ZWINT_HUMAN
ID ZWINT_HUMAN Reviewed; 277 AA.
AC O95229; A6NNV6; Q0D2I3; Q9BWD0;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=ZW10 interactor;
DE AltName: Full=ZW10-interacting protein 1;
DE Short=Zwint-1;
GN Name=ZWINT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-187.
RX PubMed=10806105; DOI=10.1242/jcs.113.11.1939;
RA Starr D.A., Saffery R., Li Z., Simpson A.E., Choo K.H., Yen T.J.,
RA Goldberg M.L.;
RT "HZwint-1, a novel human kinetochore component that interacts with HZW10.";
RL J. Cell Sci. 113:1939-1950(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-187.
RC TISSUE=Colon, Lymph, and Muscle;
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 [4]
RP FUNCTION.
RX PubMed=15094189; DOI=10.1016/j.gene.2004.01.028;
RA Musio A., Mariani T., Montagna C., Zambroni D., Ascoli C., Ried T.,
RA Vezzoni P.;
RT "Recapitulation of the Roberts syndrome cellular phenotype by inhibition of
RT INCENP, ZWINT-1 and ZW10 genes.";
RL Gene 331:33-40(2004).
RN [5]
RP FUNCTION, INTERACTION WITH ZW10, AND SUBCELLULAR LOCATION.
RX PubMed=15485811; DOI=10.1074/jbc.m407588200;
RA Wang H., Hu X., Ding X., Dou Z., Yang Z., Shaw A.W., Teng M.,
RA Cleveland D.W., Goldberg M.L., Niu L., Yao X.;
RT "Human Zwint-1 specifies localization of Zeste White 10 to kinetochores and
RT is essential for mitotic checkpoint signaling.";
RL J. Biol. Chem. 279:54590-54598(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MIS12, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15502821; DOI=10.1038/ncb1187;
RA Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.;
RT "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and
RT outer kinetochore protein Zwint-1.";
RL Nat. Cell Biol. 6:1135-1141(2004).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH KNL1;
RP CETN3; DSN1; NDC80; MIS12; PMFF1 AND ZW10, AND SUBCELLULAR LOCATION.
RX PubMed=15824131; DOI=10.1083/jcb.200411118;
RA Kops G.J.P.L., Kim Y., Weaver B.A.A., Mao Y., McLeod I., Yates J.R. III,
RA Tagaya M., Cleveland D.W.;
RT "ZW10 links mitotic checkpoint signaling to the structural kinetochore.";
RL J. Cell Biol. 169:49-60(2005).
RN [8]
RP FUNCTION, INTERACTION WITH NDC80 AND ZW10, AND SUBCELLULAR LOCATION.
RX PubMed=16732327; DOI=10.1038/sj.onc.1209687;
RA Lin Y.-T., Chen Y., Wu G., Lee W.-H.;
RT "Hec1 sequentially recruits Zwint-1 and ZW10 to kinetochores for faithful
RT chromosome segregation and spindle checkpoint control.";
RL Oncogene 25:6901-6914(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Part of the MIS12 complex, which is required for kinetochore
CC formation and spindle checkpoint activity. Required to target ZW10 to
CC the kinetochore at prometaphase. {ECO:0000269|PubMed:15094189,
CC ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131,
CC ECO:0000269|PubMed:16732327}.
CC -!- SUBUNIT: Interacts with ZW10 and MIS12. Interacts with the NDC80
CC subunit of the NDC80 complex specifically during mitosis. Also
CC interacts with KNL1, CETN3, DSN1 and PMF1.
CC {ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15502821,
CC ECO:0000269|PubMed:15824131, ECO:0000269|PubMed:16732327}.
CC -!- INTERACTION:
CC O95229; O75934: BCAS2; NbExp=3; IntAct=EBI-1001132, EBI-1050106;
CC O95229; Q14457: BECN1; NbExp=6; IntAct=EBI-1001132, EBI-949378;
CC O95229; Q12934-2: BFSP1; NbExp=3; IntAct=EBI-1001132, EBI-12123320;
CC O95229; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-1001132, EBI-10175300;
CC O95229; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-1001132, EBI-6658203;
CC O95229; O14901: KLF11; NbExp=3; IntAct=EBI-1001132, EBI-948266;
CC O95229; O95678: KRT75; NbExp=3; IntAct=EBI-1001132, EBI-2949715;
CC O95229; A6NI15: MSGN1; NbExp=3; IntAct=EBI-1001132, EBI-11991020;
CC O95229; O14777: NDC80; NbExp=14; IntAct=EBI-1001132, EBI-715849;
CC O95229; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-1001132, EBI-741048;
CC O95229; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-1001132, EBI-2811583;
CC O95229; Q99816: TSG101; NbExp=3; IntAct=EBI-1001132, EBI-346882;
CC O95229; O43264: ZW10; NbExp=6; IntAct=EBI-1001132, EBI-1001217;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Note=Localizes to kinetochores from late prophase to anaphase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95229-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95229-2; Sequence=VSP_047660;
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DR EMBL; AF067656; AAC78629.1; -; mRNA.
DR EMBL; AC010996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000411; AAH00411.1; -; mRNA.
DR EMBL; BC020979; AAH20979.1; -; mRNA.
