| Tag | Content |
|---|
| CPLM ID | CPLM-011640 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Guanine nucleotide-binding protein subunit beta 1 |
Protein Synonyms/Alias | Gbeta mimic kelch protein 1 |
Gene Name | GPB1 |
Gene Synonyms/Alias | KRH2; YOR371C |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 66 | NIDSRIRKENEALLK | ubiquitination | [1] |
|
Reference | [1] Identification, analysis, and prediction of protein ubiquitination sites. Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM. Proteins. 2010 Feb 1;78(2):365-80. [ PMID: 19722269] |
Functional Description | Beta subunit of a guanine nucleotide-binding protein (G proteins). G proteins are involved as modulators or transducers in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Involved in the determination of the cAMP level according to nutritional conditions, most probably as a regulator of cAMP phosphodiesterase. Required for the control of pseudohyphal and haploid invasive growth. |
Sequence Annotation | REPEAT 304 352 Kelch 1.
REPEAT 390 438 Kelch 2.
REPEAT 543 589 Kelch 3.
REPEAT 715 761 Kelch 4.
MOD_RES 91 91 Phosphoserine.
MOD_RES 161 161 Phosphothreonine. |
Keyword | Complete proteome; Cytoplasm; Kelch repeat; Phosphoprotein; Reference proteome; Repeat. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 897 AA |
Protein Sequence | MPQASTFGSH SLEAHPLHIQ PAVHIKLSKE ERSHYREQYD SLKYISNYVS VFDQALSDNI 60
DSRIRKENEA LLKKYYESRK PFTFTSFRQG SVISSSDSST GFTERTKTYC FLNDFVSNCV 120
NEVDPYTLKM TVRNRNTALN MENLDDERKS KDDIYDFEDN TDDECNAKCH GAFHYSSERL 180
EILRSRSTIS YFKYYKKLLT VDLRDSDVLK RHNLWMPMIT RRFRFLLVSS SKPEDVRLTT 240
PIPTFSESDL DIFKNKTCPL FINGTDCVPR SYDTFSGSSV IASIFSEYKL PSLSYHCSVE 300
LNDQLFIVGG LMACHRYDEE APDLKDFYVD GIKNLPPPLI PELINNPSMI PNPHLYCFSL 360
TSSRLTRPDI SGYIPPPLVC TQGCKLTERH IFLYGGFEIK SETQVDDKGR YFIRKRAFLN 420
NTGYILDTVT FNFSKIELVA PPYQFAIYNN FSPRFGHMQA SISNSNNNVS NENTTTSAKG 480
RRSISPYRQG NGDHKIDDLV GSPGSTDYLE DDAIPPVTNP RSTDSLSSKH CSTATHICSS 540
VNTILIFGGY SQTGDDKYEA MNDMWKINIP VVSRGKRNYY KFADTVTATK IPIIDDPELW 600
PSRRAFSACC VPDYFTKDVE PIETRLLRNL KNDFSIDLEI RPGNKPSQPL FPNIPHSRKE 660
KKSGRDSMHI SNSNNSTSED TSSKSTRNTT SSPPTSPKHT PPLNPSKKCA SIGRTIAFHG 720
GSDGYDVCSD MWWFDFDSET WTKIDLYAKT QEESDGLVPI NLCMVGHSMT TVGHKVVLIG 780
GLRQGDVDRI YRDETLPEEV ISGVPLGSGV INVVDLNTQC LQGCKLIRND GDTKESVIMD 840
PHVGTPHQVL AVAGTIELVK GTMTLIGGVV AGREDISSLY LRGAVLQFIL PSMNLAN 897 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:SGD. GO:0005886; C:plasma membrane; IGI:SGD. GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IGI:SGD. GO:0004871; F:signal transducer activity; IPI:SGD. GO:0010255; P:glucose mediated signaling pathway; IMP:SGD. GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD. GO:0046580; P:negative regulation of Ras protein signal transduction; IGI:SGD. GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:SGD. GO:0000209; P:protein polyubiquitination; IDA:SGD. GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:SGD. GO:0007124; P:pseudohyphal growth; IMP:SGD. |
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