RHOB_HUMAN - dbPTM
RHOB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHOB_HUMAN
UniProt AC P62745
Protein Name Rho-related GTP-binding protein RhoB
Gene Name RHOB
Organism Homo sapiens (Human).
Sequence Length 196
Subcellular Localization Late endosome membrane
Lipid-anchor. Cell membrane
Lipid-anchor. Nucleus. Cleavage furrow. Late endosomal membrane (geranylgeranylated form). Plasma membrane (farnesylated form). Also detected at the nuclear margin and in the nucleus. Translocates
Protein 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..
Protein Sequence MAAIRKKLVVVGDGACGKTCLLIVFSKDEFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSVDSPDSLENIPEKWVPEVKHFCPNVPIILVANKKDLRSDEHVRTELARMKQEPVRTDDGRAMAVRIQAYDYLECSAKTKEGVREVFETATRAALQKRYGSQNGCINCCKVL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Ubiquitination-MAAIRKKLVVVGDG
-CCCCCCEEEEECCC		36.3429967540
19PhosphorylationGDGACGKTCLLIVFS
CCCCCCCEEEEEEEE		8.1521712546
26PhosphorylationTCLLIVFSKDEFPEV
EEEEEEEECCCCCCE		28.4421712546
34PhosphorylationKDEFPEVYVPTVFEN
CCCCCCEECCCEEEC		10.0722817900
34O-linked_GlycosylationKDEFPEVYVPTVFEN
CCCCCCEECCCEEEC		10.0724141704
37O-linked_GlycosylationFPEVYVPTVFENYVA
CCCEECCCEEECEEE		27.9924905543
37PhosphorylationFPEVYVPTVFENYVA
CCCEECCCEEECEEE		27.9923532336
41ADP-ribosylationYVPTVFENYVADIEV
ECCCEEECEEEEEEE		25.72-
41ADP-ribosylationYVPTVFENYVADIEV
ECCCEEECEEEEEEE		25.72-
42PhosphorylationVPTVFENYVADIEVD
CCCEEECEEEEEEEC		6.99-
51UbiquitinationADIEVDGKQVELALW
EEEEECCEEEEEEEE		46.8616196087
60PhosphorylationVELALWDTAGQEDYD
EEEEEEECCCCCCHH		22.5529978859
66PhosphorylationDTAGQEDYDRLRPLS
ECCCCCCHHHCCCCC		11.3825884760
73PhosphorylationYDRLRPLSYPDTDVI
HHHCCCCCCCCCCEE		36.98-
104UbiquitinationEKWVPEVKHFCPNVP
HHHCCHHHHHCCCCC		29.3332015554
118UbiquitinationPIILVANKKDLRSDE
CEEEEECHHHCCCCH		37.6232015554
123PhosphorylationANKKDLRSDEHVRTE
ECHHHCCCCHHHHHH		55.4320873877
129PhosphorylationRSDEHVRTELARMKQ
CCCHHHHHHHHHHHC		33.97-
135UbiquitinationRTELARMKQEPVRTD
HHHHHHHHCCCCCCC		46.0523000965
154PhosphorylationMAVRIQAYDYLECSA
EEEEEEEEEEECCCC		6.6919060867
156PhosphorylationVRIQAYDYLECSAKT
EEEEEEEEECCCCCC		7.5427642862
159S-palmitoylationQAYDYLECSAKTKEG
EEEEEECCCCCCHHH		4.4129575903
162UbiquitinationDYLECSAKTKEGVRE
EEECCCCCCHHHHHH		43.7832015554
185PhosphorylationALQKRYGSQNGCINC
HHHHHHCCCCCCCCC		16.1322817900
189S-palmitoylationRYGSQNGCINCCKVL
HHCCCCCCCCCEEEC		2.3715713677
192S-palmitoylationSQNGCINCCKVL---
CCCCCCCCEEEC---		0.9015713677
193FarnesylationQNGCINCCKVL----
CCCCCCCEEEC----		2.717713879
193GeranylgeranylationQNGCINCCKVL----
CCCCCCCEEEC----		2.717713879
193MethylationQNGCINCCKVL----
CCCCCCCEEEC----		2.711400319
193S-palmitoylationQNGCINCCKVL----
CCCCCCCEEEC----		2.7129575903
193FarnesylationQNGCINCCKVL----
CCCCCCCEEEC----		2.717713879
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
185SPhosphorylationKinaseCSNK1A1P48729
GPS
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:26949039
-KUbiquitinationE3 ubiquitin ligaseKCTD10Q9H3F6
PMID:29358211
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHOB_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RHOB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTRO_HUMANCITphysical
8543060
ARHG3_HUMANARHGEF3physical
12221096
RHPN2_HUMANRHPN2physical
12473120
GDIR3_HUMANARHGDIGphysical
8939998
BACD2_HUMANTNFAIP1physical
19637314
RAC1_HUMANRAC1physical
25301945
CUL2_HUMANCUL2physical
25540389
RBX1_HUMANRBX1physical
25540389
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RHOB_HUMAN

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Post-translational modifications of p21rho proteins.";
Adamson P., Marshall C.J., Hall A., Tilbrook P.A.;
J. Biol. Chem. 267:20033-20038(1992).
Cited for: PALMITOYLATION AT CYS-189 AND CYS-192, ISOPRENYLATION AT CYS-193,METHYLATION AT CYS-193, AND MUTAGENESIS OF CYS-189; CYS-192; CYS-193AND LYS-194.
Palmitoylation
ReferencePubMed
"Post-translational modifications of p21rho proteins.";
Adamson P., Marshall C.J., Hall A., Tilbrook P.A.;
J. Biol. Chem. 267:20033-20038(1992).
Cited for: PALMITOYLATION AT CYS-189 AND CYS-192, ISOPRENYLATION AT CYS-193,METHYLATION AT CYS-193, AND MUTAGENESIS OF CYS-189; CYS-192; CYS-193AND LYS-194.
Prenylation
ReferencePubMed
"CAAX geranylgeranyl transferase transfers farnesyl as efficiently asgeranylgeranyl to RhoB.";
Armstrong S.A., Hannah V.C., Goldstein J.L., Brown M.S.;
J. Biol. Chem. 270:7864-7868(1995).
Cited for: ISOPRENYLATION AT CYS-193, AND MUTAGENESIS OF CYS-192 AND CYS-193.
"Post-translational modifications of p21rho proteins.";
Adamson P., Marshall C.J., Hall A., Tilbrook P.A.;
J. Biol. Chem. 267:20033-20038(1992).
Cited for: PALMITOYLATION AT CYS-189 AND CYS-192, ISOPRENYLATION AT CYS-193,METHYLATION AT CYS-193, AND MUTAGENESIS OF CYS-189; CYS-192; CYS-193AND LYS-194.

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