TISB_MOUSE
ID TISB_MOUSE Reviewed; 338 AA.
AC P23950;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=mRNA decay activator protein ZFP36L1 {ECO:0000305};
DE AltName: Full=Butyrate response factor 1 {ECO:0000250|UniProtKB:Q07352};
DE AltName: Full=TPA-induced sequence 11b {ECO:0000303|PubMed:1996120};
DE AltName: Full=Zinc finger protein 36, C3H1 type-like 1 {ECO:0000312|MGI:MGI:107946};
DE Short=ZFP36-like 1 {ECO:0000312|MGI:MGI:107946};
GN Name=Zfp36l1 {ECO:0000312|MGI:MGI:107946};
GN Synonyms=Brf1 {ECO:0000250|UniProtKB:Q07352},
GN Tis11b {ECO:0000303|PubMed:1996120};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=1996120; DOI=10.1128/mcb.11.3.1754-1758.1991;
RA Varnum B.C., Ma Q., Chi T., Fletcher B.S., Herschman H.R.;
RT "The TIS11 primary response gene is a member of a gene family that encodes
RT proteins with a highly conserved sequence containing an unusual Cys-His
RT repeat.";
RL Mol. Cell. Biol. 11:1754-1758(1991).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11796723; DOI=10.1074/jbc.m111457200;
RA Phillips R.S., Ramos S.B., Blackshear P.J.;
RT "Members of the tristetraprolin family of tandem CCCH zinc finger proteins
RT exhibit CRM1-dependent nucleocytoplasmic shuttling.";
RL J. Biol. Chem. 277:11606-11613(2002).
RN [3]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15465005; DOI=10.1016/j.bbrc.2004.09.030;
RA Reppe S., Olstad O.K., Rian E., Gautvik V.T., Gautvik K.M., Jemtland R.;
RT "Butyrate response factor 1 is regulated by parathyroid hormone and bone
RT morphogenetic protein-2 in osteoblastic cells.";
RL Biochem. Biophys. Res. Commun. 324:218-223(2004).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15226444; DOI=10.1128/mcb.24.14.6445-6455.2004;
RA Stumpo D.J., Byrd N.A., Phillips R.S., Ghosh S., Maronpot R.R.,
RA Castranio T., Meyers E.N., Mishina Y., Blackshear P.J.;
RT "Chorioallantoic fusion defects and embryonic lethality resulting from
RT disruption of Zfp36L1, a gene encoding a CCCH tandem zinc finger protein of
RT the Tristetraprolin family.";
RL Mol. Cell. Biol. 24:6445-6455(2004).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=17013884; DOI=10.1002/dvdy.20949;
RA Bell S.E., Sanchez M.J., Spasic-Boskovic O., Santalucia T., Gambardella L.,
RA Burton G.J., Murphy J.J., Norton J.D., Clark A.R., Turner M.;
RT "The RNA binding protein Zfp36l1 is required for normal vascularisation and
RT post-transcriptionally regulates VEGF expression.";
RL Dev. Dyn. 235:3144-3155(2006).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=17889962; DOI=10.1016/j.ejcb.2007.07.005;
RA Busse M., Schwarzburger M., Berger F., Hacker C., Munz B.;
RT "Strong induction of the Tis11B gene in myogenic differentiation.";
RL Eur. J. Cell Biol. 87:31-38(2008).
RN [7]
RP PHOSPHORYLATION, AND INDUCTION.
RX PubMed=19179481; DOI=10.1210/me.2008-0296;
RA Duan H., Cherradi N., Feige J.J., Jefcoate C.;
RT "cAMP-dependent posttranscriptional regulation of steroidogenic acute
RT regulatory (STAR) protein by the zinc finger protein ZFP36L1/TIS11b.";
RL Mol. Endocrinol. 23:497-509(2009).
RN [8]
RP FUNCTION, RNA-BINDING, AND DISRUPTION PHENOTYPE.
