BIRC6_HUMAN
ID BIRC6_HUMAN Reviewed; 4857 AA.
AC Q9NR09; Q9ULD1;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Baculoviral IAP repeat-containing protein 6;
DE EC=2.3.2.27 {ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:18329369};
DE AltName: Full=BIR repeat-containing ubiquitin-conjugating enzyme;
DE Short=BRUCE;
DE AltName: Full=RING-type E3 ubiquitin transferase BIRC6 {ECO:0000305};
DE AltName: Full=Ubiquitin-conjugating BIR domain enzyme apollon;
DE Short=APOLLON;
GN Name=BIRC6; Synonyms=KIAA1289;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-4857.
RC TISSUE=Brain;
RX PubMed=10544019; DOI=10.1006/bbrc.1999.1585;
RA Chen Z., Naito M., Hori S., Mashima T., Yamori T., Tsuruo T.;
RT "A human IAP-family gene, apollon, expressed in human brain cancer cells.";
RL Biochem. Biophys. Res. Commun. 264:847-854(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2063-4857.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP INTERACTION WITH RNF41, UBIQUITINATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14765125; DOI=10.1038/sj.emboj.7600075;
RA Qiu X.B., Markant S.L., Yuan J., Goldberg A.L.;
RT "Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel pathway
RT for triggering apoptosis.";
RL EMBO J. 23:800-810(2004).
RN [6]
RP FUNCTION, SUBUNIT, ACTIVITY REGULATION, DOMAIN BIR, AND INTERACTION WITH
RP HTRA2; CASP3; CASP6; CASP7; CASP9 AND DIABLO/SMAC.
RX PubMed=15200957; DOI=10.1016/j.molcel.2004.05.018;
RA Bartke T., Pohl C., Pyrowolakis G., Jentsch S.;
RT "Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin
RT ligase.";
RL Mol. Cell 14:801-811(2004).
RN [7]
RP REVIEW ON FUNCTION.
RX PubMed=15340445; DOI=10.1038/ncb0904-804;
RA Martin S.J.;
RT "An Apollon vista of death and destruction.";
RL Nat. Cell Biol. 6:804-806(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION,
RP UBIQUITINATION, DEUBIQUITINATION, AND INTERACTION WITH KIF23/MKLP1;
RP USP8/UBPY; BIRC5/SURVIVIN; MAP2K1/MEK1; RAB8A/RAB8; RAB11A/RAB11; PLK1;
RP EXOC3/SEC6 AND EXOC4/SEC8.
RX PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
RA Pohl C., Jentsch S.;
RT "Final stages of cytokinesis and midbody ring formation are controlled by
RT BRUCE.";
RL Cell 132:832-845(2008).
RN [10]
RP REVIEW ON FUNCTION.
RX PubMed=18414036; DOI=10.4161/cc.7.8.5783;
RA Dubrez-Daloz L., Dupoux A., Cartier J.;
RT "IAPs: more than just inhibitors of apoptosis proteins.";
RL Cell Cycle 7:1036-1046(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; SER-581; SER-590;
RP SER-2222; SER-2955; THR-3931 AND SER-4023, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND THR-1710, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 4498-4820.
RG Structural genomics consortium (SGC);
RT "Ubc domain of the ubiquitin-protein ligase baculoviral IAP repeat-
RT containing protein 6.";
RL Submitted (APR-2008) to the PDB data bank.
RN [20] {ECO:0007744|PDB:3CEG}
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 4498-4820.
RX PubMed=22496338; DOI=10.1074/mcp.o111.013706;
RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V.,
RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H.,
RA Raught B., Dhe-Paganon S.;
RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
RT function screen.";
RL Mol. Cell. Proteomics 11:329-341(2012).
CC -!- FUNCTION: Anti-apoptotic protein which can regulate cell death by
CC controlling caspases and by acting as an E3 ubiquitin-protein ligase.
CC Has an unusual ubiquitin conjugation system in that it could combine in
CC a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase
CC (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its targets
CC include CASP9 and DIABLO/SMAC. Acts as an inhibitor of CASP3, CASP7 and
CC CASP9. Important regulator for the final stages of cytokinesis. Crucial
CC for normal vesicle targeting to the site of abscission, but also for
CC the integrity of the midbody and the midbody ring, and its striking
CC ubiquitin modification. {ECO:0000269|PubMed:14765125,
CC ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:18329369}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:14765125,
CC ECO:0000269|PubMed:18329369};
CC -!- ACTIVITY REGULATION: Inhibited by DIABLO/SMAC, HTRA2, CASP3, CASP6,
CC CASP7 and CASP9. {ECO:0000269|PubMed:15200957}.
