RHG05_HUMAN - dbPTM
RHG05_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG05_HUMAN
UniProt AC Q13017
Protein Name Rho GTPase-activating protein 5
Gene Name ARHGAP5
Organism Homo sapiens (Human).
Sequence Length 1502
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein . Also membrane-associated in a fibrillar pattern that colocalizes with the alpha5-beta1 integrin receptor (ITGA5/ITGB1) for fibronectin.
Protein Description GTPase-activating protein for Rho family members. [PubMed: 8537347]
Protein Sequence MMAKNKEPRPPSYTISIVGLSGTEKDKGNCGVGKSCLCNRFVRSKADEYYPEHTSVLSTIDFGGRVVNNDHFLYWGDIIQNSEDGVECKIHVIEQTEFIDDQTFLPHRSTNLQPYIKRAAASKLQSAEKLMYICTDQLGLEQDFEQKQMPEGKLNVDGFLLCIDVSQGCNRKFDDQLKFVNNLFVQLSKSKKPVIIAATKCDECVDHYLREVQAFASNKKNLLVVETSARFNVNIETCFTALVQMLDKTRSKPKIIPYLDAYKTQRQLVVTATDKFEKLVQTVRDYHATWKTVSNKLKNHPDYEEYINLEGTRKARNTFSKHIEQLKQEHIRKRREEYINTLPRAFNTLLPNLEEIEHLNWSEALKLMEKRADFQLCFVVLEKTPWDETDHIDKINDRRIPFDLLSTLEAEKVYQNHVQHLISEKRRVEMKEKFKKTLEKIQFISPGQPWEEVMCFVMEDEAYKYITEADSKEVYGRHQREIVEKAKEEFQEMLFEHSELFYDLDLNATPSSDKMSEIHTVLSEEPRYKALQKLAPDRESLLLKHIGFVYHPTKETCLSGQNCTDIKVEQLLASSLLQLDHGRLRLYHDSTNIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLSFIGEFIGKIRTEASQIRKDKYMANLPFTLILANQRDSISKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALRGVLESVKHNLDVVSPIPANKDLSEADLRIVMCAMCGDPFSVDLILSPFLDSHSCSAAQAGQNNSLMLDKIIGEKRRRIQITILSYHSSIGVRKDELVHGYILVYSAKRKASMGMLRAFLSEVQDTIPVQLVAVTDSQADFFENEAIKELMTEGEHIATEITAKFTALYSLSQYHRQTEVFTLFFSDVLEKKNMIENSYLSDNTRESTHQSEDVFLPSPRDCFPYNNYPDSDDDTEAPPPYSPIGDDVQLLPTPSDRSRYRLDLEGNEYPIHSTPNCHDHERNHKVPPPIKPKPVVPKTNVKKLDPNLLKTIEAGIGKNPRKQTSRVPLAHPEDMDPSDNYAEPIDTIFKQKGYSDEIYVVPDDSQNRIKIRNSFVNNTQGDEENGFSDRTSKSHGERRPSKYKYKSKTLFSKAKSYYRRTHSDASDDEAFTTSKTKRKGRHRGSEEDPLLSPVETWKGGIDNPAITSDQELDDKKMKKKTHKVKEDKKQKKKTKNFNPPTRRNWESNYFGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMRPDFENREFLSTTKIHQSVVETFIQQCQFFFYNGEIVETTNIVAPPPPSNPGQLVEPMVPLQLPPPLQPQLIQPQLQTDPLGII
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
12PhosphorylationNKEPRPPSYTISIVG
CCCCCCCCEEEEEEE		37.2824719451
16PhosphorylationRPPSYTISIVGLSGT
CCCCEEEEEEECCCC		11.92-
21PhosphorylationTISIVGLSGTEKDKG
EEEEEECCCCCCCCC		37.4324719451
23PhosphorylationSIVGLSGTEKDKGNC
EEEECCCCCCCCCCC		36.1624719451
192UbiquitinationVQLSKSKKPVIIAAT
HHHHCCCCCEEEEEE		52.1629967540
199PhosphorylationKPVIIAATKCDECVD
CCEEEEEECCHHHHH		24.1522817900
227PhosphorylationKNLLVVETSARFNVN
CCEEEEEECCCCCCC		18.9724719451
264PhosphorylationPYLDAYKTQRQLVVT
