ARHG8_HUMAN - dbPTM
ARHG8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARHG8_HUMAN
UniProt AC Q7Z628
Protein Name Neuroepithelial cell-transforming gene 1 protein
Gene Name NET1
Organism Homo sapiens (Human).
Sequence Length 596
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase. May be involved in activation of the SAPK/JNK pathway Stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death..
Protein Sequence MEPELAAQKQPRPRRRSRRASGLSTEGATGPSADTSGSELDGRCSLRRGSSFTFLTPGPNWDFTLKRKRREKDDDVVSLSSLDLKEPSNKRVRPLARVTSLANLISPVRNGAVRRFGQTIQSFTLRGDHRSPASAQKFSSRSTVPTPAKRRSSALWSEMLDITMKESLTTREIRRQEAIYEMSRGEQDLIEDLKLARKAYHDPMLKLSIMSEEELTHIFGDLDSYIPLHEDLLTRIGEATKPDGTVEQIGHILVSWLPRLNAYRGYCSNQLAAKALLDQKKQDPRVQDFLQRCLESPFSRKLDLWSFLDIPRSRLVKYPLLLKEILKHTPKEHPDVQLLEDAILIIQGVLSDINLKKGESECQYYIDKLEYLDEKQRDPRIEASKVLLCHGELRSKSGHKLYIFLFQDILVLTRPVTRNERHSYQVYRQPIPVQELVLEDLQDGDVRMGGSFRGAFSNSEKAKNIFRIRFHDPSPAQSHTLQANDVFHKQQWFNCIRAAIAPFQSAGSPPELQGLPELHEECEGNHPSARKLTAQRRASTVSSVTQVEVDENAYRCGSGMQMAEDSKSLKTHQTQPGIRRARDKALSGGKRKETLV
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-------MEPELAAQ
-------CCHHHHHC		20.4822814378
9UbiquitinationEPELAAQKQPRPRRR
CHHHHHCCCCCCCCH		58.50-
9AcetylationEPELAAQKQPRPRRR
CHHHHHCCCCCCCCH		58.5025953088
17PhosphorylationQPRPRRRSRRASGLS
CCCCCCHHHHHCCCC		25.0623898821
21PhosphorylationRRRSRRASGLSTEGA
CCHHHHHCCCCCCCC		38.1530266825
24PhosphorylationSRRASGLSTEGATGP
HHHHCCCCCCCCCCC		28.1230266825
25PhosphorylationRRASGLSTEGATGPS
HHHCCCCCCCCCCCC		43.4030266825
29PhosphorylationGLSTEGATGPSADTS
CCCCCCCCCCCCCCC		61.5630266825
32PhosphorylationTEGATGPSADTSGSE
CCCCCCCCCCCCCCC		39.8723927012
35PhosphorylationATGPSADTSGSELDG
CCCCCCCCCCCCCCC		34.4030576142
36PhosphorylationTGPSADTSGSELDGR
CCCCCCCCCCCCCCC		40.6530576142
38PhosphorylationPSADTSGSELDGRCS
CCCCCCCCCCCCCCE		34.4523927012
50PhosphorylationRCSLRRGSSFTFLTP
CCEECCCCCCEEECC		22.0728450419
51PhosphorylationCSLRRGSSFTFLTPG
CEECCCCCCEEECCC		31.0028464451
53PhosphorylationLRRGSSFTFLTPGPN
ECCCCCCEEECCCCC		21.4928464451
56PhosphorylationGSSFTFLTPGPNWDF
CCCCEEECCCCCCCC		23.2428464451
64PhosphorylationPGPNWDFTLKRKRRE
CCCCCCCEECCCCCC		28.97-
78PhosphorylationEKDDDVVSLSSLDLK
CCCCCEEEHHHCCCC		23.5322199227
80PhosphorylationDDDVVSLSSLDLKEP
CCCEEEHHHCCCCCC		22.7320873877
81PhosphorylationDDVVSLSSLDLKEPS
CCEEEHHHCCCCCCC		31.0627251275
85UbiquitinationSLSSLDLKEPSNKRV
EHHHCCCCCCCCCCC		68.21-
99PhosphorylationVRPLARVTSLANLIS
CCHHHHHHHHHHHHH		16.6929978859
100PhosphorylationRPLARVTSLANLISP
CHHHHHHHHHHHHHH		23.7226055452
106PhosphorylationTSLANLISPVRNGAV
HHHHHHHHHHHCCHH		22.1026055452
119PhosphorylationAVRRFGQTIQSFTLR
HHHHCHHEEEEEEEC		22.7423186163
122PhosphorylationRFGQTIQSFTLRGDH
HCHHEEEEEEECCCC		19.1523186163
124PhosphorylationGQTIQSFTLRGDHRS
HHEEEEEEECCCCCC		22.3124719451
126MethylationTIQSFTLRGDHRSPA
EEEEEEECCCCCCHH		45.49115484821
137UbiquitinationRSPASAQKFSSRSTV
CCHHHHCHHCCCCCC		47.10-
139PhosphorylationPASAQKFSSRSTVPT
HHHHCHHCCCCCCCC		31.7028985074
140 (in isoform 2)Ubiquitination-33.1221906983
140PhosphorylationASAQKFSSRSTVPTP
HHHCHHCCCCCCCCC		33.1228985074
142PhosphorylationAQKFSSRSTVPTPAK
HCHHCCCCCCCCCCH		35.3928985074
149UbiquitinationSTVPTPAKRRSSALW
CCCCCCCHHHHHHHH		49.93-
152PhosphorylationPTPAKRRSSALWSEM
CCCCHHHHHHHHHHH		24.8124719451
