RHOB
entrez
388
canonical
uniprot
P62745
canonical
ensembl
ENSG00000143878
resolver
ensp
ENSP00000272233
resolver
enst
ENST00000272233
resolver
genesymbol
RHOB
resolver
genesymbol_syn
ARH6
resolver
genesymbol_syn
ARHB
resolver
hgnc
HGNC:668
resolver
uniprot
B2R692
resolver
uniprot
P01121
resolver
uniprot
Q5U0H6
resolver
uniprot
Q7RTN5
resolver
uniprot
Q7RTR9
resolver
uniprot
Q9CUV7
resolver
uniprot_entry
RHOB_HUMAN
resolver
uniprot_sec
B2R692
resolver
uniprot_sec
P01121
resolver
uniprot_sec
Q5U0H6
resolver
uniprot_sec
Q7RTN5
resolver
uniprot_sec
Q7RTR9
resolver
uniprot_sec
Q9CUV7
resolver
amino_acid_sequence
MAAIRKKLVVVGDGACGKTCLLIVFSKDEFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSVDSPDSLENIPEKWVPEVKHFCPNVPIILVANKKDLRSDEHVRTELARMKQEPVRTDDGRAMAVRIQAYDYLECSAKTKEGVREVFETATRAALQKRYGSQNGCINCCKVL
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:10508588, ECO:0000269|PubMed:15226397, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:21373644, ECO:0000269|PubMed:29358211, ECO:0000269|PubMed:9478917}.
uniprot
proteins
mass_dalton
22123
uniprot
proteins
mutagenesis
MUTAGEN 14; /note="G->V: No effect on internalization of EGF receptor but decreases trafficking of receptor to the lysosome with associated accumulation in late endosomes."; /evidence="ECO:0000269|PubMed:15226397"; MUTAGEN 39; /note="F->G: Abolishes binding to PKN1 and trafficking of EGF receptor."; /evidence="ECO:0000269|PubMed:10508588"; MUTAGEN 162; /note="K->R: Complete loss of ubiquitination; when associated with R-181."; /evidence="ECO:0000269|PubMed:29358211"; MUTAGEN 181; /note="K->R: Complete loss of ubiquitination; when associated with R-162."; /evidence="ECO:0000269|PubMed:29358211"; MUTAGEN 189; /note="C->S: No effect on prenylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-192."; /evidence="ECO:0000269|PubMed:1400319"; MUTAGEN 192; /note="C->S: Reduced geranylgeranylation but no effect on farnesylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-189."; /evidence="ECO:0000269|PubMed:1400319, ECO:0000269|PubMed:7713879"; MUTAGEN 193; /note="C->S: Abolishes methylation, palmitoylation and prenylation."; /evidence="ECO:0000269|PubMed:1400319, ECO:0000269|PubMed:7713879"; MUTAGEN 194; /note="K->L: No effect on palmitoylation or prenylation."; /evidence="ECO:0000269|PubMed:1400319
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:1400319, ECO:0000269|PubMed:7713879}.; PTM: Ubiquitinated via 'Lys-63'-linked ubiquitin chains by the BCR(BACURD3) E3 ubiquitin ligase complex, at least composed of CUL3, KCTD10/BACURD3 and RBX1; leading to targeting RHOB to lysosomes. {ECO:0000269|PubMed:29358211}.; PTM: (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rho and leads to actin disassembly. {ECO:0000269|PubMed:24141704}.; PTM: (Microbial infection) Glucosylated at Thr-37 by C.difficile toxins TcdA and TcdB in the colonic epithelium (PubMed:24905543). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption (PubMed:24905543). {ECO:0000269|PubMed:24905543}.
uniprot
proteins
protein_family
Rho family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10508588
uniprot
proteins
pubmed
11546812
uniprot
proteins
pubmed
12221096
uniprot
proteins
pubmed
1400319
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15226397
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16236794
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21373644
uniprot
proteins
pubmed
24141704
uniprot
proteins
pubmed
24905543
uniprot
proteins
pubmed
27807006
uniprot
proteins
pubmed
29358211
uniprot
proteins
pubmed
31522999
uniprot
proteins
pubmed
3283705
uniprot
proteins
pubmed
3888408
uniprot
proteins
pubmed
7537292
uniprot
proteins
pubmed
7713879
uniprot
proteins
pubmed
9478917
uniprot
proteins
sequence_length
196
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Late endosome membrane; Lipid-anchor. Cell membrane; Lipid-anchor. Nucleus. Cleavage furrow. 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.
uniprot
proteins