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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 248GTPBy similarity
Nucleotide bindingi64 – 685GTPBy similarity
Nucleotide bindingi122 – 1254GTPBy similarity

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
  • protein transport Source: InterPro
  • 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-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-5625900. RHO GTPases activate CIT.
R-SCE-5627117. RHO GTPases Activate ROCKs.
R-SCE-5666185. RHO GTPases Activate Rhotekin and Rhophilins.
R-SCE-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221G → A: Abolishes GTP-binding.
Mutagenesisi24 – 241T → N: Abolishes GTP-binding. 1 Publication
Mutagenesisi42 – 421T → A: Impairs interaction with targets. 1 Publication
Mutagenesisi43 – 431V → T: Temperature sensitive growth defect. 1 Publication
Mutagenesisi44 – 441F → Y: Temperature sensitive growth defect. 1 Publication
Mutagenesisi45 – 451E → I: Temperature sensitive growth defect. 2 Publications
Mutagenesisi45 – 451E → V in RHO1-2; temperature sensitive, fails to activate PKC1. 2 Publications
Mutagenesisi60 – 601L → P in RHO1-3; temperature sensitive, severely decreases beta-1,3-glucan synthase activation. 1 Publication
Mutagenesisi68 – 681Q → H: Locks RHO1 in the GTP-bound form by abolishing GTP hydrolysis. 1 Publication
Mutagenesisi70 – 701D → G in RHO1-10; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with P-165. 1 Publication
Mutagenesisi102 – 1021E → K in RHO1-11; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with E-166. 1 Publication
Mutagenesisi104 – 1041W → R in RHO1-4; temperature sensitive, severely decreases beta-1,3-glucan synthase activation. 1 Publication
Mutagenesisi121 – 1211G → C in RHO1-5; temperature sensitive, fails to activate PCK1. 1 Publication
Mutagenesisi165 – 1651S → P in RHO1-10; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with G-69. 1 Publication
Mutagenesisi167 – 1671K → E in RHO1-11; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with K-101. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 206205GTP-binding protein RHO1PRO_0000198945Add
BLAST
Propeptidei207 – 2093Removed in mature formPRO_0000281275

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources1 Publication
Modified residuei206 – 2061Cysteine methyl esterBy similarity
Lipidationi206 – 2061S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP06780.
PeptideAtlasiP06780.
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. 97 interactions.
DIPiDIP-1040N.
IntActiP06780. 7 interactions.
MINTiMINT-399819.

Structurei

Secondary structure

1
209
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 1810Combined sources
Helixi23 – 319Combined sources
Beta strandi45 – 539Combined sources
Beta strandi56 – 649Combined sources
Helixi69 – 779Combined sources
Beta strandi83 – 908Combined sources
Helixi94 – 1029Combined sources
Helixi104 – 1118Combined sources
Beta strandi117 – 1226Combined sources
Helixi124 – 1263Combined sources
Helixi130 – 1389Combined sources
Helixi146 – 15510Combined sources
Beta strandi161 – 1633Combined sources
Turni166 – 1683Combined sources
Helixi172 – 18413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A58X-ray2.60B/D/F1-188[»]
ProteinModelPortaliP06780.
SMRiP06780. Positions 7-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06780.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi39 – 479Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
InParanoidiP06780.
KOiK04513.
OMAiKSGCALL.
OrthoDBiEOG7SN8QP.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3A58X-ray2.60B/D/F1-188[»]
ProteinModelPortaliP06780.
SMRiP06780. Positions 7-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36338. 97 interactions.
DIPiDIP-1040N.
IntActiP06780. 7 interactions.
MINTiMINT-399819.

Proteomic databases

MaxQBiP06780.
PeptideAtlasiP06780.
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.
OMAiKSGCALL.
OrthoDBiEOG7SN8QP.

