GENTAUR Molecular Products.

 INCE_HUMAN              Reviewed;         918 AA.
 Q9NQS7; A8MQD2; Q5Y192;
 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
 04-NOV-2008, sequence version 3.
 12-SEP-2018, entry version 160.
 RecName: Full=Inner centromere protein;
 Name=INCENP;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
 VARIANT ASP-644.
 TISSUE=Cervix carcinoma;
 PubMed=11453556; DOI=10.1007/s004120100130;
 Adams R.R., Eckley D.M., Vagnarelli P., Wheatley S.P., Gerloff D.L.,
 Mackay A.M., Svingen P.A., Kaufmann S.H., Earnshaw W.C.;
 "Human INCENP colocalizes with the Aurora-B/AIRK2 kinase on
 chromosomes and is overexpressed in tumour cells.";
 Chromosoma 110:65-74(2001).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
 AURKB AND AURKC, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-195, AND
 VARIANT ASP-644.
 TISSUE=Testis;
 PubMed=15316025; DOI=10.1074/jbc.M403029200;
 Li X., Sakashita G., Matsuzaki H., Sugimoto K., Kimura K., Hanaoka F.,
 Taniguchi H., Furukawa K., Urano T.;
 "Direct association with inner centromere protein (INCENP) activates
 the novel chromosomal passenger protein, Aurora-C.";
 J. Biol. Chem. 279:47201-47211(2004).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=16554811; DOI=10.1038/nature04632;
 Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
 Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
 Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
 FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
 Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
 Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
 Sakaki Y.;
 "Human chromosome 11 DNA sequence and analysis including novel gene
 identification.";
 Nature 440:497-500(2006).
 [4]
 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.
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
 ASP-644.
 TISSUE=Lung;
 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).
 [6]
 INTERACTION WITH CBX3.
 PubMed=9864353; DOI=10.1083/jcb.143.7.1763;
 Ainsztein A.M., Kandels-Lewis S.E., Mackay A.M., Earnshaw W.C.;
 "INCENP centromere and spindle targeting: identification of essential
 conserved motifs and involvement of heterochromatin protein HP1.";
 J. Cell Biol. 143:1763-1774(1998).
 [7]
 INTERACTION WITH TUBULIN BETA CHAIN.
 PubMed=11139336; DOI=10.1006/excr.2000.5088;
 Wheatley S.P., Kandels-Lewis S.E., Adams R.R., Ainsztein A.M.,
 Earnshaw W.C.;
 "INCENP binds directly to tubulin and requires dynamic microtubules to
 target to the cleavage furrow.";
 Exp. Cell Res. 262:122-127(2001).
 [8]
 IDENTIFICATION IN THE CPC COMPLEX, FUNCTION OF THE CPC COMPLEX,
 INDUCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-892;
 SER-893 AND SER-894.
 PubMed=12925766; DOI=10.1091/mbc.E02-11-0769;
 Honda R., Korner R., Nigg E.A.;
 "Exploring the functional interactions between Aurora B, INCENP, and
 survivin in mitosis.";
 Mol. Biol. Cell 14:3325-3341(2003).
 [9]
 INTERACTION WITH BIRC5.
 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).
 [10]
 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).
 [11]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-275, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
 Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
 Mann M.;
 "Global, in vivo, and site-specific phosphorylation dynamics in
 signaling networks.";
 Cell 127:635-648(2006).
 [12]
 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).
 [13]
 FUNCTION, AND SUBCELLULAR LOCATION.
 PubMed=16760428; DOI=10.1091/mbc.E06-03-0240;
 Qi W., Tang Z., Yu H.;
 "Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is
 required for the kinetochore localization of Plk1.";
 Mol. Biol. Cell 17:3705-3716(2006).
 [14]
 INTERACTION WITH BIRC5 AND CDCA8.
