GPB2_YEAST
ID GPB2_YEAST Reviewed; 880 AA.
AC P39717; D6VPG2; P39716;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Guanine nucleotide-binding protein subunit beta 2;
DE AltName: Full=Gbeta mimic kelch protein 2;
GN Name=GPB2; Synonyms=KRH1; OrderedLocusNames=YAL056W;
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], FUNCTION, AND INTERACTION WITH GPA2.
RC STRAIN=Sigma 1278B;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [3]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Fisk D., Cherry J.M.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 661; 802 AND 814-815.
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 [5]
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 [6]
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 [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 SER-24, 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 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 protein). 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 -!- INTERACTION:
CC P39717; P10823: GPA2; NbExp=4; IntAct=EBI-20711, EBI-7382;
CC P39717; P06244: TPK1; NbExp=3; IntAct=EBI-20711, EBI-9458;
CC P39717; P05132: Prkaca; Xeno; NbExp=2; IntAct=EBI-20711, EBI-400564;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Mitochondrion {ECO:0000269|PubMed:14562095}.
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DR EMBL; AB127946; BAD04042.1; -; Genomic_DNA.
DR EMBL; AB127947; BAD04043.1; -; Genomic_DNA.
DR EMBL; U12980; AAC04977.2; -; Genomic_DNA.
DR EMBL; BK006935; DAA06932.2; -; Genomic_DNA.
DR PIR; S51965; S51965.
DR RefSeq; NP_009345.3; NM_001178199.2.
DR AlphaFoldDB; P39717; -.
DR BioGRID; 31773; 114.
DR DIP; DIP-7315N; -.
DR IntAct; P39717; 7.
DR STRING; 4932.YAL056W; -.
DR iPTMnet; P39717; -.
DR MaxQB; P39717; -.
DR PaxDb; P39717; -.
DR PRIDE; P39717; -.
DR EnsemblFungi; YAL056W_mRNA; YAL056W; YAL056W.
DR GeneID; 851243; -.
DR KEGG; sce:YAL056W; -.
DR SGD; S000000052; GPB2.
DR VEuPathDB; FungiDB:YAL056W; -.
DR eggNOG; ENOG502QV98; Eukaryota.
DR GeneTree; ENSGT00940000176635; -.
DR HOGENOM; CLU_015198_0_0_1; -.
DR InParanoid; P39717; -.
DR OMA; MNDLWKI; -.
DR BioCyc; YEAST:G3O-28860-MON; -.
DR PRO; PR:P39717; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39717; 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:0005739; C:mitochondrion; 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:0030437; P:ascospore formation; HMP: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:0046580; P:negative regulation of Ras protein signal transduction; IGI:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; HMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR Gene3D; 2.120.10.80; -; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR SUPFAM; SSF50965; SSF50965; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Kelch repeat; Mitochondrion; Phosphoprotein; Reference proteome;
KW Repeat; Transducer.
FT CHAIN 1..880
FT /note="Guanine nucleotide-binding protein subunit beta 2"
FT /id="PRO_0000119071"
FT REPEAT 291..339
FT /note="Kelch 1"
FT REPEAT 377..425
FT /note="Kelch 2"
FT REPEAT 501..552
FT /note="Kelch 3"
FT REPEAT 691..738
FT /note="Kelch 4"
FT REGION 624..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT VARIANT 215
FT /note="Y -> H (in strain: Sigma 1278B)"
FT VARIANT 221
FT /note="L -> P (in strain: Sigma 1278B)"
FT VARIANT 552
FT /note="S -> R (in strain: Sigma 1278B)"
FT VARIANT 674
FT /note="A -> T (in strain: Sigma 1278B)"
FT VARIANT 777
FT /note="P -> S (in strain: Sigma 1278B)"
FT CONFLICT 661
FT /note="V -> I (in Ref. 2; AAC04977)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="C -> F (in Ref. 2; AAC04977)"
FT /evidence="ECO:0000305"
FT CONFLICT 814..815
FT /note="ED -> AA (in Ref. 2; AAC04977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 880 AA; 98656 MW; 343627001C52020E CRC64;
MEISSSPWND GGYSPYERNR VAVSPFSSAL EGEERIETSR SLGDHCFEPL PYVTNYLSIF
ALFGKEIFGD KGNVSSRNEY LLKKYYSLKK PFVLRHNGHA LKNPDMPLQR NDILQTNFMV
DKFLNRTVRS VNFNNFKIIS DMQSKSGRGT KSGTNQNQSA DAIQNICLPS IPSALPYFQY
YRKLLTVNTK EWDILKLHSL WVPKLRKDFK DFSLYGDKNS LKPIDSHYDE DNTMKKNLFF
ERSPSRQTLD GKGCASKGYD ISSGNMIIPS LFSEDKLPAL TYHCSVELNG NIYIFGGLMP
CYSYEEDAPM LNDFFVDGIK NLPPPLLPQV INNPSMVNNP HLYVASIPSC RFSKPKMGGY
IPPPLLCVQG SKLTDRHIFF YGGFEIRTET RGDENGKYHL KKRLYVNNTG YILDIMSFKF
TKIDIIVQPS KYNAYPTMSS RFGHLQISID NPNRRASVHS SSMNEIHKMG SASMKQGSSI
TSGRLEKAAV LSSLPHNTVH TVIIFGGYRQ TGDDRYEAMN DLWKIEIPVI RRGKKGYCKF
SETANAILLT PSEKDKSDWP EERAFSAFSV HGTSLMDRSS LDMRLLNNLK NHFVLKPSYI
SQDRVVSPKP VFPMMVHGTH QDLFNSGSAA QESPKAGASA SSASAASFDP DMDDNLENYI
VNPGRKSSSI PMTAIGRQRL ILSQEKPVGK TVVLHGGSNG LNVLDDMWLM DLECETWTPI
ETFAKADSSE DGDEKLDSVN VGLVGHRMES IGRICVCIGG MVQEDVDQFY SENDDEPPRK
RKVDTLPLGG NFLNTIDLST QCWEEHKITL SKKEDDEDRQ DSENEDTNSN IVVGVGGTSL
QCDKSIILIG GLISRRSNVK EIYLHGTITK SIFPSVNPSA
