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Protein

Centromere/kinetochore protein zw10 homolog

Gene

Zw10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex. Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the interphase NRZ complex which is believed to play a role in SNARE assembly at the ER (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiREACT_306375. Mitotic Prometaphase.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_358264. RHO GTPases Activate Formins.

Names & Taxonomyi

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

Complete GO annotation...

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.
GenevisibleiO54692. MM.

Interactioni

Subunit structurei

Interacts with NBAS and KNTC1/ROD; the interactions are mutually exclusive and indicative for its association in two different vesicle tethering complexes. Component of the RZZ complex composed of KNTC1/ROD, ZW10 and ZWILCH. Component of the NRZ complex composed of NBAS, ZW10 and RINT1/TIP20L; NRZ associates with SNAREs STX18, USE1L, BNIP1/SEC20L and SEC22B (the assembly has been described as syntaxin 18 complex). Interacts directly with RINT1/TIP20L bound to BNIP1/SEC20L. Interacts with C19orf25 and ZWINT STOPPED 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

Protein-protein interaction databases

BioGridi205086. 9 interactions.
IntActiO54692. 9 interactions.
STRINGi10090.ENSMUSP00000034803.

Structurei

3D structure databases

ProteinModelPortaliO54692.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 317316Interaction with RINT1By similarityAdd
BLAST
Regioni2 – 8180Interaction with ZWINTBy 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.
OMAiYNEVVNL.
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

        10         20         30         40         50
MASFVTEVLA HSGSLEKEDL GTRISRLTRR VEEIKGEVCN MISKKYSEFL
60 70 80 90 100
PTMQSAQALV TQVDTLSNDI DQLKSRIETE VCRDLHISTV EFTNLKQQLE
110 120 130 140 150
RDSVVLTLLK QLQEFSSAIE EYNSALAEKK YIPAARHLEE AQECLKLLKS
160 170 180 190 200
RKCFDLKMLK SLSMELTVQK QNILYHLGED WQKLVVWKFP PAKDTSSLES
210 220 230 240 250
CLQTELHLCT EQPEKEDMTP LPSISSVLLA FSILGELPTK LKSFGQMLLK
260 270 280 290 300
YILKPLVTCP SLHAVIERQP SSVSICFESL TTDLEHPSPP EAFAKIRLVL
310 320 330 340 350
EVLQKQLLDL PLDADLEIGK VPGIVLAEML GEGIWEDLSE CLIRNCLVYS
360 370 380 390 400
IPTNSSKLQE YEEIIQSTEE FEKFLKEMRF LKGDTTDLLK YARNINSHFA
410 420 430 440 450
NKKCQDVIVA ARNLMTSEIH NTVKIGPDCK EALPDLPSPD ADHKLQVQTV
460 470 480 490 500
CKAQFTDAGN LEPETSLDPQ SFSLPTCRIS EAVKKLMELA YQTLLEATTS
510 520 530 540 550
SDQCAVQLFY SVRNIFHLFH DVVPTYHKEN LRKLPQLAAI HHNNCMYIAH
560 570 580 590 600
HLLTLGHQFR LRLAPILCDG TTTFVDLVPG FRRLGTECFL AQMQAQKGEL
610 620 630 640 650
LERLSSARSF ANMDDEENYS AASKAVRQVL HQLRRLGIVW QDVLPVNIYC
660 670 680 690 700
KAMGTLLNTA IAEMMSRITA LEDISTEDGD RLYSLCKTVM DEGPQVFAPL
710 720 730 740 750
SDENKNKKYQ EEVPVYVSKW MPFKELMIML QASLQEIGDR WADGKGPLAT
760 770
AFPSSEVKAL IRALFQNTER RAAALAKIK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliO54692.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205086. 9 interactions.
IntActiO54692. 9 interactions.
STRINGi10090.ENSMUSP00000034803.

PTM databases

PhosphoSiteiO54692.

Proteomic databases

MaxQBiO54692.
PaxDbiO54692.
PRIDEiO54692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9183.
MGIiMGI:1349478. Zw10.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_306375. Mitotic Prometaphase.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_358264. RHO GTPases Activate Formins.

Miscellaneous databases

NextBioi304895.
PROiO54692.
SOURCEiSearch...

Gene expression databases

BgeeiO54692.
GenevisibleiO54692. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 114 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.