ZW10_MOUSE
ID ZW10_MOUSE Reviewed; 779 AA.
AC O54692; Q3TIA5; Q3ULW1; Q921H3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Centromere/kinetochore protein zw10 homolog;
GN Name=Zw10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Kidney, and Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 522-779.
RX PubMed=9298984; DOI=10.1083/jcb.138.6.1289;
RA Starr D.A., Williams B.C., Li Z., Etemad-Moghadam B., Dawe R.K.,
RA Goldberg M.L.;
RT "Conservation of the centromere/kinetochore protein ZW10.";
RL J. Cell Biol. 138:1289-1301(1997).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC cells from prematurely exiting mitosis. Required for the assembly of
CC the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its
CC function related to the spindle assembly machinery is proposed to
CC depend on its association in the mitotic RZZ complex. Involved in
CC regulation of membrane traffic between the Golgi and the endoplasmic
CC reticulum (ER); the function is proposed to depend on its association
CC in the interphase NRZ complex which is believed to play a role in SNARE
CC assembly at the ER (By similarity). {ECO:0000250|UniProtKB:O43264}.
CC -!- SUBUNIT: Interacts with NBAS and KNTC1/ROD; the interactions are
CC mutually exclusive and indicative for its association in two different
CC vesicle tethering complexes (By similarity). Component of the RZZ
CC complex composed of KNTC1/ROD, ZW10 and ZWILCH (By similarity).
CC Component of the NRZ complex composed of NBAS, ZW10 and RINT1/TIP20L;
CC NRZ associates with SNAREs STX18, USE1L, BNIP1/SEC20L and SEC22B (the
CC assembly has been described as syntaxin 18 complex) (By similarity).
CC Interacts directly with RINT1/TIP20L bound to BNIP1/SEC20L (By
CC similarity). Interacts with C19orf25 and ZWINT (By similarity).
CC Interacts with ZFYVE1 (By similarity). Interacts with RAB18 and this
CC interaction is enhanced in the presence of ZFYVE1 (By similarity).
CC {ECO:0000250|UniProtKB:O43264}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43264}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43264};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:O43264}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:O43264}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:O43264}. Lipid droplet
CC {ECO:0000250|UniProtKB:O43264}. Note=Dynamic pattern of localization
CC during the cell cycle. In most cells at interphase, present diffusely
CC in the cytoplasm. In prometaphase, associated with the kinetochore. At
CC metaphase, detected both at the kinetochores and, most prominently, at
CC the spindle, particularly at the spindle poles. In very early anaphase,
CC detected on segregating kinetochores. In late anaphase and telophase,
CC accumulates at the spindle midzone. {ECO:0000250|UniProtKB:O43264}.
CC -!- SIMILARITY: Belongs to the ZW10 family. {ECO:0000305}.
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DR EMBL; AK145270; BAE26337.1; -; mRNA.
DR EMBL; AK167251; BAE39372.1; -; mRNA.
DR EMBL; AK167937; BAE39941.1; -; mRNA.
DR EMBL; AK168479; BAE40368.1; -; mRNA.
DR EMBL; BC012435; AAH12435.1; -; mRNA.
DR EMBL; AF003951; AAB88256.1; -; mRNA.
DR CCDS; CCDS23161.1; -.
DR RefSeq; NP_036169.1; NM_012039.2.
DR AlphaFoldDB; O54692; -.
DR BioGRID; 205086; 35.
DR IntAct; O54692; 19.
DR MINT; O54692; -.
DR STRING; 10090.ENSMUSP00000034803; -.
DR iPTMnet; O54692; -.
DR PhosphoSitePlus; O54692; -.
DR EPD; O54692; -.
DR jPOST; O54692; -.
DR MaxQB; O54692; -.
DR PaxDb; O54692; -.
DR PeptideAtlas; O54692; -.
DR PRIDE; O54692; -.
DR ProteomicsDB; 275171; -.
DR Antibodypedia; 3162; 171 antibodies from 25 providers.
DR DNASU; 26951; -.
DR Ensembl; ENSMUST00000034803; ENSMUSP00000034803; ENSMUSG00000032264.
DR GeneID; 26951; -.
DR KEGG; mmu:26951; -.
DR UCSC; uc009piu.2; mouse.
DR CTD; 9183; -.
