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

 TISB_HUMAN              Reviewed;         338 AA.
Q07352; Q13851;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 165.
RecName: Full=mRNA decay activator protein ZFP36L1 {ECO:0000305};
AltName: Full=Butyrate response factor 1 {ECO:0000303|PubMed:10367403, ECO:0000303|PubMed:12198173};
AltName: Full=EGF-response factor 1 {ECO:0000303|PubMed:8346037};
Short=ERF-1 {ECO:0000303|PubMed:8346037};
AltName: Full=TPA-induced sequence 11b {ECO:0000250|UniProtKB:P23950};
AltName: Full=Zinc finger protein 36, C3H1 type-like 1 {ECO:0000312|HGNC:HGNC:1107};
Short=ZFP36-like 1 {ECO:0000312|HGNC:HGNC:1107};
Name=ZFP36L1 {ECO:0000312|HGNC:HGNC:1107};
Synonyms=BERG36 {ECO:0000303|PubMed:8898945},
BRF1 {ECO:0000303|PubMed:10367403, ECO:0000303|PubMed:12198173},
ERF1 {ECO:0000303|PubMed:8346037}, RNF162B,
TIS11B {ECO:0000250|UniProtKB:P23950};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8346037; DOI=10.1093/nar/21.15.3580;
Barnard R.C., Pascall J.C., Brown K.D., McKay I.A., Williams N.S.,
Bustin S.A.;
"Coding sequence of ERF-1, the human homologue of Tis11b/cMG1, members
of the Tis11 family of early response genes.";
Nucleic Acids Res. 21:3580-3580(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8024689; DOI=10.1089/dna.1994.13.449;
Bustin S.A., Nie X.F., Barnard R.C., Kumar V., Pascall J.C.,
Brown K.D., Leigh I.M., Williams N.S., McKay L.A.;
"Cloning and characterization of ERF-1, a human member of the Tis11
family of early-response genes.";
DNA Cell Biol. 13:449-459(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8898945; DOI=10.1002/eji.1830261013;
Ning Z.Q., Norton J.D., Li J., Murphy J.J.;
"Distinct mechanisms for rescue from apoptosis in Ramos human B cells
by signaling through CD40 and interleukin-4 receptor: role for
inhibition of an early response gene, Berg36.";
Eur. J. Immunol. 26:2356-2363(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
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).
[6]
INDUCTION.
PubMed=10367403;
Maclean K.N., McKay I.A., Bustin S.A.;
"Differential effects of sodium butyrate on the transcription of the
human TIS11 family of early-response genes in colorectal cancer
cells.";
Br. J. Biomed. Sci. 55:184-191(1998).
[7]
FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
CYS-120 AND CYS-158.
PubMed=12198173; DOI=10.1093/emboj/cdf444;
Stoecklin G., Colombi M., Raineri I., Leuenberger S., Mallaun M.,
Schmidlin M., Gross B., Lu M., Kitamura T., Moroni C.;
"Functional cloning of BRF1, a regulator of ARE-dependent mRNA
turnover.";
EMBO J. 21:4709-4718(2002).
[8]
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).
[9]
FUNCTION, RNA-BINDING, INTERACTION WITH YWHAB, PHOSPHORYLATION AT
SER-90 AND SER-92, AND MUTAGENESIS OF SER-90 AND SER-92.
PubMed=15538381; DOI=10.1038/sj.emboj.7600477;
Schmidlin M., Lu M., Leuenberger S.A., Stoecklin G., Mallaun M.,
Gross B., Gherzi R., Hess D., Hemmings B.A., Moroni C.;
"The ARE-dependent mRNA-destabilizing activity of BRF1 is regulated by
protein kinase B.";
EMBO J. 23:4760-4769(2004).
[10]
FUNCTION, AND RNA-BINDING.
PubMed=15467755; DOI=10.1038/sj.onc.1207939;
Ciais D., Cherradi N., Bailly S., Grenier E., Berra E., Pouyssegur J.,
Lamarre J., Feige J.J.;
"Destabilization of vascular endothelial growth factor mRNA by the
zinc-finger protein TIS11b.";
Oncogene 23:8673-8680(2004).
