{"gene":"DCP1B","run_date":"2026-06-09T23:54:41","timeline":{"discoveries":[{"year":2024,"finding":"Human DCP1b is a cofactor of the mRNA decapping enzyme DCP2; the EVH1 domain of DCP1 enhances the mRNA-binding affinity of DCP2. DCP1b knockout cells show distinct transcriptome and metabolome changes compared to DCP1a knockouts, demonstrating paralog-specific regulation of endogenous mRNA targets and biological processes.","method":"DCP1a/DCP1b knockout cell lines, transcriptome analysis, metabolome analysis, biochemical characterization of EVH1 domain function","journal":"eLife","confidence":"High","confidence_rationale":"Tier 2 / Moderate — clean KO cell lines with defined cellular and molecular phenotypes, multiple orthogonal methods (transcriptomics, metabolomics, domain functional assay) in a single rigorous study","pmids":["39485278"],"is_preprint":false},{"year":2024,"finding":"DCP1b is a non-redundant cofactor of DCP2 with a unique role in decapping complex interactions with protein degradation and translational machinery, distinct from DCP1a which is required for decapping complex assembly and interactions with mRNA cap-binding proteins. DCP1a and DCP1b regulate turnover of distinct sets of mRNAs.","method":"Functional dissection using DCP1a and DCP1b knockdown/knockout, decapping complex interaction assays, mRNA turnover analysis","journal":"Life science alliance","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal functional dissection of two paralogs with multiple orthogonal methods (complex integrity assays, mRNA turnover, interaction studies), replicated conceptually by independent lab (PMID:39485278)","pmids":["39256052"],"is_preprint":false},{"year":2025,"finding":"p53 transcriptionally activates DCP1B expression. DCP1B promotes the turnover of MAPK4 mRNA, thereby reducing MAPK4 protein levels. Reduced MAPK4 suppresses AKT phosphorylation independent of PI3K, sensitizing NSCLC cells to PI3K inhibitors. DCP1B overexpression inhibits NSCLC cell growth and migration.","method":"p53 transcriptional activation assays, DCP1B overexpression/knockdown, mRNA decay assays for MAPK4, AKT phosphorylation assays, in vitro and in vivo proliferation assays","journal":"Cell death and differentiation","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods in a single lab (transcriptional activation, mRNA turnover, signaling readouts, in vivo xenograft), no independent replication","pmids":["40200093"],"is_preprint":false},{"year":2024,"finding":"DCP1b localizes to processing bodies (P-bodies), which contain RNA decay machinery. During West Nile, Zika, or dengue virus infection, sfRNAs accumulate in P-bodies containing DCP1b, but upon RNase L activation sfRNAs re-localize away from P-bodies (including DCP1b-containing structures) to RNase L-induced bodies, coinciding with increased viral RNA decay.","method":"Single-molecule RNA fluorescence in situ hybridization (smRNA-FISH), co-localization imaging of DCP1b with viral sfRNAs during infection","journal":"Cell reports","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — direct imaging-based localization with functional consequence (viral RNA decay), single lab, single primary method (smRNA-FISH)","pmids":["39196777"],"is_preprint":false},{"year":2023,"finding":"DCP1B was identified as a proximity interactor of GSK-3α (preferentially over GSK-3β) by BioID proximity-dependent biotinylation mass spectrometry, and reciprocal interaction was evaluated, suggesting DCP1B associates with the GSK-3α isoform.","method":"Affinity purification mass spectrometry and BioID proximity labeling in HEK293 and HeLa cells, reciprocal interaction assessment","journal":"Journal of proteome research","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, BioID proximity labeling (not direct binding), reciprocal validation mentioned but not detailed in abstract","pmids":["36779422"],"is_preprint":false}],"current_model":"DCP1b is a paralog-specific cofactor of the mRNA decapping enzyme DCP2 that enhances DCP2's mRNA-binding affinity via its EVH1 domain, localizes to cytoplasmic processing bodies (P-bodies), and non-redundantly regulates the turnover of distinct subsets of mRNAs (including MAPK4 mRNA downstream of p53 activation) through unique interactions with protein degradation and translational machinery, distinguishing it functionally from its paralog DCP1a."