Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9WU62

- INCE_MOUSE

UniProt

Q9WU62 - INCE_MOUSE

Protein

Inner centromere protein

Gene

Incenp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (23 Apr 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 By similarity.By similarity

    GO - Biological processi

    1. chromosome segregation Source: UniProtKB
    2. cytokinesis Source: UniProtKB
    3. mitotic nuclear division Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, Chromosome partition, Mitosis

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inner centromere protein
    Gene namesi
    Name:Incenp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1313288. Incenp.

    Subcellular locationi

    Chromosomecentromere 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication. Nucleus 1 Publication. Chromosomecentromerekinetochore 1 Publication
    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. Localized at synaptonemal complex central element from zygotene up to late pachytene when it begins to relocalize to heterochromatic chromocenters. Colocalizes with AURKB at a connecting strand traversing the centromere region and joining sister kinetochores, in metaphase II centromeres. This strand disappears at the metaphase II/anaphase II transition and relocalizes to the spindle midzone.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 880880Inner centromere proteinPRO_0000084202Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei142 – 1421PhosphoserineBy similarity
    Modified residuei147 – 1471PhosphoserineBy similarity
    Modified residuei189 – 1891PhosphothreonineBy similarity
    Modified residuei190 – 1901PhosphoserineBy similarity
    Modified residuei215 – 2151Phosphothreonine2 Publications
    Modified residuei218 – 2181Phosphoserine2 Publications
    Modified residuei239 – 2391PhosphoserineBy similarity
    Modified residuei245 – 2451PhosphoserineBy similarity
    Modified residuei251 – 2511PhosphoserineBy similarity
    Modified residuei270 – 2701PhosphothreonineBy similarity
    Modified residuei284 – 2841PhosphoserineBy similarity
    Modified residuei290 – 2901PhosphoserineBy similarity
    Modified residuei376 – 3761PhosphoserineBy similarity
    Modified residuei382 – 3821PhosphothreonineBy similarity
    Modified residuei421 – 4211PhosphoserineBy similarity
    Modified residuei488 – 4881PhosphoserineBy similarity
    Modified residuei796 – 7961Phosphoserine2 Publications
    Modified residuei799 – 7991Phosphoserine2 Publications
    Modified residuei800 – 8001Phosphothreonine2 Publications
    Modified residuei860 – 8601Phosphothreonine; by AURKBBy similarity
    Modified residuei861 – 8611Phosphoserine; by AURKBBy similarity
    Modified residuei862 – 8621Phosphoserine; by AURKBBy similarity
    Modified residuei867 – 8671PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation by AURKB at its C-terminal part is important for AURKB activation by INCENP.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9WU62.

    PTM databases

    PhosphoSiteiQ9WU62.

    Expressioni

    Gene expression databases

    BgeeiQ9WU62.
    CleanExiMM_INCENP.
    GenevestigatoriQ9WU62.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi200760. 6 interactions.
    DIPiDIP-56678N.
    IntActiQ9WU62. 8 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WU62.
    SMRiQ9WU62. Positions 3-47, 581-752, 808-850.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili506 – 759254Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the INCENP family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG327385.
    GeneTreeiENSGT00730000111073.
    HOGENOMiHOG000113069.
    HOVERGENiHBG006157.
    InParanoidiQ9WU62.
    KOiK11515.
    OMAiLCDQKLM.
    OrthoDBiEOG71VSWZ.
    PhylomeDBiQ9WU62.
    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: Q9WU62-1) [UniParc]FASTAAdd to Basket

    Also known as: B

    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

    MGTTAPGPIC LLDLCDQKLL DFVCNVDNKD FMWLKEIEEE AERMFIREFS    50
    NEPELMPKTP SQKNRRKKRR VSNIQDENRD PVRKRLSRRK SRSSQVGTRH 100
    LRSKPVTIVE ENGFPVLQRI TRATAAAAAA AAAASVASAS SSSTAGSPTV 150
    LTKKAVVEIS TSERLSAELQ LTKLKGSLPP SPVSQGTLTS EEELTPKKSE 200
    AGKLDSVTVN SLKATPQSPK NRGVGEGRSV SKLKIARASW GLQDSPGSTD 250
    SPWQERVLSP ILLNNILPTT AKSPLGNIRS VRRSLISQDS QVPLASKYNL 300
    VAKQENGSRR SSRRIAKKAG KEPEASARII CHSYLERLLN VEVPQNVGLE 350
    QEPVEVAEPE EAEEEQEVSK NSGCPSKPRS ATKIAISTPT SKPAAAGQTT 400
    TVEEQEAELD QTDGHREPPQ SVRRKRSYKQ AISEPDEEQL EDEELQPCQN 450
    KTPSPPCPAN KVVRPLRTFL HTVQKNQMLM TPTLASRSSV MKSFIKRNTP 500
    LRVDPKCSFV EKERQRLESL RRKEEAEQRR RQKVEEDKRR RLEEVKLKRE 550
    ERLRKVLQAR ERVEQMKEEK KKQIEQKFAQ IDEKTEKAKE ERLAEKAKKK 600
    ATAKKMEEVE ARRKQEEEAR RLRWLQQEEE ERRHQEMLQR KKEEEQERRK 650
    AAEARRLAEQ REQERRREQE RREQERREQE RREQERKEQE RREQEQERLR 700
    AKREMQEREK ALRLQKERLQ KELEEKKRKE EQQRLAEQQL QEEQAKKAKE 750
    VAAARKVLNM TVDVQSPVCT SYQMTPQGPK SIPKISVDDY GMDLNSDDST 800
    DDESHPRKPI PSWAKGTQLS QAIVHQYYHP PNILELFGSI LPLDLEDIFK 850
    KRKTRYHKRT SSAVWNSPPL KATMVPSSGD 880

    Note: Major isoform in thymic lymphoma 3SB cells. Fourfold more abundant than isoform 2.

