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Q53HL2 (BOREA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Borealin
Alternative name(s):
Cell division cycle-associated protein 8
Dasra-B
Short name=hDasra-B
Pluripotent embryonic stem cell-related gene 3 protein
Gene names
Name:CDCA8
Synonyms:PESCRG3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length280 AA.
Sequence statusComplete.
Protein existenceEvidence 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.7 Ref.8 Ref.14 Ref.18

Subunit structure

May form homooligomers and homodimers. Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB and AURKC. Interacts with BIRC5/survivin and INCENP; interaction is direct. Interacts with SENP3, UBE2I and RANBP2. Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.21 Ref.26 Ref.27

Subcellular location

Nucleusnucleolus. Cytoplasm. Cytoplasmcytoskeletonspindle. Chromosomecentromere. 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.8 Ref.9 Ref.11 Ref.13 Ref.15 Ref.21

Developmental stage

Cell-cycle regulated. Increases during G2/M phase and then reduces after exit from M phase. Ref.11

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.8 Ref.18 Ref.27

Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3. Ref.21

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 280280Borealin
PRO_0000247075

Regions

Region1 – 140140Required for interaction with SENP3
Region1 – 8888Required for centromere localization
Region1 – 5858Required for interaction with INCENP
Region10 – 109100Required 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
Region20 – 7859Required for interaction with INCENP and BIRC5
Compositional bias125 – 1339Poly-Glu

Amino acid modifications

Modified residue881Phosphothreonine; by TTK Ref.27
Modified residue941Phosphothreonine; by TTK Ref.27
Modified residue1061Phosphothreonine Ref.16 Ref.19 Ref.23
Modified residue1101Phosphoserine Ref.16
Modified residue1651Phosphoserine; by AURKB Ref.8
Modified residue1691Phosphothreonine; by TTK Ref.27
Modified residue1891Phosphothreonine Ref.16 Ref.19 Ref.24
Modified residue2041Phosphothreonine Ref.16 Ref.19
Modified residue2191Phosphoserine Ref.16 Ref.19 Ref.22 Ref.23 Ref.24 Ref.25
Modified residue2241Phosphoserine Ref.22
Modified residue2301Phosphothreonine; by TTK Ref.27
Modified residue2381Phosphoserine Ref.27
Modified residue2441Phosphoserine Ref.16

Natural variations

Natural variant121K → N. Ref.6
Corresponds to variant rs17851453 [ dbSNP | Ensembl ].
VAR_027063

Experimental info

Mutagenesis171R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-19 and E-20. Ref.26
Mutagenesis191R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-20. Ref.26
Mutagenesis201K → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-19. Ref.26
Mutagenesis261K → R: Fails to exhibit normal localization to the nucleolus in interphase depleted cells. Ref.21
Mutagenesis351R → E: Loss of binding to INCENP; when associated with Y-46. Ref.26
Mutagenesis461L → Y: Loss of binding to INCENP; when associated with E-35. Ref.26
Mutagenesis701W → E: Loss of binding to BIRC5; when associated with E-74. Ref.26
Mutagenesis741F → E: Loss of binding to BIRC5; when associated with E-70. Ref.26
Mutagenesis881T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-94; A-169 and A-230. Ref.27
Mutagenesis941T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-169 and A-230. Ref.27
Mutagenesis1651S → A: Results in reduction but not abolition of phosphorylation. Ref.8
Mutagenesis1691T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-94 and A-230. Ref.27
Mutagenesis2191S → D or K: No effect on the structure.
Mutagenesis2301T → 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
Mutagenesis2301T → D or K: Substantial loss of structure. Ref.27
Mutagenesis2301T → V: Decrease in AURKB activity and no effect on the structure. Ref.27
Sequence conflict1551I → M in BAD96288. Ref.4
Sequence conflict2131N → D in BAD96269. Ref.4

Secondary structure

............... 280
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q53HL2 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: 519978A7C295C571

FASTA28031,323
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-12.
Tissue: Colon, Kidney and Lung.
[7]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPONENT OF THE CPC COMPLEX.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE CPC COMPLEX, PHOSPHORYLATION AT SER-165, MUTAGENESIS OF SER-165.
[9]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BIRC5.
[11]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BIRC5, DEVELOPMENTAL STAGE.
[12]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BIRC5.
[13]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BIRC5.
[14]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[16]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; SER-110; THR-189; THR-204; SER-219 AND SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BIRC5.
[18]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY TTK, FUNCTION.
[19]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; THR-189; THR-204 AND SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SENP3; UBE2I AND RANBP2, SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-26.
[22]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106 AND SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[24]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189 AND SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: 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, 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.
CH471059 Genomic DNA. Translation: EAX07324.1.
CH471059 Genomic DNA. Translation: EAX07325.1.
BC000703 mRNA. Translation: AAH00703.1.
BC001651 mRNA. Translation: AAH01651.1.
BC016944 mRNA. Translation: AAH16944.1.
BC008079 mRNA. Translation: AAH08079.1.
CCDSCCDS424.1.
RefSeqNP_001243804.1. NM_001256875.1.
NP_060571.1. NM_018101.3.
UniGeneHs.524571.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KDDNMR-A/B207-280[»]
2QFAX-ray1.40B15-76[»]
2RAWX-ray2.40B20-78[»]
2RAXX-ray3.30B/F/Y20-78[»]
ProteinModelPortalQ53HL2.
SMRQ53HL2. Positions 15-76, 224-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120446. 24 interactions.
DIPDIP-37995N.
IntActQ53HL2. 11 interactions.
MINTMINT-4509527.
STRING9606.ENSP00000316121.

PTM databases

PhosphoSiteQ53HL2.

Polymorphism databases

DMDM110832774.

Proteomic databases

MaxQBQ53HL2.
PaxDbQ53HL2.
PeptideAtlasQ53HL2.
PRIDEQ53HL2.

Protocols and materials databases

DNASU55143.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327331; ENSP00000316121; ENSG00000134690.
ENST00000373055; ENSP00000362146; ENSG00000134690.
GeneID55143.
KEGGhsa:55143.
UCSCuc001cbr.4. human.

Organism-specific databases

CTD55143.
GeneCardsGC01P038158.
HGNCHGNC:14629. CDCA8.
HPACAB040294.
HPA028120.
HPA028258.
HPA028783.
MIM609977. gene.
neXtProtNX_Q53HL2.
PharmGKBPA26281.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39975.
HOGENOMHOG000261628.
HOVERGENHBG080103.
InParanoidQ53HL2.
KOK11514.
OMAQIESDRQ.
OrthoDBEOG7ZPNKN.
PhylomeDBQ53HL2.
TreeFamTF101077.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

BgeeQ53HL2.
CleanExHS_CDCA8.
GenevestigatorQ53HL2.

Family and domain databases

InterProIPR018851. Borealin-like_N.
IPR018867. Cell_div_borealin.
[Graphical view]
PfamPF10512. Borealin. 1 hit.
PF10444. Nbl1_Borealin_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ53HL2.
GeneWikiCDCA8.
GenomeRNAi55143.
NextBio58844.
PROQ53HL2.
SOURCESearch...

Entry information

Entry nameBOREA_HUMAN
AccessionPrimary (citable) accession number: Q53HL2
Secondary accession number(s): D3DPT4 expand/collapse secondary AC list , Q53HN1, Q96AM3, Q9NVW5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: July 9, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM