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Borealin (Cell division cycle-associated protein 8) (Dasra-B) (hDasra-B) (Pluripotent embryonic stem cell-related gene 3 protein)

 BOREA_HUMAN             Reviewed;         280 AA.
Q53HL2; D3DPT4; Q53HN1; Q96AM3; Q9NVW5;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
25-JUL-2006, sequence version 2.
25-OCT-2017, entry version 122.
RecName: Full=Borealin;
AltName: Full=Cell division cycle-associated protein 8;
AltName: Full=Dasra-B;
Short=hDasra-B;
AltName: Full=Pluripotent embryonic stem cell-related gene 3 protein;
Name=CDCA8; Synonyms=PESCRG3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12188893; DOI=10.2174/1568009013334241;
Walker M.G.;
"Drug target discovery by gene expression analysis: cell cycle
genes.";
Curr. Cancer Drug Targets 1:73-83(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Nie Z., Du J., Lin G., Lu G.;
"The cloning and functional analysis of HPESCRG3.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Coronary arterial endothelium;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-12.
TISSUE=Colon, Kidney, and 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).
[7]
FUNCTION, AND COMPONENT OF THE CPC COMPLEX.
PubMed=15260989; DOI=10.1016/j.cell.2004.06.026;
Sampath S.C., Ohi R., Leismann O., Salic A., Pozniakovski A.,
Funabiki H.;
"The chromosomal passenger complex is required for chromatin-induced
microtubule stabilization and spindle assembly.";
Cell 118:187-202(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE CPC COMPLEX,
PHOSPHORYLATION AT SER-165, AND MUTAGENESIS OF SER-165.
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).
[9]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15561729; DOI=10.1074/mcp.M400158-MCP200;
Sauer G., Koerner R., Hanisch A., Ries A., Nigg E.A., Sillje H.H.W.;
"Proteome analysis of the human mitotic spindle.";
Mol. Cell. Proteomics 4:35-43(2005).
[10]
INTERACTION WITH BIRC5.
PubMed=16239925; DOI=10.1038/sj.embor.7400562;
Vader G., Kauw J.J.W., Medema R.H., Lens S.M.A.;
"Survivin mediates targeting of the chromosomal passenger complex to
the centromere and midbody.";
EMBO Rep. 7:85-92(2006).
[11]
SUBCELLULAR LOCATION, INTERACTION WITH BIRC5, AND DEVELOPMENTAL STAGE.
PubMed=16427043; DOI=10.1016/j.yexcr.2005.12.015;
Chang J.-L., Chen T.-H., Wang C.-F., Chiang Y.-H., Huang Y.-L.,
Wong F.-H., Chou C.-K., Chen C.-M.;
"Borealin/Dasra B is a cell cycle-regulated chromosomal passenger
protein and its nuclear accumulation is linked to poor prognosis for
human gastric cancer.";
Exp. Cell Res. 312:962-973(2006).
[12]
INTERACTION WITH BIRC5.
PubMed=16291752; DOI=10.1074/jbc.M508773200;
Noton E.A., Colnaghi R., Tate S., Starck C., Carvalho A.,
Ko Ferrigno P., Wheatley S.P.;
"Molecular analysis of survivin isoforms: evidence that alternatively
spliced variants do not play a role in mitosis.";
J. Biol. Chem. 281:1286-1295(2006).
[13]
SUBCELLULAR LOCATION, AND INTERACTION WITH BIRC5.
PubMed=16436504; DOI=10.1091/mbc.E05-08-0727;
Lens S.M.A., Rodriguez J.A., Vader G., Span S.W., Giaccone G.,
Medema R.H.;
"Uncoupling the central spindle-associated function of the chromosomal
passenger complex from its role at centromeres.";
Mol. Biol. Cell 17:1897-1909(2006).
[14]
FUNCTION.
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]
SUBCELLULAR LOCATION.
PubMed=16547492; DOI=10.1038/sj.onc.1209499;
Rodriguez J.A., Lens S.M.A., Span S.W., Vader G., Medema R.H.,
Kruyt F.A.E., Giaccone G.;
"Subcellular localization and nucleocytoplasmic transport of the
chromosomal passenger proteins before nuclear envelope breakdown.";
Oncogene 25:4867-4879(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; SER-110; THR-189;
THR-204; SER-219 AND SER-244, 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]
INTERACTION WITH BIRC5.
