Search Results
Overview
| Uniprot ID | Q9UBB9 |
|---|---|
| Protein Name | Tuftelin-interacting protein 11 |
| Gene Name | TFIP11 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 120 | DFGPRKLKTGGNFKP |
| 155 | HTKGIGQKLLQKMGY |
| 159 | IGQKLLQKMGYVPGR |
| 170 | VPGRGLGKNAQGIIN |
| 182 | IINPIEAKQRKGKGA |
| 187 | EAKQRKGKGAVGAYG |
| 241 | KKPKYSYKTVEELKA |
| 249 | TVEELKAKGRISKKL |
| 255 | AKGRISKKLTAPQKE |
| 261 | KKLTAPQKELSQVKV |
| 741 | LTHTERRKDFQYEAM |
| 794 | VFMPVIGKRHEGKQL |
| 86 | NFISAGLKKGAAEEA |
Function
Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. Intron turnover seems to proceed through reactions in two lariat-intron associated complexes termed Intron Large (IL) and Intron Small (IS). In cooperation with DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extracellular matrix
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0071013 | catalytic step 2 spliceosome |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0031012 | extracellular matrix |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005681 | spliceosomal complex |
| Cellular Component | GO:0071008 | U2-type post-mRNA release spliceosomal complex |
| Molecular Function | GO:0003676 | nucleic acid binding |
| Biological Process | GO:0031214 | biomineral tissue development |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:2001033 | negative regulation of double-strand break repair via nonhomologous end joining |
| Biological Process | GO:0031333 | negative regulation of protein-containing complex assembly |
| Biological Process | GO:0031848 | protection from non-homologous end joining at telomere |
| Biological Process | GO:0006396 | RNA processing |
| Biological Process | GO:0000390 | spliceosomal complex disassembly |
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] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[7] 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.