[11]
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).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15967811; DOI=10.1083/jcb.200502088;
Kedersha N., Stoecklin G., Ayodele M., Yacono P., Lykke-Andersen J.,
Fritzler M.J., Scheuner D., Kaufman R.J., Golan D.E., Anderson P.;
"Stress granules and processing bodies are dynamically linked sites of
mRNP remodeling.";
J. Cell Biol. 169:871-884(2005).
[13]
FUNCTION, RNA-BINDING, INTERACTION WITH YWHAB, PHOSPHORYLATION AT
SER-203, UBIQUITINATION, AND MUTAGENESIS OF SER-92 AND SER-203.
PubMed=17030608; DOI=10.1128/MCB.01099-06;
Benjamin D., Schmidlin M., Min L., Gross B., Moroni C.;
"BRF1 protein turnover and mRNA decay activity are regulated by
protein kinase B at the same phosphorylation sites.";
Mol. Cell. Biol. 26:9497-9507(2006).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[15]
FUNCTION, INTERACTION WITH CNOT6; DCP2; EXOSC2 AND YWHAB,
PHOSPHORYLATION AT SER-54; SER-92 AND SER-203, AND MUTAGENESIS OF
SER-54; SER-92 AND SER-203.
PubMed=18326031; DOI=10.1261/rna.983708;
Maitra S., Chou C.F., Luber C.A., Lee K.Y., Mann M., Chen C.Y.;
"The AU-rich element mRNA decay-promoting activity of BRF1 is
regulated by mitogen-activated protein kinase-activated protein kinase
2.";
RNA 14:950-959(2008).
[16]
FUNCTION, RNA-BINDING, 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).
[17]
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).
[18]
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).
[19]
FUNCTION, RNA-BINDING, AND INDUCTION.
PubMed=21832157; DOI=10.1091/mbc.E11-02-0149;
Desroches-Castan A., Cherradi N., Feige J.J., Ciais D.;
"A novel function of Tis11b/BRF1 as a regulator of Dll4 mRNA 3'-end
processing.";
Mol. Biol. Cell 22:3625-3633(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, 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).
[22]
FUNCTION, RNA-BINDING, AND MUTAGENESIS OF CYS-120 AND CYS-158.
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-318, AND
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).
[24]
FUNCTION, RNA-BINDING, INTERACTION WITH CNOT1 AND CNOT7,
PHOSPHORYLATION AT SER-334, MUTAGENESIS OF SER-334 AND SER-336, AND
IDENTIFICATION BY MASS SPECTROMETRY.
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).
[25]
FUNCTION, AND RNA-BINDING.
PubMed=25014217; DOI=10.1371/journal.pone.0102625;
Zekavati A., Nasir A., Alcaraz A., Aldrovandi M., Marsh P.,
Norton J.D., Murphy J.J.;
"Post-transcriptional regulation of BCL2 mRNA by the RNA-binding
protein ZFP36L1 in malignant B cells.";
PLoS ONE 9:E102625-E102625(2014).
[26]
FUNCTION, RNA-BINDING, AND INDUCTION.
PubMed=26542173; DOI=10.1038/srep16229;
Chen M.T., Dong L., Zhang X.H., Yin X.L., Ning H.M., Shen C., Su R.,
Li F., Song L., Ma Y.N., Wang F., Zhao H.L., Yu J., Zhang J.W.;
"ZFP36L1 promotes monocyte/macrophage differentiation by repressing
CDK6.";
Sci. Rep. 5:16229-16229(2015).
[27]
FUNCTION, 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).
[28]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 325-333 IN COMPLEX WITH MAJOR
HISTOCOMPATIBILITY COMPLEX HLA.
PubMed=15713487; DOI=10.1016/j.jmb.2004.12.047;
Hulsmeyer M., Welfle K., Pohlmann T., Misselwitz R., Alexiev U.,
Welfle H., Saenger W., Uchanska-Ziegler B., Ziegler A.;
"Thermodynamic and structural equivalence of two HLA-B27 subtypes
complexed with a self-peptide.";
J. Mol. Biol. 346:1367-1379(2005).
-!- 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:12198173, PubMed:15538381,
PubMed:15467755, PubMed:17030608, PubMed:19179481,
PubMed:20702587, PubMed:24700863, PubMed:25106868,
PubMed:25014217, PubMed:26542173). Acts as a 3'-untranslated
region (UTR) ARE mRNA-binding adapter protein to communicate
signaling events to the mRNA decay machinery (PubMed:15687258).
