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Overview

Uniprot IDP26599
Protein NamePolypyrimidine tract-binding protein 1
Gene NamePTBP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
13 PDIAVGTKRGSDELF
134 YIQFSNHKELKTDSS
137 FSNHKELKTDSSPNQ
259 TLRIDFSKLTSLNVK
266 KLTSLNVKYNNDKSR
394 YGDVQRVKILFNKKE
436 PIRITLSKHQNVQLP
92 VTNLLMLKGKNQAFI

Function

Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10 (PubMed:15009664). Binds to polypyrimidine-rich controlling element (PCE) of CFTR and promotes exon skipping of CFTR exon 9, thereby antagonizing TIA1 and its role in exon inclusion of CFTR exon 9 (PubMed:14966131). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to a polypyrimidine tract flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). In case of infection by picornaviruses, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation (PubMed:21518806)

Protein Sequence

10 MDGIVPDIAV 20 GTKRGSDELF 30 STCVTNGPFI 40 MSSNSASAAN 50 GNDSKKFKGD 60 SRSAGVPSRV 70 IHIRKLPIDV 80 TEGEVISLGL 90 PFGKVTNLLM 100 LKGKNQAFIE 110 MNTEEAANTM 120 VNYYTSVTPV 130 LRGQPIYIQF 140 SNHKELKTDS 150 SPNQARAQAA 160 LQAVNSVQSG 170 NLALAASAAA 180 VDAGMAMAGQ 190 SPVLRIIVEN 200 LFYPVTLDVL 210 HQIFSKFGTV 220 LKIITFTKNN 230 QFQALLQYAD 240 PVSAQHAKLS 250 LDGQNIYNAC 260 CTLRIDFSKL 270 TSLNVKYNND 280 KSRDYTRPDL 290 PSGDSQPSLD 300 QTMAAAFGAP 310 GIISASPYAG 320 AGFPPTFAIP 330 QAAGLSVPNV 340 HGALAPLAIP 350 SAAAAAAAAG 360 RIAIPGLAGA 370 GNSVLLVSNL 380 NPERVTPQSL 390 FILFGVYGDV 400 QRVKILFNKK 410 ENALVQMADG 420 NQAQLAMSHL 430 NGHKLHGKPI 440 RITLSKHQNV 450 QLPREGQEDQ 460 GLTKDYGNSP 470 LHRFKKPGSK 480 NFQNIFPPSA 490 TLHLSNIPPS 500 VSEEDLKVLF 510 SSNGGVVKGF 520 KFFQKDRKMA 530 LIQMGSVEEA 540 VQALIDLHNH 550 DLGENHHLRV SFSKSTI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0008187 poly-pyrimidine tract binding
Molecular Function GO:0036002 pre-mRNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0075522 IRES-dependent viral translational initiation
Biological Process GO:0006397 mRNA processing
Biological Process GO:0048025 negative regulation of mRNA splicing, via spliceosome
Biological Process GO:0051148 negative regulation of muscle cell differentiation
Biological Process GO:0045665 negative regulation of neuron differentiation
Biological Process GO:0033119 negative regulation of RNA splicing
Biological Process GO:0070886 positive regulation of calcineurin-NFAT signaling cascade
Biological Process GO:0000381 regulation of alternative mRNA splicing, via spliceosome
Biological Process GO:0045595 regulation of cell differentiation
Biological Process GO:0043484 regulation of RNA splicing
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] 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] 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.

[6] 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.

[7] 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.