SKG3_YEAST
ID SKG3_YEAST Reviewed; 1026 AA.
AC Q06315; D6VYJ0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein SKG3;
DE AltName: Full=Suppressor of lethality of KEX2-GAS1 double null mutant protein 3;
GN Name=SKG3; OrderedLocusNames=YLR187W;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 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 [4]
RP DOMAIN, AND INTERACTION WITH PHOSPHATIDYLINOSITOL-3-PHOSPHATE.
RX PubMed=15023338; DOI=10.1016/s1097-2765(04)00083-8;
RA Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B.,
RA Murray D., Emr S.D., Lemmon M.A.;
RT "Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin
RT homology domains.";
RL Mol. Cell 13:677-688(2004).
RN [5]
RP FUNCTION.
RX PubMed=15645486; DOI=10.1002/yea.1206;
RA Tomishige N., Noda Y., Adachi H., Shimoi H., Yoda K.;
RT "SKG1, a suppressor gene of synthetic lethality of kex2Deltagas1Delta
RT mutations, encodes a novel membrane protein that affects cell wall
RT composition.";
RL Yeast 22:141-155(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-701, 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 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-578; SER-592 AND SER-701, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; THR-578; SER-580;
RP SER-592; SER-701 AND SER-954, 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: May play a role in cell wall integrity.
CC {ECO:0000269|PubMed:15645486}.
CC -!- SUBUNIT: Interacts with phosphatidylinositol 3-phosphate.
CC {ECO:0000269|PubMed:15023338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Bud neck
CC {ECO:0000269|PubMed:14562095}. Cell membrane
CC {ECO:0000269|PubMed:14562095}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562095}; Cytoplasmic side
CC {ECO:0000269|PubMed:14562095}.
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DR EMBL; U17246; AAB67456.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09506.1; -; Genomic_DNA.
DR PIR; S51432; S51432.
DR RefSeq; NP_013288.1; NM_001182074.1.
DR AlphaFoldDB; Q06315; -.
DR BioGRID; 31457; 48.
DR DIP; DIP-6525N; -.
DR IntAct; Q06315; 3.
DR MINT; Q06315; -.
DR STRING; 4932.YLR187W; -.
DR iPTMnet; Q06315; -.
DR MaxQB; Q06315; -.
DR PaxDb; Q06315; -.
DR PRIDE; Q06315; -.
DR EnsemblFungi; YLR187W_mRNA; YLR187W; YLR187W.
DR GeneID; 850884; -.
DR KEGG; sce:YLR187W; -.
DR SGD; S000004177; SKG3.
DR VEuPathDB; FungiDB:YLR187W; -.
DR eggNOG; ENOG502QPV9; Eukaryota.
DR GeneTree; ENSGT00940000176380; -.
DR HOGENOM; CLU_006977_1_0_1; -.
DR InParanoid; Q06315; -.
DR OMA; THRRYHK; -.
DR BioCyc; YEAST:G3O-32310-MON; -.
DR PRO; PR:Q06315; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06315; protein.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1026
FT /note="Protein SKG3"
FT /id="PRO_0000269649"
FT DOMAIN 90..221
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 254..433
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 578
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 954
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1026 AA; 114111 MW; 19505E5E694FC47A CRC64;
MKRIFSGVKS PKLSAPPKVF KNDESPSTPS SPKFDQGLRS LSASASRLFS NSISTPGSPT
LDLPQEHSIN GDISPELVPI VTLLSAQAHR RYHYGIFLIL HDLKTDGTPA ARQWEECYGV
LLGTQLALWD AKELSDSKNN KNTSTMKKAA SRPSFINFTD ASVRSLDAND QVIIASENEK
TKKDLDNVLV VSTTLKNRYF LKFKNSKSFK TWNAAIRLSL FEFTALQEAY TGSFLSSRGV
KLGDIKVVMA DTKFTYEDWV SVRFGTGMPW KRCYAVISPQ SGKKKKNSKG SICFYENNKK
TKKSNIMTTV VDARALYAVY PSSPILIDTS TIIKLEGFVS FDKSEEPQET NLFIMPEKHQ
GVPGYDTIIR FLIPAMNAFY LYGRPKGLIA NRTDPDSLLF ALPTLPHIYY LQVDDVLSLT
KDKNYIHWSA ADWRNNIVQV LQKKLSKGYK GCGNKTVSVS SGMMKSPAIS SAELFEGYDS
LPERQMESPQ KSKMKSPTLA STDDINSASA SVNSHATSVK QTELFVTDNS SKINDSVSAQ
SSVTTNFKDT FTTPMTSGML NHENSERSFG SGLKLKITDS NLENMEDVEA KSANEFSTTP
EDKHIHLANA AELSALYDKY STSPFGKSEA NSSPKPQKLE VKDRSKNENR SPYERYVGTS
AESKTFEIGN VRESKSTINT SLSSPLRVED SRRSKNEDLG SLKEFEELSQ KISNMGMANI
SSEALSDTAE NSSFVTDLNL NINNSSSVNL NEEQRVPDFG EENVFDPDYM EQNQMLETES
RYTTDEFDFS DNQDAASSNY SNGQTNRTVT ETLSASDRND KIPHSSLFTN LNQLTSNGGN
YQDREDFSGD QINKPQQSQP LHVKGPQTSS FGYRNSSANS SQPQAPYPVG RPLGKIRTGP
LTVQPMQQGG NSSMYSFQSS QHRFHSSQQR QNQSLSFRNN TYGSGNNQNT FHPSPQLQQQ
PQNMRYLNNK LPINDRSPIP QTQHHVPDGR PSLHINTTNR TNPLTAQSGF SQFMPPNSTS
TNPYSS