Functions by recruiting the CCR4-NOT deadenylase 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 (PubMed:15687258,
PubMed:18326031, PubMed:25106868). 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:12198173, PubMed:15538381, PubMed:15467755,
PubMed:17030608, PubMed:19179481, PubMed:20702587,
PubMed:24700863, PubMed:25106868, PubMed:25014217,
PubMed:26542173). Positively regulates early adipogenesis by
promoting ARE-mediated mRNA decay of immediate early genes (IEGs)
(By similarity). 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
(PubMed:20702587). Positively regulates monocyte/macrophage cell
differentiation by promoting ARE-mediated mRNA decay of the
cyclin-dependent kinase CDK6 mRNA (PubMed:26542173). 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 (By similarity). May play a role in
mediating pro-apoptotic effects in malignant B-cells by promoting
ARE-mediated mRNA decay of BCL2 mRNA (PubMed:25014217). 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
(By similarity). 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 (By
similarity). Participates in the delivery of target ARE-mRNAs to
processing bodies (PBs) (PubMed:17369404). 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 (PubMed:21832157). Also involved in the
regulation of stress granule (SG) and P-body (PB) formation and
fusion (PubMed:15967811). Plays a role in vasculogenesis and
endocardial development (By similarity). Plays a role in the
regulation of keratinocyte proliferation, differentiation and
apoptosis (PubMed:27182009). Plays a role in myoblast cell
differentiation (By similarity). {ECO:0000250|UniProtKB:P17431,
ECO:0000250|UniProtKB:P23950, ECO:0000269|PubMed:12198173,
ECO:0000269|PubMed:15467755, ECO:0000269|PubMed:15538381,
ECO:0000269|PubMed:15687258, ECO:0000269|PubMed:15967811,
ECO:0000269|PubMed:17030608, ECO:0000269|PubMed:17369404,
ECO:0000269|PubMed:18326031, ECO:0000269|PubMed:19179481,
ECO:0000269|PubMed:20702587, ECO:0000269|PubMed:21832157,
ECO:0000269|PubMed:24700863, ECO:0000269|PubMed:25014217,
ECO:0000269|PubMed:25106868, ECO:0000269|PubMed:26542173,
ECO:0000269|PubMed:27182009}.
-!- SUBUNIT: Associates with the cytoplasmic CCR4-NOT deadenylase and
RNA exosome complexes to trigger ARE-containing mRNA deadenylation
and decay processes (PubMed:15687258, PubMed:18326031,
PubMed:25106868). Interacts with CNOT1 (PubMed:25106868).
Interacts (via N-terminus) with CNOT6 (PubMed:15687258,
PubMed:18326031). Interacts with CNOT7; this interaction is
inhibited in response to phorbol 12-myristate 13-acetate (PMA)
treatment in a p38 MAPK-dependent manner (PubMed:25106868).
Interacts with DCP1A (PubMed:15687258). Interacts (via N-terminus)
with DCP2 (PubMed:15687258, PubMed:18326031). Interacts (via N-
terminus) with EXOSC2 (PubMed:15687258, PubMed:18326031).
Interacts with XRN1 (PubMed:15687258). Interacts (via
phosphorylated form) with YWHAB; this interaction occurs in a
protein kinase AKT1-dependent manner (PubMed:15538381,
PubMed:17030608, PubMed:18326031). Interacts (via phosphorylated
form) with YWHAZ; this interaction occurs in a p38 MAPK- and AKT-
signaling pathways (By similarity). {ECO:0000250|UniProtKB:P23950,
ECO:0000269|PubMed:12198173, ECO:0000269|PubMed:15467755,
ECO:0000269|PubMed:15538381, ECO:0000269|PubMed:15687258,
ECO:0000269|PubMed:15967811, ECO:0000269|PubMed:17030608,
ECO:0000269|PubMed:17369404, ECO:0000269|PubMed:18326031,
ECO:0000269|PubMed:19179481, ECO:0000269|PubMed:20702587,
ECO:0000269|PubMed:21832157, ECO:0000269|PubMed:24700863,
ECO:0000269|PubMed:25014217, ECO:0000269|PubMed:25106868,
ECO:0000269|PubMed:26542173, ECO:0000269|PubMed:27182009}.
