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Protein Page:
ARHGEF1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
ARHGEF1 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. Interacts with RHOA, GNA12 and GNA13. Homooligomerizes through the coiled coil region. May interact with CCPG1. Interacts with CTNNAL1. Ubiquitously expressed. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Guanine nucleotide exchange factor, Rac/Rho; Motility/polarity/chemotaxis
Cellular Component: cytoplasm; plasma membrane; cytosol
Molecular Function: protein binding; Rho guanyl-nucleotide exchange factor activity; phospholipid binding; GTPase activator activity
Biological Process: cell proliferation; nerve growth factor receptor signaling pathway; regulation of Rho protein signal transduction; negative regulation of axonogenesis; regulation of axonogenesis; Rho protein signal transduction
Reference #:  Q92888 (UniProtKB)
Alt. Names/Synonyms: 115 kDa guanine nucleotide exchange factor; 115-kD protein; ARHG1; ARHGEF1; GEF1; LBCL2; LSC; Lsc homolog; p115-RhoGEF; p115RhoGEF; Rho guanine nucleotide exchange factor (GEF) 1; Rho guanine nucleotide exchange factor 1; Sub1.5
Gene Symbols: ARHGEF1
Molecular weight: 102,435 Da
Basal Isoelectric point: 5.47  Predict pI for various phosphorylation states
CST Pathways:  Regulation of Actin Dynamics  |  Regulation of Microtubule Dynamics
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ARHGEF1
Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
activation: Y738‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

► Hide Isoforms 		 
0 2 S10-p DFARGAAsPGPSRPG
0 1 K234-a RHLGVRTkSGDKKsG
0 6 S240-p TkSGDKKsGRNFFRK
0 2 K263-u DEPAKTKkGLSSILD
0 1 D292-ca RHLKAEVdAEKPGAT
0 1 D332-ca SLHPLSLdSPDREPG
0 1 - gap
0 1 - gap
0 6 - gap
0 1 - gap
0 1 - gap
0 1 - gap
0 5 - gap
0 2 - gap
0 6 S374 DEGAETESPEPGDEG
1 0 Y487-p KRRQESGyLIEEIGD
0 11 K510-u AEGSWFQkISSRFCS
0 1 K567-u TEMQRLTkYPLLLQS
0 2 S631-p LSHLRQSsDPMLSEF
0 1 K639-u DPMLSEFkNLDITKK
0 2 T695-p KSHSRTLtPTPDGkT
0 1 K701-u LtPTPDGkTMLRPVL
1 0 Y738-p WDQEAQIyELVAQTV
0 2 S786-p STREPLLsSsENGNG
0 1 S788-p REPLLsSsENGNGGR
0 1 S798-p GNGGRETsPADARTE
0 5 S863-p VPGGGPLsPARTQEI
0 4 V906 SQLGGNSVPQPGCT_
0 1 - gap
  ARHGEF1 iso3  
S70 DFARGAASPGPSRPG
K294 RHLGVRTKSGDKKSG
S300 TKSGDKKSGRNFFRK
K323 DEPAKTKKGLSSILD
D352 RHLKAEVDAEKPGAT
D392 SLHPLSLDSPDREPG
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
T592-p PPCPLPPtPRLAPAS
  mouse

► Hide Isoforms 		 
- gap
K232 RHLGVRTKSGDKKSG
S238 TKSGDKKSGRNFFRK
K261 DEPPKTKKGLSSILD
D290 RHLKVEADAEKPGPA
D330 SLHPLSTDSVDSREP
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S373 EDNGETESPEPGDDG
Y486 KRRQESGYLIEEIGD
K509 AEGSWFQKISSRFCS
K566 TEMQRLTKYPLLLQS
S630 LTHLRQSSDPMLSEF
K638 DPMLSEFKNLDITKK
T694 KSHSRTLTPTPDGKT
K700 LTPTPDGKTMLRPVL
Y737 WDQEAQIYELVAQTS
S785 SIREPLLSSSENGTG
S787 REPLLSSSENGTGGA
A797 GTGGAEMAPADARTE
G862 VPGGRAPGPVHTQEI
S905-p SQLGGTLsPNLAAPE
- gap
  ARHGEF1 iso2  
- gap
K232 RHLGVRTKSGDKKSG
S238 TKSGDKKSGRNFFRK
K261 DEPPKTKKGLSSILD
D290 RHLKVEADEKPGPAD
D329 SLHPLSTDSVDSREP
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S372 EDNGETESPEPGDDG
Y485 KRRQESGYLIEEIGD
K508 AEGSWFQKISSRFCS
K565 TEMQRLTKYPLLLQS
S629 LTHLRQSSDPMLSEF
K637 DPMLSEFKNLDITKK
T693 KSHSRTLTPTPDGKT
K699 LTPTPDGKTMLRPVL
Y736 WDQEAQIYELVAQTS
S784 SIREPLLSSSENGTG
S786 REPLLSSSENGTGGA
A796 GTGGAEMAPADARTE
G861 VPGGRAPGPVHTQEI
S904 SQLGGTLSPNLAAPE
- gap
  ARHGEF1 iso5  
- gap
K232 RHLGVRTKSGDKKSG
S238 TKSGDKKSGRNFFRK
K261 DEPPKTKKGLSSILD
D290 RHLKVEADEKPGPAD
D329 SLHPLSTDSVDSREP
S384-p LSGRLGRsEsLRVsD
S386-p GRLGRsEsLRVsDRR
S390-p RsEsLRVsDRRRPsR
S396-p VsDRRRPsRGsLGAK
S399-p RRRPsRGsLGAKGRG
S410-p KGRGGGRsRsDVDMD
S412-p RGGGRsRsDVDMDPG
S420-p DVDMDPGsATAVLGP
T432-p LGPTRRAtPEPGDDG
Y545 KRRQESGYLIEEIGD
K568 AEGSWFQKISSRFCS
K625 TEMQRLTKYPLLLQS
S689 LTHLRQSSDPMLSEF
K697 DPMLSEFKNLDITKK
T753 KSHSRTLTPTPDGKT
K759 LTPTPDGKTMLRPVL
Y796 WDQEAQIYELVAQTS
S844 SIREPLLSSSENGTG
S846 REPLLSSSENGTGGA
A856 GTGGAEMAPADARTE
G921 VPGGRAPGPVHTQEI
S964-p SQLGGTLsPNLAAPE
- gap
  rat

 
- gap
K232 RHLGVRTKSGDKKSG
S238 TKSGDKKSGRNFFRK
K261 DEPPKTKKGLSSILD
D290 RHLKVEVDEKPGPAD
D329 SLHPLSVDSLDSREP
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S372 EDNGETESPEPGDDG
Y485-p KRRQESGyLIEEIGD
K508 AEGSWFQKISSRFCS
K565 TEMQRLTKYPLLLQS
N629 LTHLRQSNDPMLSEF
K637 DPMLSEFKNLDITKK
T693 SHTSRTLTPTPDGKT
K699 LTPTPDGKTMLRPVL
Y736-p WDQEAQIyELVAQTS
S784 STREPLLSSSENGTG
S786 REPLLSSSENGTGGT
A796 GTGGTEAAPADARTE
G861 VPGGGAPGPTHTQEV
S904 SQLGEILSPNLAAPE
- gap
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