Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-559292-00914
Entry Name
UniProt Accession
Theoretical PI
6.77
Molecular Weight
34705.2
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
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
318
Canonical
SKSGSGGCCIIS***
[1][2]
S-Palmitoylation
319
Canonical
KSGSGGCCIIS****
[3]
S-Farnesylation
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
NCBI Taxa ID
559292
Reference
[1] Deschenes RJ, Broach JR. Fatty acylation is important but not essential forSaccharomyces cerevisiae RAS function. Mol Cell Biol. 1987 Jul;7(7):2344-51.[PMID:3302674]
[2] Dong X, Mitchell DA, Lobo S, Zhao L, Bartels DJ, Deschenes RJ. Palmitoylation and plasma membrane localization of Ras2p by a nonclassical trafficking pathwayin Saccharomyces cerevisiae. Mol Cell Biol. 2003 Sep;23(18):6574-84.[PMID:12944483]
[3] He B, Chen P, Chen SY, Vancura KL, Michaelis S, Powers S. RAM2, an essentialgene of yeast, and RAM1 encode the two polypeptide components of thefarnesyltransferase that prenylates a-factor and Ras proteins. Proc Natl Acad SciU S A. 1991 Dec 15;88(24):11373-7.[PMID:1763050]
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
Nucleotide-binding: 17 24 GTP.
Nucleotide-binding: 64 68 GTP.
Nucleotide-binding: 123 126 GTP.
Motif: 39 47 Effector region.
Modified residue: 198 198 Phosphoserine.
Modified residue: 202 202 Phosphoserine.
Modified residue: 207 207 Phosphoserine.
Modified residue: 214 214 Phosphoserine.
Modified residue: 235 235 Phosphoserine.
Modified residue: 238 238 Phosphoserine.
Modified residue: 319 319 Cysteine methyl ester.
Protein Length
322 AA.
Protein Sequence
(Canonical)
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
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
FASTA
(Canonical)
>LipidDB-559292-00914|P01120
MPLNKSNIREYKLVVVGGGGVGKSALTIQLTQSHFVDEYDPTIEDSYRKQVVIDDEVSIL
DILDTAGQEEYSAMREQYMRNGEGFLLVYSITSKSSLDELMTYYQQILRVKDTDYVPIVV
VGNKSDLENEKQVSYQDGLNMAKQMNAPFLETSAKQAINVEEAFYTLARLVRDEGGKYNK
TLTENDNSKQTSQDTKGSGANSVPRNSGGHRKMSNAANGKNVNSSTTVVNARNASIESKT
GLAGNQATNGKTQTDRTNIDNSTGQAGQANAQSANTVNNRVNNNSKAGQVSNAKQARKQQ
AAPGGNTSEASKSGSGGCCIIS
MPLNKSNIREYKLVVVGGGGVGKSALTIQLTQSHFVDEYDPTIEDSYRKQVVIDDEVSIL
DILDTAGQEEYSAMREQYMRNGEGFLLVYSITSKSSLDELMTYYQQILRVKDTDYVPIVV
VGNKSDLENEKQVSYQDGLNMAKQMNAPFLETSAKQAINVEEAFYTLARLVRDEGGKYNK
TLTENDNSKQTSQDTKGSGANSVPRNSGGHRKMSNAANGKNVNSSTTVVNARNASIESKT
GLAGNQATNGKTQTDRTNIDNSTGQAGQANAQSANTVNNRVNNNSKAGQVSNAKQARKQQ
AAPGGNTSEASKSGSGGCCIIS
Gene Ontology
GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD
GO:0005739; C:mitochondrion; IDA:SGD
GO:0005634; C:nucleus; 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:0045762; P:positive regulation of adenylate cyclase activity; IGI:SGD
GO:0000411; P:positive regulation of transcription by galactose; IMP:SGD
GO:0097271; P:protein localization to bud neck; IGI:SGD
GO:0007124; P:pseudohyphal growth; IMP:SGD
GO:0032880; P:regulation of protein localization; IMP:SGD
GO:0001302; P:replicative cell aging; IMP:SGD
GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR020849; Small_GTPase_Ras
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00173; RAS;
PROSITE
PROSITE; PS51421; RAS;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;