},"narrative":{"mechanistic_narrative":"DCP1B is a paralog-specific cofactor of the mRNA decapping enzyme DCP2 that controls the turnover of distinct subsets of cytoplasmic mRNAs [PMID:39485278, PMID:39256052]. Its EVH1 domain enhances the mRNA-binding affinity of DCP2, and loss of DCP1B produces transcriptome and metabolome changes distinct from those caused by loss of its paralog DCP1a, establishing non-redundant regulation of endogenous targets [PMID:39485278]. Functionally, DCP1B is distinguished from DCP1a by its unique role in coupling the decapping complex to protein-degradation and translational machinery, whereas DCP1a drives decapping-complex assembly and interactions with cap-binding proteins [PMID:39256052]. DCP1B localizes to cytoplasmic processing bodies that concentrate RNA decay machinery [PMID:39196777]. Within a regulatory program, p53 transcriptionally activates DCP1B, which promotes MAPK4 mRNA turnover to lower MAPK4 protein, thereby suppressing PI3K-independent AKT phosphorylation and restraining NSCLC cell growth and migration [PMID:40200093].","teleology":[{"year":2024,"claim":"Establishing that DCP1B is not a redundant copy of DCP1a but a distinct decapping cofactor answered whether the two paralogs serve separable functions in mRNA turnover.","evidence":"Reciprocal functional dissection of DCP1a and DCP1b by knockdown/knockout, decapping-complex interaction assays, and mRNA turnover analysis","pmids":["39256052"],"confidence":"High","gaps":["The specific protein-degradation and translational machinery components engaged by DCP1B are not enumerated","Which mRNA features dictate DCP1B versus DCP1a target selectivity is unresolved"]},{"year":2024,"claim":"Defining the EVH1 domain's biochemical contribution and mapping paralog-specific endogenous consequences clarified how DCP1B mechanistically supports DCP2 and shapes cellular state.","evidence":"DCP1a/DCP1b knockout cell lines with transcriptomics, metabolomics, and biochemical EVH1 domain functional assays","pmids":["39485278"],"confidence":"High","gaps":["Structural basis for how the EVH1 domain enhances DCP2 mRNA-binding affinity is not resolved","Direct endogenous mRNA substrates of DCP1B were not individually identified"]},{"year":2024,"claim":"Imaging placed DCP1B within P-bodies and linked its compartment to viral RNA fate, addressing where DCP1B acts and how its decay environment is remodeled during infection.","evidence":"Single-molecule RNA FISH and co-localization of DCP1b with flaviviral sfRNAs during West Nile, Zika, and dengue infection","pmids":["39196777"],"confidence":"Medium","gaps":["Single primary method (smRNA-FISH) from one lab","Whether DCP1B directly catalyzes or recruits machinery for sfRNA decay is not demonstrated"]},{"year":2025,"claim":"Connecting DCP1B to a p53-driven program answered how its decapping activity is regulated transcriptionally and translated into a tumor-suppressive signaling outcome.","evidence":"p53 transcriptional activation assays, DCP1B perturbation, MAPK4 mRNA decay assays, AKT phosphorylation readouts, and in vitro/in vivo NSCLC proliferation assays","pmids":["40200093"],"confidence":"Medium","gaps":["No independent replication of the p53–DCP1B–MAPK4 axis","Whether MAPK4 mRNA is a direct DCP1B/DCP2 decapping substrate is not biochemically established"]},{"year":2023,"claim":"A proximity-labeling screen flagged DCP1B as an isoform-selective GSK-3α associate, raising the possibility of links between decapping and kinase signaling.","evidence":"AP-MS and BioID proximity labeling in HEK293 and HeLa cells with reciprocal interaction assessment","pmids":["36779422"],"confidence":"Low","gaps":["Proximity labeling does not establish direct binding and reciprocal validation was not detailed","Functional consequence of any DCP1B–GSK-3α association is unknown"]},{"year":null,"claim":"The direct endogenous mRNA substrates of DCP1B and the molecular basis of its selectivity over DCP1a remain undefined.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No genome-wide direct-substrate map for DCP1B","Structural mechanism of EVH1-mediated DCP2 enhancement unresolved","Identity of the protein-degradation/translational partners distinguishing DCP1B from DCP1a not established"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[0,1]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,1]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[3]}],"pathway":[{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[0,1]}],"complexes":["mRNA decapping complex"],"partners":["DCP2"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q8IZD4","full_name":"mRNA-decapping enzyme 