Fkbp8
entrez
290652
canonical
uniprot
Q3B7U9
canonical
ensembl
ENSRNOG00000058359
resolver
ensembl
ENSRNOG00055003640
resolver
ensembl
ENSRNOG00060009606
resolver
ensembl
ENSRNOG00065024000
resolver
ensp
ENSRNOP00000074539
resolver
ensp
ENSRNOP00000087668
resolver
ensp
ENSRNOP00055004283
resolver
ensp
ENSRNOP00060012686
resolver
ensp
ENSRNOP00065033619
resolver
enst
ENSRNOT00055005707
resolver
enst
ENSRNOT00060016239
resolver
enst
ENSRNOT00065041170
resolver
genesymbol
Fkbp8
resolver
uniprot_entry
FKBP8_RAT
resolver
amino_acid_sequence
MASWAEPSEPAAQLLCGAPLLEGFEVLDGVDDAEEEDDLSGLPPLEDMGQPTVEEAEQPGALAREFLAATEPEPAPAPAPEEWLDILGNGLLRKKTLVPGPTGSSRPLKGQVVTVHLQMSLENGTRVQEEPELAFTLGDCDVIQALDLSVPLMHVGETAMVTADSKYCYGPQGSRSPYIPPHAALCLEVTLKTAEDGPDLEMLSGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSNAKVDMTCEEEEELLQLKVKCLNNLAASQLKLDHYRAALRSCSQVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKRAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN
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 (By similarity). {ECO:0000250}.
uniprot
proteins
mass_dalton
43556
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q14318}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
403
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 381..401; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins