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Overview

Uniprot IDQ96PK6
Protein NameRNA-binding protein 14
Gene NameRBM14
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
149 INVELSTKGQKKGPG
153 LSTKGQKKGPGLAVQ
593 ASYDDPYKKAVAMSK
600 KKAVAMSKRYGSDRR

Function

Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, functions as a transcriptional repressor, modulating transcriptional activities of coactivators including isoform 1, NCOA6 and CITED1 (PubMed:11443112). Regulates centriole biogenesis by suppressing the formation of aberrant centriolar protein complexes in the cytoplasm and thus preserving mitotic spindle integrity. Prevents the formation of the STIL-CPAP complex (which can induce the formation of aberrant centriolar protein complexes) by interfering with the interaction of STIL with CPAP (PubMed:25385835). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Also involved in the regulation of pre-mRNA alternative splicing (PubMed:37548402)

Protein Sequence

10 MKIFVGNVDG 20 ADTTPEELAA 30 LFAPYGTVMS 40 CAVMKQFAFV 50 HMRENAGALR 60 AIEALHGHEL 70 RPGRALVVEM 80 SRPRPLNTWK 90 IFVGNVSAAC 100 TSQELRSLFE 110 RRGRVIECDV 120 VKDYAFVHME 130 KEADAKAAIA 140 QLNGKEVKGK 150 RINVELSTKG 160 QKKGPGLAVQ 170 SGDKTKKPGA 180 GDTAFPGTGG 190 FSATFDYQQA 200 FGNSTGGFDG 210 QARQPTPPFF 220 GRDRSPLRRS 230 PPRASYVAPL 240 TAQPATYRAQ 250 PSVSLGAAYR 260 AQPSASLGVG 270 YRTQPMTAQA 280 ASYRAQPSVS 290 LGAPYRGQLA 300 SPSSQSAAAS 310 SLGPYGGAQP 320 SASALSSYGG 330 QAAAASSLNS 340 YGAQGSSLAS 350 YGNQPSSYGA 360 QAASSYGVRA 370 AASSYNTQGA 380 ASSLGSYGAQ 390 AASYGAQSAA 400 SSLAYGAQAA 410 SYNAQPSASY 420 NAQSAPYAAQ 430 QAASYSSQPA 440 AYVAQPATAA 450 AYASQPAAYA 460 AQATTPMAGS 470 YGAQPVVQTQ 480 LNSYGAQASM 490 GLSGSYGAQS 500 AAAATGSYGA 510 AAAYGAQPSA 520 TLAAPYRTQS 530 SASLAASYAA 540 QQHPQAAASY 550 RGQPGNAYDG 560 AGQPSAAYLS 570 MSQGAVANAN 580 STPPPYERTR 590 LSPPRASYDD 600 PYKKAVAMSK 610 RYGSDRRLAE 620 LSDYRRLSES 630 QLSFRRSPTK 640 SSLDYRRLPD 650 AHSDYARYSG 660 SYNDYLRAAQ MHSGYQRRM

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Cellular Component GO:0005667 transcription regulator complex
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:1990935 splicing factor binding
Molecular Function GO:0003713 transcription coactivator activity
Biological Process GO:0002218 activation of innate immune response
Biological Process GO:0098534 centriole assembly
Biological Process GO:0045087 innate immune response
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0046600 negative regulation of centriole replication
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0000381 regulation of alternative mRNA splicing, via spliceosome
Biological Process GO:0009725 response to hormone
Biological Process GO:0045815 transcription initiation-coupled chromatin remodeling

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] 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.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[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.