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mRNA decay activator protein ZFP36 (G0/G1 switch regulatory protein 24) (Growth factor-inducible nuclear protein NUP475) (Tristetraprolin) (Zinc finger protein 36) (Zfp-36)

 TTP_HUMAN               Reviewed;         326 AA.
P26651; B2RA54;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
25-OCT-2017, entry version 170.
RecName: Full=mRNA decay activator protein ZFP36 {ECO:0000305};
AltName: Full=G0/G1 switch regulatory protein 24;
AltName: Full=Growth factor-inducible nuclear protein NUP475 {ECO:0000305};
AltName: Full=Tristetraprolin {ECO:0000303|PubMed:2062660};
AltName: Full=Zinc finger protein 36 {ECO:0000312|HGNC:HGNC:12862};
Short=Zfp-36 {ECO:0000250|UniProtKB:P22893};
Name=ZFP36 {ECO:0000312|HGNC:HGNC:12862};
Synonyms=G0S24, NUP475 {ECO:0000250|UniProtKB:P22893}, RNF162A,
TIS11A, TTP {ECO:0000303|PubMed:2062660};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=2062660; DOI=10.1093/nar/19.12.3454;
Taylor G.A., Lai W.S., Oakey R.J., Seldin M.F., Shows T.B.,
Eddy R.L. Jr., Blackshear P.J.;
"The human TTP protein: sequence, alignment with related proteins, and
chromosomal localization of the mouse and human genes.";
Nucleic Acids Res. 19:3454-3454(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-37; PHE-259 AND
PHE-324.
NIEHS SNPs program;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND RNA-BINDING.
PubMed=9703499; DOI=10.1126/science.281.5379.1001;
Carballo E., Lai W.S., Blackshear P.J.;
"Feedback inhibition of macrophage tumor necrosis factor-alpha
production by tristetraprolin.";
Science 281:1001-1005(1998).
[6]
FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS
OF CYS-124 AND CYS-147.
PubMed=10330172; DOI=10.1128/MCB.19.6.4311;
Lai W.S., Carballo E., Strum J.R., Kennington E.A., Phillips R.S.,
Blackshear P.J.;
"Evidence that tristetraprolin binds to AU-rich elements and promotes
the deadenylation and destabilization of tumor necrosis factor alpha
mRNA.";
Mol. Cell. Biol. 19:4311-4323(1999).
[7]
FUNCTION, AND RNA-BINDING.
PubMed=10751406; DOI=10.1074/jbc.M001696200;
Lai W.S., Carballo E., Thorn J.M., Kennington E.A., Blackshear P.J.;
"Interactions of CCCH zinc finger proteins with mRNA. Binding of
tristetraprolin-related zinc finger proteins to Au-rich elements and
destabilization of mRNA.";
J. Biol. Chem. 275:17827-17837(2000).
[8]
FUNCTION, AND ASSOCIATION WITH THE RNA EXOSOME COMPLEX.
PubMed=11719186; DOI=10.1016/S0092-8674(01)00578-5;
Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R.,
Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.;
"AU binding proteins recruit the exosome to degrade ARE-containing
mRNAs.";
Cell 107:451-464(2001).
[9]
FUNCTION.
PubMed=11279239; DOI=10.1074/jbc.M100680200;
Lai W.S., Blackshear P.J.;
"Interactions of CCCH zinc finger proteins with mRNA: tristetraprolin-
mediated AU-rich element-dependent mRNA degradation can occur in the
absence of a poly(A) tail.";
J. Biol. Chem. 276:23144-23154(2001).
[10]
FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=12115244; DOI=10.1002/art.10235;
Brooks S.A., Connolly J.E., Diegel R.J., Fava R.A., Rigby W.F.;
"Analysis of the function, expression, and subcellular distribution of
human tristetraprolin.";
Arthritis Rheum. 46:1362-1370(2002).
[11]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HTLV-1 TAX (MICROBIAL
INFECTION), AND SUBCELLULAR LOCATION (MICROBIAL INFECTION).
