ID INCE_HUMAN Reviewed; 918 AA. AC Q9NQS7; A8MQD2; Q5Y192; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 3. DT 27-MAR-2024, entry version 193. DE RecName: Full=Inner centromere protein; GN Name=INCENP; 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 [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND VARIANT RP ASP-644. RC TISSUE=Cervix carcinoma; RX PubMed=11453556; DOI=10.1007/s004120100130; RA Adams R.R., Eckley D.M., Vagnarelli P., Wheatley S.P., Gerloff D.L., RA Mackay A.M., Svingen P.A., Kaufmann S.H., Earnshaw W.C.; RT "Human INCENP colocalizes with the Aurora-B/AIRK2 kinase on chromosomes and RT is overexpressed in tumour cells."; RL Chromosoma 110:65-74(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH AURKB RP AND AURKC, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-195, AND VARIANT RP ASP-644. RC TISSUE=Testis; RX PubMed=15316025; DOI=10.1074/jbc.m403029200; RA Li X., Sakashita G., Matsuzaki H., Sugimoto K., Kimura K., Hanaoka F., RA Taniguchi H., Furukawa K., Urano T.; RT "Direct association with inner centromere protein (INCENP) activates the RT novel chromosomal passenger protein, Aurora-C."; RL J. Biol. Chem. 279:47201-47211(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-644. RC TISSUE=Lung; 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 [6] RP INTERACTION WITH CBX3. RX PubMed=9864353; DOI=10.1083/jcb.143.7.1763; RA Ainsztein A.M., Kandels-Lewis S.E., Mackay A.M., Earnshaw W.C.; RT "INCENP centromere and spindle targeting: identification of essential RT conserved motifs and involvement of heterochromatin protein HP1."; RL J. Cell Biol. 143:1763-1774(1998). RN [7] RP INTERACTION WITH TUBULIN BETA CHAIN. RX PubMed=11139336; DOI=10.1006/excr.2000.5088; RA Wheatley S.P., Kandels-Lewis S.E., Adams R.R., Ainsztein A.M., RA Earnshaw W.C.; RT "INCENP binds directly to tubulin and requires dynamic microtubules to RT target to the cleavage furrow."; RL Exp. Cell Res. 262:122-127(2001). RN [8] RP IDENTIFICATION IN THE CPC COMPLEX, FUNCTION OF THE CPC COMPLEX, INDUCTION, RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-892; SER-893 AND SER-894. RX PubMed=12925766; DOI=10.1091/mbc.e02-11-0769; RA Honda R., Korner R., Nigg E.A.; RT "Exploring the functional interactions between Aurora B, INCENP, and RT survivin in mitosis."; RL Mol. Biol. Cell 14:3325-3341(2003). RN [9] RP INTERACTION WITH BIRC5. 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 [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-275, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [12] 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 [13] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16760428; DOI=10.1091/mbc.e06-03-0240; RA Qi W., Tang Z., Yu H.; RT "Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is RT required for the kinetochore localization of Plk1."; RL Mol. Biol. Cell 17:3705-3716(2006). RN [14] RP INTERACTION WITH BIRC5 AND CDCA8. RX PubMed=16571674; DOI=10.1091/mbc.e05-12-1133; RA Klein U.R., Nigg E.A., Gruneberg U.; RT "Centromere targeting of the chromosomal passenger complex requires a RT ternary subcomplex of borealin, survivin, and the N-terminal domain of RT INCENP."; RL Mol. Biol. Cell 17:2547-2558(2006). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-239; SER-263; SER-269; RP SER-275; SER-306; SER-400; THR-406; SER-476 AND SER-899, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-148; THR-239; RP THR-292; SER-296; SER-306; SER-312; SER-314; SER-446; SER-510; SER-514; RP SER-828; SER-831; THR-832; SER-894; SER-899 AND SER-914, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-828 AND SER-899, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; THR-199; THR-213; RP SER-214; THR-239; SER-306; SER-314; SER-828; SER-831; THR-832 AND SER-899, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [21] RP INTERACTION WITH CBX5; POGZ AND AURKB, AND MUTAGENESIS OF VAL-169 AND RP ILE-171. RX PubMed=20562864; DOI=10.1038/ncb2075; RA Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., RA Kimura H., Obuse C.; RT "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms RT through Aurora B activation."; RL Nat. Cell Biol. 12:719-727(2010). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-143; THR-239; RP SER-263; SER-275; THR-292; SER-312; SER-314; SER-330 AND SER-899, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [23] 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 [24] RP FUNCTION, INTERACTION WITH CBX1; CBX3 AND CBX5, AND MUTAGENESIS OF PRO-167; RP VAL-169 AND ILE-171. RX PubMed=21346195; DOI=10.1091/mbc.e11-01-0009; RA Kang J., Chaudhary J., Dong H., Kim S., Brautigam C.A., Yu H.; RT "Mitotic centromeric targeting of HP1 and its binding to Sgo1 are RT dispensable for sister-chromatid cohesion in human cells."; RL Mol. Biol. Cell 22:1181-1190(2011). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-306; SER-314 AND RP SER-828, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-119; SER-263; RP SER-275; THR-292; SER-306; SER-446; SER-894; SER-899 AND SER-914, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [27] RP INTERACTION WITH AURKC, FUNCTION, AND PHOSPHORYLATION AT THR-892; SER-893 RP AND SER-894. 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 [28] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 3-46, INTERACTION WITH CDCA8 AND RP BIRC5, AND MUTAGENESIS OF PHE-22; LEU-34; GLU-35; GLU-36; GLU-39 AND RP GLU-40. 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 [29] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 835-903 IN COMPLEX WITH AURKB. RX PubMed=22920039; DOI=10.1021/jm3008954; RA Elkins J.M., Santaguida S., Musacchio A., Knapp S.; RT "Crystal structure of human aurora B in complex with INCENP and VX-680."; RL J. Med. Chem. 55:7841-7848(2012). CC -!- FUNCTION: Component of the chromosomal passenger complex (CPC), a CC complex that acts as a key regulator of mitosis. The CPC complex has CC essential functions at the centromere in ensuring correct chromosome CC alignment and segregation and is required for chromatin-induced CC microtubule stabilization and spindle assembly. Acts as a scaffold CC regulating CPC localization and activity. The C-terminus associates CC with AURKB or AURKC, the N-terminus associated with BIRC5/survivin and CC CDCA8/borealin tethers the CPC to the inner centromere, and the CC microtubule binding activity within the central SAH domain directs CC AURKB/C toward substrates near microtubules (PubMed:15316025, CC PubMed:12925766, PubMed:27332895). The flexibility of the SAH domain is CC proposed to allow AURKB/C to follow substrates on dynamic microtubules CC while ensuring CPC docking to static chromatin (By similarity). CC Activates AURKB and AURKC (PubMed:27332895). Required for localization CC of CBX5 to mitotic centromeres (PubMed:21346195). Controls the CC kinetochore localization of BUB1 (PubMed:16760428). CC {ECO:0000250|UniProtKB:P53352, ECO:0000269|PubMed:12925766, CC ECO:0000269|PubMed:15316025, ECO:0000269|PubMed:16760428, CC ECO:0000269|PubMed:21346195, ECO:0000269|PubMed:27332895}. CC -!- SUBUNIT: Component of the chromosomal passenger complex (CPC) composed CC of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in CC the complex binds directly to AURKB or AURKC via the IN box, and forms CC a triple-helix bundle-based subcomplex with BIRC5 and CDCA8 via its N- CC terminus (PubMed:17956729, PubMed:27332895). The reported CC homodimerization is questioned as the SAH domain is shown to be CC monomeric (By similarity). Interacts with H2AZ1 (By similarity). CC Interacts with CBX1 and CBX3. Interacts with tubulin beta chain. CC Interacts with EVI5. Interacts with CBX5; POGZ and INCENP compete for CC interaction with CBX5; regulates INCENP (and probably CPC) localization CC to centromeres in interphase and not required for proper mitotic CC progression or sister chromatid cohesion. Interacts with POGZ. CC Interacts with JTB. {ECO:0000250|UniProtKB:P53352, CC ECO:0000250|UniProtKB:Q9WU62, ECO:0000269|PubMed:11139336, CC ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14610074, CC ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:15316025, CC ECO:0000269|PubMed:16764853, ECO:0000269|PubMed:17956729, CC ECO:0000269|PubMed:20562864, ECO:0000269|PubMed:21225229, CC ECO:0000269|PubMed:21346195, ECO:0000269|PubMed:22920039, CC ECO:0000269|PubMed:27332895, ECO:0000269|PubMed:9864353}. CC -!