RHG17_MOUSE - dbPTM
RHG17_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG17_MOUSE
UniProt AC Q3UIA2
Protein Name Rho GTPase-activating protein 17
Gene Name Arhgap17
Organism Mus musculus (Mouse).
Sequence Length 846
Subcellular Localization Membrane
Peripheral membrane protein. Cytoplasm. Cell junction, tight junction. Associates with membranes and concentrates at sites of cell-cell contact..
Protein Description Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca(2+)-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1 (By similarity)..
Protein Sequence MKKQFNRMKQLANQTVGRAEKTEVLSEDLLQIERRLDTVRSMCHHSHKRLIACFQGQHGTDAERRHKKLPLTALAQNMQEASAQLEESLLGKMLETCGDAENQLALELSQHEVFVEKEIMDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGTNFQGLPSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKALPEMRAHQDKWAEKPAFGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFSLYEEWTQVASVQDQDKKLQYLWTTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWAKQEGTLAEIAAATSVHVVAVIEPIIQHADWFFPGEVEFNVSEAFVPLATPNSNHSSHTGNDSDSGTLERKRPASMAVMEGDLVKKESFGVKLMDFQAHRRGGTLNRKHIAPAFQPPLPPTDGNALAPAGPEPPSQSSRADSSSGGGPVFSSTGILEQGLSPGDSSPPKPKDSVSAAVPAAGRNSNQMTTVPNQAQTGGNSHQLSVSTPHSAAGPSPHTLRRAVKKPAPAPPKPGNLPPGHPGGQSSPGTGTSPKPSARSPSPPQQQQQQQQQQQQQQQQQTPGMRRCSSSLPPIQAPSHPPPQPPTQPRLGEQGPEPGPTPPQTPTPPSTPPLAKQNPSQSETTQLHGTLPRPRPVPKPRNRPSVPPPPHPPGTHTVDGGLTSSVPTASRIVTDTNSRVSESLRSIFPEIHSDLASKEVPGHILLDIDNDTESTAL
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
9UbiquitinationKKQFNRMKQLANQTV
HHHHHHHHHHHHHHC		38.6322790023
67AcetylationTDAERRHKKLPLTAL
CHHHHHHHHCCHHHH		54.9415613283
68AcetylationDAERRHKKLPLTALA
HHHHHHHHCCHHHHH		49.5715613291
82PhosphorylationAQNMQEASAQLEESL
HHHHHHHHHHHHHHH		18.78-
88PhosphorylationASAQLEESLLGKMLE
HHHHHHHHHHHHHHH		21.37-
161PhosphorylationRWNQAHKSSGTNFQG
HHHHHHHHCCCCCCC		24.9225521595
162PhosphorylationWNQAHKSSGTNFQGL
HHHHHHHCCCCCCCC		55.2125521595
164PhosphorylationQAHKSSGTNFQGLPS
HHHHHCCCCCCCCCH		34.5025521595
484PhosphorylationLERKRPASMAVMEGD
CCCCCCCCEEEEECC		15.2325521595
497 (in isoform 4)Phosphorylation-35.8625266776
497 (in isoform 3)Phosphorylation-35.8625266776
497 (in isoform 2)Phosphorylation-35.8625266776
497PhosphorylationGDLVKKESFGVKLMD
CCEECCHHHCCEECC		35.8624719451
510DimethylationMDFQAHRRGGTLNRK
CCHHHHCCCCCCCCC		37.72-
551PhosphorylationSQSSRADSSSGGGPV
CCCCCCCCCCCCCCC		25.9725619855
552PhosphorylationQSSRADSSSGGGPVF
CCCCCCCCCCCCCCC		33.2825619855
553PhosphorylationSSRADSSSGGGPVFS
CCCCCCCCCCCCCCC		45.4625619855
560PhosphorylationSGGGPVFSSTGILEQ
CCCCCCCCCCCHHHC		27.5025619855
561PhosphorylationGGGPVFSSTGILEQG
CCCCCCCCCCHHHCC		21.1325619855
562PhosphorylationGGPVFSSTGILEQGL
CCCCCCCCCHHHCCC		27.3525619855
570PhosphorylationGILEQGLSPGDSSPP