PubMed=14679154; DOI=10.1093/jnci/djg118;
Twizere J.-C., Kruys V., Lefebvre L., Vanderplasschen A., Collete D.,
Debacq C., Lai W.S., Jauniaux J.-C., Bernstein L.R., Semmes J.O.,
Burny A., Blackshear P.J., Kettmann R., Willems L.;
"Interaction of retroviral Tax oncoproteins with tristetraprolin and
regulation of tumor necrosis factor-alpha expression.";
J. Natl. Cancer Inst. 95:1846-1859(2003).
[12]
FUNCTION, RNA-BINDING, AND MUTAGENESIS OF CYS-124.
PubMed=12748283; DOI=10.1128/MCB.23.11.3798-3812.2003;
Lai W.S., Kennington E.A., Blackshear P.J.;
"Tristetraprolin and its family members can promote the cell-free
deadenylation of AU-rich element-containing mRNAs by poly(A)
ribonuclease.";
Mol. Cell. Biol. 23:3798-3812(2003).
[13]
INTERACTION WITH NUP214, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=14766228; DOI=10.1016/j.bbrc.2004.01.080;
Carman J.A., Nadler S.G.;
"Direct association of tristetraprolin with the nucleoporin
CAN/Nup214.";
Biochem. Biophys. Res. Commun. 315:445-449(2004).
[14]
SUBCELLULAR LOCATION.
PubMed=15014438; DOI=10.1038/sj.emboj.7600163;
Stoecklin G., Stubbs T., Kedersha N., Wax S., Rigby W.F.,
Blackwell T.K., Anderson P.;
"MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule
association and ARE-mRNA decay.";
EMBO J. 23:1313-1324(2004).
[15]
FUNCTION, RNA-BINDING, AND INDUCTION.
PubMed=15187101; DOI=10.4049/jimmunol.172.12.7263;
Brooks S.A., Connolly J.E., Rigby W.F.;
"The role of mRNA turnover in the regulation of tristetraprolin
expression: evidence for an extracellular signal-regulated kinase-
specific, AU-rich element-dependent, autoregulatory pathway.";
J. Immunol. 172:7263-7271(2004).
[16]
FUNCTION, AND INTERACTION WITH AGO2 AND AGO4.
PubMed=15766526; DOI=10.1016/j.cell.2004.12.038;
Jing Q., Huang S., Guth S., Zarubin T., Motoyama A., Chen J.,
Di Padova F., Lin S.C., Gram H., Han J.;
"Involvement of microRNA in AU-rich element-mediated mRNA
instability.";
Cell 120:623-634(2005).
[17]
FUNCTION, IDENTIFICATION IN A MRNA DECAY ACTIVATION COMPLEX, AND
INTERACTION WITH CNOT6; DCP1A; DCP2; EXOSC2 AND XRN1.
PubMed=15687258; DOI=10.1101/gad.1282305;
Lykke-Andersen J., Wagner E.;
"Recruitment and activation of mRNA decay enzymes by two ARE-mediated
decay activation domains in the proteins TTP and BRF-1.";
Genes Dev. 19:351-361(2005).
[18]
FUNCTION, RNA-BINDING, AND INDUCTION.
PubMed=15634918; DOI=10.4049/jimmunol.174.2.953;
Ogilvie R.L., Abelson M., Hau H.H., Vlasova I., Blackshear P.J.,
Bohjanen P.R.;
"Tristetraprolin down-regulates IL-2 gene expression through AU-rich
element-mediated mRNA decay.";
J. Immunol. 174:953-961(2005).
[19]
FUNCTION, INTERACTION WITH DCP2 AND EDC3, AND MUTAGENESIS OF PHE-126.
PubMed=16364915; DOI=10.1016/j.molcel.2005.10.031;
Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.;
"Multiple processing body factors and the ARE binding protein TTP
activate mRNA decapping.";
Mol. Cell 20:905-915(2005).
[20]
INTERACTION WITH KHSRP.
PubMed=16126846; DOI=10.1093/nar/gki797;
Linker K., Pautz A., Fechir M., Hubrich T., Greeve J., Kleinert H.;
"Involvement of KSRP in the post-transcriptional regulation of human
iNOS expression-complex interplay of KSRP with TTP and HuR.";
Nucleic Acids Res. 33:4813-4827(2005).
