ARHG1_MOUSE - dbPTM
ARHG1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARHG1_MOUSE
UniProt AC Q61210
Protein Name Rho guanine nucleotide exchange factor 1
Gene Name Arhgef1
Organism Mus musculus (Mouse).
Sequence Length 920
Subcellular Localization Cytoplasm. Membrane. Translocated to the membrane by activated GNA13 or LPA stimulation..
Protein Description Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12. Mediates angiotensin-2-induced RhoA activation. Isoform 3 and isoform 4 do not homooligomerize and show an enhanced RhoGEF activity..
Protein Sequence MGEVAGGAAPGPPRSGLVSIIIGAEDEDFENELEANSEDQNSQFQSLEQVKRRPAHLMALLQHVALQFEPGPLLCCLHADMLSSLGPKEAKKAFLDFYHSFLEKTAVLRVPVPPSVAFELDRTRPDLISEDVQRRFIQEVVQSQQAAVSRQLEDFRSKRLMGMTPWEQELSLLEPWIGKDRGNYEARERHVAERLLSHLEETQHTISTDEEKSAAVVTAISLYMRHLGVRTKSGDKKSGRNFFRKKVMGNRRSDEPPKTKKGLSSILDPARWNRGEPSAPDCRHLKVEADAEKPGPADRKGGLGMSSRDRTVGTPGQDNPGVSLHPLSTDSVDSREPGVDTPQEPGDTPPQGPTSLEPLAPPESTEDNGETESPEPGDDGEPGRSGLELEPEEPPGWRELVPPDTLLSLPKSQVKRQEVISELLVTEAAHVRMLRVLHDLFYQPMADGGFFPLDELQNIFPSLDELIEVHSLFLDRLMKRRQESGYLIEEIGDVLLARFDGAEGSWFQKISSRFCSRQSFALEQLKAKQRKEPRFCAFVQEAESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQNTEESTERGKVELAAECCREILHHVNQAVRDMEDLLRLKDYQRRLDLTHLRQSSDPMLSEFKNLDITKKKLVHEGPLTWRVTKDKAIEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTPTPDGKTMLRPVLRLTSAMTREVATDHKAFYVIFTWDQEAQIYELVAQTSSERKNWCNLITETAGSLKVPAPASRLKPRPSPSSIREPLLSSSENGTGGAEMAPADARTERLLNDLLPFCRPGPEGQLAATALQKVLSLKQILLSTEEDSGAGPPRDGDGVPGGRAPGPVHTQEIEENLLSLEVAIRQLEELEEEFCRLRPLLSQLGGTLSPNLAAPERSAQTGLS
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
123PhosphorylationVAFELDRTRPDLISE
HHHCCCCCCCCCCCH		46.3422871156
197PhosphorylationHVAERLLSHLEETQH
HHHHHHHHHHHHHCC		30.5326370283
207PhosphorylationEETQHTISTDEEKSA
HHHCCCCCCCHHHHH		30.8429514104
253PhosphorylationKVMGNRRSDEPPKTK
HHHCCCCCCCCCCCC		42.9925266776
264PhosphorylationPKTKKGLSSILDPAR
CCCCCCHHHHCCHHH		24.8129472430
265PhosphorylationKTKKGLSSILDPARW
CCCCCHHHHCCHHHC		32.0129472430
286AcetylationAPDCRHLKVEADAEK
CCCCCCCCEEECCCC		31.7222826441
305 (in isoform 2)Phosphorylation-3.8525266776
305 (in isoform 5)Phosphorylation-3.8525266776
306PhosphorylationRKGGLGMSSRDRTVG
CCCCCCCCCCCCCCC		22.0325266776
307PhosphorylationKGGLGMSSRDRTVGT
CCCCCCCCCCCCCCC		29.3429176673
314PhosphorylationSRDRTVGTPGQDNPG
CCCCCCCCCCCCCCC		21.6528066266
348PhosphorylationTPQEPGDTPPQGPTS
CCCCCCCCCCCCCCC		42.6623140645
354PhosphorylationDTPPQGPTSLEPLAP
CCCCCCCCCCCCCCC		53.4123140645
355PhosphorylationTPPQGPTSLEPLAPP
CCCCCCCCCCCCCCC		33.5923140645
364PhosphorylationEPLAPPESTEDNGET
CCCCCCCCCCCCCCC		42.7623140645
365PhosphorylationPLAPPESTEDNGETE
CCCCCCCCCCCCCCC		45.7723140645
371PhosphorylationSTEDNGETESPEPGD
CCCCCCCCCCCCCCC		43.0623140645
373PhosphorylationEDNGETESPEPGDDG
CCCCCCCCCCCCCCC		41.8225521595
384 (in isoform 5)Phosphorylation-37.9625266776
385PhosphorylationDDGEPGRSGLELEPE
CCCCCCCCCCCCCCC		54.3625266776
386 (in isoform 5)Phosphorylation-23.0827566939
