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Baculoviral IAP repeat-containing protein 5 (Apoptosis inhibitor 4) (Apoptosis inhibitor survivin)

 BIRC5_HUMAN             Reviewed;         142 AA.
O15392; A2SUH6; B2R4R1; Q2I3N8; Q4VGX0; Q53F61; Q5MGC6; Q6FHL2;
Q75SP2; Q9P2W8;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
21-MAR-2012, sequence version 3.
27-SEP-2017, entry version 204.
RecName: Full=Baculoviral IAP repeat-containing protein 5;
AltName: Full=Apoptosis inhibitor 4;
AltName: Full=Apoptosis inhibitor survivin;
Name=BIRC5; Synonyms=API4, IAP4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=9256286; DOI=10.1038/nm0897-917;
Ambrosini G., Adida C., Altieri D.C.;
"A novel anti-apoptosis gene, survivin, expressed in cancer and
lymphoma.";
Nat. Med. 3:917-921(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=10626797;
Mahotka C., Wenzel M., Springer E., Gabbert H.E., Gerharz C.D.;
"Survivin-deltaEx3 and survivin-2B: two novel splice variants of the
apoptosis inhibitor survivin with different antiapoptotic
properties.";
Cancer Res. 59:6097-6102(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
PubMed=11084331; DOI=10.1016/S0960-9822(00)00769-7;
Uren A.G., Wong L., Pakusch M., Fowler K.J., Burrows F.J., Vaux D.L.,
Choo K.H.;
"Survivin and the inner centromere protein INCENP show similar cell-
cycle localization and gene knockout phenotype.";
Curr. Biol. 10:1319-1328(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
TISSUE=Myeloid leukemia cell;
PubMed=14741722; DOI=10.1016/j.bbrc.2003.12.178;
Badran A., Yoshida A., Ishikawa K., Goi T., Yamaguchi A., Ueda T.,
Inuzuka M.;
"Identification of a novel splice variant of the human anti-apoptosis
gene survivin.";
Biochem. Biophys. Res. Commun. 314:902-907(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND TISSUE SPECIFICITY.
TISSUE=Mammary cancer;
PubMed=16329164; DOI=10.1080/10425170500226490;
Zheng W., Ma X., Wei D., Wang T., Ma Y., Yang S.;
"Molecular cloning and bioinformatics analysis of a novel spliced
variant of survivin from human breast cancer cells.";
DNA Seq. 16:321-328(2005).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Neuroblastoma;
Kageyama H., Islam A., Takayasu H., Nakagawara A.;
"An isoform of survivin (survivin-beta) which has 23 amino acids
insertion into the BIR domain.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
Caldas H., Honsey L.E., Altura R.A.;
"Survivin 2 alpha: a novel survivin splice variant expressed in human
malignancies.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
TISSUE=Myeloid leukemia cell;
Vietri M.T., Cioffi M., Sessa M., Sica V., Molinari A.M.;
"Identification of a novel survivin splicing variant 3alpha in acute
myeloid leukemia.";
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-129.
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, Mammary gland, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[16]
FUNCTION.
PubMed=9859993; DOI=10.1038/25141;
Li F., Ambrosini G., Chu E.Y., Plescia J., Tognin S., Marchisio P.C.,
Altieri D.C.;
"Control of apoptosis and mitotic spindle checkpoint by survivin.";
Nature 396:580-584(1998).
[17]
PHOSPHORYLATION AT THR-34.
PubMed=11069302; DOI=10.1073/pnas.240390697;
O'Connor D.S., Grossman D., Plescia J., Li F., Zhang H., Villa A.,
Tognin S., Marchisio P.C., Altieri D.C.;
"Regulation of apoptosis at cell division by p34cdc2 phosphorylation
of survivin.";
Proc. Natl. Acad. Sci. U.S.A. 97:13103-13107(2000).
[18]
FUNCTION IN APOPTOSIS SUPPRESSION, INTERACTION WITH LAMTOR5/HBXIP,
MUTAGENESIS OF THR-34, AND SUBCELLULAR LOCATION.
PubMed=12773388; DOI=10.1093/emboj/cdg263;
Marusawa H., Matsuzawa S., Welsh K., Zou H., Armstrong R., Tamm I.,
Reed J.C.;
"HBXIP functions as a cofactor of survivin in apoptosis suppression.";
EMBO J. 22:2729-2740(2003).
[19]
INTERACTION WITH INCENP, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
THR-117, AND MUTAGENESIS OF THR-117.
PubMed=14610074; DOI=10.1074/jbc.M311299200;
Wheatley S.P., Henzing A.J., Dodson H., Khaled W., Earnshaw W.C.;
"Aurora-B phosphorylation in vitro identifies a residue of survivin
that is essential for its localization and binding to inner centromere
protein (INCENP) in vivo.";
J. Biol. Chem. 279:5655-5660(2004).
[20]
INTERACTION WITH CDCA8.
PubMed=15249581; DOI=10.1083/jcb.200404001;
Gassmann R., Carvalho A., Henzing A.J., Ruchaud S., Hudson D.F.,
Honda R., Nigg E.A., Gerloff D.L., Earnshaw W.C.;
"Borealin: a novel chromosomal passenger required for stability of the
bipolar mitotic spindle.";
J. Cell Biol. 166:179-191(2004).
[21]
SUBCELLULAR LOCATION, AND INTERACTION WITH BIRC2/C-IAP1.
PubMed=15665297;
Samuel T., Okada K., Hyer M., Welsh K., Zapata J.M., Reed J.C.;
"cIAP1 Localizes to the nuclear compartment and modulates the cell
cycle.";
Cancer Res. 65:210-218(2005).
[22]
REVIEW ON FUNCTION.
PubMed=16344111; DOI=10.1016/S0074-7696(05)47002-3;
Wheatley S.P., McNeish I.A.;
"Survivin: a protein with dual roles in mitosis and apoptosis.";
Int. Rev. Cytol. 247:35-88(2005).
[23]
FUNCTION, INTERACTION WITH USP9X, SUBCELLULAR LOCATION,
UBIQUITINATION, AND MUTAGENESIS OF LYS-23; LYS-62; LYS-78 AND LYS-79.
PubMed=16322459; DOI=10.1126/science.1120160;
Vong Q.P., Cao K., Li H.Y., Iglesias P.A., Zheng Y.;
"Chromosome alignment and segregation regulated by ubiquitination of
survivin.";
Science 310:1499-1504(2005).
[24]
MUTAGENESIS OF ASP-70; ASP-71 AND 70-ASP--ASP-71.
PubMed=16762323; DOI=10.1016/j.bbrc.2006.05.131;
Cao L., Yan X., Wu Y., Hu H., Li Q., Zhou T., Jiang S., Yu L.;
"Survivin mutant (Surv-DD70, 71AA) disrupts the interaction of
Survivin with Aurora B and causes multinucleation in HeLa cells.";
Biochem. Biophys. Res. Commun. 346:400-407(2006).
[25]
INTERACTION WITH CDCA8.
PubMed=16239925; DOI=10.1038/sj.embor.7400562;
Vader G., Kauw J.J.W., Medema R.H., Lens S.M.A.;
"Survivin mediates targeting of the chromosomal passenger complex to
the centromere and midbody.";
EMBO Rep. 7:85-92(2006).
[26]
INTERACTION WITH CDCA8.
PubMed=16427043; DOI=10.1016/j.yexcr.2005.12.015;
Chang J.-L., Chen T.-H., Wang C.-F., Chiang Y.-H., Huang Y.-L.,
Wong F.-H., Chou C.-K., Chen C.-M.;
"Borealin/Dasra B is a cell cycle-regulated chromosomal passenger
protein and its nuclear accumulation is linked to poor prognosis for
human gastric cancer.";
Exp. Cell Res. 312:962-973(2006).
[27]
INTERACTION WITH EVI5.
PubMed=16764853; DOI=10.1016/j.yexcr.2006.03.032;
Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.;
"EVI5 protein associates with the INCENP-aurora B kinase-survivin
chromosomal passenger complex and is involved in the completion of
cytokinesis.";
Exp. Cell Res. 312:2325-2335(2006).
[28]
FUNCTION, AND INTERACTION WITH CDCA8.
PubMed=16291752; DOI=10.1074/jbc.M508773200;
Noton E.A., Colnaghi R., Tate S., Starck C., Carvalho A.,
Ko Ferrigno P., Wheatley S.P.;
"Molecular analysis of survivin isoforms: evidence that alternatively
spliced variants do not play a role in mitosis.";
J. Biol. Chem. 281:1286-1295(2006).
[29]
INTERACTION WITH CDCA8.
PubMed=16436504; DOI=10.1091/mbc.E05-08-0727;
Lens S.M.A., Rodriguez J.A., Vader G., Span S.W., Giaccone G.,
Medema R.H.;
"Uncoupling the central spindle-associated function of the chromosomal
passenger complex from its role at centromeres.";
Mol. Biol. Cell 17:1897-1909(2006).
[30]
INTERACTION WITH BIRC6/BRUCE.
PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
Pohl C., Jentsch S.;
"Final stages of cytokinesis and midbody ring formation are controlled
by BRUCE.";
Cell 132:832-845(2008).
[31]
INDUCTION.
PubMed=17993464; DOI=10.1074/jbc.M704035200;
Gagarina V., Carlberg A.L., Pereira-Mouries L., Hall D.J.;
"Cartilage oligomeric matrix protein protects cells against death by
elevating members of the IAP family of survival proteins.";
J. Biol. Chem. 283:648-659(2008).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[33]
FUNCTION, INTERACTION WITH RAN; AURKB AND CDCA8, SUBCELLULAR LOCATION,
DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLU-65.
PubMed=18591255; DOI=10.1128/MCB.02039-07;
Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.;
"A survivin-ran complex regulates spindle formation in tumor cells.";
Mol. Cell. Biol. 28:5299-5311(2008).
[34]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=21364656; DOI=10.1038/cddis.2010.25;
Knauer S.K., Heinrich U.R., Bier C., Habtemichael N., Docter D.,
Helling K., Mann W.J., Stauber R.H.;
"An otoprotective role for the apoptosis inhibitor protein survivin.";
Cell Death Dis. 1:E51-E51(2010).
[35]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAT3 AND XPO1/CRM1,
ACETYLATION AT LYS-23; LYS-90; LYS-110; LYS-112; LYS-115; LYS-121 AND
LYS-129, MUTAGENESIS OF LYS-129, AND CHARACTERIZATION OF VARIANT
GLU-129.
