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Q9ESN5

- CENPK_MOUSE

UniProt

Q9ESN5 - CENPK_MOUSE

Protein

Centromere protein K

Gene

Cenpk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 2 (19 Sep 2006)
      Previous versions | rss
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    Functioni

    Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Acts in coordination with CASC5/KNL1 to recruit the NDC80 complex to the outer kinetochore By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: MGI

    GO - Biological processi

    1. positive regulation of transcription from RNA polymerase II promoter Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_198597. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Centromere protein K
    Short name:
    CENP-K
    Alternative name(s):
    SoxLZ/Sox6 leucine zipper-binding protein in testis
    Gene namesi
    Name:Cenpk
    Synonyms:Solt
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1926210. Cenpk.

    Subcellular locationi

    Nucleus By similarity. Chromosomecentromere By similarity. Chromosomecentromerekinetochore By similarity
    Note: Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex By similarity.By similarity

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Centromere, Chromosome, Kinetochore, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 271271Centromere protein KPRO_0000249483Add
    BLAST

    Proteomic databases

    PRIDEiQ9ESN5.

    PTM databases

    PhosphoSiteiQ9ESN5.

    Expressioni

    Tissue specificityi

    Highly expressed in testis.1 Publication

    Gene expression databases

    BgeeiQ9ESN5.
    CleanExiMM_CENPK.
    GenevestigatoriQ9ESN5.

    Interactioni

    Subunit structurei

    Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. May interact with Sox6.

    Protein-protein interaction databases

    IntActiQ9ESN5. 1 interaction.
    MINTiMINT-8174098.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili11 – 4434Sequence AnalysisAdd
    BLAST
    Coiled coili102 – 15150Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CENPK family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG46525.
    GeneTreeiENSGT00390000006243.
    HOGENOMiHOG000111542.
    HOVERGENiHBG081084.
    InParanoidiQ9ESN5.
    KOiK11503.
    OMAiCESKNET.
    OrthoDBiEOG780RN0.
    PhylomeDBiQ9ESN5.
    TreeFamiTF333264.

    Family and domain databases

    InterProiIPR020993. Centromere_CenpK.
    [Graphical view]
    PfamiPF11802. CENP-K. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9ESN5-1) [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

    MSENKQEVHP DTITDVEAVI DTEEELIKEC EEMWKDMEDC QNKLSLIGTE    50
    TLTNADAQLS LLIMQMKCLT AELGQWKKRK PEIIPLNEDV LLTLGKEEFQ 100
    KLRCDLEMVL STIQSKNEKL KEDLEREQQW LDEQQQILDT LNVLNSDVEN 150
    QVVTLTESRI FNELTTKIRG IKEFKEKLLL TLGAFLDNHF PLPEASTPKK 200
    RKNIQDSNAQ LITLNEILEM LINRMFDVPH DPYVKIRDSF WPPYIELLLR 250
    YGIALRHPED PSQIRLEAFH Q 271
    Length:271
    Mass (Da):31,686
    Last modified:September 19, 2006 - v2
    Checksum:i0805A7930078B014
    GO
    Isoform 2 (identifier: Q9ESN5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         220-271: MLINRMFDVP...SQIRLEAFHQ → VPLRAMGSTLESCWFPRETLLEEAAFSLASASVG

    Note: No experimental confirmation available.

    Show »
    Length:253
    Mass (Da):28,978
    Checksum:i066A7EF2AB4DD2DD
    GO
    Isoform 3 (identifier: Q9ESN5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-107: Missing.
         266-271: LEAFHQ → TSCMVGACGDQKSHH

    Note: No experimental confirmation available.

    Show »
    Length:173
    Mass (Da):20,140
    Checksum:iEA4651E29E5F58A7
    GO

    Sequence cautioni

    The sequence AAH92351.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAB16367.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1151S → T in AAH92351. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 107107Missing in isoform 3. 1 PublicationVSP_020437Add
    BLAST
    Alternative sequencei220 – 27152MLINR…EAFHQ → VPLRAMGSTLESCWFPRETL LEEAAFSLASASVG in isoform 2. 1 PublicationVSP_020438Add
    BLAST
    Alternative sequencei266 – 2716LEAFHQ → TSCMVGACGDQKSHH in isoform 3. 1 PublicationVSP_020439

