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mRNA decay activator protein ZFP36L2 (Butyrate response factor 2) (EGF-response factor 2) (ERF-2) (TPA-induced sequence 11d) (Zinc finger protein 36, C3H1 type-like 2) (ZFP36-like 2)

 TISD_HUMAN              Reviewed;         494 AA.
P47974; Q53TB4; Q9BSJ3;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 3.
25-OCT-2017, entry version 163.
RecName: Full=mRNA decay activator protein ZFP36L2 {ECO:0000305};
AltName: Full=Butyrate response factor 2 {ECO:0000303|PubMed:10367403};
AltName: Full=EGF-response factor 2 {ECO:0000303|PubMed:7835719};
Short=ERF-2 {ECO:0000303|PubMed:7835719};
AltName: Full=TPA-induced sequence 11d {ECO:0000303|PubMed:7835719};
AltName: Full=Zinc finger protein 36, C3H1 type-like 2 {ECO:0000312|HGNC:HGNC:1108};
Short=ZFP36-like 2 {ECO:0000312|HGNC:HGNC:1108};
Name=ZFP36L2 {ECO:0000312|HGNC:HGNC:1108};
Synonyms=BRF2, ERF2 {ECO:0000303|PubMed:7835719}, RNF162C,
TIS11D {ECO:0000303|PubMed:7835719};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8545129;
Ino T., Yasui H., Hirano M., Kurosawa Y.;
"Identification of a member of the TIS11 early response gene family at
the insertion point of a DNA fragment containing a gene for the T-cell
receptor beta chain in an acute T-cell leukemia.";
Oncogene 11:2705-2710(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7835719; DOI=10.1016/0378-1119(94)00696-P;
Nie X.F., Maclean K.N., Kumar V., McKay I.A., Bustin S.A.;
"ERF-2, the human homologue of the murine Tis11d early response
gene.";
Gene 152:285-286(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
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).
[9]
RNA-BINDING, AND MUTAGENESIS OF GLU-157 AND GLU-195.
PubMed=20506496; DOI=10.1002/pro.401;
Morgan B.R., Massi F.;
"A computational study of RNA binding and specificity in the tandem
zinc finger domain of TIS11d.";
Protein Sci. 19:1222-1234(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
POSSIBLE INVOLVEMENT IN LEUKEMIAS.
PubMed=21109922;
Iwanaga E., Nanri T., Mitsuya H., Asou N.;
"Mutation in the RNA binding protein TIS11D/ZFP36L2 is associated with
the pathogenesis of acute leukemia.";
Int. J. Oncol. 38:25-31(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-238, 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).
[14]
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).
[15]
FUNCTION, RNA-BINDING, INTERACTION WITH CNOT7, PHOSPHORYLATION AT
SER-490 AND SER-492, 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).
[16]
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).
[17]
STRUCTURE BY NMR OF 151-220 IN COMPLEX WITH RNA, FUNCTION, AND
RNA-BINDING.
PubMed=14981510; DOI=10.1038/nsmb738;
Hudson B.P., Martinez-Yamout M.A., Dyson H.J., Wright P.E.;
"Recognition of the mRNA AU-rich element by the zinc finger domain of
TIS11d.";
Nat. Struct. Mol. Biol. 11:257-264(2004).
-!- 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:25106868, PubMed:14981510). Acts as a
3'-untranslated region (UTR) ARE mRNA-binding adapter protein to
communicate signaling events to the mRNA decay machinery
(PubMed:25106868). Functions by recruiting the CCR4-NOT
deadenylase complex and probably other components of the
cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs,
and hence promotes ARE-mediated mRNA deadenylation and decay
processes (PubMed:25106868). Binds to 3'-UTR ARE of numerous mRNAs
(PubMed:20506496, PubMed:25106868, PubMed:14981510). Promotes ARE-
containing mRNA decay of the low-density lipoprotein (LDL)
receptor (LDLR) mRNA in response to phorbol 12-myristate 13-
acetate (PMA) treatment in a p38 MAPK-dependent manner
(PubMed:25106868). Positively regulates early adipogenesis by
promoting ARE-mediated mRNA decay of immediate early genes (IEGs).
