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Q9NQS7

- INCE_HUMAN

UniProt

Q9NQS7 - INCE_HUMAN

Protein

Inner centromere protein

Gene

INCENP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (04 Nov 2008)
      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. Probably acts through association with AURKB or AURKC. Seems to bind directly to microtubules. Controls the kinetochore localization of BUB1.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Biological processi

    Cell cycle, Cell division, Chromosome partition, 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:
    Inner centromere protein
    Gene namesi
    Name:INCENP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:6058. INCENP.

    Subcellular locationi

    Chromosomecentromere. Cytoplasmcytoskeletonspindle. Nucleus. Chromosomecentromerekinetochore
    Note: Localizes to inner kinetochore. 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 AURKB at mitotic chromosomes.

    GO - Cellular componenti

    1. central element Source: Ensembl
    2. chromocenter Source: Ensembl
    3. chromosome, centromeric region Source: UniProtKB
    4. condensed chromosome kinetochore Source: UniProtKB-SubCell
    5. cytosol Source: Reactome
    6. kinetochore Source: UniProtKB
    7. lateral element Source: Ensembl
    8. microtubule Source: UniProtKB-KW
    9. midbody Source: Ensembl
    10. pericentric heterochromatin Source: UniProtKB
    11. protein complex Source: UniProtKB
    12. spindle Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 221F → R: Loss of binding to CDCA8 and BIRC5; when associated with R-34. 1 Publication
    Mutagenesisi34 – 341L → R: Loss of binding to CDCA8 and BIRC5; when associated with R-22. 1 Publication
    Mutagenesisi35 – 351E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-36; R-39 and R-40. 1 Publication
    Mutagenesisi36 – 361E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-39 and R-40. 1 Publication
    Mutagenesisi39 – 391E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-36 and R-40. 1 Publication
    Mutagenesisi40 – 401E → R: Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-36 and R-39. 1 Publication
    Mutagenesisi169 – 1691V → E: Abolishes interaction with CBX5. 1 Publication
    Mutagenesisi171 – 1711I → E: Abolishes interaction with CBX5 and AURKB. 1 Publication

    Organism-specific databases

    PharmGKBiPA29868.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 918918Inner centromere proteinPRO_0000084201Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei119 – 1191Phosphoserine2 Publications
    Modified residuei143 – 1431Phosphoserine1 Publication
    Modified residuei148 – 1481Phosphoserine1 Publication
    Modified residuei195 – 1951Phosphothreonine1 Publication
    Modified residuei197 – 1971Phosphoserine1 Publication
    Modified residuei199 – 1991Phosphothreonine1 Publication
    Modified residuei213 – 2131Phosphothreonine1 Publication
    Modified residuei214 – 2141Phosphoserine1 Publication
    Modified residuei239 – 2391Phosphothreonine4 Publications
    Modified residuei263 – 2631Phosphoserine5 Publications
    Modified residuei269 – 2691Phosphoserine1 Publication
    Modified residuei275 – 2751Phosphoserine3 Publications
    Modified residuei292 – 2921Phosphothreonine2 Publications
    Modified residuei296 – 2961Phosphoserine1 Publication
    Modified residuei306 – 3061Phosphoserine4 Publications
    Modified residuei312 – 3121Phosphoserine2 Publications
    Modified residuei314 – 3141Phosphoserine4 Publications
    Modified residuei330 – 3301Phosphoserine1 Publication
    Modified residuei400 – 4001Phosphoserine1 Publication
    Modified residuei406 – 4061Phosphothreonine1 Publication
    Modified residuei446 – 4461Phosphoserine1 Publication
    Modified residuei476 – 4761Phosphoserine1 Publication
    Modified residuei510 – 5101Phosphoserine1 Publication
    Modified residuei514 – 5141Phosphoserine1 Publication
    Modified residuei828 – 8281Phosphoserine4 Publications
    Modified residuei831 – 8311Phosphoserine2 Publications
    Modified residuei832 – 8321Phosphothreonine2 Publications
    Modified residuei892 – 8921Phosphothreonine; by AURKB1 Publication
    Modified residuei893 – 8931Phosphoserine; by AURKB1 Publication
    Modified residuei894 – 8941Phosphoserine; by AURKB2 Publications
    Modified residuei899 – 8991Phosphoserine5 Publications
    Modified residuei914 – 9141Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation by AURKB at its C-terminal part is important for AURKB activation by INCENP.9 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NQS7.
    PaxDbiQ9NQS7.
    PRIDEiQ9NQS7.

    PTM databases

    PhosphoSiteiQ9NQS7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NQS7.
    BgeeiQ9NQS7.
    CleanExiHS_INCENP.
    GenevestigatoriQ9NQS7.

