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O54692

- ZW10_MOUSE

UniProt

O54692 - ZW10_MOUSE

Protein

Centromere/kinetochore protein zw10 homolog

Gene

Zw10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum By similarity.By similarity

    GO - Biological processi

    1. ER to Golgi vesicle-mediated transport Source: HGNC
    2. establishment of mitotic spindle orientation Source: Ensembl
    3. mitotic cell cycle checkpoint Source: HGNC
    4. mitotic metaphase plate congression Source: Ensembl
    5. mitotic sister chromatid segregation Source: HGNC
    6. protein complex assembly Source: HGNC
    7. protein localization to kinetochore Source: Ensembl
    8. protein transport Source: UniProtKB-KW
    9. regulation of exit from mitosis Source: HGNC

    Keywords - Biological processi

    Cell cycle, Cell division, ER-Golgi transport, Mitosis, Protein transport, Transport

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Centromere/kinetochore protein zw10 homolog
    Gene namesi
    Name:Zw10
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1349478. Zw10.

    Subcellular locationi

    Cytoplasm By similarity. Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonspindle By similarity
    Note: Dynamic pattern of localization during the cell cycle. In most cells at interphase, present diffusely in the cytoplasm By similarity. In prometaphase, associated with the kinetochore. At metaphase, detected both at the kinetochores and, most prominently, at the spindle, particularly at the spindle poles. In very early anaphase, detected on segregating kinetochores. In late anaphase and telophase, accumulates at the spindle midzone By similarity.By similarity

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. endoplasmic reticulum Source: HGNC
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. kinetochore Source: HGNC
    5. kinetochore microtubule Source: HGNC
    6. nucleus Source: HGNC
    7. spindle pole Source: HGNC

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Kinetochore, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 779778Centromere/kinetochore protein zw10 homologPRO_0000184958Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei777 – 7771N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO54692.
    PaxDbiO54692.
    PRIDEiO54692.

    PTM databases

    PhosphoSiteiO54692.

    Expressioni

    Gene expression databases

    BgeeiO54692.
    GenevestigatoriO54692.

    Interactioni

    Subunit structurei

    Associated with a SNARE complex consisting of STX18, USE1L, BNIP1/SEC20L, and SEC22B through direct interaction with RINT1/TIP20L bound to BNIP1/SEC20L. Component of the RZZ complex composed of KNTC1/ROD, ZW10 and ZWILCH. Interacts with C19orf25, KNTC1 and ZWINT By similarity.By similarity

    Protein-protein interaction databases

    BioGridi205086. 9 interactions.
    IntActiO54692. 9 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliO54692.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 317316Interaction with RINT1By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili14 – 130117Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ZW10 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG299329.
    GeneTreeiENSGT00390000016427.
    HOGENOMiHOG000007982.
    HOVERGENiHBG004603.
    InParanoidiO54692.
    KOiK11578.
    OMAiVVNLEPE.
    OrthoDBiEOG718KBR.
    PhylomeDBiO54692.
    TreeFamiTF105966.