-!- INTERACTION:
Q16539:MAPK14; NbExp=2; IntAct=EBI-721823, EBI-73946;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12198173}.
Cytoplasm {ECO:0000269|PubMed:12198173}. Cytoplasmic granule
{ECO:0000269|PubMed:15967811}. Cytoplasm, P-body
{ECO:0000269|PubMed:15967811, ECO:0000269|PubMed:17369404}.
Note=Shuttles between the nucleus and the cytoplasm in a
XPO1/CRM1-dependent manner (By similarity). Component of
cytoplasmic stress granules (PubMed:15967811). Localizes in
processing bodies (PBs) (PubMed:17369404).
{ECO:0000250|UniProtKB:P23950, ECO:0000269|PubMed:15967811,
ECO:0000269|PubMed:17369404}.
-!- TISSUE SPECIFICITY: Expressed mainly in the basal epidermal layer,
weakly in the suprabasal epidermal layers (PubMed:27182009).
Expressed in epidermal keratinocytes (at protein level)
(PubMed:27182009). Expressed in osteoblasts (PubMed:15465005).
{ECO:0000269|PubMed:15465005, ECO:0000269|PubMed:27182009}.
-!- INDUCTION: Down-regulated under hypoxic conditions in endothelial
cells (at protein level) (PubMed:21832157). Up-regulated by growth
factor (TGF-beta), cytokines, tumor necrosis factor (TNF-alpha)
and epidermal growth factor (EGF) in keratinocytes
(PubMed:20166898). Up-regulated also by glucocorticoid
dexamethasone in keratinocytes (PubMed:20166898). Up-regulated in
keratinocytes in response to wounding in a p38 MAPK-dependent
manner (PubMed:20166898, PubMed:27182009). Up-regulated by the
parathyroid hormone (PTH) in osteoblast-like cells in a cAMP/PKA-
dependent manner (PubMed:15465005, PubMed:19179481). Up-regulated
in response to adrenocorticotropic hormone (ACTH)
(PubMed:19179481). Up-regulated during monocyte/macrophage
differentiation in response to phorbol ester 12-O-
tetradecanoylphorbol-13-acetate (TPA) (PubMed:26542173). Down-
regulated by butyrate in colorectal cancer cells
(PubMed:10367403). {ECO:0000269|PubMed:10367403,
ECO:0000269|PubMed:15465005, ECO:0000269|PubMed:19179481,
ECO:0000269|PubMed:20166898, ECO:0000269|PubMed:21832157,
ECO:0000269|PubMed:26542173, ECO:0000269|PubMed:27182009}.
-!- 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 (PubMed:25106868).
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 (PubMed:15538381, PubMed:17030608).
AKT1-mediated phosphorylation at Ser-92 does not impair ARE-
containing RNA-binding (PubMed:15538381). 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 (PubMed:18326031). MAPKAPK2-mediated phosphorylations at
Ser-54, Ser-92 and Ser-203 do not impair ARE-containing RNA-
binding (PubMed:18326031). 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 (By similarity). {ECO:0000250|UniProtKB:P23950,
ECO:0000269|PubMed:15538381, ECO:0000269|PubMed:17030608,
ECO:0000269|PubMed:18326031, ECO:0000269|PubMed:19179481,
ECO:0000269|PubMed:25106868}.
-!- PTM: Ubiquitinated. Ubiquitination leads to proteasomal
degradation, a process inhibited by phosphorylations at Ser-90,
Ser-92 and Ser-203 (PubMed:17030608).
{ECO:0000269|PubMed:17030608}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ZFP36L1ID42866ch14q22.html";
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EMBL; X79066; CAA55670.1; -; mRNA.
EMBL; X79067; CAA55670.1; JOINED; mRNA.
EMBL; X99404; CAA67781.1; -; mRNA.
EMBL; BT019468; AAV38275.1; -; mRNA.
EMBL; BC018340; AAH18340.1; -; mRNA.
CCDS; CCDS9791.1; -.
PIR; S34854; S34854.
RefSeq; NP_001231627.1; NM_001244698.1.
RefSeq; NP_001231630.1; NM_001244701.1.
RefSeq; NP_004917.2; NM_004926.3.
UniGene; Hs.707091; -.
UniGene; Hs.85155; -.