PubMed=18591255; DOI=10.1128/MCB.02039-07;
Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.;
"A survivin-ran complex regulates spindle formation in tumor cells.";
Mol. Cell. Biol. 28:5299-5311(2008).
[18]
PHOSPHORYLATION BY TTK, AND FUNCTION.
PubMed=18243099; DOI=10.1016/j.cell.2007.11.046;
Jelluma N., Brenkman A.B., van den Broek N.J., Cruijsen C.W.A.,
van Osch M.H.J., Lens S.M.A., Medema R.H., Kops G.J.P.L.;
"Mps1 phosphorylates Borealin to control Aurora B activity and
chromosome alignment.";
Cell 132:233-246(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; THR-189; THR-204
AND SER-219, 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).
[20]
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).
[21]
INTERACTION WITH SENP3; UBE2I AND RANBP2, SUMOYLATION, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LYS-26.
PubMed=18946085; DOI=10.1091/mbc.E08-05-0511;
Klein U.R., Haindl M., Nigg E.A., Muller S.;
"RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-
deconjugation cycle on Borealin.";
Mol. Biol. Cell 20:410-418(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219 AND SER-224, 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106 AND SER-219, 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).
[24]
INTERACTION WITH SGO1 AND SGO2, SUBCELLULAR LOCATION, MUTAGENESIS OF
THR-106; THR-171; THR-185; THR-189; THR-199; THR-204 AND SER-219, AND
PHOSPHORYLATION.
PubMed=20739936; DOI=10.1038/nature09390;
Tsukahara T., Tanno Y., Watanabe Y.;
"Phosphorylation of the CPC by Cdk1 promotes chromosome bi-
orientation.";
Nature 467:719-723(2010).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189 AND SER-219, 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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, 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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; THR-189; THR-204
AND SER-219, 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).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-135, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[29]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 15-76, INTERACTION WITH BIRC5
AND INCENP, AND MUTAGENESIS OF ARG-17; ARG-19; LYS-20; ARG-35; LEU-46;
TRP-70 AND PHE-74.
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).
[30]
STRUCTURE BY NMR OF 207-280, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF
20-78, OLIGOMERIZATION, PHOSPHORYLATION AT THR-88; THR-94; THR-169;
THR-230 AND SER-238, AND MUTAGENESIS OF THR-88; THR-94; THR-169 AND
THR-230.
PubMed=19530738; DOI=10.1021/bi900530v;
Bourhis E., Lingel A., Phung Q., Fairbrother W.J., Cochran A.G.;
"Phosphorylation of a borealin dimerization domain is required for
proper chromosome segregation.";
Biochemistry 48:6783-6793(2009).
-!- 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.
Major effector of the TTK kinase in the control of attachment-
error-correction and chromosome alignment.
{ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:15260989,
ECO:0000269|PubMed:16571674, ECO:0000269|PubMed:18243099}.
-!- SUBUNIT: May form homooligomers and homodimers. Component of the
chromosomal passenger complex (CPC) composed of at least
BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the
complex forms a triple-helix bundle-based subcomplex with INCENP
and BIRC5 (PubMed:17956729). Interacts with SENP3, UBE2I and
RANBP2. Interacts (phosphorylated) with SGO1 and SGO2; the
association is dependent on CDK1. {ECO:0000269|PubMed:15249581,
ECO:0000269|PubMed:16239925, ECO:0000269|PubMed:16291752,
ECO:0000269|PubMed:16427043, ECO:0000269|PubMed:16436504,
ECO:0000269|PubMed:17956729, ECO:0000269|PubMed:18591255,
ECO:0000269|PubMed:18946085, ECO:0000269|PubMed:20739936}.
-!- INTERACTION:
Q96GD4:AURKB; NbExp=8; IntAct=EBI-979174, EBI-624291;
E7CU85:BIRC5; NbExp=2; IntAct=EBI-979174, EBI-10488580;
O15392:BIRC5; NbExp=18; IntAct=EBI-979174, EBI-518823;
O15392-1:BIRC5; NbExp=2; IntAct=EBI-979174, EBI-518838;
O15392-2:BIRC5; NbExp=2; IntAct=EBI-979174, EBI-518842;
Q86XJ1:GAS2L3; NbExp=2; IntAct=EBI-979174, EBI-9248152;
Q9NQS7:INCENP; NbExp=5; IntAct=EBI-979174, EBI-307907;
Q5FBB7:SGO1; NbExp=3; IntAct=EBI-979174, EBI-989069;
Q562F6:SGO2; NbExp=3; IntAct=EBI-979174, EBI-989213;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:18946085}. Cytoplasm
{ECO:0000269|PubMed:18946085}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:15561729}. Chromosome, centromere
{ECO:0000269|PubMed:20739936}. Note=Localizes on chromosome arms
and inner centromeres from prophase through metaphase and then
transferring to the spindle midzone and midbody from anaphase
through cytokinesis. Colocalizes with SENP3 in the nucleolus in
interphase cells. {ECO:0000269|PubMed:18946085}.
