INCE_MOUSE
ID INCE_MOUSE Reviewed; 880 AA.
AC Q9WU62; Q7TN28; Q8BGN4; Q8CGI4;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Inner centromere protein;
GN Name=Incenp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129;
RX PubMed=10087305; DOI=10.1007/s003359901014;
RA Saffery R., Irvine D.V., Kile B.T., Hudson D.F., Cutts S.M., Choo K.H.;
RT "Cloning, expression, and promoter structure of a mammalian inner
RT centromere protein (INCENP).";
RL Mamm. Genome 10:415-418(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Thymus;
RA Katayama H., Terada Y., Tatsuka M.;
RT "Cloning of mouse inner centromere protein (INCENP) cDNAs.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N;
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 [5]
RP INTERACTION WITH H2AZ1.
RX PubMed=12660166; DOI=10.1093/emboj/cdg160;
RA Rangasamy D., Berven L., Ridgway P., Tremethick D.J.;
RT "Pericentric heterochromatin becomes enriched with H2A.Z during early
RT mammalian development.";
RL EMBO J. 22:1599-1607(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12584241; DOI=10.1242/jcs.00330;
RA Parra M.T., Viera A., Gomez R., Page J., Carmena M., Earnshaw W.C.,
RA Rufas J.S., Suja J.A.;
RT "Dynamic relocalization of the chromosomal passenger complex proteins inner
RT centromere protein (INCENP) and aurora-B kinase during male mouse
RT meiosis.";
RL J. Cell Sci. 116:961-974(2003).
RN [7]
RP PHOSPHORYLATION BY AURKB.
RX PubMed=14722118; DOI=10.1074/jbc.m311128200;
RA Yasui Y., Urano T., Kawajiri A., Nagata K., Tatsuka M., Saya H.,
RA Furukawa K., Takahashi T., Izawa I., Inagaki M.;
RT "Autophosphorylation of a newly identified site of Aurora-B is
RT indispensable for cytokinesis.";
RL J. Biol. Chem. 279:12997-13003(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-215 AND SER-218, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-796; SER-799 AND THR-800, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-149; SER-190; THR-195;
RP THR-215; SER-218; SER-239; SER-245; SER-248; SER-251; SER-259; SER-284;
RP THR-452; SER-454; SER-796; SER-799; THR-800; SER-861; SER-862 AND SER-867,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP GLYCOSYLATION AT ASN-450, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20571061; DOI=10.1074/mcp.m110.000430;
RA Kurogochi M., Matsushista T., Amano M., Furukawa J., Shinohara Y.,
RA Aoshima M., Nishimura S.;
RT "Sialic acid-focused quantitative mouse serum glycoproteomics by multiple
RT reaction monitoring assay.";
RL Mol. Cell. Proteomics 9:2354-2368(2010).
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. The flexibility of the SAH
CC domain is proposed to allow AURKB/C to follow substrates on dynamic
CC microtubules while ensuring CPC docking to static chromatin (By
CC similarity). Activates AURKB and AURKC. Controls the kinetochore
CC localization of BUB1. {ECO:0000250|UniProtKB:P53352,
CC ECO:0000250|UniProtKB:Q9NQS7}.
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. The reported homodimerization is questioned as the SAH domain
CC is shown to be monomeric. Interacts with H2AZ1. Interacts with CBX1 and
CC CBX3. Interacts with tubulin beta chain. Interacts with EVI5. Interacts
CC with CBX5; POGZ and INCENP compete for interaction with CBX5. Interacts
CC with POGZ. Interacts with JTB. {ECO:0000250|UniProtKB:P53352,
CC ECO:0000250|UniProtKB:Q9NQS7, ECO:0000269|PubMed:12660166}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000269|PubMed:12584241}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:12584241}. Nucleus {ECO:0000269|PubMed:12584241}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12584241}.