PDB; 1W0V; X-ray; 2.27 A; C=325-333.
PDB; 1W0W; X-ray; 2.10 A; C=325-333.
PDBsum; 1W0V; -.
PDBsum; 1W0W; -.
ProteinModelPortal; Q07352; -.
SMR; Q07352; -.
BioGrid; 107144; 15.
IntAct; Q07352; 11.
MINT; MINT-1375566; -.
STRING; 9606.ENSP00000337386; -.
iPTMnet; Q07352; -.
PhosphoSitePlus; Q07352; -.
BioMuta; ZFP36L1; -.
DMDM; 1351254; -.
EPD; Q07352; -.
MaxQB; Q07352; -.
PaxDb; Q07352; -.
PeptideAtlas; Q07352; -.
PRIDE; Q07352; -.
DNASU; 677; -.
Ensembl; ENST00000336440; ENSP00000337386; ENSG00000185650.
Ensembl; ENST00000439696; ENSP00000388402; ENSG00000185650.
GeneID; 677; -.
KEGG; hsa:677; -.
UCSC; uc001xkh.3; human.
CTD; 677; -.
DisGeNET; 677; -.
EuPathDB; HostDB:ENSG00000185650.9; -.
GeneCards; ZFP36L1; -.
HGNC; HGNC:1107; ZFP36L1.
HPA; HPA001301; -.
MIM; 601064; gene.
neXtProt; NX_Q07352; -.
OpenTargets; ENSG00000185650; -.
PharmGKB; PA35027; -.
eggNOG; KOG1677; Eukaryota.
eggNOG; COG5063; LUCA.
GeneTree; ENSGT00530000063262; -.
HOGENOM; HOG000233479; -.
HOVERGEN; HBG008483; -.
InParanoid; Q07352; -.
KO; K18753; -.
OMA; LQHSYSF; -.
OrthoDB; EOG091G0957; -.
PhylomeDB; Q07352; -.
TreeFam; TF315463; -.
Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
SIGNOR; Q07352; -.
ChiTaRS; ZFP36L1; human.
EvolutionaryTrace; Q07352; -.
GeneWiki; ZFP36L1; -.
GenomeRNAi; 677; -.
PRO; PR:Q07352; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000185650; -.
CleanEx; HS_BRF1; -.
CleanEx; HS_ZFP36L1; -.
ExpressionAtlas; Q07352; baseline and differential.
Genevisible; Q07352; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0071889; F:14-3-3 protein binding; IDA: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:MGI.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:ProtInc.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0071320; P:cellular response to cAMP; 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; ISS:UniProtKB.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IMP:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA: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; IDA:UniProtKB.
GO; GO:0097403; P:cellular response to raffinose; ISS:UniProtKB.
GO; GO:0071472; P:cellular response to salt stress; ISS:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0060710; P:chorio-allantoic fusion; IEA:Ensembl.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
GO; GO:0048382; P:mesendoderm development; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; IMP:UniProtKB.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IDA:UniProtKB.
GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; ISS:UniProtKB.
GO; GO:0021915; P:neural tube development; IEA:Ensembl.
GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl.
GO; GO:0031086; P:nuclear-transcribed mRNA catabolic process, deadenylation-independent decay; ISS:UniProtKB.
GO; GO:0038066; P:p38MAPK cascade; ISS:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:1904582; P:positive regulation of intracellular mRNA localization; IMP:UniProtKB.
GO; GO:0045657; P:positive regulation of monocyte differentiation; IDA:UniProtKB.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
GO; GO:0003342; P:proepicardium development; IEA:Ensembl.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0045577; P:regulation of B cell differentiation; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; 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:0031440; P:regulation of mRNA 3'-end processing; IDA:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
GO; GO:0045661; P:regulation of myoblast differentiation; ISS:UniProtKB.
GO; GO:0072091; P:regulation of stem cell proliferation; ISS:UniProtKB.
GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
GO; GO:0060712; P:spongiotrophoblast layer development; IEA:Ensembl.
GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
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;
3D-structure; 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_0000089167.
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:0000269|PubMed:15687258}.
REGION 185 338 Necessary for mRNA decay activation.
{ECO:0000269|PubMed:15687258}.
COMPBIAS 307 316 Poly-Ser.
