Search Results

Overview

Uniprot ID	Q14498
Protein Name	RNA-binding protein 39
Gene Name	RBM39
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
103	RSPYSGPKFNSAIRG
111	FNSAIRGKIGLPHSI
119	IGLPHSIKLSRRRSR
21	PYKKDENKLSSANGH
244	AMANNLQKGSAGPMR

Function

RNA-binding protein that acts as a pre-mRNA splicing factor (PubMed:15694343, PubMed:24795046, PubMed:28302793, PubMed:28437394, PubMed:31271494). Acts by promoting exon inclusion via regulation of exon cassette splicing (PubMed:31271494). Also acts as a transcriptional coactivator for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and JUN/AP-1, independently of the pre-mRNA splicing factor activity (By similarity)

Protein Sequence

10 MADDIDIEAM 20 LEAPYKKDEN 30 KLSSANGHEE 40 RSKKRKKSKS 50 RSRSHERKRS 60 KSKERKRSRD 70 RERKKSKSRE 80 RKRSRSKERR 90 RSRSRSRDRR 100 FRGRYRSPYS 110 GPKFNSAIRG 120 KIGLPHSIKL 130 SRRRSRSKSP 140 FRKDKSPVRE 150 PIDNLTPEER 160 DARTVFCMQL 170 AARIRPRDLE 180 EFFSTVGKVR 190 DVRMISDRNS 200 RRSKGIAYVE 210 FVDVSSVPLA 220 IGLTGQRVLG 230 VPIIVQASQA 240 EKNRAAAMAN 250 NLQKGSAGPM 260 RLYVGSLHFN 270 ITEDMLRGIF 280 EPFGRIESIQ 290 LMMDSETGRS 300 KGYGFITFSD 310 SECAKKALEQ 320 LNGFELAGRP 330 MKVGHVTERT 340 DASSASSFLD 350 SDELERTGID 360 LGTTGRLQLM 370 ARLAEGTGLQ 380 IPPAAQQALQ 390 MSGSLAFGAV 400 AEFSFVIDLQ 410 TRLSQQTEAS 420 ALAAAASVQP 430 LATQCFQLSN 440 MFNPQTEEEV 450 GWDTEIKDDV 460 IEECNKHGGV 470 IHIYVDKNSA 480 QGNVYVKCPS 490 IAAAIAAVNA 500 LHGRWFAGKM 510 ITAAYVPLPT 520 YHNLFPDSMT 530 ATQLLVPSRR

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0016607	nuclear speck
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0032991	protein-containing complex
Molecular Function	GO:0003723	RNA binding
Molecular Function	GO:0050733	RS domain binding
Molecular Function	GO:1990446	U1 snRNP binding
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0006397	mRNA processing
Biological Process	GO:0048024	regulation of mRNA splicing, via spliceosome
Biological Process	GO:0006396	RNA processing
Biological Process	GO:0008380	RNA splicing

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] 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.

[3] 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.

[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] 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.