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Protein

Endoribonuclease ZC3H12A

Gene

ZC3H12A

Organism
Homo sapiens (Human)
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:19909337). 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:26320658). 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) (By similarity). 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 (By similarity). 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:19909337, PubMed:26320658, PubMed:26134560, PubMed:22561375). Plays a role in the inhibition of microRNAs (miRNAs) biogenesis (PubMed:22055188). 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 (PubMed:22055188). 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 (PubMed:24048733). Affects the overall ubiquitination of cellular proteins (By similarity). 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 (PubMed:24048733). 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 (PubMed:25861989). Prevents stress granule (SGs) formation and promotes macrophage apoptosis under stress conditions, including arsenite-induced oxidative stress, heat shock and energy deprivation (By similarity). Plays a role in the regulation of macrophage polarization; promotes IL4-induced polarization of macrophages M1 into anti-inflammatory M2 state (By similarity). May also act as a transcription factor that regulates the expression of multiple genes involved in inflammatory response, angiogenesis, adipogenesis and apoptosis (PubMed:16574901, PubMed:18364357). Functions as a positive regulator of glial differentiation of neuroprogenitor cells through an amyloid precursor protein (APP)-dependent signaling pathway (PubMed:19185603). 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).By similarity10 Publications
(Microbial infection) Binds to Japanese encephalitis virus (JEV) and Dengue virus (DEN) RNAs.1 Publication
(Microbial infection) Exhibits antiviral activity against HIV-1 in lymphocytes by decreasing the abundance of HIV-1 viral RNA species.1 Publication

Caution

Was originally proposed to bind to DNA and act as transcription factor.1 Publication

<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:22561375).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 bindingi226Magnesium1 Publication1

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, Repressor, RNA-binding
Biological processAngiogenesis, Antiviral defense, Apoptosis, Differentiation, DNA damage, Immunity, Inflammatory response, Neurogenesis, Stress response, Transcription, Transcription regulation
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:
Reg1By similarity
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:ZC3H12AImported
Synonyms:MCPIP1 Publication, MCPIP1
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000163874.8

Human Gene Nomenclature Database

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HGNCi
HGNC:26259 ZC3H12A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
610562 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q5D1E8

<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

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>Mutagenesisi141D → N: Abolishes RNase activity. 1 Publication1
Mutagenesisi141D → N: Loss of pre-miRNA RNase activity. Attenuates strongly miRNA silencing activity. Loss of interleukin IL17A and IL6 mRNA instabilities. Reduces angiogenic differentiation. Loss of RNase activity on JEV and DEN viral RNAs and antiviral effects. Loss of HIV-1 antiviral activity. Loss of IL1B mRNA instability; when associated with A-226. 6 Publications1
Mutagenesisi144N → A: No change in RNase activity. 1 Publication1
Mutagenesisi157C → A: Does not inhibit antiviral effects. 1 Publication1
Mutagenesisi214R → A: Abolishes RNase activity. 1 Publication1
Mutagenesisi225D → A: Loss of pre-miRNA RNase activity, IL17A mRNA instability and antiviral effects; when associated with A-226. 3 Publications1
Mutagenesisi226D → A: Loss of pre-miRNA RNase activity, IL17A mRNA instability and antiviral effects; when associated with A-225. Loss of IL1B mRNA instability; when associated with N-141. 4 Publications1
Mutagenesisi306C → R: Loss of interleukin IL17A mRNA instability. Reduces weakly pre-miRNA RNase activity. Attenuates miRNA silencing activity. Does not inhibits binding to Japanese encephalitis virus (JEV) and dengue virus (DEN) RNAs and weakly attenuates antiviral effects. Loss of HIV-1 antiviral activity. 4 Publications1
Mutagenesisi311K → G: Inhibits transcriptional activity; when associated with G-312. 1 Publication1
Mutagenesisi312C → G: Inhibits transcriptional activity; when associated with G-311. 1 Publication1
Mutagenesisi317K → G: Inhibits transcriptional activity; when associated with G-318. 1 Publication1
Mutagenesisi318C → G: Inhibits transcriptional activity; when associated with G-317. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
80149

