Search Results
Overview
| Uniprot ID | Q8NI27 |
|---|---|
| Protein Name | THO complex subunit 2 |
| Gene Name | THOC2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1239 | ERSQCGVKAVNKASS |
| 1243 | CGVKAVNKASSTTPK |
| 1284 | KEKEKKEKTPATTPE |
| 1343 | KAKDEKFKTTVPNAE |
| 1352 | TVPNAESKSTQERER |
| 1392 | TPVSGSLKSPVPRSD |
| 1411 | EREQKRRKIDTHPSP |
| 1449 | HTPPPLSKSKEREMD |
| 1451 | PPPLSKSKEREMDKK |
| 147 | QSQQFNQKSVKIKTK |
| 1552 | FKSEKMDKISSGGKK |
| 158 | IKTKLFYKQQKFNLL |
| 312 | EAKQIVRKLTMVVLS |
Function
Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for efficient export of polyadenylated RNA and spliced mRNA (PubMed:23222130). The THOC1-THOC2-THOC3 core complex alone is sufficient to bind export factor NXF1-NXT1 and promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for NXF1 localization to the nuclear rim (PubMed:22893130). THOC2 (and probably the THO complex) is involved in releasing mRNA from nuclear speckle domains
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0000347 | THO complex |
| Cellular Component | GO:0000445 | THO complex part of transcription export complex |
| Cellular Component | GO:0000346 | transcription export complex |
| Molecular Function | GO:0003729 | mRNA binding |
| Biological Process | GO:0048699 | generation of neurons |
| Biological Process | GO:0006406 | mRNA export from nucleus |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:0010977 | negative regulation of neuron projection development |
| Biological Process | GO:0048666 | neuron development |
| Biological Process | GO:0016973 | poly(A)+ mRNA export from nucleus |
| 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] 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.