CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001880
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ras-like protein 2 
Protein Synonyms/Alias
  
Gene Name
 RAS2 
Gene Synonyms/Alias
 ASC1; CTN5; GLC5; YNL098C; N2198 
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
131KSDLENEKQVSYQDGubiquitination[1, 2]
143QDGLNMAKQMNAPFLubiquitination[2]
180DEGGKYNKTLTENDNubiquitination[2]
189LTENDNSKQTSQDTKubiquitination[2]
196KQTSQDTKGSGANSVubiquitination[2]
220MSNAANGKNVNSSTTubiquitination[2]
239RNASIESKTGLAGNQubiquitination[1, 2]
251GNQATNGKTQTDRTNubiquitination[2]
286NRVNNNSKAGQVSNAubiquitination[2]
294AGQVSNAKQARKQQAubiquitination[2]
298SNAKQARKQQAAPGGubiquitination[2]
Reference
 [1] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [2] 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
 The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP. 
Sequence Annotation
 NP_BIND 17 24 GTP (By similarity).
 NP_BIND 64 68 GTP (By similarity).
 NP_BIND 123 126 GTP (By similarity).
 MOTIF 39 47 Effector region (By similarity).
 MOD_RES 198 198 Phosphoserine.
 MOD_RES 202 202 Phosphoserine.
 MOD_RES 207 207 Phosphoserine.
 MOD_RES 214 214 Phosphoserine.
 MOD_RES 235 235 Phosphoserine.
 MOD_RES 238 238 Phosphoserine.
 MOD_RES 319 319 Cysteine methyl ester.
 LIPID 318 318 S-palmitoyl cysteine.
 LIPID 319 319 S-farnesyl cysteine.  
Keyword
 Cell membrane; Complete proteome; Direct protein sequencing; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Palmitate; Phosphoprotein; Prenylation; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 322 AA 
Protein Sequence
MPLNKSNIRE YKLVVVGGGG VGKSALTIQL TQSHFVDEYD PTIEDSYRKQ VVIDDEVSIL 60
DILDTAGQEE YSAMREQYMR NGEGFLLVYS ITSKSSLDEL MTYYQQILRV KDTDYVPIVV 120
VGNKSDLENE KQVSYQDGLN MAKQMNAPFL ETSAKQAINV EEAFYTLARL VRDEGGKYNK 180
TLTENDNSKQ TSQDTKGSGA NSVPRNSGGH RKMSNAANGK NVNSSTTVVN ARNASIESKT 240
GLAGNQATNG KTQTDRTNID NSTGQAGQAN AQSANTVNNR VNNNSKAGQV SNAKQARKQQ 300
AAPGGNTSEA SKSGSGGCCI IS 322 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0005525; F:GTP binding; IDA:SGD.
 GO:0003924; F:GTPase activity; IDA:SGD.
 GO:0007190; P:activation of adenylate cyclase activity; IDA:SGD.
 GO:0030437; P:ascospore formation; IMP:SGD.
 GO:0000411; P:positive regulation of transcription by galactose; IMP:SGD.
 GO:0007124; P:pseudohyphal growth; IMP:SGD.
 GO:0007265; P:Ras protein signal transduction; TAS:SGD.
 GO:0032880; P:regulation of protein localization; IMP:SGD.
 GO:0001302; P:replicative cell aging; IMP:SGD. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR001806; Small_GTPase.
 IPR020849; Small_GTPase_Ras. 
Pfam
 PF00071; Ras 
SMART
 SM00173; RAS 
PROSITE
 PS51421; RAS 
PRINTS
 PR00449; RASTRNSFRMNG.