TISD_HUMAN
ID TISD_HUMAN Reviewed; 494 AA.
AC P47974; Q53TB4; Q9BSJ3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=mRNA decay activator protein ZFP36L2 {ECO:0000305};
DE AltName: Full=Butyrate response factor 2 {ECO:0000303|PubMed:10367403};
DE AltName: Full=EGF-response factor 2 {ECO:0000303|PubMed:7835719};
DE Short=ERF-2 {ECO:0000303|PubMed:7835719};
DE AltName: Full=TPA-induced sequence 11d {ECO:0000303|PubMed:7835719};
DE AltName: Full=Zinc finger protein 36, C3H1 type-like 2 {ECO:0000312|HGNC:HGNC:1108};
DE Short=ZFP36-like 2 {ECO:0000312|HGNC:HGNC:1108};
GN Name=ZFP36L2 {ECO:0000312|HGNC:HGNC:1108};
GN Synonyms=ERF2 {ECO:0000303|PubMed:7835719}, RNF162C,
GN TIS11D {ECO:0000303|PubMed:7835719};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8545129;
RA Ino T., Yasui H., Hirano M., Kurosawa Y.;
RT "Identification of a member of the TIS11 early response gene family at the
RT insertion point of a DNA fragment containing a gene for the T-cell receptor
RT beta chain in an acute T-cell leukemia.";
RL Oncogene 11:2705-2710(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7835719; DOI=10.1016/0378-1119(94)00696-p;
RA Nie X.F., Maclean K.N., Kumar V., McKay I.A., Bustin S.A.;
RT "ERF-2, the human homologue of the murine Tis11d early response gene.";
RL Gene 152:285-286(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [6]
RP INDUCTION.
RX PubMed=10367403;
RA Maclean K.N., McKay I.A., Bustin S.A.;
RT "Differential effects of sodium butyrate on the transcription of the human
RT TIS11 family of early-response genes in colorectal cancer cells.";
RL Br. J. Biomed. Sci. 55:184-191(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP INDUCTION.
RX PubMed=20166898; DOI=10.3109/08977190903578660;
RA Hacker C., Valchanova R., Adams S., Munz B.;
RT "ZFP36L1 is regulated by growth factors and cytokines in keratinocytes and
RT influences their VEGF production.";
RL Growth Factors 28:178-190(2010).
RN [9]
RP RNA-BINDING, AND MUTAGENESIS OF GLU-157 AND GLU-195.
RX PubMed=20506496; DOI=10.1002/pro.401;
RA Morgan B.R., Massi F.;
RT "A computational study of RNA binding and specificity in the tandem zinc
RT finger domain of TIS11d.";
RL Protein Sci. 19:1222-1234(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP POSSIBLE INVOLVEMENT IN LEUKEMIAS.
RX PubMed=21109922;
RA Iwanaga E., Nanri T., Mitsuya H., Asou N.;
RT "Mutation in the RNA binding protein TIS11D/ZFP36L2 is associated with the
RT pathogenesis of acute leukemia.";
RL Int. J. Oncol. 38:25-31(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP FUNCTION, RNA-BINDING, INTERACTION WITH CNOT7, PHOSPHORYLATION AT SER-490
RP AND SER-492, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25106868; DOI=10.1093/nar/gku652;
RA Adachi S., Homoto M., Tanaka R., Hioki Y., Murakami H., Suga H.,
RA Matsumoto M., Nakayama K.I., Hatta T., Iemura S., Natsume T.;
RT "ZFP36L1 and ZFP36L2 control LDLR mRNA stability via the ERK-RSK pathway.";
RL Nucleic Acids Res. 42:10037-10049(2014).
RN [16]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=27182009; DOI=10.1016/j.ejcb.2016.04.007;
RA Prenzler F., Fragasso A., Schmitt A., Munz B.;
RT "Functional analysis of ZFP36 proteins in keratinocytes.";
RL Eur. J. Cell Biol. 95:277-284(2016).
RN [17]
RP STRUCTURE BY NMR OF 151-220 IN COMPLEX WITH RNA, FUNCTION, AND RNA-BINDING.
RX PubMed=14981510; DOI=10.1038/nsmb738;
RA Hudson B.P., Martinez-Yamout M.A., Dyson H.J., Wright P.E.;
RT "Recognition of the mRNA AU-rich element by the zinc finger domain of
RT TIS11d.";
RL Nat. Struct. Mol. Biol. 11:257-264(2004).
