RHOC_HUMAN - dbPTM
RHOC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHOC_HUMAN
UniProt AC P08134
Protein Name Rho-related GTP-binding protein RhoC
Gene Name RHOC
Organism Homo sapiens (Human).
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
7Ubiquitination-MAAIRKKLVIVGDG
-CCCCCCEEEEECCC		37.83-
16S-palmitoylationVIVGDGACGKTCLLI
EEECCCCCCCEEEEE		7.6029575903
19PhosphorylationGDGACGKTCLLIVFS
CCCCCCCEEEEEEEE		8.1519060867
26PhosphorylationTCLLIVFSKDQFPEV
EEEEEEEECCCCCCE		25.1619060867
27SumoylationCLLIVFSKDQFPEVY
EEEEEEECCCCCCEE		44.05-
34PhosphorylationKDQFPEVYVPTVFEN
CCCCCCEECCCEECC		10.0720736484
34O-linked_GlycosylationKDQFPEVYVPTVFEN
CCCCCCEECCCEECC		10.0724141704
37O-linked_GlycosylationFPEVYVPTVFENYIA
CCCEECCCEECCEEE		27.9924905543
41ADP-ribosylationYVPTVFENYIADIEV
ECCCEECCEEEEEEE		23.26-
41ADP-ribosylationYVPTVFENYIADIEV
ECCCEECCEEEEEEE		23.26-
60PhosphorylationVELALWDTAGQEDYD
EEEEEEECCCCCCHH		22.5529978859
66PhosphorylationDTAGQEDYDRLRPLS
ECCCCCCHHHCCCCC		11.3825884760
73PhosphorylationYDRLRPLSYPDTDVI
HHHCCCCCCCCCCEE		36.98-
88PhosphorylationLMCFSIDSPDSLENI
EEEEECCCCHHHHCC		29.01-
100PhosphorylationENIPEKWTPEVKHFC
HCCCCCCCHHHHHHC		22.19-
104UbiquitinationEKWTPEVKHFCPNVP
CCCCHHHHHHCCCCC		29.3321890473
104AcetylationEKWTPEVKHFCPNVP
CCCCHHHHHHCCCCC		29.3325953088
107S-palmitoylationTPEVKHFCPNVPIIL
CHHHHHHCCCCCEEE		2.1029575903
118AcetylationPIILVGNKKDLRQDE
CEEEECCHHHHCCCH		41.5625953088
118UbiquitinationPIILVGNKKDLRQDE
CEEEECCHHHHCCCH		41.56-
119UbiquitinationIILVGNKKDLRQDEH
EEEECCHHHHCCCHH		67.03-
119MethylationIILVGNKKDLRQDEH
EEEECCHHHHCCCHH		67.03-
135UbiquitinationRRELAKMKQEPVRSE
HHHHHHHHHCCCCCH		51.29-
152PhosphorylationRDMANRISAFGYLEC
HHHHHHHHHHHHHHC		17.8226657352
156PhosphorylationNRISAFGYLECSAKT
HHHHHHHHHHCCCCC		7.9028152594
160PhosphorylationAFGYLECSAKTKEGV
HHHHHHCCCCCHHHH		24.3528152594
173SulfoxidationGVREVFEMATRAGLQ
HHHHHHHHHHHHCCH		2.9121406390
190MethylationKNKRRRGCPIL----
HCCCCCCCCCC----		1.47-
190GeranylgeranylationKNKRRRGCPIL----
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHOC_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 RHOC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHG01_HUMANARHGAP1physical
16189514
CTRO_HUMANCITphysical
8543060
LNX1_HUMANLNX1physical
19701800
CAV1_HUMANCAV1physical
20460433
RIPR2_HUMANFAM65Bphysical
25416956
GBB2_HUMANGNB2physical
26344197
RAC3_HUMANRAC3physical
26344197
RHOA_HUMANRHOAphysical
28514442
DAAM2_HUMANDAAM2physical
28514442
ARHGB_HUMANARHGEF11physical
28514442
CA198_HUMANC1orf198physical
28514442
DAAM1_HUMANDAAM1physical
28514442
RTKN_HUMANRTKNphysical
28514442
ARHG1_HUMANARHGEF1physical
28514442
ARHGC_HUMANARHGEF12physical
28514442
DIAP1_HUMANDIAPH1physical
28514442
ZMYM4_HUMANZMYM4physical
28514442
GDS1_HUMANRAP1GDS1physical
28514442
RTKN2_HUMANRTKN2physical
28514442
ARP10_HUMANACTR10physical
28514442
BGAL_HUMANGLB1physical
28514442
PPGB_HUMANCTSAphysical
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 RHOC_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-156, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory