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Protein

Endoribonuclease ZC3H12A

Gene

Zc3h12a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 (PubMed:26000482). 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 (PubMed:19322177, PubMed:21115689, PubMed:23185455, PubMed:26000482). 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) (PubMed:23706741, PubMed:26000482, PubMed:19322177, PubMed:21115689, PubMed:23185455). 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 (PubMed:25282160). Self regulates by destabilizing its own mRNA (PubMed:22037600). 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 (PubMed:19322177, PubMed:23185455, PubMed:23706741, PubMed:26000482, PubMed:26134560). 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 (PubMed:21115689). 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 (PubMed:21115689). 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 (PubMed:21971051). Plays a role in the regulation of macrophage polarization; promotes IL4-induced polarization of macrophages M1 into anti-inflammatory M2 state (PubMed:25934862). May also act as a transcription factor that regulates the expression of multiple genes involved in inflammatory response, angiogenesis, adipogenesis and apoptosis (PubMed:18178554, PubMed:19666473, PubMed:22739135). 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 (PubMed:21616078).By similarity14 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 PublicationNote: Mg2+ is required for RNase activity (PubMed:19322177).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi226MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri301 – 324C3H1-typeAdd BLAST24

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, DNA-binding, Endonuclease, Hydrolase, Nuclease, RNA-binding
Biological processAngiogenesis, Apoptosis, Differentiation, DNA damage, Immunity, Inflammatory response, Neurogenesis, Stress response
LigandMagnesium, Metal-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Endoribonuclease ZC3H12ACurated (EC:3.1.-.-1 Publication)
Alternative name(s):
Monocyte chemotactic protein-induced protein 11 Publication
Short name:
MCP-induced protein 11 Publication
Short name:
MCPIP-11 Publication
Regnase-11 Publication
Short name:
Reg11 Publication
Zinc finger CCCH domain-containing protein 12AImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Zc3h12a1 PublicationImported
Synonyms:Mcpip1 Publication, Mcpip11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:2385891 Zc3h12a

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Increased expression of ZC3H12A is associated with ischemic heart disease (PubMed:16574901).1 Publication

