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UniProtKB - P26651 (TTP_HUMAN)

Protein

mRNA decay activator protein ZFP36

Gene

ZFP36

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

Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:9703499, PubMed:10330172, PubMed:10751406, PubMed:11279239, PubMed:12115244, PubMed:12748283, PubMed:15187101, PubMed:15634918, PubMed:17030620, PubMed:16702957, PubMed:20702587, PubMed:20221403, PubMed:21775632, PubMed:27193233, PubMed:23644599, PubMed:25815583). Acts as an 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (PubMed:15687258, PubMed:23644599). Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1, and hence promotes ARE-mediated mRNA deadenylation (PubMed:23644599). Functions also by recruiting components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs (PubMed:11719186, PubMed:12748283, PubMed:15687258, PubMed:16364915). Self regulates by destabilizing its own mRNA (PubMed:15187101). Binds to 3'-UTR ARE of numerous mRNAs and of its own mRNA (PubMed:10330172, PubMed:10751406, PubMed:12115244, PubMed:15187101, PubMed:15634918, PubMed:17030620, PubMed:16702957, PubMed:19188452, PubMed:20702587, PubMed:20221403, PubMed:21775632, PubMed:25815583). Plays a role in anti-inflammatory responses; suppresses tumor necrosis factor (TNF)-alpha production by stimulating ARE-mediated TNF-alpha mRNA decay and several other inflammatory ARE-containing mRNAs in interferon (IFN)- and/or lipopolysaccharide (LPS)-induced macrophages (By similarity). Plays also a role in the regulation of dendritic cell maturation at the post-transcriptional level, and hence operates as part of a negative feedback loop to limit the inflammatory response (PubMed:18367721). Promotes ARE-mediated mRNA decay of hypoxia-inducible factor HIF1A mRNA during the response of endothelial cells to hypoxia (PubMed:21775632). Positively regulates early adipogenesis of preadipocytes by promoting ARE-mediated mRNA decay of immediate early genes (IEGs) (By similarity). Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA (PubMed:20702587). Plays a role in maintaining skeletal muscle satellite cell quiescence by promoting ARE-mediated mRNA decay of the myogenic determination factor MYOD1 mRNA (By similarity). Associates also with and regulates the expression of non-ARE-containing target mRNAs at the post-transcriptional level, such as MHC class I mRNAs (PubMed:18367721). Participates in association with argonaute RISC catalytic components in the ARE-mediated mRNA decay mechanism; assists microRNA (miRNA) targeting ARE-containing mRNAs (PubMed:15766526). May also play a role in the regulation of cytoplasmic mRNA decapping; enhances decapping of ARE-containing RNAs, in vitro (PubMed:16364915). Involved in the delivery of target ARE-mRNAs to processing bodies (PBs) (PubMed:17369404). In addition to its cytosolic mRNA-decay function, affects nuclear pre-mRNA processing (By similarity). Negatively regulates nuclear poly(A)-binding protein PABPN1-stimulated polyadenylation activity on ARE-containing pre-mRNA during LPS-stimulated macrophages (By similarity). Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion (By similarity). Plays a role in the regulation of keratinocyte proliferation, differentiation and apoptosis (PubMed:27182009). Plays a role as a tumor suppressor by inhibiting cell proliferation in breast cancer cells (PubMed:26926077).By similarity25 Publications
(Microbial infection) Negatively regulates HTLV-1 TAX-dependent transactivation of viral long terminal repeat (LTR) promoter.1 Publication

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 fingeri103 – 131C3H1-type 1PROSITE-ProRule annotationAdd BLAST29
Zinc fingeri141 – 169C3H1-type 2PROSITE-ProRule annotationAdd BLAST29

<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

  • 14-3-3 protein binding Source: UniProtKB
  • AU-rich element binding Source: UniProtKB
  • C-C chemokine binding Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • enzyme binding Source: BHF-UCL
  • heat shock protein binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • mRNA 3'-UTR AU-rich region binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: GO_Central
  • mRNA binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA polymerase binding Source: UniProtKB
  • single-stranded RNA binding Source: ProtInc
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionDNA-binding, Ribonucleoprotein, RNA-binding
Biological processmRNA transport, RNA-mediated gene silencing, Transport
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-450513 Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P26651

SIGNOR Signaling Network Open Resource

More...SIGNORi		P26651

<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:
mRNA decay activator protein ZFP36Curated
Alternative name(s):
G0/G1 switch regulatory protein 24
Growth factor-inducible nuclear protein NUP475Curated
Tristetraprolin1 Publication
Zinc finger protein 36Imported
Short name:
Zfp-36By similarity
<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:ZFP36Imported
Synonyms:G0S24, NUP475By similarity, RNF162A, TIS11A, TTP1 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>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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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: Unplaced

