ARHG6_MOUSE - dbPTM
ARHG6_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARHG6_MOUSE
UniProt AC Q8K4I3
Protein Name Rho guanine nucleotide exchange factor 6
Gene Name Arhgef6
Organism Mus musculus (Mouse).
Sequence Length 771
Subcellular Localization Cell projection, lamellipodium .
Protein Description Acts as a RAC1 guanine nucleotide exchange factor (GEF)..
Protein Sequence MNPEERLVTWLISLGVLESPKKTVCDPEEFLKSSLKNGVVLCKLINRLLPGSVEKYCLEPQTEADCIDNINDFLKGCATLQVEVFEPDDLYSGANFSKVLNTLLAVNKATEDQLSERPCGRSSSLSAATSSQTNPQVAVPSTAPEQHSEEKAEMTENGSHQLIVKARFNFKQTNEDELSVCKGDIIYVTRVEEGGWWEGTLNGRTGWFPSNYVREIKPSERPLSPKAIKGFDTAPLTKNYYTVVLQNILDTEKEYAKELQSLLVTYLRPLQSNNNLSTVEFTCLLGNFEEVCTFQQTLCQALEECSKFPENQHKVGGCLLNLMPHFKSMYLAYCANHPSAVNVLTQHSDDLERFMENQGASSPGILILTTSLSKPFMRLEKYVTLLQELERHMEDTHPDHQDILKAIIAFKTLMGQCQDLRKRKQLELQILSEPIQAWEGDDIKTLGNVIFMSQVVMQHGACEEKEERYFLLFSSVLIMLSASPRMSGFMYQGKIPIAGMVVNRLDEIEGSDCMFEITGSTVERIVVHCNNNQDFQEWMEQLNRLTKGPTSCGSLSKTSSSSCSTHSSFSSTGQPRGPLEPPQIIKPWSLSCLRPAPPLRPSAALGYKERMSYILKESSKSPKTMKKFLHKRKTERKASEEEYVIRKSTAALEEDAQILKVIEAYCTSASFQQGTRKDSVPQVLLPEEEKLIIEETRSNGQTIIEEKSLVDTVYALKDEVKELKQENKKMKQCLEEELKSRKDLEKLVRKLLKQTDECIRSESSSKTSILQ
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
13PhosphorylationRLVTWLISLGVLESP
HHHHHHHHHCCCCCC		19.5326160508
33PhosphorylationDPEEFLKSSLKNGVV
CHHHHHHHHCCCCHH		42.9518268350
34PhosphorylationPEEFLKSSLKNGVVL
HHHHHHHHCCCCHHH		41.6018268350
122PhosphorylationSERPCGRSSSLSAAT
CCCCCCCCCCHHHHH		15.0126160508
123PhosphorylationERPCGRSSSLSAATS
CCCCCCCCCHHHHHC		33.6626160508
124PhosphorylationRPCGRSSSLSAATSS
CCCCCCCCHHHHHCC		27.8226160508
126PhosphorylationCGRSSSLSAATSSQT
CCCCCCHHHHHCCCC		20.1526160508
129PhosphorylationSSSLSAATSSQTNPQ
CCCHHHHHCCCCCCC		28.7323984901
130PhosphorylationSSLSAATSSQTNPQV
CCHHHHHCCCCCCCC		18.7429472430
131PhosphorylationSLSAATSSQTNPQVA
CHHHHHCCCCCCCCC		36.3529472430
133PhosphorylationSAATSSQTNPQVAVP
HHHHCCCCCCCCCCC		51.3029472430
181GlutathionylationNEDELSVCKGDIIYV
CHHHHEEECCCEEEE		3.5124333276
219PhosphorylationYVREIKPSERPLSPK
HEEECCCCCCCCCHH		41.0326824392
224PhosphorylationKPSERPLSPKAIKGF
CCCCCCCCHHHCCCC		27.3426824392
248PhosphorylationYTVVLQNILDTEKEY
HHHHHHHHHHCHHHH		2.0724719451
487PhosphorylationLSASPRMSGFMYQGK
HHCCCCCCCCCCCCC		30.1125521595
491PhosphorylationPRMSGFMYQGKIPIA
CCCCCCCCCCCCCCC		16.3228833060
511PhosphorylationRLDEIEGSDCMFEIT
CHHHCCCCCCEEEEC		18.1724719451
551PhosphorylationRLTKGPTSCGSLSKT
HHHCCCCCCCCCCCC		21.4428833060
552GlutathionylationLTKGPTSCGSLSKTS
HHCCCCCCCCCCCCC		4.7624333276
554PhosphorylationKGPTSCGSLSKTSSS
CCCCCCCCCCCCCCC		33.5228833060
556PhosphorylationPTSCGSLSKTSSSSC
CCCCCCCCCCCCCCC		35.2728833060
558PhosphorylationSCGSLSKTSSSSCST
CCCCCCCCCCCCCCC		30.3920531401
558O-linked_GlycosylationSCGSLSKTSSSSCST
CCCCCCCCCCCCCCC		30.3930059200
