BIRC5_HUMAN
ID BIRC5_HUMAN Reviewed; 142 AA.
AC O15392; A2SUH6; B2R4R1; Q2I3N8; Q4VGX0; Q53F61; Q5MGC6; Q6FHL2; Q75SP2;
AC Q9P2W8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 235.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 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 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-cycle
RT 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 gene
RT 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 variant
RT 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 insertion
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., 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 the
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 of
RT 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 THR-117,
RP 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 that is
RT essential for its localization and binding to inner centromere protein
RT (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., Honda R.,
RA 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 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, UBIQUITINATION, AND
RP 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 Survivin
RT 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 the
RT 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., Wong F.-H.,
RA Chou C.-K., Chen C.-M.;
RT "Borealin/Dasra B is a cell cycle-regulated chromosomal passenger protein
RT and its nuclear accumulation is linked to poor prognosis for human gastric
RT 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., Ko Ferrigno P.,
RA 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., 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 by
RT 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 BY
RP 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 the
RT 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 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., Mann W.J.;
RT "Expression analysis suggests a potential cytoprotective role of Birc5 in
RT 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 and
RT anti-apoptotic activities and can be phosphorylated by CK2 in 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., Xiong Y.;
RT "CUL9 mediates the functions of the 3M complex and ubiquitylates survivin
RT to maintain genome integrity.";
RL Mol. Cell 54:805-819(2014).
RN [43]
RP FUNCTION, INTERACTION WITH FBXL7, AND MUTAGENESIS OF 90-LYS-LYS-91 AND
RP GLU-126.
RX PubMed=25778398; DOI=10.1074/jbc.m114.629931;
RA Liu Y., Lear T., Iannone O., Shiva S., Corey C., Rajbhandari S., Jerome J.,
RA Chen B.B., Mallampalli R.K.;
RT "The Proapoptotic F-box Protein Fbxl7 Regulates Mitochondrial Function by
RT Mediating the Ubiquitylation and Proteasomal Degradation of Survivin.";
RL J. Biol. Chem. 290:11843-11852(2015).
RN [44]
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 distinct
RT features compared with Aurora-B chromosome passenger protein complex.";
RL PLoS ONE 11:E0157305-E0157305(2016).
RN [45]
RP FUNCTION, AND INTERACTION WITH FBXL7.
RX PubMed=28218735; DOI=10.1038/oncsis.2016.80;
RA Kamran M., Long Z.J., Xu D., Lv S.S., Liu B., Wang C.L., Xu J., Lam E.W.,
RA Liu Q.;
RT "Aurora kinase A regulates Survivin stability through targeting FBXL7 in
RT gastric cancer drug resistance and prognosis.";
RL Oncogenesis 6:E298-E298(2017).
RN [46]
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 with
RT two unusual alpha-helical extensions.";
RL Mol. Cell 6:183-189(2000).
RN [47]
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 dimeric
RT arrangement.";
RL Nat. Struct. Biol. 7:602-608(2000).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT,
RP 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., 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 [49]
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 proper
RT chromosome segregation.";
RL Biochemistry 48:6783-6793(2009).
CC -!- FUNCTION: Multitasking protein that has dual roles in promoting cell
CC proliferation and preventing apoptosis (PubMed:9859993,
CC PubMed:21364656, PubMed:20627126, PubMed:25778398, PubMed:28218735).
CC Component of a chromosome passage protein complex (CPC) which is
CC essential for chromosome alignment and segregation during mitosis and
CC cytokinesis (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 center
CC spindle by associating with polymerized microtubules (PubMed:20826784).
CC Involved in the recruitment of CPC to centromeres during early mitosis
CC via association with histone H3 phosphorylated at 'Thr-3' (H3pT3)
CC during mitosis (PubMed:20929775). The complex with RAN plays a role in
CC mitotic 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 in
CC G2/M phase (PubMed:9859993). The acetylated form represses STAT3
CC transactivation of target gene promoters (PubMed:20826784). May play a
CC role in neoplasia (PubMed:10626797). Inhibitor of CASP3 and CASP7
CC (PubMed:21536684). Essential for the maintenance of mitochondrial
CC integrity and function (PubMed:25778398). Isoform 2 and isoform 3 do
CC not appear to play vital roles in mitosis (PubMed:12773388,
CC PubMed:16291752). Isoform 3 shows a marked reduction in its anti-
CC apoptotic effects 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:25778398,
CC ECO:0000269|PubMed:28218735, ECO:0000269|PubMed:9859993}.
CC -!- SUBUNIT: Monomer or homodimer. Exists as a homodimer in the apo state
CC and as a monomer in the CPC-bound state. The monomer protects cells
CC against apoptosis more efficiently than the dimer. Only the dimeric
CC form is capable of enhancing tubulin stability in cells. When
CC phosphorylated, interacts with LAMTOR5/HBXIP; the resulting complex
CC binds pro-CASP9, as well as active CASP9, but much less efficiently.
CC Component of the chromosomal passenger complex (CPC) composed of at
CC least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the
CC complex forms a triple-helix bundle-based subcomplex with INCENP and
CC CDCA8 (PubMed:17956729). Interacts with JTB. Interacts (via BIR domain)
CC with histone H3 phosphorylated at 'Thr-3' (H3pT3). Interacts with EVI5.
CC Interacts with GTP-bound RAN in both the S and M phases of the cell
CC cycle. Interacts with USP9X. Interacts with tubulin. Interacts with
CC BIRC2/c-IAP1. The acetylated form at Lys-129 interacts with STAT3. The
CC monomeric form deacetylated at Lys-129 interacts with XPO1/CRM1. The
CC monomeric form interacts with XIAP/BIRC4. Both the dimeric and
CC monomeric form can interact with DIABLO/SMAC. Interacts with
CC BIRC6/bruce. Interacts with FBXL7; this interaction facilitates the
CC polyubiquitination and subsequent proteasomal degradation of BIRC5 by
CC the SCF(FBXL7) E3 ubiquitin-protein ligase complex (PubMed:25778398,
CC PubMed:28218735). {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, ECO:0000269|PubMed:25778398,
CC ECO:0000269|PubMed:28218735}.
CC -!- INTERACTION:
CC O15392; Q92870-2: APBB2; NbExp=3; IntAct=EBI-518823, EBI-21535880;
CC O15392; P05067: APP; NbExp=3; IntAct=EBI-518823, EBI-77613;
CC O15392; P05067-2: APP; NbExp=3; IntAct=EBI-518823, EBI-17264467;
CC O15392; O14965: AURKA; NbExp=2; IntAct=EBI-518823, EBI-448680;
CC O15392; Q96GD4: AURKB; NbExp=13; IntAct=EBI-518823, EBI-624291;
CC O15392; Q9UQB9: AURKC; NbExp=10; IntAct=EBI-518823, EBI-3926851;
CC O15392; Q14457: BECN1; NbExp=3; IntAct=EBI-518823, EBI-949378;
CC O15392; O15392: BIRC5; NbExp=2; IntAct=EBI-518823, EBI-518823;
CC O15392; Q15834: CCDC85B; NbExp=3; IntAct=EBI-518823, EBI-739674;
CC O15392; Q53HL2: CDCA8; NbExp=19; IntAct=EBI-518823, EBI-979174;
CC O15392; P06493: CDK1; NbExp=6; IntAct=EBI-518823, EBI-444308;
CC O15392; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-518823, EBI-25840379;
CC O15392; Q9NR28: DIABLO; NbExp=2; IntAct=EBI-518823, EBI-517508;
CC O15392; Q86XJ1: GAS2L3; NbExp=4; IntAct=EBI-518823, EBI-9248152;
CC O15392; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-518823, EBI-11110431;
CC O15392; P42858: HTT; NbExp=15; IntAct=EBI-518823, EBI-466029;
CC O15392; Q9NQS7: INCENP; NbExp=10; IntAct=EBI-518823, EBI-307907;
CC O15392; A0A0C4DGV4: LAMTOR5; NbExp=3; IntAct=EBI-518823, EBI-10173304;
CC O15392; Q96CV9: OPTN; NbExp=3; IntAct=EBI-518823, EBI-748974;
CC O15392; Q7Z412: PEX26; NbExp=3; IntAct=EBI-518823, EBI-752057;
CC O15392; Q9BXM7: PINK1; NbExp=3; IntAct=EBI-518823, EBI-2846068;
CC O15392; P62826: RAN; NbExp=7; IntAct=EBI-518823, EBI-286642;
CC O15392; P37840: SNCA; NbExp=3; IntAct=EBI-518823, EBI-985879;
CC O15392; Q13148: TARDBP; NbExp=6; IntAct=EBI-518823, EBI-372899;
CC O15392; P09936: UCHL1; NbExp=3; IntAct=EBI-518823, EBI-714860;
CC O15392; O14980: XPO1; NbExp=2; IntAct=EBI-518823, EBI-355867;
CC O15392-1; Q96GD4: AURKB; NbExp=2; IntAct=EBI-518838, EBI-624291;
CC O15392-1; O15392-1: BIRC5; NbExp=2; IntAct=EBI-518838, EBI-518838;
CC O15392-1; Q53HL2: CDCA8; NbExp=2; IntAct=EBI-518838, EBI-979174;
CC O15392-2; Q96GD4: AURKB; NbExp=2; IntAct=EBI-518842, EBI-624291;
CC O15392-2; O15392-1: BIRC5; NbExp=2; IntAct=EBI-518842, EBI-518838;
CC O15392-2; Q53HL2: CDCA8; NbExp=2; IntAct=EBI-518842, EBI-979174;
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 {ECO:0000269|PubMed:14610074}.
