ID BIRC5_HUMAN Reviewed; 142 AA. AC O15392; A2SUH6; B2R4R1; Q2I3N8; Q4VGX0; Q53F61; Q5MGC6; Q6FHL2; AC Q75SP2; Q9P2W8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2012, sequence version 3. DT 07-NOV-2018, entry version 214. DE RecName: Full=Baculoviral IAP repeat-containing protein 5; DE AltName: Full=Apoptosis inhibitor 4; DE AltName: Full=Apoptosis inhibitor survivin; GN Name=BIRC5; Synonyms=API4, IAP4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=9256286; DOI=10.1038/nm0897-917; RA Ambrosini G., Adida C., Altieri D.C.; RT "A novel anti-apoptosis gene, survivin, expressed in cancer and RT lymphoma."; RL Nat. Med. 3:917-921(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, AND TISSUE RP SPECIFICITY. RX PubMed=10626797; RA Mahotka C., Wenzel M., Springer E., Gabbert H.E., Gerharz C.D.; RT "Survivin-deltaEx3 and survivin-2B: two novel splice variants of the RT apoptosis inhibitor survivin with different antiapoptotic RT properties."; RL Cancer Res. 59:6097-6102(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION. RX PubMed=11084331; DOI=10.1016/S0960-9822(00)00769-7; RA Uren A.G., Wong L., Pakusch M., Fowler K.J., Burrows F.J., Vaux D.L., RA Choo K.H.; RT "Survivin and the inner centromere protein INCENP show similar cell- RT cycle localization and gene knockout phenotype."; RL Curr. Biol. 10:1319-1328(2000). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY. RC TISSUE=Myeloid leukemia cell; RX PubMed=14741722; DOI=10.1016/j.bbrc.2003.12.178; RA Badran A., Yoshida A., Ishikawa K., Goi T., Yamaguchi A., Ueda T., RA Inuzuka M.; RT "Identification of a novel splice variant of the human anti-apoptosis RT gene survivin."; RL Biochem. Biophys. Res. Commun. 314:902-907(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND TISSUE SPECIFICITY. RC TISSUE=Mammary cancer; RX PubMed=16329164; DOI=10.1080/10425170500226490; RA Zheng W., Ma X., Wei D., Wang T., Ma Y., Yang S.; RT "Molecular cloning and bioinformatics analysis of a novel spliced RT variant of survivin from human breast cancer cells."; RL DNA Seq. 16:321-328(2005). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Neuroblastoma; RA Kageyama H., Islam A., Takayasu H., Nakagawara A.; RT "An isoform of survivin (survivin-beta) which has 23 amino acids RT insertion into the BIR domain."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7). RA Caldas H., Honsey L.E., Altura R.A.; RT "Survivin 2 alpha: a novel survivin splice variant expressed in human RT malignancies."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6). RC TISSUE=Myeloid leukemia cell; RA Vietri M.T., Cioffi M., Sessa M., Sica V., Molinari A.M.; RT "Identification of a novel survivin splicing variant 3alpha in acute RT myeloid leukemia."; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-129. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in RT the human lineage."; RL Nature 440:1045-1049(2006). RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, Mammary gland, and Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [16] RP FUNCTION. RX PubMed=9859993; DOI=10.1038/25141; RA Li F., Ambrosini G., Chu E.Y., Plescia J., Tognin S., Marchisio P.C., RA Altieri D.C.; RT "Control of apoptosis and mitotic spindle checkpoint by survivin."; RL Nature 396:580-584(1998). RN [17] RP PHOSPHORYLATION AT THR-34. RX PubMed=11069302; DOI=10.1073/pnas.240390697; RA O'Connor D.S., Grossman D., Plescia J., Li F., Zhang H., Villa A., RA Tognin S., Marchisio P.C., Altieri D.C.; RT "Regulation of apoptosis at cell division by p34cdc2 phosphorylation RT of survivin."; RL Proc. Natl. Acad. Sci. U.S.A. 97:13103-13107(2000). RN [18] RP FUNCTION IN APOPTOSIS SUPPRESSION, INTERACTION WITH LAMTOR5/HBXIP, RP MUTAGENESIS OF THR-34, AND SUBCELLULAR LOCATION. RX PubMed=12773388; DOI=10.1093/emboj/cdg263; RA Marusawa H., Matsuzawa S., Welsh K., Zou H., Armstrong R., Tamm I., RA Reed J.C.; RT "HBXIP functions as a cofactor of survivin in apoptosis suppression."; RL EMBO J. 22:2729-2740(2003). RN [19] RP INTERACTION WITH INCENP, SUBCELLULAR LOCATION, PHOSPHORYLATION AT RP THR-117, AND MUTAGENESIS OF THR-117. RX PubMed=14610074; DOI=10.1074/jbc.M311299200; RA Wheatley S.P., Henzing A.J., Dodson H., Khaled W., Earnshaw W.C.; RT "Aurora-B phosphorylation in vitro identifies a residue of survivin RT that is essential for its localization and binding to inner centromere RT protein (INCENP) in vivo."; RL J. Biol. Chem. 279:5655-5660(2004). RN [20] RP INTERACTION WITH CDCA8. RX