CC Midbody {ECO:0000250|UniProtKB:Q9NQS7}. Note=Localizes to inner
CC kinetochore. Localizes on chromosome arms and inner centromeres from
CC prophase through metaphase and then transferring to the spindle midzone
CC and midbody from anaphase through cytokinesis. Colocalizes to the
CC equatorial cell cortex at anaphase (By similarity). Localized at
CC synaptonemal complex central element from zygotene up to late pachytene
CC when it begins to relocalize to heterochromatic chromocenters
CC (PubMed:12584241). Colocalizes with AURKB at a connecting strand
CC traversing the centromere region and joining sister kinetochores, in
CC metaphase II centromeres. This strand disappears at the metaphase
CC II/anaphase II transition and relocalizes to the spindle midzone
CC (PubMed:12584241). {ECO:0000250|UniProtKB:Q9NQS7,
CC ECO:0000269|PubMed:12584241}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=B;
CC IsoId=Q9WU62-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=Q9WU62-2; Sequence=VSP_007233;
CC -!- DOMAIN: The IN box mediates interaction with AURKB and AURKC.
CC {ECO:0000250|UniProtKB:O13024, ECO:0000250|UniProtKB:Q9NQS7}.
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 at its C-terminal part is important for
CC AURKB activation by INCENP. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform in thymic lymphoma 3SB cells.
CC Fourfold more abundant than isoform 2.
CC -!- MISCELLANEOUS: [Isoform 2]: Minor isoform in thymic lymphoma 3SB cells.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the INCENP family. {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; AF117610; AAD32094.1; -; mRNA.
DR EMBL; AB100432; BAC55879.1; -; mRNA.
DR EMBL; AB100433; BAC55880.1; -; mRNA.
DR EMBL; AK081841; BAC38346.1; -; mRNA.
DR EMBL; AK088627; BAC40462.1; -; mRNA.
DR EMBL; BC037011; AAH37011.1; -; mRNA.
DR EMBL; BC052414; AAH52414.1; -; mRNA.
DR CCDS; CCDS37912.1; -. [Q9WU62-2]
DR CCDS; CCDS89338.1; -. [Q9WU62-1]
DR RefSeq; NP_057901.2; NM_016692.3. [Q9WU62-2]
DR RefSeq; XP_006526775.1; XM_006526712.1.
DR AlphaFoldDB; Q9WU62; -.
DR SMR; Q9WU62; -.
DR BioGRID; 200760; 11.
DR ComplexPortal; CPX-119; Chromosomal passenger complex.
DR DIP; DIP-56678N; -.
DR IntAct; Q9WU62; 9.
DR STRING; 10090.ENSMUSP00000025562; -.
DR GlyConnect; 806; 1 N-Linked glycan (1 site).
DR GlyGen; Q9WU62; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q9WU62; -.
DR PhosphoSitePlus; Q9WU62; -.
DR EPD; Q9WU62; -.
DR jPOST; Q9WU62; -.
DR MaxQB; Q9WU62; -.
DR PaxDb; Q9WU62; -.
DR PeptideAtlas; Q9WU62; -.
DR PRIDE; Q9WU62; -.
DR ProteomicsDB; 267135; -. [Q9WU62-1]
DR ProteomicsDB; 267136; -. [Q9WU62-2]
DR Antibodypedia; 4598; 180 antibodies from 30 providers.
DR DNASU; 16319; -.
DR Ensembl; ENSMUST00000025562; ENSMUSP00000025562; ENSMUSG00000024660. [Q9WU62-2]
DR Ensembl; ENSMUST00000237439; ENSMUSP00000157547; ENSMUSG00000024660. [Q9WU62-1]
DR GeneID; 16319; -.
DR KEGG; mmu:16319; -.
DR UCSC; uc008gor.2; mouse. [Q9WU62-1]
DR UCSC; uc008gos.2; mouse. [Q9WU62-2]
DR CTD; 3619; -.
DR MGI; MGI:1313288; Incenp.
DR VEuPathDB; HostDB:ENSMUSG00000024660; -.
DR eggNOG; KOG4456; Eukaryota.
DR GeneTree; ENSGT00730000111073; -.
DR HOGENOM; CLU_015997_0_0_1; -.
