RHG01_MOUSE - dbPTM
RHG01_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG01_MOUSE
UniProt AC Q5FWK3
Protein Name Rho GTPase-activating protein 1
Gene Name Arhgap1
Organism Mus musculus (Mouse).
Sequence Length 439
Subcellular Localization Cytoplasm.
Protein Description GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate (By similarity)..
Protein Sequence MDPLSELQDDLTLDDTSQALNQLKLASIDEKNWPSDEMPDFPKSDDSKSSSPEPVTHLKWDDPYYDIARHQIVEVAGDDKYGRKIIVFSACRMPPSHQLDHSKLLGYLKHTLDQYVESDYTLLYLHHGLTSDNKPSLSWLRDAYREFDRKYKKNIKALYIVHPTMFIKTLLILFKPLISFKFGRKIFYVNYLSELSEHVKLEQLGIPRQVLKYDDFLKSTQKSPATAPKPMPPRPPLPNQQFGVSLQHLQEKSPGQDPIPIVLRETVAYLQAHALTTEGIFRRSANTQVVREVQQKYNMGLPVDFDQYNELHLPAVILKTFLRELPEPLLTFDLYPHVVGFLNIDESQRVEVTQQVLQTLPEENYQVLHFLTAFLVQISAHCDQNKMTNTNLAVVFGPNLLWAKDAAITLKAINPINTFTKFLLDHQGELFPSTDAQGV
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
1Acetylation-------MDPLSELQ
-------CCHHHHHC
12.35-
27PhosphorylationLNQLKLASIDEKNWP
HHHHHHHHCCCCCCC
40.8025521595
31UbiquitinationKLASIDEKNWPSDEM
HHHHCCCCCCCCCCC
61.64-
35PhosphorylationIDEKNWPSDEMPDFP
CCCCCCCCCCCCCCC
37.5125521595
44PhosphorylationEMPDFPKSDDSKSSS
CCCCCCCCCCCCCCC
47.0624925903
47PhosphorylationDFPKSDDSKSSSPEP
CCCCCCCCCCCCCCC
39.1524925903
49PhosphorylationPKSDDSKSSSPEPVT
CCCCCCCCCCCCCCC
39.7525521595
50PhosphorylationKSDDSKSSSPEPVTH
CCCCCCCCCCCCCCC
54.3625521595
51PhosphorylationSDDSKSSSPEPVTHL
CCCCCCCCCCCCCCC
40.1324925903
56PhosphorylationSSSPEPVTHLKWDDP
CCCCCCCCCCCCCCC
32.0024925903
59AcetylationPEPVTHLKWDDPYYD
CCCCCCCCCCCCCHH
40.7623806337
64PhosphorylationHLKWDDPYYDIARHQ
CCCCCCCCHHHHHHH
22.2919737024
65PhosphorylationLKWDDPYYDIARHQI
CCCCCCCHHHHHHHE
13.2717947660
80AcetylationVEVAGDDKYGRKIIV
EEECCCCCCCCEEEE
55.11-
89PhosphorylationGRKIIVFSACRMPPS
CCEEEEEEECCCCCH
18.6324719451
212UbiquitinationGIPRQVLKYDDFLKS
CCCHHHHCHHHHHHH
48.02-
212AcetylationGIPRQVLKYDDFLKS
CCCHHHHCHHHHHHH
48.0223236377
223PhosphorylationFLKSTQKSPATAPKP
HHHHCCCCCCCCCCC
15.2226824392
226PhosphorylationSTQKSPATAPKPMPP
HCCCCCCCCCCCCCC
47.0420531401
245PhosphorylationPNQQFGVSLQHLQEK
CCCCCCEEHHHHHHH
23.7720531401
253PhosphorylationLQHLQEKSPGQDPIP
HHHHHHHCCCCCCCC
33.2529233185
388PhosphorylationHCDQNKMTNTNLAVV
HCCCCCCCCCCEEEE
40.2725367039
390PhosphorylationDQNKMTNTNLAVVFG
CCCCCCCCCEEEEEC
23.5725367039
411UbiquitinationKDAAITLKAINPINT
HCHHHHHHHCCCCHH
38.27-

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 RHG01_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHG01_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 RHG01_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NDEL1_MOUSENdel1physical
18331715
LIS1_MOUSEPafah1b1physical
18331715
RAC1_MOUSERac1physical
14966113
CDC42_MOUSECdc42physical
14966113
RHOA_MOUSERhoaphysical
14966113

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RHG01_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65, AND MASSSPECTROMETRY.

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