    Organism-specific databases

    HPAiCAB013292.
    HPA054857.

    Interactioni

    Subunit structurei

    Homodimer or heterodimer. Interacts with H2AFZ By similarity. Interacts with CBX3. Interacts with tubulin beta chain. Interacts with AURKB and AURKC. Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB and AURKC. Interacts with EVI5. Interacts with CDCA8 and BIRC5; interaction is direct. Interacts with CBX5; POGZ and INCENP compete for interaction with CBX5. Interacts with POGZ. Interacts with JTB.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AURKBQ96GD47EBI-307907,EBI-624291
    BIRC5O1539210EBI-307907,EBI-518823
    CBX5P459736EBI-307907,EBI-78219
    CDCA8Q53HL24EBI-307907,EBI-979174

    Protein-protein interaction databases

    BioGridi109831. 17 interactions.
    DIPiDIP-31304N.
    IntActiQ9NQS7. 10 interactions.
    MINTiMINT-1488062.
    STRINGi9606.ENSP00000378295.

    Structurei

    Secondary structure

    1
    918
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 103
    Helixi11 – 2818
    Helixi30 – 4516
    Helixi844 – 8463
    Helixi848 – 86013
    Helixi865 – 8695
    Turni878 – 8803

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QFAX-ray1.40C1-47[»]
    4AF3X-ray2.75D835-903[»]
    ProteinModelPortaliQ9NQS7.
    SMRiQ9NQS7. Positions 3-47, 840-882.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NQS7.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili528 – 791264Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the INCENP family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG327385.
    HOGENOMiHOG000113069.
    HOVERGENiHBG006157.
    InParanoidiQ9NQS7.
    KOiK11515.
    OMAiLCDQKLM.
    OrthoDBiEOG71VSWZ.
    PhylomeDBiQ9NQS7.
    TreeFamiTF101172.

    Family and domain databases

    InterProiIPR022006. INCENP_N.
    IPR005635. Inner_centromere_prot_ARK-bd.
    [Graphical view]
    PfamiPF03941. INCENP_ARK-bind. 1 hit.
    PF12178. INCENP_N. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NQS7-1) [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

    MGTTAPGPIH LLELCDQKLM EFLCNMDNKD LVWLEEIQEE AERMFTREFS    50
    KEPELMPKTP SQKNRRKKRR ISYVQDENRD PIRRRLSRRK SRSSQLSSRR 100
    LRSKDSVEKL ATVVGENGSV LRRVTRAAAA AAAATMALAA PSSPTPESPT 150
    MLTKKPEDNH TQCQLVPVVE IGISERQNAE QHVTQLMSTE PLPRTLSPTP 200
    ASATAPTSQG IPTSDEESTP KKSKARILES ITVSSLMATP QDPKGQGVGT 250
    GRSASKLRIA QVSPGPRDSP AFPDSPWRER VLAPILPDNF STPTGSRTDS 300
    QSVRHSPIAP SSPSPQVLAQ KYSLVAKQES VVRRASRRLA KKTAEEPAAS 350
    GRIICHSYLE RLLNVEVPQK VGSEQKEPPE EAEPVAAAEP EVPENNGNNS 400
    WPHNDTEIAN STPNPKPAAS SPETPSAGQQ EAKTDQADGP REPPQSARRK 450
    RSYKQAVSEL DEEQHLEDEE LQPPRSKTPS SPCPASKVVR PLRTFLHTVQ 500
    RNQMLMTPTS APRSVMKSFI KRNTPLRMDP KCSFVEKERQ RLENLRRKEE 550
    AEQLRRQKVE EDKRRRLEEV KLKREERLRK VLQARERVEQ MKEEKKKQIE 600
    QKFAQIDEKT EKAKEERLAE EKAKKKAAAK KMEEVEARRK QEEEARRLRW 650
    LQQEEEERRH QELLQKKKEE EQERLRKAAE AKRLAEQREQ ERREQERREQ 700
    ERREQERREQ ERREQERQLA EQERRREQER LQAERELQER EKALRLQKEQ 750
    LQRELEEKKK KEEQQRLAER QLQEEQEKKA KEAAGASKAL NVTVDVQSPA 800
    CTSYQMTPQG HRAPPKINPD NYGMDLNSDD STDDEAHPRK PIPTWARGTP 850
    LSQAIIHQYY HPPNLLELFG TILPLDLEDI FKKSKPRYHK RTSSAVWNSP 900
    PLQGARVPSS LAYSLKKH 918
    Length:918
    Mass (Da):105,429
    Last modified:November 4, 2008 - v3
    Checksum:i644D081DCC9035E8
    GO
    Isoform 2 (identifier: Q9NQS7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         532-535: Missing.