DR InParanoid; Q9WU62; -.
DR OMA; IICESGG; -.
DR OrthoDB; 671886at2759; -.
DR PhylomeDB; Q9WU62; -.
DR TreeFam; TF101172; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 16319; 24 hits in 73 CRISPR screens.
DR ChiTaRS; Incenp; mouse.
DR PRO; PR:Q9WU62; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9WU62; protein.
DR Bgee; ENSMUSG00000024660; Expressed in respiratory primordium and 246 other tissues.
DR ExpressionAtlas; Q9WU62; baseline and differential.
DR Genevisible; Q9WU62; MM.
DR GO; GO:0000801; C:central element; IDA:MGI.
DR GO; GO:0010369; C:chromocenter; IDA:MGI.
DR GO; GO:0032133; C:chromosome passenger complex; ISO:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0000800; C:lateral element; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0030496; C:midbody; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; ISS: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; ISS: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 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 Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Glycoprotein;
KW Kinetochore; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..880
FT /note="Inner centromere protein"
FT /id="PRO_0000084202"
FT REGION 52..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..733
FT /note="SAH"
FT /evidence="ECO:0000250|UniProtKB:P53352"
FT REGION 513..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..868
FT /note="IN box"
FT /evidence="ECO:0000305"
FT COILED 506..759
FT /evidence="ECO:0000255"
FT COMPBIAS 70..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 195
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 270
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT MOD_RES 382
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT MOD_RES 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT MOD_RES 796
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 800
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 860
FT /note="Phosphothreonine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20571061"
FT VAR_SEQ 507..510
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_007233"
FT CONFLICT 397
FT /note="G -> S (in Ref. 1; AAD32094)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="T -> I (in Ref. 4; AAH52414)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="C -> F (in Ref. 1; AAD32094)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="K -> R (in Ref. 1; AAD32094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 880 AA; 101209 MW; 92169889A921FEFC CRC64;
MGTTAPGPIC LLDLCDQKLL DFVCNVDNKD FMWLKEIEEE AERMFIREFS NEPELMPKTP
SQKNRRKKRR VSNIQDENRD PVRKRLSRRK SRSSQVGTRH LRSKPVTIVE ENGFPVLQRI
TRATAAAAAA AAAASVASAS SSSTAGSPTV LTKKAVVEIS TSERLSAELQ LTKLKGSLPP
SPVSQGTLTS EEELTPKKSE AGKLDSVTVN SLKATPQSPK NRGVGEGRSV SKLKIARASW
GLQDSPGSTD SPWQERVLSP ILLNNILPTT AKSPLGNIRS VRRSLISQDS QVPLASKYNL
VAKQENGSRR SSRRIAKKAG KEPEASARII CHSYLERLLN VEVPQNVGLE QEPVEVAEPE
EAEEEQEVSK NSGCPSKPRS ATKIAISTPT SKPAAAGQTT TVEEQEAELD QTDGHREPPQ
SVRRKRSYKQ AISEPDEEQL EDEELQPCQN KTPSPPCPAN KVVRPLRTFL HTVQKNQMLM
TPTLASRSSV MKSFIKRNTP LRVDPKCSFV EKERQRLESL RRKEEAEQRR RQKVEEDKRR
RLEEVKLKRE ERLRKVLQAR ERVEQMKEEK KKQIEQKFAQ IDEKTEKAKE ERLAEKAKKK
ATAKKMEEVE ARRKQEEEAR RLRWLQQEEE ERRHQEMLQR KKEEEQERRK AAEARRLAEQ
REQERRREQE RREQERREQE RREQERKEQE RREQEQERLR AKREMQEREK ALRLQKERLQ
KELEEKKRKE EQQRLAEQQL QEEQAKKAKE VAAARKVLNM TVDVQSPVCT SYQMTPQGPK
SIPKISVDDY GMDLNSDDST DDESHPRKPI PSWAKGTQLS QAIVHQYYHP PNILELFGSI
LPLDLEDIFK KRKTRYHKRT SSAVWNSPPL KATMVPSSGD