PubMed=15249581; DOI=10.1083/jcb.200404001; RA Gassmann R., Carvalho A., Henzing A.J., Ruchaud S., Hudson D.F., RA Honda R., Nigg E.A., Gerloff D.L., Earnshaw W.C.; RT "Borealin: a novel chromosomal passenger required for stability of the RT bipolar mitotic spindle."; RL J. Cell Biol. 166:179-191(2004). RN [21] RP SUBCELLULAR LOCATION, AND INTERACTION WITH BIRC2/C-IAP1. RX PubMed=15665297; RA Samuel T., Okada K., Hyer M., Welsh K., Zapata J.M., Reed J.C.; RT "cIAP1 Localizes to the nuclear compartment and modulates the cell RT cycle."; RL Cancer Res. 65:210-218(2005). RN [22] RP REVIEW ON FUNCTION. RX PubMed=16344111; DOI=10.1016/S0074-7696(05)47002-3; RA Wheatley S.P., McNeish I.A.; RT "Survivin: a protein with dual roles in mitosis and apoptosis."; RL Int. Rev. Cytol. 247:35-88(2005). RN [23] RP FUNCTION, INTERACTION WITH USP9X, SUBCELLULAR LOCATION, RP UBIQUITINATION, AND MUTAGENESIS OF LYS-23; LYS-62; LYS-78 AND LYS-79. RX PubMed=16322459; DOI=10.1126/science.1120160; RA Vong Q.P., Cao K., Li H.Y., Iglesias P.A., Zheng Y.; RT "Chromosome alignment and segregation regulated by ubiquitination of RT survivin."; RL Science 310:1499-1504(2005). RN [24] RP MUTAGENESIS OF ASP-70; ASP-71 AND 70-ASP--ASP-71. RX PubMed=16762323; DOI=10.1016/j.bbrc.2006.05.131; RA Cao L., Yan X., Wu Y., Hu H., Li Q., Zhou T., Jiang S., Yu L.; RT "Survivin mutant (Surv-DD70, 71AA) disrupts the interaction of RT Survivin with Aurora B and causes multinucleation in HeLa cells."; RL Biochem. Biophys. Res. Commun. 346:400-407(2006). RN [25] RP INTERACTION WITH CDCA8. RX PubMed=16239925; DOI=10.1038/sj.embor.7400562; RA Vader G., Kauw J.J.W., Medema R.H., Lens S.M.A.; RT "Survivin mediates targeting of the chromosomal passenger complex to RT the centromere and midbody."; RL EMBO Rep. 7:85-92(2006). RN [26] RP INTERACTION WITH CDCA8. RX PubMed=16427043; DOI=10.1016/j.yexcr.2005.12.015; RA Chang J.-L., Chen T.-H., Wang C.-F., Chiang Y.-H., Huang Y.-L., RA Wong F.-H., Chou C.-K., Chen C.-M.; RT "Borealin/Dasra B is a cell cycle-regulated chromosomal passenger RT protein and its nuclear accumulation is linked to poor prognosis for RT human gastric cancer."; RL Exp. Cell Res. 312:962-973(2006). RN [27] RP INTERACTION WITH EVI5. RX PubMed=16764853; DOI=10.1016/j.yexcr.2006.03.032; RA Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.; RT "EVI5 protein associates with the INCENP-aurora B kinase-survivin RT chromosomal passenger complex and is involved in the completion of RT cytokinesis."; RL Exp. Cell Res. 312:2325-2335(2006). RN [28] RP FUNCTION, AND INTERACTION WITH CDCA8. RX PubMed=16291752; DOI=10.1074/jbc.M508773200; RA Noton E.A., Colnaghi R., Tate S., Starck C., Carvalho A., RA Ko Ferrigno P., Wheatley S.P.; RT "Molecular analysis of survivin isoforms: evidence that alternatively RT spliced variants do not play a role in mitosis."; RL J. Biol. Chem. 281:1286-1295(2006). RN [29] RP INTERACTION WITH CDCA8. RX PubMed=16436504; DOI=10.1091/mbc.E05-08-0727; RA Lens S.M.A., Rodriguez J.A., Vader G., Span S.W., Giaccone G., RA Medema R.H.; RT "Uncoupling the central spindle-associated function of the chromosomal RT passenger complex from its role at centromeres."; RL Mol. Biol. Cell 17:1897-1909(2006). RN [30] RP INTERACTION WITH BIRC6/BRUCE. 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 RT by BRUCE."; RL Cell 132:832-845(2008). RN [31] RP INDUCTION. RX PubMed=17993464; DOI=10.1074/jbc.M704035200; RA Gagarina V., Carlberg A.L., Pereira-Mouries L., Hall D.J.; RT "Cartilage oligomeric matrix protein protects cells against death by RT elevating members of the IAP family of survival proteins."; RL J. Biol. Chem. 283:648-659(2008). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [33] RP FUNCTION, INTERACTION WITH RAN; AURKB AND CDCA8, SUBCELLULAR LOCATION, RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLU-65. RX PubMed=18591255; DOI=10.1128/MCB.02039-07; RA Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.; RT "A survivin-ran complex regulates spindle formation in tumor cells."; RL Mol. Cell. Biol. 28:5299-5311(2008). RN [34] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=21364656; DOI=10.1038/cddis.2010.25; RA Knauer S.K., Heinrich U.R., Bier C., Habtemichael N., Docter D., RA Helling K., Mann W.J., Stauber R.H.; RT "An otoprotective role for the apoptosis inhibitor protein survivin."; RL Cell Death Dis. 1:E51-E51(2010). RN [35] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAT3 AND