RX PubMed=20622884; DOI=10.1038/ni.1901;
RA Hodson D.J., Janas M.L., Galloway A., Bell S.E., Andrews S., Li C.M.,
RA Pannell R., Siebel C.W., MacDonald H.R., De Keersmaecker K., Ferrando A.A.,
RA Grutz G., Turner M.;
RT "Deletion of the RNA-binding proteins ZFP36L1 and ZFP36L2 leads to
RT perturbed thymic development and T lymphoblastic leukemia.";
RL Nat. Immunol. 11:717-724(2010).
RN [9]
RP FUNCTION, RNA-BINDING, INTERACTION WITH YWHAZ, PHOSPHORYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22701344; DOI=10.7150/ijbs.4036;
RA Lin N.Y., Lin T.Y., Yang W.H., Wang S.C., Wang K.T., Su Y.L., Jiang Y.W.,
RA Chang G.D., Chang C.J.;
RT "Differential expression and functional analysis of the tristetraprolin
RT family during early differentiation of 3T3-L1 preadipocytes.";
RL Int. J. Biol. Sci. 8:761-777(2012).
RN [10]
RP INDUCTION.
RX PubMed=23046558; DOI=10.1186/2044-5040-2-21;
RA Farina N.H., Hausburg M., Betta N.D., Pulliam C., Srivastava D.,
RA Cornelison D., Olwin B.B.;
RT "A role for RNA post-transcriptional regulation in satellite cell
RT activation.";
RL Skelet. Muscle 2:21-21(2012).
RN [11]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=24700863; DOI=10.1681/asn.2013091023;
RA Viengchareun S., Lema I., Lamribet K., Keo V., Blanchard A., Cherradi N.,
RA Lombes M.;
RT "Hypertonicity compromises renal mineralocorticoid receptor signaling
RT through Tis11b-mediated post-transcriptional control.";
RL J. Am. Soc. Nephrol. 25:2213-2221(2014).
RN [12]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=24733888; DOI=10.1073/pnas.1320873111;
RA Tan F.E., Elowitz M.B.;
RT "Brf1 posttranscriptionally regulates pluripotency and differentiation
RT responses downstream of Erk MAP kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:1740-1748(2014).
RN [13]
RP INDUCTION.
RX PubMed=25815583; DOI=10.7554/elife.03390;
RA Hausburg M.A., Doles J.D., Clement S.L., Cadwallader A.B., Hall M.N.,
RA Blackshear P.J., Lykke-Andersen J., Olwin B.B.;
RT "Post-transcriptional regulation of satellite cell quiescence by TTP-
RT mediated mRNA decay.";
RL Elife 4:E03390-E03390(2015).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT IN LYMPHOCYTE B CELLS,
RP AND TISSUE SPECIFICITY.
RX PubMed=27102483; DOI=10.1126/science.aad5978;
RA Galloway A., Saveliev A., Lukasiak S., Hodson D.J., Bolland D.,
RA Balmanno K., Ahlfors H., Monzon-Casanova E., Mannurita S.C., Bell L.S.,
RA Andrews S., Diaz-Munoz M.D., Cook S.J., Corcoran A., Turner M.;
RT "RNA-binding proteins ZFP36L1 and ZFP36L2 promote cell quiescence.";
RL Science 352:453-459(2016).
CC -!- FUNCTION: Zinc-finger RNA-binding protein that destabilizes several
CC cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by
CC promoting their poly(A) tail removal or deadenylation, and hence
CC provide a mechanism for attenuating protein synthesis (PubMed:22701344,
CC PubMed:24700863, PubMed:24733888, PubMed:27102483). Acts as a 3'-
CC untranslated region (UTR) ARE mRNA-binding adapter protein to
CC communicate signaling events to the mRNA decay machinery (By
CC similarity). Functions by recruiting the CCR4-NOT deadenylating complex
CC and components of the cytoplasmic RNA decay machinery to the bound ARE-
CC containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation
CC and decay processes (By similarity). Induces also the degradation of
CC ARE-containing mRNAs even in absence of poly(A) tail (By similarity).