CC Chromosome, centromere {ECO:0000269|PubMed:11084331,
CC ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:16322459}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:11084331}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:11084331}. Midbody
CC {ECO:0000269|PubMed:15665297}. Note=Localizes at the centromeres from
CC prophase to metaphase, at the spindle midzone during anaphase and a the
CC midbody during telophase and cytokinesis. Accumulates in the nucleus
CC upon treatment with leptomycin B (LMB), a XPO1/CRM1 nuclear export
CC inhibitor (By similarity). Localizes on chromosome arms and inner
CC centromeres from prophase through metaphase. Localizes to kinetochores
CC in metaphase, distributes to the midzone microtubules in anaphase and
CC at telophase, localizes exclusively to the midbody (PubMed:11084331).
CC Colocalizes with AURKB at mitotic chromosomes (PubMed:14610074).
CC Acetylation at Lys-129 directs its localization to the nucleus by
CC enhancing homodimerization and thereby inhibiting XPO1/CRM1-mediated
CC nuclear 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 to
CC lesser extent, lung and brain (PubMed:10626797). Abundantly expressed
CC in adenocarcinoma (lung, pancreas, colon, breast, and prostate) and in
CC high-grade lymphomas (PubMed:14741722, PubMed:16329164). Also expressed
CC in various renal cell carcinoma cell lines (PubMed:10626797). Expressed
CC in cochlea including the organ of Corti, the lateral wall, the
CC interdental cells of the Limbus as well as in Schwann cells and cells
CC of the cochlear nerve and the spiral ganglions (at protein level). Not
CC expressed in cells of the inner and outer sulcus or the Reissner's
CC membrane (at 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 at
CC 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 binding.
CC {ECO:0000269|PubMed:12773388}.
CC -!- PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex,
CC leading to its degradation. Ubiquitination is required for centrosomal
CC targeting. {ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:24793696}.
CC -!- PTM: In vitro phosphorylation at Thr-117 by AURKB prevents interaction
CC with INCENP and localization to mitotic chromosomes (PubMed:14610074).
CC Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-
CC apoptotic activities (PubMed:21252625). Phosphorylation at Thr-34 by
CC CDK15 is critical for its anti-apoptotic activity (PubMed:24866247).
CC Phosphorylation at Ser-20 by AURKC is critical for regulation of proper
CC chromosome alignment 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 homodimerization,
CC while deacetylation promotes the formation of monomers which
CC heterodimerize with XPO1/CRM1 which facilitates its nuclear export. The
CC acetylated form represses STAT3 transactivation. The dynamic
CC equilibrium between its acetylation and deacetylation at Lys-129
CC determines its interaction with XPO1/CRM1, its subsequent subcellular
CC localization, and its 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/";
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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 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 PDB; 6SHO; X-ray; 3.20 A; A/B=1-142.
DR PDB; 6YIE; X-ray; 3.49 A; A/D=1-142.
DR PDB; 6YIF; X-ray; 1.81 A; A=1-142.
DR PDB; 6YIH; X-ray; 2.55 A; A=1-142.
