Search Results

Overview

Uniprot IDP31943
Protein NameHeterogeneous nuclear ribonucleoprotein H
Gene NameHNRNPH1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
185 HRYIEIFKSSRAEVR
200 THYDPPRKLMAMQRP
349 VAAMSKDKANMQHRY

Function

This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with CUGBP1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds poly(RG)

Protein Sequence

10 MMLGTEGGEG 20 FVVKVRGLPW 30 SCSADEVQRF 40 FSDCKIQNGA 50 QGIRFIYTRE 60 GRPSGEAFVE 70 LESEDEVKLA 80 LKKDRETMGH 90 RYVEVFKSNN 100 VEMDWVLKHT 110 GPNSPDTAND 120 GFVRLRGLPF 130 GCSKEEIVQF 140 FSGLEIVPNG 150 ITLPVDFQGR 160 STGEAFVQFA 170 SQEIAEKALK 180 KHKERIGHRY 190 IEIFKSSRAE 200 VRTHYDPPRK 210 LMAMQRPGPY 220 DRPGAGRGYN 230 SIGRGAGFER 240 MRRGAYGGGY 250 GGYDDYNGYN 260 DGYGFGSDRF 270 GRDLNYCFSG 280 MSDHRYGDGG 290 STFQSTTGHC 300 VHMRGLPYRA 310 TENDIYNFFS 320 PLNPVRVHIE 330 IGPDGRVTGE 340 ADVEFATHED 350 AVAAMSKDKA 360 NMQHRYVELF 370 LNSTAGASGG 380 AYEHRYVELF 390 LNSTAGASGG 400 AYGSQMMGGM 410 GLSNQSSYGG 420 PASQQLSGGY 430 GGGYGGQSSM 440 SGYDQVLQEN SSDFQSNIA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0008266 poly(U) RNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0000398 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] 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.

[4] 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.

[5] 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.

[6] 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.