Search Results
Overview
| Uniprot ID | P06737 |
|---|---|
| Protein Name | Glycogen phosphorylase, liver form |
| Gene Name | PYGL |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 10 | KPLTDQEKRRQISIR |
| 170 | EYGIFNQKIRDGWQV |
| 206 | LPVHFYGKVEHTNTG |
| 29 | VENVAELKKSFNRHL |
| 290 | NDNFFEGKELRLKQE |
| 3 | *****MAKPLTDQEK |
| 30 | ENVAELKKSFNRHLH |
| 316 | IRRFKASKFGSTRGA |
| 364 | IEKLPWSKAWELTQK |
| 410 | IIYEINQKHLDRIVA |
| 42 | HLHFTLVKDRNVATT |
| 421 | RIVALFPKDVDRLRR |
| 438 | LIEEEGSKRINMAHL |
| 465 | KIHSDIVKTKVFKDF |
| 470 | IVKTKVFKDFSELEP |
| 483 | EPDKFQNKTNGITPR |
| 521 | KDLSQLTKLHSFLGD |
| 545 | VKQENKLKFSQFLET |
| 555 | QFLETEYKVKINPSS |
| 557 | LETEYKVKINPSSMF |
| 609 | RTVIIGGKAAPGYHM |
| 618 | APGYHMAKMIIKLIT |
| 640 | NDPMVGSKLKVIFLE |
| 642 | PMVGSKLKVIFLENY |
| 724 | DDVAALDKKGYEAKE |
| 725 | DVAALDKKGYEAKEY |
| 730 | DKKGYEAKEYYEALP |
| 78 | TQQHYYDKCPKRVYY |
| 783 | ADYEAYVKCQDKVSQ |
| 804 | AWNTMVLKNIAASGK |
| 811 | KNIAASGKFSSDRTI |
| 819 | FSSDRTIKEYAQNIW |
| 843 | SLSNESNKVNGN*** |
Function
Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:1904813 | ficolin-1-rich granule lumen |
| Cellular Component | GO:0034774 | secretory granule lumen |
| Molecular Function | GO:0016208 | AMP binding |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0032052 | bile acid binding |
| Molecular Function | GO:0005536 | D-glucose binding |
| Molecular Function | GO:0008184 | glycogen phosphorylase activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0002060 | purine nucleobase binding |
| Molecular Function | GO:0030170 | pyridoxal phosphate binding |
| Molecular Function | GO:0019842 | vitamin binding |
| Biological Process | GO:0042593 | glucose homeostasis |
| Biological Process | GO:0005980 | glycogen catabolic process |
| Biological Process | GO:0005977 | glycogen metabolic process |
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.
[4] 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.
[5] 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.