Birc6
entrez
12211
canonical
uniprot
O88738
canonical
ensembl
ENSMUSG00000024073
resolver
ensp
ENSMUSP00000136329
resolver
ensp
ENSMUSP00000138270
resolver
ensp
ENSMUSP00000138333
resolver
ensp
ENSMUSP00000138693
resolver
ensp
ENSMUSP00000138732
resolver
genesymbol
Birc6
resolver
genesymbol_syn
Kiaa1289
resolver
uniprot
A0A1S6GWH3
resolver
uniprot
E9PYU6
resolver
uniprot
Q3UYZ6
resolver
uniprot
Q69ZM5
resolver
uniprot
Q8BNX0
resolver
uniprot
Q8BR72
resolver
uniprot
Q8BRV7
resolver
uniprot
Q8C737
resolver
uniprot_entry
A0A1S6GWH3_MOUSE
resolver
uniprot_entry
BIRC6_MOUSE
resolver
uniprot_entry
Q3UYZ6_MOUSE
resolver
uniprot_sec
E9PYU6
resolver
uniprot_sec
Q69ZM5
resolver
uniprot_sec
Q8BNX0
resolver
uniprot_sec
Q8BR72
resolver
uniprot_sec
Q8BRV7
resolver
uniprot_sec
Q8C737
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by DIABLO/SMAC, which competes for the substrate-binding sites on BIRC6 (By similarity). BIRC6 inhibits caspases and protease by ubiquitination but BIRC6 itself is subjected to protease cleavage by CASP3, CASP6, CASP7, CASP9 and HTRA2 by protease cleavage (By similarity). {ECO:0000250|UniProtKB:Q9NR09}.
uniprot
proteins
amino_acid_sequence
MVTGCGAAPPGTVTERLPSVIVLSAGRKMAAAAAEASGPSCSSAAAAAGAGAAGVSEWLVLRDGCMRCDADGLHSLSYHPALNAILAVTSRGTIKVIDGTSGATLQASALSAKPGGQVKCQYISAVDKVIFVDDYAVGCRKDLNGILLLDTALQTPVSKQDDVVQLELPVTEAQQLLSACIEKIDVSSTEGYDLFITQLKDGLKNTSHETAANHKVAKWATVTFHLPHHVLKSIASAIVNELKKINQNVAALPVASSVMDRLSYLLPSARPELGVGPGRSVDRALMYSEANRRETFTSWPHVGYRWAQPDPMAQAGFYHQPASSGDDRAMCFTCSVCLVCWEPTDEPWSEHERHSPNCPFVKGEHTQNVPLSVTLATSPAQLPSADGADRIACFGSGSCPQFLAAATKRGKICIWDVSKLMKVHLKFEINAYDPAIVQQLILSGDPSSGVDSRRPTLAWLEDSSSCSDIPKLEGDSDDLLEDSDSEEHSRSDSVTGHTSQKEAMEVSLDITALSILQQPEKLQWEIVANVLEDTVKDLEELGANPSLTNSKSEKTKEKHQEQHNIPFPCLLAGGLLTYKSPATSPISSNSHRSLDGLSRTQGESISEQGSTDNESCTNSELNSPLVRRTLPVLLLYSIKESDEKAGKIFSQMNNIMSKSLHDDGFTVPQIIEMELDNQEQLLLQDPPVTYIQQFADAAASLTSPDSEKWNSVFPKPGALVQCLRLPKFAEEETLCIDSITPCADGIHLLVGLRTCSVESLSAINQVEALNNLNKLNSALCNRRKGDLESNLAVVNGANISVIQHESPADVPEHLLIRPEQRNVVSGGYLVLYKMNYTTRIVTLEEEPVKIQHIKDPQDTITSLILLPPDILDNREDDCEEPAEEMQLASKNGIEREKKSDISTLGHLVVTTQGGYVKVLDLSNFEILAKVEPPKKEGTEEQDTFVSVIYCSGTDRLCACTKGGELHFLQIGGTCDDIDEADILVDGSLSKGIEPALEGSRPLSNPSSPGISGVELLVDQPFTLEILTSLVELTRFETLTPRFSATVPPCWVEVQQEQQQRRHPQHLHQQHHGDAAQHTRTWKLQTDSNSWDEHVFELVLPKACMVGHVDFKFVLNSNITSVPQIQVTLLKNKAPGLGKANALNIEVEHNGNPSLVDLNEEMHHMDVEESQCLRLCPFLEDHKEDILCGPVWLASGLDLSGHAGMLTLTSPKLVKGMAGGKYRSFLIHVKAVSDRGAADEMCSSGLRPVVRLPSLKQQGHKGYSLASLLAKVAAGKEKSSNVKNENAGGTRKSENLRGCDLLQEVSVTIRRFKKTSICKERVQRCAMLQFSEFHEKLLNTLCRRSDDGQVTEHAQSLVLDALCWLAGVHSNGSGSSKEGNECLLSKTRKCLSDIVRVCFFEAGRSIAHKCARFLALCISNGKCEPCQPGFGSVLLKALLDNMCFLPAAATGGSVYWYFVLLNYVKDEDLAGCSTACAALLTAVSRQLQDRLTPLEALLQTRYGLYSSPFDPVLFDLEMSGSSWKTVYSSSTAVQSDEIDLSDVLSGNGRVSSCTAAEGSFTSLTGLLEVEPLHFTCVSTSDGTRIERDDASTFTVSSFGVPPAVGGLSSGTVGEASTALSSAAQVALQSLSHAMASAEQQLQVLQEKQQQLLKLQQQKAKLEAKLHQTTAAAAAAASAAAAAAAGPVHNAVPSNPVAAPGFFIHPSDVIPPTPKTTPLFMTPPLTPPNEAVSVVINAELAQLFPGSVIDPPAVNLAAQNKNSSKSRMNPLGSGLALAISHASHFLQPPPHQSIIIERMHSGARRFVTLDFGRPILLTDVLIPTCGDLASLSIDIWTLGEEVDGRRLVVATDISTHSLILHDLIPPPVCRFMKITVIGRYGSTNARAKIPLGFYYGHSYILPWESELKLMHDPLRGEGESASQPEIDQHLAMMVALQEDIQCRYNLACHRLEALLQSIDLPPLNSANNAQYFLRKPDKAVEEDSRVFSAYQDCIQLQLQLNLAHNAVQRLKVAIGASRKLLNETSGPEDLIQTSSTEQLRTIVRYLLDTLLSLLHSSNGHSVPAVLQSTFHAQACEELFKHLCISGTPKIRLHTGLLLVQLCGGERWWGQFLSNVLQELYNSEQLLIFPQDRVFMLLSCIGQRSLSNSGVLESLLNLLDNLLSPLQPELSMHRRTEGVLDIPMISWVVMLVSRLLDYVATVEDEAAAAKKPLNGKDRERFLTGNQWSFINNNLHTQNLNRSSKGGSSLDRLYSRKIRKQLVHHKQQLNLLKAKQKALVEQMEKEKIQSNKGSSYKLLVEQAKLKQATSKHFKDLIRLRRTAEWSRSNLDTEVTTTKESPEIEPLPFTLAHDRCISVVQKLVLFLLSMDFTCHADLLLFVCKVLARIANATRPTIHLCEIVNEPQLERLLLLLVGTDFNRGDISWGGAWAQYSLTCMLQDILAGELLAPVAAEAMEECTVSEDVGATAGDSDDSLQQSPAQLLETIDEPLTHEIAGTPPLSSLEKDKEIDLELLQDLMEVDIDPLDIDLEKDPLAAKVFKPISSTWYDYWGADYGTYNYNPYIGGLGMPVAKPPSNTEKNGSQTVSVSVSQALDARLEVGLEQQAELMLKMMSTLEADSILQALTNTSPTFSQSPTGTDDSLLGNLQPANQNSQLMIQLSSVPMLNVCFNKLFSMLQVHHVQLESLLQLWLTLSLNSSSSGNKENGADIFLYNANRIPVISLNQASIASFLTVLAWYPNTLLRTWCLVLHSLTLMTNMQLNSGSSSSIGIQETTAHLLVSDPNLIHVLVKFLSGTSPHGTNQHSPQVGPTATQAMQEFLTRLQVHLSSTCPQIFSELLLKLIHILSTERGAFQTGQGPLDAQVKLLEFTLEQNFEVVSVSTISAVIESVTFLVHHYITCSDKVMSRSGSDSSAGARACFGGLFANLIRPGDAKAVCGEMTRDQLMFDLLKLVNILVQLPLSSNREYSARVSVTTNTTDSVSDEEKVSGGKDVNGSSASTPGSPACVADLVLANQQIMSQILSALGLCNSSAMAMIIGASGLHLTKHENFHGGLDAISVGDGLFTILTTLSKKASTVHMMLQPILTYMACGYMGRQGSLATCQLSEPLLWFILRVLDTSDALKAFHDMGGVQLICNNMVTSTRAIVNTARSMVSTIMKFLDSGPNKAVDSTLKTRILASEPDNAEGIHNFAPLGTITSSSPTAQPAEVLLQATPPHRRARSAAWSYIFLPEEAWCDLTIHLPSAVLLKEIHIQPHLASLATCPSSVSVEVSADGVNMLPLSTPVVTSGLTYIKIQLVKAEVASAVCLRLHRPRDASTLGLSQIKLLGLTAFGTTSSATVNNPFLPSEDQVSKTSIGWLRLLHHCLTHISDLEGMMASAAAPTANLLQTCAALLMSPYCGMHSPNIEVVLVKIGLQSTRIGLKLIDILLRNCAASGSDPTDLNSPLLFGRLNGLSSDSTIDILYQLGTTQDPGTKDRIQALLKWVSDSAKMAALKRSGRMNYMCPSSSAVEYGLLMPSPSHLHCVAAILWHSYELLVEYDLPALLDRELFELLFNWSMSLPCNVVLKKAVDSLLCSMCHIHPNYFSLLMGWMGIIPPPVQCHHRLSMTDDSKKQDLSSSLTDDSKNAQAPLSLTESHLATLASSSQSPEAIKQLLDSGLPSLLVRSLASFCFSHISYSESIAQSVDNSQDKLRRHHVPQHCNKMPITADLVAPILRFLTEVGNSHIMKDWLGGSEVNPLWTALLFLLCHSGSTAGGHNLGAQQSSTRSASHSSATTTVLTTQQRTAIENATVAFFLQCISCHPNNQKLMAQVLCELFQTAPQRGSLPTSGNISGFVRRLFLQLMLEDEKVTMFLQSPCPLYKGRINATSHVIQHPMFGAGHKFRTLHLPVSTTLSDVLDRVSDTPSITAKLISEQKDDKEKKNHEEKEKVKAENGFQDNYSVVVASGLKSQSKRAMASTPPRPPSRRGRTIPDKIGSASSSADAASKIITVPVFHLFHRLLAGQPLPAEMTLAQLLTLLYDRKLPQGYRSIDLTVKLGSKVITDPSLSKTDSFKRLHPEKDHGDLVGSCPEDEALTPSDECMDGVLDESLLETCPIQSPLQVFAGMGGLALIAERLPMLYPEVIQQVSAPVIASTTQEKPKDSDQFEWVTIEQSGELVYEAPETIAAEPPPVKSAVQATSPIPAHSLAAFGLFLRLPGYAEVLLKERKHAQCLLRLVLGVTDDGEGSHILQSPSANVLPTLPFHVLRSLFSATPLTTDDGVLLRRMALEIGALHLILVCLSALSHHAPRVPNSSLSQTEPQVSNSHNPTSAEEQQLYWAKGTGFGTGSTASGWDVEQALTKQRLEEEHVTCLLQVLASYINPMSGAVNGEAQASPESRAQNSSALPSVLLELLSQSCLIPAMSSYLRNDSVLDMARHVPLYRALLELLRAIASCTSMVPLLLPLSTENGEEEEDEQSECQTSVGTLLAKMKTCVDTYTNRLRSKRENVKAGVKPDAPDQEPEGLALLVPDIQRTAEIVHAATANLRQANQEKKLGEYSKKVVMKPKPLSVLKSLEEKYVAVMKKLQFDTFEMVSEDDDGKLGFKVNYHYMSQVKNANDANSAARARRLAQEAVTLSTSLPLSSSSSVFVRCDEERLDIMKVLITGPADTPYANGCFEFDVYFPQDYPSSPPLVNLETTGGHSVRFNPNLYNDGKVCLSILNTWHGRPEEKWNPQTSSFLQVLVSVQSLILVAEPYFNEPGYERSRGTPSGTQSSREYDGNIRQATVKWAMLEQIRNPSPCFKEVIHKHFYLKRIELMAQCEEWIADIQQYSSDKRVGRTMSHHAAALKRHTAQLREELLKLPCPEGLDPDIEDASPVCRATAGAEDTLTHDHVNPSSSKDLPSDFQL
uniprot
proteins
ec_number
2.3.2.24
uniprot
proteins
function
FUNCTION: Anti-apoptotic protein known as inhibitor of apoptosis (IAP) which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase (PubMed:9628897, PubMed:15485903). Unlike most IAPs, does not contain a RING domain and it is not a RING-type E3 ligase (By similarity). Instead acts as a dual E2/E3 enzyme that combines ubiquitin conjugating (E2) and ubiquitin ligase (E3) activities in a single polypeptide (PubMed:15485903, PubMed:15300255). Ubiquitination is mediated by a non-canonical E1 ubiquitin activating enzyme UBA6 (By similarity). Ubiquitinates CASP3, CASP7 and CASP9 and inhibits their caspase activity; also ubiquitinates their procaspases but to a weaker extent (By similarity). Ubiquitinates pro-apoptotic factors DIABLO/SMAC and HTRA2 (PubMed:15300255). DIABLO/SMAC antagonizes the caspase inhibition activity of BIRC6 by competing for the same binding sites as the caspases (By similarity). Ubiquitinates the autophagy protein MAP1LC3B; this activity is also inhibited by DIABLO/SMAC (By similarity). Important regulator for the final stages of cytokinesis (By similarity). Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification. Required for normal placenta development (By similarity). {ECO:0000250|UniProtKB:Q9NR09, ECO:0000269|PubMed:15300255, ECO:0000269|PubMed:15485903, ECO:0000269|PubMed:9628897}.
uniprot
proteins
mass_dalton
532170
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. Ubiquitination is mediated by RNF41 E3 ligase and leads to proteasomal degradation, impairing inhibition of apoptosis. Deubiquitinated by USP8/UBPY. Autoubiquitinated; mediated by E1 ubiquitin activating enzyme UBA6. {ECO:0000250|UniProtKB:Q9NR09}.; PTM: Proteolytically cleaved. Acts as substrate for CASP3, CASP6, CASP7, CASP9 and HTRA2. {ECO:0000250|UniProtKB:Q9NR09}.
uniprot
proteins
protein_family
BIRC6 family
uniprot
proteins
pubmed
15300255
uniprot
proteins
pubmed
15368895
uniprot
proteins
pubmed
15485903
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
9628897
uniprot
proteins
sequence_length
4882
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9NR09}. Endosome {ECO:0000250|UniProtKB:Q9NR09}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9NR09}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NR09}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9NR09}. Note=Exhibits cell cycle-dependent localization. Concentrates in a pericentriolar compartment in interphase, moves partially to spindle poles in metaphase, and finally localizes to the spindle midzone and the midbody in telophase and during cytokinesis. On the midbody, localizes to the midbody ring, also called Flemming body. In interphase cells, localizes to the trans-Golgi network membrane and endosomes. During cytokinesis, a fraction moves to the midzone where it specifically arrives at the midbody ring. After abscission completion, travels with the midbody remnant into one daughter cell, and remains bound to it until a new midbody ring is formed during the next cell division. {ECO:0000250|UniProtKB:Q9NR09}.
uniprot
proteins