RHOQ_HUMAN - dbPTM
RHOQ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHOQ_HUMAN
UniProt AC P17081
Protein Name Rho-related GTP-binding protein RhoQ
Gene Name RHOQ
Organism Homo sapiens (Human).
Sequence Length 205
Subcellular Localization Cytoplasm . Cell membrane
Lipid-anchor .
Protein Description Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia..
Protein Sequence MAHGPGALMLKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLGLYDTAGQEDYDRLRPLSYPMTDVFLICFSVVNPASFQNVKEEWVPELKEYAPNVPFLLIGTQIDLRDDPKTLARLNDMKEKPICVEQGQKLAKEIGACCYVECSALTQKGLKTVFDEAIIAILTPKKHTVKKRIGSRCINCCLIT
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
12S-palmitoylationPGALMLKCVVVGDGA
CCEEEEEEEEECCCC
2.1829575903
23PhosphorylationGDGAVGKTCLLMSYA
CCCCCCHHHHHHHHC
11.4921406692
28PhosphorylationGKTCLLMSYANDAFP
CHHHHHHHHCCCCCC
22.5121406692
29PhosphorylationKTCLLMSYANDAFPE
HHHHHHHHCCCCCCH
8.7521406692
38PhosphorylationNDAFPEEYVPTVFDH
CCCCCHHHCCCCCCE
15.2921406692
41PhosphorylationFPEEYVPTVFDHYAV
CCHHHCCCCCCEEEE
24.6221406692
46PhosphorylationVPTVFDHYAVSVTVG
CCCCCCEEEEEEEEC
15.5621406692
49PhosphorylationVFDHYAVSVTVGGKQ
CCCEEEEEEEECCEE
12.1421406692
51PhosphorylationDHYAVSVTVGGKQYL
CEEEEEEEECCEEEE
13.1121406692
70PhosphorylationDTAGQEDYDRLRPLS
CCCCCCCHHHCCCCC
11.3820736484
160PhosphorylationKEIGACCYVECSALT
HHHCCCEEEECHHHC
10.1229759185
163S-palmitoylationGACCYVECSALTQKG
CCCEEEECHHHCHHC
1.7429575903
164PhosphorylationACCYVECSALTQKGL
CCEEEECHHHCHHCH
16.8929759185
169UbiquitinationECSALTQKGLKTVFD
ECHHHCHHCHHHHHC
62.062189047
169AcetylationECSALTQKGLKTVFD
ECHHHCHHCHHHHHC
62.0625953088
172UbiquitinationALTQKGLKTVFDEAI
HHCHHCHHHHHCHHH
51.84-
173PhosphorylationLTQKGLKTVFDEAII
HCHHCHHHHHCHHHH
31.29-
202MethylationGSRCINCCLIT----
CCCEEEEEEEC----
2.38-
202FarnesylationGSRCINCCLIT----
CCCEEEEEEEC----
2.38-

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 RHOQ_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHOQ_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 RHOQ_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GOPC_HUMANGOPCphysical
11162552
EXOC7_HUMANEXOC7physical
12687004
PAR6B_HUMANPARD6Bphysical
11162552
CIP4_HUMANTRIP10physical
12242347
GOPC_HUMANGOPCphysical
25416956

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 RHOQ_HUMAN

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Related Literatures of Post-Translational Modification

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