Plays a role in mature peripheral neuron integrity by promoting
ARE-containing mRNA decay of the transcriptional repressor REST
mRNA. Plays a role in ovulation and oocyte meiotic maturation by
promoting ARE-mediated mRNA decay of the luteinizing hormone
receptor LHCGR mRNA. Acts as a negative regulator of erythroid
cell differentiation: promotes glucocorticoid-induced self-renewal
of erythroid cells by binding mRNAs that are induced or highly
expressed during terminal erythroid differentiation and promotes
their degradation, preventing erythroid cell differentiation. In
association with ZFP36L1 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 process and functional immune cell
formation. Together with ZFP36L1 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.
{ECO:0000250|UniProtKB:P23949, ECO:0000269|PubMed:14981510,
ECO:0000269|PubMed:20506496, ECO:0000269|PubMed:25106868}.
-!- SUBUNIT: Associates with the cytoplasmic CCR4-NOT deadenylase to
trigger ARE-containing mRNA deadenylation and decay processes
(PubMed:25106868). 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).
{ECO:0000269|PubMed:25106868}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P23949}.
Cytoplasm {ECO:0000250|UniProtKB:P23949}. Note=Shuttles between
the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner.
{ECO:0000250|UniProtKB:P23949}.
-!- 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). {ECO:0000269|PubMed:27182009}.
-!- INDUCTION: Up-regulated by butyrate in colorectal cancer cells
(PubMed:10367403). Up-regulated in keratinocytes after wounding
(PubMed:20166898, PubMed:27182009). Up-regulated strongly by
granulocyte macrophage colony-stimulating factor (GM-CSF) in
keratinocytes (PubMed:20166898). Up-regulated moderately by
transforming growth factor (TGF-beta), epidermal growth factor
(EGF), tumor necrosis factor (TNF-alpha) and fibroblast growth
factor (FGF1) in keratinocytes (PubMed:20166898). Up-regulated
also by glucocorticoid dexamethasone in keratinocytes
(PubMed:20166898). {ECO:0000269|PubMed:10367403,
ECO:0000269|PubMed:20166898, ECO:0000269|PubMed:27182009}.
-!- PTM: Phosphorylated by RPS6KA1 at Ser-490 and Ser-492 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 (LDL) receptor (LDLR) mRNA (PubMed:25106868).
Phosphorylation occurs during early preadipocyte differentiation
(By similarity). {ECO:0000250|UniProtKB:P23949,
ECO:0000269|PubMed:25106868}.
-!- DISEASE: Note=Defects in ZFP36L2 may be a cause of leukemias.
Frameshfits mutations disrupting ZFP36L2 have been found in a
patient with acute myeloid leukemia (PubMed:21109922).
{ECO:0000269|PubMed:21109922}.
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EMBL; U07802; AAA91778.1; -; Genomic_DNA.
EMBL; X78992; CAA55592.1; -; mRNA.
EMBL; AC010883; AAY14992.1; -; Genomic_DNA.
EMBL; CH471053; EAX00306.1; -; Genomic_DNA.
EMBL; BC005010; AAH05010.1; -; mRNA.
CCDS; CCDS1811.1; -.
PIR; S49147; S49147.
RefSeq; NP_008818.3; NM_006887.4.
UniGene; Hs.503093; -.
PDB; 1RGO; NMR; -; A=151-220.
PDBsum; 1RGO; -.
ProteinModelPortal; P47974; -.
SMR; P47974; -.
BioGrid; 107145; 9.
IntAct; P47974; 8.
STRING; 9606.ENSP00000282388; -.
iPTMnet; P47974; -.
PhosphoSitePlus; P47974; -.
BioMuta; ZFP36L2; -.
DMDM; 146291085; -.
EPD; P47974; -.
MaxQB; P47974; -.