DR EMBL; BC110399; AAI10400.1; -; mRNA.
DR CCDS; CCDS31205.1; -. [O95229-2]
DR CCDS; CCDS7249.1; -. [O95229-1]
DR RefSeq; NP_001005413.1; NM_001005413.1. [O95229-2]
DR RefSeq; NP_008988.2; NM_007057.3. [O95229-1]
DR RefSeq; NP_127490.1; NM_032997.2. [O95229-1]
DR AlphaFoldDB; O95229; -.
DR SMR; O95229; -.
DR BioGRID; 116303; 150.
DR ComplexPortal; CPX-5644; Kinetochore KNL1 complex.
DR CORUM; O95229; -.
DR IntAct; O95229; 109.
DR MINT; O95229; -.
DR STRING; 9606.ENSP00000363055; -.
DR iPTMnet; O95229; -.
DR PhosphoSitePlus; O95229; -.
DR BioMuta; ZWINT; -.
DR EPD; O95229; -.
DR jPOST; O95229; -.
DR MassIVE; O95229; -.
DR MaxQB; O95229; -.
DR PaxDb; O95229; -.
DR PeptideAtlas; O95229; -.
DR PRIDE; O95229; -.
DR ProteomicsDB; 1641; -.
DR ProteomicsDB; 50728; -. [O95229-1]
DR Antibodypedia; 28018; 273 antibodies from 31 providers.
DR DNASU; 11130; -.
DR Ensembl; ENST00000361148.6; ENSP00000354921.6; ENSG00000122952.17. [O95229-2]
DR Ensembl; ENST00000373944.8; ENSP00000363055.3; ENSG00000122952.17. [O95229-1]
DR Ensembl; ENST00000395405.5; ENSP00000378801.1; ENSG00000122952.17. [O95229-1]
DR GeneID; 11130; -.
DR KEGG; hsa:11130; -.
DR MANE-Select; ENST00000373944.8; ENSP00000363055.3; NM_007057.4; NP_008988.2.
DR UCSC; uc001jjx.2; human. [O95229-1]
DR CTD; 11130; -.
DR DisGeNET; 11130; -.
DR GeneCards; ZWINT; -.
DR HGNC; HGNC:13195; ZWINT.
DR HPA; ENSG00000122952; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 609177; gene.
DR neXtProt; NX_O95229; -.
DR OpenTargets; ENSG00000122952; -.
DR PharmGKB; PA37761; -.
DR VEuPathDB; HostDB:ENSG00000122952; -.
DR eggNOG; ENOG502S6PG; Eukaryota.
DR GeneTree; ENSGT00390000017639; -.
DR HOGENOM; CLU_089675_0_0_1; -.
DR InParanoid; O95229; -.
DR OMA; QSIGDTM; -.
DR OrthoDB; 1313012at2759; -.
DR PhylomeDB; O95229; -.
DR TreeFam; TF338101; -.
DR PathwayCommons; O95229; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; O95229; -.
DR SIGNOR; O95229; -.
DR BioGRID-ORCS; 11130; 405 hits in 1091 CRISPR screens.
DR ChiTaRS; ZWINT; human.
DR GeneWiki; ZWINT; -.
DR GenomeRNAi; 11130; -.
DR Pharos; O95229; Tbio.
DR PRO; PR:O95229; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O95229; protein.
DR Bgee; ENSG00000122952; Expressed in oocyte and 174 other tissues.
DR ExpressionAtlas; O95229; baseline and differential.
DR Genevisible; O95229; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:BHF-UCL.
DR GO; GO:0031617; C:NMS complex; IC:ComplexPortal.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:HGNC-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:HGNC-UCL.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IDA:HGNC-UCL.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IDA:HGNC-UCL.
DR InterPro; IPR029092; Zwint-1.
DR PANTHER; PTHR31504; PTHR31504; 1.
DR Pfam; PF15556; Zwint; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Kinetochore; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..277
FT /note="ZW10 interactor"
FT /id="PRO_0000066594"
FT REGION 80..155
FT /note="Interaction with NDC80 and ZW10"
FT REGION 228..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..217
FT /evidence="ECO:0000255"
FT COMPBIAS 240..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 174..220
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047660"
FT VARIANT 4
FT /note="A -> S (in dbSNP:rs11005328)"
FT /id="VAR_028783"
FT VARIANT 187
FT /note="R -> G (in dbSNP:rs2241666)"
FT /evidence="ECO:0000269|PubMed:10806105,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_051505"
SQ SEQUENCE 277 AA; 31293 MW; 3335FBA5731AD0DC CRC64;
MEAAETEAEA AALEVLAEVA GILEPVGLQE EAELPAKILV EFVVDSQKKD KLLCSQLQVA
DFLQNILAQE DTAKGLDPLA SEDTSRQKAI AAKEQWKELK ATYREHVEAI KIGLTKALTQ
MEEAQRKRTQ LREAFEQLQA KKQMAMEKRR AVQNQWQLQQ EKHLQHLAEV SAEVRERKTG
TQQELDRVFQ KLGNLKQQAE QERDKLQRYQ TFLQLLYTLQ GKLLFPEAEA EAENLPDDKP
QQPTRPQEQS TGDTMGRDPG VSFKAVGLQP AGDVNLP
