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Q53HL2

- BOREA_HUMAN

UniProt

Q53HL2 - BOREA_HUMAN

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Protein

Borealin

Gene

CDCA8

Organism
Homo sapiens (Human)
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.4 Publications

GO - Biological processi

  1. chromosome organization Source: UniProtKB
  2. mitotic cell cycle Source: Reactome
  3. mitotic metaphase plate congression Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:14629. CDCA8.

Subcellular locationi

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.

GO - Cellular componenti

  1. chromocenter Source: Ensembl
  2. chromosome, centromeric region Source: UniProtKB
  3. chromosome passenger complex Source: UniProtKB
  4. cytosol Source: Reactome
  5. intercellular bridge Source: HPA
  6. midbody Source: FlyBase
  7. nucleolus Source: HPA
  8. nucleus Source: HPA
  9. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-19 and E-20. 1 Publication
Mutagenesisi19 – 191R → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-20. 1 Publication
Mutagenesisi20 – 201K → E: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-19. 1 Publication
Mutagenesisi26 – 261K → R: Fails to exhibit normal localization to the nucleolus in interphase depleted cells. 1 Publication
Mutagenesisi35 – 351R → E: Loss of binding to INCENP; when associated with Y-46. 1 Publication
Mutagenesisi46 – 461L → Y: Loss of binding to INCENP; when associated with E-35. 1 Publication
Mutagenesisi70 – 701W → E: Loss of binding to BIRC5; when associated with E-74. 1 Publication
Mutagenesisi74 – 741F → E: Loss of binding to BIRC5; when associated with E-70. 1 Publication
Mutagenesisi88 – 881T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-94; A-169 and A-230. 1 Publication
Mutagenesisi94 – 941T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-169 and A-230. 1 Publication
Mutagenesisi165 – 1651S → A: Results in reduction but not abolition of phosphorylation. 1 Publication
Mutagenesisi169 – 1691T → A: Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-94 and A-230. 1 Publication
Mutagenesisi219 – 2191S → D or K: No effect on the structure.
Mutagenesisi230 – 2301T → 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 Publication
Mutagenesisi230 – 2301T → D or K: Substantial loss of structure. 1 Publication
Mutagenesisi230 – 2301T → V: Decrease in AURKB activity and no effect on the structure. 1 Publication

Organism-specific databases

PharmGKBiPA26281.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 280280BorealinPRO_0000247075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881Phosphothreonine; by TTK1 Publication
Modified residuei94 – 941Phosphothreonine; by TTK1 Publication
Modified residuei106 – 1061Phosphothreonine3 Publications
Modified residuei110 – 1101Phosphoserine1 Publication
Modified residuei165 – 1651Phosphoserine; by AURKB1 Publication
Modified residuei169 – 1691Phosphothreonine; by TTK1 Publication
Modified residuei189 – 1891Phosphothreonine3 Publications
Modified residuei204 – 2041Phosphothreonine2 Publications
Modified residuei219 – 2191Phosphoserine6 Publications
Modified residuei224 – 2241Phosphoserine1 Publication
Modified residuei230 – 2301Phosphothreonine; by TTK1 Publication
Modified residuei238 – 2381Phosphoserine1 Publication
Modified residuei244 – 2441Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by TTK, essentially at Thr-88, Thr94, Thr-169 and Thr-230.9 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

MaxQBiQ53HL2.
PaxDbiQ53HL2.
PeptideAtlasiQ53HL2.
PRIDEiQ53HL2.

PTM databases

PhosphoSiteiQ53HL2.

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiQ53HL2.
CleanExiHS_CDCA8.
GenevestigatoriQ53HL2.

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 and AURKC. Interacts with BIRC5/survivin and INCENP; interaction is direct. Interacts with SENP3, UBE2I and RANBP2.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
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. 40 interactions.
DIPiDIP-37995N.
IntActiQ53HL2. 12 interactions.
MINTiMINT-4509527.
STRINGi9606.ENSP00000316121.