 PubMed=16571674; DOI=10.1091/mbc.E05-12-1133;
 Klein U.R., Nigg E.A., Gruneberg U.;
 "Centromere targeting of the chromosomal passenger complex requires a
 ternary subcomplex of borealin, survivin, and the N-terminal domain of
 INCENP.";
 Mol. Biol. Cell 17:2547-2558(2006).
 [15]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=18220336; DOI=10.1021/pr0705441;
 Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
 Yates J.R. III;
 "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
 efficient phosphoproteomic analysis.";
 J. Proteome Res. 7:1346-1351(2008).
 [16]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-239; SER-263; SER-269;
 SER-275; SER-306; SER-400; THR-406; SER-476 AND SER-899, 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).
 [17]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-148; THR-239;
 THR-292; SER-296; SER-306; SER-312; SER-314; SER-446; SER-510;
 SER-514; SER-828; SER-831; THR-832; SER-894; SER-899 AND SER-914, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=18669648; DOI=10.1073/pnas.0805139105;
 Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
 Elledge S.J., Gygi S.P.;
 "A quantitative atlas of mitotic phosphorylation.";
 Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
 [18]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=19413330; DOI=10.1021/ac9004309;
 Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
 Mohammed S.;
 "Lys-N and trypsin cover complementary parts of the phosphoproteome in
 a refined SCX-based approach.";
 Anal. Chem. 81:4493-4501(2009).
 [19]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-828 AND
 SER-899, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
 Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
 Mann M., Daub H.;
 "Large-scale proteomics analysis of the human kinome.";
 Mol. Cell. Proteomics 8:1751-1764(2009).
 [20]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; THR-199; THR-213;
 SER-214; THR-239; SER-306; SER-314; SER-828; SER-831; THR-832 AND
 SER-899, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 TISSUE=Leukemic T-cell;
 PubMed=19690332; DOI=10.1126/scisignal.2000007;
 Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
 Rodionov V., Han D.K.;
 "Quantitative phosphoproteomic analysis of T cell receptor signaling
 reveals system-wide modulation of protein-protein interactions.";
 Sci. Signal. 2:RA46-RA46(2009).
 [21]
 INTERACTION WITH CBX5; POGZ AND AURKB, AND MUTAGENESIS OF VAL-169 AND
 ILE-171.
 PubMed=20562864; DOI=10.1038/ncb2075;
 Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N.,
 Kimura H., Obuse C.;
 "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome
 arms through Aurora B activation.";
 Nat. Cell Biol. 12:719-727(2010).
 [22]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-143; THR-239;
 SER-263; SER-275; THR-292; SER-312; SER-314; SER-330 AND SER-899, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=20068231; DOI=10.1126/scisignal.2000475;
 Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
 Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
 Mann M.;
 "Quantitative phosphoproteomics reveals widespread full
 phosphorylation site occupancy during mitosis.";
 Sci. Signal. 3:RA3-RA3(2010).
 [23]
 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).
 [24]
 FUNCTION, INTERACTION WITH CBX1; CBX3 AND CBX5, AND MUTAGENESIS OF
 PRO-167; VAL-169 AND ILE-171.
 PubMed=21346195; DOI=10.1091/mbc.E11-01-0009;
 Kang J., Chaudhary J., Dong H., Kim S., Brautigam C.A., Yu H.;
 "Mitotic centromeric targeting of HP1 and its binding to Sgo1 are
 dispensable for sister-chromatid cohesion in human cells.";
 Mol. Biol. Cell 22:1181-1190(2011).
 [25]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-306; SER-314
 AND SER-828, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 PubMed=21406692; DOI=10.1126/scisignal.2001570;
 Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
 Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
 Blagoev B.;
 "System-wide temporal characterization of the proteome and
 phosphoproteome of human embryonic stem cell differentiation.";
 Sci. Signal. 4:RS3-RS3(2011).