[21]
PHOSPHORYLATION AT SER-66; SER-88; THR-92; SER-169; SER-186; SER-197;
SER-218; SER-228; SER-276 AND SER-296.
PubMed=16262601; DOI=10.1042/BJ20051316;
Cao H., Deterding L.J., Venable J.D., Kennington E.A., Yates J.R. III,
Tomer K.B., Blackshear P.J.;
"Identification of the anti-inflammatory protein tristetraprolin as a
hyperphosphorylated protein by mass spectrometry and site-directed
mutagenesis.";
Biochem. J. 394:285-297(2006).
[22]
INDUCTION.
PubMed=16508015; DOI=10.1128/MCB.26.6.2408-2418.2006;
Brook M., Tchen C.R., Santalucia T., McIlrath J., Arthur J.S.,
Saklatvala J., Clark A.R.;
"Posttranslational regulation of tristetraprolin subcellular
localization and protein stability by p38 mitogen-activated protein
kinase and extracellular signal-regulated kinase pathways.";
Mol. Cell. Biol. 26:2408-2418(2006).
[23]
FUNCTION, RNA-BINDING, AND MUTAGENESIS OF CYS-124.
PubMed=17030620; DOI=10.1128/MCB.00945-06;
Lai W.S., Parker J.S., Grissom S.F., Stumpo D.J., Blackshear P.J.;
"Novel mRNA targets for tristetraprolin (TTP) identified by global
analysis of stabilized transcripts in TTP-deficient fibroblasts.";
Mol. Cell. Biol. 26:9196-9208(2006).
[24]
FUNCTION, RNA-BINDING, INTERACTION WITH 14-3-3 PROTEINS, AND
PHOSPHORYLATION.
PubMed=16702957; DOI=10.1038/sj.onc.1209645;
Marderosian M., Sharma A., Funk A.P., Vartanian R., Masri J., Jo O.D.,
Gera J.F.;
"Tristetraprolin regulates Cyclin D1 and c-Myc mRNA stability in
response to rapamycin in an Akt-dependent manner via p38 MAPK
signaling.";
Oncogene 25:6277-6290(2006).
[25]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-124.
PubMed=17369404; DOI=10.1101/gad.1494707;
Franks T.M., Lykke-Andersen J.;
"TTP and BRF proteins nucleate processing body formation to silence
mRNAs with AU-rich elements.";
Genes Dev. 21:719-735(2007).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[27]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=18367721; DOI=10.1261/rna.748408;
Emmons J., Townley-Tilson W.H., Deleault K.M., Skinner S.J.,
Gross R.H., Whitfield M.L., Brooks S.A.;
"Identification of TTP mRNA targets in human dendritic cells reveals
TTP as a critical regulator of dendritic cell maturation.";
RNA 14:888-902(2008).
[28]
RNA-BINDING, AND MUTAGENESIS OF CYS-124.
PubMed=19188452; DOI=10.1128/MCB.00982-08;
Horner T.J., Lai W.S., Stumpo D.J., Blackshear P.J.;
"Stimulation of polo-like kinase 3 mRNA decay by tristetraprolin.";
Mol. Cell. Biol. 29:1999-2010(2009).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[30]
INDUCTION.
PubMed=20166898; DOI=10.3109/08977190903578660;
Hacker C., Valchanova R., Adams S., Munz B.;
"ZFP36L1 is regulated by growth factors and cytokines in keratinocytes
and influences their VEGF production.";
Growth Factors 28:178-190(2010).
[31]
FUNCTION, AND RNA-BINDING.
PubMed=20702587; DOI=10.1091/mbc.E10-01-0040;
Vignudelli T., Selmi T., Martello A., Parenti S., Grande A.,
Gemelli C., Zanocco-Marani T., Ferrari S.;
"ZFP36L1 negatively regulates erythroid differentiation of CD34+
hematopoietic stem cells by interfering with the Stat5b pathway.";
Mol. Biol. Cell 21:3340-3351(2010).