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:12862 ZFP36

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		190700 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P26651

<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, Exosome, 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

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>Mutagenesisi60S → A: Inhibits PKM-induced ZFP36 degradation through a p38 MAPK signaling pathway. 1 Publication1
Mutagenesisi124C → R: Inhibits binding to ARE-containing transcripts. Inhibits binding to and deadenylation activities of ARE-containing mRNAs. Inhibits localization of ARE-containing mRNAs to processing bodies (PBs). 5 Publications1
Mutagenesisi126F → N: Inhibits ARE-containing RNA-binding, deadenylation and RNA decapping activities. 3 Publications1
Mutagenesisi147C → R: Inhibits both ARE-binding and mRNA deadenylation activities. 1 Publication1
Mutagenesisi309P → V: Inhibits interaction with SH3KBP1. 1 Publication1
Mutagenesisi315R → A: Abolishes interaction with CNOT1. 1 Publication1
Mutagenesisi319F → A: Abolishes interaction with CNOT1 and impairs TNF mRNA deadenylation. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		7538

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA37451

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ZFP36

Domain mapping of disease mutations (DMDM)

More...DMDMi		136471

<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_00000891631 – 326mRNA decay activator protein ZFP36Add BLAST326

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 residuei60Phosphoserine; by MAPKAPK2By similarity1
Modified residuei66Phosphoserine2 Publications1
Modified residuei88Phosphoserine1 Publication1
Modified residuei90PhosphoserineBy similarity1
Modified residuei92Phosphothreonine1 Publication1
Modified residuei93PhosphoserineCombined sources1 Publication1
Modified residuei169Phosphoserine1 Publication1
Modified residuei186Phosphoserine; by MAPKAPK2Combined sources1 Publication1
Modified residuei197Phosphoserine1 Publication1
Modified residuei218Phosphoserine1 Publication1
Modified residuei228Phosphoserine; by MAPK1; in vitro1 Publication1
Modified residuei276Phosphoserine1 Publication1
Modified residuei296Phosphoserine1 Publication1
Modified residuei323PhosphoserineCombined sources1

<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. Phosphorylation at serine and/or threonine residues occurs in a p38 MAPK- and MAPKAPK2-dependent manner (PubMed:16702957). Phosphorylated by MAPKAPK2 at Ser-60 and Ser-186; phosphorylation increases its stability and cytoplasmic localization, promotes binding to 14-3-3 adapter proteins and inhibits the recruitment of cytoplasmic CCR4-NOT and PAN2-PAN3 deadenylase complexes to the mRNA decay machinery, thereby inhibiting ZFP36-induced ARE-containing mRNA deadenylation and decay processes. Phosphorylation by MAPKAPK2 does not impair ARE-containing RNA-binding. Phosphorylated in a MAPKAPK2- and p38 MAPK-dependent manner upon skeletal muscle satellite cell activation; this phosphorylation inhibits ZFP36-mediated mRNA decay activity, and hence stabilizes MYOD1 mRNA (By similarity). Phosphorylated by MAPK1 upon mitogen stimulation (By similarity). Phosphorylated at Ser-66 and Ser-93; these phosphorylations increase in a SH3KBP1-dependent manner (PubMed:20221403). Phosphorylated at serine and threonine residues in a pyruvate kinase PKM- and p38 MAPK-dependent manner (PubMed:26926077). Phosphorylation at Ser-60 may participate in the PKM-mediated degradation of ZFP36 in a p38 MAPK-dependent manner (PubMed:26926077). Dephosphorylated by serine/threonine phosphatase 2A at Ser-186 (By similarity).By similarity3 Publications
Ubiquitinated; pyruvate kinase (PKM)-dependent ubiquitination leads to proteasomal degradation through a p38 MAPK signaling pathway (PubMed:26926077).1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P26651

