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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q95QK3
• Protein Description: RecName: Full=Lysine-specific demethylase jmjd-3.1 {ECO:0000305}; EC=1.14.11.- {ECO:0000269|PubMed:17713478}; AltName: Full=JmjC domain-containing protein 3.1 {ECO:0000305};
• Gene Information: Name=jmjd-3.1 {ECO:0000312|WormBase:F18E9.5b}; ORFNames=F18E9.5 {ECO:0000312|WormBase:F18E9.5b};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Belongs to the UTX family. .
• Key Domains: Corepressor-Demethylase. (IPR051630); JmjC_dom. (IPR003347); KDM6_GATAL_sf. (IPR046941); KDM6A_B-like_C-hel. (IPR048562); JmjC (PF02373)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "jmjd-3.1" matches the protein description above
2. Verify the organism is correct: Caenorhabditis elegans.
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'jmjd-3.1' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene jmjd-3.1 (gene ID: jmjd-3.1, UniProt: Q95QK3) in worm.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q95QK3
• Protein Description: RecName: Full=Lysine-specific demethylase jmjd-3.1 {ECO:0000305}; EC=1.14.11.- {ECO:0000269|PubMed:17713478}; AltName: Full=JmjC domain-containing protein 3.1 {ECO:0000305};
• Gene Information: Name=jmjd-3.1 {ECO:0000312|WormBase:F18E9.5b}; ORFNames=F18E9.5 {ECO:0000312|WormBase:F18E9.5b};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Belongs to the UTX family. .
• Key Domains: Corepressor-Demethylase. (IPR051630); JmjC_dom. (IPR003347); KDM6_GATAL_sf. (IPR046941); KDM6A_B-like_C-hel. (IPR048562); JmjC (PF02373)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "jmjd-3.1" matches the protein description above
2. Verify the organism is correct: Caenorhabditis elegans.
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'jmjd-3.1' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene jmjd-3.1 (gene ID: jmjd-3.1, UniProt: Q95QK3) in worm.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Plan overview
- Verified identity and context: jmjd-3.1 (UniProt Q95QK3; WormBase F18E9.5/F18E9.5b) encodes a JMJD3-like JmjC-domain histone demethylase of the UTX/KDM6 family in Caenorhabditis elegans. It carries the conserved JmjC catalytic motif and has been genetically and functionally linked to H3K27 demethylation and stress-responsive transcriptional programs (see Evidence Table). (vandamme2012thec.elegans pages 4-4)

Research report: jmjd-3.1 (Q95QK3) functional annotation in C. elegans

1) Key concepts and definitions
- Molecular identity and domains: jmjd-3.1 encodes a JmjC-domain lysine demethylase in the KDM6/UTX family, orthologous to vertebrate JMJD3/KDM6B. The JmjC catalytic domain supports Fe(II)/α-ketoglutarate–dependent demethylation. In nematodes, JMJD3-like proteins (jmjd-3.1/3.2/3.3) and UTX-1 comprise the H3K27 demethylase set. Family assignments and domain architecture in C. elegans are consistent with a corepressor–demethylase role for jmjd-3.1. URL: https://doi.org/10.1371/journal.pgen.1002647 (May 2012). (vandamme2012thec.elegans pages 4-4, vandamme2012thec.elegans pages 8-10)
- Catalytic activity and substrate specificity: Functional and genetic data position jmjd-3.1 as an H3K27me2/3 demethylase acting at specific loci. While triple deletion of jmjd-3.1/3.2/3.3 increases global H3K27me3, single jmjd-3.1 mutants often lack strong global effects, implying locus specificity and partial redundancy with other KDM6 enzymes (UTX-1 being the dominant global H3K27 demethylase). URL: https://doi.org/10.1371/journal.pgen.1002647 (May 2012); supportive functional placement in stress pathways: https://doi.org/10.1016/j.cell.2016.04.012 (May 2016). (vandamme2012thec.elegans pages 4-4, vandamme2012thec.elegans pages 8-10, merkwirth2016twoconservedhistone pages 4-6, merkwirth2016twoconservedhistone pages 1-3)
- Subcellular localization: jmjd-3.1 functions in the nucleus; nuclear entry is required for transcriptional effects. Overexpressed jmjd-3.1::mCherry shows diffuse nuclear localization across multiple tissues in transgenic worms. URL: https://doi.org/10.1016/j.molcel.2015.06.027 (Aug 2015). (labbadia2015repressionofthe pages 6-8)

2) Recent developments and latest research
- Mitochondrial stress reprogramming and longevity: jmjd-3.1 is necessary and sufficient to activate the mitochondrial unfolded protein response (UPRmt) and to mediate transcriptional programs downstream of respiratory-chain perturbation. Overexpression of jmjd-3.1 (under its endogenous promoter) induces UPRmt gene expression and extends lifespan, and this pro-longevity effect requires canonical UPRmt components (ATFS-1, UBL-5, CLPP-1). URL: https://doi.org/10.1016/j.cell.2016.04.012 (May 2016). While not 2023–2024, this remains the most definitive mechanistic study of jmjd-3.1 in stress-induced longevity. (merkwirth2016twoconservedhistone pages 7-10, merkwirth2016twoconservedhistone pages 4-6, merkwirth2016twoconservedhistone pages 6-7)
- Heat-shock response (HSR) maintenance with age: jmjd-3.1 supports stress-gene inducibility during early adulthood. Loss of jmjd-3.1 compromises HSR target induction and survival after heat shock, while overexpression preserves HSR inducibility and stress resilience in aging adults. URL: https://doi.org/10.1016/j.molcel.2015.06.027 (Aug 2015). (labbadia2015repressionofthe pages 6-8)
- KDM6 family context in development and redundancy: Comparative C. elegans work indicates UTX-1 is the predominant enzyme for global H3K27me2/3 removal during development, whereas JMJD3-like paralogs (including jmjd-3.1) contribute more locus-specifically and in stress/aging contexts. URL: https://doi.org/10.1371/journal.pgen.1002647 (May 2012). (vandamme2012thec.elegans pages 4-4, vandamme2012thec.elegans pages 8-10)

3) Current applications and real-world implementations
- Genetic epistasis to place jmjd-3.1 in UPRmt: RNAi against ubl-5 or atfs-1 suppresses UPRmt induction and lifespan extension in jmjd-3.1 overexpressors, establishing dependency on core UPRmt machinery. This has become a common strategy to test UPRmt involvement in long-lived genetic backgrounds. URL: https://doi.org/10.1016/j.cell.2016.04.012 (May 2016). (merkwirth2016twoconservedhistone pages 6-7)
- Chemical probing of H3K27 demethylase activity: The cell-permeable inhibitor GSK-J4 attenuates UPRmt activation in C. elegans, functionally linking H3K27 demethylase activity to mitochondrial stress signaling. URL: https://doi.org/10.1016/j.cell.2016.04.012 (May 2016). (merkwirth2016twoconservedhistone pages 4-6)
- Stress-physiology assays in aging: Heat shock survival, thermotolerance, and late-life transcriptional inducibility assays have used jmjd-3.1 mutants and overexpressors to dissect chromatin control of proteostasis with age. URL: https://doi.org/10.1016/j.molcel.2015.06.027 (Aug 2015). (labbadia2015repressionofthe pages 6-8)

4) Expert opinions and analysis from authoritative sources
- Stress and longevity programs require chromatin remodeling: Cell and Molecular Cell studies conclude that histone demethylases act as upstream effectors that license stress-specific transcriptional programs and lifespan extension. jmjd-3.1/JMJD3 is a conserved arthropod/vertebrate demethylase whose induction or activity correlates with UPRmt output and longevity phenotypes. URLs: https://doi.org/10.1016/j.cell.2016.04.012 (May 2016); https://doi.org/10.1016/j.molcel.2015.06.027 (Aug 2015). (merkwirth2016twoconservedhistone pages 1-3, labbadia2015repressionofthe pages 6-8)
- Developmental vs stress roles: In C. elegans, UTX-1 plays the dominant developmental H3K27 demethylase role (enzymatic activity-independent developmental functions also reported for UTX-1), while jmjd-3.1 contributes more evidently to stress responses and aging pathways under laboratory conditions. URL: https://doi.org/10.1371/journal.pgen.1002647 (May 2012). (vandamme2012thec.elegans pages 4-4, vandamme2012thec.elegans pages 16-16)

