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mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)

 TISB_MOUSE              Reviewed;         338 AA.
P23950;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=mRNA decay activator protein ZFP36L1 {ECO:0000305};
AltName: Full=Butyrate response factor 1 {ECO:0000250|UniProtKB:Q07352};
AltName: Full=TPA-induced sequence 11b {ECO:0000303|PubMed:1996120};
AltName: Full=Zinc finger protein 36, C3H1 type-like 1 {ECO:0000312|MGI:MGI:107946};
Short=ZFP36-like 1 {ECO:0000312|MGI:MGI:107946};
Name=Zfp36l1 {ECO:0000312|MGI:MGI:107946};
Synonyms=Brf1 {ECO:0000250|UniProtKB:Q07352},
Tis11b {ECO:0000303|PubMed:1996120};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=1996120; DOI=10.1128/MCB.11.3.1754;
Varnum B.C., Ma Q., Chi T., Fletcher B.S., Herschman H.R.;
"The TIS11 primary response gene is a member of a gene family that
encodes proteins with a highly conserved sequence containing an
unusual Cys-His repeat.";
Mol. Cell. Biol. 11:1754-1758(1991).
[2]
SUBCELLULAR LOCATION.
PubMed=11796723; DOI=10.1074/jbc.M111457200;
Phillips R.S., Ramos S.B., Blackshear P.J.;
"Members of the tristetraprolin family of tandem CCCH zinc finger
proteins exhibit CRM1-dependent nucleocytoplasmic shuttling.";
J. Biol. Chem. 277:11606-11613(2002).
[3]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15465005; DOI=10.1016/j.bbrc.2004.09.030;
Reppe S., Olstad O.K., Rian E., Gautvik V.T., Gautvik K.M.,
Jemtland R.;
"Butyrate response factor 1 is regulated by parathyroid hormone and
bone morphogenetic protein-2 in osteoblastic cells.";
Biochem. Biophys. Res. Commun. 324:218-223(2004).
[4]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=15226444; DOI=10.1128/MCB.24.14.6445-6455.2004;
Stumpo D.J., Byrd N.A., Phillips R.S., Ghosh S., Maronpot R.R.,
Castranio T., Meyers E.N., Mishina Y., Blackshear P.J.;
"Chorioallantoic fusion defects and embryonic lethality resulting from
disruption of Zfp36L1, a gene encoding a CCCH tandem zinc finger
protein of the Tristetraprolin family.";
Mol. Cell. Biol. 24:6445-6455(2004).
[5]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=17013884; DOI=10.1002/dvdy.20949;
Bell S.E., Sanchez M.J., Spasic-Boskovic O., Santalucia T.,
Gambardella L., Burton G.J., Murphy J.J., Norton J.D., Clark A.R.,
Turner M.;
"The RNA binding protein Zfp36l1 is required for normal
vascularisation and post-transcriptionally regulates VEGF
expression.";
Dev. Dyn. 235:3144-3155(2006).
[6]
FUNCTION, AND INDUCTION.
PubMed=17889962; DOI=10.1016/j.ejcb.2007.07.005;
Busse M., Schwarzburger M., Berger F., Hacker C., Munz B.;
"Strong induction of the Tis11B gene in myogenic differentiation.";
Eur. J. Cell Biol. 87:31-38(2008).
[7]
PHOSPHORYLATION, AND INDUCTION.
PubMed=19179481; DOI=10.1210/me.2008-0296;
Duan H., Cherradi N., Feige J.J., Jefcoate C.;
"cAMP-dependent posttranscriptional regulation of steroidogenic acute
regulatory (STAR) protein by the zinc finger protein ZFP36L1/TIS11b.";
Mol. Endocrinol. 23:497-509(2009).
[8]
FUNCTION, RNA-BINDING, AND DISRUPTION PHENOTYPE.
