RHOC_MOUSE - dbPTM
RHOC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHOC_MOUSE
UniProt AC Q62159
Protein Name Rho-related GTP-binding protein RhoC
Gene Name Rhoc
Organism Mus musculus (Mouse).
Sequence Length 193
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Cleavage furrow. Translocates to the equatorial region before furrow formation in a ECT2-dependent manner..
Protein Description Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells..
Protein Sequence MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYIADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRQDEHTRRELAKMKQEPVRSEEGRDMANRISAFGYLECSAKTKEGVREVFEMATRAGLQVRKNKRRRGCPIL
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
7Acetylation-MAAIRKKLVIVGDG
-CCCCCCEEEEECCC
37.8323806337
7Succinylation-MAAIRKKLVIVGDG
-CCCCCCEEEEECCC
37.8323806337
16S-nitrosocysteineVIVGDGACGKTCLLI
EEECCCCCCCEEEEE
7.60-
16S-nitrosylationVIVGDGACGKTCLLI
EEECCCCCCCEEEEE
7.6021278135
19PhosphorylationGDGACGKTCLLIVFS
CCCCCCCEEEEEEEE
8.1517203969
26PhosphorylationTCLLIVFSKDQFPEV
EEEEEEEECCCCCCE
25.1617203969
34PhosphorylationKDQFPEVYVPTVFEN
CCCCCCEECCCEECC
10.0729514104
66PhosphorylationDTAGQEDYDRLRPLS
ECCCCCCHHHCCCCC
11.3825159016
104UbiquitinationEKWTPEVKHFCPNVP
CCCCHHHHHHCCCCC
29.33-
107S-nitrosocysteineTPEVKHFCPNVPIIL
CHHHHHHCCCCCEEE
2.10-
107S-nitrosylationTPEVKHFCPNVPIIL
CHHHHHHCCCCCEEE
2.1020925432
118UbiquitinationPIILVGNKKDLRQDE
CEEEECCHHHHCCCH
41.56-
119UbiquitinationIILVGNKKDLRQDEH
EEEECCHHHHCCCHH
67.03-
135UbiquitinationRRELAKMKQEPVRSE
HHHHHHHHHCCCCCH
51.29-
159S-nitrosylationSAFGYLECSAKTKEG
HHHHHHHCCCCCHHH
4.4121278135
159S-nitrosocysteineSAFGYLECSAKTKEG
HHHHHHHCCCCCHHH
4.41-
190GeranylgeranylationKNKRRRGCPIL----
HCCCCCCCCCC----
1.47-
190MethylationKNKRRRGCPIL----
HCCCCCCCCCC----
1.47-

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 RHOC_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHOC_MOUSE !!

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 RHOC_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RHOC_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RHOC_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19 AND SER-26, AND MASSSPECTROMETRY.

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