153PhosphorylationTPAKRRSSALWSEML
CCCHHHHHHHHHHHH		26.1028348404
180PhosphorylationIRRQEAIYEMSRGEQ
HHHHHHHHHHHCCCH		16.78-
183PhosphorylationQEAIYEMSRGEQDLI
HHHHHHHHCCCHHHH		25.79-
194 (in isoform 1)Ubiquitination-53.0421906983
194UbiquitinationQDLIEDLKLARKAYH
HHHHHHHHHHHHHHC		53.042190698
198UbiquitinationEDLKLARKAYHDPML
HHHHHHHHHHCCCCH		47.92-
241UbiquitinationTRIGEATKPDGTVEQ
HHHHHHCCCCCCHHH		48.43-
274UbiquitinationCSNQLAAKALLDQKK
HHHHHHHHHHHHHHC		33.68-
280UbiquitinationAKALLDQKKQDPRVQ
HHHHHHHHCCCHHHH		52.66-
301UbiquitinationLESPFSRKLDLWSFL
HHCCCCCCCCHHHHH		45.19-
317UbiquitinationIPRSRLVKYPLLLKE
CCHHHHHCHHHHHHH		45.82-
357UbiquitinationLSDINLKKGESECQY
HHHCCCCCCCCHHHH		71.70-
360PhosphorylationINLKKGESECQYYID
CCCCCCCCHHHHHHH		52.95-
368UbiquitinationECQYYIDKLEYLDEK
HHHHHHHHHHHHCHH		33.39-
375UbiquitinationKLEYLDEKQRDPRIE
HHHHHCHHHCCCCHH		50.75-
385UbiquitinationDPRIEASKVLLCHGE
CCCHHHHHEEEEECC		43.90-
396UbiquitinationCHGELRSKSGHKLYI
EECCHHCCCCCEEEE		54.76-
451PhosphorylationGDVRMGGSFRGAFSN
CCCCCCCCCCCCCCC		13.1724719451
453MethylationVRMGGSFRGAFSNSE
CCCCCCCCCCCCCCH		36.91115484829
489UbiquitinationQANDVFHKQQWFNCI
CHHHHHCHHHHHHHH		32.49-
505PhosphorylationAAIAPFQSAGSPPEL
HHHHHHHHCCCCHHH		34.6730576142
508PhosphorylationAPFQSAGSPPELQGL
HHHHHCCCCHHHCCC		36.6825849741
528PhosphorylationECEGNHPSARKLTAQ
HHCCCCHHHHHHHHH		32.9121712546
533PhosphorylationHPSARKLTAQRRAST
CHHHHHHHHHHHHHC		24.6322817900
539PhosphorylationLTAQRRASTVSSVTQ
HHHHHHHHCCCCCEE		27.7727273156
540PhosphorylationTAQRRASTVSSVTQV
HHHHHHHCCCCCEEE		24.3425159151
542PhosphorylationQRRASTVSSVTQVEV
HHHHHCCCCCEEEEE		21.1228450419
543PhosphorylationRRASTVSSVTQVEVD
HHHHCCCCCEEEEEC		25.5026657352
545PhosphorylationASTVSSVTQVEVDEN
HHCCCCCEEEEECCC		28.9226657352
554PhosphorylationVEVDENAYRCGSGMQ
EEECCCCEECCCCCH		20.3022210691
558PhosphorylationENAYRCGSGMQMAED
CCCEECCCCCHHHCC		34.4223882029
567SumoylationMQMAEDSKSLKTHQT
CHHHCCCHHHCCCCC		72.61-
567UbiquitinationMQMAEDSKSLKTHQT
CHHHCCCHHHCCCCC		72.61-
567SumoylationMQMAEDSKSLKTHQT
CHHHCCCHHHCCCCC		72.61-
570SumoylationAEDSKSLKTHQTQPG
HCCCHHHCCCCCCHH		51.56-
570SumoylationAEDSKSLKTHQTQPG
HCCCHHHCCCCCCHH		51.56-
570UbiquitinationAEDSKSLKTHQTQPG
HCCCHHHCCCCCCHH		51.56-
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
100SPhosphorylationKinasePRKAA1Q13131
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARHG8_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 ARHG8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAGI1_HUMANMAGI1physical
11350080
DLG1_HUMANDLG1physical
19586902
MAGI1_HUMANMAGI1physical
19586902
DLG4_MOUSEDlg4physical
17938206
DLG1_MOUSEDlg1physical
17938206
DLG3_MOUSEDlg3physical
17938206
MAGI1_MOUSEMagi1physical
17938206
MPP2_MOUSEMpp2physical
17938206
MPP6_MOUSEMpp6physical
17938206
CSKP_MOUSECaskphysical
17938206
LIN7C_MOUSELin7cphysical
17938206
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 ARHG8_HUMAN

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Related Literatures of Post-Translational Modification
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-21; SER-32; SER-100 ANDSER-106, AND MASS SPECTROMETRY.
"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-100 AND SER-106, ANDMASS SPECTROMETRY.

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