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Q8BHX3

- BOREA_MOUSE

UniProt

Q8BHX3 - BOREA_MOUSE

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Protein

Borealin

Gene

Cdca8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Biological processi

  1. chromosome organization Source: Ensembl
  2. mitotic nuclear division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_207679. Separation of Sister Chromatids.

Names & Taxonomyi

Protein namesi
Recommended name:
Borealin
Alternative name(s):
Cell division cycle-associated protein 8
MESrg
Gene namesi
Name:Cdca8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1196274. Cdca8.

Subcellular locationi

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. Colocalizes with SENP3 in the nucleolus in interphase cells.By similarity

GO - Cellular componenti

  1. chromocenter Source: MGI
  2. chromosome, centromeric region Source: UniProtKB-KW
  3. chromosome passenger complex Source: UniProtKB
  4. cytoplasm Source: UniProtKB-KW
  5. intercellular bridge Source: Ensembl
  6. midbody Source: Ensembl
  7. nucleolus Source: Ensembl
  8. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 289289BorealinPRO_0000247076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 911Citrulline1 Publication
Modified residuei94 – 941Phosphothreonine; by TTKBy similarity
Modified residuei106 – 1061PhosphothreonineBy similarity
Modified residuei110 – 1101PhosphoserineBy similarity
Modified residuei175 – 1751Phosphoserine; by AURKBBy similarity
Modified residuei198 – 1981PhosphothreonineBy similarity
Modified residuei213 – 2131PhosphothreonineBy similarity
Modified residuei228 – 2281PhosphoserineBy similarity
Modified residuei233 – 2331PhosphoserineBy similarity
Modified residuei247 – 2471PhosphoserineBy similarity
Modified residuei253 – 2531PhosphoserineBy similarity

Post-translational modificationi

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).By similarity
Citrullinated by PADI4.1 Publication

Keywords - PTMi

Citrullination, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8BHX3.
PRIDEiQ8BHX3.

PTM databases

PhosphoSiteiQ8BHX3.

Expressioni

Gene expression databases

BgeeiQ8BHX3.
CleanExiMM_CDCA8.
ExpressionAtlasiQ8BHX3. baseline and differential.
GenevestigatoriQ8BHX3.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi206490. 7 interactions.
IntActiQ8BHX3. 9 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8BHX3.
SMRiQ8BHX3. Positions 21-76, 233-289.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 150150Required for interaction with SENP3By similarityAdd
BLAST
Regioni1 – 8888Required for centromere localizationBy similarityAdd
BLAST
Regioni1 – 5858Required for interaction with INCENPBy similarityAdd
BLAST
Regioni10 – 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 cytokinesisBy similarityAdd
BLAST
Regioni20 – 7859Required for interaction with INCENP and BIRC5By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi125 – 1328Poly-Glu
Compositional biasi133 – 1386Poly-Gly

Domaini

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

Sequence similaritiesi

Belongs to the borealin family.Curated

Phylogenomic databases

eggNOGiNOG39975.
GeneTreeiENSGT00390000011115.
HOVERGENiHBG080103.
InParanoidiQ8BHX3.
KOiK11514.
OMAiQIESDRQ.
OrthoDBiEOG7ZPNKN.
PhylomeDBiQ8BHX3.
TreeFamiTF101077.

Family and domain databases

InterProiIPR018851. Borealin-like_N.
IPR018867. Cell_div_borealin.
[Graphical view]
PfamiPF10512. Borealin. 1 hit.
PF10444. Nbl1_Borealin_N. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BHX3-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAPKKRSSRG TRTNTLRSRK LASFLKDFDR EVQVRTKQIE SDRQTLLKEV
60 70 80 90 100
ENLYNIEILR LPKALQGMKW LDYFALGGNK QALEEAAKAD RDITEINNLT
110 120 130 140 150
AEAIQTPLKS VKKRKVIEVE ESIKEEEEEE EEGGGGGGRT KKSHKNLRSA
160 170 180 190 200
KVKRCLPSKK RTQSIQGRGR SKRLSHDFVT PAMSRLEPSL VKPTPGMTPR
210 220 230 240 250
FDSRVFKTPG LRTPAAKEQV YNISINGSPL ADSKEISLSV PIGGGASLRL
260 270 280
LASDLQRIDI AQLNPEALGN IRKLSSRLAQ ICSSIRTGR
Length:289
Mass (Da):32,214
Last modified:July 25, 2006 - v2
Checksum:i3971F9666DA8EEF5
GO
Isoform 2 (identifier: Q8BHX3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     276-289: SRLAQICSSIRTGR → GRVILQHLCASLPRLRNESPLRSRLGKLERQEHLRLQRTQVWLSANMAVHL

Note: No experimental confirmation available.