CC Binds to 3'-UTR ARE of numerous mRNAs (PubMed:22701344,
CC PubMed:24700863, PubMed:24733888). Positively regulates early
CC adipogenesis by promoting ARE-mediated mRNA decay of immediate early
CC genes (IEGs) (PubMed:22701344). Promotes ARE-mediated mRNA decay of
CC mineralocorticoid receptor NR3C2 mRNA in response to hypertonic stress
CC (PubMed:24700863). Negatively regulates hematopoietic/erythroid cell
CC differentiation by promoting ARE-mediated mRNA decay of the
CC transcription factor STAT5B mRNA (By similarity). Positively regulates
CC monocyte/macrophage cell differentiation by promoting ARE-mediated mRNA
CC decay of the cyclin-dependent kinase CDK6 mRNA (By similarity).
CC Promotes degradation of ARE-containing pluripotency-associated mRNAs in
CC embryonic stem cells (ESCs), such as NANOG, through a fibroblast growth
CC factor (FGF)-induced MAPK-dependent signaling pathway, and hence
CC attenuates ESC self-renewal and positively regulates mesendoderm
CC differentiation (PubMed:24733888). May play a role in mediating pro-
CC apoptotic effects in malignant B-cells by promoting ARE-mediated mRNA
CC decay of BCL2 mRNA (By similarity). In association with ZFP36L2
CC maintains quiescence on developing B lymphocytes by promoting ARE-
CC mediated decay of several mRNAs encoding cell cycle regulators that
CC help B cells progress through the cell cycle, and hence ensuring
CC accurate variable-diversity-joining (VDJ) recombination and functional
CC immune cell formation (PubMed:27102483). Together with ZFP36L2 is also
CC necessary for thymocyte development and prevention of T-cell acute
CC lymphoblastic leukemia (T-ALL) transformation by promoting ARE-mediated
CC mRNA decay of the oncogenic transcription factor NOTCH1 mRNA
CC (PubMed:20622884). Involved in the delivery of target ARE-mRNAs to
CC processing bodies (PBs) (By similarity). In addition to its cytosolic
CC mRNA-decay function, plays a role in the regulation of nuclear mRNA 3'-
CC end processing; modulates mRNA 3'-end maturation efficiency of the DLL4
CC mRNA through binding with an ARE embedded in a weak noncanonical
CC polyadenylation (poly(A)) signal in endothelial cells (By similarity).
CC Also involved in the regulation of stress granule (SG) and P-body (PB)
CC formation and fusion (By similarity). Plays a role in vasculogenesis
CC and endocardial development (PubMed:15226444, PubMed:17013884).
CC Involved in the regulation of keratinocyte proliferation,
CC differentiation and apoptosis (By similarity). Plays a role in myoblast
CC cell differentiation (PubMed:17889962). {ECO:0000250|UniProtKB:P17431,
CC ECO:0000250|UniProtKB:Q07352, ECO:0000269|PubMed:15226444,
CC ECO:0000269|PubMed:17013884, ECO:0000269|PubMed:17889962,
CC ECO:0000269|PubMed:20622884, ECO:0000269|PubMed:22701344,
CC ECO:0000269|PubMed:24700863, ECO:0000269|PubMed:24733888,
CC ECO:0000269|PubMed:27102483}.
CC -!- SUBUNIT: Associates with the cytoplasmic CCR4-NOT deadenylase and RNA
CC exosome complexes to trigger ARE-containing mRNA deadenylation and
CC decay processes. Interacts with CNOT1. Interacts (via N-terminus) with
CC CNOT6. Interacts with CNOT7; this interaction is inhibited in response
CC to phorbol 12-myristate 13-acetate (PMA) treatment in a p38 MAPK-
CC dependent manner. Interacts with DCP1A. Interacts (via N-terminus) with
CC DCP2. Interacts (via N-terminus) with EXOSC2. Interacts with XRN1.
CC Interacts (via phosphorylated form) with YWHAB; this interaction occurs
CC in a protein kinase AKT1-dependent manner (By similarity). Interacts
CC (via phosphorylated form) with YWHAZ; this interaction occurs in a p38
CC MAPK- and AKT-signaling pathways (PubMed:22701344).
