ID RHOB_RAT Reviewed; 196 AA. AC P62747; P01121; Q9CUV7; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 02-SEP-2026, entry version 164. DE RecName: Full=Rho-related GTP-binding protein RhoB; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61586}; DE Flags: Precursor; GN Name=Rhob; Synonyms=Arhb; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1710770; DOI=10.1128/mcb.11.7.3682-3690.1991; RA Jaehner D., Hunter T.; RT "The ras-related gene rhoB is an immediate-early gene inducible by v-Fps, RT epidermal growth factor, and platelet-derived growth factor in rat RT fibroblasts."; RL Mol. Cell. Biol. 11:3682-3690(1991). RN [2] RP INTERACTION WITH ROCK1 AND ROCK2. RX PubMed=8816443; DOI=10.1128/mcb.16.10.5313; RA Leung T., Chen X.-Q., Manser E., Lim L.; RT "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and RT is involved in the reorganization of the cytoskeleton."; RL Mol. Cell. Biol. 16:5313-5327(1996). RN [3] RP INDUCTION. RX PubMed=13679852; DOI=10.1038/sj.onc.1206638; RA Malcolm T., Ettehadieh E., Sadowski I.; RT "Mitogen-responsive expression of RhoB is regulated by RNA stability."; RL Oncogene 22:6142-6150(2003). CC -!- FUNCTION: Mediates apoptosis in neoplastically transformed cells after CC DNA damage. Not essential for development but affects cell adhesion and CC growth factor signaling in transformed cells. Plays a negative role in CC tumorigenesis as deletion causes tumor formation. Involved in CC intracellular protein trafficking of a number of proteins. Targets PKN1 CC to endosomes and is involved in trafficking of the EGF receptor from CC late endosomes to lysosomes. Also required for stability and nuclear CC trafficking of AKT1/AKT which promotes endothelial cell survival during CC vascular development. Serves as a microtubule-dependent signal that is CC required for the myosin contractile ring formation during cell cycle CC cytokinesis. Required for genotoxic stress-induced cell death in breast CC cancer cells (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; CC Evidence={ECO:0000250|UniProtKB:P61586}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P61586}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P61586}; CC -!- SUBUNIT: Binds ROCK1 and ROCK2 (PubMed:8816443). Also binds PKN1/PRK1. CC Interacts with ARGGEF3. Interacts with RTKN. Interacts with AKAP13. CC Interacts with RIPOR1 (By similarity). {ECO:0000250|UniProtKB:P62745, CC ECO:0000250|UniProtKB:P62746, ECO:0000269|PubMed:8816443}. CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Lipid- CC anchor {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor CC {ECO:0000250}. Nucleus {ECO:0000250}. Cleavage furrow {ECO:0000250}. CC Note=Late endosomal membrane (geranylgeranylated form). Plasma membrane CC (farnesylated form). Also detected at the nuclear margin and in the CC nucleus. Translocates to the equatorial region before furrow formation CC in a ECT2-dependent manner (By similarity). {ECO:0000250}. CC -!- INDUCTION: Expressed at very low levels in quiescent cells but is CC transiently induced by serum stimulation with levels increasing to a CC maximum within 30 minutes and declining over the next hour. CC {ECO:0000269|PubMed:13679852}. CC -!- PTM: Prenylation specifies the subcellular location of RHOB. The CC farnesylated form is localized to the plasma membrane while the CC geranylgeranylated form is localized to the endosome (By similarity). CC {ECO:0000250}. CC -!- PTM: Ubiquitinated via 'Lys-63'-linked ubiquitin chains by the CC BCR(BACURD3) E3 ubiquitin ligase complex, at least composed of CUL3, CC KCTD10/BACURD3 and RBX1; leading to targeting RHOB to lysosomes. CC {ECO:0000250|UniProtKB:P62745}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M74295; AAA42040.1; -; mRNA. DR PIR; A39727; TVRTRH. DR RefSeq; NP_071987.1; NM_022542.2. DR AlphaFoldDB; P62747; -. DR SMR; P62747; -. DR BioGRID; 249057; 1. DR FunCoup; P62747; 1056. DR STRING; 10116.ENSRNOP00000008008; -. DR iPTMnet; P62747; -. DR PhosphoSitePlus; P62747; -. DR SwissPalm; P62747; -. DR jPOST; P62747; -. DR PaxDb; 10116-ENSRNOP00000008008; -. DR Ensembl; ENSRNOT00000008008.5; ENSRNOP00000104619.1; ENSRNOG00000021403.4. DR Ensembl; ENSRNOT00000095242.2; ENSRNOP00000101374.1; ENSRNOG00000021403.4. DR Ensembl; ENSRNOT00000121412.1; ENSRNOP00000110952.1; ENSRNOG00000021403.4. DR GeneID; 64373; -. DR KEGG; rno:64373; -. DR AGR; RGD:621309; -. DR CTD; 388; -. DR RGD; 621309; Rhob. DR eggNOG; KOG0393; Eukaryota. DR GeneTree; ENSGT00950000182945; -. DR HOGENOM; CLU_041217_21_2_1; -. DR InParanoid; P62747; -. DR OrthoDB; 4627at9989; -. DR