    Length:880
    Mass (Da):101,209
    Last modified:April 23, 2003 - v2
    Checksum:i92169889A921FEFC
    GO
    Isoform 2 (identifier: Q9WU62-2) [UniParc]FASTAAdd to Basket

    Also known as: A

    The sequence of this isoform differs from the canonical sequence as follows:
         507-510: Missing.

    Note: Minor isoform in thymic lymphoma 3SB cells.

    Show »
    Length:876
    Mass (Da):100,772
    Checksum:i836922856F05C81E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti397 – 3971G → S in AAD32094. (PubMed:10087305)Curated
    Sequence conflicti412 – 4121T → I in AAH52414. (PubMed:15489334)Curated
    Sequence conflicti448 – 4481C → F in AAD32094. (PubMed:10087305)Curated
    Sequence conflicti687 – 6871K → R in AAD32094. (PubMed:10087305)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei507 – 5104Missing in isoform 2. 2 PublicationsVSP_007233

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF117610 mRNA. Translation: AAD32094.1.
    AB100432 mRNA. Translation: BAC55879.1.
    AB100433 mRNA. Translation: BAC55880.1.
    AK081841 mRNA. Translation: BAC38346.1.
    AK088627 mRNA. Translation: BAC40462.1.
    BC037011 mRNA. Translation: AAH37011.1.
    BC052414 mRNA. Translation: AAH52414.1.
    CCDSiCCDS37912.1. [Q9WU62-2]
    RefSeqiNP_057901.2. NM_016692.3. [Q9WU62-2]
    XP_006526775.1. XM_006526712.1. [Q9WU62-1]
    UniGeneiMm.29755.

    Genome annotation databases

    EnsembliENSMUST00000025562; ENSMUSP00000025562; ENSMUSG00000024660. [Q9WU62-2]
    GeneIDi16319.
    KEGGimmu:16319.
    UCSCiuc008gor.2. mouse. [Q9WU62-1]
    uc008gos.2. mouse. [Q9WU62-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF117610 mRNA. Translation: AAD32094.1 .
    AB100432 mRNA. Translation: BAC55879.1 .
    AB100433 mRNA. Translation: BAC55880.1 .
    AK081841 mRNA. Translation: BAC38346.1 .
    AK088627 mRNA. Translation: BAC40462.1 .
    BC037011 mRNA. Translation: AAH37011.1 .
    BC052414 mRNA. Translation: AAH52414.1 .
    CCDSi CCDS37912.1. [Q9WU62-2 ]
    RefSeqi NP_057901.2. NM_016692.3. [Q9WU62-2 ]
    XP_006526775.1. XM_006526712.1. [Q9WU62-1 ]
    UniGenei Mm.29755.

    3D structure databases

    ProteinModelPortali Q9WU62.
    SMRi Q9WU62. Positions 3-47, 581-752, 808-850.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200760. 6 interactions.
    DIPi DIP-56678N.
    IntActi Q9WU62. 8 interactions.

    PTM databases

    PhosphoSitei Q9WU62.

    Proteomic databases

    PRIDEi Q9WU62.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025562 ; ENSMUSP00000025562 ; ENSMUSG00000024660 . [Q9WU62-2 ]
    GeneIDi 16319.
    KEGGi mmu:16319.
    UCSCi uc008gor.2. mouse. [Q9WU62-1 ]
    uc008gos.2. mouse. [Q9WU62-2 ]

    Organism-specific databases

    CTDi 3619.
    MGIi MGI:1313288. Incenp.

    Phylogenomic databases

    eggNOGi NOG327385.
    GeneTreei ENSGT00730000111073.
    HOGENOMi HOG000113069.
    HOVERGENi HBG006157.
    InParanoidi Q9WU62.
    KOi K11515.
    OMAi LCDQKLM.
    OrthoDBi EOG71VSWZ.
    PhylomeDBi Q9WU62.
    TreeFami TF101172.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi INCENP. mouse.
    NextBioi 289382.
    PROi Q9WU62.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9WU62.
    CleanExi MM_INCENP.
    Genevestigatori Q9WU62.

    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. "Cloning, expression, and promoter structure of a mammalian inner centromere protein (INCENP)."
      Saffery R., Irvine D.V., Kile B.T., Hudson D.F., Cutts S.M., Choo K.H.
      Mamm. Genome 10:415-418(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: 129.
    2. "Cloning of mouse inner centromere protein (INCENP) cDNAs."
      Katayama H., Terada Y., Tatsuka M.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Thymus.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J and NOD.
      Tissue: Head and Thymus.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6 and FVB/N.
    5. "Pericentric heterochromatin becomes enriched with H2A.Z during early mammalian development."
      Rangasamy D., Berven L., Ridgway P., Tremethick D.J.
      EMBO J. 22:1599-1607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH H2AFZ.
    6. "Dynamic relocalization of the chromosomal passenger complex proteins inner centromere protein (INCENP) and aurora-B kinase during male mouse meiosis."
      Parra M.T., Viera A., Gomez R., Page J., Carmena M., Earnshaw W.C., Rufas J.S., Suja J.A.
      J. Cell Sci. 116:961-974(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis."
      Yasui Y., Urano T., Kawajiri A., Nagata K., Tatsuka M., Saya H., Furukawa K., Takahashi T., Izawa I., Inagaki M.
      J. Biol. Chem. 279:12997-13003(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY AURKB.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-215 AND SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-796; SER-799 AND THR-800, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiINCE_MOUSE
    AccessioniPrimary (citable) accession number: Q9WU62
    Secondary accession number(s): Q7TN28, Q8BGN4, Q8CGI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: April 23, 2003
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3