ID   CYK3_YEAST              Reviewed;         885 AA.
AC   Q07533; D6VRN3;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Cytokinesis protein 3;
GN   Name=CYK3; OrderedLocusNames=YDL117W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10959846; DOI=10.1016/s0960-9822(00)00626-6;
RA   Korinek W.S., Bi E., Epp J.A., Wang L., Ho J., Chant J.;
RT   "Cyk3, a novel SH3-domain protein, affects cytokinesis in yeast.";
RL   Curr. Biol. 10:947-950(2000).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-354, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-391, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [9]
RP   SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH INN1.
RX   PubMed=19528296; DOI=10.1083/jcb.200903125;
RA   Nishihama R., Schreiter J.H., Onishi M., Vallen E.A., Hanna J.,
RA   Moravcevic K., Lippincott M.F., Han H., Lemmon M.A., Pringle J.R., Bi E.;
RT   "Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage
RT   furrow and septum formation in S. cerevisiae.";
RL   J. Cell Biol. 185:995-1012(2009).
RN   [10]
RP   SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH INN1.
RX   PubMed=19707790; DOI=10.1007/s00438-009-0476-0;
RA   Jendretzki A., Ciklic I., Rodicio R., Schmitz H.P., Heinisch J.J.;
RT   "Cyk3 acts in actomyosin ring independent cytokinesis by recruiting Inn1 to
RT   the yeast bud neck.";
RL   Mol. Genet. Genomics 282:437-451(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-313, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Involved in cytokinesis by recruiting INN1 to the bud neck.
CC       Cooperates with INN1 to stimulate the synthesis of the primary septum
CC       (PS) by CHS2. {ECO:0000269|PubMed:10959846,
CC       ECO:0000269|PubMed:19528296, ECO:0000269|PubMed:19707790}.
CC   -!- SUBUNIT: Interacts with INN1. {ECO:0000269|PubMed:19528296,
CC       ECO:0000269|PubMed:19707790}.
CC   -!- INTERACTION:
CC       Q07533; Q05080: HOF1; NbExp=5; IntAct=EBI-31510, EBI-5412;
CC       Q07533; P40073: SHO1; NbExp=4; IntAct=EBI-31510, EBI-18140;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Bud neck. Note=Found in association
CC       with the actin ring and the cortex at the mother-bud neck.
CC   -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CYK3 family. {ECO:0000305}.
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DR   EMBL; Z74165; CAA98685.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11743.1; -; Genomic_DNA.
DR   PIR; S67660; S67660.
DR   RefSeq; NP_010166.1; NM_001180176.1.
DR   AlphaFoldDB; Q07533; -.
DR   BioGRID; 31945; 363.
DR   ComplexPortal; CPX-1140; HICS complex.
DR   DIP; DIP-6625N; -.
DR   IntAct; Q07533; 25.
DR   MINT; Q07533; -.
DR   STRING; 4932.YDL117W; -.
DR   iPTMnet; Q07533; -.
DR   MaxQB; Q07533; -.
DR   PaxDb; 4932-YDL117W; -.
DR   PeptideAtlas; Q07533; -.
DR   EnsemblFungi; YDL117W_mRNA; YDL117W; YDL117W.
DR   GeneID; 851440; -.
DR   KEGG; sce:YDL117W; -.
DR   AGR; SGD:S000002275; -.
DR   SGD; S000002275; CYK3.
DR   VEuPathDB; FungiDB:YDL117W; -.
DR   eggNOG; KOG4575; Eukaryota.
DR   HOGENOM; CLU_008674_1_0_1; -.
DR   InParanoid; Q07533; -.
DR   OMA; CTPYELT; -.
DR   OrthoDB; 2788097at2759; -.
DR   BioCyc; YEAST:G3O-29517-MONOMER; -.
DR   BioGRID-ORCS; 851440; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q07533; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q07533; Protein.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0000142; C:cellular bud neck contractile ring; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0044697; C:HICS complex; IPI:SGD.
DR   GO; GO:0016020; C:membrane; NAS:ComplexPortal.
DR   GO; GO:0110085; C:mitotic actomyosin contractile ring; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0030234; F:enzyme regulator activity; IGI:SGD.
DR   GO; GO:1902410; P:mitotic cytokinetic process; NAS:ComplexPortal.
DR   GO; GO:0140278; P:mitotic division septum assembly; IBA:GO_Central.
DR   GO; GO:1990344; P:secondary cell septum biogenesis; IGI:SGD.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   PANTHER; PTHR46333; CYTOKINESIS PROTEIN 3; 1.
DR   PANTHER; PTHR46333:SF6; CYTOKINESIS PROTEIN 3; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Phosphoprotein; Reference proteome;
KW   SH3 domain.
FT   CHAIN           1..885
FT                   /note="Cytokinesis protein 3"
FT                   /id="PRO_0000079751"
FT   DOMAIN          9..70
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          97..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          815..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        815..829
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         313
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         391
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
SQ   SEQUENCE   885 AA;  100621 MW;  A1B7FD5B7076EC7F CRC64;
     MATNLTSLKP PFKVKARYGW SGQTKGDLGF LEGDIMEVTR IAGSWFYGKL LRNKKCSGYF
     PHNFVILLEE RLNSSTENGR QPSKIVESFE KSNKVVIPPV PSRYSDERPR PKKKLSSSMP
     NSPKKPVDSL TKARKAKSKE MVNEKNIYNT QSSRHHNNSA PNLPLASHSK PQVRNFEESM
     NNPLPPLPPL PDLDNMRKTD KRAPKKSYSA NDLHMARSSR EYNYYKDNQK FYDGFIPEKR
     YSLEEDSISS GLFSNSQYLN DSACSSENSF ALMSDFSATS AGSFARHKYA QSFSDSLQRS
     QNANGCSTKI NDSQEFGDSN ASSRNGKMGD ILRKIIIPKR NTNIYSSSVS SPKSPKAYPK
     LPDIQNLNLS ATPDEARDWI AVKCHLNRAR TLTKYDKHPR YMRALEENRD LILHPQDSIY
     NGLNTNEVKG NTKPGLVDVE LAELNIEYID KMTWKRCIRD GTMTLDSWAQ TTFSARYSTV
     LEKLRGIYIF CTEMFALTDD NGTSDFSAEP QNLEKILYRK HCTPYELTWL FKKLANSLGI
     TCEIVIGFLK TPSAINWEFK YNHCWLRILV NKEWRFIDVI LGNVTNPIHE FVNNRKIKKA
     ENSYFLMAPL EMIYTHIPPR EFEQHIVPSI DQLSALYLPL VFPSFFKNEL KLYKFSTALS
     FLEDSEIYEC SLEIPNDVEV FASVVIPTDN EEASSAYRNM ELALTQIKKQ KAESGRRIAL
     IKAVLPPNVN KGSLYIHSGV RGTQTSIANI HPLSMMVPLT HKGSNMKYEF VIKIPSESIQ
     KIELYIVEPQ SRYLFVGNEY SFEVIQSPSD GIVYSSDEGP NQNRKQPMAI KSPSGRVHEL
     VKSDPHFPYG TWKGSIKIKE PGVWSALVIA DSGIGWSVFA EWLCV
//