Search Results
Overview
| Uniprot ID | O60506 |
|---|---|
| Protein Name | Heterogeneous nuclear ribonucleoprotein Q |
| Gene Name | SYNCRIP |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 100 | AFLCGVMKTYRQREK |
| 221 | EAAQEAVKLYNNHEI |
| 252 | LFVGSIPKSKTKEQI |
| 256 | SIPKSKTKEQILEEF |
| 338 | PEVMAKVKVLFVRNL |
| 363 | KAFSQFGKLERVKKL |
| 371 | LERVKKLKDYAFIHF |
| 566 | GNVGGKRKADGYNQP |
| 576 | GYNQPDSKRRQTNNQ |
Function
Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; does not seem to be essential for GAIT complex function
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0071013 | catalytic step 2 spliceosome |
| Cellular Component | GO:0070937 | CRD-mediated mRNA stability complex |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0097452 | GAIT complex |
| Cellular Component | GO:0071204 | histone pre-mRNA 3'end processing complex |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Molecular Function | GO:0048027 | mRNA 5'-UTR binding |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0071346 | cellular response to type II interferon |
| Biological Process | GO:0141166 | chromosomal 5-methylcytosine DNA demethylation pathway |
| Biological Process | GO:0070934 | CRD-mediated mRNA stabilization |
| Biological Process | GO:0016556 | mRNA modification |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:1901194 | negative regulation of formation of translation preinitiation complex |
| Biological Process | GO:1900152 | negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay |
| Biological Process | GO:2000623 | negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| Biological Process | GO:0017148 | negative regulation of translation |
| Biological Process | GO:0001649 | osteoblast differentiation |
| Biological Process | GO:2000767 | positive regulation of cytoplasmic translation |
| Biological Process | GO:0006396 | RNA processing |
| 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 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.
[4] 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.