[32]
FUNCTION, INTERACTION WITH HEAT SHOCK 70 KDA PROTEINS; MAP3K4; NCL;
PABPC1 AND SH3KBP1, PHOSPHORYLATION AT SER-66 AND SER-93, RNA-BINDING,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-309.
PubMed=20221403; DOI=10.1371/journal.pone.0009588;
Kedar V.P., Darby M.K., Williams J.G., Blackshear P.J.;
"Phosphorylation of human tristetraprolin in response to its
interaction with the Cbl interacting protein CIN85.";
PLoS ONE 5:E9588-E9588(2010).
[33]
FUNCTION, AND RNA-BINDING.
PubMed=21775632; DOI=10.1091/mbc.E10-07-0617;
Chamboredon S., Ciais D., Desroches-Castan A., Savi P., Bono F.,
Feige J.J., Cherradi N.;
"Hypoxia-inducible factor-1alpha mRNA: a new target for
destabilization by tristetraprolin in endothelial cells.";
Mol. Biol. Cell 22:3366-3378(2011).
[34]
MUTAGENESIS OF PHE-126.
PubMed=21078877; DOI=10.1128/MCB.00717-10;
Clement S.L., Scheckel C., Stoecklin G., Lykke-Andersen J.;
"Phosphorylation of tristetraprolin by MK2 impairs AU-rich element
mRNA decay by preventing deadenylase recruitment.";
Mol. Cell. Biol. 31:256-266(2011).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[36]
INTERACTION WITH PRR5L.
PubMed=21964062; DOI=10.1016/j.cellsig.2011.09.015;
Holmes B., Artinian N., Anderson L., Martin J., Masri J.,
Cloninger C., Bernath A., Bashir T., Benavides-Serrato A., Gera J.;
"Protor-2 interacts with tristetraprolin to regulate mRNA stability
during stress.";
Cell. Signal. 24:309-315(2012).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-186 AND SER-323,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[39]
INTERACTION WITH CNOT7.
PubMed=25106868; DOI=10.1093/nar/gku652;
Adachi S., Homoto M., Tanaka R., Hioki Y., Murakami H., Suga H.,
Matsumoto M., Nakayama K.I., Hatta T., Iemura S., Natsume T.;
"ZFP36L1 and ZFP36L2 control LDLR mRNA stability via the ERK-RSK
pathway.";
Nucleic Acids Res. 42:10037-10049(2014).
[40]
FUNCTION, RNA-BINDING, AND MUTAGENESIS OF PHE-126.
PubMed=25815583; DOI=10.7554/eLife.03390;
Hausburg M.A., Doles J.D., Clement S.L., Cadwallader A.B., Hall M.N.,
Blackshear P.J., Lykke-Andersen J., Olwin B.B.;
"Post-transcriptional regulation of satellite cell quiescence by TTP-
mediated mRNA decay.";
Elife 4:E03390-E03390(2015).
[41]
FUNCTION.
PubMed=27193233; DOI=10.1007/s00726-016-2261-9;
Nowotarski S.L., Origanti S., Sass-Kuhn S., Shantz L.M.;
"Destabilization of the ornithine decarboxylase mRNA transcript by the
RNA-binding protein tristetraprolin.";
Amino Acids 48:2303-2311(2016).
[42]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=27182009; DOI=10.1016/j.ejcb.2016.04.007;
Prenzler F., Fragasso A., Schmitt A., Munz B.;
"Functional analysis of ZFP36 proteins in keratinocytes.";
Eur. J. Cell Biol. 95:277-284(2016).
[43]
FUNCTION, INTERACTION WITH PKM, PHOSPHORYLATION, UBIQUITINATION, AND
MUTAGENESIS OF SER-60.
PubMed=26926077; DOI=10.1038/srep22449;
Huang L., Yu Z., Zhang Z., Ma W., Song S., Huang G.;
"Interaction with pyruvate kinase M2 destabilizes tristetraprolin by
proteasome degradation and regulates cell proliferation in breast
cancer.";
Sci. Rep. 6:22449-22449(2016).
[44]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 312-326 IN COMPLEX WITH
CNOT1, INTERACTION WITH CNOT1, FUNCTION, AND MUTAGENESIS OF ARG-315
AND PHE-319.