5) Statistics and data from recent studies
- Transcriptional overlap with mitochondrial ETC perturbation: RNA-seq comparing jmjd-3.1 overexpression to cco-1(RNAi) ETC knockdown revealed 1,405 overlapping differentially expressed genes, with 99% (1,385/1,405) concordant directionality; UPRmt genes (e.g., hsp-6, dve-1, spg-7) upregulated and nuclear OXPHOS genes broadly downregulated in both contexts. URL: https://doi.org/10.1016/j.cell.2016.04.012 (May 2016). (merkwirth2016twoconservedhistone pages 7-10)
- Genetic dependencies for longevity: Lifespan extension by jmjd-3.1 overexpression is suppressed by ubl-5 RNAi and requires atfs-1 and clpp-1 for UPRmt signaling; jmjd-3.1 knockdown suppresses lifespan extension induced by cco-1(RNAi). URL: https://doi.org/10.1016/j.cell.2016.04.012 (May 2016). (merkwirth2016twoconservedhistone pages 6-7)
- Heat-shock response metrics: jmjd-3.1 null mutants show approximately 60% reduction in heat-shock gene induction and diminished survival/recovery after acute heat stress; jmjd-3.1 overexpression increases thermotolerance and preserves inducibility of stress genes. URL: https://doi.org/10.1016/j.molcel.2015.06.027 (Aug 2015). (labbadia2015repressionofthe pages 6-8)
- Longevity effects in adult worms: In a transgenic context, jmjd-3.1 overexpression increased median lifespan by roughly 20% and maximal lifespan by approximately 12% in day-2 adults, with a concomitant ≈20% reduction in brood size and mitigation of age-related motility and pharyngeal phenotypes. URL: https://doi.org/10.1016/j.molcel.2015.06.027 (Aug 2015). (labbadia2015repressionofthe pages 6-8)

Biological processes and pathways
- Mitochondrial UPR pathway positioning: jmjd-3.1 acts upstream of UPRmt transcriptional modules and requires UBL-5 and ATFS-1. Its overexpression is sufficient to recapitulate most of the ETC perturbation–driven transcriptome, emphasizing a chromatin-priming role for mitochondrial stress responses. URL: https://doi.org/10.1016/j.cell.2016.04.012 (May 2016). (merkwirth2016twoconservedhistone pages 7-10, merkwirth2016twoconservedhistone pages 6-7)
- Heat-shock response and proteostasis: jmjd-3.1 maintains stress gene inducibility during the reproductive transition, when the HSR is normally repressed, highlighting a role in age-related proteostasis decline. Nuclear localization is necessary for these effects. URL: https://doi.org/10.1016/j.molcel.2015.06.027 (Aug 2015). (labbadia2015repressionofthe pages 6-8)
- Development and H3K27 demethylation landscape: Family-level work shows UTX-1 strongly controls developmental H3K27me2/3 levels, while jmjd-3.1 and paralogs modulate specific gene sets and contribute to stress/aging programs. Triple deletion of JMJD3-like genes increases global H3K27me3, yet animals remain viable, consistent with nonessential developmental roles for jmjd-3.1 under standard conditions. URL: https://doi.org/10.1371/journal.pgen.1002647 (May 2012). (vandamme2012thec.elegans pages 4-4, vandamme2012thec.elegans pages 8-10)

Subcellular localization and expression
- Localization: Nuclear; nuclear entry is required for transcriptional reprogramming. URL: https://doi.org/10.1016/j.molcel.2015.06.027 (Aug 2015). (labbadia2015repressionofthe pages 6-8)
- Tissue expression: Reporter and qPCR data indicate expression in neurons, intestine, muscle, and hypodermis in overexpression lines; endogenous jmjd-3.1 is expressed at levels comparable to utx-1, whereas jmjd-3.2/3.3 are weaker. URL: https://doi.org/10.1371/journal.pgen.1002647 (May 2012); https://doi.org/10.1016/j.molcel.2015.06.027 (Aug 2015). (vandamme2012thec.elegans pages 4-4, labbadia2015repressionofthe pages 6-8)

Interaction partners and complexes
- jmjd-3.1 partners are not firmly established in the retrieved literature. By contrast, the related UTX-1 co-purifies with SET-16/MLL-like complexes, suggesting that while UTX-1 integrates into large chromatin assemblies, jmjd-3.1 may be more locus-specific or conditionally recruited during stress responses. URL: https://doi.org/10.1371/journal.pgen.1002647 (May 2012). (vandamme2012thec.elegans pages 4-4, vandamme2012thec.elegans pages 16-16)

Ambiguity check and symbol verification
- The symbol “jmjd-3.1” in C. elegans refers specifically to the JMJD3-like KDM6 family demethylase encoded by F18E9.5; this is distinct from human JMJD3/KDM6B. All claims herein refer to the C. elegans protein matching UniProt Q95QK3. (vandamme2012thec.elegans pages 4-4)

Limitations and open questions
- Direct biochemical assays in C. elegans establishing jmjd-3.1’s kinetic parameters and genome-wide H3K27 substrate maps under defined stresses remain areas for expansion. Most precise pathway placement derives from genetic/chemical epistasis and transcriptomics. While 2023–2024 nematode reviews acknowledge the KDM6/JMJD3 role in embryonic chromatin and stress physiology, the definitive mechanistic jmjd-3.1 studies remain the 2012–2016 primary literature cited here. (merkwirth2016twoconservedhistone pages 7-10, vandamme2012thec.elegans pages 4-4)

Practical takeaways
- Primary function: H3K27me2/3 demethylase that licenses stress-responsive transcriptional programs, notably UPRmt and aspects of the HSR, in the nucleus. (merkwirth2016twoconservedhistone pages 7-10, labbadia2015repressionofthe pages 6-8, vandamme2012thec.elegans pages 4-4)
- Localization and context: Nuclear demethylase acting at select loci; functions prominently under mitochondrial stress and during early adult proteostasis transitions. (merkwirth2016twoconservedhistone pages 7-10, labbadia2015repressionofthe pages 6-8)
- Pathways: UPRmt (requires ATFS-1, UBL-5, CLPP-1), with reported effects on heat-shock inducibility and longevity; developmental H3K27 regulation predominantly mediated by UTX-1. (merkwirth2016twoconservedhistone pages 6-7, labbadia2015repressionofthe pages 6-8, vandamme2012thec.elegans pages 4-4)

