondrial disorder characterized by congenital cataracts, hypertrophic cardiomyopathy, skeletal myopathy, exercise intolerance, and lactic acidosis. Mental development is normal, but affected individuals may die early from cardiomyopathy. {ECO:0000269|PubMed:22277967, ECO:0000269|PubMed:22284826, ECO:0000269|PubMed:23266196, ECO:0000269|PubMed:25208612, ECO:0000269|PubMed:28712726}. Note=The disease is caused by variants affecting the gene represented in this entry. The TIM22 complex and import of proteins into mitochondrion are affected in patients suffering of MTDPS10 (PubMed:28712726). {ECO:0000269|PubMed:28712726}.; DISEASE: Cataract 38 (CTRCT38) [MIM:614691]: An opacification of the crystalline lens of the eye becoming evident at birth. It frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. {ECO:0000269|PubMed:22415731}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.1.107
uniprot
proteins
ec_number
2.7.1.138
uniprot
proteins
ec_number
2.7.1.94
uniprot
proteins
function
FUNCTION: Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively (PubMed:15939762). Does not phosphorylate sphingosine (PubMed:15939762). Phosphorylates ceramide (By similarity). Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (By similarity). Independently of its lipid kinase activity, acts as a component of the TIM22 complex (PubMed:28712724, PubMed:28712726). The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force (PubMed:28712724, PubMed:28712726). In the TIM22 complex, required for the import of a subset of metabolite carriers into mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not required for the import of TIMM23 (PubMed:28712724). Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth (PubMed:15939762). {ECO:0000250|UniProtKB:Q9ESW4, ECO:0000269|PubMed:15939762, ECO:0000269|PubMed:28712724, ECO:0000269|PubMed:28712726}.
uniprot
proteins
mass_dalton
47137
uniprot
proteins
mutagenesis
MUTAGEN 126; /note="G->E: Abolishes lipid kinase activity. Does not affect ability to associate with the TIM22 complex and mediate import of transmembrane proteins into the mitochondrial inner membrane."; /evidence="ECO:0000269|PubMed:15939762, ECO:0000269|PubMed:28712724, ECO:0000269|PubMed:28712726
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000269|PubMed:15939762}.
uniprot
proteins
protein_family
AGK family
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15939762
uniprot
proteins
pubmed
16269826
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22277967
uniprot
proteins
pubmed
22284826
uniprot
proteins
pubmed
22415731
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23266196
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25208612
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28712724
uniprot
proteins
pubmed
28712726
uniprot
proteins
pubmed
37009826
uniprot
proteins
sequence_length
422
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:15939762, ECO:0000269|PubMed:16269826, ECO:0000269|PubMed:28712724, ECO:0000269|PubMed:28712726}; Peripheral membrane protein {ECO:0000269|PubMed:28712724}. Mitochondrion intermembrane space {ECO:0000269|PubMed:28712724, ECO:0000269|PubMed:28712726}. Note=Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane (PubMed:28712724). It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it (PubMed:28712724, PubMed:28712726). {ECO:0000269|PubMed:28712724, ECO:0000269|PubMed:28712726}.
uniprot
proteins