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Q8BHX3 (BOREA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
MESrg
Gene names
Name:Cdca8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length289 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 By similarity.

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 By similarity. Interacts with BIRC5/survivin and INCENP; interaction is direct. Interacts with SENP3, UBE2I and RANBP2 By similarity.

Subcellular location

Nucleusnucleolus By similarity. Cytoplasm By similarity. Chromosomecentromere By similarity. Cytoplasmcytoskeletonspindle By similarity. 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 By similarity. Colocalizes with SENP3 in the nucleolus in interphase cells By similarity.

Domain

The C-terminal region (aa 216-289) represents the dimerization motif By similarity.

Post-translational modification

Phosphorylated by TTK, essentially at Thr-94 By similarity.

Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3 By similarity.

Citrullinated by PADI4.

Sequence similarities

Belongs to the borealin family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BHX3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8BHX3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     276-289: SRLAQICSSIRTGR → GRVILQHLCASLPRLRNESPLRSRLGKLERQEHLRLQRTQVWLSANMAVHL
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8BHX3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     129-162: EEEEGGGGGGRTKKSHKNLRSAKVKRCLPSKKRT → QKRAIRIFDLQKSKDAFHPRREPSPYKEEAEVKG
     163-289: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Borealin
PRO_0000247076

Regions

Region1 – 150150Required for interaction with SENP3 By similarity
Region1 – 8888Required for centromere localization By similarity
Region1 – 5858Required for interaction with INCENP By similarity
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 By similarity
Region20 – 7859Required for interaction with INCENP and BIRC5 By similarity
Compositional bias125 – 1328Poly-Glu
Compositional bias133 – 1386Poly-Gly

Amino acid modifications

Modified residue911Citrulline
Modified residue941Phosphothreonine; by TTK By similarity
Modified residue1061Phosphothreonine By similarity
Modified residue1101Phosphoserine By similarity
Modified residue1751Phosphoserine; by AURKB By similarity
Modified residue1981Phosphothreonine By similarity
Modified residue2131Phosphothreonine By similarity
Modified residue2281Phosphoserine By similarity
Modified residue2331Phosphoserine By similarity
Modified residue2471Phosphoserine By similarity
Modified residue2531Phosphoserine By similarity

Natural variations

Alternative sequence129 – 16234EEEEG…SKKRT → QKRAIRIFDLQKSKDAFHPR REPSPYKEEAEVKG in isoform 3.
VSP_019922
Alternative sequence163 – 289127Missing in isoform 3.
VSP_019923
Alternative sequence276 – 28914SRLAQ…IRTGR → GRVILQHLCASLPRLRNESP LRSRLGKLERQEHLRLQRTQ VWLSANMAVHL in isoform 2.
VSP_019924

Experimental info

Sequence conflict251L → P in BAB27258. Ref.2
Sequence conflict1361G → E in AAT34966. Ref.1
Sequence conflict1361G → E in BAC36334. Ref.2
Sequence conflict1531K → E in BAC37258. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: 3971F9666DA8EEF5

FASTA28932,214
        10         20         30         40         50         60 
MAPKKRSSRG TRTNTLRSRK LASFLKDFDR EVQVRTKQIE SDRQTLLKEV ENLYNIEILR 

        70         80         90        100        110        120 
LPKALQGMKW LDYFALGGNK QALEEAAKAD RDITEINNLT AEAIQTPLKS VKKRKVIEVE 

       130        140        150        160        170        180 
ESIKEEEEEE EEGGGGGGRT KKSHKNLRSA KVKRCLPSKK RTQSIQGRGR SKRLSHDFVT 

       190        200        210        220        230        240 
PAMSRLEPSL VKPTPGMTPR FDSRVFKTPG LRTPAAKEQV YNISINGSPL ADSKEISLSV 

       250        260        270        280 
PIGGGASLRL LASDLQRIDI AQLNPEALGN IRKLSSRLAQ ICSSIRTGR 

« Hide

Isoform 2 [UniParc].

Checksum: 5AB6F6FEFF61A039
Show »

FASTA32636,648
Isoform 3 [UniParc].

Checksum: 65CEEF398D5C60C1
Show »

FASTA16218,856

References

« Hide 'large scale' references
[1]"The cloning and functional analysis of MESrg."
Nie Z., Du J., Lu G.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Head, Liver, Testis and Wolffian duct.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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] (ISOFORM 3).
Strain: C57BL/6.
Tissue: Brain.
[5]"Citrullination regulates pluripotency and histone H1 binding to chromatin."
Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S., Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C., Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.
Nature 507:104-108(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-91.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY550907 mRNA. Translation: AAT34966.1.
AK003755 mRNA. Translation: BAB22980.1.
AK010905 mRNA. Translation: BAB27258.1.
AK020070 mRNA. Translation: BAB31983.3.
AK076065 mRNA. Translation: BAC36158.1.
AK076422 mRNA. Translation: BAC36334.1.
AK077717 mRNA. Translation: BAC36977.1.
AK077920 mRNA. Translation: BAC37063.1.
AK078404 mRNA. Translation: BAC37258.1.
AK082800 mRNA. Translation: BAC38627.1.
AL606933 Genomic DNA. Translation: CAM16105.1.
AL606933 Genomic DNA. Translation: CAM16106.1.
BC068181 mRNA. Translation: AAH68181.1.
CCDSCCDS18631.1. [Q8BHX3-1]
RefSeqNP_080836.3. NM_026560.4. [Q8BHX3-1]
UniGeneMm.28038.

3D structure databases

ProteinModelPortalQ8BHX3.
SMRQ8BHX3. Positions 21-76, 233-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206490. 7 interactions.
IntActQ8BHX3. 9 interactions.

PTM databases

PhosphoSiteQ8BHX3.

Proteomic databases

PRIDEQ8BHX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030690; ENSMUSP00000030690; ENSMUSG00000028873. [Q8BHX3-2]
ENSMUST00000084296; ENSMUSP00000081319; ENSMUSG00000028873. [Q8BHX3-1]
GeneID52276.
KEGGmmu:52276.
UCSCuc008urj.2. mouse. [Q8BHX3-1]
uc008urk.2. mouse. [Q8BHX3-3]

Organism-specific databases

CTD55143.
MGIMGI:1196274. Cdca8.

Phylogenomic databases

eggNOGNOG39975.
GeneTreeENSGT00390000011115.
HOVERGENHBG080103.
InParanoidB1ARX1.
KOK11514.
OMAQIESDRQ.
OrthoDBEOG7ZPNKN.
PhylomeDBQ8BHX3.
TreeFamTF101077.

Gene expression databases

ArrayExpressQ8BHX3.
BgeeQ8BHX3.
CleanExMM_CDCA8.
GenevestigatorQ8BHX3.

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

NextBio308732.
PROQ8BHX3.
SOURCESearch...

Entry information

Entry nameBOREA_MOUSE
AccessionPrimary (citable) accession number: Q8BHX3
Secondary accession number(s): B1ARX0 expand/collapse secondary AC list , B1ARX1, Q6NVD3, Q8BHB1, Q8BHQ5, Q8BHQ9, Q9CRN4, Q9CS02, Q9CTF4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: July 9, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot