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Inner centromere protein

 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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