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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.
02-JUN-2021, entry version 147.
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:
Q53HL2; Q96GD4: AURKB; NbExp=9; IntAct=EBI-979174, EBI-624291;
Q53HL2; E7CU85: BIRC5; NbExp=2; IntAct=EBI-979174, EBI-10488580;
Q53HL2; O15392: BIRC5; NbExp=19; IntAct=EBI-979174, EBI-518823;
Q53HL2; O15392-1: BIRC5; NbExp=2; IntAct=EBI-979174, EBI-518838;
Q53HL2; O15392-2: BIRC5; NbExp=2; IntAct=EBI-979174, EBI-518842;
Q53HL2; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-979174, EBI-11748557;
Q53HL2; Q96EF6: FBXO17; NbExp=3; IntAct=EBI-979174, EBI-2510157;
Q53HL2; Q86XJ1: GAS2L3; NbExp=2; IntAct=EBI-979174, EBI-9248152;
Q53HL2; P13807: GYS1; NbExp=3; IntAct=EBI-979174, EBI-740553;
Q53HL2; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-979174, EBI-2549423;
Q53HL2; Q9NQS7: INCENP; NbExp=5; IntAct=EBI-979174, EBI-307907;
Q53HL2; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-979174, EBI-3920396;
Q53HL2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-979174, EBI-741158;
Q53HL2; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-979174, EBI-10232538;
Q53HL2; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-979174, EBI-747925;
Q53HL2; Q01105-2: SET; NbExp=3; IntAct=EBI-979174, EBI-7481343;
Q53HL2; Q5FBB7: SGO1; NbExp=3; IntAct=EBI-979174, EBI-989069;
Q53HL2; Q562F6: SGO2; NbExp=3; IntAct=EBI-979174, EBI-989213;
Q53HL2; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-979174, EBI-12004298;
Q53HL2; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-979174, EBI-12023934;
Q53HL2; G5E9M4: ZNF277; NbExp=3; IntAct=EBI-979174, EBI-11995620;
-!- 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; 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.
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.
PDB; 6YIE; X-ray; 3.49 A; B/E=10-109.
PDB; 6YIF; X-ray; 1.81 A; B=10-76.
PDB; 6YIH; X-ray; 2.55 A; B=10-76.
PDBsum; 2KDD; -.
PDBsum; 2QFA; -.
PDBsum; 2RAW; -.
PDBsum; 2RAX; -.
PDBsum; 6YIE; -.
PDBsum; 6YIF; -.
PDBsum; 6YIH; -.
BMRB; Q53HL2; -.
SMR; Q53HL2; -.
BioGRID; 120446; 91.
ComplexPortal; CPX-116; Chromosomal passenger complex.
CORUM; Q53HL2; -.
DIP; DIP-37995N; -.
IntAct; Q53HL2; 55.
MINT; Q53HL2; -.
STRING; 9606.ENSP00000362146; -.
iPTMnet; Q53HL2; -.
PhosphoSitePlus; Q53HL2; -.
BioMuta; CDCA8; -.
DMDM; 110832774; -.
EPD; Q53HL2; -.
jPOST; Q53HL2; -.
MassIVE; Q53HL2; -.
MaxQB; Q53HL2; -.
PaxDb; Q53HL2; -.
PeptideAtlas; Q53HL2; -.
PRIDE; Q53HL2; -.
ProteomicsDB; 62507; -.
Antibodypedia; 31756; 463 antibodies.
CPTC; Q53HL2; 1 antibody.
DNASU; 55143; -.
Ensembl; ENST00000327331; ENSP00000316121; ENSG00000134690.
Ensembl; ENST00000373055; ENSP00000362146; ENSG00000134690.
GeneID; 55143; -.
KEGG; hsa:55143; -.
UCSC; uc001cbr.5; human.
CTD; 55143; -.
DisGeNET; 55143; -.
GeneCards; CDCA8; -.
HGNC; HGNC:14629; CDCA8.
HPA; ENSG00000134690; Group enriched (bone marrow, lymphoid tissue, testis).
MIM; 609977; gene.
neXtProt; NX_Q53HL2; -.
OpenTargets; ENSG00000134690; -.
PharmGKB; PA26281; -.
VEuPathDB; HostDB:ENSG00000134690.10; -.
eggNOG; ENOG502QS4S; Eukaryota.
GeneTree; ENSGT00390000011115; -.
HOGENOM; CLU_074128_0_0_1; -.
InParanoid; Q53HL2; -.
OMA; PLITPKF; -.
OrthoDB; 1587028at2759; -.
PhylomeDB; Q53HL2; -.
TreeFam; TF101077; -.
PathwayCommons; Q53HL2; -.
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.
Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
SIGNOR; Q53HL2; -.
BioGRID-ORCS; 55143; 672 hits in 1009 CRISPR screens.
ChiTaRS; CDCA8; human.
EvolutionaryTrace; Q53HL2; -.
GeneWiki; CDCA8; -.
GenomeRNAi; 55143; -.
Pharos; Q53HL2; Tbio.
PRO; PR:Q53HL2; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; Q53HL2; protein.