PubMed=20826784; DOI=10.1074/jbc.M110.152777;
Wang H., Holloway M.P., Ma L., Cooper Z.A., Riolo M., Samkari A.,
Elenitoba-Johnson K.S., Chin Y.E., Altura R.A.;
"Acetylation directs survivin nuclear localization to repress STAT3
oncogenic activity.";
J. Biol. Chem. 285:36129-36137(2010).
[36]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=20627126; DOI=10.1016/j.mcn.2010.07.003;
Habtemichael N., Heinrich U.R., Knauer S.K., Schmidtmann I., Bier C.,
Docter D., Brochhausen C., Helling K., Brieger J., Stauber R.H.,
Mann W.J.;
"Expression analysis suggests a potential cytoprotective role of Birc5
in the inner ear.";
Mol. Cell. Neurosci. 45:297-305(2010).
[37]
FUNCTION, HISTONE-BINDING, AND MUTAGENESIS OF ARG-18; TRP-25; CYS-33;
CYS-57 AND TRP-67.
PubMed=20929775; DOI=10.1126/science.1194498;
Yamagishi Y., Honda T., Tanno Y., Watanabe Y.;
"Two histone marks establish the inner centromere and chromosome bi-
orientation.";
Science 330:239-243(2010).
[38]
PHOSPHORYLATION AT THR-48, AND MUTAGENESIS OF THR-48.
PubMed=21252625; DOI=10.4161/cc.10.3.14758;
Barrett R.M., Colnaghi R., Wheatley S.P.;
"Threonine 48 in the BIR domain of survivin is critical to its mitotic
and anti-apoptotic activities and can be phosphorylated by CK2 in
vitro.";
Cell Cycle 10:538-548(2011).
[39]
INTERACTION WITH JTB.
PubMed=21225229; DOI=10.3892/ijo.2011.900;
Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.;
"PAR, a protein involved in the cell cycle, is functionally related to
chromosomal passenger proteins.";
Int. J. Oncol. 38:777-785(2011).
[40]
FUNCTION, SUBUNIT, AND INTERACTION WITH XIAP/BIRC4 AND DIABLO/SMAC.
PubMed=21536684; DOI=10.1074/jbc.M111.237586;
Pavlyukov M.S., Antipova N.V., Balashova M.V., Vinogradova T.V.,
Kopantzev E.P., Shakhparonov M.I.;
"Survivin monomer plays an essential role in apoptosis regulation.";
J. Biol. Chem. 286:23296-23307(2011).
[41]
PHOSPHORYLATION AT THR-34 BY CDK15.
PubMed=24866247; DOI=10.1016/j.bbrc.2014.05.070;
Park M.H., Kim S.Y., Kim Y.J., Chung Y.H.;
"ALS2CR7 (CDK15) attenuates TRAIL induced apoptosis by inducing
phosphorylation of survivin Thr34.";
Biochem. Biophys. Res. Commun. 450:129-134(2014).
[42]
UBIQUITINATION.
PubMed=24793696; DOI=10.1016/j.molcel.2014.03.046;
Li Z., Pei X.H., Yan J., Yan F., Cappell K.M., Whitehurst A.W.,
Xiong Y.;
"CUL9 mediates the functions of the 3M complex and ubiquitylates
survivin to maintain genome integrity.";
Mol. Cell 54:805-819(2014).
[43]
SUBUNIT, AND PHOSPHORYLATION AT SER-20.
PubMed=27332895; DOI=10.1371/journal.pone.0157305;
Sasai K., Katayama H., Hawke D.H., Sen S.;
"Aurora-C interactions with survivin and INCENP reveal shared and
distinct features compared with Aurora-B chromosome passenger protein
complex.";
PLoS ONE 11:E0157305-E0157305(2016).
[44]
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF ISOFORM 1.
PubMed=10949039; DOI=10.1016/S1097-2765(05)00020-1;
Chantalat L., Skoufias D.A., Kleman J.P., Jung B., Dideberg O.,
Margolis R.L.;
"Crystal structure of human survivin reveals a bow tie-shaped dimer
with two unusual alpha-helical extensions.";
Mol. Cell 6:183-189(2000).
[45]
X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF ISOFORM 1.
PubMed=10876248; DOI=10.1038/76838;
Verdecia M.A., Huang H., Dutil E., Kaiser D.A., Hunter T., Noel J.P.;
"Structure of the human anti-apoptotic protein survivin reveals a
dimeric arrangement.";
Nat. Struct. Biol. 7:602-608(2000).
[46]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC IONS,
SUBUNIT, AND INTERACTION WITH CDCA8 AND INCENP.
PubMed=17956729; DOI=10.1016/j.cell.2007.07.045;
Jeyaprakash A.A., Klein U.R., Lindner D., Ebert J., Nigg E.A.,
Conti E.;
"Structure of a Survivin-Borealin-INCENP core complex reveals how
chromosomal passengers travel together.";
Cell 131:271-285(2007).
[47]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=19530738; DOI=10.1021/bi900530v;
Bourhis E., Lingel A., Phung Q., Fairbrother W.J., Cochran A.G.;
"Phosphorylation of a borealin dimerization domain is required for
proper chromosome segregation.";
Biochemistry 48:6783-6793(2009).