PubMed=20622884; DOI=10.1038/ni.1901;
Hodson D.J., Janas M.L., Galloway A., Bell S.E., Andrews S., Li C.M.,
Pannell R., Siebel C.W., MacDonald H.R., De Keersmaecker K.,
Ferrando A.A., Grutz G., Turner M.;
"Deletion of the RNA-binding proteins ZFP36L1 and ZFP36L2 leads to
perturbed thymic development and T lymphoblastic leukemia.";
Nat. Immunol. 11:717-724(2010).
[9]
FUNCTION, RNA-BINDING, INTERACTION WITH YWHAZ, PHOSPHORYLATION, AND
TISSUE SPECIFICITY.
PubMed=22701344; DOI=10.7150/ijbs.4036;
Lin N.Y., Lin T.Y., Yang W.H., Wang S.C., Wang K.T., Su Y.L.,
Jiang Y.W., Chang G.D., Chang C.J.;
"Differential expression and functional analysis of the
tristetraprolin family during early differentiation of 3T3-L1
preadipocytes.";
Int. J. Biol. Sci. 8:761-777(2012).
[10]
INDUCTION.
PubMed=23046558; DOI=10.1186/2044-5040-2-21;
Farina N.H., Hausburg M., Betta N.D., Pulliam C., Srivastava D.,
Cornelison D., Olwin B.B.;
"A role for RNA post-transcriptional regulation in satellite cell
activation.";
Skelet. Muscle 2:21-21(2012).
[11]
FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
INDUCTION.
PubMed=24700863; DOI=10.1681/ASN.2013091023;
Viengchareun S., Lema I., Lamribet K., Keo V., Blanchard A.,
Cherradi N., Lombes M.;
"Hypertonicity compromises renal mineralocorticoid receptor signaling
through Tis11b-mediated post-transcriptional control.";
J. Am. Soc. Nephrol. 25:2213-2221(2014).
[12]
FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
INDUCTION.
PubMed=24733888; DOI=10.1073/pnas.1320873111;
Tan F.E., Elowitz M.B.;
"Brf1 posttranscriptionally regulates pluripotency and differentiation
responses downstream of Erk MAP kinase.";
Proc. Natl. Acad. Sci. U.S.A. 111:1740-1748(2014).
[13]
INDUCTION.
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).
[14]
FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT IN LYMPHOCYTE B
CELLS, AND TISSUE SPECIFICITY.
PubMed=27102483; DOI=10.1126/science.aad5978;
Galloway A., Saveliev A., Lukasiak S., Hodson D.J., Bolland D.,
Balmanno K., Ahlfors H., Monzon-Casanova E., Mannurita S.C.,
Bell L.S., Andrews S., Diaz-Munoz M.D., Cook S.J., Corcoran A.,
Turner M.;
"RNA-binding proteins ZFP36L1 and ZFP36L2 promote cell quiescence.";
Science 352:453-459(2016).
-!- 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:22701344, PubMed:24700863,
PubMed:24733888, PubMed:27102483). Acts as a 3'-untranslated
region (UTR) ARE mRNA-binding adapter protein to communicate
signaling events to the mRNA decay machinery (By similarity).
