TISD_MOUSE
ID TISD_MOUSE Reviewed; 484 AA.
AC P23949; B9EIF6; Q3TCE3; Q3TU59;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=mRNA decay activator protein ZFP36L2 {ECO:0000305};
DE AltName: Full=Butyrate response factor 2 {ECO:0000250|UniProtKB:P47974};
DE AltName: Full=TPA-induced sequence 11d {ECO:0000303|PubMed:1996120};
DE AltName: Full=Zinc finger protein 36, C3H1 type-like 2 {ECO:0000312|MGI:MGI:107945};
DE Short=ZFP36-like 2 {ECO:0000312|MGI:MGI:107945};
GN Name=Zfp36l2 {ECO:0000312|MGI:MGI:107945};
GN Synonyms=Tis11d {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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RA Fletcher B.S.;
RT "Structure and expression of two mitogen inducible genes.";
RL Thesis (1992), University of California Los Angeles, United States.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-396.
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 [6]
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 [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=15342461; DOI=10.1242/dev.01336;
RA Ramos S.B., Stumpo D.J., Kennington E.A., Phillips R.S., Bock C.B.,
RA Ribeiro-Neto F., Blackshear P.J.;
RT "The CCCH tandem zinc-finger protein Zfp36l2 is crucial for female
RT fertility and early embryonic development.";
RL Development 131:4883-4893(2004).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=19633199; DOI=10.1182/blood-2009-04-214619;
RA Stumpo D.J., Broxmeyer H.E., Ward T., Cooper S., Hangoc G., Chung Y.J.,
RA Shelley W.C., Richfield E.K., Ray M.K., Yoder M.C., Aplan P.D.,
RA Blackshear P.J.;
RT "Targeted disruption of Zfp36l2, encoding a CCCH tandem zinc finger RNA-
RT binding protein, results in defective hematopoiesis.";
RL Blood 114:2401-2410(2009).
RN [9]
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 [10]
RP FUNCTION, RNA-BINDING, PHOSPHORYLATION, AND TISSUE 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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22367205; DOI=10.1074/jbc.m111.330837;
RA Ramos S.B.;
RT "Characterization of DeltaN-Zfp36l2 mutant associated with arrest of early
RT embryonic development and female infertility.";
RL J. Biol. Chem. 287:13116-13127(2012).
RN [12]
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 [13]
RP FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, AND RNA-BINDING.
RX PubMed=23748442; DOI=10.1038/nature12215;
RA Zhang L., Prak L., Rayon-Estrada V., Thiru P., Flygare J., Lim B.,
RA Lodish H.F.;
RT "ZFP36L2 is required for self-renewal of early burst-forming unit erythroid
RT progenitors.";
RL Nature 499:92-96(2013).
RN [14]
RP FUNCTION, RNA-BINDING, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-176, AND
RP TISSUE SPECIFICITY.
RX PubMed=25505318; DOI=10.1523/jneurosci.1650-14.2014;
RA Cargnin F., Nechiporuk T., Muellendorff K., Stumpo D.J., Blackshear P.J.,
RA Ballas N., Mandel G.;
RT "An RNA binding protein promotes axonal integrity in peripheral neurons by
RT destabilizing REST.";
RL J. Neurosci. 34:16650-16661(2014).
RN [15]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=24830504; DOI=10.1371/journal.pone.0097324;
RA Ball C.B., Rodriguez K.F., Stumpo D.J., Ribeiro-Neto F., Korach K.S.,
RA Blackshear P.J., Birnbaumer L., Ramos S.B.;
RT "The RNA-binding protein, ZFP36L2, influences ovulation and oocyte
RT maturation.";
RL PLoS ONE 9:E97324-E97324(2014).
RN [16]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND 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 [17]
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 [18]
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:22367205, PubMed:25505318, PubMed:24830504, PubMed:27102483).