 [26]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-119; SER-263;
 SER-275; THR-292; SER-306; SER-446; SER-894; SER-899 AND SER-914, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma, and Erythroleukemia;
 PubMed=23186163; DOI=10.1021/pr300630k;
 Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
 Mohammed S.;
 "Toward a comprehensive characterization of a human cancer cell
 phosphoproteome.";
 J. Proteome Res. 12:260-271(2013).
 [27]
 INTERACTION WITH AURKC, FUNCTION, AND PHOSPHORYLATION AT THR-892;
 SER-893 AND SER-894.
 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).
 [28]
 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 3-46, INTERACTION WITH CDCA8
 AND BIRC5, AND MUTAGENESIS OF PHE-22; LEU-34; GLU-35; GLU-36; GLU-39
 AND GLU-40.
 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).
 [29]
 X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 835-903 IN COMPLEX WITH
 AURKB.
 PubMed=22920039; DOI=10.1021/jm3008954;
 Elkins J.M., Santaguida S., Musacchio A., Knapp S.;
 "Crystal structure of human aurora B in complex with INCENP and VX-
 680.";
 J. Med. Chem. 55:7841-7848(2012).
 -!- FUNCTION: Component of the chromosomal passenger complex (CPC), a
     complex that acts as a key regulator of mitosis. The CPC complex
     has essential functions at the centromere in ensuring correct
     chromosome alignment and segregation and is required for
     chromatin-induced microtubule stabilization and spindle assembly.
     Acts as a scaffold regulating CPC localization and activity. The
     C-terminus associates with AURKB or AURKC, the N-terminus
     associated with BIRC5/survivin and CDCA8/borealin tethers the CPC
     to the inner centromere, and the microtubule binding activity
     within the central SAH domain directs AURKB/C toward substrates
     near microtubules (PubMed:15316025, PubMed:12925766,
     PubMed:27332895). The flexibility of the SAH domain is proposed to
     allow AURKB/C to follow substrates on dynamic microtubules while
     ensuring CPC docking to static chromatin (By similarity).
     Activates AURKB and AURKC (PubMed:27332895). Required for
     localization of CBX5 to mitotic centromeres (PubMed:21346195).
     Controls the kinetochore localization of BUB1 (PubMed:16760428).
     {ECO:0000250|UniProtKB:P53352, ECO:0000269|PubMed:12925766,
     ECO:0000269|PubMed:15316025, ECO:0000269|PubMed:16760428,
     ECO:0000269|PubMed:21346195, ECO:0000269|PubMed:27332895}.
 -!- SUBUNIT: Component of the chromosomal passenger complex (CPC)
     composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB
     or AURKC; in the complex binds directly to AURKB or AURKC via the
     IN box, and forms a triple-helix bundle-based subcomplex with
     BIRC5 and CDCA8 via its N-terminus (PubMed:17956729,
     PubMed:27332895). The reported homodimerization is questioned as
     the SAH domain is shown to be monomeric (By similarity). Interacts
     with H2AFZ (By similarity). Interacts with CBX1 and CBX3.
     Interacts with tubulin beta chain. Interacts with EVI5. Interacts
     with CBX5; POGZ and INCENP compete for interaction with CBX5;
     regulates INCENP (and probably CPC) localization to centromeres in
     interphase and not required for proper mitotic progression or
     sister chromatid cohesion. Interacts with POGZ. Interacts with
     JTB. {ECO:0000250|UniProtKB:P53352, ECO:0000250|UniProtKB:Q9WU62,
     ECO:0000269|PubMed:11139336, ECO:0000269|PubMed:12925766,
     ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:15249581,
     ECO:0000269|PubMed:15316025, ECO:0000269|PubMed:16764853,
     ECO:0000269|PubMed:17956729, ECO:0000269|PubMed:20562864,
     ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:21346195,
     ECO:0000269|PubMed:22920039, ECO:0000269|PubMed:27332895,
     ECO:0000269|PubMed:9864353}.