CHHHCCCCCCCCCCC		33.3921082442
574PhosphorylationQGLSPGDSSPPKPKD
CCCCCCCCCCCCCCC		51.1425521595
575PhosphorylationGLSPGDSSPPKPKDS
CCCCCCCCCCCCCCC		50.3825521595
582PhosphorylationSPPKPKDSVSAAVPA
CCCCCCCCCCCCCCC		24.8926026062
594PhosphorylationVPAAGRNSNQMTTVP
CCCCCCCCCCCEECC		27.3825777480
598PhosphorylationGRNSNQMTTVPNQAQ
CCCCCCCEECCCCCC		18.1925777480
599PhosphorylationRNSNQMTTVPNQAQT
CCCCCCEECCCCCCC		28.7325777480
606PhosphorylationTVPNQAQTGGNSHQL
ECCCCCCCCCCCCEE		50.5026160508
610PhosphorylationQAQTGGNSHQLSVST
CCCCCCCCCEEEECC		18.8426160508
614PhosphorylationGGNSHQLSVSTPHSA
CCCCCEEEECCCCCC		13.8826160508
616PhosphorylationNSHQLSVSTPHSAAG
CCCEEEECCCCCCCC		32.6126160508
617PhosphorylationSHQLSVSTPHSAAGP
CCEEEECCCCCCCCC		23.9026160508
620PhosphorylationLSVSTPHSAAGPSPH
EEECCCCCCCCCCHH		22.4826824392
625PhosphorylationPHSAAGPSPHTLRRA
CCCCCCCCHHHHHHH		28.5326160508
628PhosphorylationAAGPSPHTLRRAVKK
CCCCCHHHHHHHHCC		25.9126160508
655PhosphorylationPGHPGGQSSPGTGTS
CCCCCCCCCCCCCCC		41.6026643407
656PhosphorylationGHPGGQSSPGTGTSP
CCCCCCCCCCCCCCC		21.3326643407
659PhosphorylationGGQSSPGTGTSPKPS
CCCCCCCCCCCCCCC		40.4429233185
661PhosphorylationQSSPGTGTSPKPSAR
CCCCCCCCCCCCCCC		41.5126643407
662PhosphorylationSSPGTGTSPKPSARS
CCCCCCCCCCCCCCC		32.0726643407
666PhosphorylationTGTSPKPSARSPSPP
CCCCCCCCCCCCCCH		42.3026643407
669PhosphorylationSPKPSARSPSPPQQQ
CCCCCCCCCCCHHHH		29.4625521595
671PhosphorylationKPSARSPSPPQQQQQ
CCCCCCCCCHHHHHH		50.9225521595
691PhosphorylationQQQQQQQTPGMRRCS
HHHHHHHCHHHHHCC		19.9225159016
698PhosphorylationTPGMRRCSSSLPPIQ
CHHHHHCCCCCCCCC		22.5825521595
699PhosphorylationPGMRRCSSSLPPIQA
HHHHHCCCCCCCCCC		39.2521082442
700PhosphorylationGMRRCSSSLPPIQAP
HHHHCCCCCCCCCCC		28.7121082442
708PhosphorylationLPPIQAPSHPPPQPP
CCCCCCCCCCCCCCC		52.2025619855
730PhosphorylationQGPEPGPTPPQTPTP
CCCCCCCCCCCCCCC		54.2227087446
734PhosphorylationPGPTPPQTPTPPSTP
CCCCCCCCCCCCCCC		34.6027087446
736PhosphorylationPTPPQTPTPPSTPPL
CCCCCCCCCCCCCCH		51.7427087446
739PhosphorylationPQTPTPPSTPPLAKQ
CCCCCCCCCCCHHHC		55.5427087446
740PhosphorylationQTPTPPSTPPLAKQN
CCCCCCCCCCHHHCC		34.4027087446
759PhosphorylationETTQLHGTLPRPRPV
CCCCCCCCCCCCCCC		23.8826824392
784PhosphorylationPPPHPPGTHTVDGGL
CCCCCCCCCCCCCCC		21.8329899451
786PhosphorylationPHPPGTHTVDGGLTS
CCCCCCCCCCCCCCC		21.8229899451
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 RHG17_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHG17_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 RHG17_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RHG17_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RHG17_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.

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