Reviewed, UniProtKB/Swiss-Prot Q53HL2 (BOREA_HUMAN)

Names and origin

Protein names

Recommended name:
    Borealin
Alternative name(s):
    Dasra-B
      Short name=hDasra-B
    Cell division cycle-associated protein 8
    Pluripotent embryonic stem cell-related gene 3 protein

Gene names

Name:	CDCA8
Synonyms:	PESCRG3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. In the complex, it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment. Ref.6 Ref.7 Ref.13 Ref.19
Subunit structure	May form homooligomers and homodimers. Component of the CPC at least composed of BIRC5/survivin, CDCA8/borealin, INCENP and AURKB/Aurora-B. Interacts with BIRC5/survivin and INCENP; interaction is direct. Interacts with SENP3, UBE2I and RANBP2. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.23 Ref.26 Ref.27
Subcellular location	Nucleus › nucleolus. Cytoplasm. Cytoplasm › cytoskeleton › spindle. Centromere. 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. Ref.7 Ref.10 Ref.12 Ref.23 Ref.8 Ref.14
Developmental stage	Cell-cycle regulated. Increases during G2/M phase and then reduces after exit from M phase. Ref.10
Domain	The C-terminal region (aa 207-280) represents the dimerization motif.
Post-translational modification	Phosphorylated by TTK, essentially at Thr-88, Thr94, Thr-169 and Thr-230. Ref.7 Ref.19 Ref.23 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3. Ref.23
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.
Sequence similarities	Belongs to the borealin family.
Sequence caution	The sequence BG354581 differs from that shown. Reason: Frameshift at positions 123 and 200.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosomal protein Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome organization Ref.6 Inferred from mutant phenotype. Source: UniProtKB mitotic metaphase Ref.6 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	chromosome passenger complex Ref.6 Ref.15 Inferred from physical interaction. Source: UniProtKB chromosome, centromeric region Ref.6 Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Ref.9 Ref.11 Ref.19 Ref.26 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BIRC5	O15392	2	EBI-979174,EBI-518823
BIRC5	O15392-1	2	EBI-979174,EBI-518838
BIRC5	O15392-2	2	EBI-979174,EBI-518842
TTK	P33981	1	EBI-979174,EBI-1645856

