Search Results

Overview

Uniprot IDP52565
Protein NameRho GDP-dissociation inhibitor 1
Gene NameARHGDIA
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
105 KKQSFVLKEGVEYRI
127 REIVSGMKYIQHTYR
141 RKGVKIDKTDYMVGS
178 ARGSYSIKSRFTDDD
52 DESLRKYKEALLGRV
99 GDLESFKKQSFVLKE

Function

Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1

Protein Sequence

10 MAEQEPTAEQ 20 LAQIAAENEE 30 DEHSVNYKPP 40 AQKSIQEIQE 50 LDKDDESLRK 60 YKEALLGRVA 70 VSADPNVPNV 80 VVTGLTLVCS 90 SAPGPLELDL 100 TGDLESFKKQ 110 SFVLKEGVEY 120 RIKISFRVNR 130 EIVSGMKYIQ 140 HTYRKGVKID 150 KTDYMVGSYG 160 PRAEEYEFLT 170 PVEEAPKGML 180 ARGSYSIKSR 190 FTDDDKTDHL 200 SWEWNLTIKK DWKD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0001772 immunological synapse
Cellular Component GO:0016020 membrane
Cellular Component GO:0005634 nucleus
Cellular Component GO:0098685 Schaffer collateral - CA1 synapse
Molecular Function GO:0005096 GTPase activator activity
Molecular Function GO:0005094 Rho GDP-dissociation inhibitor activity
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0035023 regulation of Rho protein signal transduction
Biological Process GO:0098693 regulation of synaptic vesicle cycle
Biological Process GO:0007266 Rho protein signal transduction
Biological Process GO:0071526 semaphorin-plexin signaling pathway

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[5] 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.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[8] 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.