Structurei

Secondary structure

1
280
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 6045
Helixi63 – 664
Helixi70 – 756
Beta strandi233 – 2375
Turni243 – 2453
Helixi248 – 2525
Helixi256 – 27520

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KDDNMR-A/B207-280[»]
2QFAX-ray1.40B15-76[»]
2RAWX-ray2.40B20-78[»]
2RAXX-ray3.30B/F/Y20-78[»]
ProteinModelPortaliQ53HL2.
SMRiQ53HL2. Positions 15-76, 224-280.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53HL2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 140140Required for interaction with SENP3Add
BLAST
Regioni1 – 8888Required for centromere localizationAdd
BLAST
Regioni1 – 5858Required for interaction with INCENPAdd
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 cytokinesisAdd
BLAST
Regioni20 – 7859Required for interaction with INCENP and BIRC5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi125 – 1339Poly-Glu

Domaini

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

Sequence similaritiesi

Belongs to the borealin family.Curated

Phylogenomic databases

eggNOGiNOG39975.
GeneTreeiENSGT00390000011115.
HOGENOMiHOG000261628.
HOVERGENiHBG080103.
InParanoidiQ53HL2.
KOiK11514.
OMAiQIESDRQ.
OrthoDBiEOG7ZPNKN.
PhylomeDBiQ53HL2.
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]

Sequencei

Sequence statusi: Complete.

Q53HL2 [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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551I → M in BAD96288. 1 PublicationCurated
Sequence conflicti213 – 2131N → D in BAD96269. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121K → N.1 Publication
Corresponds to variant rs17851453 [ dbSNP | Ensembl ].
VAR_027063

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.4. human.

Polymorphism databases

DMDMi110832774.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS424.1.
RefSeqi NP_001243804.1. NM_001256875.1.
NP_060571.1. NM_018101.3.
UniGenei Hs.524571.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q53HL2.
SMRi Q53HL2. Positions 15-76, 224-280.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120446. 40 interactions.
DIPi DIP-37995N.
IntActi Q53HL2. 12 interactions.
MINTi MINT-4509527.
STRINGi 9606.ENSP00000316121.

PTM databases

PhosphoSitei Q53HL2.

Polymorphism databases

DMDMi 110832774.

Proteomic databases

MaxQBi Q53HL2.
PaxDbi Q53HL2.
PeptideAtlasi Q53HL2.
PRIDEi Q53HL2.

Protocols and materials databases

DNASUi 55143.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000327331 ; ENSP00000316121 ; ENSG00000134690 .
ENST00000373055 ; ENSP00000362146 ; ENSG00000134690 .
GeneIDi 55143.
KEGGi hsa:55143.
UCSCi uc001cbr.4. human.

Organism-specific databases

CTDi 55143.
GeneCardsi GC01P038158.
HGNCi HGNC:14629. CDCA8.
HPAi CAB040294.
HPA028120.
HPA028258.
HPA028783.
MIMi 609977. gene.
neXtProti NX_Q53HL2.
PharmGKBi PA26281.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39975.
GeneTreei ENSGT00390000011115.
HOGENOMi HOG000261628.
HOVERGENi HBG080103.
InParanoidi Q53HL2.
KOi K11514.
OMAi QIESDRQ.
OrthoDBi EOG7ZPNKN.
PhylomeDBi Q53HL2.
TreeFami TF101077.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

EvolutionaryTracei Q53HL2.
GeneWikii CDCA8.
GenomeRNAii 55143.
NextBioi 58844.
PROi Q53HL2.
SOURCEi Search...

Gene expression databases

Bgeei Q53HL2.
CleanExi HS_CDCA8.
Genevestigatori Q53HL2.

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. "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.
    , 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. 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. 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. 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. 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.

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: October 29, 2014
This is version 95 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

External Data

Dasty 3