DR PDB; 7LBK; X-ray; 2.70 A; A/B=1-142.
DR PDB; 7LBO; X-ray; 2.50 A; A/B=1-142.
DR PDB; 7LBP; X-ray; 2.60 A; A/C=1-142.
DR PDB; 7LBQ; X-ray; 2.69 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 PDBsum; 6SHO; -.
DR PDBsum; 6YIE; -.
DR PDBsum; 6YIF; -.
DR PDBsum; 6YIH; -.
DR PDBsum; 7LBK; -.
DR PDBsum; 7LBO; -.
DR PDBsum; 7LBP; -.
DR PDBsum; 7LBQ; -.
DR AlphaFoldDB; O15392; -.
DR BMRB; O15392; -.
DR SMR; O15392; -.
DR BioGRID; 106829; 93.
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; 50.
DR MINT; O15392; -.
DR BindingDB; O15392; -.
DR ChEMBL; CHEMBL5989; -.
DR DrugBank; DB04115; Berberine.
DR DrugBank; DB05141; LY2181308.
DR DrugBank; DB00206; Reserpine.
DR DrugCentral; O15392; -.
DR GuidetoPHARMACOLOGY; 2795; -.
DR MEROPS; I32.005; -.
DR iPTMnet; O15392; -.
DR PhosphoSitePlus; O15392; -.
DR BioMuta; BIRC5; -.
DR EPD; O15392; -.
DR jPOST; O15392; -.
DR MassIVE; O15392; -.
DR MaxQB; O15392; -.
DR PeptideAtlas; O15392; -.
DR PRIDE; O15392; -.
DR ProteomicsDB; 48627; -. [O15392-1]
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 ABCD; O15392; 5 sequenced antibodies.
DR Antibodypedia; 1073; 1805 antibodies from 53 providers.
DR DNASU; 332; -.
DR Ensembl; ENST00000374948.6; ENSP00000364086.1; ENSG00000089685.15. [O15392-3]
DR Ensembl; ENST00000590449.1; ENSP00000465868.1; ENSG00000089685.15. [O15392-7]
DR Ensembl; ENST00000590925.6; ENSP00000467336.1; ENSG00000089685.15. [O15392-4]
DR Ensembl; ENST00000592734.5; ENSP00000466617.1; ENSG00000089685.15. [O15392-6]
DR GeneID; 332; -.
DR KEGG; hsa:332; -.
DR UCSC; uc002jvh.4; human. [O15392-1]
DR CTD; 332; -.
DR DisGeNET; 332; -.
DR GeneCards; BIRC5; -.
DR HGNC; HGNC:593; BIRC5.
DR HPA; ENSG00000089685; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MIM; 603352; gene.
DR neXtProt; NX_O15392; -.
DR OpenTargets; ENSG00000089685; -.
DR PharmGKB; PA25362; -.
DR VEuPathDB; HostDB:ENSG00000089685; -.
DR GeneTree; ENSGT00510000047537; -.
DR HOGENOM; CLU_1869818_0_0_1; -.
DR InParanoid; O15392; -.
DR OrthoDB; 1404665at2759; -.
DR PathwayCommons; O15392; -.
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 Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; O15392; -.
DR SIGNOR; O15392; -.
DR BioGRID-ORCS; 332; 805 hits in 1083 CRISPR screens.
DR ChiTaRS; BIRC5; human.
DR EvolutionaryTrace; O15392; -.
DR GeneWiki; Survivin; -.
DR GenomeRNAi; 332; -.
DR Pharos; O15392; Tchem.
DR PRO; PR:O15392; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O15392; protein.
DR Bgee; ENSG00000089685; Expressed in ventricular zone and 125 other tissues.
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: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:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:ComplexPortal.
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:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:1990713; C:survivin complex; IPI:ComplexPortal.
DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR GO; GO:0050897; F:cobalt ion binding; NAS:UniProtKB.
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:0031267; F:small 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:0051301; P:cell division; IMP:UniProtKB.
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 signaling; IMP:UniProtKB.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IC:ComplexPortal.
DR GO; GO:0007052; P:mitotic spindle organization; IC:ComplexPortal.
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:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population 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:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IC:ComplexPortal.
DR GO; GO:1903490; P:positive regulation of mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; IC:ComplexPortal.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0031503; P:protein-containing complex localization; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IEA:UniProt.
DR GO; GO:0007605; P:sensory perception of sound; IEP:UniProtKB.
DR CDD; cd00022; BIR; 1.
DR IDEAL; IID00186; -.
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; Cell cycle;
KW Cell division; Centromere; Chromosome; Chromosome partition; Cytoplasm;
KW Cytoskeleton; Kinetochore; Metal-binding; Microtubule; Mitosis; Nucleus;
KW Phosphoprotein; Protease inhibitor; Reference proteome; Repressor;
KW Thiol protease inhibitor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc.
FT CHAIN 1..142
FT /note="Baculoviral IAP repeat-containing protein 5"
FT /id="PRO_0000122356"
FT REPEAT 18..88
FT /note="BIR"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17956729,
FT ECO:0007744|PDB:2QFA"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17956729,
FT ECO:0007744|PDB:2QFA"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17956729,
FT ECO:0007744|PDB:2QFA"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17956729,
FT ECO:0007744|PDB:2QFA"
FT SITE 126
FT /note="Interaction with FBXL7"
FT /evidence="ECO:0000269|PubMed:25778398"
FT MOD_RES 20
FT /note="Phosphoserine; by AURKC"
FT /evidence="ECO:0000269|PubMed:27332895"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20826784"
FT MOD_RES 34
FT /note="Phosphothreonine; by CDK1 and CDK15"
FT /evidence="ECO:0000269|PubMed:11069302,
FT ECO:0000269|PubMed:24866247, ECO:0007744|PubMed:18691976"
FT MOD_RES 48
FT /note="Phosphothreonine; by CK2; in vitro"
FT /evidence="ECO:0000269|PubMed:21252625"
FT MOD_RES 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20826784"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20826784"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20826784"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20826784"
FT MOD_RES 117
FT /note="Phosphothreonine; by AURKB"
FT /evidence="ECO:0000269|PubMed:14610074"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20826784"
FT MOD_RES 129
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20826784"
FT VAR_SEQ 74..142
FT /note="IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFE
FT ETAKKVRRAIEQLAAMD -> MQRKPTIRRKNLRKLRRKCAVPSSSWLPWIEASGRSCL
FT VPEWLHHFQGLFPGATSLPVGPLAMS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10626797"
FT /id="VSP_020338"
FT VAR_SEQ 74..142
FT /note="IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFE
FT ETAKKVRRAIEQLAAMD -> MRELC (in isoform 6)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_020339"
FT VAR_SEQ 74..142
FT /note="IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFE
FT ETAKKVRRAIEQLAAMD -> M (in isoform 7)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_020340"
FT VAR_SEQ 74
FT /note="I -> IGPGTVAYACNTSTLGGRGGRITR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10626797, ECO:0000303|Ref.6"
FT /id="VSP_002454"
FT VAR_SEQ 105..142
FT /note="DRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD -> VRETLPPPRS
FT FIR (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16329164"
FT /id="VSP_020341"
FT VAR_SEQ 114..142
FT /note="AKETNNKKKEFEETAKKVRRAIEQLAAMD -> ERALLAE (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14741722"
FT /id="VSP_020342"
FT VARIANT 129
FT /note="K -> E (loss of acetylation; localization primarily
FT within the cytoplasm; increased likelihood of existing as
FT monomer; stronger binding to XPO1/CRM1; dbSNP:rs2071214)"
FT /evidence="ECO:0000269|PubMed:16625196,
FT ECO:0000269|PubMed:20826784"
FT /id="VAR_021071"
FT MUTAGEN 18
FT /note="R->A: Disrupts interaction with histone H3pT3, no
FT effect on interaction with INCENP."
FT /evidence="ECO:0000269|PubMed:20929775"
FT MUTAGEN 23
FT /note="K->R: Increases ubiquitination and blocks
FT dissociation from centromeres; when associated with R-62;
FT R-78 and R-79."
FT /evidence="ECO:0000269|PubMed:16322459"
FT MUTAGEN 25
FT /note="W->A: Disrupts interaction with histone H3pT3, no
FT effect on interaction with INCENP."
FT /evidence="ECO:0000269|PubMed:20929775"
FT MUTAGEN 33
FT /note="C->R: Disrupts interaction with histone H3pT3, no
FT effect on interaction with INCENP."