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB043687 mRNA. Translation: BAB16367.1. Different initiation.
    AK082939 mRNA. Translation: BAC38702.1.
    AK135773 mRNA. Translation: BAE22654.1.
    BC092351 mRNA. Translation: AAH92351.1. Sequence problems.
    CCDSiCCDS26750.1. [Q9ESN5-2]
    RefSeqiNP_068562.1. NM_021790.2.
    NP_851406.1. NM_181061.5. [Q9ESN5-2]
    XP_006517792.1. XM_006517729.1. [Q9ESN5-1]
    XP_006517793.1. XM_006517730.1. [Q9ESN5-1]
    UniGeneiMm.281498.

    Genome annotation databases

    EnsembliENSMUST00000022227; ENSMUSP00000022227; ENSMUSG00000021714.
    ENSMUST00000070761; ENSMUSP00000070910; ENSMUSG00000021714. [Q9ESN5-2]
    GeneIDi60411.
    KEGGimmu:60411.
    UCSCiuc007rtc.1. mouse. [Q9ESN5-2]
    uc007rtd.1. mouse. [Q9ESN5-1]
    uc007rtf.1. mouse. [Q9ESN5-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB043687 mRNA. Translation: BAB16367.1 . Different initiation.
    AK082939 mRNA. Translation: BAC38702.1 .
    AK135773 mRNA. Translation: BAE22654.1 .
    BC092351 mRNA. Translation: AAH92351.1 . Sequence problems.
    CCDSi CCDS26750.1. [Q9ESN5-2 ]
    RefSeqi NP_068562.1. NM_021790.2.
    NP_851406.1. NM_181061.5. [Q9ESN5-2 ]
    XP_006517792.1. XM_006517729.1. [Q9ESN5-1 ]
    XP_006517793.1. XM_006517730.1. [Q9ESN5-1 ]
    UniGenei Mm.281498.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9ESN5. 1 interaction.
    MINTi MINT-8174098.

    PTM databases

    PhosphoSitei Q9ESN5.

    Proteomic databases

    PRIDEi Q9ESN5.

    Protocols and materials databases

    DNASUi 60411.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022227 ; ENSMUSP00000022227 ; ENSMUSG00000021714 .
    ENSMUST00000070761 ; ENSMUSP00000070910 ; ENSMUSG00000021714 . [Q9ESN5-2 ]
    GeneIDi 60411.
    KEGGi mmu:60411.
    UCSCi uc007rtc.1. mouse. [Q9ESN5-2 ]
    uc007rtd.1. mouse. [Q9ESN5-1 ]
    uc007rtf.1. mouse. [Q9ESN5-3 ]

    Organism-specific databases

    CTDi 64105.
    MGIi MGI:1926210. Cenpk.

    Phylogenomic databases

    eggNOGi NOG46525.
    GeneTreei ENSGT00390000006243.
    HOGENOMi HOG000111542.
    HOVERGENi HBG081084.
    InParanoidi Q9ESN5.
    KOi K11503.
    OMAi CESKNET.
    OrthoDBi EOG780RN0.
    PhylomeDBi Q9ESN5.
    TreeFami TF333264.

    Enzyme and pathway databases

    Reactomei REACT_198597. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.

    Miscellaneous databases

    NextBioi 314857.
    PROi Q9ESN5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9ESN5.
    CleanExi MM_CENPK.
    Genevestigatori Q9ESN5.

    Family and domain databases

    InterProi IPR020993. Centromere_CenpK.
    [Graphical view ]
    Pfami PF11802. CENP-K. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of Solt, a novel SoxLZ/Sox6 binding protein expressed in adult mouse testis."
      Yamashita A., Ito M., Takamatsu N., Shiba T.
      FEBS Lett. 481:147-151(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, POSSIBLE INTERACTION WITH SOX6.
    2. "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] (ISOFORMS 2 AND 3).
      Strain: C57BL/6J.
      Tissue: Egg and Spinal cord.
    3. "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] OF 1-120.
      Strain: NMRI.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiCENPK_MOUSE
    AccessioniPrimary (citable) accession number: Q9ESN5
    Secondary accession number(s): Q3UXA9, Q569Q3, Q8C469
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: September 19, 2006
    Last modified: October 1, 2014
    This is version 78 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