- INTERACTION: CC Q9NQS7; O14965: AURKA; NbExp=2; IntAct=EBI-307907, EBI-448680; CC Q9NQS7; Q96GD4: AURKB; NbExp=19; IntAct=EBI-307907, EBI-624291; CC Q9NQS7; Q9UQB9: AURKC; NbExp=17; IntAct=EBI-307907, EBI-3926851; CC Q9NQS7; O15392: BIRC5; NbExp=10; IntAct=EBI-307907, EBI-518823; CC Q9NQS7; P45973: CBX5; NbExp=11; IntAct=EBI-307907, EBI-78219; CC Q9NQS7; Q53HL2: CDCA8; NbExp=5; IntAct=EBI-307907, EBI-979174; CC Q9NQS7-1; O14965: AURKA; NbExp=2; IntAct=EBI-15767972, EBI-448680; CC Q9NQS7-1; Q96GD4: AURKB; NbExp=2; IntAct=EBI-15767972, EBI-624291; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11453556}. CC Chromosome, centromere {ECO:0000269|PubMed:11453556, CC ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:15316025, CC ECO:0000269|PubMed:16760428}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:11453556, ECO:0000269|PubMed:15316025}. Midbody CC {ECO:0000269|PubMed:15316025}. Chromosome, centromere, kinetochore CC {ECO:0000269|PubMed:14610074}. Note=Colocalized at synaptonemal complex CC central element from zygotene up to late pachytene when it begins to CC relocalize to heterochromatic chromocenters. Colocalizes with AURKB at CC a connecting strand traversing the centromere region and joining sister CC kinetochores, in metaphase II centromeres. This strand disappears at CC the metaphase II/anaphase II transition and relocalizes to the spindle CC midzone (By similarity). Colocalizes with AURKB at mitotic chromosomes CC (PubMed:11453556). Localizes to inner kinetochore (PubMed:16760428). CC Localizes on chromosome arms and inner centromeres from prophase CC through metaphase and then transferring to the spindle midzone and CC midbody from anaphase through cytokinesis (PubMed:15316025). Cocalizes CC to the equatorial cell cortex at anaphase (PubMed:11453556). CC {ECO:0000250|UniProtKB:Q9WU62, ECO:0000269|PubMed:11453556, CC ECO:0000269|PubMed:15316025, ECO:0000269|PubMed:16760428}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NQS7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NQS7-2; Sequence=VSP_035651; CC -!- DOMAIN: The IN box mediates interaction with AURKB and AURKC. CC {ECO:0000250|UniProtKB:O13024, ECO:0000269|PubMed:27332895}. CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a high CC content of charged residues which are predicted to stabilize the alpha- CC helical structure by ionic bonds. It can refold after extension CC suggesting an in vivo force-dependent function. The isolated SAH domain CC is monomeric. {ECO:0000250|UniProtKB:P53352}. CC -!- PTM: Phosphorylation by AURKB or AURKC at its C-terminal part is CC important for AURKB or AURKC activation by INCENP. CC {ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:15316025, CC ECO:0000269|PubMed:27332895}. CC -!- SIMILARITY: Belongs to the INCENP family. {ECO:0000305}. CC -!- CAUTION: PubMed:11139336 experiments have been carried out partly in CC chicken and partly in human. {ECO:0000305}. CC -!- CAUTION: Originally predicted to contain a coiled coil domain but shown CC to contain a stable SAH domain instead. {ECO:0000250|UniProtKB:P53352}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF282265; AAF87584.1; -; mRNA. DR EMBL; AY714053; AAU04398.1; -; mRNA. DR EMBL; AP002793; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74004.1; -; Genomic_DNA. DR EMBL; BC098576; AAH98576.1; -; mRNA. DR CCDS; CCDS31582.1; -. [Q9NQS7-2] DR CCDS; CCDS44624.1; -. [Q9NQS7-1] DR RefSeq; NP_001035784.1; NM_001040694.1. [Q9NQS7-1] DR RefSeq; NP_064623.2; NM_020238.2. [Q9NQS7-2] DR PDB; 2QFA; X-ray; 1.40 A; C=1-47. DR PDB; 4AF3; X-ray; 2.75 A; D=835-903. DR PDB; 5IEH; X-ray; 1.50 A; C=47-55. DR PDB; 5IEK; X-ray; 1.80 A; C=47-55. DR PDB; 6GR8; X-ray; 1.75 A; B=835-903. DR PDB; 6GR9; X-ray; 2.25 A; B=835-903. DR PDB; 6YIE; X-ray; 3.49 