XPO1/CRM1, RP ACETYLATION AT LYS-23; LYS-90; LYS-110; LYS-112; LYS-115; LYS-121 AND RP LYS-129, MUTAGENESIS OF LYS-129, AND CHARACTERIZATION OF VARIANT RP GLU-129. RX PubMed=20826784; DOI=10.1074/jbc.M110.152777; RA Wang H., Holloway M.P., Ma L., Cooper Z.A., Riolo M., Samkari A., RA Elenitoba-Johnson K.S., Chin Y.E., Altura R.A.; RT "Acetylation directs survivin nuclear localization to repress STAT3 RT oncogenic activity."; RL J. Biol. Chem. 285:36129-36137(2010). RN [36] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=20627126; DOI=10.1016/j.mcn.2010.07.003; RA Habtemichael N., Heinrich U.R., Knauer S.K., Schmidtmann I., Bier C., RA Docter D., Brochhausen C., Helling K., Brieger J., Stauber R.H., RA Mann W.J.; RT "Expression analysis suggests a potential cytoprotective role of Birc5 RT in the inner ear."; RL Mol. Cell. Neurosci. 45:297-305(2010). RN [37] RP FUNCTION, HISTONE-BINDING, AND MUTAGENESIS OF ARG-18; TRP-25; CYS-33; RP CYS-57 AND TRP-67. RX PubMed=20929775; DOI=10.1126/science.1194498; RA Yamagishi Y., Honda T., Tanno Y., Watanabe Y.; RT "Two histone marks establish the inner centromere and chromosome bi- RT orientation."; RL Science 330:239-243(2010). RN [38] RP PHOSPHORYLATION AT THR-48, AND MUTAGENESIS OF THR-48. RX PubMed=21252625; DOI=10.4161/cc.10.3.14758; RA Barrett R.M., Colnaghi R., Wheatley S.P.; RT "Threonine 48 in the BIR domain of survivin is critical to its mitotic RT and anti-apoptotic activities and can be phosphorylated by CK2 in RT vitro."; RL Cell Cycle 10:538-548(2011). RN [39] RP INTERACTION WITH JTB. RX PubMed=21225229; DOI=10.3892/ijo.2011.900; RA Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.; RT "PAR, a protein involved in the cell cycle, is functionally related to RT chromosomal passenger proteins."; RL Int. J. Oncol. 38:777-785(2011). RN [40] RP FUNCTION, SUBUNIT, AND INTERACTION WITH XIAP/BIRC4 AND DIABLO/SMAC. RX PubMed=21536684; DOI=10.1074/jbc.M111.237586; RA Pavlyukov M.S., Antipova N.V., Balashova M.V., Vinogradova T.V., RA Kopantzev E.P., Shakhparonov M.I.; RT "Survivin monomer plays an essential role in apoptosis regulation."; RL J. Biol. Chem. 286:23296-23307(2011). RN [41] RP PHOSPHORYLATION AT THR-34 BY CDK15. RX PubMed=24866247; DOI=10.1016/j.bbrc.2014.05.070; RA Park M.H., Kim S.Y., Kim Y.J., Chung Y.H.; RT "ALS2CR7 (CDK15) attenuates TRAIL induced apoptosis by inducing RT phosphorylation of survivin Thr34."; RL Biochem. Biophys. Res. Commun. 450:129-134(2014). RN [42] RP UBIQUITINATION. RX PubMed=24793696; DOI=10.1016/j.molcel.2014.03.046; RA Li Z., Pei X.H., Yan J., Yan F., Cappell K.M., Whitehurst A.W., RA Xiong Y.; RT "CUL9 mediates the functions of the 3M complex and ubiquitylates RT survivin to maintain genome integrity."; RL Mol. Cell 54:805-819(2014). RN [43] RP SUBUNIT, AND PHOSPHORYLATION AT SER-20. RX PubMed=27332895; DOI=10.1371/journal.pone.0157305; RA Sasai K., Katayama H., Hawke D.H., Sen S.; RT "Aurora-C interactions with survivin and INCENP reveal shared and RT distinct features compared with Aurora-B chromosome passenger protein RT complex."; RL PLoS ONE 11:E0157305-E0157305(2016). RN [44] RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF ISOFORM 1. RX PubMed=10949039; DOI=10.1016/S1097-2765(05)00020-1; RA Chantalat L., Skoufias D.A., Kleman J.P., Jung B., Dideberg O., RA Margolis R.L.; RT "Crystal structure of human survivin reveals a bow tie-shaped dimer RT with two unusual alpha-helical extensions."; RL Mol. Cell 6:183-189(2000). RN [45] RP X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF ISOFORM 1. RX PubMed=10876248; DOI=10.1038/76838; RA Verdecia M.A., Huang H., Dutil E., Kaiser D.A., Hunter T., Noel J.P.; RT "Structure of the human anti-apoptotic protein survivin reveals a RT dimeric arrangement."; RL Nat. Struct. Biol. 7:602-608(2000). RN [46] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC IONS, RP SUBUNIT, AND INTERACTION WITH CDCA8 AND INCENP. RX PubMed=17956729; DOI=10.1016/j.cell.2007.07.045; RA Jeyaprakash A.A., Klein U.R., Lindner D., Ebert J., Nigg E.A., RA Conti E.; RT "Structure of a Survivin-Borealin-INCENP core complex reveals how RT chromosomal passengers travel together."; RL Cell 131:271-285(2007). RN [47] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=19530738; DOI=10.1021/bi900530v; RA Bourhis E., Lingel A., Phung Q., Fairbrother W.J., Cochran A.G.; RT "Phosphorylation of a borealin dimerization domain is required for RT proper chromosome segregation."; RL Biochemistry 48:6783-6793(2009). CC -!