 -!- INTERACTION:
     O14965:AURKA; NbExp=2; IntAct=EBI-307907, EBI-448680;
     Q96GD4:AURKB; NbExp=18; IntAct=EBI-307907, EBI-624291;
     Q9UQB9:AURKC; NbExp=16; IntAct=EBI-307907, EBI-3926851;
     O15392:BIRC5; NbExp=10; IntAct=EBI-307907, EBI-518823;
     P45973:CBX5; NbExp=11; IntAct=EBI-307907, EBI-78219;
     Q53HL2:CDCA8; NbExp=5; IntAct=EBI-307907, EBI-979174;
 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11453556}.
     Chromosome, centromere {ECO:0000269|PubMed:11453556,
     ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:15316025,
     ECO:0000269|PubMed:16760428}. Cytoplasm, cytoskeleton, spindle
     {ECO:0000269|PubMed:11453556, ECO:0000269|PubMed:15316025}.
     Midbody {ECO:0000269|PubMed:15316025}. Chromosome, centromere,
     kinetochore {ECO:0000269|PubMed:14610074}. Note=Colocalized at
     synaptonemal complex central element from zygotene up to late
     pachytene when it begins to relocalize to heterochromatic
     chromocenters. Colocalizes with AURKB at a connecting strand
     traversing the centromere region and joining sister kinetochores,
     in metaphase II centromeres. This strand disappears at the
     metaphase II/anaphase II transition and relocalizes to the spindle
     midzone (By similarity). Colocalizes with AURKB at mitotic
     chromosomes (PubMed:11453556). Localizes to inner kinetochore
     (PubMed:16760428). Localizes on chromosome arms and inner
     centromeres from prophase through metaphase and then transferring
     to the spindle midzone and midbody from anaphase through
     cytokinesis (PubMed:15316025). Cocalizes to the equatorial cell
     cortex at anaphase (PubMed:11453556).
     {ECO:0000250|UniProtKB:Q9WU62, ECO:0000269|PubMed:11453556,
     ECO:0000269|PubMed:15316025, ECO:0000269|PubMed:16760428}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=2;
     Name=1;
       IsoId=Q9NQS7-1; Sequence=Displayed;
     Name=2;
       IsoId=Q9NQS7-2; Sequence=VSP_035651;
 -!- DOMAIN: The IN box mediates interaction with AURKB and AURKC.
     {ECO:0000250|UniProtKB:O13024, ECO:0000269|PubMed:27332895}.
 -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a
     high content of charged residues which are predicted to stabilize
     the alpha-helical structure by ionic bonds. It can refold after
     extension suggesting an in vivo force-dependent function. The
     isolated SAH domain is monomeric. {ECO:0000250|UniProtKB:P53352}.
 -!- PTM: Phosphorylation by AURKB or AURKC at its C-terminal part is
     important for AURKB or AURKC activation by INCENP.
     {ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:15316025,
     ECO:0000269|PubMed:27332895}.
 -!- SIMILARITY: Belongs to the INCENP family. {ECO:0000305}.
 -!- CAUTION: PubMed:11139336 experiments have been carried out partly
     in chicken and partly in human. {ECO:0000305}.
 -!- CAUTION: Originally predicted to contain a coiled coil domain but
     shown to contain a stable SAH domain instead.
     {ECO:0000250|UniProtKB:P53352}.
 -----------------------------------------------------------------------
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 EMBL; AF282265; AAF87584.1; -; mRNA.
 EMBL; AY714053; AAU04398.1; -; mRNA.
 EMBL; AP002793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; CH471076; EAW74004.1; -; Genomic_DNA.
 EMBL; BC098576; AAH98576.1; -; mRNA.
 CCDS; CCDS31582.1; -. [Q9NQS7-2]
 CCDS; CCDS44624.1; -. [Q9NQS7-1]
 RefSeq; NP_001035784.1; NM_001040694.1. [Q9NQS7-1]
 RefSeq; NP_064623.2; NM_020238.2. [Q9NQS7-2]
 UniGene; Hs.142179; -.
