Search Results

Overview

Uniprot IDP49756
Protein NameRNA-binding protein 25
Gene NameRBM25
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
155 HDLQIGEKKLLVKVD
240 PRKKKKEKKEDIFRR
241 RKKKKEKKEDIFRRF
297 KLEEEKGKKEKERQE
453 LERKLREKEAAYQER
671 PKIGLSLKLGASNSP
685 PGQPNSVKRKKLPVD
688 PNSVKRKKLPVDSVF
69 GKHLGARKDHPGLKA
711 DDVPRKRKLVPLDYG
722 LDYGEDDKNATKGTV
726 EDDKNATKGTVNTEE
739 EEKRKHIKSLIEKIP

Function

RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing. Involved in apoptotic cell death through the regulation of the apoptotic factor BCL2L1 isoform expression. Modulates the ratio of proapoptotic BCL2L1 isoform S to antiapoptotic BCL2L1 isoform L mRNA expression. When overexpressed, stimulates proapoptotic BCL2L1 isoform S 5'-splice site (5'-ss) selection, whereas its depletion caused the accumulation of antiapoptotic BCL2L1 isoform L. Promotes BCL2L1 isoform S 5'-ss usage through the 5'-CGGGCA-3' RNA sequence. Its association with LUC7L3 promotes U1 snRNP binding to a weak 5' ss in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic splicing enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of the BCL2L1 pre-mRNA. Also involved in the generation of an abnormal and truncated splice form of SCN5A in heart failure

Protein Sequence

10 MSFPPHLNRP 20 PMGIPALPPG 30 IPPPQFPGFP 40 PPVPPGTPMI 50 PVPMSIMAPA 60 PTVLVPTVSM 70 VGKHLGARKD 80 HPGLKAKEND 90 ENCGPTTTVF 100 VGNISEKASD 110 MLIRQLLAKC 120 GLVLSWKRVQ 130 GASGKLQAFG 140 FCEYKEPEST 150 LRALRLLHDL 160 QIGEKKLLVK 170 VDAKTKAQLD 180 EWKAKKKASN 190 GNARPETVTN 200 DDEEALDEET 210 KRRDQMIKGA 220 IEVLIREYSS 230 ELNAPSQESD 240 SHPRKKKKEK 250 KEDIFRRFPV 260 APLIPYPLIT 270 KEDINAIEME 280 EDKRDLISRE 290 ISKFRDTHKK 300 LEEEKGKKEK 310 ERQEIEKERR 320 ERERERERER 330 ERRERERERE 340 REREREKEKE 350 RERERERDRD 360 RDRTKERDRD 370 RDRERDRDRD 380 RERSSDRNKD 390 RSRSREKSRD 400 RERERERERE 410 RERERERERE 420 RERERERERE 430 REREREKDKK 440 RDREEDEEDA 450 YERRKLERKL 460 REKEAAYQER 470 LKNWEIRERK 480 KTREYEKEAE 490 REEERRREMA 500 KEAKRLKEFL 510 EDYDDDRDDP 520 KYYRGSALQK 530 RLRDREKEME 540 ADERDRKREK 550 EELEEIRQRL 560 LAEGHPDPDA 570 ELQRMEQEAE 580 RRRQPQIKQE 590 PESEEEEEEK 600 QEKEEKREEP 610 MEEEEEPEQK 620 PCLKPTLRPI 630 SSAPSVSSAS 640 GNATPNTPGD 650 ESPCGIIIPH 660 ENSPDQQQPE 670 EHRPKIGLSL 680 KLGASNSPGQ 690 PNSVKRKKLP 700 VDSVFNKFED 710 EDSDDVPRKR 720 KLVPLDYGED 730 DKNATKGTVN 740 TEEKRKHIKS 750 LIEKIPTAKP 760 ELFAYPLDWS 770 IVDSILMERR 780 IRPWINKKII 790 EYIGEEEATL 800 VDFVCSKVMA 810 HSSPQSILDD 820 VAMVLDEEAE 830 VFIVKMWRLL 840 IYETEAKKIG LVK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006397 mRNA processing
Biological Process GO:0000381 regulation of alternative mRNA splicing, via spliceosome
Biological Process GO:0042981 regulation of apoptotic process
Biological Process GO:0008380 RNA splicing

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.