Search Results

Overview

Uniprot IDQ13247
Protein NameSerine/arginine-rich splicing factor 6
Gene NameSRSF6
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
101 RRTSGRDKYGPPVRT
165 DMKRALDKLDGTEIN
182 NIRLIEDKPRTSHRR

Function

Plays a role in constitutive splicing and modulates the selection of alternative splice sites. Plays a role in the alternative splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-mRNA and promotes the expression of alternatively spliced TNC. Plays a role in wound healing and in the regulation of keratinocyte differentiation and proliferation via its role in alternative splicing

Protein Sequence

10 MPRVYIGRLS 20 YNVREKDIQR 30 FFSGYGRLLE 40 VDLKNGYGFV 50 EFEDSRDADD 60 AVYELNGKEL 70 CGERVIVEHA 80 RGPRRDRDGY 90 SYGSRSGGGG 100 YSSRRTSGRD 110 KYGPPVRTEY 120 RLIVENLSSR 130 CSWQDLKDFM 140 RQAGEVTYAD 150 AHKERTNEGV 160 IEFRSYSDMK 170 RALDKLDGTE 180 INGRNIRLIE 190 DKPRTSHRRS 200 YSGSRSRSRS 210 RRRSRSRSRR 220 SSRSRSRSIS 230 KSRSRSRSRS 240 KGRSRSRSKG 250 RKSRSKSKSK 260 PKSDRGSHSH 270 SRSRSKDEYE 280 KSRSRSRSRS 290 PKENGKGDIK 300 SKSRSRSQSR 310 SNSPLPVPPS 320 KARSVSPPPK 330 RATSRSRSRS 340 RSKSRSRSRS SSRD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0036002 pre-mRNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0000380 alternative mRNA splicing, via spliceosome
Biological Process GO:0006376 mRNA splice site recognition
Biological Process GO:0045617 negative regulation of keratinocyte differentiation
Biological Process GO:0048025 negative regulation of mRNA splicing, via spliceosome
Biological Process GO:2000675 negative regulation of type B pancreatic cell apoptotic process
Biological Process GO:0060501 positive regulation of epithelial cell proliferation involved in lung morphogenesis
Biological Process GO:0000381 regulation of alternative mRNA splicing, via spliceosome
Biological Process GO:0010837 regulation of keratinocyte proliferation
Biological Process GO:0061041 regulation of wound healing
Biological Process GO:0032868 response to insulin

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] 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.

[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] 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.

[7] 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.