Search Results
Overview
| Uniprot ID | P50440 |
|---|---|
| Protein Name | Glycine amidinotransferase, mitochondrial |
| Gene Name | GATM |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 102 | VKANTYEKYWPFYQK |
| 109 | KYWPFYQKQGGHYFP |
| 117 | QGGHYFPKDHLKKAV |
| 122 | FPKDHLKKAVAEIEE |
| 152 | DPIDWSLKYKTPDFE |
| 154 | IDWSLKYKTPDFEST |
| 201 | RAYRSIIKDYFHRGA |
| 209 | DYFHRGAKWTTAPKP |
| 237 | HSVEDRHKLAAQGKF |
| 332 | HQIDLFKKAGWTIIT |
| 381 | ANEVPIQKMFEKLGI |
| 385 | PIQKMFEKLGITTIK |
| 392 | KLGITTIKVNIRNAN |
| 55 | NSCAADDKATEPLPK |
| 96 | PPFTIEVKANTYEKY |
Function
Transamidinase that catalyzes the transfer of the amidino group of L-arginine onto the amino moiety of acceptor metabolites such as glycine, beta-alanine, gamma-aminobutyric acid (GABA) and taurine yielding the corresponding guanidine derivatives (PubMed:16820567, PubMed:27233232, PubMed:36543883, PubMed:3800397). Catalyzes the rate-limiting step of creatine biosynthesis, namely the transfer of the amidino group from L-arginine to glycine to generate guanidinoacetate, which is then methylated by GAMT to form creatine. Provides creatine as a source for ATP generation in tissues with high energy demands, in particular skeletal muscle, heart and brain (Probable) (PubMed:27233232, PubMed:36543883, PubMed:3800397, PubMed:9266688)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0005758 | mitochondrial intermembrane space |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0015067 | amidinotransferase activity |
| Molecular Function | GO:0015068 | glycine amidinotransferase activity |
| Biological Process | GO:0006601 | creatine biosynthetic process |
| Biological Process | GO:0006600 | creatine metabolic process |
| Biological Process | GO:0007611 | learning or memory |
| Biological Process | GO:0014889 | muscle atrophy |
| Biological Process | GO:0120162 | positive regulation of cold-induced thermogenesis |
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] 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.
[3] 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.