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Overview

Uniprot IDQ92888
Protein NameRho guanine nucleotide exchange factor 1
Gene NameARHGEF1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
263 DEPAKTKKGLSSILD
288 VPDFRHLKAEVDAEK
646 KNLDITKKKLVHEGP

Function

Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits (PubMed:9641915, PubMed:9641916). Acts as a GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase (PubMed:30521495, PubMed:8810315, PubMed:9641915, PubMed:9641916). Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain (PubMed:9641916). This GEF activity is inhibited by binding to activated GNA12 (PubMed:9641916). Mediates angiotensin-2-induced RhoA activation (PubMed:20098430). In lymphoid follicles, may trigger activation of GNA13 as part of S1PR2-dependent signaling pathway that leads to inhibition of germinal center (GC) B cell growth and migration outside the GC niche

Protein Sequence

10 MEDFARGAAS 20 PGPSRPGLVP 30 VSIIGAEDED 40 FENELETNSE 50 EQNSQFQSLE 60 QVKRRPAHLM 70 ALLQHVALQF 80 EPGPLLCCLH 90 ADMLGSLGPK 100 EAKKAFLDFY 110 HSFLEKTAVL 120 RVPVPPNVAF 130 ELDRTRADLI 140 SEDVQRRFVQ 150 EVVQSQQVAV 160 GRQLEDFRSK 170 RLMGMTPWEQ 180 ELAQLEAWVG 190 RDRASYEARE 200 RHVAERLLMH 210 LEEMQHTIST 220 DEEKSAAVVN 230 AIGLYMRHLG 240 VRTKSGDKKS 250 GRNFFRKKVM 260 GNRRSDEPAK 270 TKKGLSSILD 280 AARWNRGEPQ 290 VPDFRHLKAE 300 VDAEKPGATD 310 RKGGVGMPSR 320 DRNIGAPGQD 330 TPGVSLHPLS 340 LDSPDREPGA 350 DAPLELGDSS 360 PQGPMSLESL 370 APPESTDEGA 380 ETESPEPGDE 390 GEPGRSGLEL 400 EPEEPPGWRE 410 LVPPDTLHSL 420 PKSQVKRQEV 430 ISELLVTEAA 440 HVRMLRVLHD 450 LFFQPMAECL 460 FFPLEELQNI 470 FPSLDELIEV 480 HSLFLDRLMK 490 RRQESGYLIE 500 EIGDVLLARF 510 DGAEGSWFQK 520 ISSRFCSRQS 530 FALEQLKAKQ 540 RKDPRFCAFV 550 QEAESRPRCR 560 RLQLKDMIPT 570 EMQRLTKYPL 580 LLQSIGQNTE 590 EPTEREKVEL 600 AAECCREILH 610 HVNQAVRDME 620 DLLRLKDYQR 630 RLDLSHLRQS 640 SDPMLSEFKN 650 LDITKKKLVH 660 EGPLTWRVTK 670 DKAVEVHVLL 680 LDDLLLLLQR 690 QDERLLLKSH 700 SRTLTPTPDG 710 KTMLRPVLRL 720 TSAMTREVAT 730 DHKAFYVLFT 740 WDQEAQIYEL 750 VAQTVSERKN 760 WCALITETAG 770 SLKVPAPASR 780 PKPRPSPSST 790 REPLLSSSEN 800 GNGGRETSPA 810 DARTERILSD 820 LLPFCRPGPE 830 GQLAATALRK 840 VLSLKQLLFP 850 AEEDNGAGPP 860 RDGDGVPGGG 870 PLSPARTQEI 880 QENLLSLEET 890 MKQLEELEEE 900 FCRLRPLLSQ 910 LGGNSVPQPG CT

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0001664 G protein-coupled receptor binding
Molecular Function GO:0005096 GTPase activator activity
Molecular Function GO:0005085 guanyl-nucleotide exchange factor activity
Molecular Function GO:0003723 RNA binding
Biological Process GO:0007186 G protein-coupled receptor signaling pathway
Biological Process GO:0051056 regulation of small GTPase mediated signal transduction
Biological Process GO:0007266 Rho protein signal transduction
Biological Process GO:0160221 Rho-activating G protein-coupled receptor signaling pathway

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.