Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-559292-00025
Entry Name
UniProt Accession
Theoretical PI
5.97
Molecular Weight
23152.45
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
GTP-binding protein RHO1
Protein Synonyms/Alias
Rho-type GTPase 1;
Gene Name
RHO1
Gene Synonyms/Alias
YPR165W; P9325.3;
Created Date
01-JAN-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
206
Canonical
TEKKKKKCVLL****
[1]
S-Geranylgeranylation
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
NCBI Taxa ID
559292
Reference
[1] Inoue SB, Qadota H, Arisawa M, Watanabe T, Ohya Y. Prenylation of Rho1p isrequired for activation of yeast 1, 3-beta-glucan synthase. J Biol Chem. 1999 Dec31;274(53):38119-24.[PMID:10608882]
Functional Description
Acts as a central regulator in the cell wall integrity signaling pathway, which is regulated by the cell cycle and in response to various types of cell wall stress. Integrates signals from different cell surface sensors, and activates a set of effectors, regulating processes including beta-glucan synthesis at the site of wall remodeling, gene expression related to cell wall biogenesis, organization of the actin cytoskeleton, and protein- and secretory vesicle-targeting to the growth site. Activates the protein kinase C (PKC1) MAP kinase cascade, the beta-1,3-glucan synthase (FKS1), the formin BNI1, the exocyst component SEC3 and the transcription factor SKN7.
Sequence Annotation
Nucleotide-binding: 17 24 GTP.
Nucleotide-binding: 64 68 GTP.
Nucleotide-binding: 122 125 GTP.
Motif: 39 47 Effector region.
Modified residue: 2 2 N-acetylserine.
Modified residue: 206 206 Cysteine methyl ester.
Protein Length
209 AA.
Protein Sequence
(Canonical)
MSQQVGNSIR RKLVIVGDGA CGKTCLLIVF SKGQFPEVYV PTVFENYVAD VEVDGRRVEL  60
ALWDTAGQED YDRLRPLSYP DSNVVLICFS IDLPDSLENV QEKWIAEVLH FCQGVPIILV  120
GCKVDLRNDP QTIEQLRQEG QQPVTSQEGQ SVADQIGATG YYECSAKTGY GVREVFEAAT  180
RASLMGKSKT NGKAKKNTTE KKKKKCVLL                                    209
FASTA
(Canonical)
>LipidDB-559292-00025|P06780
MSQQVGNSIRRKLVIVGDGACGKTCLLIVFSKGQFPEVYVPTVFENYVADVEVDGRRVEL
ALWDTAGQEDYDRLRPLSYPDSNVVLICFSIDLPDSLENVQEKWIAEVLHFCQGVPIILV
GCKVDLRNDPQTIEQLRQEGQQPVTSQEGQSVADQIGATGYYECSAKTGYGVREVFEAAT
RASLMGKSKTNGKAKKNTTEKKKKKCVLL
Gene Ontology
GO:0000148; C:1,3-beta-D-glucan synthase complex; IDA:SGD
GO:0005935; C:cellular bud neck; IDA:SGD
GO:0005934; C:cellular bud tip; IDA:SGD
GO:0005768; C:endosome; IEA:UniProtKB-KW
GO:0005794; C:Golgi apparatus; IDA:SGD
GO:0000131; C:incipient cellular bud site; IDA:SGD
GO:0043332; C:mating projection tip; IDA:SGD
GO:0005777; C:peroxisome; IDA:SGD
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IDA:SGD
GO:0030036; P:actin cytoskeleton organization; IMP:SGD
GO:0031532; P:actin cytoskeleton reorganization; IGI:SGD
GO:0007117; P:budding cell bud growth; IMP:SGD
GO:0006184; P:GTP catabolic process; IDA:GOC
GO:0045807; P:positive regulation of endocytosis; IMP:SGD
GO:0090037; P:positive regulation of protein kinase C signaling; IDA:SGD
GO:0008361; P:regulation of cell size; IMP:SGD
GO:0090334; P:regulation of cell wall (1->3)-beta-D-glucan biosynthetic process; IDA:SGD
GO:0060178; P:regulation of exocyst localization; IMP:SGD
GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD
GO:0032880; P:regulation of protein localization; IMP:SGD
GO:0032889; P:regulation of vacuole fusion, non-autophagic; IMP:SGD
GO:0007264; P:small GTPase mediated signal transduction; IDA:SGD
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR003578; Small_GTPase_Rho
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00174; RHO;
PROSITE
PROSITE; PS51420; RHO;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;