390 (in isoform 5)Phosphorylation-41.0927566939
396 (in isoform 5)Phosphorylation-46.9525266776
399 (in isoform 5)Phosphorylation-47.8425266776
408PhosphorylationVPPDTLLSLPKSQVK
CCHHHHHCCCHHHHC		45.82-
410 (in isoform 5)Phosphorylation-30.7625521595
412 (in isoform 5)Phosphorylation-37.9625521595
412PhosphorylationTLLSLPKSQVKRQEV
HHHCCCHHHHCHHHH		37.9624704852
420 (in isoform 5)Phosphorylation-2.3224704852
422 (in isoform 5)Phosphorylation-34.6926745281
428 (in isoform 5)Phosphorylation-8.1026745281
432 (in isoform 5)Phosphorylation-14.4625521595
444 (in isoform 5)Phosphorylation-14.4625367039
484PhosphorylationLMKRRQESGYLIEEI
HHHHHHHHCCCHHEE		25.1325367039
486PhosphorylationKRRQESGYLIEEIGD
HHHHHHCCCHHEEHH		17.4925367039
536GlutathionylationQRKEPRFCAFVQEAE
HCCCCCHHHHHHHHH		2.7924333276
629PhosphorylationDLTHLRQSSDPMLSE
CHHHHHCCCCCCHHH		30.2128833060
630PhosphorylationLTHLRQSSDPMLSEF
HHHHHCCCCCCHHHH		37.0828833060
635PhosphorylationQSSDPMLSEFKNLDI
CCCCCCHHHHCCCCC		34.4328833060
694PhosphorylationKSHSRTLTPTPDGKT
HHHCCCCCCCCCCCC		25.2228833060
696PhosphorylationHSRTLTPTPDGKTML
HCCCCCCCCCCCCCH		28.8628833060
737PhosphorylationWDQEAQIYELVAQTS
CCHHHHHHHHHHCCC		7.3620098430
775PhosphorylationSRLKPRPSPSSIREP
HHCCCCCCCHHCCCC		38.4026824392
777PhosphorylationLKPRPSPSSIREPLL
CCCCCCCHHCCCCCC		42.6129472430
778PhosphorylationKPRPSPSSIREPLLS
CCCCCCHHCCCCCCC		29.1129472430
785PhosphorylationSIREPLLSSSENGTG
HCCCCCCCCCCCCCC		39.2325367039
786PhosphorylationIREPLLSSSENGTGG
CCCCCCCCCCCCCCC		41.4625266776
787PhosphorylationREPLLSSSENGTGGA
CCCCCCCCCCCCCCC		31.5325266776
791PhosphorylationLSSSENGTGGAEMAP
CCCCCCCCCCCCCCC		43.9830635358
815MethylationNDLLPFCRPGPEGQL
HHHHHHCCCCCCHHH		39.32-
832PhosphorylationTALQKVLSLKQILLS
HHHHHHHCHHHHHHC		36.1930387612
898PhosphorylationCRLRPLLSQLGGTLS
HHHHHHHHHCCCCCC		30.9226239621
903PhosphorylationLLSQLGGTLSPNLAA
HHHHCCCCCCCCCCC		23.4326239621
905PhosphorylationSQLGGTLSPNLAAPE
HHCCCCCCCCCCCCH		16.1626824392
914PhosphorylationNLAAPERSAQTGLS-
CCCCCHHHHHCCCC-		24.0626745281
917PhosphorylationAPERSAQTGLS----
CCHHHHHCCCC----		39.5426745281
920PhosphorylationRSAQTGLS-------
HHHHCCCC-------		39.2526745281
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
737YPhosphorylationKinaseJAK2Q62120
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
390SPhosphorylation

19144319
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 ARHG1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ARHG1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARHG1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The Rho exchange factor Arhgef1 mediates the effects of angiotensinII on vascular tone and blood pressure.";
Guilluy C., Bregeon J., Toumaniantz G., Rolli-Derkinderen M.,Retailleau K., Loufrani L., Henrion D., Scalbert E., Bril A.,Torres R.M., Offermanns S., Pacaud P., Loirand G.;
Nat. Med. 16:183-190(2010).
Cited for: FUNCTION, DISRUPTION PHENOTYPE, AND PHOSPHORYLATION AT TYR-737.

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