HHHHHHHCCCEEEEE		19.1330622161
271PhosphorylationTQRQLVVTATDKFEK
CCCEEEEEEHHHHHH		19.1630622161
273PhosphorylationRQLVVTATDKFEKLV
CEEEEEEHHHHHHHH		30.2930622161
289PhosphorylationTVRDYHATWKTVSNK
HHHHHHCHHHHHHHH		17.7428060719
296UbiquitinationTWKTVSNKLKNHPDY
HHHHHHHHHHCCCCH		54.0227667366
306PhosphorylationNHPDYEEYINLEGTR
CCCCHHHHHCCHHHH		5.3312705864
314AcetylationINLEGTRKARNTFSK
HCCHHHHHHHHHHHH		52.087910503
321AcetylationKARNTFSKHIEQLKQ
HHHHHHHHHHHHHHH		44.407910515
327UbiquitinationSKHIEQLKQEHIRKR
HHHHHHHHHHHHHHH		54.0229967540
394UbiquitinationDETDHIDKINDRRIP
CCCCCHHHCCCCCCC		42.6929967540
423PhosphorylationNHVQHLISEKRRVEM
HHHHHHHHHHHHHHH		43.3424719451
533UbiquitinationPRYKALQKLAPDRES
HHHHHHHHHCCCHHH		47.6829967540
540PhosphorylationKLAPDRESLLLKHIG
HHCCCHHHHHHHHHC		25.8023312004
550Nitrated tyrosineLKHIGFVYHPTKETC
HHHHCEEECCCCCCC		10.38-
550NitrationLKHIGFVYHPTKETC
HHHHCEEECCCCCCC		10.3816777052
550NitrationLKHIGFVYHPTKETC
HHHHCEEECCCCCCC		10.3816777052
587PhosphorylationDHGRLRLYHDSTNID
CCCCEEEEECCCCCC		9.3525850435
590PhosphorylationRLRLYHDSTNIDKVN
CEEEEECCCCCCEEE		15.2725159151
591PhosphorylationLRLYHDSTNIDKVNL
EEEEECCCCCCEEEE		42.1021955146
630PhosphorylationYALDGKIYELDLRPV
HHCCCEEEEEECCCC		17.5818083107
680PhosphorylationEFIGKIRTEASQIRK
HHHHHHHHHHHHHHH		39.1018452278
706PhosphorylationILANQRDSISKNLPI
EEECCHHHHHHCCCH		30.8328176443
709UbiquitinationNQRDSISKNLPILRH
CCHHHHHHCCCHHHH		61.9133845483
724UbiquitinationQGQQLANKLQCPFVD
HHHHHHHHCCCCEEC		34.0429967540
765PhosphorylationKHNLDVVSPIPANKD
HHCCCCCCCCCCCCC		19.5729255136
774PhosphorylationIPANKDLSEADLRIV
CCCCCCCCCCCHHHH		40.6523312004
836PhosphorylationIQITILSYHSSIGVR
EEEEEEEECCCCCCC		11.4122817900
862PhosphorylationYSAKRKASMGMLRAF
EEHHHHHCHHHHHHH		20.92-
948PhosphorylationKKNMIENSYLSDNTR
HCCCCCCCCCCCCCC		18.0527732954
949PhosphorylationKNMIENSYLSDNTRE
CCCCCCCCCCCCCCC		23.0827732954
951PhosphorylationMIENSYLSDNTREST
CCCCCCCCCCCCCCC		22.1525159151
954PhosphorylationNSYLSDNTRESTHQS
CCCCCCCCCCCCCCC		40.5829978859
957PhosphorylationLSDNTRESTHQSEDV
CCCCCCCCCCCCCCC		28.0923403867
968PhosphorylationSEDVFLPSPRDCFPY
CCCCCCCCCCCCCCC		34.4123401153
975PhosphorylationSPRDCFPYNNYPDSD
CCCCCCCCCCCCCCC		8.8627251275
978PhosphorylationDCFPYNNYPDSDDDT
CCCCCCCCCCCCCCC		12.5527251275
981PhosphorylationPYNNYPDSDDDTEAP
CCCCCCCCCCCCCCC		38.1320873877
985PhosphorylationYPDSDDDTEAPPPYS
CCCCCCCCCCCCCCC		40.8320873877
991PhosphorylationDTEAPPPYSPIGDDV
CCCCCCCCCCCCCCE		32.6226074081