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P26651

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

More...PaxDbi		P26651

PeptideAtlas

More...PeptideAtlasi		P26651

PRoteomics IDEntifications database

More...PRIDEi		P26651

ProteomicsDB human proteome resource

More...ProteomicsDBi		54360

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P26651

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

More...PhosphoSitePlusi		P26651

<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 both basal and suprabasal epidermal layers (PubMed:27182009). Expressed in epidermal keratinocytes (PubMed:27182009). Expressed strongly in mature dendritic cells (PubMed:18367721). Expressed in immature dendritic cells (at protein level) (PubMed:18367721).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 T cell activation (PubMed:15634918). Up-regulated in keratinocytes in response to wounding (PubMed:27182009). Up-regulated by lipopolysaccharide (LPS) in a p38 MAPK- and ERK-dependent manner (at protein level) (PubMed:15187101, PubMed:16508015). Up-regulated strongly during epidermal repair after wounding in keratinocytes (PubMed:20166898). Up-regulated strongly by epidermal growth factor (EGF) and tumor necrosis factor (TNF-alpha) in keratinocytes (PubMed:20166898). Up-regulated moderately by granulocyte macrophage colony-stimulating factor (GM-CSF) and fibroblast growth factor (FGF1) in keratinocytes (PubMed:20166898). Up-regulated also by glucocorticoid dexamethasone in keratinocytes (PubMed:20166898). Up-regulated in keratinocytes in response to wounding (PubMed:27182009). Up-regulated by LPS in a p38 MAPK-dependent manner (PubMed:14766228, PubMed:15187101).6 Publications

Gene expression databases

CleanEx database of gene expression profiles

More...CleanExi		HS_ZFP36

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA006009

<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

Associates with cytoplasmic CCR4-NOT and PAN2-PAN3 deadenylase complexes to trigger ARE-containing mRNA deadenylation and decay processes (By similarity). Part of a mRNA decay activation complex at least composed of poly(A)-specific exoribonucleases CNOT6, EXOSC2 and XRN1 and mRNA-decapping enzymes DCP1A and DCP2 (PubMed:15687258). Associates with the RNA exosome complex (PubMed:11719186). Interacts (via phosphorylated form) with 14-3-3 proteins; these interactions promote exclusion of ZFP36 from cytoplasmic stress granules in response to arsenite treatment in a MAPKAPK2-dependent manner and does not prevent CCR4-NOT deadenylase complex recruitment or ZFP36-induced ARE-containing mRNA deadenylation and decay processes (By similarity). Interacts with 14-3-3 proteins; these interactions occur in response to rapamycin in an Akt-dependent manner (PubMed:16702957). Interacts with AGO2 and AGO4 (PubMed:15766526). Interacts (via C-terminus) with CNOT1; this interaction occurs in a RNA-independent manner and induces mRNA deadenylation (PubMed:23644599). Interacts (via N-terminus) with CNOT6 (PubMed:15687258). Interacts with CNOT6L (By similarity). Interacts (via C-terminus) with CNOT7; this interaction occurs in a RNA-independent manner, induces mRNA deadenylation and is inhibited in a phosphorylation MAPKAPK2-dependent manner (PubMed:25106868). Interacts (via unphosphorylated form) with CNOT8; this interaction occurs in a RNA-independent manner and is inhibited in a phosphorylation MAPKAPK2-dependent manner (By similarity). Interacts with DCP1A (PubMed:15687258). Interacts (via N-terminus) with DCP2 (PubMed:15687258, PubMed:16364915). Interacts with EDC3 (PubMed:16364915). Interacts (via N-terminus) with EXOSC2 (PubMed:15687258). Interacts with heat shock 70 kDa proteins (PubMed:20221403). Interacts with KHSRP; this interaction increases upon cytokine-induced treatment (PubMed:16126846). Interacts with MAP3K4; this interaction enhances the association with SH3KBP1/CIN85 (PubMed:20221403). Interacts with MAPKAPK2; this interaction occurs upon skeletal muscle satellite cell activation (By similarity). Interacts with NCL (PubMed:20221403). Interacts with NUP214; this interaction increases upon lipopolysaccharide (LPS) stimulation (PubMed:14766228). Interacts with PABPC1; this interaction occurs in a RNA-dependent manner (PubMed:20221403). Interacts (via hypophosphorylated form) with PABPN1 (via RRM domain and C-terminal arginine-rich region); this interaction occurs in the nucleus in a RNA-independent manner, decreases in presence of single-stranded poly(A) RNA-oligomer and in a p38 MAPK-dependent-manner and inhibits nuclear poly(A) tail synthesis (By similarity). Interacts with PAN2 (By similarity). Interacts (via C3H1-type zinc finger domains) with PKM (PubMed:26926077). Interacts (via C3H1-type zinc finger domains) with nuclear RNA poly(A) polymerase (By similarity). Interacts with PPP2CA; this interaction occurs in LPS-stimulated cells and induces ZFP36 dephosphorylation, and hence may promote ARE-containing mRNAs decay (By similarity). Interacts (via C-terminus) with PRR5L (via C-terminus); this interaction may accelerate ZFP36-mediated mRNA decay during stress (PubMed:21964062). Interacts (via C-terminus) with SFN; this interaction occurs in a phosphorylation-dependent manner (By similarity). Interacts (via extreme C-terminal region) with SH3KBP1/CIN85 (via SH3 domains); this interaction enhances MAP3K4-induced phosphorylation of ZFP36 at Ser-66 and Ser-93 and does not alter neither ZFP36 binding to ARE-containing transcripts nor TNF-alpha mRNA decay (PubMed:20221403). Interacts with XRN1 (PubMed:15687258). Interacts (via C-terminus and Ser-186 phosphorylated form) with YWHAB; this interaction occurs in a p38/MAPKAPK2-dependent manner, increases cytoplasmic localization of ZFP36 and protects ZFP36 from Ser-186 dephosphorylation by serine/threonine phosphatase 2A, and hence may be crucial for stabilizing ARE-containing mRNAs (By similarity). Interacts (via phosphorylated form) with YWHAE (By similarity). Interacts (via C-terminus) with YWHAG; this interaction occurs in a phosphorylation-dependent manner (By similarity). Interacts with YWHAH; this interaction occurs in a phosphorylation-dependent manner (By similarity). Interacts with YWHAQ; this interaction occurs in a phosphorylation-dependent manner (By similarity). Interacts with (via C-terminus) YWHAZ; this interaction occurs in a phosphorylation-dependent manner (By similarity). Interacts (via P-P-P-P-G repeats) with GIGYF2; the interaction is direct (By similarity).By similarity12 Publications
(Microbial infection) Interacts (via C-terminus) with HTLV-1 TAX (via C-terminus); this interaction inhibits HTLV-1 TAX to transactivate viral long terminal repeat (LTR) promoter (PubMed:14679154).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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		113370, 57 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P26651

