Search Results

Overview

Uniprot IDP62995
Protein NameTransformer-2 protein homolog beta
Gene NameTRA2B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
197 RVDFSITKRPHTPTP

Function

Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA

Protein Sequence

10 MSDSGEQNYG 20 ERESRSASRS 30 GSAHGSGKSA 40 RHTPARSRSK 50 EDSRRSRSKS 60 RSRSESRSRS 70 RRSSRRHYTR 80 SRSRSRSHRR 90 SRSRSYSRDY 100 RRRHSHSHSP 110 MSTRRRHVGN 120 RANPDPNCCL 130 GVFGLSLYTT 140 ERDLREVFSK 150 YGPIADVSIV 160 YDQQSRRSRG 170 FAFVYFENVD 180 DAKEAKERAN 190 GMELDGRRIR 200 VDFSITKRPH 210 TPTPGIYMGR 220 PTYGSSRRRD 230 YYDRGYDRGY 240 DDRDYYSRSY 250 RGGGGGGGGW 260 RAAQDRDQIY 270 RRRSPSPYYS 280 RGGYRSRSRS RSYSPRRY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005637 nuclear inner membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0005681 spliceosomal complex
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0036002 pre-mRNA binding
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0071333 cellular response to glucose stimulus
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0048026 positive regulation of mRNA splicing, via spliceosome
Biological Process GO:0000381 regulation of alternative mRNA splicing, via spliceosome
Biological Process GO:0043484 regulation of RNA splicing
Biological Process GO:0000375 RNA splicing, via transesterification reactions

Reference

[1] 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.

[2] 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.

[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[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] 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] 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.