Overview
| Uniprot ID | Q9NUL5 |
|---|
| Protein Name | Shiftless antiviral inhibitor of ribosomal frameshifting protein |
|---|
| Gene Name | SHFL |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 27 |
HGKVSSKKAGALMRK |
Function
Inhibits programmed -1 ribosomal frameshifting (-1PRF) of a variety of mRNAs from viruses, such as HIV1, and cellular genes, such as PEG10. Interacts with the -1PRF signal of target mRNA and translating ribosomes and causes premature translation termination at the frameshifting site (PubMed:30682371). Regulates HIV1 GAG-POL expression by inhibiting -1PRF (PubMed:30682371). Exhibits antiviral activity against dengue virus (DENV) and can inhibit the replication of all DENV serotypes. May block the protein translation of DENV RNA via its association with cellular mRNA-binding proteins and viral RNA. Also interrupts Zika virus replication by promoting viral NS3 degradation via a lysosome-dependent pathway (PubMed:32150556). Can also limit the replication of hepatitis C virus (HCV) by restricting formation of viral replication organelle, West Nile virus (WNV), Chikungunya virus (CHIKV), herpes simplex virus type 1 (HHV-1), herpes virus type 8 (HHV-8) and human adenovirus (PubMed:26735137, PubMed:27974568, PubMed:30944177, PubMed:32294532). Binds nucleic acids with a higher affinity for ssRNA and ssDNA than for dsDNA (PubMed:27974568)
Protein Sequence
10
MSQEGVELEK
20
SVRRLREKFH
30
GKVSSKKAGA
40
LMRKFGSDHT
50
GVGRSIVYGV
60
KQKDGQELSN
70
DLDAQDPPED
80
MKQDRDIQAV
90
ATSLLPLTEA
100
NLRMFQRAQD
110
DLIPAVDRQF
120
ACSSCDHVWW
130
RRVPQRKEVS
140
RCRKCRKRYE
150
PVPADKMWGL
160
AEFHCPKCRH
170
NFRGWAQMGS
180
PSPCYGCGFP
190
VYPTRILPPR
200
WDRDPDRRST
210
HTHSCSAADC
220
YNRREPHVPG
230
TSCAHPKSRK
240
QNHLPKVLHP
250
SNPHISSGST
260
VATCLSQGGL
270
LEDLDNLILE
280
DLKEEEEEEE
290
EVEDEEGGPR
E
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0000932 |
P-body |
| Molecular Function |
GO:0042802 |
identical protein binding |
| Molecular Function |
GO:0043022 |
ribosome binding |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:1990825 |
sequence-specific mRNA binding |
| Biological Process |
GO:0051607 |
defense response to virus |
| Biological Process |
GO:0045087 |
innate immune response |
| Biological Process |
GO:2001125 |
negative regulation of translational frameshifting |
| Biological Process |
GO:0045071 |
negative regulation of viral genome replication |
| Biological Process |
GO:0006449 |
regulation of translational termination |
| Biological Process |
GO:0035456 |
response to interferon-beta |
| Biological Process |
GO:0034340 |
response to type I interferon |
| Biological Process |
GO:0034341 |
response to type II interferon |
| Biological Process |
GO:0034342 |
response to type III interferon |
| Biological Process |
GO:0075523 |
viral translational frameshifting |
Reference
[1] 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.