Search Results

Overview

Uniprot IDP14866
Protein NameHeterogeneous nuclear ribonucleoprotein L
Gene NameHNRNPL
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
248 VQSAQRAKASLNGAD
269 TLKIEYAKPTRLNVF
302 DPGSNPNKRQRQPPL
34 RRSGAMVKMAAAGGG
418 KVKFMKSKPGAAMVE
455 KLNVCVSKQPAIMPG
493 STPEQAAKNRIQHPS
538 SVKVFSGKSERSSSG
59 SEGGRAPKRLKTDNA
62 GRAPKRLKTDNAGDQ

Function

Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements (PubMed:11809897, PubMed:22570490, PubMed:24164894, PubMed:25623890, PubMed:26051023). Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts (PubMed:2687284). Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter (PubMed:11809897). As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841). Regulates alternative splicing of a core group of genes involved in neuronal differentiation, likely by mediating H3K36me3-coupled transcription elongation and co-transcriptional RNA processing via interaction with CHD8

Protein Sequence

10 MSRRLLPRAE 20 KRRRRLEQRQ 30 QPDEQRRRSG 40 AMVKMAAAGG 50 GGGGGRYYGG 60 GSEGGRAPKR 70 LKTDNAGDQH 80 GGGGGGGGGA 90 GAAGGGGGGE 100 NYDDPHKTPA 110 SPVVHIRGLI 120 DGVVEADLVE 130 ALQEFGPISY 140 VVVMPKKRQA 150 LVEFEDVLGA 160 CNAVNYAADN 170 QIYIAGHPAF 180 VNYSTSQKIS 190 RPGDSDDSRS 200 VNSVLLFTIL 210 NPIYSITTDV 220 LYTICNPCGP 230 VQRIVIFRKN 240 GVQAMVEFDS 250 VQSAQRAKAS 260 LNGADIYSGC 270 CTLKIEYAKP 280 TRLNVFKNDQ 290 DTWDYTNPNL 300 SGQGDPGSNP 310 NKRQRQPPLL 320 GDHPAEYGGP 330 HGGYHSHYHD 340 EGYGPPPPHY 350 EGRRMGPPVG 360 GHRRGPSRYG 370 PQYGHPPPPP 380 PPPEYGPHAD 390 SPVLMVYGLD 400 QSKMNCDRVF 410 NVFCLYGNVE 420 KVKFMKSKPG 430 AAMVEMADGY 440 AVDRAITHLN 450 NNFMFGQKLN 460 VCVSKQPAIM 470 PGQSYGLEDG 480 SCSYKDFSES 490 RNNRFSTPEQ 500 AAKNRIQHPS 510 NVLHFFNAPL 520 EVTEENFFEI 530 CDELGVKRPS 540 SVKVFSGKSE 550 RSSSGLLEWE 560 SKSDALETLG 570 FLNHYQMKNP 580 NGPYPYTLKL CFSTAQHAS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0045120 pronucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Cellular Component GO:0035770 ribonucleoprotein granule
Cellular Component GO:0045202 synapse
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0097157 pre-mRNA intronic binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0000976 transcription cis-regulatory region binding
Biological Process GO:0006397 mRNA processing
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0000381 regulation of alternative mRNA splicing, via spliceosome
Biological Process GO:0043484 regulation of RNA splicing
Biological Process GO:0006396 RNA processing

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] 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] 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.

[8] 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.

[9] 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.

[10] 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.