BOREA_HUMAN
ID BOREA_HUMAN Reviewed; 280 AA.
AC Q53HL2; D3DPT4; Q53HN1; Q96AM3; Q9NVW5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Borealin;
DE AltName: Full=Cell division cycle-associated protein 8;
DE AltName: Full=Dasra-B;
DE Short=hDasra-B;
DE AltName: Full=Pluripotent embryonic stem cell-related gene 3 protein;
GN Name=CDCA8; Synonyms=PESCRG3;
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].
RX PubMed=12188893; DOI=10.2174/1568009013334241;
RA Walker M.G.;
RT "Drug target discovery by gene expression analysis: cell cycle genes.";
RL Curr. Cancer Drug Targets 1:73-83(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nie Z., Du J., Lin G., Lu G.;
RT "The cloning and functional analysis of HPESCRG3.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Coronary arterial endothelium;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-12.
RC TISSUE=Colon, Kidney, and 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 [7]
RP FUNCTION, AND COMPONENT OF THE CPC COMPLEX.
RX PubMed=15260989; DOI=10.1016/j.cell.2004.06.026;
RA Sampath S.C., Ohi R., Leismann O., Salic A., Pozniakovski A., Funabiki H.;
RT "The chromosomal passenger complex is required for chromatin-induced
RT microtubule stabilization and spindle assembly.";
RL Cell 118:187-202(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE CPC COMPLEX,
RP PHOSPHORYLATION AT SER-165, AND MUTAGENESIS OF SER-165.
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 [9]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15561729; DOI=10.1074/mcp.m400158-mcp200;
RA Sauer G., Koerner R., Hanisch A., Ries A., Nigg E.A., Sillje H.H.W.;
RT "Proteome analysis of the human mitotic spindle.";
RL Mol. Cell. Proteomics 4:35-43(2005).
RN [10]
RP INTERACTION WITH BIRC5.
RX PubMed=16239925; DOI=10.1038/sj.embor.7400562;
RA Vader G., Kauw J.J.W., Medema R.H., Lens S.M.A.;
RT "Survivin mediates targeting of the chromosomal passenger complex to the
RT centromere and midbody.";
RL EMBO Rep. 7:85-92(2006).
RN [11]
RP SUBCELLULAR LOCATION, INTERACTION WITH BIRC5, AND DEVELOPMENTAL STAGE.
RX PubMed=16427043; DOI=10.1016/j.yexcr.2005.12.015;
RA Chang J.-L., Chen T.-H., Wang C.-F., Chiang Y.-H., Huang Y.-L., Wong F.-H.,
RA Chou C.-K., Chen C.-M.;
RT "Borealin/Dasra B is a cell cycle-regulated chromosomal passenger protein
RT and its nuclear accumulation is linked to poor prognosis for human gastric
RT cancer.";
RL Exp. Cell Res. 312:962-973(2006).
RN [12]
RP INTERACTION WITH BIRC5.
RX PubMed=16291752; DOI=10.1074/jbc.m508773200;
RA Noton E.A., Colnaghi R., Tate S., Starck C., Carvalho A., Ko Ferrigno P.,
RA Wheatley S.P.;
RT "Molecular analysis of survivin isoforms: evidence that alternatively
RT spliced variants do not play a role in mitosis.";
RL J. Biol. Chem. 281:1286-1295(2006).
RN [13]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BIRC5.
RX PubMed=16436504; DOI=10.1091/mbc.e05-08-0727;
RA Lens S.M.A., Rodriguez J.A., Vader G., Span S.W., Giaccone G., Medema R.H.;
RT "Uncoupling the central spindle-associated function of the chromosomal
RT passenger complex from its role at centromeres.";
RL Mol. Biol. Cell 17:1897-1909(2006).
RN [14]
RP FUNCTION.
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 SUBCELLULAR LOCATION.
RX PubMed=16547492; DOI=10.1038/sj.onc.1209499;
RA Rodriguez J.A., Lens S.M.A., Span S.W., Vader G., Medema R.H.,
RA Kruyt F.A.E., Giaccone G.;
RT "Subcellular localization and nucleocytoplasmic transport of the
RT chromosomal passenger proteins before nuclear envelope breakdown.";
RL Oncogene 25:4867-4879(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; SER-110; THR-189;
RP THR-204; SER-219 AND SER-244, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 INTERACTION WITH BIRC5.
