Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01106
Entry Name
UniProt Accession
Theoretical PI
5.1
Molecular Weight
22123.39
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Rho-related GTP-binding protein RhoB
Protein Synonyms/Alias
Rho cDNA clone 6; h6;
Gene Name
RHOB
Gene Synonyms/Alias
ARH6; ARHB;
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
189
Canonical
RYGSQNGCINCCKVL
[1]
S-Palmitoylation
192
Canonical
SQNGCINCCKVL***
[1]
S-Palmitoylation
193
Canonical
QNGCINCCKVL****
[2][3]
S-Farnesylation
193
Canonical
QNGCINCCKVL****
[2][3]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Wang DA, Sebti SM. Palmitoylated cysteine 192 is required for RhoBtumor-suppressive and apoptotic activities. J Biol Chem. 2005 May13;280(19):19243-9. Epub 2005 Feb 15.[PMID:15713677]
[2] Armstrong SA, Hannah VC, Goldstein JL, Brown MS. CAAX geranylgeranyltransferase transfers farnesyl as efficiently as geranylgeranyl to RhoB. J BiolChem. 1995 Apr 7;270(14):7864-8.[PMID:7713879]
[3] Adamson P, Marshall CJ, Hall A, Tilbrook PA. Post-translational modifications of p21rho proteins. J Biol Chem. 1992 Oct 5;267(28):20033-8.[PMID:1400319]
Functional Description
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.
Sequence Annotation
Nucleotide-binding: 12 19 GTP.
Nucleotide-binding: 59 63 GTP.
Nucleotide-binding: 117 120 GTP.
Motif: 34 42 Effector region.
Modified residue: 41 41 ADP-ribosylasparagine; by botulinumtoxin.
Modified residue: 154 154 Phosphotyrosine.
Modified residue: 193 193 Cysteine methyl ester.
Protein Length
196 AA.
Protein Sequence
(Canonical)
MAAIRKKLVV VGDGACGKTC LLIVFSKDEF PEVYVPTVFE NYVADIEVDG KQVELALWDT  60
AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWV PEVKHFCPNV PIILVANKKD  120
LRSDEHVRTE LARMKQEPVR TDDGRAMAVR IQAYDYLECS AKTKEGVREV FETATRAALQ  180
KRYGSQNGCI NCCKVL                                                  196
MAAIRKKLVV VGDGACGKTC LLIVFSKDEF PEVYVPTVFE NYVADIEVDG KQVELALWDT  60
AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWV PEVKHFCPNV PIILVANKKD  120
LRSDEHVRTE LARMKQEPVR TDDGRAMAVR IQAYDYLECS AKTKEGVREV FETATRAALQ  180
KRYGSQNGCI NCCKVL                                                  196
MAAIRKKLVV VGDGACGKTC LLIVFSKDEF PEVYVPTVFE NYVADIEVDG KQVELALWDT  60
AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWV PEVKHFCPNV PIILVANKKD  120
LRSDEHVRTE LARMKQEPVR TDDGRAMAVR IQAYDYLECS AKTKEGVREV FETATRAALQ  180
KRYGSQNGCI NCCKVL                                                  196
FASTA
(Canonical)
>LipidDB-9606-01106|P62745
MAAIRKKLVVVGDGACGKTCLLIVFSKDEFPEVYVPTVFENYVADIEVDGKQVELALWDT
AGQEDYDRLRPLSYPDTDVILMCFSVDSPDSLENIPEKWVPEVKHFCPNVPIILVANKKD
LRSDEHVRTELARMKQEPVRTDDGRAMAVRIQAYDYLECSAKTKEGVREVFETATRAALQ
KRYGSQNGCINCCKVL
MAAIRKKLVVVGDGACGKTCLLIVFSKDEFPEVYVPTVFENYVADIEVDGKQVELALWDT
AGQEDYDRLRPLSYPDTDVILMCFSVDSPDSLENIPEKWVPEVKHFCPNVPIILVANKKD
LRSDEHVRTELARMKQEPVRTDDGRAMAVRIQAYDYLECSAKTKEGVREVFETATRAALQ
KRYGSQNGCINCCKVL
MAAIRKKLVVVGDGACGKTCLLIVFSKDEFPEVYVPTVFENYVADIEVDGKQVELALWDT
AGQEDYDRLRPLSYPDTDVILMCFSVDSPDSLENIPEKWVPEVKHFCPNVPIILVANKKD
LRSDEHVRTELARMKQEPVRTDDGRAMAVRIQAYDYLECSAKTKEGVREVFETATRAALQ
KRYGSQNGCINCCKVL
Gene Ontology
GO:0032154; C:cleavage furrow; IDA:UniProtKB
GO:0005829; C:cytosol; TAS:Reactome
GO:0010008; C:endosome membrane; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0005634; C:nucleus; ISS:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0019003; F:GDP binding; IEA:Ensembl
GO:0005525; F:GTP binding; TAS:UniProtKB
GO:0003924; F:GTPase activity; TAS:UniProtKB
GO:0001525; P:angiogenesis; IEA:UniProtKB-KW
GO:0006915; P:apoptotic process; TAS:UniProtKB
GO:0007411; P:axon guidance; TAS:Reactome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0007155; P:cell adhesion; ISS:UniProtKB
GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB
GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB
GO:0000910; P:cytokinesis; IMP:UniProtKB
GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB
GO:0006184; P:GTP catabolic process; TAS:GOC
GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB
GO:0030168; P:platelet activation; TAS:Reactome
GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB
GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB
GO:0015031; P:protein transport; IEA:UniProtKB-KW
GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome
GO:0007266; P:Rho protein signal transduction; TAS:UniProtKB
GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome
GO:0006927; P:transformed cell apoptotic process; ISS:UniProtKB
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;