Database of interacting proteins

More...DIPi		DIP-29845N

Protein interaction database and analysis system

More...IntActi		P26651, 26 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000248673

<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

1326
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4J8SX-ray1.55B312-326[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P26651

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

More...SMRi		P26651

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati71 – 75P-P-P-P-G5
Repeati198 – 202P-P-P-P-G5
Repeati219 – 223P-P-P-P-G5

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>Regioni1 – 174Necessary for localization of ARE-containing mRNAs to processing bodies (PBs)1 PublicationAdd BLAST174
Regioni1 – 100Necessary and sufficient for the association with mRNA decay enzymes and mRNA decay activation1 PublicationAdd BLAST100
Regioni1 – 15Necessary for nuclear exportBy similarityAdd BLAST15
Regioni95 – 168Necessary for nuclear localizationBy similarityAdd BLAST74
Regioni97 – 173Necessary for RNA-binding2 PublicationsAdd BLAST77
Regioni100 – 326Necessary for localization of ARE-containing mRNAs to processing bodies (PBs)1 PublicationAdd BLAST227
Regioni103 – 194Necessary for interaction with PABPN1By similarityAdd BLAST92
Regioni174 – 326Necessary for mRNA decay activation1 PublicationAdd BLAST153
Regioni312 – 326Interaction with CNOT11 PublicationAdd BLAST15

<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 domains are necessary for ARE-binding activity (PubMed:10330172).1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri103 – 131C3H1-type 1PROSITE-ProRule annotationAdd BLAST29
Zinc fingeri141 – 169C3H1-type 2PROSITE-ProRule annotationAdd BLAST29

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1677 Eukaryota
COG5063 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000233479

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG008483

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P26651

KEGG Orthology (KO)

More...KOi		K15308

Database of Orthologous Groups

More...OrthoDBi		1541140at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P26651

TreeFam database of animal gene trees

More...TreeFami		TF315463

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000571 Znf_CCCH
IPR036855 Znf_CCCH_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00642 zf-CCCH, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00356 ZnF_C3H1, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF90229 SSF90229, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50103 ZF_C3H1, 2 hits

<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 4 potential isoforms that are computationally mapped.Show allAlign All

P26651-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDLTAIYESL LSLSPDVPVP SDHGGTESSP GWGSSGPWSL SPSDSSPSGV 
        60         70         80         90        100
TSRLPGRSTS LVEGRSCGWV PPPPGFAPLA PRLGPELSPS PTSPTATSTT 
       110        120        130        140        150
PSRYKTELCR TFSESGRCRY GAKCQFAHGL GELRQANRHP KYKTELCHKF 
       160        170        180        190        200
YLQGRCPYGS RCHFIHNPSE DLAAPGHPPV LRQSISFSGL PSGRRTSPPP 
       210        220        230        240        250
PGLAGPSLSS SSFSPSSSPP PPGDLPLSPS AFSAAPGTPL ARRDPTPVCC 
       260        270        280        290        300
PSCRRATPIS VWGPLGGLVR TPSVQSLGSD PDEYASSGSS LGGSDSPVFE 
       310        320 
AGVFAPPQPV AAPRRLPIFN RISVSE
Length:326
Mass (Da):34,003
Last modified:August 1, 1992 - 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:iDDD9AD950AF7AF98
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0QY76M0QY76_HUMAN
Zinc finger protein 36, C3H type, h...
ZFP36 hCG_43352
332Annotation score:

Annotation score:3 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>
M0R0H3M0R0H3_HUMAN
mRNA decay activator protein ZFP36
ZFP36
343Annotation 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>
M0QZ04M0QZ04_HUMAN
mRNA decay activator protein ZFP36
ZFP36
148Annotation 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>
M0R252M0R252_HUMAN
mRNA decay activator protein ZFP36
ZFP36
71Annotation 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>

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_02106437P → S1 PublicationCorresponds to variant dbSNP:rs17878633Ensembl.1
Natural variantiVAR_05232455P → S. Corresponds to variant dbSNP:rs2229272Ensembl.1
Natural variantiVAR_021065259I → F1 PublicationCorresponds to variant dbSNP:rs17886974Ensembl.1
Natural variantiVAR_021066324V → F1 PublicationCorresponds to variant dbSNP:rs17884899Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M92843 mRNA Translation: AAA58489.1
M92844 Genomic DNA Translation: AAC37600.1
M63625 mRNA Translation: AAA61240.1
AK314042 mRNA Translation: BAG36751.1
AY771351 Genomic DNA Translation: AAV28731.1
BC009693 mRNA Translation: AAH09693.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS12534.2

Protein sequence database of the Protein Information Resource

More...PIRi		S34427

NCBI Reference Sequences

More...RefSeqi		NP_003398.2, NM_003407.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.534052

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000248673; ENSP00000248673; ENSG00000128016

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7538

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7538

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92843 mRNA Translation: AAA58489.1
M92844 Genomic DNA Translation: AAC37600.1
M63625 mRNA Translation: AAA61240.1
AK314042 mRNA Translation: BAG36751.1
AY771351 Genomic DNA Translation: AAV28731.1
BC009693 mRNA Translation: AAH09693.1
CCDSiCCDS12534.2
PIRiS34427
RefSeqiNP_003398.2, NM_003407.3
UniGeneiHs.534052

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4J8SX-ray1.55B312-326[»]
ProteinModelPortaliP26651
SMRiP26651
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113370, 57 interactors
CORUMiP26651
DIPiDIP-29845N
IntActiP26651, 26 interactors
STRINGi9606.ENSP00000248673

PTM databases

iPTMnetiP26651
PhosphoSitePlusiP26651

Polymorphism and mutation databases

BioMutaiZFP36
DMDMi136471

Proteomic databases

EPDiP26651
jPOSTiP26651
PaxDbiP26651
PeptideAtlasiP26651
PRIDEiP26651
ProteomicsDBi54360

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		7538
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000248673; ENSP00000248673; ENSG00000128016
GeneIDi7538
KEGGihsa:7538

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7538
DisGeNETi7538

GeneCards: human genes, protein and diseases

More...GeneCardsi		ZFP36
HGNCiHGNC:12862 ZFP36
HPAiHPA006009
MIMi190700 gene
neXtProtiNX_P26651
PharmGKBiPA37451

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1677 Eukaryota
COG5063 LUCA
HOGENOMiHOG000233479
HOVERGENiHBG008483
InParanoidiP26651
KOiK15308
OrthoDBi1541140at2759
PhylomeDBiP26651
TreeFamiTF315463

Enzyme and pathway databases

ReactomeiR-HSA-450513 Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA
SignaLinkiP26651
SIGNORiP26651

Miscellaneous databases

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

More...ChiTaRSi		ZFP36 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		ZFP36

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

More...GenomeRNAii		7538

Protein Ontology

More...PROi		PR:P26651

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

CleanExiHS_ZFP36

Family and domain databases

InterProiView protein in InterPro
IPR000571 Znf_CCCH
IPR036855 Znf_CCCH_sf
PfamiView protein in Pfam
PF00642 zf-CCCH, 2 hits
SMARTiView protein in SMART
SM00356 ZnF_C3H1, 2 hits
SUPFAMiSSF90229 SSF90229, 2 hits
PROSITEiView protein in PROSITE
PS50103 ZF_C3H1, 2 hits

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 nameiTTP_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: P26651
Secondary accession number(s): B2RA54
<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: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 16, 2019
This is version 178 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
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