-!- DEVELOPMENTAL STAGE: Cell-cycle regulated. Increases during G2/M
phase and then reduces after exit from M phase.
{ECO:0000269|PubMed:16427043}.
-!- DOMAIN: The C-terminal region (aa 207-280) represents the
dimerization motif.
-!- PTM: Phosphorylated by TTK, essentially at Thr-88, Thr94, Thr-169
and Thr-230. Phosphorylation (probably by CDK1) promotes targeting
of the CPC to centromeric DNA. {ECO:0000269|PubMed:15249581,
ECO:0000269|PubMed:18243099, ECO:0000269|PubMed:19530738}.
-!- PTM: Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through
the removal of SUMO2 and SUMO3. {ECO:0000269|PubMed:18946085}.
-!- MISCELLANEOUS: Cells lacking CDCA8 display a slight decrease in
histone H3 'Ser-10' phosphorylation, suggesting that the CPC
complex mediates phosphorylation of 'Ser-10' of histone H3.
-!- SIMILARITY: Belongs to the borealin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BG354581; Type=Frameshift; Positions=123, 200; Evidence={ECO:0000305};
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EMBL; BG354581; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY508815; AAR91699.1; -; mRNA.
EMBL; AK001330; BAA91629.1; -; mRNA.
EMBL; AK022104; BAB13961.1; -; mRNA.
EMBL; AK022606; BAB14125.1; -; mRNA.
EMBL; AK222549; BAD96269.1; -; mRNA.
EMBL; AK222568; BAD96288.1; -; mRNA.
EMBL; CH471059; EAX07324.1; -; Genomic_DNA.
EMBL; CH471059; EAX07325.1; -; Genomic_DNA.
EMBL; BC000703; AAH00703.1; -; mRNA.
EMBL; BC001651; AAH01651.1; -; mRNA.
EMBL; BC016944; AAH16944.1; -; mRNA.
EMBL; BC008079; AAH08079.1; -; mRNA.
CCDS; CCDS424.1; -.
RefSeq; NP_001243804.1; NM_001256875.1.
RefSeq; NP_060571.1; NM_018101.3.
UniGene; Hs.524571; -.
PDB; 2KDD; NMR; -; A/B=207-280.
PDB; 2QFA; X-ray; 1.40 A; B=15-76.
PDB; 2RAW; X-ray; 2.40 A; B=20-78.
PDB; 2RAX; X-ray; 3.30 A; B/F/Y=20-78.
PDBsum; 2KDD; -.
PDBsum; 2QFA; -.
PDBsum; 2RAW; -.
PDBsum; 2RAX; -.
ProteinModelPortal; Q53HL2; -.
SMR; Q53HL2; -.
BioGrid; 120446; 56.
CORUM; Q53HL2; -.
DIP; DIP-37995N; -.
IntAct; Q53HL2; 22.
MINT; MINT-4509527; -.
STRING; 9606.ENSP00000316121; -.
iPTMnet; Q53HL2; -.
PhosphoSitePlus; Q53HL2; -.
BioMuta; CDCA8; -.
DMDM; 110832774; -.
EPD; Q53HL2; -.
MaxQB; Q53HL2; -.
PaxDb; Q53HL2; -.
PeptideAtlas; Q53HL2; -.
PRIDE; Q53HL2; -.
DNASU; 55143; -.
Ensembl; ENST00000327331; ENSP00000316121; ENSG00000134690.
Ensembl; ENST00000373055; ENSP00000362146; ENSG00000134690.
GeneID; 55143; -.
KEGG; hsa:55143; -.
UCSC; uc001cbr.5; human.
CTD; 55143; -.
DisGeNET; 55143; -.
