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Protein

Borealin

Gene

CDCA8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment.4 Publications

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • chromosome organization Source: UniProtKB
  • mitotic metaphase plate congression Source: UniProtKB
  • protein sumoylation Source: Reactome
  • sister chromatid cohesion Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SIGNORiQ53HL2.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CDCA8
Synonyms:PESCRG3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:14629. CDCA8.

Subcellular locationi

  • Nucleusnucleolus 1 Publication
  • Cytoplasm 1 Publication
  • Cytoplasmcytoskeletonspindle 1 Publication
  • Chromosomecentromere 1 Publication

  • 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.1 Publication

GO - Cellular componenti

  • chromocenter Source: Ensembl
  • chromosome, centromeric region Source: UniProtKB
  • chromosome passenger complex Source: UniProtKB
  • cytosol Source: Reactome
  • intercellular bridge Source: HPA
  • midbody Source: FlyBase
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
  • protein complex Source: UniProtKB
  • spindle midzone Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi17R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-19 and E-20. 1 Publication1
Mutagenesisi19R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-20. 1 Publication1
Mutagenesisi20K → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-19. 1 Publication1
Mutagenesisi26K → R: Fails to exhibit normal localization to the nucleolus in interphase depleted cells. 1 Publication1
Mutagenesisi35R → E: Loss of binding to INCENP; when associated with Y-46. 1 Publication1
Mutagenesisi46L → Y: Loss of binding to INCENP; when associated with E-35. 1 Publication1
Mutagenesisi70W → E: Loss of binding to BIRC5; when associated with E-74. 1 Publication1
Mutagenesisi74F → E: Loss of binding to BIRC5; when associated with E-70. 1 Publication1
Mutagenesisi88T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-94; A-169 and A-230. 1 Publication1
Mutagenesisi94T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-169 and A-230. 1 Publication1
Mutagenesisi106T → 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. 1 Publication1
Mutagenesisi165S → A: Results in reduction but not abolition of phosphorylation. 1 Publication1
Mutagenesisi169T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-94 and A-230. 1 Publication1
Mutagenesisi171T → 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. 1 Publication1
Mutagenesisi185T → 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. 1 Publication1
Mutagenesisi189T → 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. 1 Publication1
Mutagenesisi199T → 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. 1 Publication1
Mutagenesisi204T → 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. 1 Publication1
Mutagenesisi219S → 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. 1 Publication1
Mutagenesisi219S → D or K: No effect on the structure. 1
Mutagenesisi230T → 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. 1 Publication1
Mutagenesisi230T → D or K: Substantial loss of structure. 1 Publication1
Mutagenesisi230T → V: Decrease in AURKB activity and no effect on the structure. 1 Publication1

Organism-specific databases

DisGeNETi55143.
OpenTargetsiENSG00000134690.
PharmGKBiPA26281.

Polymorphism and mutation databases

BioMutaiCDCA8.
DMDMi110832774.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002470751 – 280BorealinAdd BLAST280

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei88Phosphothreonine; by TTK1 Publication1
Modified residuei94Phosphothreonine; by TTK1 Publication1
Modified residuei106PhosphothreonineCombined sources1
Modified residuei110PhosphoserineCombined sources1
Modified residuei165Phosphoserine; by AURKB1 Publication1
Modified residuei169Phosphothreonine; by TTK1 Publication1
Modified residuei189PhosphothreonineCombined sources1
Modified residuei204PhosphothreonineCombined sources1
Modified residuei219PhosphoserineCombined sources1
Modified residuei224PhosphoserineCombined sources1
Modified residuei230Phosphothreonine; by TTK1 Publication1
Modified residuei238Phosphoserine1 Publication1
Modified residuei244PhosphoserineCombined sources1

Post-translational modificationi

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.3 Publications
Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ53HL2.
MaxQBiQ53HL2.
PaxDbiQ53HL2.
PeptideAtlasiQ53HL2.
PRIDEiQ53HL2.

PTM databases

iPTMnetiQ53HL2.
PhosphoSitePlusiQ53HL2.

Expressioni

Developmental stagei

Cell-cycle regulated. Increases during G2/M phase and then reduces after exit from M phase.1 Publication

Gene expression databases

BgeeiENSG00000134690.
CleanExiHS_CDCA8.
GenevisibleiQ53HL2. HS.

Organism-specific databases

HPAiCAB040294.
HPA028120.
HPA028258.
HPA028783.

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 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 CDK1.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BIRC5E7CU852EBI-979174,EBI-10488580
BIRC5O1539214EBI-979174,EBI-518823
BIRC5O15392-12EBI-979174,EBI-518838
BIRC5O15392-22EBI-979174,EBI-518842
GAS2L3Q86XJ12EBI-979174,EBI-9248152
INCENPQ9NQS74EBI-979174,EBI-307907

Protein-protein interaction databases

BioGridi120446. 54 interactors.
DIPiDIP-37995N.
IntActiQ53HL2. 20 interactors.
MINTiMINT-4509527.
STRINGi9606.ENSP00000316121.