CC {ECO:0000250|UniProtKB:Q07352, ECO:0000269|PubMed:22701344}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11796723}. Cytoplasm
CC {ECO:0000269|PubMed:11796723, ECO:0000269|PubMed:24700863,
CC ECO:0000269|PubMed:24733888}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q07352}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:Q07352}. Note=Shuttles between the nucleus and
CC the cytoplasm in a XPO1/CRM1-dependent manner (PubMed:11796723).
CC Component of cytoplasmic stress granules (By similarity). Localizes in
CC processing bodies (PBs) (By similarity). {ECO:0000250|UniProtKB:Q07352,
CC ECO:0000269|PubMed:11796723}.
CC -!- TISSUE SPECIFICITY: Expressed in preadipocytes and adipocytes
CC (PubMed:22701344). Expressed in the proximal and distal tubules in the
CC renal cortex (at protein level) (PubMed:24700863). Expressed in ovary,
CC heart, kidney, lung, spleen and thymus (PubMed:15226444). Weakly
CC expressed in brain, liver and testis (PubMed:15226444). Expressed in
CC osteoblasts (PubMed:15465005). Expressed in embryonic stem cells (ESCs)
CC (PubMed:24733888). Expressed through B lymphocyte development
CC (PubMed:27102483). {ECO:0000269|PubMed:15226444,
CC ECO:0000269|PubMed:15465005, ECO:0000269|PubMed:22701344,
CC ECO:0000269|PubMed:24700863, ECO:0000269|PubMed:24733888,
CC ECO:0000269|PubMed:27102483}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos at 8 dpc, onward
CC (PubMed:15226444). Expressed in the allantois and throughout the
CC neuroectoderm and paraxial mesoderm at 8 dpc (PubMed:15226444).
CC Expressed in the chorion and blood vessels at 8.5 dpc
CC (PubMed:17013884). Expressed in the neural tube, paraxial mesoderm,
CC heart, brain, otic vesicle and yolk sac at 9.5 dpc (PubMed:17013884).
CC Expressed in embryonic stem cells (ESC) (PubMed:15226444).
CC {ECO:0000269|PubMed:15226444, ECO:0000269|PubMed:17013884}.
CC -!- INDUCTION: Up-regulated during myogenic differentiation in a p38 MAPK-
CC dependent manner (PubMed:17889962). Up-regulated in response to
CC fibroblast growth factor FGF4 in embryonic stem cells (ESCs) in a p38
CC MAPK-dependent manner (PubMed:24733888). Up-regulated during high
CC sodium diet-fed in the renal tubules (PubMed:24700863). Up-regulated
CC upon hypertonic stress condition with raffinose (at protein level)
CC (PubMed:24700863). Up-regulated by parathyroid hormone (PTH) in
CC calvarial osteoblasts (PubMed:15465005). Up-regulated in response to
CC adrenocorticotropic hormone (ACTH) (PubMed:19179481). Up-regulated in
CC response to cAMP (PubMed:19179481). Down-regulated by bone
CC morphogenetic protein BMP2 treatment in calvarial osteoblasts
CC (PubMed:15465005). Down-regulated during the conversion from quiescence
CC to activated satellite cells upon muscle injury (PubMed:23046558,
CC PubMed:25815583). {ECO:0000269|PubMed:15465005,
CC ECO:0000269|PubMed:17889962, ECO:0000269|PubMed:19179481,
CC ECO:0000269|PubMed:23046558, ECO:0000269|PubMed:24700863,
CC ECO:0000269|PubMed:24733888, ECO:0000269|PubMed:25815583}.
CC -!- PTM: Phosphorylated (PubMed:19179481). Phosphorylated by RPS6KA1 at
CC Ser-334 upon phorbol 12-myristate 13-acetate (PMA) treatment; this
CC phosphorylation results in dissociation of the CCR4-NOT deadenylase
CC complex and induces p38 MAPK-mediated stabilization of the low-density
CC lipoprotein receptor LDLR mRNA. Phosphorylated by protein kinase AKT1
CC at Ser-92 and Ser-203 in response to insulin; these phosphorylations
CC stabilize ZFP36L1, increase the association with 14-3-3 proteins and
CC mediate ARE-containing mRNA stabilization. AKT1-mediated
CC phosphorylation at Ser-92 does not impair ARE-containing RNA-binding.