EuPathDB; HostDB:ENSG00000134690.10; -.
GeneCards; CDCA8; -.
HGNC; HGNC:14629; CDCA8.
HPA; CAB040294; -.
HPA; HPA028120; -.
HPA; HPA028258; -.
HPA; HPA028783; -.
MIM; 609977; gene.
neXtProt; NX_Q53HL2; -.
OpenTargets; ENSG00000134690; -.
PharmGKB; PA26281; -.
eggNOG; ENOG410IICJ; Eukaryota.
eggNOG; ENOG4111N8R; LUCA.
GeneTree; ENSGT00390000011115; -.
HOGENOM; HOG000261628; -.
HOVERGEN; HBG080103; -.
InParanoid; Q53HL2; -.
KO; K11514; -.
OMA; QIESDRQ; -.
OrthoDB; EOG091G167R; -.
PhylomeDB; Q53HL2; -.
TreeFam; TF101077; -.
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; Q53HL2; -.
ChiTaRS; CDCA8; human.
EvolutionaryTrace; Q53HL2; -.
GeneWiki; CDCA8; -.
GenomeRNAi; 55143; -.
PRO; PR:Q53HL2; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134690; -.
CleanEx; HS_CDCA8; -.
Genevisible; Q53HL2; HS.
GO; GO:0010369; C:chromocenter; IEA:Ensembl.
GO; GO:0032133; C:chromosome passenger complex; IPI:UniProtKB.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0045171; C:intercellular bridge; IDA:HPA.
GO; GO:0030496; C:midbody; IDA:FlyBase.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0051276; P:chromosome organization; IMP:UniProtKB.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
InterPro; IPR018851; Borealin_N.
InterPro; IPR018867; Cell_div_borealin.
Pfam; PF10512; Borealin; 1.
Pfam; PF10444; Nbl1_Borealin_N; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
Complete proteome; Cytoplasm; Cytoskeleton; Isopeptide bond; Mitosis;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Ubl conjugation.
CHAIN 1 280 Borealin.
/FTId=PRO_0000247075.
REGION 1 140 Required for interaction with SENP3.
{ECO:0000269|PubMed:18946085}.
REGION 1 88 Required for centromere localization.
REGION 1 58 Required for interaction with INCENP.
{ECO:0000269|PubMed:17956729}.
REGION 10 109 Required to form a minimal CPC core
complex that localizes to the central
spindle and midbody and properly executes
the role of the CPC during cytokinesis.
REGION 20 78 Required for interaction with INCENP and
BIRC5. {ECO:0000269|PubMed:17956729}.
COMPBIAS 125 133 Poly-Glu.
MOD_RES 88 88 Phosphothreonine; by TTK.
{ECO:0000269|PubMed:19530738}.
MOD_RES 94 94 Phosphothreonine; by TTK.
{ECO:0000269|PubMed:19530738}.
MOD_RES 106 106 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 165 165 Phosphoserine; by AURKB.
{ECO:0000269|PubMed:15249581}.
MOD_RES 169 169 Phosphothreonine; by TTK.
{ECO:0000269|PubMed:19530738}.
MOD_RES 189 189 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 204 204 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 230 230 Phosphothreonine; by TTK.
{ECO:0000269|PubMed:19530738}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000269|PubMed:19530738}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
CROSSLNK 135 135 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 12 12 K -> N (in dbSNP:rs17851453).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_027063.
MUTAGEN 17 17 R->E: Loss of localization to the central
spindle and midbody in anaphase or
cytokinesis; when associated with E-19
and E-20. {ECO:0000269|PubMed:17956729}.
MUTAGEN 19 19 R->E: Loss of localization to the central
spindle and midbody in anaphase or
cytokinesis; when associated with E-17
and E-20. {ECO:0000269|PubMed:17956729}.
MUTAGEN 20 20 K->E: Loss of localization to the central
spindle and midbody in anaphase or
cytokinesis; when associated with E-17
and E-19. {ECO:0000269|PubMed:17956729}.
MUTAGEN 26 26 K->R: Fails to exhibit normal
localization to the nucleolus in
interphase depleted cells.
{ECO:0000269|PubMed:18946085}.
MUTAGEN 35 35 R->E: Loss of binding to INCENP; when
associated with Y-46.
{ECO:0000269|PubMed:17956729}.
MUTAGEN 46 46 L->Y: Loss of binding to INCENP; when
associated with E-35.
