ARHG1_HUMAN - dbPTM
ARHG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARHG1_HUMAN
UniProt AC Q92888
Protein Name Rho guanine nucleotide exchange factor 1
Gene Name ARHGEF1
Organism Homo sapiens (Human).
Sequence Length 912
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..
Protein Sequence MEDFARGAASPGPSRPGLVPVSIIGAEDEDFENELETNSEEQNSQFQSLEQVKRRPAHLMALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDFYHSFLEKTAVLRVPVPPNVAFELDRTRADLISEDVQRRFVQEVVQSQQVAVGRQLEDFRSKRLMGMTPWEQELAQLEAWVGRDRASYEARERHVAERLLMHLEEMQHTISTDEEKSAAVVNAIGLYMRHLGVRTKSGDKKSGRNFFRKKVMGNRRSDEPAKTKKGLSSILDAARWNRGEPQVPDFRHLKAEVDAEKPGATDRKGGVGMPSRDRNIGAPGQDTPGVSLHPLSLDSPDREPGADAPLELGDSSPQGPMSLESLAPPESTDEGAETESPEPGDEGEPGRSGLELEPEEPPGWRELVPPDTLHSLPKSQVKRQEVISELLVTEAAHVRMLRVLHDLFFQPMAECLFFPLEELQNIFPSLDELIEVHSLFLDRLMKRRQESGYLIEEIGDVLLARFDGAEGSWFQKISSRFCSRQSFALEQLKAKQRKDPRFCAFVQEAESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQNTEEPTEREKVELAAECCREILHHVNQAVRDMEDLLRLKDYQRRLDLSHLRQSSDPMLSEFKNLDITKKKLVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTPTPDGKTMLRPVLRLTSAMTREVATDHKAFYVLFTWDQEAQIYELVAQTVSERKNWCALITETAGSLKVPAPASRPKPRPSPSSTREPLLSSSENGNGGRETSPADARTERILSDLLPFCRPGPEGQLAATALRKVLSLKQLLFPAEEDNGAGPPRDGDGVPGGGPLSPARTQEIQENLLSLEETMKQLEELEEEFCRLRPLLSQLGGNSVPQPGCT
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
5 (in isoform 3)Phosphorylation-22.7126270265
5 (in isoform 4)Phosphorylation-22.7126270265
6 (in isoform 3)Phosphorylation-34.9626270265
6 (in isoform 4)Phosphorylation-34.9626270265
8 (in isoform 3)Phosphorylation-10.1422199227
8 (in isoform 4)Phosphorylation-10.1422199227
9 (in isoform 3)Phosphorylation-21.0522199227
9 (in isoform 4)Phosphorylation-21.0522199227
10PhosphorylationDFARGAASPGPSRPG
CCCCCCCCCCCCCCC		29.8320058876
14PhosphorylationGAASPGPSRPGLVPV
CCCCCCCCCCCEEEE		57.9527794612
22PhosphorylationRPGLVPVSIIGAEDE
CCCEEEEEEECCCCC		11.4728464451
25 (in isoform 3)Phosphorylation-22.6518669648
25 (in isoform 4)Phosphorylation-22.6518669648
37PhosphorylationDFENELETNSEEQNS
HHHHHHHCCCHHHHH		57.5820873877
39PhosphorylationENELETNSEEQNSQF
HHHHHCCCHHHHHHH		50.3520873877
44PhosphorylationTNSEEQNSQFQSLEQ
CCCHHHHHHHHCHHH		31.8730175587
100PhosphorylationKKAFLDFYHSFLEKT
HHHHHHHHHHHHHHC		9.0220873877
102PhosphorylationAFLDFYHSFLEKTAV
HHHHHHHHHHHHCCE		21.8320873877
234AcetylationRHLGVRTKSGDKKSG
HHHCCCCCCCCCCCC		41.717467733
240PhosphorylationTKSGDKKSGRNFFRK
CCCCCCCCCCCCCHH		49.04-
255PhosphorylationKVMGNRRSDEPAKTK
HHHCCCCCCCCCCCH		42.9928985074
263UbiquitinationDEPAKTKKGLSSILD
CCCCCCHHHHHHHHH		71.02-
266PhosphorylationAKTKKGLSSILDAAR
CCCHHHHHHHHHHHH		24.8125850435
267PhosphorylationKTKKGLSSILDAARW
CCHHHHHHHHHHHHH		32.0125850435
278 (in isoform 3)Ubiquitination-29.35-
281 (in isoform 3)Phosphorylation-7.8027251275
282 (in isoform 3)Phosphorylation-29.7627251275
288UbiquitinationVPDFRHLKAEVDAEK
CCCHHHHHEEECCCC		36.05-
295AcetylationKAEVDAEKPGATDRK
HEEECCCCCCCCCCC		50.9325953088
303 (in isoform 3)Ubiquitination-36.59-
321PhosphorylationIGAPGQDTPGVSLHP
CCCCCCCCCCCCCCC		17.6626074081
325PhosphorylationGQDTPGVSLHPLSLD
CCCCCCCCCCCCCCC		27.2029255136
330PhosphorylationGVSLHPLSLDSPDRE
CCCCCCCCCCCCCCC		34.2829255136