PaxDb; P47974; -.
PeptideAtlas; P47974; -.
PRIDE; P47974; -.
DNASU; 678; -.
Ensembl; ENST00000282388; ENSP00000282388; ENSG00000152518.
GeneID; 678; -.
KEGG; hsa:678; -.
UCSC; uc002rsv.5; human.
CTD; 678; -.
DisGeNET; 678; -.
EuPathDB; HostDB:ENSG00000152518.6; -.
GeneCards; ZFP36L2; -.
HGNC; HGNC:1108; ZFP36L2.
HPA; HPA047428; -.
MIM; 612053; gene.
neXtProt; NX_P47974; -.
OpenTargets; ENSG00000152518; -.
PharmGKB; PA35028; -.
eggNOG; KOG1677; Eukaryota.
eggNOG; COG5063; LUCA.
GeneTree; ENSGT00530000063262; -.
HOGENOM; HOG000233479; -.
HOVERGEN; HBG008483; -.
InParanoid; P47974; -.
KO; K18753; -.
OMA; QRDRPKL; -.
OrthoDB; EOG091G0957; -.
PhylomeDB; P47974; -.
TreeFam; TF315463; -.
ChiTaRS; ZFP36L2; human.
EvolutionaryTrace; P47974; -.
GenomeRNAi; 678; -.
PRO; PR:P47974; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000152518; -.
CleanEx; HS_BRF2; -.
CleanEx; HS_ZFP36L2; -.
Genevisible; P47974; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0017091; F:AU-rich element 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:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:UniProtKB.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IDA: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:0060216; P:definitive hemopoiesis; ISS:UniProtKB.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; ISS:UniProtKB.
GO; GO:2000737; P:negative regulation of stem cell differentiation; ISS:UniProtKB.
GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
GO; GO:0045577; P:regulation of B cell differentiation; ISS:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB.
GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
GO; GO:0048103; P:somatic stem cell division; ISS:UniProtKB.
GO; GO:0035019; P:somatic stem cell population maintenance; ISS:UniProtKB.
GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
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; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Zinc;
Zinc-finger.
CHAIN 1 494 mRNA decay activator protein ZFP36L2.
/FTId=PRO_0000089170.
ZN_FING 153 181 C3H1-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 191 219 C3H1-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
REGION 170 211 RNA-binding.
{ECO:0000269|PubMed:14981510,
ECO:0000269|PubMed:20506496}.
MOTIF 153 158 RNA-binding.
{ECO:0000269|PubMed:14981510,
ECO:0000269|PubMed:20506496}.
COMPBIAS 106 109 Poly-Gly.
COMPBIAS 138 141 Poly-Gln.
COMPBIAS 143 146 Poly-Gly.
COMPBIAS 288 291 Poly-Pro.
COMPBIAS 323 332 Poly-Ala.
COMPBIAS 384 390 Poly-Ala.
COMPBIAS 395 401 Poly-Gln.
MOD_RES 57 57 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 238 238 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 490 490 Phosphoserine; by RPS6KA1.
{ECO:0000269|PubMed:25106868}.
MOD_RES 492 492 Phosphoserine; by RPS6KA1.
{ECO:0000269|PubMed:25106868}.
MUTAGEN 157 157 E->R: Impaired mRNA-binding; when
associated with K-195.
{ECO:0000269|PubMed:20506496}.
MUTAGEN 195 195 E->K: Impaired mRNA-binding; when
associated with R-157.
{ECO:0000269|PubMed:20506496}.
CONFLICT 96 97 TS -> DL (in Ref. 1; AAA91778).
{ECO:0000305}.
CONFLICT 318 318 A -> T (in Ref. 2; CAA55592).
{ECO:0000305}.
CONFLICT 329 332 AAAA -> LR (in Ref. 2; CAA55592).
{ECO:0000305}.
CONFLICT 331 332 Missing (in Ref. 1; AAA91778).
{ECO:0000305}.