Key evidence table
| Aspect | Key finding (1–3 sentences) | Quantitative details | Organism/context | Source | Citation IDs |
|---|---|---:|---|---|---|
| Identity / family / domains | jmjd-3.1 is a JMJD3-like member of the KDM6 (UTX/JMJD3) family; contains a JmjC catalytic domain and corepressor‑demethylase annotations (matches UniProt Q95QK3 / ORF F18E9.5). | — | Caenorhabditis elegans | Vandamme et al., PLoS Genet (2012) - https://doi.org/10.1371/journal.pgen.1002647 | (vandamme2012thec.elegans pages 4-4) |
| Catalytic activity & substrate | Evidence consistent with H3K27me2/3 demethylase activity (JmjC catalytic motif present); contributes to removal of H3K27me3 at specific loci rather than globally (UTX-1 is dominant global demethylase). | Triple jmjd-3.1/3.2/3.3 deletions ↑ global H3K27me3; single jmjd-3.1 loss often shows little global change. | C. elegans; biochemical/ genetics | Merkwirth et al., Cell (2016) - https://doi.org/10.1016/j.cell.2016.04.012; Vandamme et al., PLoS Genet (2012) - https://doi.org/10.1371/journal.pgen.1002647 | (merkwirth2016twoconservedhistone pages 7-10, vandamme2012thec.elegans pages 4-4) |
| Subcellular localization | jmjd-3.1 shows diffuse nuclear localization; nuclear entry is required for its transcriptional effects (nuclear targeting needed for overexpression phenotypes). | Overexpressed jmjd-3.1::mCherry line shows ~30-fold higher expression than WT (transgenic context). | C. elegans; transgenic reporter studies | Labbadia & Morimoto, Mol Cell (2015) - https://doi.org/10.1016/j.molcel.2015.06.027 | (labbadia2015repressionofthe pages 6-8) |
| Expression / tissue pattern | Expressed in multiple somatic tissues (reported in neurons, intestine, muscle, hypodermis for overexpression reporter); endogenous jmjd-3.1 expressed at levels comparable to utx-1, while jmjd-3.2/3.3 are weaker. | Endogenous comparisons reported qualitatively; transgenic overexpression ≈30× WT (reporter line). | C. elegans | Vandamme et al., PLoS Genet (2012); Labbadia & Morimoto (2015) - https://doi.org/10.1371/journal.pgen.1002647; https://doi.org/10.1016/j.molcel.2015.06.027 | (vandamme2012thec.elegans pages 4-4, labbadia2015repressionofthe pages 6-8) |
| Heat shock response role | jmjd-3.1 is implicated in regulating heat-shock/stress-gene induction: loss reduces stress-induced HSR gene activation and survival after heat shock; overexpression preserves inducibility and increases thermotolerance. | jmjd-3.1 nulls show ~60% reduction in stress-induced HSR gene expression; overexpression increases median and maximal lifespan by ~20% and ~12% respectively in one report (day-2 adults) and reduces brood size ≈20% (transgenic context). | C. elegans; stress assays, transgenics | Labbadia & Morimoto, Mol Cell (2015) - https://doi.org/10.1016/j.molcel.2015.06.027 | (labbadia2015repressionofthe pages 6-8) |
| Mitochondrial UPR (UPRmt) role | jmjd-3.1 is necessary and sufficient to induce the mitochondrial unfolded protein response (UPRmt) and to mediate transcriptional programs downstream of mitochondrial ETC perturbation; acts upstream of core UPRmt factors. | Overexpression overlaps cco-1 RNAi transcriptional response: 1,405 overlapping genes with 99% concordance; pharmacologic inhibitor GSK-J4 blocks UPRmt activation. | C. elegans; UPRmt reporter and RNA‑seq | Merkwirth et al., Cell (2016) - https://doi.org/10.1016/j.cell.2016.04.012 | (merkwirth2016twoconservedhistone pages 7-10) |
| Longevity effects & dependencies | jmjd-3.1 overexpression extends lifespan; jmjd-3.1 is required for ETC/mitochondrial‑stress induced longevity and its lifespan effects depend on UPRmt components. | Lifespan extension reported with jmjd-3.1 OE (percent change context-dependent; Labbadia reported ~20% median increase for OE line); ubl-5, atfs-1, clpp-1 RNAi suppress jmjd-3.1 OE lifespan extension; jmjd-3.1 RNAi suppresses cco-1–mediated longevity. | C. elegans; genetic epistasis & RNAi | Merkwirth et al., Cell (2016) - https://doi.org/10.1016/j.cell.2016.04.012; Labbadia & Morimoto (2015) - https://doi.org/10.1016/j.molcel.2015.06.027 | (merkwirth2016twoconservedhistone pages 7-10, labbadia2015repressionofthe pages 6-8) |
| Developmental phenotypes | Single jmjd-3.1 mutants are viable with minor/no strong global developmental defects; combined deletion of JMJD3-like genes yields increased H3K27me3 but animals remain largely viable (suggesting redundancy or limited developmental requirement). | Triple jmjd-3.1/3.2/3.3 deletion increased global H3K27me3 but animals remained fertile/viable with modest gonadal defects; utx-1 shows stronger developmental necessity. | C. elegans; genetic deletion studies | Vandamme et al., PLoS Genet (2012) - https://doi.org/10.1371/journal.pgen.1002647 | (vandamme2012thec.elegans pages 4-4) |
| Specificity vs other stress pathways | Evidence is context-dependent: Merkwirth et al. report jmjd-3.1 specifically affects UPRmt with little effect on ER UPR or antioxidant reporters; Labbadia et al. report jmjd-3.1 influences heat-shock response—implying pathway-specific and experimental-condition differences. | Merkwirth: little/no effect on hsp-4p::gfp (ER UPR) or hsp-16.2p::gfp (HSR) in their assays; Labbadia: ~60% reduction in HS gene induction in jmjd-3.1 nulls. | C. elegans; stress-pathway assays | Merkwirth et al., Cell (2016) - https://doi.org/10.1016/j.cell.2016.04.012; Labbadia & Morimoto (2015) - https://doi.org/10.1016/j.molcel.2015.06.027 | (merkwirth2016twoconservedhistone pages 7-10, labbadia2015repressionofthe pages 6-8) |
| Interaction partners / complexes | Direct interaction partners for jmjd-3.1 are not well defined in available studies; by contrast UTX‑1 was biochemically found in complexes with SET‑16 (MLL‑like) and associated chromatin regulators, suggesting jmjd-3.1 may act more locus‑specifically while UTX‑1 engages multi‑subunit complexes. | UTX‑1 biochemical complex membership reported (SET‑16); jmjd-3.1 partners not specified in retrieved literature. | C. elegans; biochemical pulldown/genetics | Vandamme et al., PLoS Genet (2012) - https://doi.org/10.1371/journal.pgen.1002647 | (vandamme2012thec.elegans pages 4-4, vandamme2012thec.elegans pages 16-16) |

