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Protein

GTP-binding protein RHO1

Gene

RHO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 SKN7.15 Publications

Enzyme regulationi

Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the guanine nucleotide-exchange factors (GEFs) ROM1, ROM2 and TUS1, and inactivated by GTPase-activating proteins (GAPs) BAG7, BEM2, LRG1, and SAC7, and the Rho GDP-dissociation inhibitor RDI1. The different GAPs regulate RHO1 in a target-specific manner.8 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi17 – 24GTPBy similarity8
Nucleotide bindingi64 – 68GTPBy similarity5
Nucleotide bindingi122 – 125GTPBy similarity4

GO - Molecular functioni

  • GTPase activity Source: SGD
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • actin cytoskeleton organization Source: SGD
  • actin cytoskeleton reorganization Source: SGD
  • budding cell bud growth Source: SGD
  • cellular bud neck septin ring organization Source: SGD
  • positive regulation of endocytosis Source: SGD
  • positive regulation of protein kinase C signaling Source: SGD
  • regulation of cell size Source: SGD
  • regulation of cell wall (1->3)-beta-D-glucan biosynthetic process Source: SGD
  • regulation of exocyst localization Source: SGD
  • regulation of fungal-type cell wall organization Source: SGD
  • regulation of protein localization Source: SGD
  • regulation of secondary cell septum biogenesis Source: SGD
  • regulation of vacuole fusion, non-autophagic Source: SGD
  • small GTPase mediated signal transduction Source: SGD
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34294-MONOMER.
ReactomeiR-SCE-114604. GPVI-mediated activation cascade.
R-SCE-193634. Axonal growth inhibition (RHOA activation).
R-SCE-194840. Rho GTPase cycle.
R-SCE-198203. PI3K/AKT activation.
R-SCE-392451. G beta:gamma signalling through PI3Kgamma.
R-SCE-3928663. EPHA-mediated growth cone collapse.
R-SCE-416482. G alpha (12/13) signalling events.
R-SCE-416572. Sema4D induced cell migration and growth-cone collapse.
R-SCE-4420097. VEGFA-VEGFR2 Pathway.
R-SCE-5625740. RHO GTPases activate PKNs.
R-SCE-5627117. RHO GTPases Activate ROCKs.
R-SCE-5666185. RHO GTPases Activate Rhotekin and Rhophilins.
R-SCE-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding protein RHO1
Alternative name(s):
Rho-type GTPase 1
Gene namesi
Name:RHO1
Ordered Locus Names:YPR165W
ORF Names:P9325.3
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR165W.
SGDiS000006369. RHO1.

Subcellular locationi

GO - Cellular componenti

  • 1,3-beta-D-glucan synthase complex Source: SGD
  • cellular bud neck Source: SGD
  • cellular bud tip Source: SGD
  • endosome membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: SGD
  • incipient cellular bud site Source: SGD
  • mating projection tip Source: SGD
  • peroxisomal membrane Source: UniProtKB-SubCell
  • peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi22G → A: Abolishes GTP-binding. 1
Mutagenesisi24T → N: Abolishes GTP-binding. 1 Publication1
Mutagenesisi42T → A: Impairs interaction with targets. 1 Publication1
Mutagenesisi43V → T: Temperature sensitive growth defect. 1 Publication1
Mutagenesisi44F → Y: Temperature sensitive growth defect. 1 Publication1
Mutagenesisi45E → I: Temperature sensitive growth defect. 2 Publications1
Mutagenesisi45E → V in RHO1-2; temperature sensitive, fails to activate PKC1. 2 Publications1
Mutagenesisi60L → P in RHO1-3; temperature sensitive, severely decreases beta-1,3-glucan synthase activation. 1 Publication1
Mutagenesisi68Q → H: Locks RHO1 in the GTP-bound form by abolishing GTP hydrolysis. 1 Publication1
Mutagenesisi70D → G in RHO1-10; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with P-165. 1 Publication1
Mutagenesisi102E → K in RHO1-11; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with E-166. 1 Publication1
Mutagenesisi104W → R in RHO1-4; temperature sensitive, severely decreases beta-1,3-glucan synthase activation. 1 Publication1
Mutagenesisi121G → C in RHO1-5; temperature sensitive, fails to activate PCK1. 1 Publication1
Mutagenesisi165S → P in RHO1-10; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with G-69. 1 Publication1
Mutagenesisi167K → E in RHO1-11; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with K-101. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001989452 – 206GTP-binding protein RHO1Add BLAST205
PropeptideiPRO_0000281275207 – 209Removed in mature form3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei206Cysteine methyl esterBy similarity1
Lipidationi206S-geranylgeranyl cysteineBy similarity1

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP06780.
PRIDEiP06780.