1B","aliases":[],"length_aa":617,"mass_kda":67.7,"function":"May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (By similarity)","subcellular_location":"Cytoplasm; Nucleus","url":"https://www.uniprot.org/uniprotkb/Q8IZD4/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/DCP1B","classification":"Not Classified","n_dependent_lines":0,"n_total_lines":1208,"dependency_fraction":0.0},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000151065","cell_line_id":"CID000835","localizations":[{"compartment":"vesicles","grade":3}],"interactors":[{"gene":"DCP1A","stoichiometry":10.0},{"gene":"ARHGAP18","stoichiometry":0.2},{"gene":"CLTA","stoichiometry":0.2},{"gene":"CLTB","stoichiometry":0.2},{"gene":"CSNK2A1","stoichiometry":0.2},{"gene":"DDX6","stoichiometry":0.2},{"gene":"SEC16A","stoichiometry":0.2},{"gene":"CEPT1","stoichiometry":0.2},{"gene":"EDC3","stoichiometry":0.2},{"gene":"TNRC6B","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID000835","total_profiled":1310},"omim":[{"mim_id":"614660","title":"PAT1 HOMOLOG 1, PROCESSING BODY mRNA DECAY FACTOR; PATL1","url":"https://www.omim.org/entry/614660"},{"mim_id":"609843","title":"DECAPPING mRNA 1B; DCP1B","url":"https://www.omim.org/entry/609843"},{"mim_id":"607010","title":"DECAPPING mRNA 1A; DCP1A","url":"https://www.omim.org/entry/607010"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Vesicles","reliability":"Supported"},{"location":"Cytosol","reliability":"Supported"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/DCP1B"},"hgnc":{"alias_symbol":["FLJ31638"],"prev_symbol":[]},"alphafold":{"accession":"Q8IZD4","domains":[{"cath_id":"2.30.29.30","chopping":"28-140","consensus_level":"high","plddt":92.436,"start":28,"end":140}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8IZD4","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q8IZD4-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q8IZD4-F1-predicted_aligned_error_v6.png","plddt_mean":56.94},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=DCP1B","jax_strain_url":"https://www.jax.org/strain/search?query=DCP1B"},"sequence":{"accession":"Q8IZD4","fasta_url":"https://rest.uniprot.org/uniprotkb/Q8IZD4.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q8IZD4/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8IZD4"}},"corpus_meta":[{"pmid":"37033211","id":"PMC_37033211","title":"Microvascular and macrovascular complications of type 2 diabetes mellitus: Exome wide association analyses.","date":"2023","source":"Frontiers in endocrinology","url":"https://pubmed.ncbi.nlm.nih.gov/37033211","citation_count":71,"is_preprint":false},{"pmid":"30804981","id":"PMC_30804981","title":"Integrative Analysis of Transcriptome and GWAS Data to Identify the Hub Genes Associated With Milk Yield Trait in Buffalo.","date":"2019","source":"Frontiers in genetics","url":"https://pubmed.ncbi.nlm.nih.gov/30804981","citation_count":55,"is_preprint":false},{"pmid":"25071529","id":"PMC_25071529","title":"MicroRNA-138 is a potential regulator of memory performance in humans.","date":"2014","source":"Frontiers in human neuroscience","url":"https://pubmed.ncbi.nlm.nih.gov/25071529","citation_count":53,"is_preprint":false},{"pmid":"24659297","id":"PMC_24659297","title":"Dysregulated expression of lipid storage and membrane dynamics factors in Tia1 knockout mouse nervous 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transcriptionally activates DCP1B to suppress tumor progression and enhance tumor sensitivity to PI3K blockade in non-small cell lung cancer.","date":"2025","source":"Cell death and differentiation","url":"https://pubmed.ncbi.nlm.nih.gov/40200093","citation_count":4,"is_preprint":false},{"pmid":"37549410","id":"PMC_37549410","title":"Candidate biomarkers and persistent transcriptional responses after low and high dose ionizing radiation at high dose rate.","date":"2023","source":"International journal of radiation biology","url":"https://pubmed.ncbi.nlm.nih.gov/37549410","citation_count":4,"is_preprint":false},{"pmid":"39485278","id":"PMC_39485278","title":"Human DCP1 is crucial for mRNA decapping and possesses paralog-specific gene regulating functions.","date":"2024","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/39485278","citation_count":3,"is_preprint":false},{"pmid":"39256052","id":"PMC_39256052","title":"Non-redundant roles for the human mRNA decapping cofactor paralogs 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DCP1b knockout cells show distinct transcriptome and metabolome changes compared to DCP1a knockouts, demonstrating paralog-specific regulation of endogenous mRNA targets and biological processes.