992PhosphorylationTEAPPPYSPIGDDVQ
CCCCCCCCCCCCCEE		18.8020873877
1003PhosphorylationDDVQLLPTPSDRSRY
CCEEECCCCCCCCCE		35.0820873877
1005PhosphorylationVQLLPTPSDRSRYRL
EEECCCCCCCCCEEE		48.4026074081
1008PhosphorylationLPTPSDRSRYRLDLE
CCCCCCCCCEEEECC		38.3626074081
1010PhosphorylationTPSDRSRYRLDLEGN
CCCCCCCEEEECCCC		19.4426074081
1019PhosphorylationLDLEGNEYPIHSTPN
EECCCCCCCCCCCCC		16.1027259358
1023PhosphorylationGNEYPIHSTPNCHDH
CCCCCCCCCCCCCCC		46.4028348404
1024PhosphorylationNEYPIHSTPNCHDHE
CCCCCCCCCCCCCCC		12.3524719451
1053UbiquitinationVPKTNVKKLDPNLLK
CCCCCHHCCCHHHHH		54.5729967540
1060UbiquitinationKLDPNLLKTIEAGIG
CCCHHHHHHHHHCCC		51.1032015554
1061PhosphorylationLDPNLLKTIEAGIGK
CCHHHHHHHHHCCCC		24.8224114839
1068AcetylationTIEAGIGKNPRKQTS
HHHHCCCCCCCCCCC		62.9525953088
1088PhosphorylationHPEDMDPSDNYAEPI
CHHHCCCCCCCCCCC		33.9428796482
1091PhosphorylationDMDPSDNYAEPIDTI
HCCCCCCCCCCCHHH		19.8227273156
1097PhosphorylationNYAEPIDTIFKQKGY
CCCCCCHHHHHCCCC		29.0926356563
1100UbiquitinationEPIDTIFKQKGYSDE
CCCHHHHHCCCCCCE		47.4532015554
1102UbiquitinationIDTIFKQKGYSDEIY
CHHHHHCCCCCCEEE		61.4829967540
1104PhosphorylationTIFKQKGYSDEIYVV
HHHHCCCCCCEEEEC		21.7121712546
1105PhosphorylationIFKQKGYSDEIYVVP
HHHCCCCCCEEEECC		37.1225159151
1109PhosphorylationKGYSDEIYVVPDDSQ
CCCCCEEEECCCCCC		8.0525159151
1114PhosphorylationEIYVVPDDSQNRIKI
EEEECCCCCCCCEEE		46.1618669648
1115PhosphorylationIYVVPDDSQNRIKIR
EEECCCCCCCCEEEE		36.4125159151
1123PhosphorylationQNRIKIRNSFVNNTQ
CCCEEEEHHHCCCCC		43.1818669648
1124PhosphorylationNRIKIRNSFVNNTQG
CCEEEEHHHCCCCCC		22.2629255136
1128PhosphorylationIRNSFVNNTQGDEEN
EEHHHCCCCCCCCCC		28.6018669648
1129PhosphorylationRNSFVNNTQGDEENG
EHHHCCCCCCCCCCC		28.8225159151
1138PhosphorylationGDEENGFSDRTSKSH
CCCCCCCCCCCCCCC		27.8125159151
1141PhosphorylationENGFSDRTSKSHGER
CCCCCCCCCCCCCCC		45.5625159151
1142PhosphorylationNGFSDRTSKSHGERR
CCCCCCCCCCCCCCC		32.8125159151
1144PhosphorylationFSDRTSKSHGERRPS
CCCCCCCCCCCCCCC		36.1722985185
1157PhosphorylationPSKYKYKSKTLFSKA
CCCCCCCCHHHHHHH		27.9923312004
1159PhosphorylationKYKYKSKTLFSKAKS
CCCCCCHHHHHHHHH		39.8829759185
1162PhosphorylationYKSKTLFSKAKSYYR
CCCHHHHHHHHHHHH		34.5124719451
1166PhosphorylationTLFSKAKSYYRRTHS
HHHHHHHHHHHHCCC		32.0529514088
1171PhosphorylationAKSYYRRTHSDASDD
HHHHHHHCCCCCCCC		19.4129255136
1173PhosphorylationSYYRRTHSDASDDEA
HHHHHCCCCCCCCCC		33.9729255136
1176PhosphorylationRRTHSDASDDEAFTT
HHCCCCCCCCCCCCC		51.0529255136
1182PhosphorylationASDDEAFTTSKTKRK