Interactioni

Subunit structurei

Interacts with the GAPs BAG7, LRG1, SAC7, and with RDI1. Interacts with the 1,3-beta-glucan synthase component FKS1, with protein kinase PKC1, with the G protein beta subunit STE4 and with SKN7.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FKS1P386313EBI-15121,EBI-7708

Protein-protein interaction databases

BioGridi36338. 103 interactors.
DIPiDIP-1040N.
IntActiP06780. 7 interactors.
MINTiMINT-399819.

Structurei

Secondary structure

1209
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 18Combined sources10
Helixi23 – 31Combined sources9
Beta strandi45 – 53Combined sources9
Beta strandi56 – 64Combined sources9
Helixi69 – 77Combined sources9
Beta strandi83 – 90Combined sources8
Helixi94 – 102Combined sources9
Helixi104 – 111Combined sources8
Beta strandi117 – 122Combined sources6
Helixi124 – 126Combined sources3
Helixi130 – 138Combined sources9
Helixi146 – 155Combined sources10
Beta strandi161 – 163Combined sources3
Turni166 – 168Combined sources3
Helixi172 – 184Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A58X-ray2.60B/D/F1-188[»]
ProteinModelPortaliP06780.
SMRiP06780.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06780.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi39 – 47Effector regionBy similarity9

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
InParanoidiP06780.
KOiK04513.
OMAiAYKSLEC.
OrthoDBiEOG092C4TDG.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06780-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQQVGNSIR RKLVIVGDGA CGKTCLLIVF SKGQFPEVYV PTVFENYVAD
60 70 80 90 100
VEVDGRRVEL ALWDTAGQED YDRLRPLSYP DSNVVLICFS IDLPDSLENV
110 120 130 140 150
QEKWIAEVLH FCQGVPIILV GCKVDLRNDP QTIEQLRQEG QQPVTSQEGQ
160 170 180 190 200
SVADQIGATG YYECSAKTGY GVREVFEAAT RASLMGKSKT NGKAKKNTTE

KKKKKCVLL
Length:209
Mass (Da):23,152
Last modified:January 23, 2007 - v3
Checksum:i630B17E9E34CFE75
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15189 Genomic DNA. Translation: AAA34977.1.
U25840 Genomic DNA. Translation: AAB68152.1.
M15161 Genomic DNA. Translation: AAA74729.1.
AY558062 Genomic DNA. Translation: AAS56388.1.
BK006949 Genomic DNA. Translation: DAA11582.1.
PIRiA26587. TVBYH1.
RefSeqiNP_015491.1. NM_001184262.1.

Genome annotation databases

EnsemblFungiiYPR165W; YPR165W; YPR165W.
GeneIDi856294.
KEGGisce:YPR165W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15189 Genomic DNA. Translation: AAA34977.1.
U25840 Genomic DNA. Translation: AAB68152.1.
M15161 Genomic DNA. Translation: AAA74729.1.
AY558062 Genomic DNA. Translation: AAS56388.1.
BK006949 Genomic DNA. Translation: DAA11582.1.
PIRiA26587. TVBYH1.
RefSeqiNP_015491.1. NM_001184262.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A58X-ray2.60B/D/F1-188[»]
ProteinModelPortaliP06780.
SMRiP06780.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36338. 103 interactors.
DIPiDIP-1040N.
IntActiP06780. 7 interactors.
MINTiMINT-399819.

Proteomic databases

MaxQBiP06780.
PRIDEiP06780.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR165W; YPR165W; YPR165W.
GeneIDi856294.
KEGGisce:YPR165W.

Organism-specific databases

EuPathDBiFungiDB:YPR165W.
SGDiS000006369. RHO1.

Phylogenomic databases

GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
InParanoidiP06780.
KOiK04513.
OMAiAYKSLEC.
OrthoDBiEOG092C4TDG.

Enzyme and pathway databases

BioCyciYEAST:G3O-34294-MONOMER.
ReactomeiR-SCE-114604. GPVI-mediated activation cascade.
R-SCE-193634. Axonal growth inhibition (RHOA activation).
R-SCE-194840. Rho GTPase cycle.
R-SCE-198203. PI3K/AKT activation.
R-SCE-392451. G beta:gamma signalling through PI3Kgamma.
R-SCE-3928663. EPHA-mediated growth cone collapse.
R-SCE-416482. G alpha (12/13) signalling events.
R-SCE-416572. Sema4D induced cell migration and growth-cone collapse.
R-SCE-4420097. VEGFA-VEGFR2 Pathway.
R-SCE-5625740. RHO GTPases activate PKNs.
R-SCE-5627117. RHO GTPases Activate ROCKs.
R-SCE-5666185. RHO GTPases Activate Rhotekin and Rhophilins.
R-SCE-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP06780.
PROiP06780.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRHO1_YEAST
AccessioniPrimary (citable) accession number: P06780
Secondary accession number(s): D6W4G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 180 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.