CC -!- SUBUNIT: Homodimer. Binds the activated, processed forms of CASP3,
CC CASP6, CASP7 and CASP9. Interacts with RNF41, DIABLO/SMAC, HTRA2,
CC KIF23/MKLP1, USP8/UBPY, BIRC5/survivin, MAP2K1/MEK1, RAB8A/RAB8,
CC RAB11A/RAB11, PLK1, EXOC3/SEC6 and EXOC4/SEC8.
CC {ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:15200957,
CC ECO:0000269|PubMed:18329369}.
CC -!- INTERACTION:
CC Q9NR09; Q96A65: EXOC4; NbExp=3; IntAct=EBI-1765160, EBI-355383;
CC Q9NR09; Q02241: KIF23; NbExp=4; IntAct=EBI-1765160, EBI-306852;
CC Q9NR09; Q02750: MAP2K1; NbExp=2; IntAct=EBI-1765160, EBI-492564;
CC Q9NR09; P53350: PLK1; NbExp=4; IntAct=EBI-1765160, EBI-476768;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:18329369}. Endosome {ECO:0000269|PubMed:18329369}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18329369}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:18329369}. Midbody, Midbody ring
CC {ECO:0000269|PubMed:18329369}. Note=Exhibits cell cycle-dependent
CC localization. Concentrates in a pericentriolar compartment in
CC interphase, moves partially to spindle poles in metaphase, and finally
CC localizes to the spindle midzone and the midbody in telophase and
CC during cytokinesis. On the midbody, localizes to the midbody ring, also
CC called Flemming body (PubMed:18329369). In interphase cells, localizes
CC to the trans-Golgi network membrane and endosomes. During cytokinesis,
CC a fraction moves to the midzone where it specifically arrives at the
CC midbody ring. After abscission completion, travels with the midbody
CC remnant into one daughter cell, and remains bound to it until a new
CC midbody ring is formed during the next cell division (PubMed:18329369).
CC {ECO:0000269|PubMed:18329369}.
CC -!- TISSUE SPECIFICITY: Expressed in brain cancer cells.
CC -!- DOMAIN: The BIR domain is essential for its antiapoptotic function and
CC is important for binding to DIABLO/SMAC and CASP9.
CC {ECO:0000269|PubMed:15200957}.
CC -!- PTM: Ubiquitinated. Ubiquitination is mediated by the RNF41 E3 ligase
CC and leads to proteasomal degradation, impairing inhibition of
CC apoptosis. Deubiquitinated by USP8/UBPY. {ECO:0000269|PubMed:14765125,
CC ECO:0000269|PubMed:18329369}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ubiquitin-
CC conjugating enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86603.2; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BIRC6ID798ch2p22.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC079837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF265555; AAF75772.1; -; mRNA.
DR EMBL; AB033115; BAA86603.2; ALT_FRAME; mRNA.
DR CCDS; CCDS33175.2; -.
DR RefSeq; NP_057336.3; NM_016252.3.
DR PDB; 3CEG; X-ray; 2.01 A; A/B=4498-4820.
DR PDBsum; 3CEG; -.
DR BioGRID; 121521; 202.
DR IntAct; Q9NR09; 54.
DR MINT; Q9NR09; -.
DR STRING; 9606.ENSP00000393596; -.
DR MEROPS; I32.006; -.
DR GlyGen; Q9NR09; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NR09; -.
DR PhosphoSitePlus; Q9NR09; -.
DR SwissPalm; Q9NR09; -.
DR BioMuta; BIRC6; -.
DR DMDM; 313104079; -.
DR EPD; Q9NR09; -.
DR jPOST; Q9NR09; -.
DR MassIVE; Q9NR09; -.
DR MaxQB; Q9NR09; -.
DR PaxDb; Q9NR09; -.
DR PeptideAtlas; Q9NR09; -.
DR PRIDE; Q9NR09; -.
DR ProteomicsDB; 82241; -.
DR Antibodypedia; 29188; 224 antibodies from 31 providers.
DR DNASU; 57448; -.