-!- FUNCTION: Multitasking protein that has dual roles in promoting
cell proliferation and preventing apoptosis (PubMed:9859993,
PubMed:21364656, PubMed:20627126). Component of a chromosome
passage protein complex (CPC) which is essential for chromosome
alignment and segregation during mitosis and cytokinesis
(PubMed:16322459). Acts as an important regulator of the
localization of this complex; directs CPC movement to different
locations from the inner centromere during prometaphase to midbody
during cytokinesis and participates in the organization of the
center spindle by associating with polymerized microtubules
(PubMed:20826784). Involved in the recruitment of CPC to
centromeres during early mitosis via association with histone H3
phosphorylated at 'Thr-3' (H3pT3) during mitosis
(PubMed:20929775). The complex with RAN plays a role in mitotic
spindle formation by serving as a physical scaffold to help
deliver the RAN effector molecule TPX2 to microtubules
(PubMed:18591255). May counteract a default induction of apoptosis
in G2/M phase (PubMed:9859993). The acetylated form represses
STAT3 transactivation of target gene promoters (PubMed:20826784).
May play a role in neoplasia (PubMed:10626797). Inhibitor of CASP3
and CASP7 (PubMed:21536684). Isoform 2 and isoform 3 do not appear
to play vital roles in mitosis (PubMed:12773388, PubMed:16291752).
Isoform 3 shows a marked reduction in its anti-apoptotic effects
when compared with the displayed wild-type isoform
(PubMed:10626797). {ECO:0000269|PubMed:10626797,
ECO:0000269|PubMed:12773388, ECO:0000269|PubMed:16291752,
ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:18591255,
ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20826784,
ECO:0000269|PubMed:20929775, ECO:0000269|PubMed:21364656,
ECO:0000269|PubMed:21536684, ECO:0000269|PubMed:9859993}.
-!- SUBUNIT: Monomer or homodimer. Exists as a homodimer in the apo
state and as a monomer in the CPC-bound state. The monomer
protects cells against apoptosis more efficiently than the dimer.
Only the dimeric form is capable of enhancing tubulin stability in
cells. When phosphorylated, interacts with LAMTOR5/HBXIP; the
resulting complex binds pro-CASP9, as well as active CASP9, but
much less efficiently. Component of the chromosomal passenger
complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin,
INCENP, AURKB or AURKC; in the complex forms a triple-helix
bundle-based subcomplex with INCENP and CDCA8 (PubMed:17956729).
Interacts with JTB. Interacts (via BIR domain) with histone H3
phosphorylated at 'Thr-3' (H3pT3). Interacts with EVI5. Interacts
with GTP-bound RAN in both the S and M phases of the cell cycle.
Interacts with USP9X. Interacts with tubulin. Interacts with
BIRC2/c-IAP1. The acetylated form at Lys-129 interacts with STAT3.
The monomeric form deacetylated at Lys-129 interacts with
XPO1/CRM1. The monomeric form interacts with XIAP/BIRC4. Both the
dimeric and monomeric form can interact with DIABLO/SMAC.
Interacts with BIRC6/bruce. {ECO:0000269|PubMed:12773388,
ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:15249581,
ECO:0000269|PubMed:15665297, ECO:0000269|PubMed:16239925,
ECO:0000269|PubMed:16291752, ECO:0000269|PubMed:16322459,
ECO:0000269|PubMed:16427043, ECO:0000269|PubMed:16436504,
ECO:0000269|PubMed:16764853, ECO:0000269|PubMed:17956729,
ECO:0000269|PubMed:18329369, ECO:0000269|PubMed:18591255,
ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:21225229,
ECO:0000269|PubMed:21536684}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-518823, EBI-518823;
Q96GD4:AURKB; NbExp=10; IntAct=EBI-518823, EBI-624291;
Q9UQB9:AURKC; NbExp=10; IntAct=EBI-518823, EBI-3926851;
Q14457:BECN1; NbExp=3; IntAct=EBI-518823, EBI-949378;
P55211:CASP9; NbExp=2; IntAct=EBI-518823, EBI-516799;
Q53HL2:CDCA8; NbExp=14; IntAct=EBI-518823, EBI-979174;
P06493:CDK1; NbExp=6; IntAct=EBI-518823, EBI-444308;
Q9NR28:DIABLO; NbExp=2; IntAct=EBI-518823, EBI-517508;
Q86XJ1:GAS2L3; NbExp=4; IntAct=EBI-518823, EBI-9248152;
Q9NQS7:INCENP; NbExp=10; IntAct=EBI-518823, EBI-307907;
P62826:RAN; NbExp=7; IntAct=EBI-518823, EBI-286642;
O14980:XPO1; NbExp=2; IntAct=EBI-518823, EBI-355867;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20627126,
ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:21364656}. Nucleus
{ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20826784,
ECO:0000269|PubMed:21364656}. Chromosome
{ECO:0000269|PubMed:14610074}. Chromosome, centromere
{ECO:0000269|PubMed:11084331, ECO:0000269|PubMed:14610074,
ECO:0000269|PubMed:16322459}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:11084331}. Chromosome, centromere, kinetochore
{ECO:0000269|PubMed:11084331}. Midbody
{ECO:0000269|PubMed:15665297}. Note=Localizes at the centromeres
from prophase to metaphase, at the spindle midzone during anaphase
and a the midbody during telophase and cytokinesis. Accumulates in
the nucleus upon treatment with leptomycin B (LMB), a XPO1/CRM1
nuclear export inhibitor (By similarity). Localizes on chromosome
arms and inner centromeres from prophase through metaphase.