A; C/F=1-58. DR PDB; 6YIF; X-ray; 1.81 A; C=7-57. DR PDB; 6YIH; X-ray; 2.55 A; C=5-80. DR PDBsum; 2QFA; -. DR PDBsum; 4AF3; -. DR PDBsum; 5IEH; -. DR PDBsum; 5IEK; -. DR PDBsum; 6GR8; -. DR PDBsum; 6GR9; -. DR PDBsum; 6YIE; -. DR PDBsum; 6YIF; -. DR PDBsum; 6YIH; -. DR AlphaFoldDB; Q9NQS7; -. DR SMR; Q9NQS7; -. DR BioGRID; 109831; 76. DR ComplexPortal; CPX-116; Chromosomal passenger complex. DR CORUM; Q9NQS7; -. DR DIP; DIP-31304N; -. DR IntAct; Q9NQS7; 30. DR MINT; Q9NQS7; -. DR STRING; 9606.ENSP00000378295; -. DR BindingDB; Q9NQS7; -. DR ChEMBL; CHEMBL3430907; -. DR ChEMBL; CHEMBL4106141; -. DR DrugBank; DB07340; Reversine. DR GlyGen; Q9NQS7; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q9NQS7; -. DR PhosphoSitePlus; Q9NQS7; -. DR SwissPalm; Q9NQS7; -. DR BioMuta; INCENP; -. DR DMDM; 212276501; -. DR EPD; Q9NQS7; -. DR jPOST; Q9NQS7; -. DR MassIVE; Q9NQS7; -. DR MaxQB; Q9NQS7; -. DR PaxDb; 9606-ENSP00000378295; -. DR PeptideAtlas; Q9NQS7; -. DR ProteomicsDB; 82181; -. [Q9NQS7-1] DR ProteomicsDB; 82182; -. [Q9NQS7-2] DR Pumba; Q9NQS7; -. DR Antibodypedia; 4598; 205 antibodies from 30 providers. DR DNASU; 3619; -. DR Ensembl; ENST00000278849.4; ENSP00000278849.4; ENSG00000149503.13. [Q9NQS7-2] DR Ensembl; ENST00000394818.8; ENSP00000378295.3; ENSG00000149503.13. [Q9NQS7-1] DR GeneID; 3619; -. DR KEGG; hsa:3619; -. DR MANE-Select; ENST00000394818.8; ENSP00000378295.3; NM_001040694.2; NP_001035784.1. DR UCSC; uc001nsw.2; human. [Q9NQS7-1] DR AGR; HGNC:6058; -. DR CTD; 3619; -. DR DisGeNET; 3619; -. DR GeneCards; INCENP; -. DR HGNC; HGNC:6058; INCENP. DR HPA; ENSG00000149503; Tissue enhanced (bone). DR MIM; 604411; gene. DR neXtProt; NX_Q9NQS7; -. DR OpenTargets; ENSG00000149503; -. DR PharmGKB; PA29868; -. DR VEuPathDB; HostDB:ENSG00000149503; -. DR eggNOG; KOG4456; Eukaryota. DR GeneTree; ENSGT00730000111073; -. DR HOGENOM; CLU_015997_0_0_1; -. DR InParanoid; Q9NQS7; -. DR OMA; SNDYGMD; -. DR OrthoDB; 3094173at2759; -. DR PhylomeDB; Q9NQS7; -. DR TreeFam; TF101172; -. DR PathwayCommons; Q9NQS7; -. 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-68877; Mitotic Prometaphase. DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. DR SignaLink; Q9NQS7; -. DR SIGNOR; Q9NQS7; -. DR BioGRID-ORCS; 3619; 784 hits in 1165 CRISPR screens. DR ChiTaRS; INCENP; human. DR EvolutionaryTrace; Q9NQS7; -. DR GeneWiki; INCENP; -. DR GenomeRNAi; 3619; -. DR Pharos; Q9NQS7; Tbio. DR PRO; PR:Q9NQS7; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9NQS7; Protein. DR Bgee; ENSG00000149503; Expressed in ventricular zone and 121 other cell types or tissues. DR ExpressionAtlas; Q9NQS7; baseline and differential. DR GO; GO:0000801; C:central element; IEA:Ensembl. DR GO; GO:0010369; C:chromocenter; IEA:Ensembl. DR GO; GO:0032133; C:chromosome passenger complex; IPI:ComplexPortal. DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0000776; C:kinetochore; IDA:HPA. DR GO; GO:0000800; C:lateral element; IEA:Ensembl. DR GO; GO:1990385; C:meiotic spindle midzone; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:ComplexPortal. DR GO; GO:0030496; C:midbody; IDA:HPA. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005721; C:pericentric heterochromatin; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IDA:UniProtKB. DR GO; GO:0140677; F:molecular function activator activity; IPI:DisProt. DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB. DR GO; GO:0051257; P:meiotic spindle midzone assembly; IBA:GO_Central. DR GO; GO:0051310; P:metaphase chromosome alignment; IBA:GO_Central. DR GO; GO:0000278; P:mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB. DR GO; GO:0090307; P:mitotic spindle assembly; NAS:ComplexPortal. DR GO; GO:0051256; P:mitotic spindle midzone assembly; NAS:ComplexPortal. DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; NAS:ComplexPortal. DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; NAS:ComplexPortal. DR GO; GO:1903490; P:positive regulation of mitotic cytokinesis; NAS:ComplexPortal. DR GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; NAS:ComplexPortal. DR DisProt; DP02390; -. DR Gene3D; 1.20.5.3600; -; 1. DR Gene3D; 6.10.250.2990; -; 1. DR IDEAL; IID00224; -. DR InterPro; IPR022006; INCENP_N. DR InterPro; IPR005635; Inner_centromere_prot_ARK-bd. DR PANTHER; PTHR13142; INNER CENTROMERE PROTEIN; 1. DR PANTHER; PTHR13142:SF1; INNER CENTROMERE PROTEIN; 1. DR Pfam; PF03941; INCENP_ARK-bind; 1. DR Pfam; PF12178; INCENP_N; 1. DR Genevisible; Q9NQS7; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere; KW Chromosome; Chromosome partition; Cytoplasm; Cytoskeleton; Kinetochore; KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..918 FT /note="Inner centromere protein" FT /id="PRO_0000084201" FT REGION 48..105 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 124..248 FT /note="Interaction with CBX5" FT /evidence="ECO:0000269|PubMed:21346195" FT REGION 138..159 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 190..253 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 285..316 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 371..489 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 531..765 FT /note="SAH" FT /evidence="ECO:0000250|UniProtKB:P53352" FT REGION 607..640 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 660..740 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 754..787 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 822..897 FT /note="Interaction with AURKC" FT /evidence="ECO:0000269|PubMed:27332895" FT REGION 826..900 FT /note="IN box" FT /evidence="ECO:0000305" FT REGION 826..845 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 167..171 FT /note="PXVXL/I motif" FT /evidence="ECO:0000305|PubMed:21346195" FT COMPBIAS 70..84 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 141..159 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 190..216 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 289..316 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 393..433 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 435..461 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 754..784 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 72 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 119 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 148 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 150 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9WU62" FT MOD_RES 195 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:15316025" FT MOD_RES 197 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 199 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 213 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 214 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 219 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9WU62" FT MOD_RES 239 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231" FT MOD_RES 263 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 269 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 275 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 292 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 296 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 306 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 312 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 314 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 330 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 400 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 406 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 446 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 476 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 478 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9WU62" FT MOD_RES 480 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WU62" FT MOD_RES 510 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 514 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 828 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692" FT MOD_RES 831 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 832 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 892 FT /note="Phosphothreonine; by AURKB and AURKC" FT /evidence="ECO:0000269|PubMed:12925766, FT ECO:0000269|PubMed:27332895" FT MOD_RES 893 FT /note="Phosphoserine; by AURKB and AURKC" FT /evidence="ECO:0000269|PubMed:12925766, FT ECO:0000269|PubMed:27332895" FT MOD_RES 894 FT /note="Phosphoserine; by AURKB and AURKC" FT /evidence="ECO:0000269|PubMed:12925766, FT ECO:0000269|PubMed:27332895, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 899 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 914 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 532..535 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11453556" FT /id="VSP_035651" FT VARIANT 2 FT /note="G -> V (in dbSNP:rs1792947)" FT /id="VAR_047127" FT VARIANT 100 FT /note="R -> H (in dbSNP:rs12281503)" FT /id="VAR_047128" FT VARIANT 137 FT /note="A -> V (in dbSNP:rs34441559)" FT /id="VAR_047129" FT VARIANT 506 FT /note="M -> T (in dbSNP:rs2277283)" FT /id="VAR_047130" FT VARIANT 644 FT /note="E -> D (in dbSNP:rs7129085)" FT /evidence="ECO:0000269|PubMed:11453556, FT ECO:0000269|PubMed:15316025, ECO:0000269|PubMed:15489334" FT /id="VAR_047131" FT MUTAGEN 22 FT /note="F->R: Loss of binding to CDCA8 and BIRC5; when FT associated with R-34." FT /evidence="ECO:0000269|PubMed:17956729" FT MUTAGEN 34 FT /note="L->R: Loss of binding to CDCA8 and BIRC5; when FT associated with R-22." FT /evidence="ECO:0000269|PubMed:17956729" FT MUTAGEN 35 FT /note="E->R: Loss of localization to the central spindle FT and midbody in anaphase or cytokinesis; when associated FT with R-36; R-39 and R-40." FT /evidence="ECO:0000269|PubMed:17956729" FT MUTAGEN 36 FT /note="E->R: Loss of localization to the central spindle FT and midbody in anaphase or cytokinesis; when associated FT with R-35; R-39 and R-40." FT /evidence="ECO:0000269|PubMed:17956729" FT MUTAGEN 39 FT /note="E->R: Loss of localization to the central spindle FT and midbody in anaphase or cytokinesis; when associated FT with R-35; R-36 and R-40." FT /evidence="ECO:0000269|PubMed:17956729" FT MUTAGEN 40 FT /note="E->R: Loss of localization to the central spindle FT and midbody in anaphase or cytokinesis; when associated FT with R-35; R-36 and R-39." FT /evidence="ECO:0000269|PubMed:17956729" FT MUTAGEN 167 FT /note="P->A: Decreases interaction with CBX5, abolishes FT localization to centromeres in interphase; when associated FT with A-169 and A-171." FT /evidence="ECO:0000269|PubMed:21346195" FT MUTAGEN 169 FT /note="V->A: Decreases interaction with CBX5, abolishes FT localization to centromeres in interphase; when associated FT with A-167 and A-171." FT /evidence="ECO:0000269|PubMed:21346195" FT MUTAGEN 169 FT /note="V->E: Abolishes interaction with CBX5." FT /evidence="ECO:0000269|PubMed:20562864" FT MUTAGEN 171 FT /note="I->A: Decreases interaction with CBX5, abolishes FT localization to centromeres in interphase; when associated FT with A-167 and A-169." FT /evidence="ECO:0000269|PubMed:21346195" FT MUTAGEN 171 FT /note="I->E: Abolishes interaction with CBX5 and AURKB." FT /evidence="ECO:0000269|PubMed:20562864" FT CONFLICT 715 FT /note="Q -> QERREQ (in Ref. 1; AAF87584)" FT /evidence="ECO:0000305" FT CONFLICT 804..806 FT /note="YQM -> SPI (in Ref. 1; AAF87584)" FT /evidence="ECO:0000305" FT CONFLICT 812 FT /note="R -> K (in Ref. 1; AAF87584)" FT /evidence="ECO:0000305" FT CONFLICT 816 FT /note="K -> Q (in Ref. 1; AAF87584)" FT /evidence="ECO:0000305" FT CONFLICT 820 FT /note="D -> H (in Ref. 1; AAF87584)" FT /evidence="ECO:0000305" FT CONFLICT 861 FT /note="H -> Q (in Ref. 1; AAF87584)" FT /evidence="ECO:0000305" FT HELIX 8..10 FT /evidence="ECO:0007829|PDB:2QFA" FT HELIX 11..28 FT /evidence="ECO:0007829|PDB:2QFA" FT HELIX 30..45 FT /evidence="ECO:0007829|PDB:2QFA" FT HELIX 844..846 FT /evidence="ECO:0007829|PDB:6GR8" FT HELIX 848..860 FT /evidence="ECO:0007829|PDB:6GR8" FT HELIX 865..869 FT /evidence="ECO:0007829|PDB:6GR8" FT HELIX 877..881 FT /evidence="ECO:0007829|PDB:6GR8" FT HELIX 886..889 FT /evidence="ECO:0007829|PDB:6GR8" FT HELIX 893..895 FT /evidence="ECO:0007829|PDB:6GR8" SQ 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 //