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Q8BT07

- CEP55_MOUSE

UniProt

Q8BT07 - CEP55_MOUSE

Protein

Centrosomal protein of 55 kDa

Gene

Cep55

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
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    Functioni

    Plays a role in mitotic exit and cytokinesis. Not required for microtubule nucleation. Recruits PDCD6IP and TSG101 to midbody during cytokinesis By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. mitotic cytokinesis Source: Ensembl
    2. mitotic nuclear division Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Centrosomal protein of 55 kDa
    Short name:
    Cep55
    Gene namesi
    Name:Cep55
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1921357. Cep55.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cleavage furrow By similarity. Midbody By similarity
    Note: Present at the centrosomes at interphase. A small portion is associated preferentially with the mother centriole, whereas the majority localizes to the pericentriolar material. During mitosis, loss of affinity for the centrosome at the onset of prophase and diffusion throughout the cell. Dissociation from the centrosome is phosphorylation-dependent. May remain localized at the centrosome during mitosis in certain cell types. Appears at the cleavage furrow in late anaphase and in the midbody in cytokinesis By similarity.By similarity

    GO - Cellular componenti

    1. centriole Source: UniProtKB-SubCell
    2. cleavage furrow Source: UniProtKB-SubCell
    3. intercellular bridge Source: MGI
    4. midbody Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 462462Centrosomal protein of 55 kDaPRO_0000238665Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei423 – 4231PhosphoserineBy similarity
    Modified residuei426 – 4261Phosphoserine1 Publication
    Modified residuei434 – 4341Phosphoserine; alternate1 Publication
    Modified residuei434 – 4341Phosphoserine; by PLK1; alternate1 Publication

    Post-translational modificationi

    There is a hierachy of phosphorylation, where both Ser-423 and Ser-426 are phosphorylated at the onset of mitosis, prior to Ser-434. Phosphorylation at Ser-423 and Ser-426 is required for dissociation from the centrosome at the G2/M boundary. Phosphorylation at the 3 sites, Ser-423, Ser-426 and Ser-434, is required for protein function at the final stages of cell division to complete cytokinesis successfully By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8BT07.
    PaxDbiQ8BT07.
    PRIDEiQ8BT07.

    PTM databases

    PhosphoSiteiQ8BT07.

    Expressioni

    Gene expression databases

    BgeeiQ8BT07.
    CleanExiMM_CEP55.
    GenevestigatoriQ8BT07.

    Interactioni

    Subunit structurei

    Homodimer. Interacts (phosphorylated on Ser-423 and Ser-426) with PLK1. Interacts with AKAP9; the interaction occurs in interphase and is lost upon mitotic entry. Interacts with PCNT; the interaction occurs in interphase and is lost upon mitotic entry. Interacts with PDCD6IP; the interaction is direct; CEP55 binds PDCD6IP in a 2:1 stoechiometry; PDCD6IP competes with TSG101 for the same binding site. Interacts with TSG101; TSG101 competes with PDCD6IP for the same binding site; interaction is required for cytokinesis. Interacts with MVB12A, VPS37B, VPS37C and VPS28 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Tex14Q7M6U311EBI-2552328,EBI-6674575

    Protein-protein interaction databases

    BioGridi216498. 16 interactions.
    IntActiQ8BT07. 22 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BT07.
    SMRiQ8BT07. Positions 167-208.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni157 – 23579Interaction with TSG101By similarityAdd
    BLAST
    Regioni160 – 21455Interaction with PDCD6IPBy similarityAdd
    BLAST
    Regioni354 – 462109Required for localization to the interphase centrosome and to the midbody during cytokinesisBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili50 – 400351Sequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG135886.
    GeneTreeiENSGT00510000047961.
    HOGENOMiHOG000111547.
    HOVERGENiHBG081092.
    InParanoidiQ8BT07.
    KOiK16456.
    OMAiINISEVW.
    OrthoDBiEOG7H4DTJ.
    PhylomeDBiQ8BT07.
    TreeFamiTF331107.

