FKBP8
entrez
23770
canonical
uniprot
Q14318
canonical
ensembl
ENSG00000105701
resolver
ensp
ENSP00000222308
resolver
ensp
ENSP00000476767
resolver
genesymbol
FKBP8
resolver
genesymbol_syn
FKBP38
resolver
hgnc
HGNC:3724
resolver
uniprot
B2R8G6
resolver
uniprot
C8C9T5
resolver
uniprot
Q53GU3
resolver
uniprot
Q7Z349
resolver
uniprot
Q86YK6
resolver
uniprot_entry
B2R8G6_HUMAN
resolver
uniprot_entry
FKBP8_HUMAN
resolver
uniprot_sec
C8C9T5
resolver
uniprot_sec
Q53GU3
resolver
uniprot_sec
Q7Z349
resolver
uniprot_sec
Q86YK6
resolver
amino_acid_sequence
MASCAEPSEPSAPLPAGVPPLEDFEVLDGVEDAEGEEEEEEEEEEEDDLSELPPLEDMGQPPAEEAEQPGALAREFLAAMEPEPAPAPAPEEWLDILGNGLLRKKTLVPGPPGSSRPVKGQVVTVHLQTSLENGTRVQEEPELVFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAVDGPDLEMLTGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSSAKVDMTFEEEAQLLQLKVKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKHAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN
uniprot
proteins
ec_number
5.2.1.8
uniprot
proteins
function
FUNCTION: Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis. Involved in the inhibition of viral infection by influenza A viruses (IAV) (PubMed:28169297). {ECO:0000269|PubMed:12510191, ECO:0000269|PubMed:15757646, ECO:0000269|PubMed:16176796, ECO:0000269|PubMed:28169297}.
uniprot
proteins
mass_dalton
44562
uniprot
proteins
mutagenesis
MUTAGEN 149; /note="D->N: Abolishes calcium-binding and reduces affinity for BCL2; when associated with Asn-151."; /evidence="ECO:0000269|PubMed:20140889"; MUTAGEN 151; /note="D->N: Abolishes calcium-binding and reduces affinity for BCL2; when associated with Asn-149."; /evidence="ECO:0000269|PubMed:20140889
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000269|PubMed:25621951}.
uniprot
proteins
pubmed
12510191
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15105374
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15733859
uniprot
proteins
pubmed
15757646
uniprot
proteins
pubmed
15990872
uniprot
proteins
pubmed
16176796
uniprot
proteins
pubmed
16604427
uniprot
proteins
pubmed
16844119
uniprot
proteins
pubmed
17090549
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18385096
uniprot
proteins
pubmed
18459960
uniprot
proteins
pubmed
20140889
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25621951
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28169297
uniprot
proteins
pubmed
40246839
uniprot
proteins
pubmed
7543869
uniprot
proteins
sequence_length
412
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16176796}. Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein; Cytoplasmic side {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion membrane {ECO:0000269|PubMed:12510191, ECO:0000269|PubMed:18385096}; Single-pass membrane protein; Cytoplasmic side {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion membrane {ECO:0000269|PubMed:18385096}; Single-pass membrane protein; Cytoplasmic side {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 390..410; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins