Search Results

Overview

Uniprot IDO60828
Protein NamePolyglutamine-binding protein 1
Gene NamePQBP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
123 KSDRSHEKLDRGHDK
148 DRERGYDKVDRERER
18 LAKRGILKHLEPEPE
189 EELAPYPKSKKAVSR
191 LAPYPKSKKAVSRKD
192 APYPKSKKAVSRKDE
197 SKKAVSRKDEELDPM
223 TWSTGLPKRNEAKTG

Function

Intrinsically disordered protein that acts as a scaffold, and which is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development (PubMed:10198427, PubMed:10332029, PubMed:12062018, PubMed:20410308, PubMed:23512658). Interacts with splicing-related factors via the intrinsically disordered region and regulates alternative splicing of target pre-mRNA species (PubMed:10332029, PubMed:12062018, PubMed:20410308, PubMed:23512658). May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery (PubMed:10198427). May be involved in ATXN1 mutant-induced cell death (PubMed:12062018). The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit (PubMed:12062018). Involved in the assembly of cytoplasmic stress granule, possibly by participating in the transport of neuronal RNA granules (PubMed:21933836). Also acts as an innate immune sensor of infection by retroviruses, such as HIV, by detecting the presence of reverse-transcribed DNA in the cytosol (PubMed:26046437). Directly binds retroviral reverse-transcribed DNA in the cytosol and interacts with CGAS, leading to activate the cGAS-STING signaling pathway, triggering type-I interferon production (PubMed:26046437)

Protein Sequence

10 MPLPVALQTR 20 LAKRGILKHL 30 EPEPEEEIIA 40 EDYDDDPVDY 50 EATRLEGLPP 60 SWYKVFDPSC 70 GLPYYWNADT 80 DLVSWLSPHD 90 PNSVVTKSAK 100 KLRSSNADAE 110 EKLDRSHDKS 120 DRGHDKSDRS 130 HEKLDRGHDK 140 SDRGHDKSDR 150 DRERGYDKVD 160 RERERDRERD 170 RDRGYDKADR 180 EEGKERRHHR 190 REELAPYPKS 200 KKAVSRKDEE 210 LDPMDPSSYS 220 DAPRGTWSTG 230 LPKRNEAKTG 240 ADTTAAGPLF 250 QQRPYPSPGA 260 VLRANAEASR TKQQD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0010494 cytoplasmic stress granule
Cellular Component GO:0071598 neuronal ribonucleoprotein granule
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0003690 double-stranded DNA binding
Molecular Function GO:0043021 ribonucleoprotein complex binding
Molecular Function GO:0003713 transcription coactivator activity
Biological Process GO:0002218 activation of innate immune response
Biological Process GO:0000380 alternative mRNA splicing, via spliceosome
Biological Process GO:0071360 cellular response to exogenous dsRNA
Biological Process GO:0051607 defense response to virus
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0045087 innate immune response
Biological Process GO:0031175 neuron projection development
Biological Process GO:0002230 positive regulation of defense response to virus by host
Biological Process GO:0032481 positive regulation of type I interferon production
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0043484 regulation of 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] 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.