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:25106868,
CC PubMed:14981510). Acts as a 3'-untranslated region (UTR) ARE mRNA-
CC binding adapter protein to communicate signaling events to the mRNA
CC decay machinery (PubMed:25106868). Functions by recruiting the CCR4-NOT
CC deadenylase complex and probably other components of the cytoplasmic
CC RNA decay machinery to the bound ARE-containing mRNAs, and hence
CC promotes ARE-mediated mRNA deadenylation and decay processes
CC (PubMed:25106868). Binds to 3'-UTR ARE of numerous mRNAs
CC (PubMed:20506496, PubMed:25106868, PubMed:14981510). Promotes ARE-
CC containing mRNA decay of the low-density lipoprotein (LDL) receptor
CC (LDLR) mRNA in response to phorbol 12-myristate 13-acetate (PMA)
CC treatment in a p38 MAPK-dependent manner (PubMed:25106868). Positively
CC regulates early adipogenesis by promoting ARE-mediated mRNA decay of
CC immediate early genes (IEGs). Plays a role in mature peripheral neuron
CC integrity by promoting ARE-containing mRNA decay of the transcriptional
CC repressor REST mRNA. Plays a role in ovulation and oocyte meiotic
CC maturation by promoting ARE-mediated mRNA decay of the luteinizing
CC hormone receptor LHCGR mRNA. Acts as a negative regulator of erythroid
CC cell differentiation: promotes glucocorticoid-induced self-renewal of
CC erythroid cells by binding mRNAs that are induced or highly expressed
CC during terminal erythroid differentiation and promotes their
CC degradation, preventing erythroid cell differentiation. In association
CC with ZFP36L1 maintains quiescence on developing B lymphocytes by
CC promoting ARE-mediated decay of several mRNAs encoding cell cycle
CC regulators that help B cells progress through the cell cycle, and hence
CC ensuring accurate variable-diversity-joining (VDJ) recombination
CC process and functional immune cell formation. Together with ZFP36L1 is
CC also necessary for thymocyte development and prevention of T-cell acute
CC lymphoblastic leukemia (T-ALL) transformation by promoting ARE-mediated
CC mRNA decay of the oncogenic transcription factor NOTCH1 mRNA.
CC {ECO:0000250|UniProtKB:P23949, ECO:0000269|PubMed:14981510,
CC ECO:0000269|PubMed:20506496, ECO:0000269|PubMed:25106868}.
CC -!- SUBUNIT: Associates with the cytoplasmic CCR4-NOT deadenylase to
CC trigger ARE-containing mRNA deadenylation and decay processes
CC (PubMed:25106868). Interacts with CNOT7; this interaction is inhibited
CC in response to phorbol 12-myristate 13-acetate (PMA) treatment in a p38
CC MAPK-dependent manner (PubMed:25106868). {ECO:0000269|PubMed:25106868}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P23949}. Cytoplasm
CC {ECO:0000250|UniProtKB:P23949}. Note=Shuttles between the nucleus and
CC the cytoplasm in a XPO1/CRM1-dependent manner.
CC {ECO:0000250|UniProtKB:P23949}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in the basal epidermal layer,
CC weakly in the suprabasal epidermal layers (PubMed:27182009). Expressed
CC in epidermal keratinocytes (at protein level) (PubMed:27182009).
CC {ECO:0000269|PubMed:27182009}.
CC -!- INDUCTION: Up-regulated by butyrate in colorectal cancer cells
CC (PubMed:10367403). Up-regulated in keratinocytes after wounding
CC (PubMed:20166898, PubMed:27182009). Up-regulated strongly by
CC granulocyte macrophage colony-stimulating factor (GM-CSF) in
CC keratinocytes (PubMed:20166898). Up-regulated moderately by
CC transforming growth factor (TGF-beta), epidermal growth factor (EGF),
CC tumor necrosis factor (TNF-alpha) and fibroblast growth factor (FGF1)
CC in keratinocytes (PubMed:20166898). Up-regulated also by glucocorticoid
CC dexamethasone in keratinocytes (PubMed:20166898).
CC {ECO:0000269|PubMed:10367403, ECO:0000269|PubMed:20166898,
CC ECO:0000269|PubMed:27182009}.
CC -!- PTM: Phosphorylated by RPS6KA1 at Ser-490 and Ser-492 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 (PubMed:25106868). Phosphorylation occurs during early
CC preadipocyte differentiation (By similarity).
CC {ECO:0000250|UniProtKB:P23949, ECO:0000269|PubMed:25106868}.
CC -!- DISEASE: Note=Defects in ZFP36L2 may be a cause of leukemias.
CC Frameshift mutations disrupting ZFP36L2 have been found in a patient
CC with acute myeloid leukemia (PubMed:21109922).
CC {ECO:0000269|PubMed:21109922}.
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DR EMBL; U07802; AAA91778.1; -; Genomic_DNA.
DR EMBL; X78992; CAA55592.1; -; mRNA.
DR EMBL; AC010883; AAY14992.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00306.1; -; Genomic_DNA.
DR EMBL; BC005010; AAH05010.1; -; mRNA.
DR CCDS; CCDS1811.1; -.
DR PIR; S49147; S49147.