Bgee; ENSG00000134690; Expressed in oocyte and 146 other tissues.
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:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0032991; C:protein-containing 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:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
GO; GO:0007052; P:mitotic spindle organization; TAS:Reactome.
IDEAL; IID00215; -.
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; Cytoplasm;
Cytoskeleton; Isopeptide bond; Mitosis; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1..280
/note="Borealin"
/id="PRO_0000247075"
REGION 1..140
/note="Required for interaction with SENP3"
/evidence="ECO:0000269|PubMed:18946085"
REGION 1..88
/note="Required for centromere localization"
REGION 1..58
/note="Required for interaction with INCENP"
/evidence="ECO:0000269|PubMed:17956729"
REGION 10..109
/note="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
/note="Required for interaction with INCENP and BIRC5"
/evidence="ECO:0000269|PubMed:17956729"
REGION 130..169
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 149..169
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 88
/note="Phosphothreonine; by TTK"
/evidence="ECO:0000269|PubMed:19530738"
MOD_RES 94
/note="Phosphothreonine; by TTK"
/evidence="ECO:0000269|PubMed:19530738"
MOD_RES 106
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
ECO:0007744|PubMed:23186163"
MOD_RES 110
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18691976"
MOD_RES 165
/note="Phosphoserine; by AURKB"
/evidence="ECO:0000269|PubMed:15249581"
MOD_RES 169
/note="Phosphothreonine; by TTK"
/evidence="ECO:0000269|PubMed:19530738"
MOD_RES 189
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163"
MOD_RES 204
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163"
MOD_RES 219
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 224
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19369195"
MOD_RES 230
/note="Phosphothreonine; by TTK"
/evidence="ECO:0000269|PubMed:19530738"
MOD_RES 238
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:19530738"
MOD_RES 244
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18691976"
CROSSLNK 135
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
VARIANT 12
/note="K -> N (in dbSNP:rs17851453)"
/evidence="ECO:0000269|PubMed:15489334"
/id="VAR_027063"
MUTAGEN 17
/note="R->E: Loss of localization to the central spindle
and midbody in anaphase or cytokinesis; when associated
with E-19 and E-20."
/evidence="ECO:0000269|PubMed:17956729"
MUTAGEN 19
/note="R->E: Loss of localization to the central spindle
and midbody in anaphase or cytokinesis; when associated
with E-17 and E-20."
/evidence="ECO:0000269|PubMed:17956729"
MUTAGEN 20
/note="K->E: Loss of localization to the central spindle
and midbody in anaphase or cytokinesis; when associated
with E-17 and E-19."
/evidence="ECO:0000269|PubMed:17956729"
MUTAGEN 26
/note="K->R: Fails to exhibit normal localization to the
nucleolus in interphase depleted cells."
/evidence="ECO:0000269|PubMed:18946085"
MUTAGEN 35
/note="R->E: Loss of binding to INCENP; when associated
with Y-46."
/evidence="ECO:0000269|PubMed:17956729"
MUTAGEN 46
/note="L->Y: Loss of binding to INCENP; when associated
with E-35."
/evidence="ECO:0000269|PubMed:17956729"
MUTAGEN 70
/note="W->E: Loss of binding to BIRC5; when associated with
E-74."
/evidence="ECO:0000269|PubMed:17956729"
MUTAGEN 74
/note="F->E: Loss of binding to BIRC5; when associated with
E-70."
/evidence="ECO:0000269|PubMed:17956729"
MUTAGEN 88
/note="T->A: Decrease in AURKB activity and almost no
phosphorylation by TTK; when associated with A-94; A-169
and A-230."
/evidence="ECO:0000269|PubMed:19530738"
MUTAGEN 94
/note="T->A: Decrease in AURKB activity and almost no
phosphorylation by TTK; when associated with A-88; A-169
and A-230."
/evidence="ECO:0000269|PubMed:19530738"
MUTAGEN 106
/note="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."
/evidence="ECO:0000269|PubMed:20739936"
MUTAGEN 165
/note="S->A: Results in reduction but not abolition of
phosphorylation."
/evidence="ECO:0000269|PubMed:15249581"
MUTAGEN 169
/note="T->A: Decrease in AURKB activity and almost no
phosphorylation by TTK; when associated with A-88; A-94 and
A-230."
/evidence="ECO:0000269|PubMed:19530738"
MUTAGEN 171
/note="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."
/evidence="ECO:0000269|PubMed:20739936"
MUTAGEN 185
/note="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."
/evidence="ECO:0000269|PubMed:20739936"
MUTAGEN 189
/note="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."
/evidence="ECO:0000269|PubMed:20739936"
MUTAGEN 199
/note="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."
/evidence="ECO:0000269|PubMed:20739936"
MUTAGEN 204
/note="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."
/evidence="ECO:0000269|PubMed:20739936"
MUTAGEN 219
/note="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."
/evidence="ECO:0000269|PubMed:20739936"
MUTAGEN 219
/note="S->D,K: No effect on the structure."
MUTAGEN 230
/note="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."
/evidence="ECO:0000269|PubMed:19530738"
MUTAGEN 230
/note="T->D,K: Substantial loss of structure."