PubMed=23644599; DOI=10.1038/nsmb.2572;
Fabian M.R., Frank F., Rouya C., Siddiqui N., Lai W.S., Karetnikov A.,
Blackshear P.J., Nagar B., Sonenberg N.;
"Structural basis for the recruitment of the human CCR4-NOT
deadenylase complex by tristetraprolin.";
Nat. Struct. Mol. Biol. 20:735-739(2013).
-!- FUNCTION: 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). {ECO:0000250|UniProtKB:P22893,
ECO:0000269|PubMed:10330172, ECO:0000269|PubMed:10751406,
ECO:0000269|PubMed:11279239, ECO:0000269|PubMed:11719186,
ECO:0000269|PubMed:12115244, ECO:0000269|PubMed:12748283,
ECO:0000269|PubMed:15187101, ECO:0000269|PubMed:15634918,
ECO:0000269|PubMed:15687258, ECO:0000269|PubMed:15766526,
ECO:0000269|PubMed:16364915, ECO:0000269|PubMed:16702957,
ECO:0000269|PubMed:17030620, ECO:0000269|PubMed:17369404,
ECO:0000269|PubMed:18367721, ECO:0000269|PubMed:19188452,
ECO:0000269|PubMed:20221403, ECO:0000269|PubMed:20702587,
ECO:0000269|PubMed:21775632, ECO:0000269|PubMed:23644599,
ECO:0000269|PubMed:25815583, ECO:0000269|PubMed:26926077,
ECO:0000269|PubMed:27182009, ECO:0000269|PubMed:27193233,
ECO:0000269|PubMed:9703499}.
-!- FUNCTION: (Microbial infection) Negatively regulates HTLV-1 TAX-
dependent transactivation of viral long terminal repeat (LTR)
promoter. {ECO:0000269|PubMed:14679154}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:P22893, ECO:0000269|PubMed:11719186,
ECO:0000269|PubMed:14766228, ECO:0000269|PubMed:15687258,
ECO:0000269|PubMed:15766526, ECO:0000269|PubMed:16126846,
ECO:0000269|PubMed:16364915, ECO:0000269|PubMed:16702957,
ECO:0000269|PubMed:20221403, ECO:0000269|PubMed:21964062,
ECO:0000269|PubMed:23644599, ECO:0000269|PubMed:25106868,
ECO:0000269|PubMed:26926077}.
-!- SUBUNIT: (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). {ECO:0000269|PubMed:14679154}.
-!- INTERACTION:
A5YKK6-2:CNOT1; NbExp=4; IntAct=EBI-374248, EBI-16057352;
Q9NPI6:DCP1A; NbExp=2; IntAct=EBI-374248, EBI-374238;
Q96F86:EDC3; NbExp=2; IntAct=EBI-374248, EBI-997311;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15014438,
ECO:0000269|PubMed:27182009}. Cytoplasm
{ECO:0000269|PubMed:10330172, ECO:0000269|PubMed:12115244,
ECO:0000269|PubMed:14766228, ECO:0000269|PubMed:15014438,
ECO:0000269|PubMed:20221403}. Cytoplasmic granule
{ECO:0000269|PubMed:15014438}. Cytoplasm, P-body
{ECO:0000269|PubMed:17369404}. Note=Shuttles between nucleus and
cytoplasm in a CRM1-dependent manner (By similarity). Localized
predominantly in the cytoplasm in a p38 MAPK- and YWHAB-dependent
manner (By similarity). Colocalizes with SH3KBP1 and MAP3K4 in the
cytoplasm (PubMed:20221403). Component of cytoplasmic stress
granules (SGs) (By similarity). Localizes to cytoplasmic stress
granules upon energy starvation (PubMed:15014438). Localizes in
processing bodies (PBs) (PubMed:17369404). Excluded from stress
granules in a phosphorylation MAPKAPK2-dependent manner (By
similarity). Shuttles in and out of both cytoplasmic P-body and
SGs (By similarity). {ECO:0000250|UniProtKB:P22893,
ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:17369404,
ECO:0000269|PubMed:20221403}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14679154}.