Functions by recruiting the CCR4-NOT deadenylating complex and
components of the cytoplasmic RNA decay machinery to the bound
ARE-containing mRNAs, and hence promotes ARE-mediated mRNA
deadenylation and decay processes (By similarity). Induces also
the degradation of ARE-containing mRNAs even in absence of poly(A)
tail (By similarity). Binds to 3'-UTR ARE of numerous mRNAs
(PubMed:22701344, PubMed:24700863, PubMed:24733888). Positively
regulates early adipogenesis by promoting ARE-mediated mRNA decay
of immediate early genes (IEGs) (PubMed:22701344). Promotes ARE-
mediated mRNA decay of mineralocorticoid receptor NR3C2 mRNA in
response to hypertonic stress (PubMed:24700863). Negatively
regulates hematopoietic/erythroid cell differentiation by
promoting ARE-mediated mRNA decay of the transcription factor
STAT5B mRNA (By similarity). Positively regulates
monocyte/macrophage cell differentiation by promoting ARE-mediated
mRNA decay of the cyclin-dependent kinase CDK6 mRNA (By
similarity). Promotes degradation of ARE-containing pluripotency-
associated mRNAs in embryonic stem cells (ESCs), such as NANOG,
through a fibroblast growth factor (FGF)-induced MAPK-dependent
signaling pathway, and hence attenuates ESC self-renewal and
positively regulates mesendoderm differentiation
(PubMed:24733888). May play a role in mediating pro-apoptotic
effects in malignant B-cells by promoting ARE-mediated mRNA decay
of BCL2 mRNA (By similarity). In association with ZFP36L2
maintains quiescence on developing B lymphocytes by promoting ARE-
mediated decay of several mRNAs encoding cell cycle regulators
that help B cells progress through the cell cycle, and hence
ensuring accurate variable-diversity-joining (VDJ) recombination
and functional immune cell formation (PubMed:27102483). Together
with ZFP36L2 is also necessary for thymocyte development and
prevention of T-cell acute lymphoblastic leukemia (T-ALL)
transformation by promoting ARE-mediated mRNA decay of the
oncogenic transcription factor NOTCH1 mRNA (PubMed:20622884).
Involved in the delivery of target ARE-mRNAs to processing bodies
(PBs) (By similarity). In addition to its cytosolic mRNA-decay
function, plays a role in the regulation of nuclear mRNA 3'-end
processing; modulates mRNA 3'-end maturation efficiency of the
DLL4 mRNA through binding with an ARE embedded in a weak
noncanonical polyadenylation (poly(A)) signal in endothelial cells
(By similarity). Also involved in the regulation of stress granule
(SG) and P-body (PB) formation and fusion (By similarity). Plays a
role in vasculogenesis and endocardial development
(PubMed:15226444, PubMed:17013884). Involved in the regulation of
keratinocyte proliferation, differentiation and apoptosis (By
similarity). Plays a role in myoblast cell differentiation
(PubMed:17889962). {ECO:0000250|UniProtKB:P17431,
ECO:0000250|UniProtKB:Q07352, ECO:0000269|PubMed:15226444,
ECO:0000269|PubMed:17013884, ECO:0000269|PubMed:17889962,
ECO:0000269|PubMed:20622884, ECO:0000269|PubMed:22701344,
ECO:0000269|PubMed:24700863, ECO:0000269|PubMed:24733888,
ECO:0000269|PubMed:27102483}.
-!- SUBUNIT: Associates with the cytoplasmic CCR4-NOT deadenylase and
RNA exosome complexes to trigger ARE-containing mRNA deadenylation
and decay processes. Interacts with CNOT1. Interacts (via N-
terminus) with CNOT6. Interacts with CNOT7; this interaction is
inhibited in response to phorbol 12-myristate 13-acetate (PMA)
treatment in a p38 MAPK-dependent manner. Interacts with DCP1A.
Interacts (via N-terminus) with DCP2. Interacts (via N-terminus)
with EXOSC2. Interacts with XRN1. Interacts (via phosphorylated
form) with YWHAB; this interaction occurs in a protein kinase
AKT1-dependent manner (By similarity). Interacts (via
phosphorylated form) with YWHAZ; this interaction occurs in a p38
MAPK- and AKT-signaling pathways (PubMed:22701344).
{ECO:0000250|UniProtKB:Q07352, ECO:0000269|PubMed:22701344}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11796723}.
Cytoplasm {ECO:0000269|PubMed:11796723,
ECO:0000269|PubMed:24700863, ECO:0000269|PubMed:24733888}.
Cytoplasmic granule {ECO:0000250|UniProtKB:Q07352}. Cytoplasm, P-
body {ECO:0000250|UniProtKB:Q07352}. Note=Shuttles between the
nucleus and the cytoplasm in a XPO1/CRM1-dependent manner
(PubMed:11796723). Component of cytoplasmic stress granules (By
similarity). Localizes in processing bodies (PBs) (By similarity).
{ECO:0000250|UniProtKB:Q07352, ECO:0000269|PubMed:11796723}.
-!- TISSUE SPECIFICITY: Expressed in preadipocytes and adipocytes
(PubMed:22701344). Expressed in the proximal and distal tubules in
the renal cortex (at protein level) (PubMed:24700863). Expressed
in ovary, heart, kidney, lung, spleen and thymus
(PubMed:15226444). Weakly expressed in brain, liver and testis
(PubMed:15226444). Expressed in osteoblasts (PubMed:15465005).
Expressed in embryonic stem cells (ESCs) (PubMed:24733888).
Expressed through B lymphocyte development (PubMed:27102483).
{ECO:0000269|PubMed:15226444, ECO:0000269|PubMed:15465005,
ECO:0000269|PubMed:22701344, ECO:0000269|PubMed:24700863,
ECO:0000269|PubMed:24733888, ECO:0000269|PubMed:27102483}.
-!- DEVELOPMENTAL STAGE: Expressed in embryos at 8 dpc, onward
(PubMed:15226444). Expressed in the allantois and throughout the
neuroectoderm and paraxial mesoderm at 8 dpc (PubMed:15226444).
Expressed in the chorion and blood vessels at 8.5 dpc
(PubMed:17013884). Expressed in the neural tube, paraxial
mesoderm, heart, brain, otic vesicle and yolk sac at 9.5 dpc
(PubMed:17013884). Expressed in embryonic stem cells (ESC)
(PubMed:15226444). {ECO:0000269|PubMed:15226444,
ECO:0000269|PubMed:17013884}.
-!- INDUCTION: Up-regulated during myogenic differentiation in a p38
MAPK-dependent manner (PubMed:17889962). Up-regulated in response
to fibroblast growth factor FGF4 in embryonic stem cells (ESCs) in
a p38 MAPK-dependent manner (PubMed:24733888). Up-regulated during
high sodium diet-fed in the renal tubules (PubMed:24700863). Up-
regulated upon hypertonic stress condition with raffinose (at
protein level) (PubMed:24700863). Up-regulated by parathyroid
hormone (PTH) in calvarial osteoblasts (PubMed:15465005). Up-
regulated in response to adrenocorticotropic hormone (ACTH)
(PubMed:19179481). Up-regulated in response to cAMP
(PubMed:19179481). Down-regulated by bone morphogenetic protein
BMP2 treatment in calvarial osteoblasts (PubMed:15465005). Down-
regulated during the conversion from quiescence to activated
satellite cells upon muscle injury (PubMed:23046558,
PubMed:25815583). {ECO:0000269|PubMed:15465005,
ECO:0000269|PubMed:17889962, ECO:0000269|PubMed:19179481,
ECO:0000269|PubMed:23046558, ECO:0000269|PubMed:24700863,
ECO:0000269|PubMed:24733888, ECO:0000269|PubMed:25815583}.
-!- PTM: Phosphorylated (PubMed:19179481). Phosphorylated by RPS6KA1
at Ser-334 upon phorbol 12-myristate 13-acetate (PMA) treatment;
this phosphorylation results in dissociation of the CCR4-NOT
deadenylase complex and induces p38 MAPK-mediated stabilization of
the low-density lipoprotein receptor LDLR mRNA. Phosphorylated by
protein kinase AKT1 at Ser-92 and Ser-203 in response to insulin;
these phosphorylations stabilize ZFP36L1, increase the association
with 14-3-3 proteins and mediate ARE-containing mRNA
stabilization. AKT1-mediated phosphorylation at Ser-92 does not
impair ARE-containing RNA-binding. Phosphorylated at Ser-54, Ser-
92 and Ser-203 by MAPKAPK2; these phosphorylations increase the
association with 14-3-3 proteins and mediate ARE-containing mRNA
stabilization in a protein kinase AKT1-independent manner.
