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Demethylates MDC1, thereby promoting MDC1-RNF8 interaction and facilitating RNF8-dependent MDC1 ubiquitination essential for double-strand break (DSB) repair (By similarity). Demethylation of STAT3 at 'Lys-140', facilitates its interactions with the phosphatase PTPN6 and restrains STAT3 activation (PubMed:35995859). It is uncertain whether JMJD1C removes methyl groups from histone proteins as the other JMJD1/KDM3 proteins do (PubMed:20530532, PubMed:24006281, PubMed:32034158, PubMed:35995859). 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 (By similarity). Plays an indispensable role in spermatogenesis (PubMed:20530532, PubMed:24006281)"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15652"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Binds 1 Fe(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15652"}],"value":"Demethylase activity is regulated post-translationally via phosphorylation"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15652"}],"value":"Interacts with RNF8; promotes interaction between RNF8 and MDC1 through demethylation of MDC1"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15652"}],"value":"Nucleus","id":"SL-0191"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q69ZK6-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q69ZK6-2"],"sequenceIds":["VSP_062730"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15652"}],"value":"Ubiquitinated. Protein abundance of JMJD1C is regulated by the ubiquitin proteasome pathway"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15652"}],"value":"Phosphorylated. Phosphorylation at Thr-505 by mTORC1 complex in response to insulin/feeding"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24006281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32034158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35995859"}],"value":"Jmjd1c-deficient male mice exhibit an age-dependent infertility phenotype, accompanied by a progressive reduction of germ cells (PubMed:24006281). Liver-specific Jmjd1c knockout protects against high-carbohydrate diet-induced hepatosteatosis and insulin resistance in the absence of increased adiposity (PubMed:32034158). B cell-specific knockout of Jmjd1c in mice promotes plasma cell differentiation and, in a model of collagen-induced arthritis, leads to an earlier incidence of disease and increased disease severity (PubMed:35995859)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the JHDM2 histone demethylase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q15652"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20530532"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24006281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32034158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35995859"}],"value":"It is uncertain whether JMJD1C removes methyl groups from histone proteins as the other JMJD/KDM3 proteins do. Independent studies show conflicting conclusions that either succeeded or failed to substantiate the existence of histone demethylase activity of JMJD1C (PubMed:20530532, PubMed:24006281, PubMed:32034158, PubMed:35995859). This conflicting data suggests JMJD1C's role may be context-dependent. It may be possible that JMJD1C contributes to H3K9 demethylation in specific genomic regions. Alternatively, JMJD1C may function indirectly in chromatin regulation by serving as a scaffold or co-regulator, recruiting or stabilizing other active demethylase complexes that modify histone marks (By similarity)"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAH68318.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Miscellaneous discrepancy","sequence":"AAH68318.1","note":"Aberrant splicing.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous termination","sequence":"BAC36783.1","note":"Truncated C-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAC38410.1","note":"Truncated N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous 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