CC Phosphorylated at Ser-54, Ser-92 and Ser-203 by MAPKAPK2; these
CC phosphorylations increase the association with 14-3-3 proteins and
CC mediate ARE-containing mRNA stabilization in a protein kinase AKT1-
CC independent manner. MAPKAPK2-mediated phosphorylations at Ser-54, Ser-
CC 92 and Ser-203 do not impair ARE-containing RNA-binding (By
CC similarity). Phosphorylations increase the association with 14-3-3
CC proteins and mediate ARE-containing mRNA stabilization during early
CC adipogenesis in a p38 MAPK- and AKT-dependent manner (PubMed:22701344).
CC {ECO:0000250|UniProtKB:Q07352, ECO:0000269|PubMed:19179481,
CC ECO:0000269|PubMed:22701344}.
CC -!- PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation, a
CC process inhibited by phosphorylations at Ser-90, Ser-92 and Ser-203.
CC {ECO:0000250|UniProtKB:Q07352}.
CC -!- DISRUPTION PHENOTYPE: Embryos die in utero at 11 dpc (PubMed:15226444,
CC PubMed:17013884). Exhibit extraembryonic, intraembryonic, vascular and
CC neural tube defects and cardiac abnormalities at 9.5 dpc
CC (PubMed:17013884). Show a reduced number of circulating blood cells
CC (PubMed:17013884). Show failure of chorioallantoic fusion
CC (PubMed:15226444). Exhibited increased level of VEGFA protein level in
CC embryonic fibroblasts under both normoxic and hypoxic conditions
CC (PubMed:17013884). Knockout mice lacking both ZFP36L1 and ZFP36L2
CC during thymopoiesis lead to aberrant T cell development and
CC subsequently develop a T-cell acute lymphoblastic leukemia (T-ALL)
CC (PubMed:20622884). Show also higher levels of NOTCH1 protein and mRNA
CC in thymocytes (PubMed:20622884). Conditional knockout mice of both
CC ZFP36L1 and ZFP36L2 in pro-B cells display reduced B lymphocyte number
CC and delayed variable-diversity-joining (VDJ) recombination
CC (PubMed:27102483). Exhibit also increased protein and ARE-containing
CC mRNA expressions of several factors implicated in cell cycle
CC progression in late pre-B cells (PubMed:27102483).
CC {ECO:0000269|PubMed:15226444, ECO:0000269|PubMed:17013884,
CC ECO:0000269|PubMed:20622884, ECO:0000269|PubMed:27102483}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M58566; AAA72948.1; -; mRNA.
DR CCDS; CCDS26010.1; -.
DR PIR; B39590; B39590.
DR RefSeq; NP_031590.1; NM_007564.5.
DR AlphaFoldDB; P23950; -.
DR SMR; P23950; -.
DR BioGRID; 198385; 1.
DR IntAct; P23950; 2.
DR STRING; 10090.ENSMUSP00000021552; -.
DR iPTMnet; P23950; -.
DR PhosphoSitePlus; P23950; -.
DR jPOST; P23950; -.
DR PaxDb; P23950; -.
DR PeptideAtlas; P23950; -.
DR PRIDE; P23950; -.
DR ProteomicsDB; 259191; -.
DR Antibodypedia; 37; 375 antibodies from 34 providers.
DR DNASU; 12192; -.
DR Ensembl; ENSMUST00000021552; ENSMUSP00000021552; ENSMUSG00000021127.
DR Ensembl; ENSMUST00000165114; ENSMUSP00000127522; ENSMUSG00000021127.
DR GeneID; 12192; -.
DR KEGG; mmu:12192; -.
DR UCSC; uc007oal.1; mouse.
DR CTD; 677; -.
DR MGI; MGI:107946; Zfp36l1.
DR VEuPathDB; HostDB:ENSMUSG00000021127; -.
DR eggNOG; KOG1677; Eukaryota.
