Search Results

Overview

Uniprot ID	Q15366
Protein Name	Poly(rC)-binding protein 2
Gene Name	PCBP2
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
115	QCGSLIGKGGCKIKE
23	IRLLMHGKEVGSIIG
309	IIGRQGAKINEIRQM
31	EVGSIIGKKGESVKK
32	VGSIIGKKGESVKKM

Function

Single-stranded nucleic acid binding protein that binds preferentially to oligo dC (PubMed:12414943, PubMed:7607214). Major cellular poly(rC)-binding protein (PubMed:12414943). Also binds poly(rU) (PubMed:12414943). Acts as a negative regulator of antiviral signaling (PubMed:19881509, PubMed:35322803). Negatively regulates cellular antiviral responses mediated by MAVS signaling (PubMed:19881509). It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation (PubMed:19881509). Negativeley regulates the cGAS-STING pathway via interaction with CGAS, preventing the formation of liquid-like droplets in which CGAS is activated (PubMed:35322803). Together with PCBP1, required for erythropoiesis, possibly by regulating mRNA splicing (By similarity)

Protein Sequence

10 MDTGVIEGGL 20 NVTLTIRLLM 30 HGKEVGSIIG 40 KKGESVKKMR 50 EESGARINIS 60 EGNCPERIIT 70 LAGPTNAIFK 80 AFAMIIDKLE 90 EDISSSMTNS 100 TAASRPPVTL 110 RLVVPASQCG 120 SLIGKGGCKI 130 KEIRESTGAQ 140 VQVAGDMLPN 150 STERAITIAG 160 IPQSIIECVK 170 QICVVMLETL 180 SQSPPKGVTI 190 PYRPKPSSSP 200 VIFAGGQDRY 210 STGSDSASFP 220 HTTPSMCLNP 230 DLEGPPLEAY 240 TIQGQYAIPQ 250 PDLTKLHQLA 260 MQQSHFPMTH 270 GNTGFSGIES 280 SSPEVKGYWG 290 LDASAQTTSH 300 ELTIPNDLIG 310 CIIGRQGAKI 320 NEIRQMSGAQ 330 IKIANPVEGS 340 TDRQVTITGS 350 AASISLAQYL 360 INVRLSSETG GMGSS

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0070062	extracellular exosome
Cellular Component	GO:0005925	focal adhesion
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:1990904	ribonucleoprotein complex
Molecular Function	GO:0019899	enzyme binding
Molecular Function	GO:0106222	lncRNA binding
Molecular Function	GO:0003729	mRNA binding
Molecular Function	GO:0140585	promoter-enhancer loop anchoring activity
Molecular Function	GO:0003723	RNA binding
Molecular Function	GO:0003697	single-stranded DNA binding
Molecular Function	GO:0031625	ubiquitin protein ligase binding
Biological Process	GO:0140588	chromatin looping
Biological Process	GO:0051607	defense response to virus
Biological Process	GO:0045087	innate immune response
Biological Process	GO:0075522	IRES-dependent viral translational initiation
Biological Process	GO:0016071	mRNA metabolic process
Biological Process	GO:0160049	negative regulation of cGAS/STING signaling pathway
Biological Process	GO:0050687	negative regulation of defense response to virus
Biological Process	GO:0045944	positive regulation of transcription by RNA polymerase II
Biological Process	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process
Biological Process	GO:0039694	viral RNA genome replication

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] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.

[11] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[12] 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.