Localizes to kinetochores in metaphase, distributes to the midzone
microtubules in anaphase and at telophase, localizes exclusively
to the midbody (PubMed:11084331). Colocalizes with AURKB at
mitotic chromosomes (PubMed:14610074). Acetylation at Lys-129
directs its localization to the nucleus by enhancing
homodimerization and thereby inhibiting XPO1/CRM1-mediated nuclear
export (PubMed:20826784). {ECO:0000250|UniProtKB:E3SCZ8,
ECO:0000269|PubMed:11084331, ECO:0000269|PubMed:14610074,
ECO:0000269|PubMed:20826784}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=Alpha;
IsoId=O15392-1; Sequence=Displayed;
Name=2; Synonyms=2B, Beta;
IsoId=O15392-2; Sequence=VSP_002454;
Name=3; Synonyms=DeltaEx3;
IsoId=O15392-3; Sequence=VSP_020338;
Name=4; Synonyms=3B;
IsoId=O15392-4; Sequence=VSP_020342;
Name=5; Synonyms=SI;
IsoId=O15392-5; Sequence=VSP_020341;
Name=6; Synonyms=3 alpha;
IsoId=O15392-6; Sequence=VSP_020339;
Name=7; Synonyms=2 alpha;
IsoId=O15392-7; Sequence=VSP_020340;
-!- TISSUE SPECIFICITY: Expressed only in fetal kidney and liver, and
to lesser extent, lung and brain (PubMed:10626797). Abundantly
expressed in adenocarcinoma (lung, pancreas, colon, breast, and
prostate) and in high-grade lymphomas (PubMed:14741722,
PubMed:16329164). Also expressed in various renal cell carcinoma
cell lines (PubMed:10626797). Expressed in cochlea including the
organ of Corti, the lateral wall, the interdental cells of the
Limbus as well as in Schwann cells and cells of the cochlear nerve
and the spiral ganglions (at protein level). Not expressed in
cells of the inner and outer sulcus or the Reissner's membrane (at
protein level) (PubMed:21364656, PubMed:20627126).
{ECO:0000269|PubMed:10626797, ECO:0000269|PubMed:14741722,
ECO:0000269|PubMed:16329164, ECO:0000269|PubMed:20627126,
ECO:0000269|PubMed:21364656}.
-!- DEVELOPMENTAL STAGE: Expression is cell cycle-dependent and peaks
at mitosis. {ECO:0000269|PubMed:18591255}.
-!- INDUCTION: Up-regulated by COMP. {ECO:0000269|PubMed:17993464}.
-!- DOMAIN: The BIR repeat is necessary and sufficient for LAMTOR5
binding. {ECO:0000269|PubMed:12773388}.
-!- PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase
complex, leading to its degradation. Ubiquitination is required
for centrosomal targeting. {ECO:0000269|PubMed:16322459,
ECO:0000269|PubMed:24793696}.
-!- PTM: In vitro phosphorylation at Thr-117 by AURKB prevents
interaction with INCENP and localization to mitotic chromosomes
(PubMed:14610074). Phosphorylation at Thr-48 by CK2 is critical
for its mitotic and anti-apoptotic activities (PubMed:21252625).
Phosphorylation at Thr-34 by CDK15 is critical for its anti-
apoptotic activity (PubMed:24866247). Phosphorylation at Ser-20 by
AURKC is critical for regulation of proper chromosome alignment
and segregation, and possibly cytokinesis.
{ECO:0000269|PubMed:11069302, ECO:0000269|PubMed:14610074,
ECO:0000269|PubMed:21252625, ECO:0000269|PubMed:24866247,
ECO:0000269|PubMed:27332895}.
-!- PTM: Acetylation at Lys-129 by CBP results in its
homodimerization, while deacetylation promotes the formation of
monomers which heterodimerize with XPO1/CRM1 which facilitates its
nuclear export. The acetylated form represses STAT3
transactivation. The dynamic equilibrium between its acetylation
and deacetylation at Lys-129 determines its interaction with
XPO1/CRM1, its subsequent subcellular localization, and its
ability to inhibit STAT3 transactivation.
{ECO:0000269|PubMed:20826784}.
-!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/birc5/";
-----------------------------------------------------------------------
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EMBL; U75285; AAC51660.1; -; Genomic_DNA.
EMBL; AF077350; AAD34226.1; -; mRNA.
EMBL; AB154416; BAD11155.1; -; mRNA.
EMBL; AY830084; AAW22624.1; -; mRNA.
EMBL; AB028869; BAA93676.1; -; mRNA.
EMBL; AY927772; AAY15202.1; -; mRNA.
EMBL; DQ227257; ABB76601.1; -; mRNA.
EMBL; DQ310375; ABC42341.1; -; mRNA.
EMBL; DQ310376; ABC42342.1; -; mRNA.
EMBL; DQ310377; ABC42343.1; -; mRNA.
EMBL; DQ310378; ABC42344.1; -; mRNA.
EMBL; DQ310379; ABC42345.1; -; mRNA.
EMBL; CR541740; CAG46540.1; -; mRNA.