    Family and domain databases

    InterProiIPR022008. EABR.
    [Graphical view]
    PfamiPF12180. EABR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BT07-1) [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

    MSSRSPKDLI KSKWGSRPSS SKSDTALEKF KGEIAAFKTS LDEITSGKGK    50
    MAEKGRSRLL EKIQVLEAER EKNVYYLLEK DKEIQRLKDH LRSRYSSSSL 100
    FEQLEEKTKE CEKKQQLLES LSKETDVLKN QLSATTKRLS ELESKASTLH 150
    LSQSMPANCF NSSMNSIHEK EMQLKDALEK NQQWLVYDQQ REAYVKGLLA 200
    KIFELEKRTE TAAASLTQQM KKIESEGYLQ VEKQKYDHLL ENAKKDLEVE 250
    RQAVTQLRLE LDEFRRKYEE ARKEVEDLNQ LLSSQRKADI QHLEEDKQKT 300
    ERIQKLREES SIFKGKLEEE RKRSEELLSQ VRILYDSLLK HQEEQARVAL 350
    LEQQMQACTL DFENEKLDRQ NMQHQLYVIL KELRKAKSQI TQLESLKQLH 400
    GFTITEQPFP LQREPESRVK ATSPKSPSAA LNDSLVECPK CSVQYPATEH 450
    RDLLVHVEYC MK 462
    Length:462
    Mass (Da):53,930
    Last modified:May 30, 2006 - v2
    Checksum:i5D2308BFCEADA08B
    GO
    Isoform 2 (identifier: Q8BT07-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         397-397: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:461
    Mass (Da):53,802
    Checksum:iC0816F19989B4FA1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti70 – 701R → G in BAC40417. (PubMed:16141072)Curated
    Sequence conflicti106 – 1061E → K in BAC40417. (PubMed:16141072)Curated
    Sequence conflicti157 – 1571A → P in BAC25819. (PubMed:16141072)Curated
    Sequence conflicti253 – 2531A → T in AAH26966. (PubMed:15489334)Curated
    Sequence conflicti259 – 2591L → V in AAH26966. (PubMed:15489334)Curated
    Sequence conflicti300 – 3001T → M in AAH26966. (PubMed:15489334)Curated
    Sequence conflicti406 – 4061E → D in BAC25819. (PubMed:16141072)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551G → D.2 Publications

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei397 – 3971Missing in isoform 2. 1 PublicationVSP_018630

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004655 mRNA. Translation: BAB23446.1.
    AK028216 mRNA. Translation: BAC25819.1.
    AK088548 mRNA. Translation: BAC40417.1.
    BC026966 mRNA. Translation: AAH26966.1.
    BC031396 mRNA. Translation: AAH31396.1.
    CCDSiCCDS29782.1. [Q8BT07-2]
    CCDS50429.1. [Q8BT07-1]
    RefSeqiNP_001157834.1. NM_001164362.1. [Q8BT07-1]
    NP_082569.1. NM_028293.1. [Q8BT07-1]
    NP_083036.2. NM_028760.2. [Q8BT07-2]
    XP_006527459.1. XM_006527396.1. [Q8BT07-1]
    XP_006527460.1. XM_006527397.1. [Q8BT07-1]
    XP_006527461.1. XM_006527398.1. [Q8BT07-1]
    XP_006527462.1. XM_006527399.1. [Q8BT07-1]
    XP_006527463.1. XM_006527400.1. [Q8BT07-1]
    XP_006527464.1. XM_006527401.1. [Q8BT07-1]
    UniGeneiMm.9916.