{ECO:0000269|PubMed:17956729}.
MUTAGEN 70 70 W->E: Loss of binding to BIRC5; when
associated with E-74.
{ECO:0000269|PubMed:17956729}.
MUTAGEN 74 74 F->E: Loss of binding to BIRC5; when
associated with E-70.
{ECO:0000269|PubMed:17956729}.
MUTAGEN 88 88 T->A: Decrease in AURKB activity and
almost no phosphorylation by TTK; when
associated with A-94; A-169 and A-230.
{ECO:0000269|PubMed:19530738}.
MUTAGEN 94 94 T->A: Decrease in AURKB activity and
almost no phosphorylation by TTK; when
associated with A-88; A-169 and A-230.
{ECO:0000269|PubMed:19530738}.
MUTAGEN 106 106 T->A: Decreases interaction with SOG1 and
SOG2, abolishes localization to
centromeres in prometaphase; when
associated with A-171, A-185, A-189, A-
199, A-204 and A-219.
{ECO:0000269|PubMed:20739936}.
MUTAGEN 165 165 S->A: Results in reduction but not
abolition of phosphorylation.
{ECO:0000269|PubMed:15249581}.
MUTAGEN 169 169 T->A: Decrease in AURKB activity and
almost no phosphorylation by TTK; when
associated with A-88; A-94 and A-230.
{ECO:0000269|PubMed:19530738}.
MUTAGEN 171 171 T->A: Decreases interaction with SOG1 and
SOG2, abolishes localization to
centromeres in prometaphase; when
associated with A-106, A-185, A-189, A-
199, A-204 and A-219.
{ECO:0000269|PubMed:20739936}.
MUTAGEN 185 185 T->A: Decreases interaction with SOG1 and
SOG2, abolishes localization to
centromeres in prometaphase; when
associated with A-106, A-171, A-189, A-
199, A-204 and A-219.
{ECO:0000269|PubMed:20739936}.
MUTAGEN 189 189 T->A: Decreases interaction with SOG1 and
SOG2, abolishes localization to
centromeres in prometaphase; when
associated with A-106, A-171, A-185, A-
199, A-204 and A-219.
{ECO:0000269|PubMed:20739936}.
MUTAGEN 199 199 T->A: Decreases interaction with SOG1 and
SOG2, abolishes localization to
centromeres in prometaphase; when
associated with A-106, A-171, A-185, A-
189, A-204, A-219.
{ECO:0000269|PubMed:20739936}.
MUTAGEN 204 204 T->A: Decreases interaction with SOG1 and
SOG2, abolishes localization to
centromeres in prometaphase; when
associated with A-106, A-171, A-185, A-
189, A-199 and A-219.
{ECO:0000269|PubMed:20739936}.
MUTAGEN 219 219 S->A: Decreases interaction with SOG1 and
SOG2, abolishes localization to
centromeres in prometaphase; when
associated with A-106, A-171, A-185, A-
189, A-199 and A-204.
{ECO:0000269|PubMed:20739936}.
MUTAGEN 219 219 S->D,K: No effect on the structure.
MUTAGEN 230 230 T->A: Decrease in AURKB activity and
dimer disruption. Decrease in AURKB
activity and almost no phosphorylation by
TTK; when associated with A-88; A-94 and
A-230. {ECO:0000269|PubMed:19530738}.
MUTAGEN 230 230 T->D,K: Substantial loss of structure.
{ECO:0000269|PubMed:19530738}.
MUTAGEN 230 230 T->V: Decrease in AURKB activity and no
effect on the structure.
{ECO:0000269|PubMed:19530738}.
CONFLICT 155 155 I -> M (in Ref. 4; BAD96288).
{ECO:0000305}.
CONFLICT 213 213 N -> D (in Ref. 4; BAD96269).
{ECO:0000305}.
HELIX 16 60 {ECO:0000244|PDB:2QFA}.
HELIX 63 66 {ECO:0000244|PDB:2QFA}.
HELIX 70 75 {ECO:0000244|PDB:2QFA}.
STRAND 233 237 {ECO:0000244|PDB:2KDD}.
TURN 243 245 {ECO:0000244|PDB:2KDD}.
HELIX 248 252 {ECO:0000244|PDB:2KDD}.
HELIX 256 275 {ECO:0000244|PDB:2KDD}.
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


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