Search Results
Overview
| Uniprot ID | Q15652 |
|---|---|
| Protein Name | Jumonji domain-containing protein 1C |
| Gene Name | JMJD1C |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1038 | DVAPFTTKIKGLEGE |
| 1040 | APFTTKIKGLEGERE |
| 1060 | ASSSSSPKSHIIKQD |
| 1258 | PTLIPEPKDSQANFK |
| 1284 | RPNNNLSKEKTEWHV |
| 1326 | PAMQLASKDRVSERS |
| 1339 | RSSAGAHKTDCLKLA |
| 1344 | AHKTDCLKLAEAGET |
| 1367 | NSDSVHTKSEKNFQA |
| 1370 | SVHTKSEKNFQAVSQ |
| 1445 | VSQPVAQKQECKVST |
| 1449 | VAQKQECKVSTTAPV |
| 1483 | TTDFIHLKKHKAALA |
| 1484 | TDFIHLKKHKAALAA |
| 1486 | FIHLKKHKAALAAAQ |
| 1495 | ALAAAQYKSSNASET |
| 1606 | DSKIIVDKYVKDDKV |
| 1661 | QNDLQKRKGEIEEDL |
| 1685 | AKERSKLKLQSNSNT |
| 1741 | CRLIRSKKGEEPAHS |
| 2076 | LLTTTAGKLRVGSTD |
| 2120 | IASVVENKIPPSKTS |
| 2128 | IPPSKTSKINVKPEL |
| 2252 | VSKRQKNKSGETVVL |
| 2360 | KGNGILSKAGILKKF |
| 315 | SIRPNKRKGSDSSIP |
| 404 | PENELKNKNTSKING |
| 408 | LKNKNTSKINGEEGK |
| 536 | FGLQTLQKMDPNVSD |
| 545 | DPNVSDSKHSIANAK |
| 552 | KHSIANAKFLETAKK |
| 559 | KFLETAKKDSDQSWV |
| 626 | PPETIKSKLNTSVDT |
| 635 | NTSVDTHKIKSSPSP |
| 637 | SVDTHKIKSSPSPEV |
| 659 | SPDSVKSKATYVNSQ |
| 676 | GERRLANKIEHELSR |
| 707 | KSPLIIDKNEHFTVY |
| 976 | SVASTSAKNDLDLNR |
| 988 | LNRSQTGKDCHLHRH |
Function
Demethylates lysine in proteins, such as STAT3 or MDC1 (By similarity) (PubMed:24240613). Demethylates MDC1, thereby promoting MDC1-RNF8 interaction and facilitating RNF8-dependent MDC1 ubiquitination essential for double-strand break (DSB) repair (PubMed:24240613). Demethylation of STAT3 at 'Lys-140' facilitates its interactions with the phosphatase PTPN6 and restrains STAT3 activation (By similarity). It is uncertain whether JMJD1C removes methyl groups from histone proteins as the other JMJD1/KDM3 proteins do (PubMed:23593242, PubMed:24240613, PubMed:32034158). Nevertheless, JMJD1C may act as a context-specific histone demethylase. Implicated in lipogenic gene transcription in the liver, where USF1 recruits JMJD1C to lipogenic promoters in response to insulin or feeding stimuli, thereby potentially promoting H3K9me2 demethylation and enhancing chromatin accessibility (PubMed:32034158). Post-translational modifications may regulate JMJD1C's enzymatic activity, contributing to its context-specific functions (PubMed:32034158). Alternatively, JMJD1C may influence chromatin regulation indirectly, acting as a scaffold or co-regulator that recruits or stabilizes other active demethylase complexes modifying histone marks (PubMed:24240613). Plays an indispensable role in spermatogenesis (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0000118 | histone deacetylase complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0031490 | chromatin DNA binding |
| Molecular Function | GO:0051213 | dioxygenase activity |
| Molecular Function | GO:0032454 | histone H3K9 demethylase activity |
| Molecular Function | GO:0046966 | nuclear thyroid hormone receptor binding |
| Molecular Function | GO:0140457 | protein demethylase activity |
| Molecular Function | GO:0003712 | transcription coregulator activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0007596 | blood coagulation |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0008610 | lipid biosynthetic process |
| Biological Process | GO:0002317 | plasma cell differentiation |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
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.