/evidence="ECO:0000269|PubMed:19530738"
MUTAGEN 230
/note="T->V: Decrease in AURKB activity and no effect on
the structure."
/evidence="ECO:0000269|PubMed:19530738"
CONFLICT 155
/note="I -> M (in Ref. 4; BAD96288)"
/evidence="ECO:0000305"
CONFLICT 213
/note="N -> D (in Ref. 4; BAD96269)"
/evidence="ECO:0000305"
HELIX 16..60
/evidence="ECO:0007829|PDB:2QFA"
HELIX 63..66
/evidence="ECO:0007829|PDB:2QFA"
HELIX 70..75
/evidence="ECO:0007829|PDB:2QFA"
STRAND 233..237
/evidence="ECO:0007829|PDB:2KDD"
TURN 243..245
/evidence="ECO:0007829|PDB:2KDD"
HELIX 248..252
/evidence="ECO:0007829|PDB:2KDD"
HELIX 256..275
/evidence="ECO:0007829|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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[CDCA8 PESCRG3] Borealin (Cell division cycle-associated protein 8) (Dasra-B) (hDasra-B) (Pluripotent embryonic stem cell-related gene 3 protein)
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[CDK13 CDC2L CDC2L5 CHED KIAA1791] Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller)
[CDK11B CDC2L1 CDK11 PITSLREA PK58] Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)
[Epop E13] Elongin BC and Polycomb repressive complex 2-associated protein (Embryonic stem cell-specific PRC2 subunit p48) (ES cell-specific PRC2 subunit p48) (esPRC2p48)
[Cdk11b Cdc2l1 Cdk11] Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1)
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[cdc-48.1 C06A1.1] Transitional endoplasmic reticulum ATPase homolog 1 (EC 3.6.4.6) (Cell division cycle-related protein 48.1) (p97/CDC48 homolog 1)
[RPRD1B C20orf77 CREPT] Regulation of nuclear pre-mRNA domain-containing protein 1B (Cell cycle-related and expression-elevated protein in tumor)
[mat-3 apc-8 cdc-23 pod-4 vex-2 F10C5.1] Cell division cycle protein 23 homolog (Anaphase-promoting complex subunit 8) (APC8) (Metaphase-to-anaphase transition defect protein 3)
[VPS4B SKD1 VPS42 MIG1] Vacuolar protein sorting-associated protein 4B (EC 3.6.4.6) (Cell migration-inducing gene 1 protein) (Suppressor of K(+) transport growth defect 1) (Protein SKD1)
[Hmces Srap1 Srapd1] Abasic site processing protein HMCES (Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein) (ES cell-specific 5hmC-binding protein) (Peptidase HMCES) (EC 3.4.-.-) (SRAP domain-containing protein 1)
[CDK9 CDC2L4 TAK] Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)
[cdc-48.3 K04G2.3] ATPase family protein 2 homolog (EC 3.6.4.10) (Cell division cycle-related protein 48.3)
[cdc-14 C17G10.4] Tyrosine-protein phosphatase cdc-14 (EC 3.1.3.48) (Cell division cycle-related protein 14)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CCAR1 CARP1 DIS] Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1) (Death inducer with SAP domain)
[CDC7 CDC7L1] Cell division cycle 7-related protein kinase (CDC7-related kinase) (HsCdc7) (huCdc7) (EC 2.7.11.1)
[Esrrb Err-2 Err2 Nr3b2] Steroid hormone receptor ERR2 (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)
[HMCES C3orf37 DC12 SRAPD1] Abasic site processing protein HMCES (Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein) (ES cell-specific 5hmC-binding protein) (Peptidase HMCES) (EC 3.4.-.-) (SRAP domain-containing protein 1)
[TAL1 BHLHA17 SCL TCL5] T-cell acute lymphocytic leukemia protein 1 (TAL-1) (Class A basic helix-loop-helix protein 17) (bHLHa17) (Stem cell protein) (T-cell leukemia/lymphoma protein 5)
[CDC73 C1orf28 HRPT2] Parafibromin (Cell division cycle protein 73 homolog) (Hyperparathyroidism 2 protein)
[Cdc7 Cdc7l1] Cell division cycle 7-related protein kinase (CDC7-related kinase) (muCdc7) (EC 2.7.11.1)
[ftsZ sfiB sulB b0095 JW0093] Cell division protein FtsZ
[CDCA7 JPO1] Cell division cycle-associated protein 7 (Protein JPO1)
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[SEPTIN4 ARTS C17orf47 PNUTL2 SEP4 SEPT4 hucep-7] Septin-4 (Apoptosis-related protein in the TGF-beta signaling pathway) (ARTS) (Bradeion beta) (Brain protein H5) (CE5B3 beta) (Cell division control-related protein 2) (hCDCREL-2) (Cerebral protein 7) (Peanut-like protein 2)
[CDC6 CDC18L] Cell division control protein 6 homolog (CDC6-related protein) (Cdc18-related protein) (HsCdc18) (p62(cdc6)) (HsCDC6)

Bibliography :
No related Items