CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003842
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Guanine nucleotide-binding protein alpha-2 subunit 
Protein Synonyms/Alias
 GP2-alpha 
Gene Name
 GPA2 
Gene Synonyms/Alias
 SSP101; YER020W 
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
52NTANQQEKQQQRQQQubiquitination[1]
122ASSGSNDKELKVLLLubiquitination[1]
394TGGSDINKAAKYILWubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Alpha subunit of the heterotrimeric guanine nucleotide- binding protein (G protein) involved in glucose-induced cAMP signaling. Binds to its cognate transmembrane receptor GPR1, which senses extracellular carbon sources, and activates cAMP-PKA signaling and governs diploid pseudohyphal differentiation and haploid invasive growth. The G protein beta-mimic proteins GPB1 and GPB2 inhibit GPA2-GPR1 coupling, probably to reduce signaling in the absence of glucose. 
Sequence Annotation
 NP_BIND 130 137 GTP (By similarity).
 NP_BIND 270 276 GTP (By similarity).
 NP_BIND 296 300 GTP (By similarity).
 NP_BIND 365 368 GTP (By similarity).
 METAL 137 137 Magnesium (By similarity).
 METAL 276 276 Magnesium (By similarity).
 BINDING 420 420 GTP; via amide nitrogen (By similarity).
 LIPID 2 2 N-myristoyl glycine.
 LIPID 4 4 S-palmitoyl cysteine.  
Keyword
 Cell membrane; Complete proteome; GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate; Nucleotide-binding; Palmitate; Reference proteome; Transducer. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 449 AA 
Protein Sequence
MGLCASSEKN GSTPDTQTAS AGSDNVGKAK VPPKQEPQKT VRTVNTANQQ EKQQQRQQQP 60
SPHNVKDRKE QNGSINNAIS PTATANTSGS QQINIDSALR DRSSNVAAQP SLSDASSGSN 120
DKELKVLLLG AGESGKSTVL QQLKILHQNG FSEQEIKEYI PLIYQNLLEI GRNLIQARTR 180
FNVNLEPECE LTQQDLSRTM SYEMPNNYTG QFPEDIAGVI STLWALPSTQ DLVNGPNASK 240
FYLMDSTPYF MENFTRITSP NYRPTQQDIL RSRQMTSGIF DTVIDMGSDI KMHIYDVGGQ 300
RSERKKWIHC FDNVTLVIFC VSLSEYDQTL MEDKNQNRFQ ESLVLFDNIV NSRWFARTSV 360
VLFLNKIDLF AEKLSKVPME NYFPDYTGGS DINKAAKYIL WRFVQLNRAN LSIYPHVTQA 420
TDTSNIRLVF AAIKETILEN TLKDSGVLQ 449 
Gene Ontology
 GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome.
 GO:0001664; F:G-protein coupled receptor binding; IBA:RefGenome.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004871; F:signal transducer activity; IBA:RefGenome.
 GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IMP:SGD.
 GO:0030437; P:ascospore formation; IMP:SGD.
 GO:0010255; P:glucose mediated signaling pathway; IMP:SGD.
 GO:0007124; P:pseudohyphal growth; IMP:SGD.
 GO:0008361; P:regulation of cell size; IMP:SGD.
 GO:0001302; P:replicative cell aging; IMP:SGD. 
Interpro
 IPR002975; Fungi_Gprotein_alpha.
 IPR001019; Gprotein_alpha_su.
 IPR011025; GproteinA_insert.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00503; G-alpha 
SMART
 SM00275; G_alpha 
PROSITE
  
PRINTS
 PR00318; GPROTEINA.
 PR01241; GPROTEINAFNG.