DR RefSeq; NP_008818.3; NM_006887.4.
DR PDB; 1RGO; NMR; -; A=151-220.
DR PDBsum; 1RGO; -.
DR AlphaFoldDB; P47974; -.
DR SMR; P47974; -.
DR BioGRID; 107145; 207.
DR CORUM; P47974; -.
DR IntAct; P47974; 13.
DR STRING; 9606.ENSP00000282388; -.
DR GlyGen; P47974; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P47974; -.
DR PhosphoSitePlus; P47974; -.
DR BioMuta; ZFP36L2; -.
DR DMDM; 146291085; -.
DR EPD; P47974; -.
DR jPOST; P47974; -.
DR MassIVE; P47974; -.
DR MaxQB; P47974; -.
DR PaxDb; P47974; -.
DR PeptideAtlas; P47974; -.
DR PRIDE; P47974; -.
DR ProteomicsDB; 55827; -.
DR Antibodypedia; 14846; 248 antibodies from 31 providers.
DR DNASU; 678; -.
DR Ensembl; ENST00000282388.4; ENSP00000282388.3; ENSG00000152518.8.
DR GeneID; 678; -.
DR KEGG; hsa:678; -.
DR MANE-Select; ENST00000282388.4; ENSP00000282388.3; NM_006887.5; NP_008818.3.
DR UCSC; uc002rsv.5; human.
DR CTD; 678; -.
DR DisGeNET; 678; -.
DR GeneCards; ZFP36L2; -.
DR HGNC; HGNC:1108; ZFP36L2.
DR HPA; ENSG00000152518; Low tissue specificity.
DR MIM; 612053; gene.
DR neXtProt; NX_P47974; -.
DR OpenTargets; ENSG00000152518; -.
DR PharmGKB; PA35028; -.
DR VEuPathDB; HostDB:ENSG00000152518; -.
DR eggNOG; KOG1677; Eukaryota.
DR GeneTree; ENSGT00940000161584; -.
DR HOGENOM; CLU_033040_1_0_1; -.
DR InParanoid; P47974; -.
DR OMA; GYGQREV; -.
DR OrthoDB; 1541140at2759; -.
DR PhylomeDB; P47974; -.
DR TreeFam; TF315463; -.
DR PathwayCommons; P47974; -.
DR SignaLink; P47974; -.
DR BioGRID-ORCS; 678; 70 hits in 1088 CRISPR screens.
DR ChiTaRS; ZFP36L2; human.
DR EvolutionaryTrace; P47974; -.
DR GenomeRNAi; 678; -.
DR Pharos; P47974; Tbio.
DR PRO; PR:P47974; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P47974; protein.
DR Bgee; ENSG00000152518; Expressed in upper leg skin and 211 other tissues.
DR Genevisible; P47974; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS: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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IMP:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA: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; IDA:UniProtKB.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR GO; GO:0060216; P:definitive hemopoiesis; ISS:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; ISS:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0045577; P:regulation of B cell differentiation; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
DR GO; GO:0048103; P:somatic stem cell division; ISS:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
DR IDEAL; IID00150; -.
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 3D-structure; Cytoplasm; Developmental protein; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Zinc; Zinc-finger.
FT CHAIN 1..494
FT /note="mRNA decay activator protein ZFP36L2"
FT /id="PRO_0000089170"
FT ZN_FING 153..181
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 191..219
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 93..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..211
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:14981510,
FT ECO:0000269|PubMed:20506496"
FT REGION 257..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 153..158
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:14981510,
FT ECO:0000269|PubMed:20506496"
FT COMPBIAS 405..431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 490
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000269|PubMed:25106868"
FT MOD_RES 492
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000269|PubMed:25106868"
FT MUTAGEN 157
FT /note="E->R: Impaired mRNA-binding; when associated with K-
FT 195."
FT /evidence="ECO:0000269|PubMed:20506496"
FT MUTAGEN 195
FT /note="E->K: Impaired mRNA-binding; when associated with R-
FT 157."
FT /evidence="ECO:0000269|PubMed:20506496"
FT CONFLICT 96..97
FT /note="TS -> DL (in Ref. 1; AAA91778)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="A -> T (in Ref. 2; CAA55592)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..332
FT /note="AAAA -> LR (in Ref. 2; CAA55592)"
FT /evidence="ECO:0000305"
FT CONFLICT 331..332
FT /note="Missing (in Ref. 1; AAA91778)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="Q -> QQQQ (in Ref. 5; AAH05010)"
FT /evidence="ECO:0000305"
FT CONFLICT 453..462
FT /note="Missing (in Ref. 1; AAA91778)"
FT /evidence="ECO:0000305"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:1RGO"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1RGO"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:1RGO"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1RGO"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:1RGO"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1RGO"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:1RGO"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:1RGO"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1RGO"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1RGO"
SQ 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