RX PubMed=18591255; DOI=10.1128/mcb.02039-07;
RA Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.;
RT "A survivin-ran complex regulates spindle formation in tumor cells.";
RL Mol. Cell. Biol. 28:5299-5311(2008).
RN [18]
RP PHOSPHORYLATION BY TTK, AND FUNCTION.
RX PubMed=18243099; DOI=10.1016/j.cell.2007.11.046;
RA Jelluma N., Brenkman A.B., van den Broek N.J., Cruijsen C.W.A.,
RA van Osch M.H.J., Lens S.M.A., Medema R.H., Kops G.J.P.L.;
RT "Mps1 phosphorylates Borealin to control Aurora B activity and chromosome
RT alignment.";
RL Cell 132:233-246(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; THR-189; THR-204 AND
RP SER-219, AND IDENTIFICATION 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 [20]
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 [21]
RP INTERACTION WITH SENP3; UBE2I AND RANBP2, SUMOYLATION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-26.
RX PubMed=18946085; DOI=10.1091/mbc.e08-05-0511;
RA Klein U.R., Haindl M., Nigg E.A., Muller S.;
RT "RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation
RT cycle on Borealin.";
RL Mol. Biol. Cell 20:410-418(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219 AND SER-224, 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106 AND SER-219, AND
RP 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 [24]
RP INTERACTION WITH SGO1 AND SGO2, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP THR-106; THR-171; THR-185; THR-189; THR-199; THR-204 AND SER-219, AND
RP PHOSPHORYLATION.
RX PubMed=20739936; DOI=10.1038/nature09390;
RA Tsukahara T., Tanno Y., Watanabe Y.;
RT "Phosphorylation of the CPC by Cdk1 promotes chromosome bi-orientation.";
RL Nature 467:719-723(2010).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189 AND SER-219, 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; THR-189; THR-204 AND
RP SER-219, AND 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 [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-135, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 15-76, INTERACTION WITH BIRC5 AND
RP INCENP, AND MUTAGENESIS OF ARG-17; ARG-19; LYS-20; ARG-35; LEU-46; TRP-70
RP AND PHE-74.
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 [30]
RP STRUCTURE BY NMR OF 207-280, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF
RP 20-78, OLIGOMERIZATION, PHOSPHORYLATION AT THR-88; THR-94; THR-169; THR-230
RP AND SER-238, AND MUTAGENESIS OF THR-88; THR-94; THR-169 AND THR-230.
RX PubMed=19530738; DOI=10.1021/bi900530v;
RA Bourhis E., Lingel A., Phung Q., Fairbrother W.J., Cochran A.G.;
RT "Phosphorylation of a borealin dimerization domain is required for proper
RT chromosome segregation.";
RL Biochemistry 48:6783-6793(2009).
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. Major effector of the
CC TTK kinase in the control of attachment-error-correction and chromosome
CC alignment. {ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:15260989,
CC ECO:0000269|PubMed:16571674, ECO:0000269|PubMed:18243099}.
CC -!- SUBUNIT: May form homooligomers and homodimers. Component of the
CC chromosomal passenger complex (CPC) composed of at least
CC BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the complex
CC forms a triple-helix bundle-based subcomplex with INCENP and BIRC5
CC (PubMed:17956729). Interacts with SENP3, UBE2I and RANBP2. Interacts
CC (phosphorylated) with SGO1 and SGO2; the association is dependent on
CC CDK1. {ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:16239925,
CC ECO:0000269|PubMed:16291752, ECO:0000269|PubMed:16427043,
CC ECO:0000269|PubMed:16436504, ECO:0000269|PubMed:17956729,
CC ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:18946085,
CC ECO:0000269|PubMed:20739936}.