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Most mice die within the first 12 weeks (PubMed:21115689). Show severe inflammatory syndromes, including growth retardation, splenomegaly and lymphoadenopathy (PubMed:19322177, PubMed:21115689). show systemic inflammation characterized by T-cell and B-cell activation (PubMed:23706741). Exhibit greatly increased levels of plasma cells and infiltration of plasma cells into the lungs (PubMed:19322177, PubMed:21115689). Show elevated serum immunoglobulin levels and produce anti-nuclear autoantibodies (PubMed:19322177, PubMed:23706741). Mice show increased production of proinflammatory cytokine mRNAs and secreted protein levels, such as IL6, TNF and PTGS2 expression upon lipopolysaccharide (LPS) stimulation in bone marrow macrophages (BBMs) or embryonic fibroblasts, particularly in the early phase of the inflammatory response (PubMed:21115689, PubMed:26000482). Show impaired degradation of IL6 mRNA (PubMed:19322177, PubMed:21115689). Show an increased in both JNK and NF-kappa-B signaling pathway activations upon LPS stimulation (PubMed:21115689). Show an increase in global ubiquitinated protein level in splenocytes (PubMed:21115689). Display a drastic increase in both basal and LPS- or TNF-induced ubiquitination of TRAF2, TRAF3 and TRAF6 in splenocytes (PubMed:21115689). Splenocytes show spontaneously formed aggregation of stress granules (SGs) and were resistant to stress-induced apoptosis (PubMed:21971051). Heterozygous knockout mice display IL-17-dependent enhanced resistance to disseminated Candida albicans infection compared to wild-type mice (PubMed:26320658). Double knockout of ZC3H12A and RC3H1 result in embryonic developmental arrest and death; embryonic fibroblasts from these mice show a higher increase in IL6, TNF and PTGS2 expression upon LPS stimulation, both in early and late phases of the responses, compared to single knockout of either ZC3H12A or RC3H1 (PubMed:26000482). T-cell specific conditional knockout mice die within the first 8 to 17 weeks after birth with the development of severe splenomegaly and the development of a severe autoimmune inflammatory disease (PubMed:23706741). Show massive increase in effector/memory T-cells with elevated production of interferon IFNG, interleukins IL17A and IL4 in response to phorbol 13-acetate 12-myristate (PMA) (PubMed:23706741). Proteolytic cleavage is inhibited in T-cells in response to antigen stimulation (PubMed:23706741). Conditional knockout in myeloid cells show impairment in IL4-induced macrophage M2 polarization (PubMed:25934862).7 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi111R → A: Loss of MALT1-dependent cleavage and degradation in T-cells. 1 Publication1
Mutagenesisi130R → A: Reduces MALT1-dependent cleavage and degradation in T-cells. 1 Publication1
Mutagenesisi136R → A: Reduces MALT1-dependent cleavage and degradation in T-cells. 1 Publication1
Mutagenesisi141D → N: Loss of RNase activity. Loss of mRNAs and miRNAs degradation. Loss of protein deubiquitination and suppression of inhibition on JNK and NF-kappa-B signaling pathway activation. Inhibits induction of angiogenesis and macrophage M2 polarization. Mislocalized in stress granule (SG). Loss of the ability to inhibit SG formation under stress. Does not inhibit binding to IL6 mRNA. Increases ICOS surface expression. 7 Publications1
Mutagenesisi157C → A: Loss of protein deubiquitination and suppression of inhibition on JNK and NF-kappa-B signaling pathway activation. Loss of the ability to inhibit stress granule (SG) formation. No loss of RNase activity. No effect on ICOS surface expression. 3 Publications1
Mutagenesisi158R → A: Reduces MALT1-dependent cleavage and degradation in T-cells. 1 Publication1
Mutagenesisi214R → A: Reduces MALT1-dependent cleavage and degradation in T-cells. 1 Publication1
Mutagenesisi225 – 226DD → AA: Increases ICOS surface expression. 1 Publication2
Mutagenesisi225D → A: Loss of RNase activity, no loss of protein deubiquitination and ability to inhibit stress granule (SG) formation under stress; when associated with A-226. 1 Publication1
Mutagenesisi226D → A: Loss of RNase activity and no loss of protein deubiquitination; when associated with A-226. 1 Publication1
Mutagenesisi278D → A: Loss of inhibition on JNK and NF-kappa-B signaling pathway activation; when associated with A-279. 1 Publication1
Mutagenesisi279D → A: Loss of inhibition on JNK and NF-kappa-B signaling pathway activation; when associated with A-278. 1 Publication1
Mutagenesisi306C → R: Loss of protein deubiquitination and suppression of inhibition on JNK and NF-kappa-B signaling pathway activations. No loss of RNase activity. 2 Publications1
Mutagenesisi435S → A: Reduces its phosphorylation status, does not interact with IKBKB/IKKB and BTRC, inhibits IL6 mRNA instability and IKK-mediated degradation of ZC3H12A; when associated with A-439. 1 Publication1
Mutagenesisi439S → A: Reduces its phosphorylation status, does not interact with IKBKB/IKKB and BTRC, inhibits IL6 mRNA instability and IKK-mediated degradation of ZC3H12A; when associated with A-435. 1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003415131 – 596Endoribonuclease ZC3H12AAdd BLAST596

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei344PhosphoserineBy similarity1
Modified residuei435Phosphoserine1 Publication1
Modified residuei439Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.2 Publications
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 (PubMed:22037600).1 Publication
Ubiquitinated; ubiquitination is induced in response to interleukin IL1 receptor stimuli in a IKBKB/IKKB and IRAK1-dependent manner, leading to proteasome-mediated degradation (PubMed:22037600).1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q5D1E7

MaxQB - The MaxQuant DataBase

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MaxQBi
Q5D1E7

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q5D1E7

PRoteomics IDEntifications database

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PRIDEi
Q5D1E7

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q5D1E7

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q5D1E7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in macrophages (PubMed:18178554). Expressed in lung, lymph nodes, spleen and thymus (PubMed:22037600). Expressed weakly in heart (PubMed:21616078). Expressed weakly in cardiomyocytes (at protein level) (PubMed:16574901). Expressed in spleen, lung, intestine, brown adipose tissue and thymus (PubMed:18682727). Weakly expressed in the heart (PubMed:16574901). Weakly expressed in cardiomyocytes (PubMed:16574901).5 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by the transcription factor KLF4 in a interleukin IL4-dependent manner in macrophage (PubMed:25934862). Up-regulated by lipopolysaccharide (LPS) (at protein level) (PubMed:21616078). Up-regulated by chemokine CCL2 during adipocytes differentiation (PubMed:19666473). Up-regulated in activated T lymphocytes (PubMed:23185455). Up-regulated in response to lipopolysaccharide (LPS) in a MyD88-dependent manner in macrophages (PubMed:18178554, PubMed:18682727, PubMed:19322177). Up-regulated by phorbol 13-acetate 12-myristate (PMA) in primary T lymphocytes (PubMed:23185455). Up-regulated by interleukin IL17 in keratinocytes (PubMed:26320658).8 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000042677 Expressed in 105 organ(s), highest expression level in jejunum

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q5D1E7 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Oligomer (By similarity). Found in a deubiquitination complex with TANK, USP10 and ZC3H12A; this complex inhibits genotoxic stress- or interleukin-1-beta-mediated NF-kappaB activation by promoting IKBKG or TRAF6 deubiquitination. Interacts with IKBKG; this interaction increases in response to DNA damage. Interacts with TANK; this interaction increases in response to DNA damage and serves as a bridge to anchor both TANK and USP10 into a deubiquitinating complex. Interacts with TRAF6; this interaction increases in response to DNA damage and is stimulated by TANK. Interacts with USP10; this interaction increases in response to DNA damage and serves as a bridge to anchor both TANK and USP10 into a deubiquitinating complex. Interacts with ZC3H12D. Interacts with TNRC6A. Interacts with IKBKB/IKKB. Interacts with IKBKB/IKKB (By similarity). Interacts with IKBKB/IKKB (PubMed:22037600). Interacts with BTRC; the interaction occurs when ZC3H12A is phosphorylated in a IKBKB/IKKB-dependent manner (PubMed:22037600). Interacts with IRAK1; this interaction increases the interaction between ZC3H12A and IKBKB/IKKB (PubMed:22037600). Interacts with UPF1; this interaction occurs in a mRNA translationally active- and termination-dependent manner and is essential for ZC3H12A-mediated degradation of target mRNAs (PubMed:26000482). Associates with ribosomes (PubMed:26000482). Interacts with ubiquitin (PubMed:21115689).By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
231011, 2 interactors

Protein interaction database and analysis system

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IntActi
Q5D1E7, 4 interactors

Molecular INTeraction database

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MINTi
Q5D1E7

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000037172

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1596
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N5JNMR-A45-89[»]
2N5KNMR-A299-327[»]
2N5LNMR-A544-596[»]
5H9VX-ray2.75A/B/C/D134-339[»]
5H9WX-ray2.60A/B134-339[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q5D1E7

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q5D1E7

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni42 – 87Ubiquitin association domain1 PublicationAdd BLAST46
Regioni81 – 150Necessary for interaction with TANKBy similarityAdd BLAST70
Regioni112 – 281RNaseBy similarityAdd BLAST170
Regioni214 – 220RNA bindingBy similarity7
Regioni301 – 454Necessary for interaction with ZC3H12DBy similarityAdd BLAST154

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi476 – 533Pro-richSequence analysisAdd BLAST58

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C3H1-type zinc finger domain and C-terminal region are necessary for pre-miRNA binding (By similarity). The C-terminal region and proline-rich domain are necessary for oligomerization (By similarity).By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ZC3H12 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri301 – 324C3H1-typeAdd BLAST24

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3777 Eukaryota
ENOG410ZNK1 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155107

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000060218

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG108758

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q5D1E7

KEGG Orthology (KO)

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KOi
K18668

Identification of Orthologs from Complete Genome Data

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OMAi
YWSEPYQ

Database of Orthologous Groups

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OrthoDBi
771251at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q5D1E7