DR Ensembl; ENST00000421745.7; ENSP00000393596.2; ENSG00000115760.15.
DR GeneID; 57448; -.
DR KEGG; hsa:57448; -.
DR MANE-Select; ENST00000421745.7; ENSP00000393596.2; NM_016252.4; NP_057336.3.
DR UCSC; uc010ezu.4; human.
DR CTD; 57448; -.
DR DisGeNET; 57448; -.
DR GeneCards; BIRC6; -.
DR HGNC; HGNC:13516; BIRC6.
DR HPA; ENSG00000115760; Low tissue specificity.
DR MIM; 605638; gene.
DR neXtProt; NX_Q9NR09; -.
DR OpenTargets; ENSG00000115760; -.
DR PharmGKB; PA25363; -.
DR VEuPathDB; HostDB:ENSG00000115760; -.
DR eggNOG; KOG0895; Eukaryota.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00940000156126; -.
DR HOGENOM; CLU_000111_1_0_1; -.
DR InParanoid; Q9NR09; -.
DR OrthoDB; 1404665at2759; -.
DR PhylomeDB; Q9NR09; -.
DR TreeFam; TF105357; -.
DR PathwayCommons; Q9NR09; -.
DR Reactome; R-HSA-9700645; ALK mutants bind TKIs.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; Q9NR09; -.
DR SIGNOR; Q9NR09; -.
DR BioGRID-ORCS; 57448; 209 hits in 1125 CRISPR screens.
DR ChiTaRS; BIRC6; human.
DR EvolutionaryTrace; Q9NR09; -.
DR GeneWiki; BIRC6; -.
DR GenomeRNAi; 57448; -.
DR Pharos; Q9NR09; Tbio.
DR PRO; PR:Q9NR09; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NR09; protein.
DR Bgee; ENSG00000115760; Expressed in epithelial cell of pancreas and 194 other tissues.
DR ExpressionAtlas; Q9NR09; baseline and differential.
DR Genevisible; Q9NR09; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IMP:UniProtKB.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0060711; P:labyrinthine layer development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; TAS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; TAS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; TAS:UniProtKB.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IEA:UniProt.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0060712; P:spongiotrophoblast layer development; IEA:Ensembl.
DR CDD; cd00022; BIR; 1.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR IDEAL; IID00636; -.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR022103; BIRC6.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00653; BIR; 1.
DR Pfam; PF12356; BIRC6; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SMART; SM00238; BIR; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50143; BIR_REPEAT_2; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Endosome; Golgi apparatus; Membrane; Mitosis; Phosphoprotein;
KW Protease inhibitor; Reference proteome; Thiol protease inhibitor;
KW Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..4857
FT /note="Baculoviral IAP repeat-containing protein 6"
