ZFP36
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4J8S
Identifiers
Aliases	ZFP36, G0S24, GOS24, NUP475, RNF162A, TIS11, TTP, zfp-36, ZFP36 ring finger protein
External IDs	OMIM: 190700 MGI: 99180 HomoloGene: 2558 GeneCards: ZFP36
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19q13.2 Start 39,406,847 bp[1] End 39,409,412 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7 A3|7 16.72 cM Start 28,076,209 bp[2] End 28,079,678 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in vena cava gastric mucosa left uterine tube trachea saphenous vein cardia nipple gallbladder upper lobe of left lung right lung Top expressed in left lobe of liver ascending aorta aortic valve jejunum left lung lobe duodenum islet of Langerhans spleen right lung blood More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding C-C chemokine binding 14-3-3 protein binding metal ion binding protein binding single-stranded RNA binding mRNA 3'-UTR AU-rich region binding enzyme binding mRNA binding protein kinase binding RNA binding heat shock protein binding RNA polymerase binding mRNA 3'-UTR binding Cellular component cytoplasm cytoplasmic stress granule nucleus RISC-loading complex ribonucleoprotein complex Dcp1-Dcp2 complex exosome (RNase complex) P-body cytosol CCR4-NOT complex Biological process nuclear-transcribed mRNA poly(A) tail shortening positive regulation of nuclear-transcribed mRNA poly(A) tail shortening mRNA catabolic process regulation of tumor necrosis factor production negative regulation of transcription by RNA polymerase II nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay miRNA-mediated gene silencing by inhibition of translation response to starvation 3'-UTR-mediated mRNA stabilization negative regulation of erythrocyte differentiation cellular response to lipopolysaccharide cellular response to tumor necrosis factor positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay positive regulation of deadenylation-independent decapping of nuclear-transcribed mRNA regulation of keratinocyte apoptotic process regulation of keratinocyte proliferation positive regulation of fat cell differentiation cellular response to fibroblast growth factor stimulus cellular response to granulocyte macrophage colony-stimulating factor stimulus negative regulation of viral transcription regulation of keratinocyte differentiation response to wounding positive regulation of gene silencing by miRNA regulation of mRNA stability MAPK cascade cellular response to glucocorticoid stimulus cellular response to epidermal growth factor stimulus positive regulation of intracellular mRNA localization p38MAPK cascade nuclear-transcribed mRNA catabolic process, deadenylation-independent decay gene silencing mRNA transport 3'-UTR-mediated mRNA destabilization negative regulation of polynucleotide adenylyltransferase activity transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7538 22695 Ensembl ENSG00000128016 ENSMUSG00000044786 UniProt P26651 P22893 RefSeq (mRNA) NM_003407 NM_011756 RefSeq (protein) NP_003398 NP_035886 Location (UCSC) Chr 19: 39.41 – 39.41 Mb Chr 7: 28.08 – 28.08 Mb PubMed search [3] [4]
Wikidata
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Tristetraprolin (TTP), also known as zinc finger protein 36 homolog (ZFP36), is a protein that in humans, mice and rats is encoded by the ZFP36 gene.^[5][6] It is a member of the TIS11 (TPA-induced sequence) family, along with butyrate response factors 1 and 2.^[7]

TTP binds to AU-rich elements (AREs) in the 3'-untranslated regions (UTRs) of the mRNAs of some cytokines and promotes their degradation. For example, TTP is a component of a negative feedback loop that interferes with TNF-alpha production by destabilizing its mRNA.^[8] Mice deficient in TTP develop a complex syndrome of inflammatory diseases.^[8]

Interactions

ZFP36 has been shown to interact with 14-3-3 protein family members, such as YWHAH,^[9] and with NUP214, a member of the nuclear pore complex.^[10]

Regulation

Post-transcriptionally, TTP is regulated in several ways.^[7] The subcellular localization of TTP is influenced by interactions with protein partners such as the 14-3-3 family of proteins. These interactions and, possibly, interactions with target mRNAs are affected by the phosphorylation state of TTP, as the protein can be posttranslationally modified by a large number of protein kinases.^[7] There is some evidence that the TTP transcript may also be targeted by microRNAs, such as miR-29a.^[7]