Structurei

Secondary structure

1280
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 60Combined sources45
Helixi63 – 66Combined sources4
Helixi70 – 75Combined sources6
Beta strandi233 – 237Combined sources5
Turni243 – 245Combined sources3
Helixi248 – 252Combined sources5
Helixi256 – 275Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KDDNMR-A/B207-280[»]
2QFAX-ray1.40B15-76[»]
2RAWX-ray2.40B20-78[»]
2RAXX-ray3.30B/F/Y20-78[»]
ProteinModelPortaliQ53HL2.
SMRiQ53HL2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53HL2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 140Required for interaction with SENP31 PublicationAdd BLAST140
Regioni1 – 88Required for centromere localizationAdd BLAST88
Regioni1 – 58Required for interaction with INCENP1 PublicationAdd BLAST58
Regioni10 – 109Required to form a minimal CPC core complex that localizes to the central spindle and midbody and properly executes the role of the CPC during cytokinesisAdd BLAST100
Regioni20 – 78Required for interaction with INCENP and BIRC51 PublicationAdd BLAST59

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi125 – 133Poly-Glu9

Domaini

The C-terminal region (aa 207-280) represents the dimerization motif.

Sequence similaritiesi

Belongs to the borealin family.Curated

Phylogenomic databases

eggNOGiENOG410IICJ. Eukaryota.
ENOG4111N8R. LUCA.
GeneTreeiENSGT00390000011115.
HOGENOMiHOG000261628.
HOVERGENiHBG080103.
InParanoidiQ53HL2.
KOiK11514.
OMAiQIESDRQ.
OrthoDBiEOG091G167R.
PhylomeDBiQ53HL2.
TreeFamiTF101077.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q53HL2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPRKGSSRV AKTNSLRRRK LASFLKDFDR EVEIRIKQIE SDRQNLLKEV
60 70 80 90 100
DNLYNIEILR LPKALREMNW LDYFALGGNK QALEEAATAD LDITEINKLT
110 120 130 140 150
AEAIQTPLKS AKTRKVIQVD EMIVEEEEEE ENERKNLQTA RVKRCPPSKK
160 170 180 190 200
RTQSIQGKGK GKRSSRANTV TPAVGRLEVS MVKPTPGLTP RFDSRVFKTP
210 220 230 240 250
GLRTPAAGER IYNISGNGSP LADSKEIFLT VPVGGGESLR LLASDLQRHS
260 270 280
IAQLDPEALG NIKKLSNRLA QICSSIRTHK
Length:280
Mass (Da):31,323
Last modified:July 25, 2006 - v2
Checksum:i519978A7C295C571
GO

Sequence cautioni

The sequence BG354581 differs from that shown. Reason: Frameshift at positions 123 and 200.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti155I → M in BAD96288 (Ref. 4) Curated1
Sequence conflicti213N → D in BAD96269 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02706312K → N.1 PublicationCorresponds to variant rs17851453dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS424.1.
RefSeqiNP_001243804.1. NM_001256875.1.
NP_060571.1. NM_018101.3.
UniGeneiHs.524571.

Genome annotation databases

EnsembliENST00000327331; ENSP00000316121; ENSG00000134690.
ENST00000373055; ENSP00000362146; ENSG00000134690.
GeneIDi55143.
KEGGihsa:55143.
UCSCiuc001cbr.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS424.1.
RefSeqiNP_001243804.1. NM_001256875.1.
NP_060571.1. NM_018101.3.
UniGeneiHs.524571.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KDDNMR-A/B207-280[»]
2QFAX-ray1.40B15-76[»]
2RAWX-ray2.40B20-78[»]
2RAXX-ray3.30B/F/Y20-78[»]
ProteinModelPortaliQ53HL2.
SMRiQ53HL2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120446. 54 interactors.
DIPiDIP-37995N.
IntActiQ53HL2. 20 interactors.
MINTiMINT-4509527.
STRINGi9606.ENSP00000316121.

PTM databases

iPTMnetiQ53HL2.
PhosphoSitePlusiQ53HL2.

Polymorphism and mutation databases

BioMutaiCDCA8.
DMDMi110832774.

Proteomic databases

EPDiQ53HL2.
MaxQBiQ53HL2.
PaxDbiQ53HL2.
PeptideAtlasiQ53HL2.
PRIDEiQ53HL2.

Protocols and materials databases

DNASUi55143.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327331; ENSP00000316121; ENSG00000134690.
ENST00000373055; ENSP00000362146; ENSG00000134690.
GeneIDi55143.
KEGGihsa:55143.
UCSCiuc001cbr.5. human.

Organism-specific databases

CTDi55143.
DisGeNETi55143.
GeneCardsiCDCA8.
HGNCiHGNC:14629. CDCA8.
HPAiCAB040294.
HPA028120.
HPA028258.
HPA028783.
MIMi609977. gene.
neXtProtiNX_Q53HL2.
OpenTargetsiENSG00000134690.
PharmGKBiPA26281.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IICJ. Eukaryota.
ENOG4111N8R. LUCA.
GeneTreeiENSGT00390000011115.
HOGENOMiHOG000261628.
HOVERGENiHBG080103.
InParanoidiQ53HL2.
KOiK11514.
OMAiQIESDRQ.
OrthoDBiEOG091G167R.
PhylomeDBiQ53HL2.
TreeFamiTF101077.

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SIGNORiQ53HL2.

Miscellaneous databases

ChiTaRSiCDCA8. human.
EvolutionaryTraceiQ53HL2.
GeneWikiiCDCA8.
GenomeRNAii55143.
PROiQ53HL2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000134690.
CleanExiHS_CDCA8.
GenevisibleiQ53HL2. HS.

Family and domain databases

InterProiIPR018851. Borealin_N.
IPR018867. Cell_div_borealin.
[Graphical view]
PfamiPF10512. Borealin. 1 hit.
PF10444. Nbl1_Borealin_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBOREA_HUMAN
AccessioniPrimary (citable) accession number: Q53HL2
Secondary accession number(s): D3DPT4
, Q53HN1, Q96AM3, Q9NVW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: November 30, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.