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 280

280

Borealin

PRO_0000247075

Regions

Region

1 – 140

140

Required for interaction with SENP3

Region

1 – 88

88

Required for centromere localization

Region

1 – 58

58

Required for interaction with INCENP

Region

10 – 109

100

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

59

Required for interaction with INCENP and BIRC5

Compositional bias

125 – 133

9

Poly-Glu

Amino acid modifications

Modified residue

15

1

Phosphoserine Ref.20

Modified residue

23

1

Phosphoserine Ref.20

Modified residue

88

1

Phosphothreonine; by TTK Ref.23

Modified residue

94

1

Phosphothreonine; by TTK

Modified residue

106

1

Phosphothreonine Ref.17 Ref.18 Ref.20 Ref.21 Ref.25

Modified residue

110

1

Phosphoserine Ref.20

Modified residue

154

1

Phosphoserine Ref.18 Ref.20

Modified residue

164

1

Phosphoserine Ref.20

Modified residue

165

1

Phosphoserine Ref.7 Ref.20

Modified residue

169

1

Phosphothreonine; by TTK Ref.23 Ref.18

Modified residue

171

1

Phosphothreonine Ref.18

Modified residue

180

1

Phosphoserine Ref.18

Modified residue

189

1

Phosphothreonine Ref.20 Ref.21

Modified residue

194

1

Phosphoserine Ref.20

Modified residue

199

1

Phosphothreonine Ref.18

Modified residue

204

1

Phosphothreonine Ref.18 Ref.20 Ref.21

Modified residue

212

1

Phosphotyrosine

Modified residue

215

1

Phosphoserine Ref.18

Modified residue

219

1

Phosphoserine Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25

Modified residue

224

1

Phosphoserine

Modified residue

230

1

Phosphothreonine; by TTK Ref.23

Modified residue

238

1

Phosphoserine Ref.23

Modified residue

244

1

Phosphoserine Ref.20

Modified residue

274

1

Phosphoserine Ref.20

Natural variations

Natural variant

12

1

K → N: dbSNP rs17851453. Ref.5

VAR_027063

Experimental info

Mutagenesis

17

1

R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-19 and E-20. Ref.26

Mutagenesis

19

1

R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-20. Ref.26

Mutagenesis

20

1

K → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-19. Ref.26

Mutagenesis

26

1

K → R: Fails to exhibit normal localization to the nucleolus in interphase depleted cells. Ref.23

Mutagenesis

35

1

R → E: Loss of binding to INCENP; when associated with Y-46. Ref.26

Mutagenesis

46

1

L → Y: Loss of binding to INCENP; when associated with E-35. Ref.26

Mutagenesis

70

1

W → E: Loss of binding to BIRC5; when associated with E-74. Ref.26

Mutagenesis

74

1

F → E: Loss of binding to BIRC5; when associated with E-70. Ref.26

Mutagenesis

88

1

T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-94; A-169 and A-230. Ref.27

Mutagenesis

94

1

T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-169 and A-230. Ref.27

Mutagenesis

165

1

S → A: Results in reduction but not abolition of phosphorylation. Ref.7

Mutagenesis

169

1

T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-94 and A-230. Ref.27

Mutagenesis

219

1

S → D or K: No effect on the structure.

Mutagenesis

230

1

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. Ref.27

Mutagenesis

230

1

T → D or K: Substantial loss of structure. Ref.27

Mutagenesis

230

1

T → V: Decrease in AURKB activity and no effect on the structure. Ref.27

Sequence conflict

155

1

I → M in BAD96288. Ref.4

Sequence conflict

213

1

N → D in BAD96269. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

280

Helix Strand Turn

Details...