CONFLICT 400 400 Q -> QQQQ (in Ref. 5; AAH05010).
{ECO:0000305}.
CONFLICT 453 462 Missing (in Ref. 1; AAA91778).
{ECO:0000305}.
TURN 152 155 {ECO:0000244|PDB:1RGO}.
STRAND 156 158 {ECO:0000244|PDB:1RGO}.
HELIX 160 165 {ECO:0000244|PDB:1RGO}.
HELIX 171 173 {ECO:0000244|PDB:1RGO}.
STRAND 175 179 {ECO:0000244|PDB:1RGO}.
HELIX 180 182 {ECO:0000244|PDB:1RGO}.
TURN 190 193 {ECO:0000244|PDB:1RGO}.
HELIX 198 203 {ECO:0000244|PDB:1RGO}.
HELIX 209 211 {ECO:0000244|PDB:1RGO}.
STRAND 213 215 {ECO:0000244|PDB:1RGO}.
SEQUENCE 494 AA; 51063 MW; 10E23FA9E2DDABD4 CRC64;
MSTTLLSAFY DVDFLCKTEK SLANLNLNNM LDKKAVGTPV AAAPSSGFAP GFLRRHSASN
LHALAHPAPS PGSCSPKFPG AANGSSCGSA AAGGPTSYGT LKEPSGGGGT ALLNKENKFR
DRSFSENGDR SQHLLHLQQQ QKGGGGSQIN STRYKTELCR PFEESGTCKY GEKCQFAHGF
HELRSLTRHP KYKTELCRTF HTIGFCPYGP RCHFIHNADE RRPAPSGGAS GDLRAFGTRD
ALHLGFPREP RPKLHHSLSF SGFPSGHHQP PGGLESPLLL DSPTSRTPPP PSCSSASSCS
SSASSCSSAS AASTPSGAPT CCASAAAAAA AALLYGTGGA EDLLAPGAPC AACSSASCAN
NAFAFGPELS SLITPLAIQT HNFAAVAAAA YYRSQQQQQQ QGLAPPAQPP APPSATLPAG
AAAPPSPPFS FQLPRRLSDS PVFDAPPSPP DSLSDRDSYL SGSLSSGSLS GSESPSLDPG
RRLPIFSRLS ISDD


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Catalog number Product name Quantity
EIAAB42488 BRF2,Butyrate response factor 2,EGF-response factor 2,ERF2,ERF-2,Homo sapiens,Human,Protein TIS11D,RNF162C,TIS11D,ZFP36L2,Zinc finger protein 36, C3H1 type-like 2
EIAAB42487 Brf2,Butyrate response factor 2,Mouse,Mus musculus,Protein TIS11D,Tis11d,Zfp36l2,Zinc finger protein 36, C3H1 type-like 2
EIAAB42486 BERG36,BRF1,Butyrate response factor 1,EGF-response factor 1,ERF1,ERF-1,Homo sapiens,Human,Protein TIS11B,RNF162B,TIS11B,ZFP36L1,Zinc finger protein 36, C3H1 type-like 1
EIAAB42484 Brf1,Butyrate response factor 1,Mouse,Mus musculus,Protein TIS11B,Tis11b,Zfp36l1,Zinc finger protein 36, C3H1 type-like 1
EIAAB42485 Brf1,Butyrate response factor 1,Cmg1,EGF-inducible protein CMG1,Protein TIS11B,Rat,Rattus norvegicus,Tis11b,Zfp36l1,Zinc finger protein 36, C3H1 type-like 1
27-526 Early Growth Response Protein 1 (EGR1, Krox-24 protein, nerve growth factor-induced protein A, Transcription factor ETR103, Zinc finger protein 225) belongs to the EGR family of C2H2-type zinc-finger 0.05 mg
28-572 Early Growth Response Protein 1 (EGR1, Krox-24 protein, nerve growth factor-induced protein A, Transcription factor ETR103, Zinc finger protein 225) belongs to the EGR family of C2H2-type zinc-finger 0.1 mg
18-003-42165 Early growth response protein 1 - EGR-1; Krox-24 protein; Transcription factor Zif268; Nerve growth factor-induced protein A; NGFI-A; Transcription factor ETR103; Zinc finger protein 225; AT225 Polycl 0.05 mg Aff Pur
U0416r CLIA Early growth response protein 1,Egr1,EGR-1,Nerve growth factor-induced protein A,NGFI-A,Rat,Rattus norvegicus,Transcription factor Zif268,Zinc finger protein Krox-24 96T