DR MGI; MGI:1349478; Zw10.
DR VEuPathDB; HostDB:ENSMUSG00000032264; -.
DR eggNOG; KOG2163; Eukaryota.
DR GeneTree; ENSGT00390000016427; -.
DR HOGENOM; CLU_012948_0_0_1; -.
DR InParanoid; O54692; -.
DR OMA; LMMILQA; -.
DR OrthoDB; 422807at2759; -.
DR PhylomeDB; O54692; -.
DR TreeFam; TF105966; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 26951; 13 hits in 72 CRISPR screens.
DR ChiTaRS; Zw10; mouse.
DR PRO; PR:O54692; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O54692; protein.
DR Bgee; ENSMUSG00000032264; Expressed in gastrula and 251 other tissues.
DR ExpressionAtlas; O54692; baseline and differential.
DR Genevisible; O54692; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070939; C:Dsl1/NZR complex; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; ISS:HGNC-UCL.
DR GO; GO:0005828; C:kinetochore microtubule; ISS:HGNC-UCL.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:1990423; C:RZZ complex; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:HGNC-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:HGNC-UCL.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:HGNC-UCL.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:HGNC-UCL.
DR GO; GO:0034501; P:protein localization to kinetochore; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:HGNC-UCL.
DR GO; GO:0007096; P:regulation of exit from mitosis; ISS:HGNC-UCL.
DR Gene3D; 1.10.357.150; -; 1.
DR InterPro; IPR009361; RZZ-complex_Zw10.
DR InterPro; IPR046362; Zw10/DSL1_C_sf.
DR Pfam; PF06248; Zw10; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW ER-Golgi transport; Kinetochore; Lipid droplet; Membrane; Mitosis;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT CHAIN 2..779
FT /note="Centromere/kinetochore protein zw10 homolog"
FT /id="PRO_0000184958"
FT REGION 2..317
FT /note="Interaction with RINT1"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT REGION 2..81
FT /note="Interaction with ZWINT"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT COILED 14..130
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT MOD_RES 777
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT CONFLICT 143
FT /note="E -> A (in Ref. 1; BAE26337)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="T -> A (in Ref. 1; BAE26337/BAE39941)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="A -> T (in Ref. 1; BAE39941)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="T -> K (in Ref. 1; BAE26337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 779 AA; 88063 MW; 5C02CF77FDF5B13B CRC64;
MASFVTEVLA HSGSLEKEDL GTRISRLTRR VEEIKGEVCN MISKKYSEFL PTMQSAQALV
TQVDTLSNDI DQLKSRIETE VCRDLHISTV EFTNLKQQLE RDSVVLTLLK QLQEFSSAIE
EYNSALAEKK YIPAARHLEE AQECLKLLKS RKCFDLKMLK SLSMELTVQK QNILYHLGED
WQKLVVWKFP PAKDTSSLES CLQTELHLCT EQPEKEDMTP LPSISSVLLA FSILGELPTK
LKSFGQMLLK YILKPLVTCP SLHAVIERQP SSVSICFESL TTDLEHPSPP EAFAKIRLVL
EVLQKQLLDL PLDADLEIGK VPGIVLAEML GEGIWEDLSE CLIRNCLVYS IPTNSSKLQE
YEEIIQSTEE FEKFLKEMRF LKGDTTDLLK YARNINSHFA NKKCQDVIVA ARNLMTSEIH
NTVKIGPDCK EALPDLPSPD ADHKLQVQTV CKAQFTDAGN LEPETSLDPQ SFSLPTCRIS
EAVKKLMELA YQTLLEATTS SDQCAVQLFY SVRNIFHLFH DVVPTYHKEN LRKLPQLAAI
HHNNCMYIAH HLLTLGHQFR LRLAPILCDG TTTFVDLVPG FRRLGTECFL AQMQAQKGEL
LERLSSARSF ANMDDEENYS AASKAVRQVL HQLRRLGIVW QDVLPVNIYC KAMGTLLNTA
IAEMMSRITA LEDISTEDGD RLYSLCKTVM DEGPQVFAPL SDENKNKKYQ EEVPVYVSKW
MPFKELMIML QASLQEIGDR WADGKGPLAT AFPSSEVKAL IRALFQNTER RAAALAKIK