 PDB; 2QFA; X-ray; 1.40 A; C=1-47.
 PDB; 4AF3; X-ray; 2.75 A; D=835-903.
 PDB; 5IEH; X-ray; 1.50 A; C=47-55.
 PDB; 5IEK; X-ray; 1.80 A; C=47-55.
 PDBsum; 2QFA; -.
 PDBsum; 4AF3; -.
 PDBsum; 5IEH; -.
 PDBsum; 5IEK; -.
 ProteinModelPortal; Q9NQS7; -.
 SMR; Q9NQS7; -.
 BioGrid; 109831; 26.
 ComplexPortal; CPX-116; Chromosomal passenger complex.
 CORUM; Q9NQS7; -.
 DIP; DIP-31304N; -.
 IntAct; Q9NQS7; 19.
 MINT; Q9NQS7; -.
 STRING; 9606.ENSP00000378295; -.
 BindingDB; Q9NQS7; -.
 ChEMBL; CHEMBL3430907; -.
 iPTMnet; Q9NQS7; -.
 PhosphoSitePlus; Q9NQS7; -.
 BioMuta; INCENP; -.
 DMDM; 212276501; -.
 EPD; Q9NQS7; -.
 MaxQB; Q9NQS7; -.
 PaxDb; Q9NQS7; -.
 PeptideAtlas; Q9NQS7; -.
 PRIDE; Q9NQS7; -.
 ProteomicsDB; 82181; -.
 ProteomicsDB; 82182; -. [Q9NQS7-2]
 Ensembl; ENST00000278849; ENSP00000278849; ENSG00000149503. [Q9NQS7-2]
 Ensembl; ENST00000394818; ENSP00000378295; ENSG00000149503. [Q9NQS7-1]
 GeneID; 3619; -.
 KEGG; hsa:3619; -.
 UCSC; uc001nsw.2; human. [Q9NQS7-1]
 CTD; 3619; -.
 DisGeNET; 3619; -.
 EuPathDB; HostDB:ENSG00000149503.12; -.
 GeneCards; INCENP; -.
 H-InvDB; HIX0009706; -.
 HGNC; HGNC:6058; INCENP.
 HPA; CAB013292; -.
 HPA; HPA051339; -.
 HPA; HPA070550; -.
 MIM; 604411; gene.
 neXtProt; NX_Q9NQS7; -.
 OpenTargets; ENSG00000149503; -.
 PharmGKB; PA29868; -.
 eggNOG; KOG4456; Eukaryota.
 eggNOG; ENOG410XRQ9; LUCA.
 GeneTree; ENSGT00730000111073; -.
 HOGENOM; HOG000113069; -.
 HOVERGEN; HBG006157; -.
 InParanoid; Q9NQS7; -.
 KO; K11515; -.
 OMA; ARIICHS; -.
 OrthoDB; EOG091G0CPA; -.
 PhylomeDB; Q9NQS7; -.
 TreeFam; TF101172; -.
 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-68877; Mitotic Prometaphase.
 SIGNOR; Q9NQS7; -.
 EvolutionaryTrace; Q9NQS7; -.
 GeneWiki; INCENP; -.
 GenomeRNAi; 3619; -.
 PRO; PR:Q9NQS7; -.
 Proteomes; UP000005640; Chromosome 11.
 Bgee; ENSG00000149503; Expressed in 130 organ(s), highest expression level in cerebellum.
 CleanEx; HS_INCENP; -.
 ExpressionAtlas; Q9NQS7; baseline and differential.
 Genevisible; Q9NQS7; HS.
 GO; GO:0000801; C:central element; IEA:Ensembl.
 GO; GO:0010369; C:chromocenter; IEA:Ensembl.
 GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
 GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO; GO:0005829; C:cytosol; IDA:HPA.
 GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
 GO; GO:0000800; C:lateral element; IEA:Ensembl.
 GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO; GO:0030496; C:midbody; IDA:HPA.
 GO; GO:0016604; C:nuclear body; IDA:HPA.
 GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO; GO:0005634; C:nucleus; IDA:HPA.
 GO; GO:0005721; C:pericentric heterochromatin; IDA:UniProtKB.
 GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
 GO; GO:0005819; C:spindle; IDA:UniProtKB.
 GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
 GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
 GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:InterPro.
 GO; GO:1902412; P:regulation of mitotic cytokinesis; IEA:InterPro.
 InterPro; IPR039130; INCENP.
 InterPro; IPR022006; INCENP_N.
 InterPro; IPR005635; Inner_centromere_prot_ARK-bd.
 PANTHER; PTHR13142; PTHR13142; 1.
 Pfam; PF03941; INCENP_ARK-bind; 1.
 Pfam; PF12178; INCENP_N; 1.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Cell cycle; Cell division;
 Centromere; Chromosome; Chromosome partition; Complete proteome;
 Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis; Nucleus;
 Phosphoprotein; Polymorphism; Reference proteome.
 CHAIN         1    918       Inner centromere protein.
                              /FTId=PRO_0000084201.
 REGION      124    248       Interaction with CBX5.
                              {ECO:0000269|PubMed:21346195}.
 REGION      531    765       SAH. {ECO:0000250|UniProtKB:P53352}.
 REGION      822    897       Interaction with AURKC.
                              {ECO:0000269|PubMed:27332895}.
 REGION      826    900       IN box. {ECO:0000305}.
 MOTIF       167    171       PXVXL/I motif.
                              {ECO:0000305|PubMed:21346195}.
 MOD_RES      72     72       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES     119    119       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     143    143       Phosphoserine.
                              {ECO:0000244|PubMed:20068231}.
 MOD_RES     148    148       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     150    150       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q9WU62}.
 MOD_RES     195    195       Phosphothreonine.
                              {ECO:0000269|PubMed:15316025}.
 MOD_RES     197    197       Phosphoserine.
                              {ECO:0000244|PubMed:19690332}.
 MOD_RES     199    199       Phosphothreonine.
                              {ECO:0000244|PubMed:19690332}.
 MOD_RES     213    213       Phosphothreonine.
                              {ECO:0000244|PubMed:19690332}.
 MOD_RES     214    214       Phosphoserine.
                              {ECO:0000244|PubMed:19690332}.
 MOD_RES     219    219       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q9WU62}.
 MOD_RES     239    239       Phosphothreonine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:18691976,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:20068231}.
 MOD_RES     263    263       Phosphoserine.
                              {ECO:0000244|PubMed:17081983,
                              ECO:0000244|PubMed:18691976,
                              ECO:0000244|PubMed:19369195,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     269    269       Phosphoserine.
                              {ECO:0000244|PubMed:18691976}.
 MOD_RES     275    275       Phosphoserine.
                              {ECO:0000244|PubMed:17081983,
                              ECO:0000244|PubMed:18691976,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     292    292       Phosphothreonine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     296    296       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     306    306       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:18691976,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     312    312       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:20068231}.
 MOD_RES     314    314       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:21406692}.
 MOD_RES     330    330       Phosphoserine.
                              {ECO:0000244|PubMed:20068231}.
 MOD_RES     400    400       Phosphoserine.
                              {ECO:0000244|PubMed:18691976}.
 MOD_RES     406    406       Phosphothreonine.
                              {ECO:0000244|PubMed:18691976}.
 MOD_RES     446    446       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     476    476       Phosphoserine.
                              {ECO:0000244|PubMed:18691976}.
 MOD_RES     478    478       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q9WU62}.
 MOD_RES     480    480       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9WU62}.
