Search Results
Overview
| Uniprot ID | Q14966 |
|---|---|
| Protein Name | Zinc finger protein 638 |
| Gene Name | ZNF638 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1298 | DEKTVDKKNISEKKG |
| 1345 | MDAEKVEKMAAMKEK |
| 1360 | PAENTLFKAYPNKGV |
| 1365 | LFKAYPNKGVGQANK |
| 1395 | SSSKPSIKAVIVSSP |
| 1410 | KAKATVSKTENQKSF |
| 1415 | VSKTENQKSFPKSVP |
| 1419 | ENQKSFPKSVPRDQI |
| 1435 | AEKKLSAKEFGLLKP |
| 1455 | GLAESSSKFKPTQSS |
| 1477 | RISALQGKLSKLDYR |
| 1480 | ALQGKLSKLDYRDIT |
| 1516 | TLAEQNTKNPKSTTG |
| 1570 | GKRKETLKNVPFSEL |
| 1818 | KRAVDTKKTKLESLS |
| 1820 | AVDTKKTKLESLSQV |
| 1860 | TKRVRIGKTLPSEKA |
| 371 | VGSRGSKKNYQSQAD |
| 395 | VKASWLPKFSHADAQ |
| 403 | FSHADAQKMKRLPTP |
| 642 | HSIRCKSKNLEDDTL |
| 658 | ECKQVSDKAVSLQRK |
| 751 | VKICVPGKKKAQNKE |
| 794 | VTSTSAAKTGQAKAS |
| 799 | AAKTGQAKASVAKVN |
| 804 | QAKASVAKVNKSTGK |
| 825 | SVVTVAVKGNKASIK |
| 828 | TVAVKGNKASIKTAK |
| 853 | KTGNVKNKDSNKPVT |
| 86 | DPRLTKEKLDFHEAQ |
| 943 | LILSSHKKAYIEINR |
| 95 | DFHEAQQKKGKPHGS |
| 96 | FHEAQQKKGKPHGSR |
Function
Transcription factor that binds to cytidine clusters in double-stranded DNA (PubMed:30487602, PubMed:8647861). Plays a key role in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Mediates transcriptional repression of unintegrated viral DNA by specifically binding to the cytidine clusters of retroviral DNA and mediating the recruitment of chromatin silencers, such as the HUSH complex, SETDB1 and the histone deacetylases HDAC1 and HDAC4 (PubMed:30487602). Acts as an early regulator of adipogenesis by acting as a transcription cofactor of CEBPs (CEBPA, CEBPD and/or CEBPG), controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1 (By similarity). May also regulate alternative splicing of target genes during adipogenesis (By similarity)
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 |
| Molecular Function | GO:0003690 | double-stranded DNA binding |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0043484 | regulation of RNA splicing |
| 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.