{ "uniprot_canonical_ac": "A0JPN4-1", "sequence": { "header": "sp|A0JPN4-1|ZC12A_RAT Isoform 1 of Endoribonuclease ZC3H12A OS=Rattus norvegicus OX=10116 GN=Zc3h12a PE=2 SV=1 CANONICAL=A0JPN4-1", "length": 596, "sequence": "MSDPCGKKLVQEISPTMSLWGLEDRHSCQGQPQPDQDPVAKEASASELQMKVDFFRKLGYSSSEIHSALQKLGVQADTNTVLGELVKHGSATERECQASTDPCPQPPLVPRGGSTPKPSTVEPSLPEEDKESSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAYESDGVVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLPSEHRKQPCPYGRKCTYGIKCRFFHPERPSRPQRSVADELRANALLSPPRTPVKDKSSQRPSPASQPNSMSLEAEPGSPDGKKLGTRSSPGPHQEGSTQTCAPAGRSLPVSGGSFGPTEWLPHTLDSLPYTSQECLDSGIGSLESQMSELWGLRGGSPGESGPTRGPYTGYQTYGSKLPAAPAFSPFRQAIGTGHFSVPTDYVPPPPTYPAREYWSEPYPLPPPTPVLQEPQRPRPRASGDPWGRVSDLAKERAGVYTKLCGVFPPHLVEAVMGRFPQLLDPQQLAAEILSYKSQHLSE" }, "uniprot_id": "ZC12A_RAT", "enzyme_annotation": [ { "ec": "3.1.-.-", "activity": "" } ], "synonyms": { "protein": { "refseq": [ "endoribonuclease ZC3H12A", "ribonuclease ZC3H12A; Zinc finger CCCH domain-containing protein 12A; bifunctional endoribonuclease and deubiquitinase ZC3H12A; regnase-1; MCP-induced protein 1; monocyte chemotactic protein-induced protein 1" ], "uniprotkb": [ "Endoribonuclease ZC3H12A", "3.1.-.-", "Regnase-1", "Reg1", "Monocyte chemotactic protein-induced protein 1", "MCP-induced protein 1", "MCPIP-1", "Zinc finger CCCH domain-containing protein 12A" ] }, "gene": { "refseq": [ "Zc3h12a", "MCPIP-1", "Reg1", "RGD1306776" ], "uniprotkb": [ "Zc3h12a", "MCPIP-1", "Reg1", "RGD1306776" ] } }, "keywords": [], "species": [ { "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "Rattus norvegicus", "taxid": 10116 } ], "recommendedname": { "full": "Endoribonuclease ZC3H12A; 3.1.-.-; Regnase-1; Reg1; Monocyte chemotactic protein-induced protein 1; MCP-induced protein 1; MCPIP-1; Zinc finger CCCH domain-containing protein 12A." }, "publication": [ { "title": "MicroRNA-9 controls apoptosis of neurons by targeting monocyte chemotactic protein-induced protein 1 expression in rat acute spinal cord injury model.", "url": "https://www.ncbi.nlm.nih.gov/pubmed/26812136", "journal": "Brain research bulletin", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ], "authors": "Xu Y, An BY, Xi XB, Li ZW, Li FY", "date": "2016", "pmid": "26812136" }, { "title": "Regnase-1 in microglia negatively regulates high mobility group box 1-mediated inflammation and neuronal injury.", "url": "https://www.ncbi.nlm.nih.gov/pubmed/27044405", "journal": "Scientific reports", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ], "authors": "Liu XX, Wang C, Huang SF, Chen Q, Hu YF, Zhou L, Gu Y", "date": "2016", "pmid": "27044405" }, { "title": "MCPIP1 Regulates Alveolar Macrophage Apoptosis and Pulmonary Fibroblast Activation After in vitro Exposure to Silica.", "url": "https://www.ncbi.nlm.nih.gov/pubmed/26865670", "journal": "Toxicological sciences : an official journal of the Society of Toxicology", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ], "authors": "Wang X, Zhang Y, Zhang W, Liu H, Zhou Z, Dai X, Cheng Y, Fang S, Zhang Y, Yao H, Chao J", "date": "2016", "pmid": "26865670" }, { "title": "Regnase-1 and Roquin regulate inflammatory mRNAs.", "url": "https://www.ncbi.nlm.nih.gov/pubmed/26255671", "journal": "Oncotarget", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ], "authors": "Mino T, Takeuchi O", "date": "2015", "pmid": "26255671" }, { "title": "Monocyte Chemotactic Protein-induced Protein 1 and 4 Form a Complex but Act Independently in Regulation of Interleukin-6 mRNA Degradation.", "url": "https://www.ncbi.nlm.nih.gov/pubmed/26134560", "journal": "The Journal of biological chemistry", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ], "authors": "Huang S, Liu S, Fu JJ, Tony Wang T, Yao X, Kumar A, Liu G, Fu M", "date": "2015", "pmid": "26134560" }, { "title": "Zc3h12a is an RNase essential for controlling immune responses by regulating mRNA decay.", "url": "https://www.ncbi.nlm.nih.gov/pubmed/19322177", "journal": "Nature", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ], "authors": "Matsushita K, Takeuchi O, Standley DM, Kumagai Y, Kawagoe T, Miyake T, Satoh T, Kato H, Tsujimura T, Nakamura H, Akira S", "date": "2009", "pmid": "19322177" }, { "title": "MCP-1 (monocyte chemotactic protein-1)-induced protein, a recently identified zinc finger protein, induces adipogenesis in 3T3-L1 pre-adipocytes without peroxisome proliferator-activated receptor gamma.", "url": "https://www.ncbi.nlm.nih.gov/pubmed/19666473", "journal": "The Journal of biological chemistry", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ], "authors": "Younce CW, Azfer A, Kolattukudy