DR GeneTree; ENSGT00940000155076; -.
DR HOGENOM; CLU_033040_1_0_1; -.
DR InParanoid; P23950; -.
DR OMA; TPYFFRP; -.
DR OrthoDB; 1541140at2759; -.
DR PhylomeDB; P23950; -.
DR TreeFam; TF315463; -.
DR Reactome; R-MMU-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR BioGRID-ORCS; 12192; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Zfp36l1; mouse.
DR PRO; PR:P23950; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P23950; protein.
DR Bgee; ENSMUSG00000021127; Expressed in cerebellum ventricular layer and 234 other tissues.
DR ExpressionAtlas; P23950; baseline and differential.
DR Genevisible; P23950; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IDA:UniProtKB.
DR GO; GO:0097403; P:cellular response to raffinose; IDA:UniProtKB.
DR GO; GO:0071472; P:cellular response to salt stress; IDA:UniProtKB.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0060710; P:chorio-allantoic fusion; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
DR GO; GO:0048382; P:mesendoderm development; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:MGI.
DR GO; GO:0031086; P:nuclear-transcribed mRNA catabolic process, deadenylation-independent decay; ISS:UniProtKB.
DR GO; GO:0038066; P:p38MAPK cascade; IDA:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:UniProtKB.
DR GO; GO:1904582; P:positive regulation of intracellular mRNA localization; ISS:UniProtKB.
DR GO; GO:0045657; P:positive regulation of monocyte differentiation; ISS:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0003342; P:proepicardium development; IMP:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0045577; P:regulation of B cell differentiation; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR GO; GO:1902172; P:regulation of keratinocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0010837; P:regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; ISO:MGI.
DR GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
DR GO; GO:0045661; P:regulation of myoblast differentiation; IMP:UniProtKB.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IDA:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR GO; GO:0060712; P:spongiotrophoblast layer development; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR InterPro; IPR007635; Tis11B_N.
DR InterPro; IPR045877; ZFP36-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12547; PTHR12547; 1.
DR Pfam; PF04553; Tis11B_N; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; DNA-binding; Metal-binding;
KW mRNA processing; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Transport;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..338
FT /note="mRNA decay activator protein ZFP36L1"
FT /id="PRO_0000089168"
FT ZN_FING 114..142
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 152..180
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..111
FT /note="Necessary and sufficient for the association with
FT mRNA decay enzymes and mRNA decay activation"
FT /evidence="ECO:0000250|UniProtKB:Q07352"
FT REGION 71..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..338
FT /note="Necessary for mRNA decay activation"
FT /evidence="ECO:0000250|UniProtKB:Q07352"
FT REGION 273..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0000250|UniProtKB:Q07352"
FT MOD_RES 90
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q07352"
FT MOD_RES 92
FT /note="Phosphoserine; by PKB/AKT1 and MAPKAPK2"
FT /evidence="ECO:0000250|UniProtKB:Q07352"
FT MOD_RES 203
FT /note="Phosphoserine; by PKB/AKT1 and MAPKAPK2"
FT /evidence="ECO:0000250|UniProtKB:Q07352"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07352"
FT MOD_RES 334
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:Q07352"
SQ SEQUENCE 338 AA; 36385 MW; A28F2C8BF476496C CRC64;
MTTTLVSATI FDLSEVLCKG NKMLNYSTPS AGGCLLDRKA VGTPAGGGFP RRHSVTLPSS
KFHQNQLLSS LKGEPAPSLS SRDSRFRDRS FSEGGERLLP TQKQPGSGQV NSSRYKTELC
RPFEENGACK YGDKCQFAHG IHELRSLTRH PKYKTELCRT FHTIGFCPYG PRCHFIHNAE
ERRALAGGRD LSADRPRLQH SFSFAGFPSA AATAAATGLL DSPTSITPPP ILSADDLLGS
PTLPDGTNNP FAFSSQELAS LFAPSMGLPG GGSPTTFLFR PMSESPHMFD SPPSPQDSLS
DHEGYLSSSS SSHSGSDSPT LDNSRRLPIF SRLSISDD
