Search Results
Overview
| Uniprot ID | Q99729 |
|---|---|
| Protein Name | Heterogeneous nuclear ribonucleoprotein A/B |
| Gene Name | HNRNPAB |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 125 | KDAASVEKVLDQKEH |
| 130 | VEKVLDQKEHRLDGR |
| 215 | VKKVLEKKFHTVSGS |
| 223 | FHTVSGSKCEIKVAQ |
| 232 | EIKVAQPKEVYQQQQ |
| 86 | DTSKKDLKDYFTKFG |
| 91 | DLKDYFTKFGEVVDC |
Function
Binds single-stranded RNA. Has a high affinity for G-rich and U-rich regions of hnRNA. Also binds to APOB mRNA transcripts around the RNA editing site
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0010468 | regulation of gene expression |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0030425 | dendrite |
| Cellular Component | GO:0071598 | neuronal ribonucleoprotein granule |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Cellular Component | GO:0090575 | RNA polymerase II transcription regulator complex |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:1990837 | sequence-specific double-stranded DNA binding |
| Biological Process | GO:0071230 | cellular response to amino acid stimulus |
| Biological Process | GO:0141166 | chromosomal 5-methylcytosine DNA demethylation pathway |
| Biological Process | GO:0001837 | epithelial to mesenchymal transition |
| Biological Process | GO:0016556 | mRNA modification |
| Biological Process | GO:2000623 | negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0060341 | regulation of cellular localization |
| Biological Process | GO:1904580 | regulation of intracellular mRNA localization |
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.