Search Results
Overview
| Uniprot ID | P22626 |
|---|---|
| Protein Name | Heterogeneous nuclear ribonucleoproteins A2/B1 |
| Gene Name | HNRNPA2B1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 104 | VAREESGKPGAHVTV |
| 112 | PGAHVTVKKLFVGGI |
| 113 | GAHVTVKKLFVGGIK |
| 120 | KLFVGGIKEDTEEHH |
| 173 | VDKIVLQKYHTINGH |
| 46 | NYYEQWGKLTDCVVM |
| 59 | VMRDPASKRSRGFGF |
Function
Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs (PubMed:19099192). Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (PubMed:10567417). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts (PubMed:26321680). Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (PubMed:26321680). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Also plays a role in the activation of the innate immune response (PubMed:31320558). Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6 (PubMed:31320558). In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (PubMed:31320558)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Molecular Function | GO:1990247 | N6-methyladenosine-containing RNA reader activity |
| Molecular Function | GO:0003730 | mRNA 3'-UTR binding |
| Cellular Component | GO:0015030 | Cajal body |
| Cellular Component | GO:0071013 | catalytic step 2 spliceosome |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0016363 | nuclear matrix |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Cellular Component | GO:0005681 | spliceosomal complex |
| Molecular Function | GO:0070182 | DNA polymerase binding |
| Molecular Function | GO:0098505 | G-rich strand telomeric DNA binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0035198 | miRNA binding |
| Molecular Function | GO:0140693 | molecular condensate scaffold activity |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0043047 | single-stranded telomeric DNA binding |
| Biological Process | GO:0032392 | DNA geometric change |
| Biological Process | GO:1990428 | miRNA transport |
| Biological Process | GO:0006406 | mRNA export from nucleus |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0051028 | mRNA transport |
| Biological Process | GO:1904358 | positive regulation of telomere maintenance via telomere lengthening |
| Biological Process | GO:0031053 | primary miRNA processing |
| Biological Process | GO:0050658 | RNA transport |
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] 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.
[5] 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.
[6] Hu J, Jin Z, Gao Y, Liu Q, Yu Y et al.. Global Profiling of Lactylation Proteomics and Specific Lactylated Site Validation in Rheumatoid Arthritis Patients.. J Proteome Res 24(4):1732-1744. 2025 Apr 4. PMID: 40112136.
[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.