TreeFam database of animal gene trees

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TreeFami
TF315783

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR021869 RNase_Zc3h12_NYN

Pfam protein domain database

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Pfami
View protein in Pfam
PF11977 RNase_Zc3h12a, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q5D1E7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDPCGTKPV QESNPTMSLW SLEDRHSSQG RPQPDQDPVA KEAPTSELQM
60 70 80 90 100
KVDFFRKLGY SSSEIHSVLQ KLGVQADTNT VLGELVKHGS ATERECQALT
110 120 130 140 150
APSPQPPLVP RGGSTPKPST LEPSLPEEDR EGSDLRPVVI DGSNVAMSHG
160 170 180 190 200
NKEVFSCRGI LLAVNWFLER GHTDITVFVP SWRKEQPRPD VPITDQHILR
210 220 230 240 250
ELEKKKILVF TPSRRVGGKR VVCYDDRFIV KLAFESDGVV VSNDTYRDLQ
260 270 280 290 300
GERQEWKRFI EERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPLPSE
310 320 330 340 350
HRKQPCPYGK KCTYGIKCRF FHPERPSRPQ RSVADELRAN ALLSPPRTPV
360 370 380 390 400
KDKSSQRPSP ASQSSSVSLE AEPGSLDGKK LGARSSPGPH REGSPQTCAP
410 420 430 440 450
AGRSLPVSGG SFGPTEWLAH TQDSLPYTSQ ECLDSGIGSL ESQMSELWGV
460 470 480 490 500
RGGSPGESGP TRGPYAGYHS YGSKVPAAPS FSPFRPAMGA GHFSVPTDYV
510 520 530 540 550
PPPPTYPSRE YWSEPYPLPP PTPVLQEPQR PSPGAGGGPW GRVGDLAKER
560 570 580 590
AGVYTKLCGV FPPHLVEAVM RRFPQLLDPQ QLAAEILSYK SQHLSE
Length:596
Mass (Da):65,598
Last modified:June 10, 2008 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i420E116564B70212
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti280P → H in BAE29035 (PubMed:16141072).Curated1
Sequence conflicti315G → E in AAX14018 (PubMed:16574901).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AY920404 mRNA Translation: AAX14018.1
AK142501 mRNA Translation: BAE25089.1
AK149698 mRNA Translation: BAE29035.1
AK152196 mRNA Translation: BAE31025.1
AK161150 mRNA Translation: BAE36216.1
AK172357 mRNA Translation: BAE42965.1
AL626775 Genomic DNA No translation available.
BC006817 mRNA Translation: AAH06817.1
BC036563 mRNA Translation: AAH36563.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS18638.1

NCBI Reference Sequences

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RefSeqi
NP_694799.1, NM_153159.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.402

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000036188; ENSMUSP00000037172; ENSMUSG00000042677

Database of genes from NCBI RefSeq genomes

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GeneIDi
230738

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:230738

UCSC genome browser

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UCSCi
uc008urw.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY920404 mRNA Translation: AAX14018.1
AK142501 mRNA Translation: BAE25089.1
AK149698 mRNA Translation: BAE29035.1
AK152196 mRNA Translation: BAE31025.1
AK161150 mRNA Translation: BAE36216.1
AK172357 mRNA Translation: BAE42965.1
AL626775 Genomic DNA No translation available.
BC006817 mRNA Translation: AAH06817.1
BC036563 mRNA Translation: AAH36563.1
CCDSiCCDS18638.1
RefSeqiNP_694799.1, NM_153159.2
UniGeneiMm.402

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N5JNMR-A45-89[»]
2N5KNMR-A299-327[»]
2N5LNMR-A544-596[»]
5H9VX-ray2.75A/B/C/D134-339[»]
5H9WX-ray2.60A/B134-339[»]
ProteinModelPortaliQ5D1E7
SMRiQ5D1E7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231011, 2 interactors
IntActiQ5D1E7, 4 interactors
MINTiQ5D1E7
STRINGi10090.ENSMUSP00000037172

PTM databases

iPTMnetiQ5D1E7
PhosphoSitePlusiQ5D1E7

Proteomic databases

EPDiQ5D1E7
MaxQBiQ5D1E7
PaxDbiQ5D1E7
PRIDEiQ5D1E7

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036188; ENSMUSP00000037172; ENSMUSG00000042677
GeneIDi230738
KEGGimmu:230738
UCSCiuc008urw.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
80149
MGIiMGI:2385891 Zc3h12a

Phylogenomic databases

eggNOGiKOG3777 Eukaryota
ENOG410ZNK1 LUCA
GeneTreeiENSGT00940000155107
HOGENOMiHOG000060218
HOVERGENiHBG108758
InParanoidiQ5D1E7
KOiK18668
OMAiYWSEPYQ
OrthoDBi771251at2759
PhylomeDBiQ5D1E7
TreeFamiTF315783

Miscellaneous databases

Protein Ontology

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PROi
PR:Q5D1E7

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000042677 Expressed in 105 organ(s), highest expression level in jejunum
GenevisibleiQ5D1E7 MM

Family and domain databases

InterProiView protein in InterPro
IPR021869 RNase_Zc3h12_NYN
PfamiView protein in Pfam
PF11977 RNase_Zc3h12a, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiZC12A_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q5D1E7
Secondary accession number(s): Q3U8J3
, Q3UE76, Q8JZW9, Q922T4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: January 16, 2019
This is version 90 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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