FT /id="PRO_0000122361"
FT REPEAT 284..358
FT /note="BIR"
FT DOMAIN 4573..4740
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 465..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2945..2973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3923..3949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4260..4283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4835..4857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4666
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88738"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88738"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1710
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2955
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 3931
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 4023
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 2319
FT /note="L -> F (in Ref. 3; BAA86603)"
FT /evidence="ECO:0000305"
FT CONFLICT 2674
FT /note="T -> S (in Ref. 2; AAF75772)"
FT /evidence="ECO:0000305"
FT HELIX 4524..4533
FT /evidence="ECO:0007829|PDB:3CEG"
FT STRAND 4536..4540
FT /evidence="ECO:0007829|PDB:3CEG"
FT STRAND 4543..4545
FT /evidence="ECO:0007829|PDB:3CEG"
FT STRAND 4551..4555
FT /evidence="ECO:0007829|PDB:3CEG"
FT HELIX 4560..4564
FT /evidence="ECO:0007829|PDB:3CEG"
FT HELIX 4572..4588
FT /evidence="ECO:0007829|PDB:3CEG"
FT STRAND 4597..4604
FT /evidence="ECO:0007829|PDB:3CEG"
FT STRAND 4608..4615
FT /evidence="ECO:0007829|PDB:3CEG"
FT STRAND 4625..4631
FT /evidence="ECO:0007829|PDB:3CEG"
FT TURN 4634..4638
FT /evidence="ECO:0007829|PDB:3CEG"
FT STRAND 4642..4645
FT /evidence="ECO:0007829|PDB:3CEG"
FT TURN 4649..4652
FT /evidence="ECO:0007829|PDB:3CEG"
FT HELIX 4668..4670
FT /evidence="ECO:0007829|PDB:3CEG"
FT HELIX 4677..4679
FT /evidence="ECO:0007829|PDB:3CEG"
FT TURN 4683..4685
FT /evidence="ECO:0007829|PDB:3CEG"
FT HELIX 4688..4698
FT /evidence="ECO:0007829|PDB:3CEG"
FT HELIX 4704..4707
FT /evidence="ECO:0007829|PDB:3CEG"
FT HELIX 4711..4714
FT /evidence="ECO:0007829|PDB:3CEG"
FT HELIX 4718..4738
FT /evidence="ECO:0007829|PDB:3CEG"
FT HELIX 4741..4745
FT /evidence="ECO:0007829|PDB:3CEG"
FT TURN 4749..4751
FT /evidence="ECO:0007829|PDB:3CEG"
FT HELIX 4752..4777
FT /evidence="ECO:0007829|PDB:3CEG"
FT HELIX 4788..4810
FT /evidence="ECO:0007829|PDB:3CEG"
SQ SEQUENCE 4857 AA; 530269 MW; ACA0EB5B3EFBA0C0 CRC64;
MVTGGGAAPP GTVTEPLPSV IVLSAGRKMA AAAAAASGPG CSSAAGAGAA GVSEWLVLRD
GCMHCDADGL HSLSYHPALN AILAVTSRGT IKVIDGTSGA TLQASALSAK PGGQVKCQYI
SAVDKVIFVD DYAVGCRKDL NGILLLDTAL QTPVSKQDDV VQLELPVTEA QQLLSACLEK