Enzyme and pathway databases

BioCyciYEAST:G3O-34294-MONOMER.
ReactomeiR-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-5625900. RHO GTPases activate CIT.
R-SCE-5627117. RHO GTPases Activate ROCKs.
R-SCE-5666185. RHO GTPases Activate Rhotekin and Rhophilins.
R-SCE-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of two members of the rho gene family from the yeast Saccharomyces cerevisiae."
    Madaule P., Axel R., Myers A.M.
    Proc. Natl. Acad. Sci. U.S.A. 84:779-783(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLN-68.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Bienvenut W.V., Peters C.
    Submitted (MAY-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10; 13-73; 104-123; 128-137 AND 168-181, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Assembly of the mitochondrial membrane system. MRP1 and MRP2, two yeast nuclear genes coding for mitochondrial ribosomal proteins."
    Myers A.M., Crivellone M.D., Tzagoloff A.
    J. Biol. Chem. 262:3388-3397(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-209.
  7. "Growth site localization of Rho1 small GTP-binding protein and its involvement in bud formation in Saccharomyces cerevisiae."
    Yamochi W., Tanaka K., Nonaka H., Maeda A., Musha T., Takai Y.
    J. Cell Biol. 125:1077-1093(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "The rho-GAP encoded by BEM2 regulates cytoskeletal structure in budding yeast."
    Wang T., Bretscher A.
    Mol. Biol. Cell 6:1011-1024(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  9. "Rom1p and Rom2p are GDP/GTP exchange proteins (GEPs) for the Rho1p small GTP binding protein in Saccharomyces cerevisiae."
    Ozaki K., Tanaka K., Imamura H., Hihara T., Kameyama T., Nonaka H., Hirano H., Matsuura Y., Takai Y.
    EMBO J. 15:2196-2207(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  10. "A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae."
    Nonaka H., Tanaka K., Hirano H., Fujiwara T., Kohno H., Umikawa M., Mino A., Takai Y.
    EMBO J. 14:5931-5938(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PKC1, MUTAGENESIS OF VAL-43; PHE-44 AND GLU-45.
  11. "Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae."
    Kohno H., Tanaka K., Mino A., Umikawa M., Imamura H., Fujiwara T., Fujita Y., Hotta K., Qadota H., Watanabe T., Ohya Y., Takai Y.
    EMBO J. 15:6060-6068(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BNI1, MUTAGENESIS OF THR-24 AND THR-42.
  12. Cited for: FUNCTION, INTERACTION WITH PKC1.
  13. "Rho1p, a yeast protein at the interface between cell polarization and morphogenesis."
    Drgonova J., Drgon T., Tanaka K., Kollar R., Chen G.-C., Ford R.A., Chan C.S.M., Takai Y., Cabib E.
    Science 272:277-279(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3-beta-glucan synthase."
    Qadota H., Python C.P., Inoue S.B., Arisawa M., Anraku Y., Zheng Y., Watanabe T., Levin D.E., Ohya Y.
    Science 272:279-281(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FKS1.
  15. "The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1 and RHO2 via the exchange factor ROM2."
    Schmidt A., Bickle M., Beck T., Hall M.N.
    Cell 88:531-542(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH SAC7.
  16. "Association of the Rho family small GTP-binding proteins with Rho GDP dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae."
    Koch G., Tanaka K., Masuda T., Yamochi W., Nonaka H., Takai Y.
    Oncogene 15:417-422(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH RDI1.
  17. "Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7."
    Alberts A.S., Bouquin N., Johnston L.H., Treisman R.
    J. Biol. Chem. 273:8616-8622(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKN7.
  18. "Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from Saccharomyces cerevisiae."
    Roumanie O., Weinachter C., Larrieu I., Crouzet M., Doignon F.
    FEBS Lett. 506:149-156(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH BAG7.
  19. "Complementing yeast rho1 mutation groups with distinct functional defects."
    Saka A., Abe M., Okano H., Minemura M., Qadota H., Utsugi T., Mino A., Tanaka K., Takai Y., Ohya Y.
    J. Biol. Chem. 276:46165-46171(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-45; LEU-60; ASP-70; GLU-102; TRP-104; GLY-121; SER-165 AND LYS-167.
  20. "Spatial regulation of the exocyst complex by Rho1 GTPase."
    Guo W., Tamanoi F., Novick P.
    Nat. Cell Biol. 3:353-360(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SEC3.
  21. "Yeast Lrg1p acts as a specialized RhoGAP regulating 1,3-beta-glucan synthesis."
    Watanabe D., Abe M., Ohya Y.
    Yeast 18:943-951(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH LRG1 AND SAC7.
  22. "Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis."
    Tolliday N., VerPlank L., Li R.
    Curr. Biol. 12:1864-1870(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Yeast protein kinases and the RHO1 exchange factor TUS1 are novel components of the cell integrity pathway in yeast."
    Schmelzle T., Helliwell S.B., Hall M.N.
    Mol. Cell. Biol. 22:1329-1339(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH TUS1.
  24. "The RHO1-GAPs SAC7, BEM2 and BAG7 control distinct RHO1 functions in Saccharomyces cerevisiae."
    Schmidt A., Schmelzle T., Hall M.N.
    Mol. Microbiol. 45:1433-1441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BAG7.
  25. "Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast."
    Dong Y., Pruyne D., Bretscher A.
    J. Cell Biol. 161:1081-1092(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. "Gbetagamma recruits Rho1 to the site of polarized growth during mating in budding yeast."
    Bar E.E., Ellicott A.T., Stone D.E.
    J. Biol. Chem. 278:21798-21804(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STE4, SUBCELLULAR LOCATION.
  27. "The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III (Chs3p) from internal stores to the plasma membrane."
    Valdivia R.H., Schekman R.
    Proc. Natl. Acad. Sci. U.S.A. 100:10287-10292(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. "Lrg1p Is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast."
    Fitch P.G., Gammie A.E., Lee D.J., Brizzio de Candal V., Rose M.D.
    Genetics 168:733-746(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  29. "Quantitative mass spectrometry reveals a role for the GTPase Rho1p in actin organization on the peroxisome membrane."
    Marelli M., Smith J.J., Jung S., Yi E., Nesvizhskii A.I., Christmas R.H., Saleem R.A., Tam Y.Y.C., Fagarasanu A., Goodlett D.R., Aebersold R., Rachubinski R.A., Aitchison J.D.
    J. Cell Biol. 167:1099-1112(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: June 8, 2016
This is version 175 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.