\",\n      \"method\": \"DCP1a/DCP1b knockout cell lines, transcriptome analysis, metabolome analysis, biochemical characterization of EVH1 domain function\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean KO cell lines with defined cellular and molecular phenotypes, multiple orthogonal methods (transcriptomics, metabolomics, domain functional assay) in a single rigorous study\",\n      \"pmids\": [\"39485278\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"DCP1b is a non-redundant cofactor of DCP2 with a unique role in decapping complex interactions with protein degradation and translational machinery, distinct from DCP1a which is required for decapping complex assembly and interactions with mRNA cap-binding proteins. DCP1a and DCP1b regulate turnover of distinct sets of mRNAs.\",\n      \"method\": \"Functional dissection using DCP1a and DCP1b knockdown/knockout, decapping complex interaction assays, mRNA turnover analysis\",\n      \"journal\": \"Life science alliance\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal functional dissection of two paralogs with multiple orthogonal methods (complex integrity assays, mRNA turnover, interaction studies), replicated conceptually by independent lab (PMID:39485278)\",\n      \"pmids\": [\"39256052\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"p53 transcriptionally activates DCP1B expression. DCP1B promotes the turnover of MAPK4 mRNA, thereby reducing MAPK4 protein levels. Reduced MAPK4 suppresses AKT phosphorylation independent of PI3K, sensitizing NSCLC cells to PI3K inhibitors. DCP1B overexpression inhibits NSCLC cell growth and migration.\",\n      \"method\": \"p53 transcriptional activation assays, DCP1B overexpression/knockdown, mRNA decay assays for MAPK4, AKT phosphorylation assays, in vitro and in vivo proliferation assays\",\n      \"journal\": \"Cell death and differentiation\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods in a single lab (transcriptional activation, mRNA turnover, signaling readouts, in vivo xenograft), no independent replication\",\n      \"pmids\": [\"40200093\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"DCP1b localizes to processing bodies (P-bodies), which contain RNA decay machinery. During West Nile, Zika, or dengue virus infection, sfRNAs accumulate in P-bodies containing DCP1b, but upon RNase L activation sfRNAs re-localize away from P-bodies (including DCP1b-containing structures) to RNase L-induced bodies, coinciding with increased viral RNA decay.\",\n      \"method\": \"Single-molecule RNA fluorescence in situ hybridization (smRNA-FISH), co-localization imaging of DCP1b with viral sfRNAs during infection\",\n      \"journal\": \"Cell reports\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — direct imaging-based localization with functional consequence (viral RNA decay), single lab, single primary method (smRNA-FISH)\",\n      \"pmids\": [\"39196777\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"DCP1B was identified as a proximity interactor of GSK-3α (preferentially over GSK-3β) by BioID proximity-dependent biotinylation mass spectrometry, and reciprocal interaction was evaluated, suggesting DCP1B associates with the GSK-3α isoform.\",\n      \"method\": \"Affinity purification mass spectrometry and BioID proximity labeling in HEK293 and HeLa cells, reciprocal interaction assessment\",\n      \"journal\": \"Journal of proteome research\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, BioID proximity labeling (not direct binding), reciprocal validation mentioned but not detailed in abstract\",\n      \"pmids\": [\"36779422\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"DCP1b is a paralog-specific cofactor of the mRNA decapping enzyme DCP2 that enhances DCP2's mRNA-binding affinity via its EVH1 domain, localizes to cytoplasmic processing bodies (P-bodies), and non-redundantly regulates the turnover of distinct subsets of mRNAs (including MAPK4 mRNA downstream of p53 activation) through unique interactions with protein degradation and translational machinery, distinguishing it functionally from its paralog DCP1a.