GPB1_YEAST
ID GPB1_YEAST Reviewed; 897 AA.
AC Q08886; D6W364;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Guanine nucleotide-binding protein subunit beta 1;
DE AltName: Full=Gbeta mimic kelch protein 1;
GN Name=GPB1; Synonyms=KRH2; OrderedLocusNames=YOR371C;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 INTERACTION WITH GPA2.
RX PubMed=12150916; DOI=10.1016/s1097-2765(02)00569-5;
RA Harashima T., Heitman J.;
RT "The Galpha protein Gpa2 controls yeast differentiation by interacting with
RT kelch repeat proteins that mimic Gbeta subunits.";
RL Mol. Cell 10:163-173(2002).
RN [4]
RP FUNCTION.
RX PubMed=12538771; DOI=10.1242/jcs.00266;
RA Batlle M., Lu A., Green D.A., Xue Y., Hirsch J.P.;
RT "Krh1p and Krh2p act downstream of the Gpa2p G(alpha) subunit to negatively
RT regulate haploid invasive growth.";
RL J. Cell Sci. 116:701-710(2003).
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 FUNCTION.
RX PubMed=16278446; DOI=10.1128/ec.4.11.1794-1800.2005;
RA Lu A., Hirsch J.P.;
RT "Cyclic AMP-independent regulation of protein kinase A substrate
RT phosphorylation by Kelch repeat proteins.";
RL Eukaryot. Cell 4:1794-1800(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND THR-161, 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: Beta subunit of a guanine nucleotide-binding protein (G
CC proteins). G proteins are involved as modulators or transducers in
CC various transmembrane signaling systems. The beta and gamma chains are
CC required for the GTPase activity, for replacement of GDP by GTP, and
CC for G protein-effector interaction. Involved in the determination of
CC the cAMP level according to nutritional conditions, most probably as a
CC regulator of cAMP phosphodiesterase. Required for the control of
CC pseudohyphal and haploid invasive growth. {ECO:0000269|PubMed:12150916,
CC ECO:0000269|PubMed:12538771, ECO:0000269|PubMed:16278446}.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC GPB1 interacts with the alpha subunit GPA2.
CC {ECO:0000269|PubMed:12150916}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1640 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z75279; CAA99702.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11130.1; -; Genomic_DNA.
DR PIR; S67283; S67283.
DR RefSeq; NP_015016.3; NM_001183791.3.
DR AlphaFoldDB; Q08886; -.
DR BioGRID; 34754; 50.
DR DIP; DIP-2979N; -.
DR IntAct; Q08886; 1.
DR STRING; 4932.YOR371C; -.
DR iPTMnet; Q08886; -.
DR MaxQB; Q08886; -.
DR PaxDb; Q08886; -.
DR PRIDE; Q08886; -.
DR EnsemblFungi; YOR371C_mRNA; YOR371C; YOR371C.
DR GeneID; 854553; -.
DR KEGG; sce:YOR371C; -.
DR SGD; S000005898; GPB1.
DR VEuPathDB; FungiDB:YOR371C; -.
DR eggNOG; ENOG502QV98; Eukaryota.
DR GeneTree; ENSGT00940000176635; -.
DR HOGENOM; CLU_015198_0_0_1; -.
DR InParanoid; Q08886; -.
DR OMA; STATHIC; -.
DR BioCyc; YEAST:G3O-33839-MON; -.
DR PRO; PR:Q08886; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08886; protein.
DR GO; GO:0051285; C:cell cortex of cell tip; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IGI:SGD.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:SGD.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IMP:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IGI:SGD.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IGI:SGD.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:SGD.
DR Gene3D; 2.120.10.80; -; 1.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR SUPFAM; SSF117281; SSF117281; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Kelch repeat; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..897
FT /note="Guanine nucleotide-binding protein subunit beta 1"
FT /id="PRO_0000239649"
FT REPEAT 304..352
FT /note="Kelch 1"
FT REPEAT 390..438
FT /note="Kelch 2"
FT REPEAT 543..589
FT /note="Kelch 3"
FT REPEAT 715..761
FT /note="Kelch 4"
FT REGION 464..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 897 AA; 100940 MW; DEA78275A515BC29 CRC64;
MPQASTFGSH SLEAHPLHIQ PAVHIKLSKE ERSHYREQYD SLKYISNYVS VFDQALSDNI
DSRIRKENEA LLKKYYESRK PFTFTSFRQG SVISSSDSST GFTERTKTYC FLNDFVSNCV
NEVDPYTLKM TVRNRNTALN MENLDDERKS KDDIYDFEDN TDDECNAKCH GAFHYSSERL
EILRSRSTIS YFKYYKKLLT VDLRDSDVLK RHNLWMPMIT RRFRFLLVSS SKPEDVRLTT
PIPTFSESDL DIFKNKTCPL FINGTDCVPR SYDTFSGSSV IASIFSEYKL PSLSYHCSVE
LNDQLFIVGG LMACHRYDEE APDLKDFYVD GIKNLPPPLI PELINNPSMI PNPHLYCFSL
TSSRLTRPDI SGYIPPPLVC TQGCKLTERH IFLYGGFEIK SETQVDDKGR YFIRKRAFLN
NTGYILDTVT FNFSKIELVA PPYQFAIYNN FSPRFGHMQA SISNSNNNVS NENTTTSAKG
RRSISPYRQG NGDHKIDDLV GSPGSTDYLE DDAIPPVTNP RSTDSLSSKH CSTATHICSS
VNTILIFGGY SQTGDDKYEA MNDMWKINIP VVSRGKRNYY KFADTVTATK IPIIDDPELW
PSRRAFSACC VPDYFTKDVE PIETRLLRNL KNDFSIDLEI RPGNKPSQPL FPNIPHSRKE
KKSGRDSMHI SNSNNSTSED TSSKSTRNTT SSPPTSPKHT PPLNPSKKCA SIGRTIAFHG
GSDGYDVCSD MWWFDFDSET WTKIDLYAKT QEESDGLVPI NLCMVGHSMT TVGHKVVLIG
GLRQGDVDRI YRDETLPEEV ISGVPLGSGV INVVDLNTQC LQGCKLIRND GDTKESVIMD
PHVGTPHQVL AVAGTIELVK GTMTLIGGVV AGREDISSLY LRGAVLQFIL PSMNLAN