Table: Concise, source-linked summary of experimental evidence for C. elegans jmjd-3.1 (UniProt Q95QK3), covering identity, catalytic activity, localization, pathway roles, phenotypes and quantitative outcomes from Vandamme 2012, Merkwirth 2016, and Labbadia 2015.

References

1. (vandamme2012thec.elegans pages 4-4): Julien Vandamme, Gaëlle Lettier, Simone Sidoli, Elia Di Schiavi, Ole Nørregaard Jensen, and Anna Elisabetta Salcini. The c. elegans h3k27 demethylase utx-1 is essential for normal development, independent of its enzymatic activity. PLoS Genetics, 8:e1002647, May 2012. URL: https://doi.org/10.1371/journal.pgen.1002647, doi:10.1371/journal.pgen.1002647. This article has 84 citations and is from a domain leading peer-reviewed journal.

2. (vandamme2012thec.elegans pages 8-10): Julien Vandamme, Gaëlle Lettier, Simone Sidoli, Elia Di Schiavi, Ole Nørregaard Jensen, and Anna Elisabetta Salcini. The c. elegans h3k27 demethylase utx-1 is essential for normal development, independent of its enzymatic activity. PLoS Genetics, 8:e1002647, May 2012. URL: https://doi.org/10.1371/journal.pgen.1002647, doi:10.1371/journal.pgen.1002647. This article has 84 citations and is from a domain leading peer-reviewed journal.

3. (merkwirth2016twoconservedhistone pages 4-6): Carsten Merkwirth, Virginija Jovaisaite, Jenni Durieux, Olli Matilainen, Sabine D. Jordan, Pedro M. Quiros, Kristan K. Steffen, Evan G. Williams, Laurent Mouchiroud, Sarah U. Tronnes, Virginia Murillo, Suzanne C. Wolff, Reuben J. Shaw, Johan Auwerx, and Andrew Dillin. Two conserved histone demethylases regulate mitochondrial stress-induced longevity. Cell, 165:1209-1223, May 2016. URL: https://doi.org/10.1016/j.cell.2016.04.012, doi:10.1016/j.cell.2016.04.012. This article has 388 citations and is from a highest quality peer-reviewed journal.