333PhosphorylationLHPLSLDSPDREPGA
CCCCCCCCCCCCCCC		33.7129255136
349PhosphorylationAPLELGDSSPQGPMS
CCCCCCCCCCCCCCC		41.9626074081
350PhosphorylationPLELGDSSPQGPMSL
CCCCCCCCCCCCCCH		26.4426074081
356PhosphorylationSSPQGPMSLESLAPP
CCCCCCCCHHHCCCC		31.9226074081
365PhosphorylationESLAPPESTDEGAET
HHCCCCCCCCCCCCC		47.1026657352
372PhosphorylationSTDEGAETESPEPGD
CCCCCCCCCCCCCCC		41.0326657352
374PhosphorylationDEGAETESPEPGDEG
CCCCCCCCCCCCCCC		41.8224275569
409PhosphorylationVPPDTLHSLPKSQVK
CCCCHHHCCCHHHHC		49.8623186163
412UbiquitinationDTLHSLPKSQVKRQE
CHHHCCCHHHHCHHH		59.83-
427PhosphorylationVISELLVTEAAHVRM
HHHHHHHHHHHHHHH		21.6322210691
427 (in isoform 3)Ubiquitination-21.63-
477 (in isoform 2)Ubiquitination-38.5421890473
487PhosphorylationKRRQESGYLIEEIGD
HHHHHHCCCHHEEHH		17.4920098430
492UbiquitinationSGYLIEEIGDVLLAR
HCCCHHEEHHEEHHC		3.5621890473
510UbiquitinationAEGSWFQKISSRFCS
CCCCHHHHHHHHHHH		34.7721890473
510 (in isoform 1)Ubiquitination-34.7721890473
520PhosphorylationSRFCSRQSFALEQLK
HHHHHHHHHHHHHHH		16.0427067055
525 (in isoform 3)Ubiquitination-49.4621890473
527UbiquitinationSFALEQLKAKQRKDP
HHHHHHHHHHHCCCC		53.91-
534 (in isoform 2)Ubiquitination-33.9921890473
555UbiquitinationRCRRLQLKDMIPTEM
CCCHHCHHHHCCHHH		32.08-
567UbiquitinationTEMQRLTKYPLLLQS
HHHHHHHHHHHHHHH		49.8421906983
567 (in isoform 1)Ubiquitination-49.8421890473
568PhosphorylationEMQRLTKYPLLLQSI
HHHHHHHHHHHHHHC		8.2220873877
570 (in isoform 3)Ubiquitination-7.27-
574PhosphorylationKYPLLLQSIGQNTEE
HHHHHHHHCCCCCCC		28.7620873877
579PhosphorylationLQSIGQNTEEPTERE
HHHCCCCCCCCCHHH		33.5620873877
582 (in isoform 3)Ubiquitination-33.07-
583PhosphorylationGQNTEEPTEREKVEL
CCCCCCCCHHHHHHH		51.4520873877
587AcetylationEEPTEREKVELAAEC
CCCCHHHHHHHHHHH		47.4325953088
587UbiquitinationEEPTEREKVELAAEC
CCCCHHHHHHHHHHH		47.43-
602 (in isoform 3)Ubiquitination-3.85-
606 (in isoform 2)Ubiquitination-3.7221890473
609SulfoxidationVNQAVRDMEDLLRLK
HHHHHHCHHHHHHHH		2.7921406390
625PhosphorylationYQRRLDLSHLRQSSD
HHHHHCHHHHHHCCC		21.8320873877
630PhosphorylationDLSHLRQSSDPMLSE
CHHHHHHCCCCCHHH		30.2130108239
631PhosphorylationLSHLRQSSDPMLSEF
HHHHHHCCCCCHHHH		37.0823911959
634SulfoxidationLRQSSDPMLSEFKNL
HHHCCCCCHHHHCCC		8.4721406390
639UbiquitinationDPMLSEFKNLDITKK
CCCHHHHCCCCCCHH		53.1821906983
639 (in isoform 1)Ubiquitination-53.1821890473
640 (in isoform 3)Phosphorylation-48.5527251275
646 (in isoform 3)Phosphorylation-42.5627251275
647UbiquitinationNLDITKKKLVHEGPL
CCCCCHHHCCCCCCC		58.24-
654 (in isoform 3)Ubiquitination-12.03-
655PhosphorylationLVHEGPLTWRVTKDK
CCCCCCCEEEECCCC		17.8528857561
660 (in isoform 3)Ubiquitination-55.14-
661 (in isoform 3)Ubiquitination-34.48-
662 (in isoform 3)Ubiquitination-56.75-
668 (in isoform 2)Ubiquitination-4.9421890473
683UbiquitinationLLLQRQDERLLLKSH
HHHHHHCHHHHHHHH		36.5721890473
688UbiquitinationQDERLLLKSHSRTLT
HCHHHHHHHHCCCCC		46.20-
693PhosphorylationLLKSHSRTLTPTPDG
HHHHHCCCCCCCCCC		37.6922199227
695PhosphorylationKSHSRTLTPTPDGKT
HHHCCCCCCCCCCCC		25.2225850435
697PhosphorylationHSRTLTPTPDGKTML
HCCCCCCCCCCCCCH		28.8621815630
701UbiquitinationLTPTPDGKTMLRPVL
CCCCCCCCCCHHHHH		37.832189047
701 (in isoform 1)Ubiquitination-37.8321890473