 MOD_RES     510    510       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     514    514       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     828    828       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19369195,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:21406692}.
 MOD_RES     831    831       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332}.
 MOD_RES     832    832       Phosphothreonine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:19690332}.
 MOD_RES     892    892       Phosphothreonine; by AURKB and AURKC.
                              {ECO:0000269|PubMed:12925766,
                              ECO:0000269|PubMed:27332895}.
 MOD_RES     893    893       Phosphoserine; by AURKB and AURKC.
                              {ECO:0000269|PubMed:12925766,
                              ECO:0000269|PubMed:27332895}.
 MOD_RES     894    894       Phosphoserine; by AURKB and AURKC.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:23186163,
                              ECO:0000269|PubMed:12925766,
                              ECO:0000269|PubMed:27332895}.
 MOD_RES     899    899       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:18691976,
                              ECO:0000244|PubMed:19369195,
                              ECO:0000244|PubMed:19690332,
                              ECO:0000244|PubMed:20068231,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     914    914       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:23186163}.
 VAR_SEQ     532    535       Missing (in isoform 2).
                              {ECO:0000303|PubMed:11453556}.
                              /FTId=VSP_035651.
 VARIANT       2      2       G -> V (in dbSNP:rs1792947).
                              /FTId=VAR_047127.
 VARIANT     100    100       R -> H (in dbSNP:rs12281503).
                              /FTId=VAR_047128.
 VARIANT     137    137       A -> V (in dbSNP:rs34441559).
                              /FTId=VAR_047129.
 VARIANT     506    506       M -> T (in dbSNP:rs2277283).
                              /FTId=VAR_047130.
 VARIANT     644    644       E -> D (in dbSNP:rs7129085).
                              {ECO:0000269|PubMed:11453556,
                              ECO:0000269|PubMed:15316025,
                              ECO:0000269|PubMed:15489334}.
                              /FTId=VAR_047131.
 MUTAGEN      22     22       F->R: Loss of binding to CDCA8 and BIRC5;
                              when associated with R-34.
                              {ECO:0000269|PubMed:17956729}.
 MUTAGEN      34     34       L->R: Loss of binding to CDCA8 and BIRC5;
                              when associated with R-22.
                              {ECO:0000269|PubMed:17956729}.
 MUTAGEN      35     35       E->R: Loss of localization to the central
                              spindle and midbody in anaphase or
                              cytokinesis; when associated with R-36;
                              R-39 and R-40.
                              {ECO:0000269|PubMed:17956729}.
 MUTAGEN      36     36       E->R: Loss of localization to the central
                              spindle and midbody in anaphase or
                              cytokinesis; when associated with R-35;
                              R-39 and R-40.
                              {ECO:0000269|PubMed:17956729}.
 MUTAGEN      39     39       E->R: Loss of localization to the central
                              spindle and midbody in anaphase or
                              cytokinesis; when associated with R-35;
                              R-36 and R-40.
                              {ECO:0000269|PubMed:17956729}.
 MUTAGEN      40     40       E->R: Loss of localization to the central
                              spindle and midbody in anaphase or
                              cytokinesis; when associated with R-35;
                              R-36 and R-39.
                              {ECO:0000269|PubMed:17956729}.
 MUTAGEN     167    167       P->A: Decreases interaction with CBX5,
                              abolishes localization to centromeres in
                              interphase; when associated with A-169
                              and A-171. {ECO:0000269|PubMed:21346195}.
 MUTAGEN     169    169       V->A: Decreases interaction with CBX5,
                              abolishes localization to centromeres in
                              interphase; when associated with A-167
                              and A-171. {ECO:0000269|PubMed:21346195}.
 MUTAGEN     169    169       V->E: Abolishes interaction with CBX5.
                              {ECO:0000269|PubMed:20562864}.