    Family and domain databases

    InterProiIPR009361. RZZ-complex_Zw10.
    [Graphical view]
    PfamiPF06248. Zw10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O54692-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASFVTEVLA HSGSLEKEDL GTRISRLTRR VEEIKGEVCN MISKKYSEFL    50
    PTMQSAQALV TQVDTLSNDI DQLKSRIETE VCRDLHISTV EFTNLKQQLE 100
    RDSVVLTLLK QLQEFSSAIE EYNSALAEKK YIPAARHLEE AQECLKLLKS 150
    RKCFDLKMLK SLSMELTVQK QNILYHLGED WQKLVVWKFP PAKDTSSLES 200
    CLQTELHLCT EQPEKEDMTP LPSISSVLLA FSILGELPTK LKSFGQMLLK 250
    YILKPLVTCP SLHAVIERQP SSVSICFESL TTDLEHPSPP EAFAKIRLVL 300
    EVLQKQLLDL PLDADLEIGK VPGIVLAEML GEGIWEDLSE CLIRNCLVYS 350
    IPTNSSKLQE YEEIIQSTEE FEKFLKEMRF LKGDTTDLLK YARNINSHFA 400
    NKKCQDVIVA ARNLMTSEIH NTVKIGPDCK EALPDLPSPD ADHKLQVQTV 450
    CKAQFTDAGN LEPETSLDPQ SFSLPTCRIS EAVKKLMELA YQTLLEATTS 500
    SDQCAVQLFY SVRNIFHLFH DVVPTYHKEN LRKLPQLAAI HHNNCMYIAH 550
    HLLTLGHQFR LRLAPILCDG TTTFVDLVPG FRRLGTECFL AQMQAQKGEL 600
    LERLSSARSF ANMDDEENYS AASKAVRQVL HQLRRLGIVW QDVLPVNIYC 650
    KAMGTLLNTA IAEMMSRITA LEDISTEDGD RLYSLCKTVM DEGPQVFAPL 700
    SDENKNKKYQ EEVPVYVSKW MPFKELMIML QASLQEIGDR WADGKGPLAT 750
    AFPSSEVKAL IRALFQNTER RAAALAKIK 779
    Length:779
    Mass (Da):88,063
    Last modified:January 23, 2007 - v3
    Checksum:i5C02CF77FDF5B13B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti143 – 1431E → A in BAE26337. (PubMed:16141072)Curated
    Sequence conflicti281 – 2811T → A in BAE26337. (PubMed:16141072)Curated
    Sequence conflicti281 – 2811T → A in BAE39941. (PubMed:16141072)Curated
    Sequence conflicti292 – 2921A → T in BAE39941. (PubMed:16141072)Curated
    Sequence conflicti449 – 4491T → K in BAE26337. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK145270 mRNA. Translation: BAE26337.1.
    AK167251 mRNA. Translation: BAE39372.1.
    AK167937 mRNA. Translation: BAE39941.1.
    AK168479 mRNA. Translation: BAE40368.1.
    BC012435 mRNA. Translation: AAH12435.1.
    AF003951 mRNA. Translation: AAB88256.1.
    CCDSiCCDS23161.1.
    RefSeqiNP_036169.1. NM_012039.2.
    UniGeneiMm.24791.

    Genome annotation databases

    EnsembliENSMUST00000034803; ENSMUSP00000034803; ENSMUSG00000032264.
    GeneIDi26951.
    KEGGimmu:26951.
    UCSCiuc009piu.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK145270 mRNA. Translation: BAE26337.1 .
    AK167251 mRNA. Translation: BAE39372.1 .
    AK167937 mRNA. Translation: BAE39941.1 .
    AK168479 mRNA. Translation: BAE40368.1 .
    BC012435 mRNA. Translation: AAH12435.1 .
    AF003951 mRNA. Translation: AAB88256.1 .
    CCDSi CCDS23161.1.
    RefSeqi NP_036169.1. NM_012039.2.
    UniGenei Mm.24791.

    3D structure databases

    ProteinModelPortali O54692.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 205086. 9 interactions.
    IntActi O54692. 9 interactions.

    PTM databases

    PhosphoSitei O54692.

    Proteomic databases

    MaxQBi O54692.
    PaxDbi O54692.
    PRIDEi O54692.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034803 ; ENSMUSP00000034803 ; ENSMUSG00000032264 .
    GeneIDi 26951.
    KEGGi mmu:26951.
    UCSCi uc009piu.2. mouse.

    Organism-specific databases

    CTDi 9183.
    MGIi MGI:1349478. Zw10.

    Phylogenomic databases

    eggNOGi NOG299329.
    GeneTreei ENSGT00390000016427.
    HOGENOMi HOG000007982.
    HOVERGENi HBG004603.
    InParanoidi O54692.
    KOi K11578.
    OMAi VVNLEPE.
    OrthoDBi EOG718KBR.
    PhylomeDBi O54692.
    TreeFami TF105966.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 304895.
    PROi O54692.
    SOURCEi Search...

    Gene expression databases

    Bgeei O54692.
    Genevestigatori O54692.

    Family and domain databases

    InterProi IPR009361. RZZ-complex_Zw10.
    [Graphical view ]
    Pfami PF06248. Zw10. 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].
      Strain: C57BL/6J and DBA/2.
      Tissue: Kidney and Mammary gland.
    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].
      Strain: FVB/N.
      Tissue: Mammary gland.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 522-779.

    Entry informationi

    Entry nameiZW10_MOUSE
    AccessioniPrimary (citable) accession number: O54692
    Secondary accession number(s): Q3TIA5, Q3ULW1, Q921H3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 3 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