Search Results
Overview
| Uniprot ID | Q8N6T3 |
|---|---|
| Protein Name | ADP-ribosylation factor GTPase-activating protein 1 |
| Gene Name | ARFGAP1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 114 | AAALFRDKVVALAEG |
| 194 | GNTPPPQKKEDDFLN |
| 195 | NTPPPQKKEDDFLNN |
| 226 | SRFASAAKEGATKFG |
| 231 | AAKEGATKFGSQASQ |
| 278 | GVSQLASKVQGVGSK |
| 285 | KVQGVGSKGWRDVTT |
| 342 | AEPTKTRKSPSSDSW |
Function
GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0015031 | protein transport |
| Biological Process | GO:0032012 | regulation of ARF protein signal transduction |
| Biological Process | GO:0030100 | regulation of endocytosis |
| Biological Process | GO:0016192 | vesicle-mediated transport |
| Cellular Component | GO:0000139 | Golgi membrane |
| Cellular Component | GO:0045202 | synapse |
| Molecular Function | GO:0005096 | GTPase activator activity |
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] 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.
[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.