EMBL; AK223428; BAD97148.1; -; mRNA.
EMBL; AK311917; BAG34858.1; -; mRNA.
EMBL; AY795969; AAV40840.1; -; Genomic_DNA.
EMBL; AC087645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471099; EAW89514.1; -; Genomic_DNA.
EMBL; BC008718; AAH08718.1; -; mRNA.
EMBL; BC034148; AAH34148.1; -; mRNA.
EMBL; BC065497; AAH65497.1; -; mRNA.
CCDS; CCDS11755.1; -. [O15392-1]
CCDS; CCDS32751.1; -. [O15392-3]
CCDS; CCDS32752.1; -. [O15392-2]
RefSeq; NP_001012270.1; NM_001012270.1. [O15392-3]
RefSeq; NP_001012271.1; NM_001012271.1.
RefSeq; NP_001159.2; NM_001168.2.
UniGene; Hs.744872; -.
PDB; 1E31; X-ray; 2.71 A; A/B=1-142.
PDB; 1F3H; X-ray; 2.58 A; A/B=1-142.
PDB; 1XOX; NMR; -; A/B=1-117.
PDB; 2QFA; X-ray; 1.40 A; A=1-142.
PDB; 2RAW; X-ray; 2.40 A; A=1-142.
PDB; 2RAX; X-ray; 3.30 A; A/E/X=1-120.
PDB; 3UEC; X-ray; 2.18 A; A=1-142.
PDB; 3UED; X-ray; 2.70 A; A/C=1-142.
PDB; 3UEE; X-ray; 2.61 A; A/C=1-142.
PDB; 3UEF; X-ray; 2.45 A; A/C=1-142.
PDB; 3UEG; X-ray; 2.80 A; A/B=1-142.
PDB; 3UEH; X-ray; 2.60 A; A/B=1-142.
PDB; 3UEI; X-ray; 2.70 A; A/B=1-142.
PDB; 3UIG; X-ray; 2.40 A; A/B=1-142.
PDB; 3UIH; X-ray; 2.40 A; A/B=1-142.
PDB; 3UII; X-ray; 2.60 A; A/B=1-142.
PDB; 3UIJ; X-ray; 2.70 A; A/B=1-142.
PDB; 3UIK; X-ray; 2.70 A; A/B=1-142.
PDB; 4A0I; X-ray; 2.60 A; A/B=1-142.
PDB; 4A0J; X-ray; 2.80 A; A/B=1-142.
PDB; 4A0N; X-ray; 2.74 A; A=1-142.
PDBsum; 1E31; -.
PDBsum; 1F3H; -.
PDBsum; 1XOX; -.
PDBsum; 2QFA; -.
PDBsum; 2RAW; -.
PDBsum; 2RAX; -.
PDBsum; 3UEC; -.
PDBsum; 3UED; -.
PDBsum; 3UEE; -.
PDBsum; 3UEF; -.
PDBsum; 3UEG; -.
PDBsum; 3UEH; -.
PDBsum; 3UEI; -.
PDBsum; 3UIG; -.
PDBsum; 3UIH; -.
PDBsum; 3UII; -.
PDBsum; 3UIJ; -.
PDBsum; 3UIK; -.
PDBsum; 4A0I; -.
PDBsum; 4A0J; -.
PDBsum; 4A0N; -.
ProteinModelPortal; O15392; -.
SMR; O15392; -.
BioGrid; 106829; 59.
CORUM; O15392; -.
DIP; DIP-34662N; -.
ELM; O15392; -.
IntAct; O15392; 18.
MINT; MINT-147138; -.
BindingDB; O15392; -.
ChEMBL; CHEMBL5989; -.
DrugBank; DB05141; LY2181308.
GuidetoPHARMACOLOGY; 2795; -.
MEROPS; I32.005; -.
iPTMnet; O15392; -.
PhosphoSitePlus; O15392; -.
BioMuta; BIRC5; -.
EPD; O15392; -.
MaxQB; O15392; -.
PeptideAtlas; O15392; -.
PRIDE; O15392; -.
DNASU; 332; -.
Ensembl; ENST00000374948; ENSP00000364086; ENSG00000089685. [O15392-3]
Ensembl; ENST00000590449; ENSP00000465868; ENSG00000089685. [O15392-7]
Ensembl; ENST00000590925; ENSP00000467336; ENSG00000089685. [O15392-4]
Ensembl; ENST00000592734; ENSP00000466617; ENSG00000089685. [O15392-6]
GeneID; 332; -.
KEGG; hsa:332; -.
UCSC; uc002jvh.4; human. [O15392-1]
CTD; 332; -.
DisGeNET; 332; -.
EuPathDB; HostDB:ENSG00000089685.14; -.
GeneCards; BIRC5; -.
HGNC; HGNC:593; BIRC5.
HPA; CAB004270; -.
HPA; HPA002830; -.
MIM; 603352; gene.
neXtProt; NX_O15392; -.
OpenTargets; ENSG00000089685; -.
PharmGKB; PA25362; -.
GeneTree; ENSGT00510000047537; -.
HOGENOM; HOG000172188; -.
HOVERGEN; HBG050690; -.
InParanoid; O15392; -.
KO; K08731; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-8951664; Neddylation.
SignaLink; O15392; -.
SIGNOR; O15392; -.
