| Gene Name | PTBP1 |
| HF Protein Name | Polypyrimidine tract-binding protein 1 |
| HF Function | Important for Norwalk virus translation |
| Uniprot ID | P26599 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 5725 |
| Host Factor (HF) Name in Paper | PTB |
| Gene synonyms | PTB |
| Ensemble Gene ID | ENSG00000011304 |
| Ensemble Transcript | ENST00000349038 [P26599-1];ENST00000356948 [P26599-3];ENST00000394601 [P26599-2] |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0000381, GO:0000398, GO:0003723, GO:0005654, GO:0005730, GO:0006397, GO:0008187, GO:0008380, GO:0008543, GO:0016020, GO:0016070, GO:0033119, GO:0036002, GO:0048025, GO:0051148, GO:0070062, GO:0075522, |
| MINT ID | P26599 |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | 600693 |
| PANTHER ID | N.A. |
| PDB ID(s) | 1QM9, 1SJQ, 1SJR, 2AD9, 2ADB, 2ADC, 2EVZ, 2N3O, 3ZZY, 3ZZZ, |
| pfam ID | PF00076, |
| Drug Bank ID | N.A., |
| ChEMBL ID | CHEMBL1293230 |
| Organism | Homo sapiens (Human) |
| Virus Name | Norwalk virus |
| Virus Short Name | NLV |
| Order | Nidovirales |
| Virus Family | Caliciviridae |
| Virus Subfamily | N.A. |
| Genus | Norovirus |
| Species | Norwalk virus |
| Host | Human, mammals |
| Cell Tropism | Intestinal epithelium |
| Associated Disease | Gastroenteritis |
| Mode of Transmission | Fecal-oral route from contaminated water and food |
| VIPR DB link | https://www.viprbrc.org/brc/home.spg?decorator=calici |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/positive-sense-rna-viruses-2011/w/posrna_viruses/253/caliciviridae |
| Virus Host DB link | N.A. |
| Paper Title | Interaction of cellular proteins with the 5 End of Norwalk Virus genomic RNA |
| Author's Name | ANA LORENA GUTIERREZ-ESCOLANO, ZAMIRATH URIBE BRITO, ROSA M. DEL ANGEL AND XI JIANG |
| Journal Name | Journal Of Virology |
| Pubmed ID | 10954557 |
| Abstract | The lack of a susceptible cell line and an animal model for Norwalk virus (NV) infection has prompted the development of alternative strategies to generate in vitro RNAs that approximate the authentic viral genome. This approach has allowed the study of viral RNA replication and gene expression. In this study, using mobility shift and cross-linking assays, we detected several cellular proteins from HeLa and CaCo-2 cell extracts that bind to, and form stable complexes with, the first 110 nucleotides of the 5′ end of NV genomic RNA, a region previously predicted to form a double stem-loop structure. These proteins had molecular weights similar to those of the HeLa cellular proteins that bind to the internal ribosomal entry site of poliovirus RNA. HeLa proteins La, PCBP-2, and PTB, which are important for poliovirus translation, and hnRNP L, which is possibly implicated in hepatitis C virus translation, interact with NV RNA. These protein-RNA interactions are likely to play a role in NV translation and/or replication. |
| Used Model | HeLa and CaCo-2 cells |
| DOI | N.A. |