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"DCP1B is a paralog-specific cofactor of the mRNA decapping enzyme DCP2 that controls the turnover of distinct subsets of cytoplasmic mRNAs [#0, #1]. Its EVH1 domain enhances the mRNA-binding affinity of DCP2, and loss of DCP1B produces transcriptome and metabolome changes distinct from those caused by loss of its paralog DCP1a, establishing non-redundant regulation of endogenous targets [#0]. Functionally, DCP1B is distinguished from DCP1a by its unique role in coupling the decapping complex to protein-degradation and translational machinery, whereas DCP1a drives decapping-complex assembly and interactions with cap-binding proteins [#1]. DCP1B localizes to cytoplasmic processing bodies that concentrate RNA decay machinery [#3]. Within a regulatory program, p53 transcriptionally activates DCP1B, which promotes MAPK4 mRNA turnover to lower MAPK4 protein, thereby suppressing PI3K-independent AKT phosphorylation and restraining NSCLC cell growth and migration [#2].\",\n  \"teleology\": [\n    {\n      \"year\": 2024,\n      \"claim\": \"Establishing that DCP1B is not a redundant copy of DCP1a but a distinct decapping cofactor answered whether the two paralogs serve separable functions in mRNA turnover.\",\n      \"evidence\": \"Reciprocal functional dissection of DCP1a and DCP1b by knockdown/knockout, decapping-complex interaction assays, and mRNA turnover analysis\",\n      \"pmids\": [\"39256052\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"The specific protein-degradation and translational machinery components engaged by DCP1B are not enumerated\",\n        \"Which mRNA features dictate DCP1B versus DCP1a target selectivity is unresolved\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Defining the EVH1 domain's biochemical contribution and mapping paralog-specific endogenous consequences clarified how DCP1B mechanistically supports DCP2 and shapes cellular state.\",\n      \"evidence\": \"DCP1a/DCP1b knockout cell lines with transcriptomics, metabolomics, and biochemical EVH1 domain functional assays\",\n      \"pmids\": [\"39485278\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural basis for how the EVH1 domain enhances DCP2 mRNA-binding affinity is not resolved\",\n        \"Direct endogenous mRNA substrates of DCP1B were not individually identified\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Imaging placed DCP1B within P-bodies and linked its compartment to viral RNA fate, addressing where DCP1B acts and how its decay environment is remodeled during infection.\",\n      \"evidence\": \"Single-molecule RNA FISH and co-localization of DCP1b with flaviviral sfRNAs during West Nile, Zika, and dengue infection\",\n      \"pmids\": [\"39196777\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single primary method (smRNA-FISH) from one lab\",\n        \"Whether DCP1B directly catalyzes or recruits machinery for sfRNA decay is not demonstrated\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Connecting DCP1B to a p53-driven program answered how its decapping activity is regulated transcriptionally and translated into a tumor-suppressive signaling outcome.\",\n      \"evidence\": \"p53 transcriptional activation assays, DCP1B perturbation, MAPK4 mRNA decay assays, AKT phosphorylation readouts, and in vitro/in vivo NSCLC proliferation assays\",\n      \"pmids\": [\"40200093\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No independent replication of the p53\\u2013DCP1B\\u2013MAPK4 axis\",\n        \"Whether MAPK4 mRNA is a direct DCP1B/DCP2 decapping substrate is not biochemically established\"\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"A proximity-labeling screen flagged DCP1B as an isoform-selective GSK-3\\u03b1 associate, raising the possibility of links between decapping and kinase signaling.\",\n      \"evidence\": \"AP-MS and BioID proximity labeling in HEK293 and HeLa cells with reciprocal interaction assessment\",\n      \"pmids\": [\"36779422\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Proximity labeling does not establish direct binding and reciprocal validation was not detailed\",\n        \"Functional consequence of any DCP1B\\u2013GSK-3\\u03b1 association is unknown\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The direct endogenous mRNA substrates of DCP1B and the molecular basis of its selectivity over DCP1a remain undefined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No genome-wide direct-substrate map for DCP1B\",\n        \"Structural mechanism of EVH1-mediated DCP2 enhancement unresolved\",\n        \"Identity of the protein-degradation/translational partners distinguishing DCP1B from DCP1a not established\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [\"mRNA decapping complex\"],\n    \"partners\": [\"DCP2\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":5,"faith_total":5,"faith_pct":100.0}}