Cytoplasm {ECO:0000269|PubMed:14679154}. Note=(Microbial
infection) Colocalizes with HTLV-1 TAX in the nucleus and the
cytoplasm in a region surrounding the nucleus.
{ECO:0000269|PubMed:14679154}.
-!- TISSUE SPECIFICITY: 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).
{ECO:0000269|PubMed:18367721, ECO:0000269|PubMed:27182009}.
-!- INDUCTION: 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). {ECO:0000269|PubMed:14766228,
ECO:0000269|PubMed:15187101, ECO:0000269|PubMed:15634918,
ECO:0000269|PubMed:16508015, ECO:0000269|PubMed:20166898,
ECO:0000269|PubMed:27182009}.
-!- DOMAIN: The C3H1-type zinc finger domains are necessary for ARE-
binding activity (PubMed:10330172). {ECO:0000269|PubMed:10330172}.
-!- PTM: 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).
{ECO:0000250|UniProtKB:P22893, ECO:0000269|PubMed:16702957,
ECO:0000269|PubMed:20221403, ECO:0000269|PubMed:26926077}.
-!- PTM: Ubiquitinated; pyruvate kinase (PKM)-dependent ubiquitination
leads to proteasomal degradation through a p38 MAPK signaling
pathway (PubMed:26926077). {ECO:0000269|PubMed:26926077}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/zfp36/";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M92843; AAA58489.1; -; mRNA.
EMBL; M92844; AAC37600.1; -; Genomic_DNA.
EMBL; M63625; AAA61240.1; -; mRNA.
EMBL; AK314042; BAG36751.1; -; mRNA.
EMBL; AY771351; AAV28731.1; -; Genomic_DNA.
EMBL; BC009693; AAH09693.1; -; mRNA.
PIR; S34427; S34427.
RefSeq; NP_003398.2; NM_003407.3.
UniGene; Hs.534052; -.
PDB; 4J8S; X-ray; 1.55 A; B=312-326.
PDBsum; 4J8S; -.
ProteinModelPortal; P26651; -.
SMR; P26651; -.
BioGrid; 113370; 57.
CORUM; P26651; -.
DIP; DIP-29845N; -.
IntAct; P26651; 25.
MINT; MINT-1171915; -.
STRING; 9606.ENSP00000248673; -.
iPTMnet; P26651; -.
PhosphoSitePlus; P26651; -.
BioMuta; ZFP36; -.
DMDM; 136471; -.
PaxDb; P26651; -.
PeptideAtlas; P26651; -.
PRIDE; P26651; -.
DNASU; 7538; -.
Ensembl; ENST00000248673; ENSP00000248673; ENSG00000128016.
GeneID; 7538; -.
KEGG; hsa:7538; -.
CTD; 7538; -.
DisGeNET; 7538; -.
GeneCards; ZFP36; -.
HGNC; HGNC:12862; ZFP36.
HPA; HPA006009; -.
MIM; 190700; gene.
neXtProt; NX_P26651; -.
PharmGKB; PA37451; -.
eggNOG; KOG1677; Eukaryota.
eggNOG; COG5063; LUCA.
HOGENOM; HOG000233479; -.
HOVERGEN; HBG008483; -.
InParanoid; P26651; -.
KO; K15308; -.
PhylomeDB; P26651; -.
TreeFam; TF315463; -.
Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
SignaLink; P26651; -.
SIGNOR; P26651; -.
ChiTaRS; ZFP36; human.
GeneWiki; ZFP36; -.
GenomeRNAi; 7538; -.
PRO; PR:P26651; -.
Proteomes; UP000005640; Unplaced.
CleanEx; HS_ZFP36; -.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
GO; GO:0017091; F:AU-rich element binding; IDA:UniProtKB.
GO; GO:0019957; F:C-C chemokine binding; IPI:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0031072; F:heat shock protein binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; TAS:ProtInc.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:UniProtKB.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:UniProtKB.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0035278; P:miRNA mediated inhibition of translation; ISS:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
GO; GO:0051028; P:mRNA transport; IMP:UniProtKB.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IDA:UniProtKB.
GO; GO:0045085; P:negative regulation of interleukin-2 biosynthetic process; ISS:UniProtKB.
GO; GO:1904246; P:negative regulation of polynucleotide adenylyltransferase activity; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0032897; P:negative regulation of viral transcription; IMP:UniProtKB.
GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:UniProtKB.
GO; GO:0031086; P:nuclear-transcribed mRNA catabolic process, deadenylation-independent decay; IDA:UniProtKB.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IMP:BHF-UCL.
GO; GO:0038066; P:p38MAPK cascade; ISS:UniProtKB.
GO; GO:1901835; P:positive regulation of deadenylation-independent decapping of nuclear-transcribed mRNA; IDA:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; IMP:UniProtKB.
GO; GO:1904582; P:positive regulation of intracellular mRNA localization; IMP:UniProtKB.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:UniProtKB.
GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:UniProtKB.
GO; GO:1902172; P:regulation of keratinocyte apoptotic process; IMP:UniProtKB.
GO; GO:0045616; P:regulation of keratinocyte differentiation; IMP:UniProtKB.
GO; GO:0010837; P:regulation of keratinocyte proliferation; IMP:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
GO; GO:0032680; P:regulation of tumor necrosis factor production; IDA:UniProtKB.
GO; GO:0042594; P:response to starvation; IDA:UniProtKB.
GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
Gene3D; 4.10.1000.10; -; 2.
InterPro; IPR000571; Znf_CCCH.
InterPro; IPR036855; Znf_CCCH_sf.
Pfam; PF00642; zf-CCCH; 2.
SMART; SM00356; ZnF_C3H1; 2.
SUPFAM; SSF90229; SSF90229; 2.
PROSITE; PS50103; ZF_C3H1; 2.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; DNA-binding; Exosome;
Metal-binding; mRNA transport; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
RNA-mediated gene silencing; Transport; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 326 mRNA decay activator protein ZFP36.
/FTId=PRO_0000089163.
REPEAT 71 75 P-P-P-P-G.
REPEAT 198 202 P-P-P-P-G.
REPEAT 219 223 P-P-P-P-G.
ZN_FING 103 131 C3H1-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 141 169 C3H1-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
REGION 1 174 Necessary for localization of ARE-
containing mRNAs to processing bodies
(PBs). {ECO:0000269|PubMed:17369404}.
REGION 1 100 Necessary and sufficient for the
association with mRNA decay enzymes and
mRNA decay activation.
{ECO:0000269|PubMed:15687258}.
REGION 1 15 Necessary for nuclear export.
{ECO:0000250|UniProtKB:P47973}.
REGION 95 168 Necessary for nuclear localization.
{ECO:0000250|UniProtKB:P47973}.
REGION 97 173 Necessary for RNA-binding.
{ECO:0000269|PubMed:10751406,
ECO:0000269|PubMed:12748283}.
REGION 100 326 Necessary for localization of ARE-
containing mRNAs to processing bodies
(PBs). {ECO:0000269|PubMed:17369404}.
REGION 103 194 Necessary for interaction with PABPN1.
{ECO:0000250|UniProtKB:P22893}.
REGION 174 326 Necessary for mRNA decay activation.
{ECO:0000269|PubMed:15687258}.
REGION 312 326 Interaction with CNOT1.
{ECO:0000269|PubMed:23644599}.
MOD_RES 60 60 Phosphoserine; by MAPKAPK2.
{ECO:0000250|UniProtKB:P22893}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000269|PubMed:16262601,
ECO:0000269|PubMed:20221403}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000269|PubMed:16262601}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000250|UniProtKB:P22893}.
MOD_RES 92 92 Phosphothreonine.
{ECO:0000269|PubMed:16262601}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:20221403}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000269|PubMed:16262601}.
MOD_RES 186 186 Phosphoserine; by MAPKAPK2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16262601}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000269|PubMed:16262601}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000269|PubMed:16262601}.
MOD_RES 228 228 Phosphoserine; by MAPK1; in vitro.
{ECO:0000269|PubMed:16262601}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000269|PubMed:16262601}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000269|PubMed:16262601}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 37 37 P -> S (in dbSNP:rs17878633).
{ECO:0000269|Ref.3}.
/FTId=VAR_021064.