Show »
Length:326
Mass (Da):36,648
Checksum:i5AB6F6FEFF61A039
GO
Isoform 3 (identifier: Q8BHX3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     129-162: EEEEGGGGGGRTKKSHKNLRSAKVKRCLPSKKRT → QKRAIRIFDLQKSKDAFHPRREPSPYKEEAEVKG
     163-289: Missing.

Note: No experimental confirmation available.

Show »
Length:162
Mass (Da):18,856
Checksum:i65CEEF398D5C60C1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251L → P in BAB27258. (PubMed:16141072)Curated
Sequence conflicti136 – 1361G → E in AAT34966. 1 PublicationCurated
Sequence conflicti136 – 1361G → E in BAC36334. (PubMed:16141072)Curated
Sequence conflicti153 – 1531K → E in BAC37258. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei129 – 16234EEEEG…SKKRT → QKRAIRIFDLQKSKDAFHPR REPSPYKEEAEVKG in isoform 3. 1 PublicationVSP_019922Add
BLAST
Alternative sequencei163 – 289127Missing in isoform 3. 1 PublicationVSP_019923Add
BLAST
Alternative sequencei276 – 28914SRLAQ…IRTGR → GRVILQHLCASLPRLRNESP LRSRLGKLERQEHLRLQRTQ VWLSANMAVHL in isoform 2. 1 PublicationVSP_019924Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS18631.1. [Q8BHX3-1]
RefSeqiNP_080836.3. NM_026560.4. [Q8BHX3-1]
UniGeneiMm.28038.

Genome annotation databases

EnsembliENSMUST00000030690; ENSMUSP00000030690; ENSMUSG00000028873. [Q8BHX3-2]
ENSMUST00000084296; ENSMUSP00000081319; ENSMUSG00000028873. [Q8BHX3-1]
GeneIDi52276.
KEGGimmu:52276.
UCSCiuc008urj.2. mouse. [Q8BHX3-1]
uc008urk.2. mouse. [Q8BHX3-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS18631.1. [Q8BHX3-1 ]
RefSeqi NP_080836.3. NM_026560.4. [Q8BHX3-1 ]
UniGenei Mm.28038.

3D structure databases

ProteinModelPortali Q8BHX3.
SMRi Q8BHX3. Positions 21-76, 233-289.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 206490. 7 interactions.
IntActi Q8BHX3. 9 interactions.

PTM databases

PhosphoSitei Q8BHX3.

Proteomic databases

MaxQBi Q8BHX3.
PRIDEi Q8BHX3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030690 ; ENSMUSP00000030690 ; ENSMUSG00000028873 . [Q8BHX3-2 ]
ENSMUST00000084296 ; ENSMUSP00000081319 ; ENSMUSG00000028873 . [Q8BHX3-1 ]
GeneIDi 52276.
KEGGi mmu:52276.
UCSCi uc008urj.2. mouse. [Q8BHX3-1 ]
uc008urk.2. mouse. [Q8BHX3-3 ]

Organism-specific databases

CTDi 55143.
MGIi MGI:1196274. Cdca8.

Phylogenomic databases

eggNOGi NOG39975.
GeneTreei ENSGT00390000011115.
HOVERGENi HBG080103.
InParanoidi Q8BHX3.
KOi K11514.
OMAi QIESDRQ.
OrthoDBi EOG7ZPNKN.
PhylomeDBi Q8BHX3.
TreeFami TF101077.

Enzyme and pathway databases

Reactomei REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_207679. Separation of Sister Chromatids.

Miscellaneous databases

NextBioi 308732.
PROi Q8BHX3.
SOURCEi Search...

Gene expression databases

Bgeei Q8BHX3.
CleanExi MM_CDCA8.
ExpressionAtlasi Q8BHX3. baseline and differential.
Genevestigatori Q8BHX3.

Family and domain databases

InterProi IPR018851. Borealin-like_N.
IPR018867. Cell_div_borealin.
[Graphical view ]
Pfami PF10512. Borealin. 1 hit.
PF10444. Nbl1_Borealin_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: CITRULLINATION AT ARG-91.

Entry informationi

Entry nameiBOREA_MOUSE
AccessioniPrimary (citable) accession number: Q8BHX3
Secondary accession number(s): B1ARX0
, B1ARX1, Q6NVD3, Q8BHB1, Q8BHQ5, Q8BHQ9, Q9CRN4, Q9CS02, Q9CTF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: October 29, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3