CC -!- INTERACTION:
CC Q53HL2; Q96GD4: AURKB; NbExp=9; IntAct=EBI-979174, EBI-624291;
CC Q53HL2; E7CU85: BIRC5; NbExp=2; IntAct=EBI-979174, EBI-10488580;
CC Q53HL2; O15392: BIRC5; NbExp=19; IntAct=EBI-979174, EBI-518823;
CC Q53HL2; O15392-1: BIRC5; NbExp=2; IntAct=EBI-979174, EBI-518838;
CC Q53HL2; O15392-2: BIRC5; NbExp=2; IntAct=EBI-979174, EBI-518842;
CC Q53HL2; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-979174, EBI-11748557;
CC Q53HL2; Q96EF6: FBXO17; NbExp=3; IntAct=EBI-979174, EBI-2510157;
CC Q53HL2; Q86XJ1: GAS2L3; NbExp=2; IntAct=EBI-979174, EBI-9248152;
CC Q53HL2; P13807: GYS1; NbExp=3; IntAct=EBI-979174, EBI-740553;
CC Q53HL2; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-979174, EBI-2549423;
CC Q53HL2; Q9NQS7: INCENP; NbExp=5; IntAct=EBI-979174, EBI-307907;
CC Q53HL2; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-979174, EBI-3920396;
CC Q53HL2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-979174, EBI-741158;
CC Q53HL2; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-979174, EBI-10232538;
CC Q53HL2; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-979174, EBI-747925;
CC Q53HL2; Q01105-2: SET; NbExp=3; IntAct=EBI-979174, EBI-7481343;
CC Q53HL2; Q5FBB7: SGO1; NbExp=3; IntAct=EBI-979174, EBI-989069;
CC Q53HL2; Q562F6: SGO2; NbExp=3; IntAct=EBI-979174, EBI-989213;
CC Q53HL2; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-979174, EBI-12004298;
CC Q53HL2; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-979174, EBI-12023934;
CC Q53HL2; G5E9M4: ZNF277; NbExp=3; IntAct=EBI-979174, EBI-11995620;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:18946085}.
CC Cytoplasm {ECO:0000269|PubMed:18946085}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:15561729}. Chromosome, centromere
CC {ECO:0000269|PubMed:20739936}. Note=Localizes on chromosome arms and
CC inner centromeres from prophase through metaphase and then transferring
CC to the spindle midzone and midbody from anaphase through cytokinesis.
CC Colocalizes with SENP3 in the nucleolus in interphase cells.
CC {ECO:0000269|PubMed:18946085}.
CC -!- DEVELOPMENTAL STAGE: Cell-cycle regulated. Increases during G2/M phase
CC and then reduces after exit from M phase.
CC {ECO:0000269|PubMed:16427043}.
CC -!- DOMAIN: The C-terminal region (aa 207-280) represents the dimerization
CC motif.
CC -!- PTM: Phosphorylated by TTK, essentially at Thr-88, Thr94, Thr-169 and
CC Thr-230. Phosphorylation (probably by CDK1) promotes targeting of the
CC CPC to centromeric DNA. {ECO:0000269|PubMed:15249581,
CC ECO:0000269|PubMed:18243099, ECO:0000269|PubMed:19530738}.
CC -!- PTM: Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through the
CC removal of SUMO2 and SUMO3. {ECO:0000269|PubMed:18946085}.
CC -!- MISCELLANEOUS: Cells lacking CDCA8 display a slight decrease in histone
CC H3 'Ser-10' phosphorylation, suggesting that the CPC complex mediates
CC phosphorylation of 'Ser-10' of histone H3.
CC -!- SIMILARITY: Belongs to the borealin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BG354581; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BG354581; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY508815; AAR91699.1; -; mRNA.
DR EMBL; AK001330; BAA91629.1; -; mRNA.
DR EMBL; AK022104; BAB13961.1; -; mRNA.
DR EMBL; AK022606; BAB14125.1; -; mRNA.
DR EMBL; AK222549; BAD96269.1; -; mRNA.
DR EMBL; AK222568; BAD96288.1; -; mRNA.
DR EMBL; CH471059; EAX07324.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07325.1; -; Genomic_DNA.
DR EMBL; BC000703; AAH00703.1; -; mRNA.
DR EMBL; BC001651; AAH01651.1; -; mRNA.
DR EMBL; BC016944; AAH16944.1; -; mRNA.
DR EMBL; BC008079; AAH08079.1; -; mRNA.
DR CCDS; CCDS424.1; -.
DR RefSeq; NP_001243804.1; NM_001256875.1.
DR RefSeq; NP_060571.1; NM_018101.3.
DR PDB; 2KDD; NMR; -; A/B=207-280.
DR PDB; 2QFA; X-ray; 1.40 A; B=15-76.
DR PDB; 2RAW; X-ray; 2.40 A; B=20-78.
DR PDB; 2RAX; X-ray; 3.30 A; B/F/Y=20-78.
DR PDB; 6YIE; X-ray; 3.49 A; B/E=10-109.
DR PDB; 6YIF; X-ray; 1.81 A; B=10-76.
DR PDB; 6YIH; X-ray; 2.55 A; B=10-76.
DR PDBsum; 2KDD; -.
DR PDBsum; 2QFA; -.
DR PDBsum; 2RAW; -.
DR PDBsum; 2RAX; -.
DR PDBsum; 6YIE; -.
DR PDBsum; 6YIF; -.
DR PDBsum; 6YIH; -.
DR AlphaFoldDB; Q53HL2; -.
DR BMRB; Q53HL2; -.
DR SMR; Q53HL2; -.
DR BioGRID; 120446; 111.
DR ComplexPortal; CPX-116; Chromosomal passenger complex.
DR CORUM; Q53HL2; -.
DR DIP; DIP-37995N; -.
DR IntAct; Q53HL2; 56.
DR MINT; Q53HL2; -.
DR STRING; 9606.ENSP00000362146; -.
DR iPTMnet; Q53HL2; -.
DR PhosphoSitePlus; Q53HL2; -.
DR BioMuta; CDCA8; -.
DR DMDM; 110832774; -.
DR EPD; Q53HL2; -.
DR jPOST; Q53HL2; -.
DR MassIVE; Q53HL2; -.
DR MaxQB; Q53HL2; -.
DR PaxDb; Q53HL2; -.
DR PeptideAtlas; Q53HL2; -.
DR PRIDE; Q53HL2; -.
DR ProteomicsDB; 62507; -.
DR Antibodypedia; 31756; 486 antibodies from 34 providers.
DR CPTC; Q53HL2; 1 antibody.
DR DNASU; 55143; -.
DR Ensembl; ENST00000327331.2; ENSP00000316121.2; ENSG00000134690.11.
DR Ensembl; ENST00000373055.6; ENSP00000362146.1; ENSG00000134690.11.
DR GeneID; 55143; -.
DR KEGG; hsa:55143; -.
DR MANE-Select; ENST00000373055.6; ENSP00000362146.1; NM_001256875.2; NP_001243804.1.
DR UCSC; uc001cbr.5; human.
DR CTD; 55143; -.
DR DisGeNET; 55143; -.
DR GeneCards; CDCA8; -.
DR HGNC; HGNC:14629; CDCA8.
DR HPA; ENSG00000134690; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MIM; 609977; gene.
DR neXtProt; NX_Q53HL2; -.
DR OpenTargets; ENSG00000134690; -.
DR PharmGKB; PA26281; -.
DR VEuPathDB; HostDB:ENSG00000134690; -.
DR eggNOG; ENOG502QS4S; Eukaryota.
DR GeneTree; ENSGT00390000011115; -.
DR HOGENOM; CLU_074128_0_0_1; -.
DR InParanoid; Q53HL2; -.
DR OMA; NWLEHWK; -.
DR OrthoDB; 1587028at2759; -.
DR PhylomeDB; Q53HL2; -.
DR TreeFam; TF101077; -.
DR PathwayCommons; Q53HL2; -.
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; Q53HL2; -.
DR SIGNOR; Q53HL2; -.
DR BioGRID-ORCS; 55143; 687 hits in 1096 CRISPR screens.
DR ChiTaRS; CDCA8; human.
DR EvolutionaryTrace; Q53HL2; -.
DR GeneWiki; CDCA8; -.
DR GenomeRNAi; 55143; -.
DR Pharos; Q53HL2; Tbio.
DR PRO; PR:Q53HL2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q53HL2; protein.
DR Bgee; ENSG00000134690; Expressed in oocyte and 111 other tissues.
DR Genevisible; Q53HL2; HS.
DR GO; GO:0010369; C:chromocenter; IEA:Ensembl.
DR GO; GO:0032133; C:chromosome passenger complex; IPI:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:ComplexPortal.
