ZWILC_MOUSE
ID ZWILC_MOUSE Reviewed; 589 AA.
AC Q8R060; Q9D2E4; Q9D761;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Protein zwilch homolog;
GN Name=Zwilch;
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; TISSUE=Testis, and Tongue;
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 tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H900}.
CC -!- SUBUNIT: Component of the RZZ complex composed of KNTC1/ROD, ZW10 and
CC ZWILCH; in the complex interacts directly with KNTC1/ROD (By
CC similarity). {ECO:0000250|UniProtKB:Q9H900}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q9H900}.
CC -!- SIMILARITY: Belongs to the ZWILCH family. {ECO:0000305}.
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DR EMBL; AK009559; BAB26358.2; -; mRNA.
DR EMBL; AK019825; BAB31869.2; -; mRNA.
DR EMBL; BC027435; AAH27435.1; -; mRNA.
DR RefSeq; NP_080783.3; NM_026507.4.
DR AlphaFoldDB; Q8R060; -.
DR SMR; Q8R060; -.
DR BioGRID; 212596; 19.
DR IntAct; Q8R060; 2.
DR MINT; Q8R060; -.
DR STRING; 10090.ENSMUSP00000112790; -.
DR iPTMnet; Q8R060; -.
DR PhosphoSitePlus; Q8R060; -.
DR EPD; Q8R060; -.
DR MaxQB; Q8R060; -.
DR PaxDb; Q8R060; -.
DR PRIDE; Q8R060; -.
DR ProteomicsDB; 275319; -.
DR DNASU; 68014; -.
DR GeneID; 68014; -.
DR KEGG; mmu:68014; -.
DR UCSC; uc012gva.1; mouse.
DR CTD; 55055; -.
DR MGI; MGI:1915264; Zwilch.
DR eggNOG; KOG4803; Eukaryota.
DR InParanoid; Q8R060; -.
DR OrthoDB; 1451737at2759; -.
DR PhylomeDB; Q8R060; -.
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-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 68014; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Zwilch; mouse.
DR PRO; PR:Q8R060; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8R060; protein.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:1990423; C:RZZ complex; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0034501; P:protein localization to kinetochore; ISO:MGI.
DR InterPro; IPR018630; Zwilch.
DR PANTHER; PTHR15995; PTHR15995; 1.
DR Pfam; PF09817; Zwilch; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Kinetochore; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..589
FT /note="Protein zwilch homolog"
FT /id="PRO_0000314801"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H900"
FT CONFLICT 19
FT /note="E -> G (in Ref. 1; BAB26358)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="D -> V (in Ref. 1; BAB26358)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="E -> G (in Ref. 1; BAB26358)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 66839 MW; D4CF69E0E818A988 CRC64;
MWSRMNRAAE EFYARLRQEF NEEKKGASKD PFIYEADVQV QLISKGQPSL LKTILNENDS
VFLVEKVVLE KEETSQVEEL QSEETAISDL SAGENIRPLA LPVGRARQLI GLYTMAHNPN
MTHLKIKQPV TALPPLWVRC DGSDPEGTCW LGAELITTND IIAGVILYVL TCKADKNYSE
DLENLKTSHK KRHHVSAVTA RGFAQYELFK SDDLDDTVAP SQTTVTLDLS WSPVDEMLQT
PPLSSTAALN IRVQSGESRG CLSHLHRELK FLLVLADGIR TGVTEWLEPL ETKSALEFVQ
EFLNDLNKLD EFDDSTKKDK QKEAVNHDAA AVVRSMLLTV RGDLDFAEQL WCRMSSSVVS
YQDLVKCFTL ILQSLQRGDI QPWLHSGSNS LLSKLIHQSY HGAMDSVPLS GTTPLQMLLE
IGLDKLKKDY ISFFVSQELA SLNHLEYFIS PSVSTQEQVC RVQKLHHILE ILVICMLFIK
PQHELLFSLT QSCIKYYKQN PLDEQHIFQL PVRPAAVKNL YQSEKPQKWR VELSNSQKRV
KTVWQLSDSS PVDHSSFHRP EFPELTLNGS LEERTAFVNM LTCSQVHFK