PE", "date": "2009", "pmid": "19666473" }, { "title": "A novel CCCH-zinc finger protein family regulates proinflammatory activation of macrophages.", "url": "https://www.ncbi.nlm.nih.gov/pubmed/18178554", "journal": "The Journal of biological chemistry", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ], "authors": "Liang J, Wang J, Azfer A, Song W, Tromp G, Kolattukudy PE, Fu M", "date": "2008", "pmid": "18178554" }, { "title": "Monocyte chemotactic protein (MCP)-1 promotes angiogenesis via a novel transcription factor, MCP-1-induced protein (MCPIP).", "url": "https://www.ncbi.nlm.nih.gov/pubmed/18364357", "journal": "The Journal of biological chemistry", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ], "authors": "Niu J, Azfer A, Zhelyabovska O, Fatma S, Kolattukudy PE", "date": "2008", "pmid": "18364357" }, { "title": "Monocyte chemoattractant protein-1 induces a novel transcription factor that causes cardiac myocyte apoptosis and ventricular dysfunction.", "url": "https://www.ncbi.nlm.nih.gov/pubmed/16574901", "journal": "Circulation research", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ], "authors": "Zhou L, Azfer A, Niu J, Graham S, Choudhury M, Adamski FM, Younce C, Binkley PF, Kolattukudy PE", "date": "2006", "pmid": "16574901" } ], "glycosylation": [], "mutation": [], "isoforms": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4#A0JPN4-1", "isoform_ac": "A0JPN4-1", "locus": { "end_pos": 143112003, "start_pos": 143119339, "chromosome": "5", "evidence": [ { "url": "https://www.ensembl.org/id/ENSRNOT00000012314", "id": "ENSRNOT00000012314", "database": "Ensembl Transcript" }, { "url": "https://www.ensembl.org/id/ENSRNOP00000012314", "id": "ENSRNOP00000012314", "database": "Ensembl Peptide" } ] }, "sequence": { "header": "sp|A0JPN4-1|ZC12A_RAT Isoform 1 of Endoribonuclease ZC3H12A OS=Rattus norvegicus OX=10116 GN=Zc3h12a PE=2 SV=1 CANONICAL=A0JPN4-1", "length": 596, "sequence": "MSDPCGKKLVQEISPTMSLWGLEDRHSCQGQPQPDQDPVAKEASASELQMKVDFFRKLGYSSSEIHSALQKLGVQADTNTVLGELVKHGSATERECQASTDPCPQPPLVPRGGSTPKPSTVEPSLPEEDKESSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAYESDGVVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLPSEHRKQPCPYGRKCTYGIKCRFFHPERPSRPQRSVADELRANALLSPPRTPVKDKSSQRPSPASQPNSMSLEAEPGSPDGKKLGTRSSPGPHQEGSTQTCAPAGRSLPVSGGSFGPTEWLPHTLDSLPYTSQECLDSGIGSLESQMSELWGLRGGSPGESGPTRGPYTGYQTYGSKLPAAPAFSPFRQAIGTGHFSVPTDYVPPPPTYPAREYWSEPYPLPPPTPVLQEPQRPRPRASGDPWGRVSDLAKERAGVYTKLCGVFPPHLVEAVMGRFPQLLDPQQLAAEILSYKSQHLSE" } } ], "pathway": [ { "url": "https://www.genome.jp/dbget-bin/www_bget?rno:313587", "resource": "KEGG Pathway", "id": "rno:313587", "name": "" } ], "function": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4#function", "annotation": "Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay. Modulates the inflammatory response by promoting the degradation of a set of translationally active cytokine-induced inflammation-related mRNAs, such as IL6 and IL12B, during the early phase of inflammation. Prevents aberrant T-cell-mediated immune reaction by degradation of multiple mRNAs controlling T-cell activation, such as those encoding cytokines (IL6 and IL2), cell surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription factor (REL). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (By similarity). Self regulates by destabilizing its own mRNA. Cleaves mRNA harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-dependent manner (By similarity). Plays a role in the inhibition of microRNAs (miRNAs) biogenesis (By similarity). Cleaves the terminal loop of a set of precursor miRNAs (pre-miRNAs) important for the regulation of the inflammatory response leading to their degradation, and thus preventing the biosynthesis of mature miRNAs (By similarity). Plays also a role in promoting angiogenesis in response to inflammatory cytokines by inhibiting the production of antiangiogenic microRNAs via its anti-dicer RNase activity (By similarity). Affects the overall ubiquitination of cellular proteins. Positively regulates deubiquitinase activity promoting the cleavage at 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains on TNF receptor-associated factors (TRAFs), preventing JNK and NF-kappa-B signaling pathway activation, and hence negatively regulating macrophage-mediated inflammatory response and immune homeostasis (By similarity). Induces also deubiquitination of the transcription factor HIF1A, probably leading to its stabilization and nuclear import, thereby positively regulating the expression of proangiogenic HIF1A-targeted genes. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (By similarity). Prevents stress granules (SGs) formation and promotes macrophage apoptosis under stress conditions, including arsenite-induced oxidative stress, heat shock, and energy deprivation. Plays a role in the regulation of macrophage polarization; promotes IL4-induced polarization of macrophages M1 into anti-inflammatory M2 state. May also act as a transcription factor that regulates the expression of multiple genes involved in inflammatory response, angiogenesis, adipogenesis and apoptosis (By similarity). Functions as a positive regulator of glial differentiation of neuroprogenitor cells through an amyloid precursor protein (APP)-dependent signaling pathway (By similarity). Attenuates septic myocardial contractile dysfunction in response to lipopolysaccharide (LPS) by reducing I-kappa-B-kinase (IKK)-mediated NF-kappa-B activation, and hence myocardial proinflammatory cytokine production (By similarity).", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4#function", "id": "A0JPN4", "database": "UniProtKB" } ] }, { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "annotation": "Data suggest a vital role for MCPIP1 in alveolar macrophage apoptosis and pulmonary fibroblast activation/migration induced by SiO2.", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ] }, { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "annotation": "Regnase-1 can be induced by HMGB1 in microglia and negatively regulates HMGB1-mediated neuroinflammation and neuronal toxicity Publication Status: Online-Only", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ] }, { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "annotation": "MiR-9 expression in acute spinal cord injury tissue was significantly lower than that in normal spinal cord tissue.", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ] } ], "orthologs": [ { "uniprot_canonical_ac": "Q5D1E8-1", "protein_name": "Endoribonuclease ZC3H12A; 3.1.-.-; Regnase-1; Reg1; Monocyte chemotactic protein-induced protein 1; MCP-induced protein 1; MCPIP-1; Zinc finger CCCH domain-containing protein 12A.", "sequence": { "length": 599, "sequence": "MSGPCGEKPVLEASPTMSLWEFEDSHSRQGTPRPGQELAAEEASALELQMKVDFFRKLGYSSTEIHSVLQKLGVQADTNTVLGELVKHGTATERERQTSPDPCPQLPLVPRGGGTPKAPNLEPPLPEEEKEGSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAYESDGIVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLTLEHRKQPCPYGRKCTYGIKCRFFHPERPSCPQRSVADELRANALLSPPRAPSKDKNGRRPSPSSQSSSLLTESEQCSLDGKKLGAQASPGSRQEGLTQTYAPSGRSLAPSGGSGSSFGPTDWLPQTLDSLPYVSQDCLDSGIGSLESQMSELWGVRGGGPGEPGPPRAPYTGYSPYGSELPATAAFSAFGRAMGAGHFSVPADYPPAPPAFPPREYWSEPYPLPPPTSVLQEPPVQSPGAGRSPWGRAGSLAKEQASVYTKLCGVFPPHLVEAVMGRFPQLLDPQQLAAEILSYKSQHPSE" }, "evidence": [ { "url": "https://omabrowser.org/oma/group/A0JPN4/", "id": "A0JPN4", "database": "OMA" }, { "url": "http://www.informatics.jax.org/homology/11824", "id": "11824", "database": "MGI" } ], "organism": "Homo sapiens", "tax_id": 9606 }, { "uniprot_canonical_ac": "Q5D1E7-1", "protein_name": "Endoribonuclease ZC3H12A; 3.1.-.-; Regnase-1; Reg1; Monocyte chemotactic protein-induced protein 1; MCP-induced protein 1; MCPIP-1; Zinc finger CCCH domain-containing protein 12A.", "sequence": { "length": 596, "sequence": "MSDPCGTKPVQESNPTMSLWSLEDRHSSQGRPQPDQDPVAKEAPTSELQMKVDFFRKLGYSSSEIHSVLQKLGVQADTNTVLGELVKHGSATERECQALTAPSPQPPLVPRGGSTPKPSTLEPSLPEEDREGSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAFESDGVVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLPSEHRKQPCPYGKKCTYGIKCRFFHPERPSRPQRSVADELRANALLSPPRTPVKDKSSQRPSPASQSSSVSLEAEPGSLDGKKLGARSSPGPHREGSPQTCAPAGRSLPVSGGSFGPTEWLAHTQDSLPYTSQECLDSGIGSLESQMSELWGVRGGSPGESGPTRGPYAGYHSYGSKVPAAPSFSPFRPAMGAGHFSVPTDYVPPPPTYPSREYWSEPYPLPPPTPVLQEPQRPSPGAGGGPWGRVGDLAKERAGVYTKLCGVFPPHLVEAVMRRFPQLLDPQQLAAEILSYKSQHLSE" }, "evidence": [ { "url": "https://omabrowser.org/oma/group/A0JPN4/", "id": "A0JPN4", "database": "OMA" }, { "url": "http://www.informatics.jax.org/homology/11824", "id": "11824", "database": "MGI" } ], "organism": "Mus musculus", "tax_id": 10090 } ], "refseq": { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "ac": "NP_001071139.1", "name": "endoribonuclease ZC3H12A; ribonuclease ZC3H12A; Zinc finger CCCH domain-containing protein 12A; bifunctional endoribonuclease and deubiquitinase ZC3H12A; regnase-1; MCP-induced protein 1; monocyte chemotactic protein-induced protein 1.", "summary": "" }, "go_annotation": { "categories": [ { "go_terms": [ { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0003677", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "DNA