    Show »
    Length:914
    Mass (Da):104,992
    Checksum:i6E8C5E65A9C918E8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti715 – 7151Q → QERREQ in AAF87584. (PubMed:11453556)Curated
    Sequence conflicti804 – 8063YQM → SPI in AAF87584. (PubMed:11453556)Curated
    Sequence conflicti812 – 8121R → K in AAF87584. (PubMed:11453556)Curated
    Sequence conflicti816 – 8161K → Q in AAF87584. (PubMed:11453556)Curated
    Sequence conflicti820 – 8201D → H in AAF87584. (PubMed:11453556)Curated
    Sequence conflicti861 – 8611H → Q in AAF87584. (PubMed:11453556)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21G → V.
    Corresponds to variant rs1792947 [ dbSNP | Ensembl ].
    VAR_047127
    Natural varianti100 – 1001R → H.
    Corresponds to variant rs12281503 [ dbSNP | Ensembl ].
    VAR_047128
    Natural varianti137 – 1371A → V.
    Corresponds to variant rs34441559 [ dbSNP | Ensembl ].
    VAR_047129
    Natural varianti506 – 5061M → T.
    Corresponds to variant rs2277283 [ dbSNP | Ensembl ].
    VAR_047130
    Natural varianti644 – 6441E → D.3 Publications
    Corresponds to variant rs7129085 [ dbSNP | Ensembl ].
    VAR_047131

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei532 – 5354Missing in isoform 2. 1 PublicationVSP_035651

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF282265 mRNA. Translation: AAF87584.1.
    AY714053 mRNA. Translation: AAU04398.1.
    AP002793 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74004.1.
    BC098576 mRNA. Translation: AAH98576.1.
    CCDSiCCDS31582.1. [Q9NQS7-2]
    CCDS44624.1. [Q9NQS7-1]
    RefSeqiNP_001035784.1. NM_001040694.1. [Q9NQS7-1]
    NP_064623.2. NM_020238.2. [Q9NQS7-2]
    UniGeneiHs.142179.

    Genome annotation databases

    EnsembliENST00000278849; ENSP00000278849; ENSG00000149503. [Q9NQS7-2]
    ENST00000394818; ENSP00000378295; ENSG00000149503. [Q9NQS7-1]
    GeneIDi3619.
    KEGGihsa:3619.
    UCSCiuc001nsw.1. human. [Q9NQS7-1]
    uc001nsx.1. human. [Q9NQS7-2]

    Polymorphism databases

    DMDMi212276501.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF282265 mRNA. Translation: AAF87584.1 .
    AY714053 mRNA. Translation: AAU04398.1 .
    AP002793 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW74004.1 .
    BC098576 mRNA. Translation: AAH98576.1 .
    CCDSi CCDS31582.1. [Q9NQS7-2 ]
    CCDS44624.1. [Q9NQS7-1 ]
    RefSeqi NP_001035784.1. NM_001040694.1. [Q9NQS7-1 ]
    NP_064623.2. NM_020238.2. [Q9NQS7-2 ]
    UniGenei Hs.142179.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QFA X-ray 1.40 C 1-47 [» ]
    4AF3 X-ray 2.75 D 835-903 [» ]
    ProteinModelPortali Q9NQS7.
    SMRi Q9NQS7. Positions 3-47, 840-882.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109831. 17 interactions.
    DIPi DIP-31304N.
    IntActi Q9NQS7. 10 interactions.
    MINTi MINT-1488062.
    STRINGi 9606.ENSP00000378295.

    Chemistry

    BindingDBi Q9NQS7.

    PTM databases

    PhosphoSitei Q9NQS7.

    Polymorphism databases

    DMDMi 212276501.

    Proteomic databases

    MaxQBi Q9NQS7.
    PaxDbi Q9NQS7.
    PRIDEi Q9NQS7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000278849 ; ENSP00000278849 ; ENSG00000149503 . [Q9NQS7-2 ]
    ENST00000394818 ; ENSP00000378295 ; ENSG00000149503 . [Q9NQS7-1 ]
    GeneIDi 3619.
    KEGGi hsa:3619.
    UCSCi uc001nsw.1. human. [Q9NQS7-1 ]
    uc001nsx.1. human. [Q9NQS7-2 ]

    Organism-specific databases

    CTDi 3619.
    GeneCardsi GC11P061891.
    H-InvDB HIX0009706.
    HGNCi HGNC:6058. INCENP.
    HPAi CAB013292.
    HPA054857.
    MIMi 604411. gene.
    neXtProti NX_Q9NQS7.
    PharmGKBi PA29868.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327385.
    HOGENOMi HOG000113069.
    HOVERGENi HBG006157.
    InParanoidi Q9NQS7.
    KOi K11515.
    OMAi LCDQKLM.
    OrthoDBi EOG71VSWZ.
    PhylomeDBi Q9NQS7.
    TreeFami TF101172.

