Search Results

Overview

Uniprot IDP26368
Protein NameSplicing factor U2AF 65 kDa subunit
Gene NameU2AF2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
15 ERQLNENKQERDKEN
292 LKAFNLVKDSATGLS
431 VEVPGCGKIFVEFTS
462 ANRVVVTKYCDPDSY
70 KPLTRGAKEEHGGLI
90 EKKKKVRKYWDVPPP

Function

Plays a role in pre-mRNA splicing and 3'-end processing (PubMed:17024186). By recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA, may couple transcription to splicing (PubMed:21536736). Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10. Positively regulates pre-mRNA 3'-end processing by recruiting the CFIm complex to cleavage and polyadenylation signals (PubMed:17024186)

Protein Sequence

10 MSDFDEFERQ 20 LNENKQERDK 30 ENRHRKRSHS 40 RSRSRDRKRR 50 SRSRDRRNRD 60 QRSASRDRRR 70 RSKPLTRGAK 80 EEHGGLIRSP 90 RHEKKKKVRK 100 YWDVPPPGFE 110 HITPMQYKAM 120 QAAGQIPATA 130 LLPTMTPDGL 140 AVTPTPVPVV 150 GSQMTRQARR 160 LYVGNIPFGI 170 TEEAMMDFFN 180 AQMRLGGLTQ 190 APGNPVLAVQ 200 INQDKNFAFL 210 EFRSVDETTQ 220 AMAFDGIIFQ 230 GQSLKIRRPH 240 DYQPLPGMSE 250 NPSVYVPGVV 260 STVVPDSAHK 270 LFIGGLPNYL 280 NDDQVKELLT 290 SFGPLKAFNL 300 VKDSATGLSK 310 GYAFCEYVDI 320 NVTDQAIAGL 330 NGMQLGDKKL 340 LVQRASVGAK 350 NATLVSPPST 360 INQTPVTLQV 370 PGLMSSQVQM 380 GGHPTEVLCL 390 MNMVLPEELL 400 DDEEYEEIVE 410 DVRDECSKYG 420 LVKSIEIPRP 430 VDGVEVPGCG 440 KIFVEFTSVF 450 DCQKAMQGLT 460 GRKFANRVVV 470 TKYCDPDSYH RRDFW

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000243 commitment complex
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005681 spliceosomal complex
Cellular Component GO:0071004 U2-type prespliceosome
Cellular Component GO:0089701 U2AF complex
Molecular Function GO:0070742 C2H2 zinc finger domain binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0140678 molecular function inhibitor activity
Molecular Function GO:0008187 poly-pyrimidine tract binding
Molecular Function GO:0030628 pre-mRNA 3'-splice site binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006397 mRNA processing
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0048025 negative regulation of mRNA splicing, via spliceosome
Biological Process GO:0031397 negative regulation of protein ubiquitination
Biological Process GO:0033120 positive regulation of RNA splicing
Biological Process GO:0000245 spliceosomal complex assembly

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] 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.

[5] 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.

[6] 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.

[7] 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.

[8] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[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.