VDISSTEGYD LFITQLKDGL KNTSHETAAN HKVAKWATVT FHLPHHVLKS IASAIVNELK
KINQNVAALP VASSVMDRLS YLLPSARPEL GVGPGRSVDR SLMYSEANRR ETFTSWPHVG
YRWAQPDPMA QAGFYHQPAS SGDDRAMCFT CSVCLVCWEP TDEPWSEHER HSPNCPFVKG
EHTQNVPLSV TLATSPAQFP CTDGTDRISC FGSGSCPHFL AAATKRGKIC IWDVSKLMKV
HLKFEINAYD PAIVQQLILS GDPSSGVDSR RPTLAWLEDS SSCSDIPKLE GDSDDLLEDS
DSEEHSRSDS VTGHTSQKEA MEVSLDITAL SILQQPEKLQ WEIVANVLED TVKDLEELGA
NPCLTNSKSE KTKEKHQEQH NIPFPCLLAG GLLTYKSPAT SPISSNSHRS LDGLSRTQGE
SISEQGSTDN ESCTNSELNS PLVRRTLPVL LLYSIKESDE KAGKIFSQMN NIMSKSLHDD
GFTVPQIIEM ELDSQEQLLL QDPPVTYIQQ FADAAANLTS PDSEKWNSVF PKPGTLVQCL
RLPKFAEEEN LCIDSITPCA DGIHLLVGLR TCPVESLSAI NQVEALNNLN KLNSALCNRR
KGELESNLAV VNGANISVIQ HESPADVQTP LIIQPEQRNV SGGYLVLYKM NYATRIVTLE
EEPIKIQHIK DPQDTITSLI LLPPDILDNR EDDCEEPIED MQLTSKNGFE REKTSDISTL
GHLVITTQGG YVKILDLSNF EILAKVEPPK KEGTEEQDTF VSVIYCSGTD RLCACTKGGE
LHFLQIGGTC DDIDEADILV DGSLSKGIEP SSEGSKPLSN PSSPGISGVD LLVDQPFTLE
ILTSLVELTR FETLTPRFSA TVPPCWVEVQ QEQQQRRHPQ HLHQQHHGDA AQHTRTWKLQ
TDSNSWDEHV FELVLPKACM VGHVDFKFVL NSNITNIPQI QVTLLKNKAP GLGKVNALNI
EVEQNGKPSL VDLNEEMQHM DVEESQCLRL CPFLEDHKED ILCGPVWLAS GLDLSGHAGM
LTLTSPKLVK GMAGGKYRSF LIHVKAVNER GTEEICNGGM RPVVRLPSLK HQSNKGYSLA
SLLAKVAAGK EKSSNVKNEN TSGTRKSENL RGCDLLQEVS VTIRRFKKTS ISKERVQRCA
MLQFSEFHEK LLNTLCRKTD DGQITEHAQS LVLDTLCWLA GVHSNGPGSS KEGNENLLSK
TRKFLSDIVR VCFFEAGRSI AHKCARFLAL CISNGKCDPC QPAFGPVLLK ALLDNMSFLP
AATTGGSVYW YFVLLNYVKD EDLAGCSTAC ASLLTAVSRQ LQDRLTPMEA LLQTRYGLYS
SPFDPVLFDL EMSGSSCKNV YNSSIGVQSD EIDLSDVLSG NGKVSSCTAA EGSFTSLTGL
LEVEPLHFTC VSTSDGTRIE RDDAMSSFGV TPAVGGLSSG TVGEASTALS SAAQVALQSL
SHAMASAEQQ LQVLQEKQQQ LLKLQQQKAK LEAKLHQTTA AAAAAASAVG PVHNSVPSNP
VAAPGFFIHP SDVIPPTPKT TPLFMTPPLT PPNEAVSVVI NAELAQLFPG SVIDPPAVNL
AAHNKNSNKS RMNPLGSGLA LAISHASHFL QPPPHQSIII ERMHSGARRF VTLDFGRPIL
LTDVLIPTCG DLASLSIDIW TLGEEVDGRR LVVATDISTH SLILHDLIPP PVCRFMKITV
IGRYGSTNAR AKIPLGFYYG HTYILPWESE LKLMHDPLKG EGESANQPEI DQHLAMMVAL
QEDIQCRYNL ACHRLETLLQ SIDLPPLNSA NNAQYFLRKP DKAVEEDSRV FSAYQDCIQL
QLQLNLAHNA VQRLKVALGA SRKMLSETSN PEDLIQTSST EQLRTIIRYL LDTLLSLLHA
SNGHSVPAVL QSTFHAQACE ELFKHLCISG TPKIRLHTGL LLVQLCGGER WWGQFLSNVL
QELYNSEQLL IFPQDRVFML LSCIGQRSLS NSGVLESLLN LLDNLLSPLQ PQLPMHRRTE
GVLDIPMISW VVMLVSRLLD YVATVEDEAA AAKKPLNGNQ WSFINNNLHT QSLNRSSKGS
SSLDRLYSRK IRKQLVHHKQ QLNLLKAKQK ALVEQMEKEK IQSNKGSSYK LLVEQAKLKQ
ATSKHFKDLI RLRRTAEWSR SNLDTEVTTA KESPEIEPLP FTLAHERCIS VVQKLVLFLL
SMDFTCHADL LLFVCKVLAR IANATRPTIH LCEIVNEPQL ERLLLLLVGT DFNRGDISWG
GAWAQYSLTC MLQDILAGEL LAPVAAEAME EGTVGDDVGA TAGDSDDSLQ QSSVQLLETI
DEPLTHDITG APPLSSLEKD KEIDLELLQD LMEVDIDPLD IDLEKDPLAA KVFKPISSTW