CCCCCCCCCCCCCCC		36.8923927012
1183PhosphorylationSDDEAFTTSKTKRKG
CCCCCCCCCCCCCCC		23.0523927012
1184PhosphorylationDDEAFTTSKTKRKGR
CCCCCCCCCCCCCCC		34.9623927012
1195PhosphorylationRKGRHRGSEEDPLLS
CCCCCCCCCCCCCCC		37.4623927012
1201PhosphorylationGSEEDPLLSPVETWK
CCCCCCCCCCHHHCC		7.0918669648
1202PhosphorylationSEEDPLLSPVETWKG
CCCCCCCCCHHHCCC		34.2819664994
1206PhosphorylationPLLSPVETWKGGIDN
CCCCCHHHCCCCCCC		32.4830266825
1217PhosphorylationGIDNPAITSDQELDD
CCCCCCCCCCHHHCH		28.4929255136
1218PhosphorylationIDNPAITSDQELDDK
CCCCCCCCCHHHCHH		31.0529255136
1231 (in isoform 2)Phosphorylation-35.4926657352
1243 (in isoform 2)Phosphorylation-72.3026657352
1288PhosphorylationCVEFIEDTGLCTEGL
HHHHHHHHCCCCCCE		21.1820068231
1292PhosphorylationIEDTGLCTEGLYRVS
HHHHCCCCCCEEECC		37.8220068231
1296PhosphorylationGLCTEGLYRVSGNKT
CCCCCCEEECCCCCC		21.5920068231
1299PhosphorylationTEGLYRVSGNKTDQD
CCCEEECCCCCCCHH		27.8720068231
1387PhosphorylationVNYDVFRYVITHLNR
CCHHHHHHHHHHHHH		5.6923828894
1396PhosphorylationITHLNRVSQQHKINL
HHHHHHHCHHHCCCE		22.38-
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
306YPhosphorylationKinaseINSRP06213
PSP
1109YPhosphorylationKinasePTK6Q13882
GPS
1109YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHG05_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 RHG05_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RND3_HUMANRND3physical
12842009
RND1_HUMANRND1physical
12842009
RND2_HUMANRND2physical
12842009
PAXI_HUMANPXNphysical
10092539
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 RHG05_HUMAN

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Related Literatures of Post-Translational Modification
Nitration
ReferencePubMed
"Nitroproteins from a human pituitary adenoma tissue discovered with anitrotyrosine affinity column and tandem mass spectrometry.";
Zhan X., Desiderio D.M.;
Anal. Biochem. 354:279-289(2006).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-550, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1195 AND SER-1202, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1218, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968; SER-1115; SER-1124;THR-1129; SER-1138; SER-1173; SER-1176; SER-1195; SER-1202 ANDSER-1218, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765 AND SER-1202, ANDMASS SPECTROMETRY.
"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-1109, AND MASSSPECTROMETRY.

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