ChiTaRS; BIRC5; human.
EvolutionaryTrace; O15392; -.
GeneWiki; Survivin; -.
GenomeRNAi; 332; -.
PRO; PR:O15392; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000089685; -.
CleanEx; HS_BIRC5; -.
ExpressionAtlas; O15392; baseline and differential.
Genevisible; O15392; HS.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0032133; C:chromosome passenger complex; IPI:UniProtKB.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031021; C:interphase microtubule organizing center; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
GO; GO:0050897; F:cobalt ion binding; NAS:UniProtKB.
GO; GO:0048037; F:cofactor binding; IDA:UniProtKB.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0008536; F:Ran GTPase binding; IPI:UniProtKB.
GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IMP:UniProtKB.
GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
GO; GO:0051303; P:establishment of chromosome localization; IMP:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0000278; P:mitotic cell cycle; TAS:UniProtKB.
GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0031503; P:protein complex localization; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
GO; GO:0007605; P:sensory perception of sound; IEP:UniProtKB.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0031577; P:spindle checkpoint; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00022; BIR; 1.
InterPro; IPR001370; BIR_rpt.
Pfam; PF00653; BIR; 1.
SMART; SM00238; BIR; 1.
PROSITE; PS50143; BIR_REPEAT_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Cell cycle; Cell division; Centromere; Chromosome;
Chromosome partition; Complete proteome; Cytoplasm; Cytoskeleton;
Kinetochore; Metal-binding; Microtubule; Mitosis; Nucleus;
Phosphoprotein; Polymorphism; Protease inhibitor; Reference proteome;
Repressor; Thiol protease inhibitor; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 142 Baculoviral IAP repeat-containing protein
5.
/FTId=PRO_0000122356.
REPEAT 18 88 BIR.
METAL 57 57 Zinc. {ECO:0000244|PDB:2QFA,
ECO:0000269|PubMed:17956729}.
METAL 60 60 Zinc. {ECO:0000244|PDB:2QFA,
ECO:0000269|PubMed:17956729}.
METAL 77 77 Zinc. {ECO:0000244|PDB:2QFA,
ECO:0000269|PubMed:17956729}.
METAL 84 84 Zinc. {ECO:0000244|PDB:2QFA,
ECO:0000269|PubMed:17956729}.
MOD_RES 20 20 Phosphoserine; by AURKC.
{ECO:0000269|PubMed:27332895}.
MOD_RES 23 23 N6-acetyllysine.
{ECO:0000269|PubMed:20826784}.
MOD_RES 34 34 Phosphothreonine; by CDK1 and CDK15.
{ECO:0000244|PubMed:18691976,
ECO:0000269|PubMed:11069302,
ECO:0000269|PubMed:24866247}.
MOD_RES 48 48 Phosphothreonine; by CK2; in vitro.
{ECO:0000269|PubMed:21252625}.
MOD_RES 90 90 N6-acetyllysine.
{ECO:0000269|PubMed:20826784}.
MOD_RES 110 110 N6-acetyllysine.
{ECO:0000269|PubMed:20826784}.
MOD_RES 112 112 N6-acetyllysine.
{ECO:0000269|PubMed:20826784}.
MOD_RES 115 115 N6-acetyllysine.
{ECO:0000269|PubMed:20826784}.
MOD_RES 117 117 Phosphothreonine; by AURKB.
{ECO:0000269|PubMed:14610074}.
MOD_RES 121 121 N6-acetyllysine.
{ECO:0000269|PubMed:20826784}.
MOD_RES 129 129 N6-acetyllysine.
{ECO:0000269|PubMed:20826784}.
VAR_SEQ 74 142 IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIA
KETNNKKKEFEETAKKVRRAIEQLAAMD -> MQRKPTIRR
KNLRKLRRKCAVPSSSWLPWIEASGRSCLVPEWLHHFQGLF
PGATSLPVGPLAMS (in isoform 3).
{ECO:0000303|PubMed:10626797}.
/FTId=VSP_020338.
VAR_SEQ 74 142 IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIA
KETNNKKKEFEETAKKVRRAIEQLAAMD -> MRELC (in
isoform 6). {ECO:0000303|Ref.8}.
/FTId=VSP_020339.
VAR_SEQ 74 142 IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIA
KETNNKKKEFEETAKKVRRAIEQLAAMD -> M (in
isoform 7). {ECO:0000303|Ref.7}.
/FTId=VSP_020340.
VAR_SEQ 74 74 I -> IGPGTVAYACNTSTLGGRGGRITR (in isoform
2). {ECO:0000303|PubMed:10626797,
ECO:0000303|Ref.6}.
/FTId=VSP_002454.
VAR_SEQ 105 142 DRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD ->
VRETLPPPRSFIR (in isoform 5).
{ECO:0000303|PubMed:16329164}.
/FTId=VSP_020341.
VAR_SEQ 114 142 AKETNNKKKEFEETAKKVRRAIEQLAAMD -> ERALLAE
(in isoform 4).
{ECO:0000303|PubMed:14741722}.
/FTId=VSP_020342.
VARIANT 129 129 K -> E (loss of acetylation; localization
primarily within the cytoplasm; increased
likelihood of existing as monomer;
stronger binding to XPO1/CRM1;
dbSNP:rs2071214).
