Search Results

Overview

Uniprot ID	P09651
Protein Name	Heterogeneous nuclear ribonucleoprotein A1
Gene Name	HNRNPA1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
105	PGAHLTVKKIFVGGI
106	GAHLTVKKIFVGGIK
166	VDKIVIQKYHTVNGH
3	*****MSKSESPKEP
350	GGGQYFAKPRNQGGY
8	MSKSESPKEPEQLRK

Function

Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection (PubMed:17371836). 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). Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1 (PubMed:31498791). May bind to specific miRNA hairpins (PubMed:28431233)

Protein Sequence

10 MSKSESPKEP 20 EQLRKLFIGG 30 LSFETTDESL 40 RSHFEQWGTL 50 TDCVVMRDPN 60 TKRSRGFGFV 70 TYATVEEVDA 80 AMNARPHKVD 90 GRVVEPKRAV 100 SREDSQRPGA 110 HLTVKKIFVG 120 GIKEDTEEHH 130 LRDYFEQYGK 140 IEVIEIMTDR 150 GSGKKRGFAF 160 VTFDDHDSVD 170 KIVIQKYHTV 180 NGHNCEVRKA 190 LSKQEMASAS 200 SSQRGRSGSG 210 NFGGGRGGGF 220 GGNDNFGRGG 230 NFSGRGGFGG 240 SRGGGGYGGS 250 GDGYNGFGND 260 GGYGGGGPGY 270 SGGSRGYGSG 280 GQGYGNQGSG 290 YGGSGSYDSY 300 NNGGGGGFGG 310 GSGSNFGGGG 320 SYNDFGNYNN 330 QSSNFGPMKG 340 GNFGGRSSGP 350 YGGGGQYFAK 360 PRNQGGYGGS 370 SSSSSYGSGR RF

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0071013	catalytic step 2 spliceosome
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0070062	extracellular exosome
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:1990904	ribonucleoprotein complex
Cellular Component	GO:0005681	spliceosomal complex
Cellular Component	GO:0045202	synapse
Molecular Function	GO:0003677	DNA 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:0003730	mRNA 3'-UTR binding
Molecular Function	GO:0036002	pre-mRNA binding
Molecular Function	GO:0019904	protein domain specific binding
Molecular Function	GO:0003723	RNA binding
Molecular Function	GO:0003697	single-stranded DNA binding
Molecular Function	GO:0003727	single-stranded RNA binding
Molecular Function	GO:0061752	telomeric repeat-containing RNA binding
Biological Process	GO:0042149	cellular response to glucose starvation
Biological Process	GO:1903936	cellular response to sodium arsenite
Biological Process	GO:0051170	import into nucleus
Biological Process	GO:0000398	mRNA splicing, via spliceosome
Biological Process	GO:0051028	mRNA transport
Biological Process	GO:0032211	negative regulation of telomere maintenance via telomerase
Biological Process	GO:0051168	nuclear export
Biological Process	GO:0032212	positive regulation of telomere maintenance via telomerase
Biological Process	GO:0000381	regulation of alternative mRNA splicing, via spliceosome
Biological Process	GO:0043484	regulation of RNA splicing
Biological Process	GO:0006405	RNA export from nucleus

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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.

[11] 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.