Search Results

Overview

Uniprot IDP52597
Protein NameHeterogeneous nuclear ribonucleoprotein F
Gene NameHNRNPF
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
150 LPVDPEGKITGEAFV
200 SYSDPPLKFMSVQRP
224 RRYIGIVKQAGLERM
87 HRYIEVFKSHRTEMD

Function

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. Plays a role in the regulation of alternative splicing events. Binds G-rich sequences in pre-mRNAs and keeps target RNA in an unfolded state

Protein Sequence

10 MMLGPEGGEG 20 FVVKLRGLPW 30 SCSVEDVQNF 40 LSDCTIHDGA 50 AGVHFIYTRE 60 GRQSGEAFVE 70 LGSEDDVKMA 80 LKKDRESMGH 90 RYIEVFKSHR 100 TEMDWVLKHS 110 GPNSADSAND 120 GFVRLRGLPF 130 GCTKEEIVQF 140 FSGLEIVPNG 150 ITLPVDPEGK 160 ITGEAFVQFA 170 SQELAEKALG 180 KHKERIGHRY 190 IEVFKSSQEE 200 VRSYSDPPLK 210 FMSVQRPGPY 220 DRPGTARRYI 230 GIVKQAGLER 240 MRPGAYSTGY 250 GGYEEYSGLS 260 DGYGFTTDLF 270 GRDLSYCLSG 280 MYDHRYGDSE 290 FTVQSTTGHC 300 VHMRGLPYKA 310 TENDIYNFFS 320 PLNPVRVHIE 330 IGPDGRVTGE 340 ADVEFATHEE 350 AVAAMSKDRA 360 NMQHRYIELF 370 LNSTTGASNG 380 AYSSQVMQGM 390 GVSAAQATYS 400 GLESQSVSGC 410 YGAGYSGQNS MGGYD

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:0005886 plasma membrane
Cellular Component GO:1990904 ribonucleoprotein complex
Cellular Component GO:0045202 synapse
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003727 single-stranded 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] 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.

[4] 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.

[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.