GIN4_YEAST
ID GIN4_YEAST Reviewed; 1142 AA.
AC Q12263; D6VTC9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Serine/threonine-protein kinase GIN4;
DE EC=2.7.11.1;
DE AltName: Full=Growth inhibitory protein 4;
GN Name=GIN4; OrderedLocusNames=YDR507C; ORFNames=D9719.13;
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 [GENOMIC DNA].
RX PubMed=9813093; DOI=10.1083/jcb.143.3.719;
RA Longtine M.S., Fares H., Pringle J.R.;
RT "Role of the yeast Gin4p protein kinase in septin assembly and the
RT relationship between septin assembly and septin function.";
RL J. Cell Biol. 143:719-736(1998).
RN [2]
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 [3]
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 [4]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP GIN4 COMPLEX.
RX PubMed=12058072; DOI=10.1091/mbc.01-10-0500;
RA Mortensen E.M., McDonald H., Yates J. III, Kellogg D.R.;
RT "Cell cycle-dependent assembly of a Gin4-septin complex.";
RL Mol. Biol. Cell 13:2091-2105(2002).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471 AND SER-689, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805; SER-807 AND SER-930, AND
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-471 AND SER-689, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465; SER-471; SER-617;
RP SER-719; SER-883 AND THR-884, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Serine/threonine-protein kinase which regulates the
CC localization and the function of the septins during mitosis.
CC Phosphorylates SHS1. {ECO:0000269|PubMed:12058072}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Component of the GIN4 complex composed of at least BNI5, CDC3,
CC CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1 which forms a ring at the bud
CC neck. {ECO:0000269|PubMed:12058072}.
CC -!- INTERACTION:
CC Q12263; P32458: CDC11; NbExp=7; IntAct=EBI-7595, EBI-4178;
CC Q12263; P32490: MKK1; NbExp=2; IntAct=EBI-7595, EBI-10968;
CC Q12263; P25293: NAP1; NbExp=11; IntAct=EBI-7595, EBI-11850;
CC Q12263; Q07657: SHS1; NbExp=7; IntAct=EBI-7595, EBI-22083;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Bud neck
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. NIM1 subfamily. {ECO:0000305}.
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DR EMBL; U33140; AAA75513.1; -; Genomic_DNA.
DR EMBL; U33057; AAB64949.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12339.1; -; Genomic_DNA.
DR PIR; S59359; S59359.
DR RefSeq; NP_010795.3; NM_001180815.3.
DR AlphaFoldDB; Q12263; -.
DR SMR; Q12263; -.
DR BioGRID; 32559; 324.
DR ComplexPortal; CPX-1712; Gin4 serine/threonine kinase complex.
DR DIP; DIP-2260N; -.
DR IntAct; Q12263; 21.
DR MINT; Q12263; -.
DR STRING; 4932.YDR507C; -.
DR iPTMnet; Q12263; -.
DR MaxQB; Q12263; -.
DR PaxDb; Q12263; -.
DR PRIDE; Q12263; -.
DR EnsemblFungi; YDR507C_mRNA; YDR507C; YDR507C.
DR GeneID; 852119; -.
DR KEGG; sce:YDR507C; -.
DR SGD; S000002915; GIN4.
DR VEuPathDB; FungiDB:YDR507C; -.
DR eggNOG; KOG0588; Eukaryota.
DR GeneTree; ENSGT00940000166887; -.
DR HOGENOM; CLU_005276_0_0_1; -.
DR InParanoid; Q12263; -.
DR OMA; IFRKLSW; -.
DR BioCyc; YEAST:G3O-30028-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:Q12263; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12263; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:1990317; C:Gin4 complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007117; P:budding cell bud growth; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0044879; P:mitotic morphogenesis checkpoint signaling; IMP:SGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:1901900; P:regulation of protein localization to cell division site; IMP:SGD.
DR GO; GO:0000921; P:septin ring assembly; IMP:SGD.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IC:ComplexPortal.
DR Gene3D; 3.30.310.220; -; 1.
DR InterPro; IPR031850; Fungal_KA1_dom.
DR InterPro; IPR043024; KA1_sf_fungal.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF16797; Fungal_KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1142
FT /note="Serine/threonine-protein kinase GIN4"
FT /id="PRO_0000085964"
FT DOMAIN 19..289
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 378..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 25..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 884
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 1142 AA; 129858 MW; EC16FF4BB49DD811 CRC64;
MAINGNSIPA IKDNTIGPWK LGETLGLGST GKVQLARNGS TGQEAAVKVI SKAVFNTGNV
SGTSIVGSTT PDALPYGIER EIIIMKLLNH PNVLRLYDVW ETNTDLYLVL EYAEKGELFN
LLVERGPLPE HEAIRFFRQI IIGVSYCHAL GIVHRDLKPE NLLLDHKYNI KIADFGMAAL
ETEGKLLETS CGSPHYAAPE IVSGIPYQGF ASDVWSCGVI LFALLTGRLP FDEEDGNIRT
LLLKVQKGEF EMPSDDEISR EAQDLIRKIL TVDPERRIKT RDILKHPLLQ KYPSIRDSKS
IRGLPREDTY LTPLSESNSS IDATILQNLV ILWHGRDPEG IKEKLREPGA NAEKTLYALL
YRFKCDTQKE LIKQQQVKKR QSISSVSVSP SKKVSTTPQR RRNRESLISV TSSRKKPISF
NKFTASSASS SNLTTPGSSK RLSKNFSSKK KLSTIVNQSS PTPASRNKRA SVINVEKNQK
RASIFSTTKK NKRSSRSIKR MSLIPSMKRE SVTTKLMSTY AKLAEDDDWE YIEKETKRTS
SNFATLIDEI FEYEKYEQIR KEKEELERKV REAKAREELE RRRRKQEEKE RARKLLEKED
LKRKQEELKK QIEIDISDLE QELSKHKEEK LDGNIRSISA PMENEEKNIN HLEVDIDNIL
RRRNFSLQTR PVSRLDPGIM FSSPTEEVSP VEPKRTENER LTTEKKILET IRRSKFLGSS
FNIDKELKLS KMEYPSIIAP QRLSEERVVS DSNDGYESLI LPKDGNGVSQ LKDSTATTAP
VSDGRLRKIS EIRVPQFTRK SRHFSESNKR LSVLSMYSTK ESFTNLVDIL KNGNLDVNNQ
QSQRIPTPRS ADDSEFLFET VNEEAEYTGN SSNDERLYDV GDSTIKDKSA LKLNFADRFN
GSNEAKQTDN LHLPILPPLN GDNELRKQNS QEGDQAHPKI KSMIPESGSS SHTEKEEENE
EKEEKKPEQH KQEEDQEKRE KVVDDMEPPL NKSVQKIREK NAGSQAKDHS KDHLKEHKQD
KNTAIGNGSF FRKFSKSSDK TMELYAKISA KQLFNGLEKL LRGWTQYGLK NIKSHPNNLT
LTGKLSSDNI FSLRSTLFEV NIYPRGKMSV VQFKKVSGSF KAVKKLVNEV ENVLNKEGVL
QK