Open Targets

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OpenTargetsi
ENSG00000163874

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA142670537

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ZC3H12A

Domain mapping of disease mutations (DMDM)

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DMDMi
190479827

<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_00003415121 – 599Endoribonuclease ZC3H12AAdd BLAST599

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 residuei99PhosphoserineCombined sources1
Modified residuei344PhosphoserineCombined sources1
Modified residuei438PhosphoserineBy similarity1
Modified residuei442PhosphoserineBy similarity1

<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

Phosphorylated by IRAK1; phosphorylation is necessary for subsequent phosphorylation by the I-kappa-B-kinase (IKK) complex. Phosphorylated by I-kappa-B-kinase (IKK) subunits IKBKB/IKKB and CHUK/IKKA at Ser-438 and Ser-442; these phosphorylations promote ubiquitin proteasome-mediated degradation of ZC3H12A and hence facilitates rapid and robust production of IL-6 mRNA in response to toll-like receptor (TLR) or IL-1 receptor stimuli (By similarity).By similarity
(Microbial infection) Rapidly degraded in activated T-cells in response to phorbol 13-acetate 12-myristate (PMA) during HIV-1 viral infection (PubMed:24191027).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 (By similarity).By similarity
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.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q5D1E8

MaxQB - The MaxQuant DataBase

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MaxQBi
Q5D1E8

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

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PaxDbi
Q5D1E8

PeptideAtlas

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PeptideAtlasi
Q5D1E8

PRoteomics IDEntifications database

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PRIDEi
Q5D1E8

ProteomicsDB human proteome resource

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ProteomicsDBi
62741

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q5D1E8

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

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PhosphoSitePlusi
Q5D1E8

<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

Expressed in heart, placenta, spleen, kidney, liver and lung (PubMed:19909337). Expressed in leukocytes (PubMed:19909337). Expressed in monocyte (PubMed:16574901).2 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 ELK1 in a interleukin IL1B-dependent manner through activation of the NF-kappa-B and ERK signaling pathways (PubMed:19747262, PubMed:20137095, PubMed:22037600). Up-regulated by chemokine CCL2 in endothelial cells and in peripheral blood monocytes (PubMed:16574901, PubMed:18364357). Up-regulated in activated T lymphocytes (PubMed:23185455). Up-regulated by phorbol 12-myristate 13-acetate (PMA) in primary T lymphocytes (PubMed:19909337, PubMed:23185455). Up-regulated by interleukin IL17 in keratinocytes (PubMed:26320658). Up-regulated by lipopolysaccharide (LPS) (PubMed:19909337). Up-regulated by tumor necrosis factor TNF-alpha and interleukin IL1 in acute monocytic leukemia cell line THP-1 cells (PubMed:18178554, PubMed:19909337). Up-regulated by amyloid precursor protein (APP) (PubMed:19185603).10 Publications
(Microbial infection) Up-regulated in response to Japanese encephalitis virus (JEV) and dengue virus (DEN) infections (PubMed:23355615).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000163874 Expressed in 131 organ(s), highest expression level in right adrenal gland

CleanEx database of gene expression profiles

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CleanExi
HS_ZC3H12A

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q5D1E8 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q5D1E8 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA032052
HPA032053