    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 Q9NQS7.
    GeneWikii INCENP.
    GenomeRNAii 3619.
    NextBioi 14153.
    PROi Q9NQS7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NQS7.
    Bgeei Q9NQS7.
    CleanExi HS_INCENP.
    Genevestigatori Q9NQS7.

    Family and domain databases

    InterProi IPR022006. INCENP_N.
    IPR005635. Inner_centromere_prot_ARK-bd.
    [Graphical view ]
    Pfami PF03941. INCENP_ARK-bind. 1 hit.
    PF12178. INCENP_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human INCENP colocalizes with the Aurora-B/AIRK2 kinase on chromosomes and is overexpressed in tumour cells."
      Adams R.R., Eckley D.M., Vagnarelli P., Wheatley S.P., Gerloff D.L., Mackay A.M., Svingen P.A., Kaufmann S.H., Earnshaw W.C.
      Chromosoma 110:65-74(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, VARIANT ASP-644.
      Tissue: Cervix carcinoma.
    2. "Direct association with inner centromere protein (INCENP) activates the novel chromosomal passenger protein, Aurora-C."
      Li X., Sakashita G., Matsuzaki H., Sugimoto K., Kimura K., Hanaoka F., Taniguchi H., Furukawa K., Urano T.
      J. Biol. Chem. 279:47201-47211(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH AURKB AND AURKC, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-195, VARIANT ASP-644.
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 1), VARIANT ASP-644.
      Tissue: Lung.
    6. "INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1."
      Ainsztein A.M., Kandels-Lewis S.E., Mackay A.M., Earnshaw W.C.
      J. Cell Biol. 143:1763-1774(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBX3.
    7. "INCENP binds directly to tubulin and requires dynamic microtubules to target to the cleavage furrow."
      Wheatley S.P., Kandels-Lewis S.E., Adams R.R., Ainsztein A.M., Earnshaw W.C.
      Exp. Cell Res. 262:122-127(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TUBULIN BETA CHAIN.
    8. "Exploring the functional interactions between Aurora B, INCENP, and survivin in mitosis."
      Honda R., Korner R., Nigg E.A.
      Mol. Biol. Cell 14:3325-3341(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CPC COMPLEX, FUNCTION OF THE CPC COMPLEX, INDUCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-892; SER-893 AND SER-894.
    9. "Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to inner centromere protein (INCENP) in vivo."
      Wheatley S.P., Henzing A.J., Dodson H., Khaled W., Earnshaw W.C.
      J. Biol. Chem. 279:5655-5660(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BIRC5.
    10. "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: INTERACTION WITH CDCA8.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "EVI5 protein associates with the INCENP-aurora B kinase-survivin chromosomal passenger complex and is involved in the completion of cytokinesis."
      Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.
      Exp. Cell Res. 312:2325-2335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EVI5.
    13. "Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is required for the kinetochore localization of Plk1."
      Qi W., Tang Z., Yu H.
      Mol. Biol. Cell 17:3705-3716(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-239; SER-263; SER-269; SER-275; SER-306; SER-400; THR-406; SER-476 AND SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-148; THR-239; THR-292; SER-296; SER-306; SER-312; SER-314; SER-446; SER-510; SER-514; SER-828; SER-831; THR-832; SER-894; SER-899 AND SER-914, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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].
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-828 AND SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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 SER-197; THR-199; THR-213; SER-214; THR-239; SER-306; SER-314; SER-828; SER-831; THR-832 AND SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation."
      Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C.
      Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBX5; POGZ AND AURKB, MUTAGENESIS OF VAL-169 AND ILE-171.
    21. "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 SER-119; SER-143; THR-239; SER-263; SER-275; THR-292; SER-312; SER-314; SER-330 AND SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "PAR, a protein involved in the cell cycle, is functionally related to chromosomal passenger proteins."
      Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.
      Int. J. Oncol. 38:777-785(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH JTB.
    23. "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-263; SER-306; SER-314 AND SER-828, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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 3-46, INTERACTION WITH CDCA8 AND BIRC5, MUTAGENESIS OF PHE-22; LEU-34; GLU-35; GLU-36; GLU-39 AND GLU-40.

    Entry informationi

    Entry nameiINCE_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQS7
    Secondary accession number(s): A8MQD2, Q5Y192
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 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

    Caution

    PubMed:11139336 experiments have been carried out partly in chicken and partly in human.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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