 MUTAGEN     171    171       I->A: Decreases interaction with CBX5,
                              abolishes localization to centromeres in
                              interphase; when associated with A-167
                              and A-169. {ECO:0000269|PubMed:21346195}.
 MUTAGEN     171    171       I->E: Abolishes interaction with CBX5 and
                              AURKB. {ECO:0000269|PubMed:20562864}.
 CONFLICT    715    715       Q -> QERREQ (in Ref. 1; AAF87584).
                              {ECO:0000305}.
 CONFLICT    804    806       YQM -> SPI (in Ref. 1; AAF87584).
                              {ECO:0000305}.
 CONFLICT    812    812       R -> K (in Ref. 1; AAF87584).
                              {ECO:0000305}.
 CONFLICT    816    816       K -> Q (in Ref. 1; AAF87584).
                              {ECO:0000305}.
 CONFLICT    820    820       D -> H (in Ref. 1; AAF87584).
                              {ECO:0000305}.
 CONFLICT    861    861       H -> Q (in Ref. 1; AAF87584).
                              {ECO:0000305}.
 HELIX         8     10       {ECO:0000244|PDB:2QFA}.
 HELIX        11     28       {ECO:0000244|PDB:2QFA}.
 HELIX        30     45       {ECO:0000244|PDB:2QFA}.
 HELIX       844    846       {ECO:0000244|PDB:4AF3}.
 HELIX       848    860       {ECO:0000244|PDB:4AF3}.
 HELIX       865    869       {ECO:0000244|PDB:4AF3}.
 TURN        878    880       {ECO:0000244|PDB:4AF3}.
 SEQUENCE   918 AA;  105429 MW;  644D081DCC9035E8 CRC64;
 MGTTAPGPIH LLELCDQKLM EFLCNMDNKD LVWLEEIQEE AERMFTREFS KEPELMPKTP
 SQKNRRKKRR ISYVQDENRD PIRRRLSRRK SRSSQLSSRR LRSKDSVEKL ATVVGENGSV
 LRRVTRAAAA AAAATMALAA PSSPTPESPT MLTKKPEDNH TQCQLVPVVE IGISERQNAE
 QHVTQLMSTE PLPRTLSPTP ASATAPTSQG IPTSDEESTP KKSKARILES ITVSSLMATP
 QDPKGQGVGT GRSASKLRIA QVSPGPRDSP AFPDSPWRER VLAPILPDNF STPTGSRTDS
 QSVRHSPIAP SSPSPQVLAQ KYSLVAKQES VVRRASRRLA KKTAEEPAAS GRIICHSYLE
 RLLNVEVPQK VGSEQKEPPE EAEPVAAAEP EVPENNGNNS WPHNDTEIAN STPNPKPAAS
 SPETPSAGQQ EAKTDQADGP REPPQSARRK RSYKQAVSEL DEEQHLEDEE LQPPRSKTPS
 SPCPASKVVR PLRTFLHTVQ RNQMLMTPTS APRSVMKSFI KRNTPLRMDP KCSFVEKERQ
 RLENLRRKEE AEQLRRQKVE EDKRRRLEEV KLKREERLRK VLQARERVEQ MKEEKKKQIE
 QKFAQIDEKT EKAKEERLAE EKAKKKAAAK KMEEVEARRK QEEEARRLRW LQQEEEERRH
 QELLQKKKEE EQERLRKAAE AKRLAEQREQ ERREQERREQ ERREQERREQ ERREQERQLA
 EQERRREQER LQAERELQER EKALRLQKEQ LQRELEEKKK KEEQQRLAER QLQEEQEKKA
 KEAAGASKAL NVTVDVQSPA CTSYQMTPQG HRAPPKINPD NYGMDLNSDD STDDEAHPRK
 PIPTWARGTP LSQAIIHQYY HPPNLLELFG TILPLDLEDI FKKSKPRYHK RTSSAVWNSP
 PLQGARVPSS LAYSLKKH

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