RHOJ_HUMAN - dbPTM
RHOJ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHOJ_HUMAN
UniProt AC Q9H4E5
Protein Name Rho-related GTP-binding protein RhoJ
Gene Name RHOJ
Organism Homo sapiens (Human).
Sequence Length 214
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side .
Protein Description GTP-binding protein with GTPase activity. Elicits the formation of F-actin-rich structures in fibroblasts and is involved in the regulation of cell morphology (By similarity)..
Protein Sequence MNCKEGTDSSCGCRGNDEKKMLKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVTVTVGGKQHLLGLYDTAGQEDYNQLRPLSYPNTDVFLICFSVVNPASYHNVQEEWVPELKDCMPHVPYVLIGTQIDLRDDPKTLARLLYMKEKPLTYEHGVKLAKAIGAQCYLECSALTQKGLKAVFDEAILTIFHPKKKKKRCSEGHSCCSII
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
3S-palmitoylation-----MNCKEGTDSS
-----CCCCCCCCCC
4.0230158707
7Phosphorylation-MNCKEGTDSSCGCR
-CCCCCCCCCCCCCC
33.5222817900
10PhosphorylationCKEGTDSSCGCRGND
CCCCCCCCCCCCCCC
19.8219690332
11S-palmitoylationKEGTDSSCGCRGNDE
CCCCCCCCCCCCCCC
7.4530158707
24S-palmitoylationDEKKMLKCVVVGDGA
CCCCCEEEEEECCCC
2.1829575903
211MethylationCSEGHSCCSII----
CCCCCCCCCCC----
3.52-
211FarnesylationCSEGHSCCSII----
CCCCCCCCCCC----
3.52-

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

Oops, there are no upstream regulatory protein records of RHOJ_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHOJ_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 RHOJ_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WASP_HUMANWASphysical
10967094
PAK1_HUMANPAK1physical
10967094
PAR6B_HUMANPARD6Bphysical
25416956
IF2P_HUMANEIF5Bphysical
26186194
KPCI_HUMANPRKCIphysical
26186194
PAK2_HUMANPAK2physical
26186194
KC1D_HUMANCSNK1Dphysical
26186194
F177A_HUMANFAM177A1physical
26186194
PAR6B_HUMANPARD6Bphysical
26186194
UBP24_HUMANUSP24physical
26186194
AASD1_HUMANAARSD1physical
26186194
PAR6B_HUMANPARD6Bphysical
28514442
PAR6G_HUMANPARD6Gphysical
28514442
UBP24_HUMANUSP24physical
28514442
F177A_HUMANFAM177A1physical
28514442
PAK1_HUMANPAK1physical
28514442
KPCI_HUMANPRKCIphysical
28514442
PAK2_HUMANPAK2physical
28514442
AASD1_HUMANAARSD1physical
28514442

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 RHOJ_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7, AND MASSSPECTROMETRY.

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