CC Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein
CC to communicate signaling events to the mRNA decay machinery (By
CC similarity). Functions by recruiting the CCR4-NOT deadenylase complex
CC and probably other components of the cytoplasmic RNA decay machinery to
CC the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA
CC deadenylation and decay processes (By similarity). Binds to 3'-UTR ARE
CC of numerous mRNAs (PubMed:22701344, PubMed:22367205, PubMed:25505318,
CC PubMed:24830504). Promotes ARE-containing mRNA decay of the low-density
CC lipoprotein (LDL) receptor (LDLR) mRNA in response to phorbol 12-
CC myristate 13-acetate (PMA) treatment in a p38 MAPK-dependent manner (By
CC similarity). Positively regulates early adipogenesis by promoting ARE-
CC mediated mRNA decay of immediate early genes (IEGs) (PubMed:22701344).
CC Plays a role in mature peripheral neuron integrity by promoting ARE-
CC containing mRNA decay of the transcriptional repressor REST mRNA
CC (PubMed:25505318). Plays a role in ovulation and oocyte meiotic
CC maturation by promoting ARE-mediated mRNA decay of the luteinizing
CC hormone receptor LHCGR mRNA (PubMed:24830504). Acts as a negative
CC regulator of erythroid cell differentiation: promotes glucocorticoid-
CC induced self-renewal of erythroid cells by binding mRNAs that are
CC induced or highly expressed during terminal erythroid differentiation
CC and promotes their degradation, preventing erythroid cell
CC differentiation (PubMed:19633199, PubMed:23748442). In association with
CC ZFP36L1 maintains quiescence on developing B lymphocytes by promoting
CC ARE-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 process and
CC functional immune cell formation (PubMed:27102483). Together with
CC ZFP36L1 is also necessary for thymocyte development and prevention of
CC T-cell acute lymphoblastic leukemia (T-ALL) transformation by promoting
CC ARE-mediated mRNA decay of the oncogenic transcription factor NOTCH1
CC mRNA (PubMed:20622884). {ECO:0000250|UniProtKB:P47974,
CC ECO:0000269|PubMed:19633199, ECO:0000269|PubMed:20622884,
CC ECO:0000269|PubMed:22367205, ECO:0000269|PubMed:22701344,
CC ECO:0000269|PubMed:23748442, ECO:0000269|PubMed:24830504,
CC ECO:0000269|PubMed:25505318, ECO:0000269|PubMed:27102483}.
CC -!- SUBUNIT: Associates with the cytoplasmic CCR4-NOT deadenylase to
CC trigger ARE-containing mRNA deadenylation and decay processes.
CC Interacts with CNOT7; this interaction is inhibited in response to
CC phorbol 12-myristate 13-acetate (PMA) treatment in a p38 MAPK-dependent
CC manner. {ECO:0000250|UniProtKB:P47974}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11796723,
CC ECO:0000269|PubMed:22367205, ECO:0000269|PubMed:24733888}. Cytoplasm
CC {ECO:0000269|PubMed:11796723, ECO:0000269|PubMed:22367205,
CC ECO:0000269|PubMed:24733888}. Note=Shuttles between the nucleus and the
CC cytoplasm in a XPO1/CRM1-dependent manner (PubMed:11796723,
CC PubMed:22367205). {ECO:0000269|PubMed:11796723,
CC ECO:0000269|PubMed:22367205}.
CC -!- TISSUE SPECIFICITY: Expressed in preadipocytes and adipocytes (at
CC protein level) (PubMed:22701344). Expressed at highest level in
CC lymphoid tissues such as thymus, spleen, lung, uterus, ovary, small and
CC large intestine, mammary gland, fat and bone marrow (PubMed:19633199,
CC PubMed:22367205). Expressed at intermediate level in kidney, heart,
CC adrenal, eye and fetal liver (PubMed:19633199). Weakly expressed in
CC brain, skeletal muscle and liver (PubMed:19633199, PubMed:22367205).
CC Expressed through B lymphocyte development (PubMed:27102483). Expressed
CC in superior cervical ganglion (SCG) and dorsal root ganglion (DRG)
CC (PubMed:25505318). Expressed in embryonic stem cells (ESCs)
CC (PubMed:24733888). {ECO:0000269|PubMed:19633199,
CC ECO:0000269|PubMed:22367205, ECO:0000269|PubMed:22701344,
CC ECO:0000269|PubMed:24733888, ECO:0000269|PubMed:25505318,
CC ECO:0000269|PubMed:27102483}.