<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 (PubMed:22055188, PubMed:23355615). 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 (PubMed:25861989). Interacts with IKBKG; this interaction increases in response to DNA damage (PubMed:25861989). 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 (PubMed:25861989). Interacts with TRAF6; this interaction increases in response to DNA damage and is stimulated by TANK (PubMed:25861989). 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 (PubMed:25861989). Interacts with ZC3H12D (PubMed:26134560). Interacts with TNRC6A (PubMed:26134560). Interacts with IKBKB/IKKB (PubMed:22037600). Interacts with IKBKB/IKKB. Interacts with BTRC; the interaction occurs when ZC3H12A is phosphorylated in a IKBKB/IKKB-dependent manner (By similarity). Interacts with IRAK1; this interaction increases the interaction between ZC3H12A and IKBKB/IKKB (By similarity). 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 (By similarity). Associates with ribosomes (By similarity). Interacts with ubiquitin (By similarity).By similarity5 Publications
(Microbial infection) Oligomerization is necessary for antiviral activity (PubMed:23355615).1 Publication

<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
123141, 23 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q5D1E8

Protein interaction database and analysis system

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IntActi
Q5D1E8, 16 interactors

Molecular INTeraction database

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MINTi
Q5D1E8

STRING: functional protein association networks

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STRINGi
9606.ENSP00000362174

<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

1599
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q5D1E8

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

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SMRi
Q5D1E8

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 domainBy similarityAdd BLAST46
Regioni81 – 150Necessary for interaction with TANK1 PublicationAdd BLAST70
Regioni112 – 297RNase1 PublicationAdd BLAST186
Regioni214 – 220RNA binding1 Publication7
Regioni301 – 457Necessary for interaction with ZC3H12D1 PublicationAdd BLAST157

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 biasi458 – 536Pro-richSequence analysisAdd BLAST79

<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 (PubMed:22055188). The C-terminal region and proline-rich domain are necessary for oligomerization (PubMed:22055188).1 Publication
(Microbial infection) The C3H1-type zinc finger domain is necessary for JEV and DEN viral RNA-binding and antiviral activity (PubMed:23355615).1 Publication

<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
Q5D1E8

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
EOG091G03B2

Database for complete collections of gene phylogenies

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PhylomeDBi
Q5D1E8

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>Sequence (1+)i

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q5D1E8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGPCGEKPV LEASPTMSLW EFEDSHSRQG TPRPGQELAA EEASALELQM
60 70 80 90 100
KVDFFRKLGY SSTEIHSVLQ KLGVQADTNT VLGELVKHGT ATERERQTSP
110 120 130 140 150
DPCPQLPLVP RGGGTPKAPN LEPPLPEEEK EGSDLRPVVI DGSNVAMSHG
160 170 180 190 200
NKEVFSCRGI LLAVNWFLER GHTDITVFVP SWRKEQPRPD VPITDQHILR
210 220 230 240 250
ELEKKKILVF TPSRRVGGKR VVCYDDRFIV KLAYESDGIV VSNDTYRDLQ
260 270 280 290 300
GERQEWKRFI EERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPLTLE
310 320 330 340 350
HRKQPCPYGR KCTYGIKCRF FHPERPSCPQ RSVADELRAN ALLSPPRAPS
360 370 380 390 400
KDKNGRRPSP SSQSSSLLTE SEQCSLDGKK LGAQASPGSR QEGLTQTYAP
410 420 430 440 450
SGRSLAPSGG SGSSFGPTDW LPQTLDSLPY VSQDCLDSGI GSLESQMSEL
460 470 480 490 500
WGVRGGGPGE PGPPRAPYTG YSPYGSELPA TAAFSAFGRA MGAGHFSVPA
510 520 530 540 550
DYPPAPPAFP PREYWSEPYP LPPPTSVLQE PPVQSPGAGR SPWGRAGSLA
560 570 580 590
KEQASVYTKL CGVFPPHLVE AVMGRFPQLL DPQQLAAEIL SYKSQHPSE
Length:599
Mass (Da):65,699
Last modified:February 5, 2008 - v1
<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:i9213139FA7DCA443
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
R4GN17R4GN17_HUMAN
Endoribonuclease ZC3H12A
ZC3H12A
131Annotation score:

Annotation score:1 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>
A0A1W2PQC8A0A1W2PQC8_HUMAN
Endoribonuclease ZC3H12A
ZC3H12A
283Annotation score:

Annotation score:1 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 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 conflicti248D → G in CAG33645 (Ref. 3) Curated1
Sequence conflicti599E → D in CAG33645 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_052968240V → M. Corresponds to variant dbSNP:rs16824179Ensembl.1
Natural variantiVAR_044082547G → D3 PublicationsCorresponds to variant dbSNP:rs17849897Ensembl.1

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
AY920403 mRNA Translation: AAX14017.1
AK026884 mRNA Translation: BAB15581.1
CR457364 mRNA Translation: CAG33645.1
AL034379 Genomic DNA No translation available.
AL449284 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX07346.1
CH471059 Genomic DNA Translation: EAX07347.1
BC005001 mRNA Translation: AAH05001.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS417.1

NCBI Reference Sequences

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RefSeqi
NP_001310479.1, NM_001323550.1
NP_079355.2, NM_025079.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.656294

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000373087; ENSP00000362179; ENSG00000163874

Database of genes from NCBI RefSeq genomes

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GeneIDi
80149

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:80149

UCSC genome browser

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UCSCi
uc001cbb.5 human

Keywords - Coding sequence diversityi

Polymorphism

<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
AY920403 mRNA Translation: AAX14017.1
AK026884 mRNA Translation: BAB15581.1
CR457364 mRNA Translation: CAG33645.1
AL034379 Genomic DNA No translation available.
AL449284 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX07346.1
CH471059 Genomic DNA Translation: EAX07347.1
BC005001 mRNA Translation: AAH05001.1
CCDSiCCDS417.1
RefSeqiNP_001310479.1, NM_001323550.1
NP_079355.2, NM_025079.2
UniGeneiHs.656294

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
3V32X-ray2.00A/B112-296[»]
3V33X-ray2.00A/B112-334[»]
3V34X-ray2.00A/B112-296[»]
ProteinModelPortaliQ5D1E8
SMRiQ5D1E8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123141, 23 interactors
CORUMiQ5D1E8
IntActiQ5D1E8, 16 interactors
MINTiQ5D1E8
STRINGi9606.ENSP00000362174

PTM databases

iPTMnetiQ5D1E8
PhosphoSitePlusiQ5D1E8

Polymorphism and mutation databases

BioMutaiZC3H12A
DMDMi190479827

Proteomic databases

EPDiQ5D1E8
MaxQBiQ5D1E8
PaxDbiQ5D1E8
PeptideAtlasiQ5D1E8
PRIDEiQ5D1E8
ProteomicsDBi62741

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373087; ENSP00000362179; ENSG00000163874
GeneIDi80149
KEGGihsa:80149
UCSCiuc001cbb.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
80149
DisGeNETi80149
EuPathDBiHostDB:ENSG00000163874.8

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ZC3H12A
HGNCiHGNC:26259 ZC3H12A
HPAiHPA032052
HPA032053
MIMi610562 gene
neXtProtiNX_Q5D1E8
OpenTargetsiENSG00000163874
PharmGKBiPA142670537

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3777 Eukaryota
ENOG410ZNK1 LUCA
GeneTreeiENSGT00940000155107
HOGENOMiHOG000060218
HOVERGENiHBG108758
InParanoidiQ5D1E8
KOiK18668
OMAiYWSEPYQ
OrthoDBiEOG091G03B2
PhylomeDBiQ5D1E8
TreeFamiTF315783

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
ZC3H12A human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
80149

Protein Ontology

More...
PROi
PR:Q5D1E8

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000163874 Expressed in 131 organ(s), highest expression level in right adrenal gland
CleanExiHS_ZC3H12A
ExpressionAtlasiQ5D1E8 baseline and differential
GenevisibleiQ5D1E8 HS

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

More...
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_HUMAN
<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: Q5D1E8
Secondary accession number(s): D3DPT0, Q6I9Z1, Q9H5P1
<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: February 5, 2008
Last modified: December 5, 2018
This is version 94 of the entry and version 1 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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