    Genome annotation databases

    EnsembliENSMUST00000096096; ENSMUSP00000093802; ENSMUSG00000024989. [Q8BT07-1]
    ENSMUST00000116506; ENSMUSP00000112205; ENSMUSG00000024989. [Q8BT07-2]
    ENSMUST00000169673; ENSMUSP00000127961; ENSMUSG00000024989. [Q8BT07-1]
    GeneIDi74107.
    KEGGimmu:74107.
    UCSCiuc008hiy.2. mouse. [Q8BT07-1]
    uc008hja.2. mouse. [Q8BT07-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004655 mRNA. Translation: BAB23446.1 .
    AK028216 mRNA. Translation: BAC25819.1 .
    AK088548 mRNA. Translation: BAC40417.1 .
    BC026966 mRNA. Translation: AAH26966.1 .
    BC031396 mRNA. Translation: AAH31396.1 .
    CCDSi CCDS29782.1. [Q8BT07-2 ]
    CCDS50429.1. [Q8BT07-1 ]
    RefSeqi NP_001157834.1. NM_001164362.1. [Q8BT07-1 ]
    NP_082569.1. NM_028293.1. [Q8BT07-1 ]
    NP_083036.2. NM_028760.2. [Q8BT07-2 ]
    XP_006527459.1. XM_006527396.1. [Q8BT07-1 ]
    XP_006527460.1. XM_006527397.1. [Q8BT07-1 ]
    XP_006527461.1. XM_006527398.1. [Q8BT07-1 ]
    XP_006527462.1. XM_006527399.1. [Q8BT07-1 ]
    XP_006527463.1. XM_006527400.1. [Q8BT07-1 ]
    XP_006527464.1. XM_006527401.1. [Q8BT07-1 ]
    UniGenei Mm.9916.

    3D structure databases

    ProteinModelPortali Q8BT07.
    SMRi Q8BT07. Positions 167-208.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 216498. 16 interactions.
    IntActi Q8BT07. 22 interactions.

    PTM databases

    PhosphoSitei Q8BT07.

    Proteomic databases

    MaxQBi Q8BT07.
    PaxDbi Q8BT07.
    PRIDEi Q8BT07.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000096096 ; ENSMUSP00000093802 ; ENSMUSG00000024989 . [Q8BT07-1 ]
    ENSMUST00000116506 ; ENSMUSP00000112205 ; ENSMUSG00000024989 . [Q8BT07-2 ]
    ENSMUST00000169673 ; ENSMUSP00000127961 ; ENSMUSG00000024989 . [Q8BT07-1 ]
    GeneIDi 74107.
    KEGGi mmu:74107.
    UCSCi uc008hiy.2. mouse. [Q8BT07-1 ]
    uc008hja.2. mouse. [Q8BT07-2 ]

    Organism-specific databases

    CTDi 55165.
    MGIi MGI:1921357. Cep55.

    Phylogenomic databases

    eggNOGi NOG135886.
    GeneTreei ENSGT00510000047961.
    HOGENOMi HOG000111547.
    HOVERGENi HBG081092.
    InParanoidi Q8BT07.
    KOi K16456.
    OMAi INISEVW.
    OrthoDBi EOG7H4DTJ.
    PhylomeDBi Q8BT07.
    TreeFami TF331107.

    Miscellaneous databases

    NextBioi 339796.
    PROi Q8BT07.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BT07.
    CleanExi MM_CEP55.
    Genevestigatori Q8BT07.

    Family and domain databases

    InterProi IPR022008. EABR.
    [Graphical view ]
    Pfami PF12180. EABR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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), VARIANT ASP-55.
      Strain: C57BL/6J and NOD.
      Tissue: Embryo, Lung and Thymus.
    2. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-462 (ISOFORM 1), VARIANT ASP-55.
      Strain: Czech II and FVB/N.
      Tissue: Mammary tumor.
    3. "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-426 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCEP55_MOUSE
    AccessioniPrimary (citable) accession number: Q8BT07
    Secondary accession number(s): Q8C2J0
    , Q8K2I8, Q8R2Y4, Q9DBZ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 86 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

    External Data

    Dasty 3