DR GO; GO:0030496; C:midbody; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0051276; P:chromosome organization; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
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:0006468; P:protein phosphorylation; IC:ComplexPortal.
DR IDEAL; IID00215; -.
DR InterPro; IPR018851; Borealin_N.
DR InterPro; IPR018867; Cell_div_borealin.
DR Pfam; PF10512; Borealin; 1.
DR Pfam; PF10444; Nbl1_Borealin_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Isopeptide bond; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..280
FT /note="Borealin"
FT /id="PRO_0000247075"
FT REGION 1..140
FT /note="Required for interaction with SENP3"
FT /evidence="ECO:0000269|PubMed:18946085"
FT REGION 1..88
FT /note="Required for centromere localization"
FT REGION 1..58
FT /note="Required for interaction with INCENP"
FT /evidence="ECO:0000269|PubMed:17956729"
FT REGION 10..109
FT /note="Required to form a minimal CPC core complex that
FT localizes to the central spindle and midbody and properly
FT executes the role of the CPC during cytokinesis"
FT REGION 20..78
FT /note="Required for interaction with INCENP and BIRC5"
FT /evidence="ECO:0000269|PubMed:17956729"
FT REGION 130..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphothreonine; by TTK"
FT /evidence="ECO:0000269|PubMed:19530738"
FT MOD_RES 94
FT /note="Phosphothreonine; by TTK"
FT /evidence="ECO:0000269|PubMed:19530738"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 165
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000269|PubMed:15249581"
FT MOD_RES 169
FT /note="Phosphothreonine; by TTK"
FT /evidence="ECO:0000269|PubMed:19530738"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163"
FT MOD_RES 219
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:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 230
FT /note="Phosphothreonine; by TTK"
FT /evidence="ECO:0000269|PubMed:19530738"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19530738"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 12
FT /note="K -> N (in dbSNP:rs17851453)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027063"
FT MUTAGEN 17
FT /note="R->E: Loss of localization to the central spindle
FT and midbody in anaphase or cytokinesis; when associated
FT with E-19 and E-20."
FT /evidence="ECO:0000269|PubMed:17956729"
FT MUTAGEN 19
FT /note="R->E: Loss of localization to the central spindle
FT and midbody in anaphase or cytokinesis; when associated
FT with E-17 and E-20."
FT /evidence="ECO:0000269|PubMed:17956729"
FT MUTAGEN 20
FT /note="K->E: Loss of localization to the central spindle
FT and midbody in anaphase or cytokinesis; when associated
FT with E-17 and E-19."
FT /evidence="ECO:0000269|PubMed:17956729"
FT MUTAGEN 26
FT /note="K->R: Fails to exhibit normal localization to the
FT nucleolus in interphase depleted cells."
FT /evidence="ECO:0000269|PubMed:18946085"
FT MUTAGEN 35
FT /note="R->E: Loss of binding to INCENP; when associated
FT with Y-46."
FT /evidence="ECO:0000269|PubMed:17956729"
FT MUTAGEN 46
FT /note="L->Y: Loss of binding to INCENP; when associated
FT with E-35."
FT /evidence="ECO:0000269|PubMed:17956729"
FT MUTAGEN 70
FT /note="W->E: Loss of binding to BIRC5; when associated with
FT E-74."
FT /evidence="ECO:0000269|PubMed:17956729"
FT MUTAGEN 74
FT /note="F->E: Loss of binding to BIRC5; when associated with
FT E-70."
FT /evidence="ECO:0000269|PubMed:17956729"
FT MUTAGEN 88
FT /note="T->A: Decrease in AURKB activity and almost no
FT phosphorylation by TTK; when associated with A-94; A-169
FT and A-230."
FT /evidence="ECO:0000269|PubMed:19530738"
FT MUTAGEN 94
FT /note="T->A: Decrease in AURKB activity and almost no
FT phosphorylation by TTK; when associated with A-88; A-169
FT and A-230."
FT /evidence="ECO:0000269|PubMed:19530738"
FT MUTAGEN 106
FT /note="T->A: Decreases interaction with SOG1 and SOG2,
FT abolishes localization to centromeres in prometaphase; when
FT associated with A-171, A-185, A-189, A-199, A-204 and A-
FT 219."