FT /evidence="ECO:0000269|PubMed:20929775"
FT MUTAGEN 34
FT /note="T->A: Loss of LAMTOR5 binding."
FT /evidence="ECO:0000269|PubMed:12773388"
FT MUTAGEN 34
FT /note="T->E: Higher affinity for LAMTOR5 binding."
FT /evidence="ECO:0000269|PubMed:12773388"
FT MUTAGEN 48
FT /note="T->A,E: Localizes normally during mitosis but cannot
FT support cell proliferation. Increased affinity for
FT CDCA8/borealin."
FT /evidence="ECO:0000269|PubMed:21252625"
FT MUTAGEN 57
FT /note="C->A: Disrupts interaction with histone H3pT3, no
FT effect on interaction with INCENP."
FT /evidence="ECO:0000269|PubMed:20929775"
FT MUTAGEN 62
FT /note="K->R: Increases ubiquitination and blocks
FT dissociation from centromeres; when associated with R-23;
FT R-78 and R-79."
FT /evidence="ECO:0000269|PubMed:16322459"
FT MUTAGEN 65
FT /note="E->A: Almost abolishes RAN-binding. Does not disrupt
FT binding to AURKB or CDCA8. Disrupts mitotic spindle
FT assembly. Does not disrupt nuclear export."
FT /evidence="ECO:0000269|PubMed:18591255"
FT MUTAGEN 67
FT /note="W->A: Disrupts interaction with histone H3pT3, no
FT effect on interaction with INCENP."
FT /evidence="ECO:0000269|PubMed:20929775"
FT MUTAGEN 70
FT /note="D->A: No change. Loss of interaction with AURKB;
FT when associated with A-71."
FT /evidence="ECO:0000269|PubMed:16762323"
FT MUTAGEN 71
FT /note="D->A: No change. Loss of interaction with AURKB;
FT when associated with A-70."
FT /evidence="ECO:0000269|PubMed:16762323"
FT MUTAGEN 78
FT /note="K->R: Increases ubiquitination and blocks
FT dissociation from centromeres; when associated with R-23;
FT R-62 and R-79."
FT /evidence="ECO:0000269|PubMed:16322459"
FT MUTAGEN 79
FT /note="K->R: Increases ubiquitination and blocks
FT dissociation from centromeres; when associated with R-23;
FT R-62 and R-78."
FT /evidence="ECO:0000269|PubMed:16322459"
FT MUTAGEN 84
FT /note="C->A: Loss of cytoprotection."
FT MUTAGEN 90..91
FT /note="KK->RR: Loss of FBXL7 mediated polyubiquitination."
FT /evidence="ECO:0000269|PubMed:25778398"
FT MUTAGEN 117
FT /note="T->A: Prevents phosphorylation by AURKB. Still able
FT to localize correctly but prevents interaction with
FT INCENP."
FT /evidence="ECO:0000269|PubMed:14610074"
FT MUTAGEN 117
FT /note="T->E: Mimics phosphorylation. Disrupts subcellular
FT localization during mitosis and prevents interaction with
FT INCENP."
FT /evidence="ECO:0000269|PubMed:14610074"
FT MUTAGEN 126
FT /note="E->A: Loss of FBXL7 binding."
FT /evidence="ECO:0000269|PubMed:25778398"
FT MUTAGEN 129
FT /note="K->A,Q: Mimics acetylation. Localization primarily
FT within the nucleus."
FT /evidence="ECO:0000269|PubMed:20826784"
FT MUTAGEN 129
FT /note="K->R: Loss of acetylation. Localization primarily
FT within the cytoplasm."
FT /evidence="ECO:0000269|PubMed:20826784"
FT CONFLICT 57..58
FT /note="CF -> WV (in Ref. 5; AAW22624)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="F -> L (in Ref. 11; BAD97148)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="A -> V (in Ref. 9; CAG46540)"
FT /evidence="ECO:0000305"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2QFA"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2QFA"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:2QFA"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:6YIF"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:2QFA"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2QFA"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3UIG"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2QFA"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:2QFA"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6YIF"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:2QFA"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1F3H"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:2QFA"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2QFA"
FT HELIX 98..139
FT /evidence="ECO:0007829|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