703 (in isoform 3)Ubiquitination-3.22-
710 (in isoform 3)Phosphorylation-3.7727251275
716 (in isoform 3)Ubiquitination-24.2521890473
738PhosphorylationWDQEAQIYELVAQTV
CCHHHHHHHHHHHHH		7.3620098430
758PhosphorylationWCALITETAGSLKVP
EEEEEEECCCCCCCC		27.8927251275
761PhosphorylationLITETAGSLKVPAPA
EEEECCCCCCCCCCC		23.6624247654
763UbiquitinationTETAGSLKVPAPASR
EECCCCCCCCCCCCC		48.12-
769PhosphorylationLKVPAPASRPKPRPS
CCCCCCCCCCCCCCC		48.3229214152
776PhosphorylationSRPKPRPSPSSTREP
CCCCCCCCCCCCCCC		38.4025159151
776 (in isoform 3)Phosphorylation-38.4027251275
778PhosphorylationPKPRPSPSSTREPLL
CCCCCCCCCCCCCCC		48.9923403867
779PhosphorylationKPRPSPSSTREPLLS
CCCCCCCCCCCCCCC		34.5623403867
780PhosphorylationPRPSPSSTREPLLSS
CCCCCCCCCCCCCCC		43.3123403867
786PhosphorylationSTREPLLSSSENGNG
CCCCCCCCCCCCCCC		39.2329255136
787PhosphorylationTREPLLSSSENGNGG
CCCCCCCCCCCCCCC		41.4629255136
788PhosphorylationREPLLSSSENGNGGR
CCCCCCCCCCCCCCC		31.5328450419
791 (in isoform 3)Phosphorylation-30.0627251275
797PhosphorylationNGNGGRETSPADART
CCCCCCCCCHHHHHH		38.3526074081
798PhosphorylationGNGGRETSPADARTE
CCCCCCCCHHHHHHH		17.2121815630
801 (in isoform 3)Phosphorylation-39.7124719451
809PhosphorylationARTERILSDLLPFCR
HHHHHHHHHHCCCCC		24.6827251275
824 (in isoform 3)Phosphorylation-8.5527251275
833PhosphorylationTALRKVLSLKQLLFP
HHHHHHHCHHHHHCC		36.1924719451
835UbiquitinationLRKVLSLKQLLFPAE
HHHHHCHHHHHCCCC		35.21-
848 (in isoform 3)Phosphorylation-33.8624719451
863PhosphorylationVPGGGPLSPARTQEI
CCCCCCCCHHHHHHH		21.4629255136
867PhosphorylationGPLSPARTQEIQENL
CCCCHHHHHHHHHHH		32.4326074081
870 (in isoform 4)Phosphorylation-4.47-
872 (in isoform 4)Phosphorylation-56.35-
876PhosphorylationEIQENLLSLEETMKQ
HHHHHHHCHHHHHHH		36.5826074081
878 (in isoform 3)Phosphorylation-48.3124719451
880PhosphorylationNLLSLEETMKQLEEL
HHHCHHHHHHHHHHH		21.9426074081
891 (in isoform 3)Phosphorylation-3.1227251275
899PhosphorylationCRLRPLLSQLGGNSV
HHHHHHHHHHCCCCC		30.9220873877
905PhosphorylationLSQLGGNSVPQPGCT
HHHHCCCCCCCCCCC		38.1520873877
912PhosphorylationSVPQPGCT-------
CCCCCCCC-------		47.7820873877
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
738YPhosphorylationKinaseJAK2O60674
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARHG1_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 ARHG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARHG1_HUMANARHGEF1physical
14712228
GNA13_HUMANGNA13physical
14634662
GNA12_HUMANGNA12physical
14634662
PK3CA_HUMANPIK3CAphysical
12754211
CD44_HUMANCD44physical
12748184
RHOA_HUMANRHOAphysical
12748184
GNA13_HUMANGNA13physical
12681510
RAP1A_HUMANRAP1Aphysical
12581858
RASH_HUMANHRASphysical
12581858
GNA13_HUMANGNA13physical
9641916
SH3K1_HUMANSH3KBP1physical
15090612
CAP2_HUMANCAP2physical
22863883
CYFP1_HUMANCYFIP1physical
22863883
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 ARHG1_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-863, 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-863, AND MASSSPECTROMETRY.
"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, PHOSPHORYLATION AT TYR-738, AND MUTAGENESIS OF TYR-487 ANDTYR-738.

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