FT /evidence="ECO:0000269|PubMed:20739936"
FT MUTAGEN 165
FT /note="S->A: Results in reduction but not abolition of
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:15249581"
FT MUTAGEN 169
FT /note="T->A: Decrease in AURKB activity and almost no
FT phosphorylation by TTK; when associated with A-88; A-94 and
FT A-230."
FT /evidence="ECO:0000269|PubMed:19530738"
FT MUTAGEN 171
FT /note="T->A: Decreases interaction with SOG1 and SOG2,
FT abolishes localization to centromeres in prometaphase; when
FT associated with A-106, A-185, A-189, A-199, A-204 and A-
FT 219."
FT /evidence="ECO:0000269|PubMed:20739936"
FT MUTAGEN 185
FT /note="T->A: Decreases interaction with SOG1 and SOG2,
FT abolishes localization to centromeres in prometaphase; when
FT associated with A-106, A-171, A-189, A-199, A-204 and A-
FT 219."
FT /evidence="ECO:0000269|PubMed:20739936"
FT MUTAGEN 189
FT /note="T->A: Decreases interaction with SOG1 and SOG2,
FT abolishes localization to centromeres in prometaphase; when
FT associated with A-106, A-171, A-185, A-199, A-204 and A-
FT 219."
FT /evidence="ECO:0000269|PubMed:20739936"
FT MUTAGEN 199
FT /note="T->A: Decreases interaction with SOG1 and SOG2,
FT abolishes localization to centromeres in prometaphase; when
FT associated with A-106, A-171, A-185, A-189, A-204, A-219."
FT /evidence="ECO:0000269|PubMed:20739936"
FT MUTAGEN 204
FT /note="T->A: Decreases interaction with SOG1 and SOG2,
FT abolishes localization to centromeres in prometaphase; when
FT associated with A-106, A-171, A-185, A-189, A-199 and A-
FT 219."
FT /evidence="ECO:0000269|PubMed:20739936"
FT MUTAGEN 219
FT /note="S->A: Decreases interaction with SOG1 and SOG2,
FT abolishes localization to centromeres in prometaphase; when
FT associated with A-106, A-171, A-185, A-189, A-199 and A-
FT 204."
FT /evidence="ECO:0000269|PubMed:20739936"
FT MUTAGEN 219
FT /note="S->D,K: No effect on the structure."
FT MUTAGEN 230
FT /note="T->A: Decrease in AURKB activity and dimer
FT disruption. Decrease in AURKB activity and almost no
FT phosphorylation by TTK; when associated with A-88; A-94 and
FT A-230."
FT /evidence="ECO:0000269|PubMed:19530738"
FT MUTAGEN 230
FT /note="T->D,K: Substantial loss of structure."
FT /evidence="ECO:0000269|PubMed:19530738"
FT MUTAGEN 230
FT /note="T->V: Decrease in AURKB activity and no effect on
FT the structure."
FT /evidence="ECO:0000269|PubMed:19530738"
FT CONFLICT 155
FT /note="I -> M (in Ref. 4; BAD96288)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="N -> D (in Ref. 4; BAD96269)"
FT /evidence="ECO:0000305"
FT HELIX 16..60
FT /evidence="ECO:0007829|PDB:2QFA"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:2QFA"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:2QFA"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:2KDD"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:2KDD"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:2KDD"
FT HELIX 256..275
FT /evidence="ECO:0007829|PDB:2KDD"
SQ SEQUENCE 280 AA; 31323 MW; 519978A7C295C571 CRC64;
MAPRKGSSRV AKTNSLRRRK LASFLKDFDR EVEIRIKQIE SDRQNLLKEV DNLYNIEILR
LPKALREMNW LDYFALGGNK QALEEAATAD LDITEINKLT AEAIQTPLKS AKTRKVIQVD
EMIVEEEEEE ENERKNLQTA RVKRCPPSKK RTQSIQGKGK GKRSSRANTV TPAVGRLEVS
MVKPTPGLTP RFDSRVFKTP GLRTPAAGER IYNISGNGSP LADSKEIFLT VPVGGGESLR
LLASDLQRHS IAQLDPEALG NIKKLSNRLA QICSSIRTHK
