BIRC7
entrez
79444
canonical
uniprot
Q96CA5
canonical
ensembl
ENSG00000101197
resolver
ensp
ENSP00000217169
resolver
ensp
ENSP00000345213
resolver
genesymbol
BIRC7
resolver
genesymbol_syn
KIAP
resolver
genesymbol_syn
LIVIN
resolver
genesymbol_syn
MLIAP
resolver
genesymbol_syn
RNF50
resolver
hgnc
HGNC:13702
resolver
uniprot
Q9BQV0
resolver
uniprot
Q9H2A8
resolver
uniprot
Q9HAP7
resolver
uniprot_entry
BIRC7_HUMAN
resolver
uniprot_sec
Q9BQV0
resolver
uniprot_sec
Q9H2A8
resolver
uniprot_sec
Q9HAP7
resolver
amino_acid_sequence
MGPKDSAKCLHRGPQPSHWAAGDGPTQERCGPRSLGSPVLGLDTCRAWDHVDGQILGQLRPLTEEEEEEGAGATLSRGPAFPGMGSEELRLASFYDWPLTAEVPPELLAAAGFFHTGHQDKVRCFFCYGGLQSWKRGDDPWTEHAKWFPSCQFLLRSKGRDFVHSVQETHSQLLGSWDPWEEPEDAAPVAPSVPASGYPELPTPRREVQSESAQEPGGVSPAEAQRAWWVLEPPGARDVEAQLRRLQEERTCKVCLDRAVSIVFVPCGHLVCAECAPGLQLCPICRAPVRSRVRTFLS
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control (PubMed:11024045, PubMed:11084335, PubMed:11162435, PubMed:16729033, PubMed:17294084). Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity (PubMed:11024045, PubMed:16729033). As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival (PubMed:16729033). May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions (PubMed:16729033). Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine (PubMed:11084335, PubMed:11162435, PubMed:11865055). Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2 (PubMed:11865055). This activation depends on TAB1 and MAP3K7/TAK1 (PubMed:11865055). In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9 (PubMed:11024045). {ECO:0000269|PubMed:11024045, ECO:0000269|PubMed:11084335, ECO:0000269|PubMed:11162435, ECO:0000269|PubMed:11865055, ECO:0000269|PubMed:16729033, ECO:0000269|PubMed:17294084}.; FUNCTION: [Isoform 1]: Blocks staurosporine-induced apoptosis (PubMed:11322947). Promotes natural killer (NK) cell-mediated killing (PubMed:18034418). {ECO:0000269|PubMed:11322947, ECO:0000269|PubMed:18034418}.; FUNCTION: [Isoform 2]: Blocks etoposide-induced apoptosis (PubMed:11162435, PubMed:11322947). Protects against natural killer (NK) cell-mediated killing (PubMed:18034418). {ECO:0000269|PubMed:11162435, ECO:0000269|PubMed:11322947, ECO:0000269|PubMed:18034418}.
uniprot
proteins
mass_dalton
32798
uniprot
proteins
mutagenesis
MUTAGEN 87..88; /note="EE->AA: No change in SMAC interaction and anti-apoptotic activity."; /evidence="ECO:0000269|PubMed:11084335"; MUTAGEN 120; /note="D->A: Abolishes inhibition of caspases, SMAC binding and anti-apoptotic activity."; /evidence="ECO:0000269|PubMed:11084335"; MUTAGEN 124; /note="C->A: Abolishes inhibition of caspases and anti-apoptotic activity."; /evidence="ECO:0000269|PubMed:11084335"; MUTAGEN 138; /note="D->A: Abolishes inhibition of caspases, SMAC binding and anti-apoptotic activity."; /evidence="ECO:0000269|PubMed:11084335
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated and undergoes proteasome-mediated degradation.; PTM: The truncated protein (tLivin) not only loses its anti-apoptotic effect but also acquires a pro-apoptotic effect.
uniprot
proteins
protein_family
IAP family
uniprot
proteins
pubmed
11024045
uniprot
proteins
pubmed
11084335
uniprot
proteins
pubmed
11162435
uniprot
proteins
pubmed
11322947
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
11801603
uniprot
proteins
pubmed
11865055
uniprot
proteins
pubmed
12846571
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15485396
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16729033
uniprot
proteins
pubmed
17294084
uniprot
proteins
pubmed
18034418
uniprot
proteins
pubmed
19074843
uniprot
proteins
pubmed
21617971
uniprot
proteins
sequence_length
298
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17294084}. Cytoplasm {ECO:0000269|PubMed:17294084}. Golgi apparatus {ECO:0000269|PubMed:17294084}. Note=Nuclear, and in a filamentous pattern throughout the cytoplasm. Full-length livin is detected exclusively in the cytoplasm, whereas the truncated form (tLivin) is found in the peri-nuclear region with marked localization to the Golgi apparatus; the accumulation of tLivin in the nucleus shows positive correlation with the increase in apoptosis.
uniprot
proteins