E0416r ELISA Early growth response protein 1,Egr1,EGR-1,Nerve growth factor-induced protein A,NGFI-A,Rat,Rattus norvegicus,Transcription factor Zif268,Zinc finger protein Krox-24 96T
E0416r ELISA kit Early growth response protein 1,Egr1,EGR-1,Nerve growth factor-induced protein A,NGFI-A,Rat,Rattus norvegicus,Transcription factor Zif268,Zinc finger protein Krox-24 96T
U0416h CLIA AT225,Early growth response protein 1,EGR1,EGR-1,Homo sapiens,Human,KROX24,Nerve growth factor-induced protein A,NGFI-A,Transcription factor ETR103,Transcription factor Zif268,Zinc finger protein 96T
18-003-42365 Butyrate response factor 1 - TIS11B protein; EGF-response factor 1; ERF-1 Polyclonal 0.1 mg Protein A
18-003-44093 Butyrate response factor 2 - Protein TIS11D; EGF-response factor 2; ERF-2 Polyclonal 0.1 mg Protein A
18-003-42365 Butyrate response factor 1 - TIS11B protein; EGF-response factor 1; ERF-1 Polyclonal 0.05 mg Aff Pur
18-003-42366 Butyrate response factor 1 - TIS11B protein; EGF-response factor 1; ERF-1 Polyclonal 0.05 mg Aff Pur
E0416h ELISA kit AT225,Early growth response protein 1,EGR1,EGR-1,Homo sapiens,Human,KROX24,Nerve growth factor-induced protein A,NGFI-A,Transcription factor ETR103,Transcription factor Zif268,Zinc finger p 96T
E0416h ELISA AT225,Early growth response protein 1,EGR1,EGR-1,Homo sapiens,Human,KROX24,Nerve growth factor-induced protein A,NGFI-A,Transcription factor ETR103,Transcription factor Zif268,Zinc finger protei 96T
U0416m CLIA Early growth response protein 1,Egr1,EGR-1,Egr-1,Krox-24,Mouse,Mus musculus,Nerve growth factor-induced protein A,NGFI-A,Transcription factor Zif268,Zinc finger protein Krox-24 96T
E0416m ELISA kit Early growth response protein 1,Egr1,EGR-1,Egr-1,Krox-24,Mouse,Mus musculus,Nerve growth factor-induced protein A,NGFI-A,Transcription factor Zif268,Zinc finger protein Krox-24 96T
E0416m ELISA Early growth response protein 1,Egr1,EGR-1,Egr-1,Krox-24,Mouse,Mus musculus,Nerve growth factor-induced protein A,NGFI-A,Transcription factor Zif268,Zinc finger protein Krox-24 96T
28-842 ZFP36 is a probable regulatory protein with a novel zinc finger structure involved in regulating the response to growth factors. Knockdown of ZFP36 increased both cognate macrophage gene mRNAs and inf 0.05 mg
EIAAB39974 Cl-4,Delayed-early protein HRS,Hrs,Insulin-induced growth response protein CL-4,Pre-mRNA-splicing factor SRP40,Rat,Rattus norvegicus,Serine_arginine-rich splicing factor 5,Sfrs5,Splicing factor, argin
I3507 Zinc finger protein 36, C3H1 type-like 2 (ZFP36L2), Human, ELISA Kit 96T
CSB-EL026450MO Mouse Zinc finger protein 36, C3H1 type-like 2(ZFP36L2) ELISA kit 96T


 

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