MOD_RES 54 54 Phosphoserine; by MAPKAPK2.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:18326031}.
MOD_RES 90 90 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:15538381}.
MOD_RES 92 92 Phosphoserine; by PKB/AKT1 and MAPKAPK2.
{ECO:0000269|PubMed:15538381,
ECO:0000269|PubMed:18326031}.
MOD_RES 203 203 Phosphoserine; by PKB/AKT1 and MAPKAPK2.
{ECO:0000269|PubMed:17030608,
ECO:0000269|PubMed:18326031}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 334 334 Phosphoserine; by RPS6KA1.
{ECO:0000269|PubMed:25106868}.
MUTAGEN 54 54 S->A: Inhibits MAPKAPK2-mediated ARE-
containing mRNA stabilization; when
associated with A-92 and A-203.
{ECO:0000269|PubMed:18326031}.
MUTAGEN 90 90 S->A: Inhibits interaction with 14-3-3
proteins and AKT1-mediated ARE-containing
mRNA stabilization, but does not affect
ARE binding; when associated with A-92.
{ECO:0000269|PubMed:15538381}.
MUTAGEN 92 92 S->A: Inhibits MAPKAPK2-mediated ARE-
containing mRNA stabilization; when
associated with A-54 and A-203. Inhibits
interaction with 14-3-3 proteins and
AKT1-mediated ARE-containing mRNA
stabilization; when associated with A-
203. Inhibits interaction with 14-3-3
proteins and AKT1-mediated ARE-containing
mRNA stabilization, but does not affect
ARE binding; when associated with A-90.
{ECO:0000269|PubMed:15538381,
ECO:0000269|PubMed:17030608,
ECO:0000269|PubMed:18326031}.
MUTAGEN 120 120 C->R: Reduces binding to ARE-containing
mRNAs and ARE-mediated mRNA decay.
Inhibits binding to ARE-containing mRNAs
and ARE-mediated mRNA decay; when
associated with R-158.
{ECO:0000269|PubMed:12198173,
ECO:0000269|PubMed:24700863}.
MUTAGEN 158 158 C->R: Reduces binding to ARE-containing
mRNAs and ARE-mediated mRNA decay.
Inhibits binding to ARE-containing mRNAs
and ARE-mediated mRNA decay; when
associated with R-120.
{ECO:0000269|PubMed:12198173,
ECO:0000269|PubMed:24700863}.
MUTAGEN 203 203 S->A: Inhibits interaction with 14-3-3
proteins and AKT1-mediated ARE-containing
mRNA stabilization; when associated with
A-92. Inhibits MAPKAPK2-mediated ARE-
containing mRNA stabilization; when
associated with A-54 and A-92.
{ECO:0000269|PubMed:17030608,
ECO:0000269|PubMed:18326031}.
MUTAGEN 334 334 S->A: Inhibits p38 MAPK-mediated LDLR
mRNA stabilization, but does not inhibit
interaction with CNOT1 and CNOT7; when
associated with A-336.
{ECO:0000269|PubMed:25106868}.
MUTAGEN 336 336 S->A: Inhibits p38 MAPK-mediated LDLR
mRNA stabilization, but does not inhibit
interaction with CNOT1 and CNOT7; when
associated with A-334.
{ECO:0000269|PubMed:25106868}.
CONFLICT 63 63 H -> R (in Ref. 3; CAA67781).
{ECO:0000305}.
SEQUENCE 338 AA; 36314 MW; 98236CD40C4531D2 CRC64;
MTTTLVSATI FDLSEVLCKG NKMLNYSAPS AGGCLLDRKA VGTPAGGGFP RRHSVTLPSS
KFHQNQLLSS LKGEPAPALS SRDSRFRDRS FSEGGERLLP TQKQPGGGQV NSSRYKTELC
RPFEENGACK YGDKCQFAHG IHELRSLTRH PKYKTELCRT FHTIGFCPYG PRCHFIHNAE
ERRALAGARD LSADRPRLQH SFSFAGFPSA AATAAATGLL DSPTSITPPP ILSADDLLGS
PTLPDGTNNP FAFSSQELAS LFAPSMGLPG GGSPTTFLFR PMSESPHMFD SPPSPQDSLS
DQEGYLSSSS SSHSGSDSPT LDNSRRLPIF SRLSISDD


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