YDYWGADYGT YNYNPYIGGL GIPVAKPPAN TEKNGSQTVS VSVSQALDAR LEVGLEQQAE
LMLKMMSTLE ADSILQALTN TSPTLSQSPT GTDDSLLGGL QAANQTSQLI IQLSSVPMLN
VCFNKLFSML QVHHVQLESL LQLWLTLSLN SSSTGNKENG ADIFLYNANR IPVISLNQAS
ITSFLTVLAW YPNTLLRTWC LVLHSLTLMT NMQLNSGSSS AIGTQESTAH LLVSDPNLIH
VLVKFLSGTS PHGTNQHSPQ VGPTATQAMQ EFLTRLQVHL SSTCPQIFSE FLLKLIHILS
TERGAFQTGQ GPLDAQVKLL EFTLEQNFEV VSVSTISAVI ESVTFLVHHY ITCSDKVMSR
SGSDSSVGAR ACFGGLFANL IRPGDAKAVC GEMTRDQLMF DLLKLVNILV QLPLSGNREY
SARVSVTTNT TDSVSDEEKV SGGKDGNGSS TSVQGSPAYV ADLVLANQQI MSQILSALGL
CNSSAMAMII GASGLHLTKH ENFHGGLDAI SVGDGLFTIL TTLSKKASTV HMMLQPILTY
MACGYMGRQG SLATCQLSEP LLWFILRVLD TSDALKAFHD MGGVQLICNN MVTSTRAIVN
TARSMVSTIM KFLDSGPNKA VDSTLKTRIL ASEPDNAEGI HNFAPLGTIT SSSPTAQPAE
VLLQATPPHR RARSAAWSYI FLPEEAWCDL TIHLPAAVLL KEIHIQPHLA SLATCPSSVS
VEVSADGVNM LPLSTPVVTS GLTYIKIQLV KAEVASAVCL RLHRPRDAST LGLSQIKLLG
LTAFGTTSSA TVNNPFLPSE DQVSKTSIGW LRLLHHCLTH ISDLEGMMAS AAAPTANLLQ
TCAALLMSPY CGMHSPNIEV VLVKIGLQST RIGLKLIDIL LRNCAASGSD PTDLNSPLLF
GRLNGLSSDS TIDILYQLGT TQDPGTKDRI QALLKWVSDS ARVAAMKRSG RMNYMCPNSS
TVEYGLLMPS PSHLHCVAAI LWHSYELLVE YDLPALLDQE LFELLFNWSM SLPCNMVLKK
AVDSLLCSMC HVHPNYFSLL MGWMGITPPP VQCHHRLSMT DDSKKQDLSS SLTDDSKNAQ
APLALTESHL ATLASSSQSP EAIKQLLDSG LPSLLVRSLA SFCFSHISSS ESIAQSIDIS
QDKLRRHHVP QQCNKMPITA DLVAPILRFL TEVGNSHIMK DWLGGSEVNP LWTALLFLLC
HSGSTSGSHN LGAQQTSARS ASLSSAATTG LTTQQRTAIE NATVAFFLQC ISCHPNNQKL
MAQVLCELFQ TSPQRGNLPT SGNISGFIRR LFLQLMLEDE KVTMFLQSPC PLYKGRINAT
SHVIQHPMYG AGHKFRTLHL PVSTTLSDVL DRVSDTPSIT AKLISEQKDD KEKKNHEEKE
KVKAENGFQD NYSVVVASGL KSQSKRAVSA TPPRPPSRRG RTIPDKIGST SGAEAANKII
TVPVFHLFHK LLAGQPLPAE MTLAQLLTLL YDRKLPQGYR SIDLTVKLGS RVITDPSLSK
TDSYKRLHPE KDHGDLLASC PEDEALTPGD ECMDGILDES LLETCPIQSP LQVFAGMGGL
ALIAERLPML YPEVIQQVSA PVVTSTTQEK PKDSDQFEWV TIEQSGELVY EAPETVAAEP
PPIKSAVQTM SPIPAHSLAA FGLFLRLPGY AEVLLKERKH AQCLLRLVLG VTDDGEGSHI
LQSPSANVLP TLPFHVLRSL FSTTPLTTDD GVLLRRMALE IGALHLILVC LSALSHHSPR
VPNSSVNQTE PQVSSSHNPT STEEQQLYWA KGTGFGTGST ASGWDVEQAL TKQRLEEEHV
TCLLQVLASY INPVSSAVNG EAQSSHETRG QNSNALPSVL LELLSQSCLI PAMSSYLRND
SVLDMARHVP LYRALLELLR AIASCAAMVP LLLPLSTENG EEEEEQSECQ TSVGTLLAKM
KTCVDTYTNR LRSKRENVKT GVKPDASDQE PEGLTLLVPD IQKTAEIVYA ATTSLRQANQ
EKKLGEYSKK AAMKPKPLSV LKSLEEKYVA VMKKLQFDTF EMVSEDEDGK LGFKVNYHYM
SQVKNANDAN SAARARRLAQ EAVTLSTSLP LSSSSSVFVR CDEERLDIMK VLITGPADTP
YANGCFEFDV YFPQDYPSSP PLVNLETTGG HSVRFNPNLY NDGKVCLSIL NTWHGRPEEK
WNPQTSSFLQ VLVSVQSLIL VAEPYFNEPG YERSRGTPSG TQSSREYDGN IRQATVKWAM
LEQIRNPSPC FKEVIHKHFY LKRVEIMAQC EEWIADIQQY SSDKRVGRTM SHHAAALKRH
TAQLREELLK LPCPEGLDPD TDDAPEVCRA TTGAEETLMH DQVKPSSSKE LPSDFQL