559PhosphorylationCGSLSKTSSSSCSTH
CCCCCCCCCCCCCCC		31.7720531401
560PhosphorylationGSLSKTSSSSCSTHS
CCCCCCCCCCCCCCC		31.3520531401
561PhosphorylationSLSKTSSSSCSTHSS
CCCCCCCCCCCCCCC		34.8220531401
562PhosphorylationLSKTSSSSCSTHSSF
CCCCCCCCCCCCCCC		17.6520531401
563GlutathionylationSKTSSSSCSTHSSFS
CCCCCCCCCCCCCCC		6.1724333276
564PhosphorylationKTSSSSCSTHSSFSS
CCCCCCCCCCCCCCC		30.9720531401
565PhosphorylationTSSSSCSTHSSFSST
CCCCCCCCCCCCCCC		30.0620531401
567PhosphorylationSSSCSTHSSFSSTGQ
CCCCCCCCCCCCCCC		32.9220531401
568PhosphorylationSSCSTHSSFSSTGQP
CCCCCCCCCCCCCCC		22.8820531401
570PhosphorylationCSTHSSFSSTGQPRG
CCCCCCCCCCCCCCC		29.0120531401
571PhosphorylationSTHSSFSSTGQPRGP
CCCCCCCCCCCCCCC		34.2520531401
572PhosphorylationTHSSFSSTGQPRGPL
CCCCCCCCCCCCCCC		38.3420531401
578PhosphorylationSTGQPRGPLEPPQII
CCCCCCCCCCCCCCC		34.5324719451
612PhosphorylationLGYKERMSYILKESS
CCHHHHHHHHHHHCC		18.4229176673
613PhosphorylationGYKERMSYILKESSK
CHHHHHHHHHHHCCC		10.8329472430
621PhosphorylationILKESSKSPKTMKKF
HHHHCCCCHHHHHHH		33.3127600695
634PhosphorylationKFLHKRKTERKASEE
HHHHHHHHCCCCCHH		45.0923375375
639PhosphorylationRKTERKASEEEYVIR
HHHCCCCCHHHHHHH		48.8825521595
643PhosphorylationRKASEEEYVIRKSTA
CCCCHHHHHHHHHHH		12.4028833060
648PhosphorylationEEYVIRKSTAALEED
HHHHHHHHHHHHHHH		17.2725521595
649PhosphorylationEYVIRKSTAALEEDA
HHHHHHHHHHHHHHH		20.9825521595
663PhosphorylationAQILKVIEAYCTSAS
HHHHHHHHHHHHHCC		36.2524719451
665PhosphorylationILKVIEAYCTSASFQ
HHHHHHHHHHHCCCC		5.4025367039
666GlutathionylationLKVIEAYCTSASFQQ
HHHHHHHHHHCCCCC		2.9024333276
667PhosphorylationKVIEAYCTSASFQQG
HHHHHHHHHCCCCCC		18.0426745281
668PhosphorylationVIEAYCTSASFQQGT
HHHHHHHHCCCCCCC		20.5327600695
670PhosphorylationEAYCTSASFQQGTRK
HHHHHHCCCCCCCCC		24.2926745281
675PhosphorylationSASFQQGTRKDSVPQ
HCCCCCCCCCCCCCE		30.1526745281
679PhosphorylationQQGTRKDSVPQVLLP
CCCCCCCCCCEEECC		38.4425521595
698PhosphorylationLIIEETRSNGQTIIE
EEEEEHHHCCCEEEE		53.3722817900
703PhosphorylationTRSNGQTIIEEKSLV
HHHCCCEEEEEHHHH		2.6124719451
714PhosphorylationKSLVDTVYALKDEVK
HHHHHHHHHHHHHHH		14.3325367039
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 ARHG6_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARHG6_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 ARHG6_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433Z_MOUSEYwhazphysical
16959763
GIT1_MOUSEGit1physical
16959763
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARHG6_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487 AND SER-679, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639 AND SER-679, ANDMASS SPECTROMETRY.
"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-122 AND THR-649, ANDMASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND MASSSPECTROMETRY.

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