Search Results
Overview
| Uniprot ID | P17096 |
|---|---|
| Protein Name | High mobility group protein HMG-I/HMG-Y |
| Gene Name | HMGA1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 15 | SSQPLASKQEKDGTE |
| 31 | RGRGRPRKQPPVSPG |
| 46 | TALVGSQKEPSEVPT |
| 55 | PSEVPTPKRPRGRPK |
| 7 | *MSESSSKSSQPLAS |
| 74 | KGAAKTRKTTTTPGR |
Function
HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0031965 | nuclear membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0090575 | RNA polymerase II transcription regulator complex |
| Cellular Component | GO:0035985 | senescence-associated heterochromatin focus |
| Cellular Component | GO:0005667 | transcription regulator complex |
| Molecular Function | GO:0051575 | 5'-deoxyribose-5-phosphate lyase activity |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0000987 | cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0008301 | DNA binding, bending |
| Molecular Function | GO:0003906 | DNA-(apurinic or apyrimidinic site) endonuclease activity |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0003680 | minor groove of adenine-thymine-rich DNA binding |
| Molecular Function | GO:0060090 | molecular adaptor activity |
| Molecular Function | GO:0140677 | molecular function activator activity |
| Molecular Function | GO:0042974 | nuclear retinoic acid receptor binding |
| Molecular Function | GO:0046965 | nuclear retinoid X receptor binding |
| Molecular Function | GO:0042975 | peroxisome proliferator activated receptor binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0030527 | structural constituent of chromatin |
| Molecular Function | GO:0003713 | transcription coactivator activity |
| Molecular Function | GO:0003712 | transcription coregulator activity |
| Molecular Function | GO:0001221 | transcription coregulator binding |
| Biological Process | GO:0006284 | base-excision repair |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0035556 | intracellular signal transduction |
| Biological Process | GO:0008285 | negative regulation of cell population proliferation |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0006337 | nucleosome disassembly |
| Biological Process | GO:0090402 | oncogene-induced cell senescence |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[5] 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.
[6] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[7] 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.
[8] 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.
[9] 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.