PhylomeDB; P62747; -. DR Reactome; R-RNO-114604; GPVI-mediated activation cascade. DR Reactome; R-RNO-416482; G alpha (12/13) signalling events. DR Reactome; R-RNO-416572; Sema4D induced cell migration and growth-cone collapse. DR Reactome; R-RNO-5625740; RHO GTPases activate PKNs. DR Reactome; R-RNO-5625900; RHO GTPases activate CIT. DR Reactome; R-RNO-5627117; RHO GTPases Activate ROCKs. DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins. DR Reactome; R-RNO-9013026; RHOB GTPase cycle. DR PRO; PR:P62747; -. DR Proteomes; UP000002494; Chromosome 6. DR Bgee; ENSRNOG00000021403; Expressed in Ammon's horn and 19 other cell types or tissues. DR ExpressionAtlas; P62747; baseline and differential. DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:BHF-UCL. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0045202; C:synapse; IDA:SynGO. DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC. DR GO; GO:0019003; F:GDP binding; IEA:Ensembl. DR GO; GO:0005525; F:GTP binding; TAS:UniProtKB. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB. DR GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB. DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB. DR GO; GO:0061154; P:endothelial tube morphogenesis; IEA:Ensembl. DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB. DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl. DR GO; GO:1903141; P:negative regulation of establishment of endothelial barrier; ISS:UniProtKB. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl. DR GO; GO:0099159; P:regulation of modification of postsynaptic structure; IEA:Ensembl. DR GO; GO:0007264; P:small GTPase-mediated signal transduction; IEA:InterPro. DR CDD; cd01870; RhoA_like; 1. DR FunFam; 3.40.50.300:FF:000095; Rho-related GTP-binding protein RhoC; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR001806; Small_GTPase. DR InterPro; IPR003578; Small_GTPase_Rho. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51420; RHO; 1. PE 1: Evidence at protein level; KW ADP-ribosylation; Angiogenesis; Apoptosis; Cell adhesion; Cell membrane; KW Developmental protein; Differentiation; Endosome; GTP-binding; Hydrolase; KW Isopeptide bond; Lipoprotein; Magnesium; Membrane; Metal-binding; KW Methylation; Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; KW Prenylation; Protein transport; Reference proteome; Transport; KW Tumor suppressor; Ubl conjugation. FT CHAIN 1..193 FT /note="Rho-related GTP-binding protein RhoB" FT /id="PRO_0000030421" FT PROPEP 194..196 FT /note="Removed in mature form" FT /evidence="ECO:0000250|UniProtKB:P62745" FT /id="PRO_0000030422" FT MOTIF 34..42 FT /note="Effector region" FT /evidence="ECO:0000255" FT BINDING 15 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 16 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 17 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 18 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 19 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 19 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 20 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 34 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 37 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 37 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 62 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 118 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 120 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 160 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 161 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT BINDING 162 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62745" FT MOD_RES 154 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P62746" FT MOD_RES 193 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250|UniProtKB:P62745" FT LIPID 189 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P62745" FT LIPID 192 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P62745" FT LIPID 193 FT /note="S-farnesyl cysteine; in plasma membrane form" FT /evidence="ECO:0000250|UniProtKB:P62745" FT LIPID 193 FT /note="S-geranylgeranyl cysteine; in endosomal form" FT /evidence="ECO:0000250|UniProtKB:P62745" FT CROSSLNK 162 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P62745" FT CROSSLNK 181 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P62745" SQ SEQUENCE 196 AA; 22123 MW; CCE6FD53AE00CD83 CRC64; MAAIRKKLVV VGDGACGKTC LLIVFSKDEF PEVYVPTVFE NYVADIEVDG KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWV PEVKHFCPNV PIILVANKKD LRSDEHVRTE LARMKQEPVR TDDGRAMAVR IQAYDYLECS AKTKEGVREV FETATRAALQ KRYGSQNGCI NCCKVL //