VARIANT 55 55 P -> S (in dbSNP:rs2229272).
/FTId=VAR_052324.
VARIANT 259 259 I -> F (in dbSNP:rs17886974).
{ECO:0000269|Ref.3}.
/FTId=VAR_021065.
VARIANT 324 324 V -> F (in dbSNP:rs17884899).
{ECO:0000269|Ref.3}.
/FTId=VAR_021066.
MUTAGEN 60 60 S->A: Inhibits PKM-induced ZFP36
degradation through a p38 MAPK signaling
pathway. {ECO:0000269|PubMed:26926077}.
MUTAGEN 124 124 C->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).
{ECO:0000269|PubMed:10330172,
ECO:0000269|PubMed:12748283,
ECO:0000269|PubMed:17030620,
ECO:0000269|PubMed:17369404,
ECO:0000269|PubMed:19188452}.
MUTAGEN 126 126 F->N: Inhibits ARE-containing RNA-
binding, deadenylation and RNA decapping
activities. {ECO:0000269|PubMed:16364915,
ECO:0000269|PubMed:21078877,
ECO:0000269|PubMed:25815583}.
MUTAGEN 147 147 C->R: Inhibits both ARE-binding and mRNA
deadenylation activities.
{ECO:0000269|PubMed:10330172}.
MUTAGEN 309 309 P->V: Inhibits interaction with SH3KBP1.
{ECO:0000269|PubMed:20221403}.
MUTAGEN 315 315 R->A: Abolishes interaction with CNOT1.
{ECO:0000269|PubMed:23644599}.
MUTAGEN 319 319 F->A: Abolishes interaction with CNOT1
and impairs TNF mRNA deadenylation.
{ECO:0000269|PubMed:23644599}.
HELIX 317 322 {ECO:0000244|PDB:4J8S}.
SEQUENCE 326 AA; 34003 MW; DDD9AD950AF7AF98 CRC64;
MDLTAIYESL LSLSPDVPVP SDHGGTESSP GWGSSGPWSL SPSDSSPSGV TSRLPGRSTS
LVEGRSCGWV PPPPGFAPLA PRLGPELSPS PTSPTATSTT PSRYKTELCR TFSESGRCRY
GAKCQFAHGL GELRQANRHP KYKTELCHKF YLQGRCPYGS RCHFIHNPSE DLAAPGHPPV
LRQSISFSGL PSGRRTSPPP PGLAGPSLSS SSFSPSSSPP PPGDLPLSPS AFSAAPGTPL
ARRDPTPVCC PSCRRATPIS VWGPLGGLVR TPSVQSLGSD PDEYASSGSS LGGSDSPVFE
AGVFAPPQPV AAPRRLPIFN RISVSE


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EIAAB44513 Bos taurus,Bovine,Protein TIS11A,TIS11,Tristetraprolin,TTP,ZFP36,Zfp-36,Zinc finger protein 36 homolog
28-842 ZFP36 is a probable regulatory protein with a novel zinc finger structure involved in regulating the response to growth factors. Knockdown of ZFP36 increased both cognate macrophage gene mRNAs and inf 0.05 mg
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28-572 Early Growth Response Protein 1 (EGR1, Krox-24 protein, nerve growth factor-induced protein A, Transcription factor ETR103, Zinc finger protein 225) belongs to the EGR family of C2H2-type zinc-finger 0.1 mg
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EIAAB47355 Homo sapiens,Human,Neurotrophin receptor-interacting factor homolog,SP2114,Zf2,Zinc finger protein 274,Zinc finger protein HFB101,Zinc finger protein with KRAB and SCAN domains 19,Zinc finger protein
EIAAB45299 E3 ubiquitin-protein ligase UHRF2,Homo sapiens,Human,NIRF,Np95_ICBP90-like RING finger protein,Np95-like RING finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,RING finger protein 107
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EIAAB47874 GIOT3,GIOT-3,Gonadotropin-inducible ovary transcription repressor 3,Homo sapiens,Human,KOX3,Zinc finger protein 12,Zinc finger protein 325,Zinc finger protein KOX3,ZNF12,ZNF325
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