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Protein

Rho-related GTP-binding protein RhoB

Gene

Rhob

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates apoptosis in neoplastically transformed cells after DNA damage. Not essential for development but affects cell adhesion and growth factor signaling in transformed cells. Plays a negative role in tumorigenesis as deletion causes tumor formation. Involved in intracellular protein trafficking of a number of proteins. Targets PKN1 to endosomes and is involved in trafficking of the EGF receptor from late endosomes to lysosomes. Also required for stability and nuclear trafficking of AKT1/AKT which promotes endothelial cell survival during vascular development. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Required for genotoxic stress-induced cell death in breast cancer cells (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTPBy similarity
Nucleotide bindingi59 – 635GTPBy similarity
Nucleotide bindingi117 – 1204GTPBy similarity

GO - Molecular functioni

  • GDP binding Source: Ensembl
  • GTP binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Apoptosis, Cell adhesion, Differentiation, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-114604. GPVI-mediated activation cascade.
R-RNO-194840. Rho GTPase cycle.
R-RNO-416482. G alpha (12/13) signalling events.
R-RNO-416572. Sema4D induced cell migration and growth-cone collapse.
R-RNO-5625740. RHO GTPases activate PKNs.
R-RNO-5625900. RHO GTPases activate CIT.
R-RNO-5627117. RHO GTPases Activate ROCKs.
R-RNO-5663220. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-related GTP-binding protein RhoB
Gene namesi
Name:Rhob
Synonyms:Arhb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi621309. Rhob.

Subcellular locationi

  • Late endosome membrane By similarity; Lipid-anchor By similarity
  • Cell membrane By similarity; Lipid-anchor By similarity
  • Nucleus By similarity
  • Cleavage furrow By similarity

  • Note: Late endosomal membrane (geranylgeranylated form). Plasma membrane (farnesylated form). Also detected at the nuclear margin and in the nucleus. Translocates to the equatorial region before furrow formation in a ECT2-dependent manner (By similarity).By similarity

GO - Cellular componenti

  • cleavage furrow Source: UniProtKB
  • cytosol Source: BHF-UCL
  • early endosome Source: Ensembl
  • endosome membrane Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • focal adhesion Source: Ensembl
  • late endosome membrane Source: UniProtKB-SubCell
  • membrane Source: BHF-UCL
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 193193Rho-related GTP-binding protein RhoBPRO_0000030421Add
BLAST
Propeptidei194 – 1963Removed in mature formBy similarityPRO_0000030422

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei154 – 1541PhosphotyrosineBy similarity
Lipidationi189 – 1891S-palmitoyl cysteineBy similarity
Lipidationi192 – 1921S-palmitoyl cysteineBy similarity
Modified residuei193 – 1931Cysteine methyl esterBy similarity
Lipidationi193 – 1931S-farnesyl cysteine; in plasma membrane formBy similarity
Lipidationi193 – 1931S-geranylgeranyl cysteine; in endosomal formBy similarity

Post-translational modificationi

Prenylation specifies the subcellular location of RHOB. The farnesylated form is localized to the plasma membrane while the geranylgeranylated form is localized to the endosome (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Methylation, Palmitate, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiP62747.
PRIDEiP62747.

PTM databases

iPTMnetiP62747.
PhosphoSiteiP62747.

Expressioni

Inductioni

Expressed at very low levels in quiescent cells but is transiently induced by serum stimulation with levels increasing to a maximum within 30 minutes and declining over the next hour.1 Publication

Gene expression databases

BgeeiENSRNOG00000021403.
GenevisibleiP62747. RN.

Interactioni

Subunit structurei

Binds ROCK1 and ROCK2. Also binds PKN1/PRK1. Interacts with ARHGEF3, RTKN and AKAP13 (By similarity).By similarity

Protein-protein interaction databases

BioGridi249057. 1 interaction.
MINTiMINT-4576528.
STRINGi10116.ENSRNOP00000008008.

Structurei

3D structure databases

ProteinModelPortaliP62747.
SMRiP62747. Positions 2-185.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector regionSequence analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP62747.
KOiK07856.
OMAiDGRAMAM.
OrthoDBiEOG091G0QVS.
PhylomeDBiP62747.
TreeFamiTF300837.

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.

P62747-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAIRKKLVV VGDGACGKTC LLIVFSKDEF PEVYVPTVFE NYVADIEVDG
60 70 80 90 100
KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWV
110 120 130 140 150
PEVKHFCPNV PIILVANKKD LRSDEHVRTE LARMKQEPVR TDDGRAMAVR
160 170 180 190
IQAYDYLECS AKTKEGVREV FETATRAALQ KRYGSQNGCI NCCKVL
Length:196
Mass (Da):22,123
Last modified:August 1, 1988 - v1
Checksum:iCCE6FD53AE00CD83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74295 mRNA. Translation: AAA42040.1.
PIRiA39727. TVRTRH.
RefSeqiNP_071987.1. NM_022542.1.
UniGeneiRn.2042.

Genome annotation databases

EnsembliENSRNOT00000008008; ENSRNOP00000008008; ENSRNOG00000021403.
GeneIDi64373.
KEGGirno:64373.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74295 mRNA. Translation: AAA42040.1.
PIRiA39727. TVRTRH.
RefSeqiNP_071987.1. NM_022542.1.
UniGeneiRn.2042.

3D structure databases

ProteinModelPortaliP62747.
SMRiP62747. Positions 2-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249057. 1 interaction.
MINTiMINT-4576528.
STRINGi10116.ENSRNOP00000008008.

PTM databases

iPTMnetiP62747.
PhosphoSiteiP62747.

Proteomic databases

PaxDbiP62747.
PRIDEiP62747.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000008008; ENSRNOP00000008008; ENSRNOG00000021403.
GeneIDi64373.
KEGGirno:64373.

Organism-specific databases

CTDi388.
RGDi621309. Rhob.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP62747.
KOiK07856.
OMAiDGRAMAM.
OrthoDBiEOG091G0QVS.
PhylomeDBiP62747.
TreeFamiTF300837.

Enzyme and pathway databases

ReactomeiR-RNO-114604. GPVI-mediated activation cascade.
R-RNO-194840. Rho GTPase cycle.
R-RNO-416482. G alpha (12/13) signalling events.
R-RNO-416572. Sema4D induced cell migration and growth-cone collapse.
R-RNO-5625740. RHO GTPases activate PKNs.
R-RNO-5625900. RHO GTPases activate CIT.
R-RNO-5627117. RHO GTPases Activate ROCKs.
R-RNO-5663220. RHO GTPases Activate Formins.

Miscellaneous databases

PROiP62747.

Gene expression databases

BgeeiENSRNOG00000021403.
GenevisibleiP62747. RN.

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 nameiRHOB_RAT
AccessioniPrimary (citable) accession number: P62747
Secondary accession number(s): P01121, Q9CUV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1988
Last modified: September 7, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.