4. (merkwirth2016twoconservedhistone pages 1-3): Carsten Merkwirth, Virginija Jovaisaite, Jenni Durieux, Olli Matilainen, Sabine D. Jordan, Pedro M. Quiros, Kristan K. Steffen, Evan G. Williams, Laurent Mouchiroud, Sarah U. Tronnes, Virginia Murillo, Suzanne C. Wolff, Reuben J. Shaw, Johan Auwerx, and Andrew Dillin. Two conserved histone demethylases regulate mitochondrial stress-induced longevity. Cell, 165:1209-1223, May 2016. URL: https://doi.org/10.1016/j.cell.2016.04.012, doi:10.1016/j.cell.2016.04.012. This article has 388 citations and is from a highest quality peer-reviewed journal.

5. (labbadia2015repressionofthe pages 6-8): Johnathan Labbadia and Richard I. Morimoto. Repression of the heat shock response is a programmed event at the onset of reproduction. Molecular cell, 59 4:639-50, Aug 2015. URL: https://doi.org/10.1016/j.molcel.2015.06.027, doi:10.1016/j.molcel.2015.06.027. This article has 365 citations and is from a highest quality peer-reviewed journal.

6. (merkwirth2016twoconservedhistone pages 7-10): Carsten Merkwirth, Virginija Jovaisaite, Jenni Durieux, Olli Matilainen, Sabine D. Jordan, Pedro M. Quiros, Kristan K. Steffen, Evan G. Williams, Laurent Mouchiroud, Sarah U. Tronnes, Virginia Murillo, Suzanne C. Wolff, Reuben J. Shaw, Johan Auwerx, and Andrew Dillin. Two conserved histone demethylases regulate mitochondrial stress-induced longevity. Cell, 165:1209-1223, May 2016. URL: https://doi.org/10.1016/j.cell.2016.04.012, doi:10.1016/j.cell.2016.04.012. This article has 388 citations and is from a highest quality peer-reviewed journal.

7. (merkwirth2016twoconservedhistone pages 6-7): Carsten Merkwirth, Virginija Jovaisaite, Jenni Durieux, Olli Matilainen, Sabine D. Jordan, Pedro M. Quiros, Kristan K. Steffen, Evan G. Williams, Laurent Mouchiroud, Sarah U. Tronnes, Virginia Murillo, Suzanne C. Wolff, Reuben J. Shaw, Johan Auwerx, and Andrew Dillin. Two conserved histone demethylases regulate mitochondrial stress-induced longevity. Cell, 165:1209-1223, May 2016. URL: https://doi.org/10.1016/j.cell.2016.04.012, doi:10.1016/j.cell.2016.04.012. This article has 388 citations and is from a highest quality peer-reviewed journal.

8. (vandamme2012thec.elegans pages 16-16): Julien Vandamme, Gaëlle Lettier, Simone Sidoli, Elia Di Schiavi, Ole Nørregaard Jensen, and Anna Elisabetta Salcini. The c. elegans h3k27 demethylase utx-1 is essential for normal development, independent of its enzymatic activity. PLoS Genetics, 8:e1002647, May 2012. URL: https://doi.org/10.1371/journal.pgen.1002647, doi:10.1371/journal.pgen.1002647. This article has 84 citations and is from a domain leading peer-reviewed journal.

Citations

1. labbadia2015repressionofthe pages 6-8
2. merkwirth2016twoconservedhistone pages 6-7
3. merkwirth2016twoconservedhistone pages 4-6
4. merkwirth2016twoconservedhistone pages 7-10
5. merkwirth2016twoconservedhistone pages 1-3
6. https://doi.org/10.1371/journal.pgen.1002647
7. https://doi.org/10.1016/j.cell.2016.04.012
8. https://doi.org/10.1016/j.molcel.2015.06.027
9. https://doi.org/10.1016/j.cell.2016.04.012;
10. https://doi.org/10.1371/journal.pgen.1002647;
11. https://doi.org/10.1371/journal.pgen.1002647,
12. https://doi.org/10.1016/j.cell.2016.04.012,
13. https://doi.org/10.1016/j.molcel.2015.06.027,