CC -!- DEVELOPMENTAL STAGE: In embryos, expression is detected at 7 dpc,
CC increases at 9.5 dpc, and then remains constant through 18.5 dpc
CC (PubMed:19633199). Expression in the yolk sac is relatively constant
CC between 10.5 dpc and 18.5 dpc (PubMed:19633199). Placenta expression is
CC also constant throughout development with a slight decrease observed at
CC 18.5 dpc (PubMed:19633199). Expressed in burst-forming unit-erythroid
CC (BFU-E) progenitor cells and down-regulated as erythroid cells
CC differentiate (PubMed:23748442). {ECO:0000269|PubMed:19633199,
CC ECO:0000269|PubMed:23748442}.
CC -!- INDUCTION: Up-regulated in response to fibroblast growth factor FGF4 in
CC embryonic stem cells (ESCs) in a p38 MAPK-dependent manner (at protein
CC level) (PubMed:24733888). Up-regulated by glucocorticoid agonists, such
CC as dexamethasone (DEX), in burst-forming unit-erythroid (BFU-E)
CC progenitors in a receptor NR3C1-dependent manner (PubMed:23748442).
CC Down-regulated during erythroid cell differentiation (PubMed:23748442).
CC Down-regulated during the conversion from quiescence to activated
CC satellite cells upon muscle injury (PubMed:23046558, PubMed:25815583).
CC {ECO:0000269|PubMed:23046558, ECO:0000269|PubMed:23748442,
CC ECO:0000269|PubMed:24733888, ECO:0000269|PubMed:25815583}.
CC -!- PTM: Phosphorylated by RPS6KA1 at Ser-480 and Ser-482 upon phorbol 12-
CC myristate 13-acetate (PMA) treatment; this phosphorylation results in
CC dissociation of the CCR4-NOT-deadenylase complex and induces p38 MAPK-
CC mediated stabilization of the low-density lipoprotein (LDL) receptor
CC (LDLR) mRNA (By similarity). Phosphorylation occurs during early
CC preadipocyte differentiation (PubMed:22701344).
CC {ECO:0000250|UniProtKB:P47974, ECO:0000269|PubMed:22701344}.
CC -!- DISRUPTION PHENOTYPE: Lethality between 2 weeks of birth, due to
CC pancytopenia (PubMed:19633199). Peripheral blood shows a decrease in
CC red and white cells, hemoglobin, hematocrit and platelets
CC (PubMed:19633199). Yolk sacs from 11.5 dpc and fetal livers from 14.5
CC dpc display markedly reduced numbers of definitive multilineage and
CC lineage-committed hematopoietic progenitors (PubMed:19633199). Mice
CC lacking the N-terminus (DeltaN-ZFP36L2) display female infertility,
CC with embryos that cannot progress beyond the 2-cell stage of
CC development (PubMed:15342461). Show evidence of axonal and fiber
CC degeneration (PubMed:25505318). Exhibit increased REST mRNA stability
CC and REST protein expression in primary neuronal cells from superior
CC cervical ganglion (SCG) and dorsal root ganglion (DRG)
CC (PubMed:25505318). Mice lacking both ZFP36L2 and ZFP36L1 during
CC thymopoiesis lead to aberrant T cell development and subsequently
CC develop a T-cell acute lymphoblastic leukemia (T-ALL)
CC (PubMed:20622884). Show also higher levels of NOTCH1 mRNA and protein
CC in thymocytes (PubMed:20622884). Conditional knockout mice of both
CC ZFP36L2 and ZFP36L1 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:15342461, ECO:0000269|PubMed:19633199,
CC ECO:0000269|PubMed:20622884, ECO:0000269|PubMed:25505318,
CC ECO:0000269|PubMed:27102483}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39709.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA72946.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA72946.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK160955; BAE36112.1; -; mRNA.
DR EMBL; AK170763; BAE42014.1; -; mRNA.
DR EMBL; AC132455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139416; AAI39417.1; -; mRNA.
