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Protein

mRNA decay activator protein ZFP36

Gene

ZFP36

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • RNA polymerase binding Source: UniProtKB
  • single-stranded RNA binding Source: ProtInc

GO - Biological processi

  • 3'-UTR-mediated mRNA destabilization Source: UniProtKB
  • 3'-UTR-mediated mRNA stabilization Source: UniProtKB
  • cellular response to epidermal growth factor stimulus Source: UniProtKB
  • cellular response to fibroblast growth factor stimulus Source: UniProtKB
  • cellular response to glucocorticoid stimulus Source: UniProtKB
  • cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: UniProtKB
  • cellular response to lipopolysaccharide Source: UniProtKB
  • cellular response to tumor necrosis factor Source: UniProtKB
  • MAPK cascade Source: UniProtKB
  • miRNA mediated inhibition of translation Source: UniProtKB
  • mRNA catabolic process Source: UniProtKB
  • mRNA transport Source: UniProtKB
  • negative regulation of erythrocyte differentiation Source: UniProtKB
  • negative regulation of interleukin-2 biosynthetic process Source: UniProtKB
  • negative regulation of polynucleotide adenylyltransferase activity Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of viral transcription Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process, deadenylation-independent decay Source: UniProtKB
  • nuclear-transcribed mRNA poly(A) tail shortening Source: BHF-UCL
  • p38MAPK cascade Source: UniProtKB
  • positive regulation of deadenylation-independent decapping of nuclear-transcribed mRNA Source: UniProtKB
  • positive regulation of fat cell differentiation Source: UniProtKB
  • positive regulation of gene silencing by miRNA Source: UniProtKB
  • positive regulation of intracellular mRNA localization Source: UniProtKB
  • positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
  • positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: UniProtKB
  • regulation of keratinocyte apoptotic process Source: UniProtKB
  • regulation of keratinocyte differentiation Source: UniProtKB
  • regulation of keratinocyte proliferation Source: UniProtKB
  • regulation of mRNA stability Source: UniProtKB
  • regulation of tumor necrosis factor production Source: UniProtKB
  • response to starvation Source: UniProtKB
  • response to wounding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA transport, RNA-mediated gene silencing, Transport

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000128016-MONOMER.
ReactomeiR-HSA-450513. Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
SignaLinkiP26651.
SIGNORiP26651.

Names & Taxonomyi

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
Gene namesi
Name:ZFP36Imported
Synonyms:G0S24, NUP475By similarity, RNF162A, TIS11A, TTP1 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:12862. ZFP36.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytoplasmic stress granule Source: UniProtKB
  • cytosol Source: MGI
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • nucleus Source: UniProtKB
  • ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi7538.
PharmGKBiPA37451.

Polymorphism and mutation databases

BioMutaiZFP36.
DMDMi136471.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000891631 – 326mRNA decay activator protein ZFP36Add BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 vitroBy similarity1 Publication1
Modified residuei276Phosphoserine1 Publication1
Modified residuei296Phosphoserine1 Publication1
Modified residuei323PhosphoserineCombined sourcesBy similarity1

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

PaxDbiP26651.
PeptideAtlasiP26651.
PRIDEiP26651.

PTM databases

iPTMnetiP26651.
PhosphoSitePlusiP26651.

Expressioni

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

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

BgeeiENSG00000128016.
CleanExiHS_ZFP36.

Organism-specific databases

HPAiHPA006009.

Interactioni

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).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

Binary interactionsi

WithEntry#Exp.IntActNotes
DCP1AQ9NPI62EBI-374248,EBI-374238
EDC3Q96F862EBI-374248,EBI-997311

GO - Molecular functioni

  • 14-3-3 protein binding Source: UniProtKB
  • C-C chemokine binding Source: UniProtKB
  • enzyme binding Source: BHF-UCL
  • heat shock protein binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • RNA polymerase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113370. 50 interactors.
DIPiDIP-29845N.
IntActiP26651. 22 interactors.
MINTiMINT-1171915.
STRINGi9606.ENSP00000248673.