MAPKAPK2-mediated phosphorylations at Ser-54, Ser-92 and Ser-203
do not impair ARE-containing RNA-binding (By similarity).
Phosphorylations increase the association with 14-3-3 proteins and
mediate ARE-containing mRNA stabilization during early
adipogenesis in a p38 MAPK- and AKT-dependent manner
(PubMed:22701344). {ECO:0000250|UniProtKB:Q07352,
ECO:0000269|PubMed:19179481, ECO:0000269|PubMed:22701344}.
-!- PTM: Ubiquitinated. Ubiquitination leads to proteasomal
degradation, a process inhibited by phosphorylations at Ser-90,
Ser-92 and Ser-203. {ECO:0000250|UniProtKB:Q07352}.
-!- DISRUPTION PHENOTYPE: Embryos die in utero at 11 dpc
(PubMed:15226444, PubMed:17013884). Exhibit extraembryonic,
intraembryonic, vascular and neural tube defects and cardiac
abnormalities at 9.5 dpc (PubMed:17013884). Show a reduced number
of circulating blood cells (PubMed:17013884). Show failure of
chorioallantoic fusion (PubMed:15226444). Exhibited increased
level of VEGFA protein level in embryonic fibroblasts under both
normoxic and hypoxic conditions (PubMed:17013884). Knockout mice
lacking both ZFP36L1 and ZFP36L2 during thymopoiesis lead to
aberrant T cell development and subsequently develop a T-cell
acute lymphoblastic leukemia (T-ALL) (PubMed:20622884). Show also
higher levels of NOTCH1 protein and mRNA in thymocytes
(PubMed:20622884). Conditional knockout mice of both ZFP36L1 and
ZFP36L2 in pro-B cells display reduced B lymphocyte number and
delayed variable-diversity-joining (VDJ) recombination
(PubMed:27102483). Exhibit also increased protein and ARE-
containing mRNA expressions of several factors implicated in cell
cycle progression in late pre-B cells (PubMed:27102483).
{ECO:0000269|PubMed:15226444, ECO:0000269|PubMed:17013884,
ECO:0000269|PubMed:20622884, ECO:0000269|PubMed:27102483}.
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EMBL; M58566; AAA72948.1; -; mRNA.
CCDS; CCDS26010.1; -.
PIR; B39590; B39590.
RefSeq; NP_031590.1; NM_007564.5.
UniGene; Mm.235132; -.
ProteinModelPortal; P23950; -.
SMR; P23950; -.
BioGrid; 198385; 1.
IntAct; P23950; 1.
STRING; 10090.ENSMUSP00000021552; -.
iPTMnet; P23950; -.
PhosphoSitePlus; P23950; -.
PaxDb; P23950; -.
PeptideAtlas; P23950; -.
PRIDE; P23950; -.
Ensembl; ENSMUST00000021552; ENSMUSP00000021552; ENSMUSG00000021127.
Ensembl; ENSMUST00000165114; ENSMUSP00000127522; ENSMUSG00000021127.
GeneID; 12192; -.
KEGG; mmu:12192; -.
UCSC; uc007oal.1; mouse.
CTD; 677; -.
MGI; MGI:107946; Zfp36l1.
eggNOG; KOG1677; Eukaryota.
eggNOG; COG5063; LUCA.
GeneTree; ENSGT00530000063262; -.
HOGENOM; HOG000233479; -.
HOVERGEN; HBG008483; -.
InParanoid; P23950; -.
KO; K18753; -.
OMA; LQHSYSF; -.
OrthoDB; EOG091G0957; -.
PhylomeDB; P23950; -.
TreeFam; TF315463; -.
Reactome; R-MMU-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
ChiTaRS; Zfp36l1; mouse.
PRO; PR:P23950; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000021127; -.
CleanEx; MM_ZFP36L1; -.
ExpressionAtlas; P23950; baseline and differential.