DR EMBL; M97165; AAA39709.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M58564; AAA72946.1; ALT_SEQ; mRNA.
DR CCDS; CCDS28998.1; -.
DR PIR; C39590; C39590.
DR RefSeq; NP_001001806.1; NM_001001806.2.
DR AlphaFoldDB; P23949; -.
DR SMR; P23949; -.
DR IntAct; P23949; 4.
DR MINT; P23949; -.
DR STRING; 10090.ENSMUSP00000050820; -.
DR iPTMnet; P23949; -.
DR PhosphoSitePlus; P23949; -.
DR EPD; P23949; -.
DR MaxQB; P23949; -.
DR PaxDb; P23949; -.
DR PeptideAtlas; P23949; -.
DR PRIDE; P23949; -.
DR ProteomicsDB; 262796; -.
DR Antibodypedia; 14846; 248 antibodies from 31 providers.
DR DNASU; 12193; -.
DR Ensembl; ENSMUST00000060366; ENSMUSP00000050820; ENSMUSG00000045817.
DR GeneID; 12193; -.
DR KEGG; mmu:12193; -.
DR UCSC; uc008dsq.2; mouse.
DR CTD; 678; -.
DR MGI; MGI:107945; Zfp36l2.
DR VEuPathDB; HostDB:ENSMUSG00000045817; -.
DR eggNOG; KOG1677; Eukaryota.
DR GeneTree; ENSGT00940000161584; -.
DR HOGENOM; CLU_033040_1_0_1; -.
DR InParanoid; P23949; -.
DR OMA; GYGQREV; -.
DR OrthoDB; 1541140at2759; -.
DR PhylomeDB; P23949; -.
DR TreeFam; TF315463; -.
DR BioGRID-ORCS; 12193; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Zfp36l2; mouse.
DR PRO; PR:P23949; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P23949; protein.
DR Bgee; ENSMUSG00000045817; Expressed in ureter smooth muscle and 241 other tissues.
DR Genevisible; P23949; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0061158; P:3'-UTR-mediated mRNA destabilization; 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:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISS: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:0060216; P:definitive hemopoiesis; IMP:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IMP:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:UniProtKB.
DR GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:MGI.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:UniProtKB.
DR GO; GO:0045577; P:regulation of B cell differentiation; IMP:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR GO; GO:0048103; P:somatic stem cell division; IMP:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:UniProtKB.
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; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..484
FT /note="mRNA decay activator protein ZFP36L2"
FT /id="PRO_0000089171"
FT ZN_FING 155..183
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 193..221
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 100..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..213
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT REGION 261..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..160
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT COMPBIAS 117..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT MOD_RES 480
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT MOD_RES 482
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT MUTAGEN 176
FT /note="C->S: Inhibits RNA-binding."
FT /evidence="ECO:0000269|PubMed:25505318"
FT CONFLICT 413
FT /note="A -> T (in Ref. 1; BAE42014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 50070 MW; FBEB18B64775842A CRC64;
MSTTLLSPFY DIDFLCKTEK SLANLNLNNM LDKKAVGTPV AAAPSSSFTP GFLRRHSASN
LHALAHPVPS PGSCSPKFPG APNGGGSSCG PAGGGGLASY GQLKEPSGGS GTALVTKESK
FRDRSFSENG ERSQHLLHLQ QQQKGGSGSQ INSTRYKTEL CRPFEESGTC KYGEKCQFAH
GFHELRSLTR HPKYKTELCR TFHTIGFCPY GPRCHFIHNA DERRPAPSGG GGASGDLRAF
GARDALHLGF AREPRPKLHH SLSFSGFPSG HHQPPGGLES PLLLDSPTSR TPPPPSSSAS
SCSSSASSCS SASAASTPSG APTCCATAAA AALLYGPGGA EDLLSPGAPC ASCSSSGANN
AFAFGPELSS LITPLAIQTH NFAAAAAAAY YRNQQQGLTG PAPPPAQPPA APAPPSPPFG
FQLPRRLSES PVFDAPPSPP DSLSDRDSYL SGSLSSGSLS GSESPSLDPG RRLPIFSRLS
ISDD