- FUNCTION: Multitasking protein that has dual roles in promoting CC cell proliferation and preventing apoptosis (PubMed:9859993, CC PubMed:21364656, PubMed:20627126). Component of a chromosome CC passage protein complex (CPC) which is essential for chromosome CC alignment and segregation during mitosis and cytokinesis CC (PubMed:16322459). Acts as an important regulator of the CC localization of this complex; directs CPC movement to different CC locations from the inner centromere during prometaphase to midbody CC during cytokinesis and participates in the organization of the CC center spindle by associating with polymerized microtubules CC (PubMed:20826784). Involved in the recruitment of CPC to CC centromeres during early mitosis via association with histone H3 CC phosphorylated at 'Thr-3' (H3pT3) during mitosis CC (PubMed:20929775). The complex with RAN plays a role in mitotic CC spindle formation by serving as a physical scaffold to help CC deliver the RAN effector molecule TPX2 to microtubules CC (PubMed:18591255). May counteract a default induction of apoptosis CC in G2/M phase (PubMed:9859993). The acetylated form represses CC STAT3 transactivation of target gene promoters (PubMed:20826784). CC May play a role in neoplasia (PubMed:10626797). Inhibitor of CASP3 CC and CASP7 (PubMed:21536684). Isoform 2 and isoform 3 do not appear CC to play vital roles in mitosis (PubMed:12773388, PubMed:16291752). CC Isoform 3 shows a marked reduction in its anti-apoptotic effects CC when compared with the displayed wild-type isoform CC (PubMed:10626797). {ECO:0000269|PubMed:10626797, CC ECO:0000269|PubMed:12773388, ECO:0000269|PubMed:16291752, CC ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:18591255, CC ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20826784, CC ECO:0000269|PubMed:20929775, ECO:0000269|PubMed:21364656, CC ECO:0000269|PubMed:21536684, ECO:0000269|PubMed:9859993}. CC -!- SUBUNIT: Monomer or homodimer. Exists as a homodimer in the apo CC state and as a monomer in the CPC-bound state. The monomer CC protects cells against apoptosis more efficiently than the dimer. CC Only the dimeric form is capable of enhancing tubulin stability in CC cells. When phosphorylated, interacts with LAMTOR5/HBXIP; the CC resulting complex binds pro-CASP9, as well as active CASP9, but CC much less efficiently. Component of the chromosomal passenger CC complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, CC INCENP, AURKB or AURKC; in the complex forms a triple-helix CC bundle-based subcomplex with INCENP and CDCA8 (PubMed:17956729). CC Interacts with JTB. Interacts (via BIR domain) with histone H3 CC phosphorylated at 'Thr-3' (H3pT3). Interacts with EVI5. Interacts CC with GTP-bound RAN in both the S and M phases of the cell cycle. CC Interacts with USP9X. Interacts with tubulin. Interacts with CC BIRC2/c-IAP1. The acetylated form at Lys-129 interacts with STAT3. CC The monomeric form deacetylated at Lys-129 interacts with CC XPO1/CRM1. The monomeric form interacts with XIAP/BIRC4. Both the CC dimeric and monomeric form can interact with DIABLO/SMAC. CC Interacts with BIRC6/bruce. {ECO:0000269|PubMed:12773388, CC ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:15249581, CC ECO:0000269|PubMed:15665297, ECO:0000269|PubMed:16239925, CC ECO:0000269|PubMed:16291752, ECO:0000269|PubMed:16322459, CC ECO:0000269|PubMed:16427043, ECO:0000269|PubMed:16436504, CC ECO:0000269|PubMed:16764853, ECO:0000269|PubMed:17956729, CC ECO:0000269|PubMed:18329369, ECO:0000269|PubMed:18591255, CC ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:21225229, CC ECO:0000269|PubMed:21536684}. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-518823, EBI-518823; CC O14965:AURKA; NbExp=2; IntAct=EBI-518823, EBI-448680; CC Q96GD4:AURKB; NbExp=13; IntAct=EBI-518823, EBI-624291; CC Q9UQB9:AURKC; NbExp=10; IntAct=EBI-518823, EBI-3926851; CC Q14457:BECN1; NbExp=3; IntAct=EBI-518823, EBI-949378; CC P55211:CASP9; NbExp=2; IntAct=EBI-518823, EBI-516799; CC Q53HL2:CDCA8; NbExp=18; IntAct=EBI-518823, EBI-979174; CC P06493:CDK1; NbExp=6; IntAct=EBI-518823, EBI-444308; CC Q9NR28:DIABLO; NbExp=2; IntAct=EBI-518823, EBI-517508; CC Q86XJ1:GAS2L3; NbExp=4; IntAct=EBI-518823, EBI-9248152; CC Q9NQS7:INCENP; NbExp=10; IntAct=EBI-518823, EBI-307907; CC P62826:RAN; NbExp=7; IntAct=EBI-518823, EBI-286642; CC O14980:XPO1; NbExp=2; IntAct=EBI-518823, EBI-355867; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20627126, CC ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:21364656}. Nucleus CC {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20826784, CC ECO:0000269|PubMed:21364656}. Chromosome CC {ECO:0000269|PubMed:14610074}. Chromosome, centromere CC {ECO:0000269|PubMed:11084331, ECO:0000269|PubMed:14610074, CC ECO:0000269|PubMed:16322459}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:11084331}. Chromosome, centromere, kinetochore CC {ECO:0000269|PubMed:11084331}. Midbody CC {ECO:0000269|PubMed:15665297}. Note=Localizes at the centromeres CC from prophase to metaphase, at the spindle midzone during anaphase CC and a the midbody during telophase and cytokinesis. Accumulates in CC the nucleus upon treatment with leptomycin B (LMB), a XPO1/CRM1 CC nuclear export inhibitor (By similarity). Localizes on chromosome CC arms and inner centromeres from prophase through metaphase. CC Localizes to kinetochores in metaphase, distributes to the midzone CC microtubules in anaphase and at telophase, localizes exclusively CC to the midbody (PubMed:11084331). Colocalizes with AURKB at CC mitotic chromosomes (PubMed:14610074). Acetylation at Lys-129 CC directs its localization to the nucleus by enhancing CC homodimerization and thereby inhibiting XPO1/CRM1-mediated nuclear CC export (PubMed:20826784). {ECO:0000250|UniProtKB:E3SCZ8, CC ECO:0000269|PubMed:11084331, ECO:0000269|PubMed:14610074, CC ECO:0000269|PubMed:20826784}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=Alpha; CC IsoId=O15392-1; Sequence=Displayed; CC Name=2; Synonyms=2B, Beta; CC IsoId=O15392-2; Sequence=VSP_002454; CC Name=3; Synonyms=DeltaEx3; CC IsoId=O15392-3; Sequence=VSP_020338; CC Name=4; Synonyms=3B; CC IsoId=O15392-4; Sequence=VSP_020342; CC Name=5; Synonyms=SI; CC IsoId=O15392-5; Sequence=VSP_020341; CC Name=6; Synonyms=3 alpha; CC IsoId=O15392-6; Sequence=VSP_020339; CC Name=7; Synonyms=2 alpha; CC IsoId=O15392-7; Sequence=VSP_020340; CC -!- TISSUE SPECIFICITY: Expressed only in fetal kidney and liver, and CC to lesser extent, lung and brain (PubMed:10626797). Abundantly CC expressed in adenocarcinoma (lung, pancreas, colon, breast, and CC prostate) and in high-grade lymphomas (PubMed:14741722, CC PubMed:16329164). Also expressed in various renal cell carcinoma CC cell lines (PubMed:10626797). Expressed in cochlea including the CC organ of Corti, the lateral wall, the interdental cells of the CC Limbus as well as in Schwann cells and cells of the cochlear nerve CC and the spiral ganglions (at protein level). Not expressed in CC cells of the inner and outer sulcus or the Reissner's membrane (at CC protein level) (PubMed:21364656, PubMed:20627126). CC {ECO:0000269|PubMed:10626797, ECO:0000269|PubMed:14741722, CC ECO:0000269|PubMed:16329164, ECO:0000269|PubMed:20627126, CC ECO:0000269|PubMed:21364656}. CC -!- DEVELOPMENTAL STAGE: Expression is cell cycle-dependent and peaks CC at mitosis. {ECO:0000269|PubMed:18591255}. CC -!- INDUCTION: Up-regulated by COMP. {ECO:0000269|PubMed:17993464}. CC -!- DOMAIN: The BIR repeat is necessary and sufficient for LAMTOR5 CC binding. {ECO:0000269|PubMed:12773388}. CC -!- PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase CC complex, leading to its degradation. Ubiquitination is required CC for centrosomal targeting. {ECO:0000269|PubMed:16322459, CC ECO:0000269|PubMed:24793696}. CC -!- PTM: In vitro phosphorylation at Thr-117 by AURKB prevents CC interaction with INCENP and localization to mitotic chromosomes CC (PubMed:14610074). Phosphorylation at Thr-48 by CK2 is critical CC for its mitotic and anti-apoptotic activities (PubMed:21252625). CC Phosphorylation at Thr-34 by CDK15 is critical for its anti- CC apoptotic activity (PubMed:24866247). Phosphorylation at Ser-20 by CC AURKC is critical for regulation of proper chromosome alignment CC and segregation, and possibly cytokinesis. CC {ECO:0000269|PubMed:11069302, ECO:0000269|PubMed:14610074, CC ECO:0000269|PubMed:21252625, ECO:0000269|PubMed:24866247, CC ECO:0000269|PubMed:27332895}. CC -!