Helix

16 – 60

45

Helix

63 – 66

4

Helix

70 – 75

6

Sequences

	Sequence		Length	Mass (Da)
	Q53HL2-1 [UniParc]. Last modified July 25, 2006. Version 2. Checksum: 519978A7C295C571	FASTA	280	31,323
	10 20 30 40 50 60 MAPRKGSSRV AKTNSLRRRK LASFLKDFDR EVEIRIKQIE SDRQNLLKEV DNLYNIEILR 70 80 90 100 110 120 LPKALREMNW LDYFALGGNK QALEEAATAD LDITEINKLT AEAIQTPLKS AKTRKVIQVD 130 140 150 160 170 180 EMIVEEEEEE ENERKNLQTA RVKRCPPSKK RTQSIQGKGK GKRSSRANTV TPAVGRLEVS 190 200 210 220 230 240 MVKPTPGLTP RFDSRVFKTP GLRTPAAGER IYNISGNGSP LADSKEIFLT VPVGGGESLR 250 260 270 280 LLASDLQRHS IAQLDPEALG NIKKLSNRLA QICSSIRTHK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Drug target discovery by gene expression analysis: cell cycle genes." Walker M.G. Curr. Cancer Drug Targets 1:73-83(2001) [PubMed: 12188893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The cloning and functional analysis of HPESCRG3." Nie Z., Du J., Lin G., Lu G. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo.
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Coronary arterial endothelium.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-12. Tissue: Colon, Kidney and Lung.
[6]	"The chromosomal passenger complex is required for chromatin-induced microtubule stabilization and spindle assembly." Sampath S.C., Ohi R., Leismann O., Salic A., Pozniakovski A., Funabiki H. Cell 118:187-202(2004) [PubMed: 15260989] [Abstract] Cited for: FUNCTION, COMPONENT OF THE CPC COMPLEX.
[7]	"Borealin: a novel chromosomal passenger required for stability of the bipolar mitotic spindle." Gassmann R., Carvalho A., Henzing A.J., Ruchaud S., Hudson D.F., Honda R., Nigg E.A., Gerloff D.L., Earnshaw W.C. J. Cell Biol. 166:179-191(2004) [PubMed: 15249581] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BIRC5 AND INCENP, PHOSPHORYLATION AT SER-165, MUTAGENESIS OF SER-165.
[8]	"Proteome analysis of the human mitotic spindle." Sauer G., Koerner R., Hanisch A., Ries A., Nigg E.A., Sillje H.H.W. Mol. Cell. Proteomics 4:35-43(2005) [PubMed: 15561729] [Abstract] Cited for: SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[9]	"Survivin mediates targeting of the chromosomal passenger complex to the centromere and midbody." Vader G., Kauw J.J.W., Medema R.H., Lens S.M.A. EMBO Rep. 7:85-92(2006) [PubMed: 16239925] [Abstract] Cited for: INTERACTION WITH BIRC5.
[10]	"Borealin/Dasra B is a cell cycle-regulated chromosomal passenger protein and its nuclear accumulation is linked to poor prognosis for human gastric cancer." Chang J.-L., Chen T.-H., Wang C.-F., Chiang Y.-H., Huang Y.-L., Wong F.-H., Chou C.-K., Chen C.-M. Exp. Cell Res. 312:962-973(2006) [PubMed: 16427043] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BIRC5, DEVELOPMENTAL STAGE.
[11]	"Molecular analysis of survivin isoforms: evidence that alternatively spliced variants do not play a role in mitosis." Noton E.A., Colnaghi R., Tate S., Starck C., Carvalho A., Ko Ferrigno P., Wheatley S.P. J. Biol. Chem. 281:1286-1295(2006) [PubMed: 16291752] [Abstract] Cited for: INTERACTION WITH BIRC5.
[12]	"Uncoupling the central spindle-associated function of the chromosomal passenger complex from its role at centromeres." Lens S.M.A., Rodriguez J.A., Vader G., Span S.W., Giaccone G., Medema R.H. Mol. Biol. Cell 17:1897-1909(2006) [PubMed: 16436504] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BIRC5.
[13]	"Centromere targeting of the chromosomal passenger complex requires a ternary subcomplex of borealin, survivin, and the N-terminal domain of INCENP." Klein U.R., Nigg E.A., Gruneberg U. Mol. Biol. Cell 17:2547-2558(2006) [PubMed: 16571674] [Abstract] Cited for: FUNCTION.
[14]	"Subcellular localization and nucleocytoplasmic transport of the chromosomal passenger proteins before nuclear envelope breakdown." Rodriguez J.A., Lens S.M.A., Span S.W., Vader G., Medema R.H., Kruyt F.A.E., Giaccone G. Oncogene 25:4867-4879(2006) [PubMed: 16547492] [Abstract] Cited for: SUBCELLULAR LOCATION.
[15]	"A survivin-ran complex regulates spindle formation in tumor cells." Xia F., Canovas P.M., Guadagno T.M., Altieri D.C. Mol. Cell. Biol. 28:5299-5311(2008) [PubMed: 18591255] [Abstract] Cited for: INTERACTION WITH BIRC5.
[16]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106 AND SER-219, MASS SPECTROMETRY.
[18]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; SER-154; THR-169; THR-171; SER-180; THR-199; THR-204; SER-215 AND SER-219, MASS SPECTROMETRY.
[19]	"Mps1 phosphorylates Borealin to control Aurora B activity and chromosome alignment." 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. Cell 132:233-246(2008) [PubMed: 18243099] [Abstract] Cited for: PHOSPHORYLATION BY TTK, FUNCTION.
[20]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-23; THR-106; SER-110; SER-154; SER-164; SER-165; THR-189; SER-194; THR-204; SER-219; SER-244 AND SER-274, MASS SPECTROMETRY.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; THR-189; THR-204 AND SER-219, MASS SPECTROMETRY.
[22]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, MASS SPECTROMETRY.
[23]	"RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin." Klein U.R., Haindl M., Nigg E.A., Muller S. Mol. Biol. Cell 20:410-418(2009) [PubMed: 18946085] [Abstract] Cited for: INTERACTION WITH SENP3; UBE2I AND RANBP2, SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-26, PHOSPHORYLATION AT THR-88; THR94; THR-169; THR-230 AND SER-238.
[24]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-212; SER-219 AND SER-224, MASS SPECTROMETRY.
[25]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106 AND SER-219, MASS SPECTROMETRY. Tissue: T-cell.
[26]	"Structure of a Survivin-Borealin-INCENP core complex reveals how chromosomal passengers travel together." Jeyaprakash A.A., Klein U.R., Lindner D., Ebert J., Nigg E.A., Conti E. Cell 131:271-285(2007) [PubMed: 17956729] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 15-76, INTERACTION WITH BIRC5 AND INCENP, MUTAGENESIS OF ARG-17; ARG-19; LYS-20; ARG-35; LEU-46; TRP-70 AND PHE-74.
[27]	"Phosphorylation of a borealin dimerization domain is required for proper chromosome segregation." Bourhis E., Lingel A., Phung Q., Fairbrother W.J., Cochran A.G. Biochemistry 48:6783-6793(2009) [PubMed: 19530738] [Abstract] Cited for: STRUCTURE BY NMR OF 207-280, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-78, OLIGOMERIZATION, MUTAGENESIS OF THR-88; THR-94; THR-169 AND THR-230.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BG354581 mRNA. No translation available.
AY508815 mRNA. Translation: AAR91699.1.
AK001330 mRNA. Translation: BAA91629.1.
AK022104 mRNA. Translation: BAB13961.1.
AK022606 mRNA. Translation: BAB14125.1.
AK222549 mRNA. Translation: BAD96269.1.
AK222568 mRNA. Translation: BAD96288.1.
BC000703 mRNA. Translation: AAH00703.1.
BC001651 mRNA. Translation: AAH01651.1.
BC016944 mRNA. Translation: AAH16944.1.
BC008079 mRNA. Translation: AAH08079.1.

IPI

IPI00303099.

RefSeq

NP_060571.1.

UniGene

Hs.524571

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KDD	NMR	-	A/B	207-280	[»]
2QFA	X-ray	1.40	B	15-76	[»]
2RAW	X-ray	2.40	B	20-78	[»]
2RAX	X-ray	3.30	B/F/Y	20-78	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q53HL2. 6 interactions.

STRING

Q53HL2.

PTM databases

PhosphoSite

Q53HL2.

Proteomic databases

PeptideAtlas

Q53HL2.

PRIDE

Q53HL2.

Genome annotation databases

Ensembl

ENST00000327331; ENSP00000316121; ENSG00000134690; Homo sapiens. [Genome view]
ENST00000373055; ENSP00000362146; ENSG00000134690; Homo sapiens. [Genome view]

GeneID

55143.

KEGG

hsa:55143.

UCSC

uc001cbr.1. human.

Organism-specific databases

CTD

55143.

GeneCards

GC01P037931.

HGNC

HGNC:14629. CDCA8.

MIM

609977. gene.

PharmGKB

PA26281.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06446.

HOGENOM

HBG714853.

HOVERGEN

Q53HL2.

InParanoid

Q53HL2.

OMA

VDEMIVE.

OrthoDB

EOG969TDW.

PhylomeDB

Q53HL2.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_b_pathway. Aurora B signaling.

Reactome

REACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpress

Q53HL2.

Bgee

Q53HL2.

CleanEx

HS_CDCA8.

Genevestigator

Q53HL2.

GermOnline

ENSG00000134690. Homo sapiens.

Family and domain databases

InterPro

IPR018867. Cdc_assoc-8.
[Graphical view]

Pfam

PF10512. Borealin. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

58844.

SOURCE

Search...

Entry information

Entry name

BOREA_HUMAN

Accession

Primary (citable) accession number: Q53HL2
Secondary accession number(s): Q53HN1, Q96AM3, Q9NVW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 25, 2006
Last modified:	February 9, 2010
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.