{ECO:0000269|PubMed:16625196,
ECO:0000269|PubMed:20826784}.
/FTId=VAR_021071.
MUTAGEN 18 18 R->A: Disrupts interaction with histone
H3pT3, no effect on interaction with
INCENP. {ECO:0000269|PubMed:20929775}.
MUTAGEN 23 23 K->R: Increases ubiquitination and blocks
dissociation from centromeres; when
associated with R-62; R-78 and R-79.
{ECO:0000269|PubMed:16322459}.
MUTAGEN 25 25 W->A: Disrupts interaction with histone
H3pT3, no effect on interaction with
INCENP. {ECO:0000269|PubMed:20929775}.
MUTAGEN 33 33 C->R: Disrupts interaction with histone
H3pT3, no effect on interaction with
INCENP. {ECO:0000269|PubMed:20929775}.
MUTAGEN 34 34 T->A: Loss of LAMTOR5 binding.
{ECO:0000269|PubMed:12773388}.
MUTAGEN 34 34 T->E: Higher affinity for LAMTOR5
binding. {ECO:0000269|PubMed:12773388}.
MUTAGEN 48 48 T->A,E: Localizes normally during mitosis
but cannot support cell proliferation.
Increased affinity for CDCA8/borealin.
{ECO:0000269|PubMed:21252625}.
MUTAGEN 57 57 C->A: Disrupts interaction with histone
H3pT3, no effect on interaction with
INCENP. {ECO:0000269|PubMed:20929775}.
MUTAGEN 62 62 K->R: Increases ubiquitination and blocks
dissociation from centromeres; when
associated with R-23; R-78 and R-79.
{ECO:0000269|PubMed:16322459}.
MUTAGEN 65 65 E->A: Almost abolishes RAN-binding. Does
not disrupt binding to AURKB or CDCA8.
Disrupts mitotic spindle assembly. Does
not disrupt nuclear export.
{ECO:0000269|PubMed:18591255}.
MUTAGEN 67 67 W->A: Disrupts interaction with histone
H3pT3, no effect on interaction with
INCENP. {ECO:0000269|PubMed:20929775}.
MUTAGEN 70 70 D->A: No change. Loss of interaction with
AURKB; when associated with A-71.
{ECO:0000269|PubMed:16762323}.
MUTAGEN 71 71 D->A: No change. Loss of interaction with
AURKB; when associated with A-70.
{ECO:0000269|PubMed:16762323}.
MUTAGEN 78 78 K->R: Increases ubiquitination and blocks
dissociation from centromeres; when
associated with R-23; R-62 and R-79.
{ECO:0000269|PubMed:16322459}.
MUTAGEN 79 79 K->R: Increases ubiquitination and blocks
dissociation from centromeres; when
associated with R-23; R-62 and R-78.
{ECO:0000269|PubMed:16322459}.
MUTAGEN 84 84 C->A: Loss of cytoprotection.
MUTAGEN 117 117 T->A: Prevents phosphorylation by AURKB.
Still able to localize correctly but
prevents interaction with INCENP.
{ECO:0000269|PubMed:14610074}.
MUTAGEN 117 117 T->E: Mimics phosphorylation. Disrupts
subcellular localization during mitosis
and prevents interaction with INCENP.
{ECO:0000269|PubMed:14610074}.
MUTAGEN 129 129 K->A,Q: Mimics acetylation. Localization
primarily within the nucleus.
{ECO:0000269|PubMed:20826784}.
MUTAGEN 129 129 K->R: Loss of acetylation. Localization
primarily within the cytoplasm.
{ECO:0000269|PubMed:20826784}.
CONFLICT 57 58 CF -> WV (in Ref. 5; AAW22624).
{ECO:0000305}.
CONFLICT 58 58 F -> L (in Ref. 11; BAD97148).
{ECO:0000305}.
CONFLICT 128 128 A -> V (in Ref. 9; CAG46540).
{ECO:0000305}.
TURN 8 10 {ECO:0000244|PDB:2QFA}.
HELIX 11 13 {ECO:0000244|PDB:2QFA}.
HELIX 15 20 {ECO:0000244|PDB:2QFA}.
STRAND 31 33 {ECO:0000244|PDB:3UEC}.
HELIX 35 40 {ECO:0000244|PDB:2QFA}.
STRAND 43 45 {ECO:0000244|PDB:2QFA}.
STRAND 49 51 {ECO:0000244|PDB:3UIG}.
STRAND 55 57 {ECO:0000244|PDB:2QFA}.
TURN 58 60 {ECO:0000244|PDB:2QFA}.
STRAND 63 65 {ECO:0000244|PDB:3UEC}.
HELIX 73 80 {ECO:0000244|PDB:2QFA}.
TURN 81 83 {ECO:0000244|PDB:1F3H}.
HELIX 85 88 {ECO:0000244|PDB:2QFA}.
HELIX 93 95 {ECO:0000244|PDB:2QFA}.
HELIX 98 139 {ECO:0000244|PDB:2QFA}.
SEQUENCE 142 AA; 16389 MW; 9E7CADCDF2822286 CRC64;
MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN EPDLAQCFFC
FKELEGWEPD DDPIEEHKKH SSGCAFLSVK KQFEELTLGE FLKLDRERAK NKIAKETNNK
KKEFEETAKK VRRAIEQLAA MD


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