- PTM: Acetylation at Lys-129 by CBP results in its CC homodimerization, while deacetylation promotes the formation of CC monomers which heterodimerize with XPO1/CRM1 which facilitates its CC nuclear export. The acetylated form represses STAT3 CC transactivation. The dynamic equilibrium between its acetylation CC and deacetylation at Lys-129 determines its interaction with CC XPO1/CRM1, its subsequent subcellular localization, and its CC ability to inhibit STAT3 transactivation. CC {ECO:0000269|PubMed:20826784}. CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/birc5/"; 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; U75285; AAC51660.1; -; Genomic_DNA. DR EMBL; AF077350; AAD34226.1; -; mRNA. DR EMBL; AB154416; BAD11155.1; -; mRNA. DR EMBL; AY830084; AAW22624.1; -; mRNA. DR EMBL; AB028869; BAA93676.1; -; mRNA. DR EMBL; AY927772; AAY15202.1; -; mRNA. DR EMBL; DQ227257; ABB76601.1; -; mRNA. DR EMBL; DQ310375; ABC42341.1; -; mRNA. DR EMBL; DQ310376; ABC42342.1; -; mRNA. DR EMBL; DQ310377; ABC42343.1; -; mRNA. DR EMBL; DQ310378; ABC42344.1; -; mRNA. DR EMBL; DQ310379; ABC42345.1; -; mRNA. DR EMBL; CR541740; CAG46540.1; -; mRNA. DR EMBL; AK223428; BAD97148.1; -; mRNA. DR EMBL; AK311917; BAG34858.1; -; mRNA. DR EMBL; AY795969; AAV40840.1; -; Genomic_DNA. DR EMBL; AC087645; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471099; EAW89514.1; -; Genomic_DNA. DR EMBL; BC008718; AAH08718.1; -; mRNA. DR EMBL; BC034148; AAH34148.1; -; mRNA. DR EMBL; BC065497; AAH65497.1; -; mRNA. DR CCDS; CCDS11755.1; -. [O15392-1] DR CCDS; CCDS32751.1; -. [O15392-3] DR CCDS; CCDS32752.1; -. [O15392-2] DR RefSeq; NP_001012270.1; NM_001012270.1. [O15392-3] DR RefSeq; NP_001012271.1; NM_001012271.1. DR RefSeq; NP_001159.2; NM_001168.2. DR UniGene; Hs.744872; -. DR PDB; 1E31; X-ray; 2.71 A; A/B=1-142. DR PDB; 1F3H; X-ray; 2.58 A; A/B=1-142. DR PDB; 1XOX; NMR; -; A/B=1-117. DR PDB; 2QFA; X-ray; 1.40 A; A=1-142. DR PDB; 2RAW; X-ray; 2.40 A; A=1-142. DR PDB; 2RAX; X-ray; 3.30 A; A/E/X=1-120. DR PDB; 3UEC; X-ray; 2.18 A; A=1-142. DR PDB; 3UED; X-ray; 2.70 A; A/C=1-142. DR PDB; 3UEE; X-ray; 2.61 A; A/C=1-142. DR PDB; 3UEF; X-ray; 2.45 A; A/C=1-142. DR PDB; 3UEG; X-ray; 2.80 A; A/B=1-142. DR PDB; 3UEH; X-ray; 2.60 A; A/B=1-142. DR PDB; 3UEI; X-ray; 2.70 A; A/B=1-142. DR PDB; 3UIG; X-ray; 2.40 A; A/B=1-142. DR PDB; 3UIH; X-ray; 2.40 A; A/B=1-142. DR PDB; 3UII; X-ray; 2.60 A; A/B=1-142. DR PDB; 3UIJ; X-ray; 2.70 A; A/B=1-142. DR PDB; 3UIK; X-ray; 2.70 A; A/B=1-142. DR PDB; 4A0I; X-ray; 2.60 A; A/B=1-142. DR PDB; 4A0J; X-ray; 2.80 A; A/B=1-142. DR PDB; 4A0N; X-ray; 2.74 A; A=1-142. DR PDBsum; 1E31; -. DR PDBsum; 1F3H; -. DR PDBsum; 1XOX; -. DR PDBsum; 2QFA; -. DR PDBsum; 2RAW; -. DR PDBsum; 2RAX; -. DR PDBsum; 3UEC; -. DR PDBsum; 3UED; -. DR PDBsum; 3UEE; -. DR PDBsum; 3UEF; -. DR PDBsum; 3UEG; -. DR PDBsum; 3UEH; -. DR PDBsum; 3UEI; -. DR PDBsum; 3UIG; -. DR PDBsum; 3UIH; -. DR PDBsum; 3UII; -. DR PDBsum; 3UIJ; -. DR PDBsum; 3UIK; -. DR PDBsum; 4A0I; -. DR PDBsum; 4A0J; -. DR PDBsum; 4A0N; -. DR ProteinModelPortal; O15392; -. DR SMR; O15392; -. DR BioGrid; 106829; 59. DR ComplexPortal; CPX-111; Survivin homodimer complex. DR ComplexPortal; CPX-116; Chromosomal passenger complex. DR CORUM; O15392; -. DR DIP; DIP-34662N; -. DR ELM; O15392; -. DR IntAct; O15392; 19. DR MINT; O15392; -. DR BindingDB; O15392; -. DR ChEMBL; CHEMBL5989; -. DR DrugBank; DB05141; LY2181308. DR GuidetoPHARMACOLOGY; 2795; -. DR MEROPS; I32.005; -. DR iPTMnet; O15392; -. DR PhosphoSitePlus; O15392; -. DR BioMuta; BIRC5; -. DR EPD; O15392; -. DR MaxQB; O15392; -. DR PeptideAtlas; O15392; -. DR PRIDE; O15392; -. DR ProteomicsDB; 48627; -. DR ProteomicsDB; 48628; -. [O15392-2] DR ProteomicsDB; 48629; -. [O15392-3] DR ProteomicsDB; 48630; -. [O15392-4] DR ProteomicsDB; 48631; -. [O15392-5] DR ProteomicsDB; 48632; -. [O15392-6] DR ProteomicsDB; 48633; -. [O15392-7] DR DNASU; 332; -. DR Ensembl; ENST00000374948; ENSP00000364086; ENSG00000089685. [O15392-3] DR Ensembl; ENST00000590449; ENSP00000465868; ENSG00000089685. [O15392-7] DR Ensembl; ENST00000590925; ENSP00000467336; ENSG00000089685. [O15392-4] DR Ensembl; ENST00000592734; ENSP00000466617; ENSG00000089685. [O15392-6] DR GeneID; 332; -. DR KEGG; hsa:332; -. DR UCSC; uc002jvh.4; human. [O15392-1] DR CTD; 332; -. DR DisGeNET; 332; -. DR EuPathDB; HostDB:ENSG00000089685.14; -. DR GeneCards; BIRC5; -. DR HGNC; HGNC:593; BIRC5. DR HPA; CAB004270; -. DR HPA; HPA002830; -. DR MIM; 603352; gene. DR neXtProt; NX_O15392; -. DR OpenTargets; ENSG00000089685; -. DR PharmGKB; PA25362; -. DR GeneTree; ENSGT00510000047537; -. DR HOGENOM; HOG000172188; -. DR HOVERGEN; HBG080756; -. DR InParanoid; O15392; -. DR KO; K08731; -. DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins. DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain. DR Reactome; R-HSA-68877; Mitotic Prometaphase. DR Reactome; R-HSA-8951664; Neddylation. DR