Structurei

Secondary structure

1326
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi317 – 322Combined sources6

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...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati71 – 75P-P-P-P-G5
Repeati198 – 202P-P-P-P-G5
Repeati219 – 223P-P-P-P-G5

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Domaini

The C3H1-type zinc finger domains are necessary for ARE-binding activity (PubMed:10330172).1 Publication

Sequence similaritiesi

Contains 2 C3H1-type zinc fingers.PROSITE-ProRule annotation

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

eggNOGiKOG1677. Eukaryota.
COG5063. LUCA.
HOGENOMiHOG000233479.
HOVERGENiHBG008483.
InParanoidiP26651.
KOiK15308.
PhylomeDBiP26651.
TreeFamiTF315463.

Family and domain databases

Gene3Di4.10.1000.10. 2 hits.
InterProiIPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00642. zf-CCCH. 2 hits.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 2 hits.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 2 hits.
PROSITEiPS50103. ZF_C3H1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:iDDD9AD950AF7AF98
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02106437P → S.1 PublicationCorresponds to variant rs17878633dbSNPEnsembl.1
Natural variantiVAR_05232455P → S.Corresponds to variant rs2229272dbSNPEnsembl.1
Natural variantiVAR_021065259I → F.1 PublicationCorresponds to variant rs17886974dbSNPEnsembl.1
Natural variantiVAR_021066324V → F.1 PublicationCorresponds to variant rs17884899dbSNPEnsembl.1

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.
PIRiS34427.
RefSeqiNP_003398.2. NM_003407.3.
UniGeneiHs.534052.

Genome annotation databases

EnsembliENST00000248673; ENSP00000248673; ENSG00000128016.
GeneIDi7538.
KEGGihsa:7538.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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.
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. 50 interactors.
DIPiDIP-29845N.
IntActiP26651. 22 interactors.
MINTiMINT-1171915.
STRINGi9606.ENSP00000248673.

PTM databases

iPTMnetiP26651.
PhosphoSitePlusiP26651.

Polymorphism and mutation databases

BioMutaiZFP36.
DMDMi136471.

Proteomic databases

PaxDbiP26651.
PeptideAtlasiP26651.
PRIDEiP26651.

Protocols and materials databases

DNASUi7538.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000248673; ENSP00000248673; ENSG00000128016.
GeneIDi7538.
KEGGihsa:7538.

Organism-specific databases

CTDi7538.
DisGeNETi7538.
GeneCardsiZFP36.
HGNCiHGNC:12862. ZFP36.
HPAiHPA006009.
MIMi190700. gene.
neXtProtiNX_P26651.
PharmGKBiPA37451.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1677. Eukaryota.
COG5063. LUCA.
HOGENOMiHOG000233479.
HOVERGENiHBG008483.
InParanoidiP26651.
KOiK15308.
PhylomeDBiP26651.
TreeFamiTF315463.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000128016-MONOMER.
ReactomeiR-HSA-450513. Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
SignaLinkiP26651.
SIGNORiP26651.

Miscellaneous databases

ChiTaRSiZFP36. human.
GeneWikiiZFP36.
GenomeRNAii7538.
PROiP26651.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000128016.
CleanExiHS_ZFP36.

Family and domain databases

Gene3Di4.10.1000.10. 2 hits.
InterProiIPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00642. zf-CCCH. 2 hits.
[Graphical view]
SMARTiSM00356. ZnF_C3H1. 2 hits.
[Graphical view]
SUPFAMiSSF90229. SSF90229. 2 hits.
PROSITEiPS50103. ZF_C3H1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTTP_HUMAN
AccessioniPrimary (citable) accession number: P26651
Secondary accession number(s): B2RA54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 30, 2016
This is version 162 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.