{ "uniprot_canonical_ac": "A0JPN4-1", "ptm_annotation": [ { "annotation": "Phosphorylated by IRAK1; phosphorylation is necessary for subsequent phosphorylation by the I-kappa-B-kinase (IKK) complex. Phosphorylated by I-kappa-B-kinases (IKKs) at Ser-435 and Ser-439 upon lipopolysaccharide (LPS) or IL1B stimulation in macrophages through the MyD88-dependent signaling pathway; these phosphorylations promote rapid ubiquitin proteasome-mediated degradation of ZC3H12A in macrophages and hence allows its target mRNAs, such as IL6, to escape from degradation and accumulate during the inflammatory response.", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/Q5D1E7", "id": "Q5D1E7", "database": "PubMed" } ] }, { "annotation": "Proteolytically cleaved between Arg-111 and Arg-214 by MALT1 in activated T-cells; cleavage at Arg-111 is critical for promoting ZC3H12A degradation in response to T-cell receptor (TCR) stimulation, and hence is necessary for prolonging the stability of a set of mRNAs controlling T-cell activation and Th17 cell differentiation.", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/Q5D1E7", "id": "Q5D1E7", "database": "PubMed" } ] }, { "annotation": "Ubiquitinated; ubiquitination is induced in response to interleukin IL1 receptor stimuli in a IKBKB/IKKB and IRAK1-dependent manner, leading to proteasome-mediated degradation.", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/Q5D1E7", "id": "Q5D1E7", "database": "PubMed" } ] } ], "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": "" } ], "glycation": [], "keywords": [], "species": [ { "common_name": "Rat", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "Rattus norvegicus", "taxid": 10116 } ], "publication": [ { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/16574901", "type": [ "PubMed" ], "id": "16574901" } ], "title": "Monocyte chemoattractant protein-1 induces a novel transcription factor that causes cardiac myocyte apoptosis and ventricular dysfunction.", "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" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/18178554", "type": [ "PubMed" ], "id": "18178554" } ], "title": "A novel CCCH-zinc finger protein family regulates proinflammatory activation of macrophages.", "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" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/18364357", "type": [ "PubMed" ], "id": "18364357" } ], "title": "Monocyte chemotactic protein (MCP)-1 promotes angiogenesis via a novel transcription factor, MCP-1-induced protein (MCPIP).", "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" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/19322177", "type": [ "PubMed" ], "id": "19322177" } ], "title": "Zc3h12a is an RNase essential for controlling immune responses by regulating mRNA decay.", "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" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/19666473", "type": [ "PubMed" ], "id": "19666473" } ], "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.", "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" } ], "uniprot_ac": "A0JPN4", "site_annotation": [ { "end_pos": 245, "annotation": "n_glycosylation_sequon", "start_pos": 243 } ], "isoforms": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4#A0JPN4-1", "isoform_ac": "A0JPN4-1", "locus": { "end_pos": 143112003, "strand": "+", "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/get_linkdb?-t+pathway+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). Together with RC3H1, destabilizes TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in its 3'UTR (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": "Since MCPIP1 expression undergoes fluctuations in islets during type 1 diabetes development in the IDDM rat and regulates the beta-cell fate upon exposure to proinflammatory cytokines, manipulations of its expression and activity might open new perspectives for type 1 diabetes treatment. 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": "With the help of a cecal ligation puncture-induced model of acute lung injury (ALI) in rats, we demonstrated that MCPIP1 overexpression induced by MG132 can alleviate sepsis-induced pathologic changes, increase in water content and protein leakage in the lungs, and induction of systemic inflammatory mediators, and thereby improve the 7-day mortality rate in sepsis-induced ALI.", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "id": "NP_001071139.1", "database": "RefSeq" } ] } ], "orthologs": [ { "uniprot_canonical_ac": "Q5D1E7-1", "protein_name": "Endoribonuclease ZC3H12A", "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" } ], "common_name": "Mouse", "organism": "Mus musculus", "tax_id": 10090 }, { "uniprot_canonical_ac": "Q5D1E8-1", "protein_name": "Endoribonuclease ZC3H12A", "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" } ], "common_name": "Human", "organism": "Homo sapiens", "tax_id": 9606 } ], "interactions": [], "synthesized_glycans": [], "snv": [], "cluster_types": [ { "name": "homologset.oma", "label": "OMA Homologs" }, { "name": "homologset.mgi", "label": "MGI Homologs" } ], "refseq": { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001071139.1", "ac": "NP_001071139.1", "name": "endoribonuclease ZC3H12A", "summary": "" }, "go_annotation": { "categories": [ { "go_terms": [ { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0003677", "pmid": "", "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", "pmid": "", "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:0003723", "pmid": "", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "RNA binding", "id": "GO:0003723" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0003729", "pmid": "", "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", "pmid": "", "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:0004540", "pmid": "", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "ribonuclease activity", "id": "GO:0004540" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043022", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "mRNA 3'-UTR AU-rich region binding", "id": "GO:0035925" } ], "total": 15, "name": "Molecular Function" }, { "go_terms": [ { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0036464", "pmid": "21873635", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "cytoplasmic ribonucleoprotein granule", "id": "GO:0036464" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005634", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "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", "pmid": "", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "rough endoplasmic reticulum membrane", "id": "GO:0030867" } ], "total": 10, "name": "Cellular Component" }, { "go_terms": [ { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042307", "pmid": "", "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", "pmid": "", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": "A0JPN4", "database": "UniProtKB" } ], "name": "cellular response to chemokine", "id": "GO:1990869" }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1903799", "pmid": "", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A0JPN4", "id": 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"resource": "UniProtKB", "name": "MCPIP-1" }, { "url": "https://www.uniprot.org/uniprot/A0JPN4", "type": "synonym", "resource": "UniProtKB", "name": "Monocyte chemotactic protein-induced protein 1" }, { "url": "https://www.uniprot.org/uniprot/A0JPN4", "type": "synonym", "resource": "UniProtKB", "name": "Reg1" }, { "url": "https://www.uniprot.org/uniprot/A0JPN4", "type": "synonym", "resource": "UniProtKB", "name": "Regnase-1" }, { "url": "https://www.ncbi.nlm.nih.gov/protein/A0JPN4", "type": "synonym", "resource": "RefSeq", "name": "Zinc finger CCCH domain-containing protein 12A; ribonuclease ZC3H12A; bifunctional endoribonuclease and deubiquitinase ZC3H12A; regnase-1; MCP-induced protein 1; monocyte chemotactic protein-induced protein 1" }, { "url": "https://www.uniprot.org/uniprot/A0JPN4", "type": "synonym", "resource": "UniProtKB", "name": "Zinc finger CCCH domain-containing protein 12A" }, { "url": "https://www.ncbi.nlm.nih.gov/protein/A0JPN4", "type": "synonym", "resource": "RefSeq", "name": "endoribonuclease ZC3H12A" } ] }