SignaLink; O15392; -. DR SIGNOR; O15392; -. DR ChiTaRS; BIRC5; human. DR EvolutionaryTrace; O15392; -. DR GeneWiki; Survivin; -. DR GenomeRNAi; 332; -. DR PRO; PR:O15392; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; ENSG00000089685; Expressed in 135 organ(s), highest expression level in vagina. DR CleanEx; HS_BIRC5; -. DR ExpressionAtlas; O15392; baseline and differential. DR Genevisible; O15392; HS. DR GO; GO:0005814; C:centriole; IDA:UniProtKB. DR GO; GO:0032133; C:chromosome passenger complex; IPI:UniProtKB. DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB. DR GO; GO:0000777; C:condensed chromosome kinetochore; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0031021; C:interphase microtubule organizing center; IDA:UniProtKB. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB. DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB. DR GO; GO:0050897; F:cobalt ion binding; NAS:UniProtKB. DR GO; GO:0048037; F:cofactor binding; IDA:UniProtKB. DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0008536; F:Ran GTPase binding; IPI:UniProtKB. DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; 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; IMP:UniProtKB. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0051303; P:establishment of chromosome localization; IMP:UniProtKB. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; TAS:UniProtKB. DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB. DR GO; GO:0007094; P:mitotic spindle assembly checkpoint; IMP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:UniProtKB. DR GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:UniProtKB. DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0031503; P:protein-containing complex localization; IMP:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome. DR GO; GO:0007605; P:sensory perception of sound; IEP:UniProtKB. DR CDD; cd00022; BIR; 1. DR InterPro; IPR001370; BIR_rpt. DR Pfam; PF00653; BIR; 1. DR SMART; SM00238; BIR; 1. DR PROSITE; PS50143; BIR_REPEAT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; KW Cell cycle; Cell division; Centromere; Chromosome; KW Chromosome partition; Complete proteome; Cytoplasm; Cytoskeleton; KW Kinetochore; Metal-binding; Microtubule; Mitosis; Nucleus; KW Phosphoprotein; Polymorphism; Protease inhibitor; Reference proteome; KW Repressor; Thiol protease inhibitor; Transcription; KW Transcription regulation; Ubl conjugation; Zinc. FT CHAIN 1 142 Baculoviral IAP repeat-containing protein FT 5. FT /FTId=PRO_0000122356. FT REPEAT 18 88 BIR. FT METAL 57 57 Zinc. {ECO:0000244|PDB:2QFA, FT ECO:0000269|PubMed:17956729}. FT METAL 60 60 Zinc. {ECO:0000244|PDB:2QFA, FT ECO:0000269|PubMed:17956729}. FT METAL 77 77 Zinc. {ECO:0000244|PDB:2QFA, FT ECO:0000269|PubMed:17956729}. FT METAL 84 84 Zinc. {ECO:0000244|PDB:2QFA, FT ECO:0000269|PubMed:17956729}. FT MOD_RES 20 20 Phosphoserine; by AURKC. FT {ECO:0000269|PubMed:27332895}. FT MOD_RES 23 23 N6-acetyllysine. FT {ECO:0000269|PubMed:20826784}. FT MOD_RES 34 34 Phosphothreonine; by CDK1 and CDK15. FT {ECO:0000244|PubMed:18691976, FT ECO:0000269|PubMed:11069302, FT ECO:0000269|PubMed:24866247}. FT MOD_RES 48 48 Phosphothreonine; by CK2; in vitro. FT {ECO:0000269|PubMed:21252625}. FT MOD_RES 90 90 N6-acetyllysine. FT {ECO:0000269|PubMed:20826784}. FT MOD_RES 110 110 N6-acetyllysine. FT {ECO:0000269|PubMed:20826784}. FT MOD_RES 112 112 N6-acetyllysine. FT {ECO:0000269|PubMed:20826784}. FT MOD_RES 115 115 N6-acetyllysine. FT {ECO:0000269|PubMed:20826784}. FT MOD_RES 117 117 Phosphothreonine; by AURKB. FT {ECO:0000269|PubMed:14610074}. FT MOD_RES 121 121 N6-acetyllysine. FT {ECO:0000269|PubMed:20826784}. FT MOD_RES 129 129 N6-acetyllysine. FT {ECO:0000269|PubMed:20826784}. FT VAR_SEQ 74 142 IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIA FT KETNNKKKEFEETAKKVRRAIEQLAAMD -> MQRKPTIRR FT KNLRKLRRKCAVPSSSWLPWIEASGRSCLVPEWLHHFQGLF FT PGATSLPVGPLAMS (in isoform 3). FT {ECO:0000303|PubMed:10626797}. FT /FTId=VSP_020338. FT VAR_SEQ 74 142 IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIA FT KETNNKKKEFEETAKKVRRAIEQLAAMD -> MRELC (in FT isoform 6). {ECO:0000303|Ref.8}. FT /FTId=VSP_020339. FT VAR_SEQ 74 142 IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIA FT KETNNKKKEFEETAKKVRRAIEQLAAMD -> M (in FT isoform 7). {ECO:0000303|Ref.7}. FT /FTId=VSP_020340. FT VAR_SEQ 74 74 I -> IGPGTVAYACNTSTLGGRGGRITR (in isoform FT 2). {ECO:0000303|PubMed:10626797, FT ECO:0000303|Ref.6}. FT /FTId=VSP_002454. FT VAR_SEQ 105 142 DRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD -> FT VRETLPPPRSFIR (in isoform 5). FT {ECO:0000303|PubMed:16329164}. FT /FTId=VSP_020341. FT VAR_SEQ 114 142 AKETNNKKKEFEETAKKVRRAIEQLAAMD -> ERALLAE FT (in isoform 4). FT {ECO:0000303|PubMed:14741722}. FT /FTId=VSP_020342. FT VARIANT 129 129 K -> E (loss of acetylation; localization FT primarily within the cytoplasm; increased FT likelihood of existing as monomer; FT stronger binding to XPO1/CRM1; FT dbSNP:rs2071214). FT {ECO:0000269|PubMed:16625196, FT ECO:0000269|PubMed:20826784}. FT /FTId=VAR_021071. FT MUTAGEN 18 18 R->A: Disrupts interaction with histone FT H3pT3, no effect on interaction with FT INCENP. {ECO:0000269|PubMed:20929775}. FT MUTAGEN 23 23 K->R: Increases ubiquitination and blocks FT dissociation from centromeres; when FT associated with R-62; R-78 and R-79. FT {ECO:0000269|PubMed:16322459}. FT MUTAGEN 25 25 W->A: Disrupts interaction with histone FT H3pT3, no effect on interaction with FT INCENP. {ECO:0000269|PubMed:20929775}. FT MUTAGEN 33 33 C->R: Disrupts interaction with histone FT H3pT3, no effect on interaction with FT INCENP. {ECO:0000269|PubMed:20929775}. FT MUTAGEN 34 34 T->A: Loss of LAMTOR5 binding. FT {ECO:0000269|PubMed:12773388}. FT MUTAGEN 34 34 T->E: Higher affinity for LAMTOR5 FT binding. {ECO:0000269|PubMed:12773388}. FT MUTAGEN 48 48 T->A,E: Localizes normally during mitosis FT but cannot support cell proliferation. FT Increased affinity for CDCA8/borealin. FT {ECO:0000269|PubMed:21252625}. FT MUTAGEN 57 57 C->A: Disrupts interaction with histone FT H3pT3, no effect on interaction with FT INCENP. {ECO:0000269|PubMed:20929775}. FT MUTAGEN 62 62 K->R: Increases ubiquitination and blocks FT dissociation from centromeres; when FT associated with R-23; R-78 and R-79. FT {ECO:0000269|PubMed:16322459}. FT MUTAGEN 65 65 E->A: Almost abolishes RAN-binding. Does FT not disrupt binding to AURKB or CDCA8. FT Disrupts mitotic spindle assembly. Does FT not disrupt nuclear export. FT {ECO:0000269|PubMed:18591255}. FT MUTAGEN 67 67 W->A: Disrupts interaction with histone FT H3pT3, no effect on interaction with FT INCENP. {ECO:0000269|PubMed:20929775}. FT MUTAGEN 70 70 D->A: No change. Loss of interaction with FT AURKB; when associated with A-71. FT {ECO:0000269|PubMed:16762323}. FT MUTAGEN 71 71 D->A: No change. Loss of interaction with FT AURKB; when associated with A-70. FT {ECO:0000269|PubMed:16762323}. FT MUTAGEN 78 78 K->R: Increases ubiquitination and blocks FT dissociation from centromeres; when FT associated with R-23; R-62 and R-79. FT {ECO:0000269|PubMed:16322459}. FT MUTAGEN 79 79 K->R: Increases ubiquitination and blocks FT dissociation from centromeres; when FT associated with R-23; R-62 and R-78. FT {ECO:0000269|PubMed:16322459}. FT MUTAGEN 84 84 C->A: Loss of cytoprotection. FT MUTAGEN 117 117 T->A: Prevents phosphorylation by AURKB. FT Still able to localize correctly but FT prevents interaction with INCENP. FT {ECO:0000269|PubMed:14610074}. FT MUTAGEN 117 117 T->E: Mimics phosphorylation. Disrupts FT subcellular localization during mitosis FT and prevents interaction with INCENP. FT {ECO:0000269|PubMed:14610074}. FT MUTAGEN 129 129 K->A,Q: Mimics acetylation. Localization FT primarily within the nucleus. FT {ECO:0000269|PubMed:20826784}. FT MUTAGEN 129 129 K->R: Loss of acetylation. Localization FT primarily within the cytoplasm. FT {ECO:0000269|PubMed:20826784}. FT CONFLICT 57 58 CF -> WV (in Ref. 5; AAW22624). FT {ECO:0000305}. FT CONFLICT 58 58 F -> L (in Ref. 11; BAD97148). FT {ECO:0000305}. FT CONFLICT 128 128 A -> V (in Ref. 9; CAG46540). FT {ECO:0000305}. FT TURN 8 10 {ECO:0000244|PDB:2QFA}. FT HELIX 11 13 {ECO:0000244|PDB:2QFA}. FT HELIX 15 20 {ECO:0000244|PDB:2QFA}. FT STRAND 31 33 {ECO:0000244|PDB:3UEC}. FT HELIX 35 40 {ECO:0000244|PDB:2QFA}. FT STRAND 43 45 {ECO:0000244|PDB:2QFA}. FT STRAND 49 51 {ECO:0000244|PDB:3UIG}. FT STRAND 55 57 {ECO:0000244|PDB:2QFA}. FT TURN 58 60 {ECO:0000244|PDB:2QFA}. FT STRAND 63 65 {ECO:0000244|PDB:3UEC}. FT HELIX 73 80 {ECO:0000244|PDB:2QFA}. FT TURN 81 83 {ECO:0000244|PDB:1F3H}. FT HELIX 85 88 {ECO:0000244|PDB:2QFA}. FT HELIX 93 95 {ECO:0000244|PDB:2QFA}. FT HELIX 98 139 {ECO:0000244|PDB:2QFA}. SQ SEQUENCE 142 AA; 16389 MW; 9E7CADCDF2822286 CRC64; MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN EPDLAQCFFC FKELEGWEPD DDPIEEHKKH SSGCAFLSVK KQFEELTLGE FLKLDRERAK NKIAKETNNK KKEFEETAKK VRRAIEQLAA MD //