binding", "id": "GO:0003677" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0003682", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "chromatin binding", "id": "GO:0003682" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0003729", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "mRNA binding", "id": "GO:0003729" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046872", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "metal ion binding", "id": "GO:0046872" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043022", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "ribosome binding", "id": "GO:0043022" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035198", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "miRNA binding", "id": "GO:0035198" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0003730", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "mRNA 3'-UTR binding", "id": "GO:0003730" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004521", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "endoribonuclease activity", "id": "GO:0004521" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004518", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "nuclease activity", "id": "GO:0004518" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004532", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "exoribonuclease activity", "id": "GO:0004532" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004843", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "thiol-dependent ubiquitin-specific protease activity", "id": "GO:0004843" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035613", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "RNA stem-loop binding", "id": "GO:0035613" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035925", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "mRNA 3'-UTR AU-rich region binding", "id": "GO:0035925" } ], "total": 13, "name": "Molecular Function" }, { "go_terms": [ { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005634", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "nucleus", "id": "GO:0005634" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005654", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "nucleoplasm", "id": "GO:0005654" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005737", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "cytoplasm", "id": "GO:0005737" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005791", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "rough endoplasmic reticulum", "id": "GO:0005791" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005856", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "cytoskeleton", "id": "GO:0005856" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0000932", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "P-body", "id": "GO:0000932" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0032991", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "protein-containing complex", "id": "GO:0032991" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042406", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "extrinsic component of endoplasmic reticulum membrane", "id": "GO:0042406" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030867", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "rough endoplasmic reticulum membrane", "id": "GO:0030867" } ], "total": 9, "name": "Cellular Component" }, { "go_terms": [ { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042307", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "positive regulation of protein import into nucleus", "id": "GO:0042307" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1990869", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "cellular response to chemokine", "id": "GO:1990869" }, { "url": 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"angiogenesis", "id": "GO:0001525" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006954", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "inflammatory response", "id": "GO:0006954" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007399", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "nervous system development", "id": "GO:0007399" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016579", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "protein deubiquitination", "id": "GO:0016579" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030154", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "cell differentiation", "id": "GO:0030154" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045600", 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