Genevisible; P23950; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0003723; F:RNA binding; ISO:MGI.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IMP:MGI.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IDA:UniProtKB.
GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; ISS:UniProtKB.
GO; GO:0097403; P:cellular response to raffinose; IDA:UniProtKB.
GO; GO:0071472; P:cellular response to salt stress; IDA:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0060710; P:chorio-allantoic fusion; IMP:MGI.
GO; GO:0048568; P:embryonic organ development; IMP:MGI.
GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
GO; GO:0048382; P:mesendoderm development; IDA:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; ISO:MGI.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB.
GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
GO; GO:0021915; P:neural tube development; IMP:MGI.
GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:MGI.
GO; GO:0031086; P:nuclear-transcribed mRNA catabolic process, deadenylation-independent decay; ISS:UniProtKB.
GO; GO:0038066; P:p38MAPK cascade; IDA:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:UniProtKB.
GO; GO:1904582; P:positive regulation of intracellular mRNA localization; ISS:UniProtKB.
GO; GO:0045657; P:positive regulation of monocyte differentiation; ISS:UniProtKB.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
GO; GO:0003342; P:proepicardium development; IMP:MGI.
GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
GO; GO:0045577; P:regulation of B cell differentiation; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
GO; GO:1902172; P:regulation of keratinocyte apoptotic process; ISS:UniProtKB.
GO; GO:0045616; P:regulation of keratinocyte differentiation; ISS:UniProtKB.
GO; GO:0010837; P:regulation of keratinocyte proliferation; ISS:UniProtKB.
GO; GO:0031440; P:regulation of mRNA 3'-end processing; ISO:MGI.
GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
GO; GO:0045661; P:regulation of myoblast differentiation; IMP:UniProtKB.
GO; GO:0072091; P:regulation of stem cell proliferation; IDA:UniProtKB.
GO; GO:0006417; P:regulation of translation; IMP:MGI.
GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
GO; GO:0060712; P:spongiotrophoblast layer development; IMP:MGI.
GO; GO:0033077; P:T cell differentiation in thymus; IMP:UniProtKB.
GO; GO:0001570; P:vasculogenesis; IMP:MGI.
Gene3D; 4.10.1000.10; -; 2.
InterPro; IPR007635; Tis11B_N.
InterPro; IPR000571; Znf_CCCH.
InterPro; IPR036855; Znf_CCCH_sf.
Pfam; PF04553; Tis11B_N; 1.
Pfam; PF00642; zf-CCCH; 2.
SMART; SM00356; ZnF_C3H1; 2.
SUPFAM; SSF90229; SSF90229; 2.
PROSITE; PS50103; ZF_C3H1; 2.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Developmental protein; DNA-binding;
Metal-binding; mRNA processing; mRNA transport; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
RNA-binding; Transport; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 338 mRNA decay activator protein ZFP36L1.
/FTId=PRO_0000089168.
ZN_FING 114 142 C3H1-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 152 180 C3H1-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
REGION 1 111 Necessary and sufficient for the
association with mRNA decay enzymes and
mRNA decay activation.
{ECO:0000250|UniProtKB:Q07352}.
REGION 185 338 Necessary for mRNA decay activation.
{ECO:0000250|UniProtKB:Q07352}.
COMPBIAS 307 316 Poly-Ser.
MOD_RES 54 54 Phosphoserine; by MAPKAPK2.
{ECO:0000250|UniProtKB:Q07352}.
MOD_RES 90 90 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:Q07352}.
MOD_RES 92 92 Phosphoserine; by PKB/AKT1 and MAPKAPK2.
{ECO:0000250|UniProtKB:Q07352}.
MOD_RES 203 203 Phosphoserine; by PKB/AKT1 and MAPKAPK2.
{ECO:0000250|UniProtKB:Q07352}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:Q07352}.
MOD_RES 334 334 Phosphoserine; by RPS6KA1.
{ECO:0000250|UniProtKB:Q07352}.
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


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