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Q53HL2

- BOREA_HUMAN

UniProt

Q53HL2 - BOREA_HUMAN

Protein

Borealin

Gene

CDCA8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (25 Jul 2006)
      Previous versions | rss
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    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 - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromosome organization Source: UniProtKB
    2. mitotic cell cycle Source: Reactome
    3. mitotic metaphase Source: UniProtKB
    4. mitotic nuclear division Source: UniProtKB-KW

    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
    10. spindle Source: UniProtKB-SubCell

    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 TTK2 Publications
    Modified residuei94 – 941Phosphothreonine; by TTK2 Publications
    Modified residuei106 – 1061Phosphothreonine4 Publications
    Modified residuei110 – 1101Phosphoserine2 Publications
    Modified residuei165 – 1651Phosphoserine; by AURKB2 Publications
    Modified residuei169 – 1691Phosphothreonine; by TTK2 Publications
    Modified residuei189 – 1891Phosphothreonine4 Publications
    Modified residuei204 – 2041Phosphothreonine3 Publications
    Modified residuei219 – 2191Phosphoserine7 Publications
    Modified residuei224 – 2241Phosphoserine2 Publications
    Modified residuei230 – 2301Phosphothreonine; by TTK2 Publications
    Modified residuei238 – 2381Phosphoserine2 Publications
    Modified residuei244 – 2441Phosphoserine2 Publications

    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. 24 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.
    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.

    Q53HL2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPRKGSSRV AKTNSLRRRK LASFLKDFDR EVEIRIKQIE SDRQNLLKEV    50
    DNLYNIEILR LPKALREMNW LDYFALGGNK QALEEAATAD LDITEINKLT 100
    AEAIQTPLKS AKTRKVIQVD EMIVEEEEEE ENERKNLQTA RVKRCPPSKK 150
    RTQSIQGKGK GKRSSRANTV TPAVGRLEVS MVKPTPGLTP RFDSRVFKTP 200
    GLRTPAAGER IYNISGNGSP LADSKEIFLT VPVGGGESLR LLASDLQRHS 250
    IAQLDPEALG NIKKLSNRLA QICSSIRTHK 280
    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. 24 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.
    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

    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 1, 2014
    This is version 94 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