INCE_HUMAN
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 03-AUG-2022, entry version 184.
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}.
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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; 62.
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 iPTMnet; Q9NQS7; -.
DR PhosphoSitePlus; Q9NQS7; -.
DR BioMuta; INCENP; -.
DR DMDM; 212276501; -.
DR EPD; Q9NQS7; -.
DR jPOST; Q9NQS7; -.
DR MassIVE; Q9NQS7; -.
DR MaxQB; Q9NQS7; -.
DR PaxDb; Q9NQS7; -.
DR PeptideAtlas; Q9NQS7; -.
DR PRIDE; Q9NQS7; -.
DR ProteomicsDB; 82181; -. [Q9NQS7-1]
DR ProteomicsDB; 82182; -. [Q9NQS7-2]
DR Antibodypedia; 4598; 180 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 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; IICESGG; -.
DR OrthoDB; 671886at2759; -.
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; 760 hits in 1087 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 119 other tissues.
DR ExpressionAtlas; Q9NQS7; baseline and differential.
DR Genevisible; Q9NQS7; HS.
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:UniProtKB.
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:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
DR GO; GO:0051257; P:meiotic spindle midzone assembly; IBA:GO_Central.
DR GO; GO:0051310; P:metaphase plate congression; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IC:ComplexPortal.
DR GO; GO:0007052; P:mitotic spindle organization; IC:ComplexPortal.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IC:ComplexPortal.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IC:ComplexPortal.
DR GO; GO:1903490; P:positive regulation of mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; IC:ComplexPortal.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IC:ComplexPortal.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IC:ComplexPortal.
DR DisProt; DP02390; -.
DR IDEAL; IID00224; -.
DR InterPro; IPR039130; INCENP.
DR InterPro; IPR022006; INCENP_N.
DR InterPro; IPR005635; Inner_centromere_prot_ARK-bd.
DR PANTHER; PTHR13142; PTHR13142; 1.
DR Pfam; PF03941; INCENP_ARK-bind; 1.
DR Pfam; PF12178; INCENP_N; 1.
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
