LN28A_MOUSE
ID LN28A_MOUSE Reviewed; 209 AA.
AC Q8K3Y3; Q6NV62;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein lin-28 homolog A;
DE Short=Lin-28A;
DE AltName: Full=Testis-expressed protein 17;
GN Name=Lin28a; Synonyms=Lin28, Tex17;
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12798299; DOI=10.1016/s0012-1606(03)00126-x;
RA Moss E.G., Tang L.;
RT "Conservation of the heterochronic regulator Lin-28, its developmental
RT expression and microRNA complementary sites.";
RL Dev. Biol. 258:432-442(2003).
RN [2]
RP ERRATUM OF PUBMED:12798299.
RA Moss E.G., Tang L.;
RL Dev. Biol. 262:361-361(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 TISSUE SPECIFICITY.
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14643679; DOI=10.1016/s1567-133x(03)00140-6;
RA Yang D.-H., Moss E.G.;
RT "Temporally regulated expression of Lin-28 in diverse tissues of the
RT developing mouse.";
RL Gene Expr. Patterns 3:719-726(2003).
RN [6]
RP INDUCTION.
RX PubMed=15003116; DOI=10.1186/gb-2004-5-3-r13;
RA Sempere L.F., Freemantle S., Pitha-Rowe I., Moss E.G., Dmitrovsky E.,
RA Ambros V.;
RT "Expression profiling of mammalian microRNAs uncovers a subset of brain-
RT expressed microRNAs with possible roles in murine and human neuronal
RT differentiation.";
RL Genome Biol. 5:R13.1-R13.11(2004).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15722555; DOI=10.1074/jbc.m412247200;
RA Lee Y.S., Kim H.K., Chung S., Kim K.-S., Dutta A.;
RT "Depletion of human micro-RNA miR-125b reveals that it is critical for the
RT proliferation of differentiated cells but not for the down-regulation of
RT putative targets during differentiation.";
RL J. Biol. Chem. 280:16635-16641(2005).
RN [8]
RP INDUCTION.
RX PubMed=16227573; DOI=10.1128/mcb.25.21.9198-9208.2005;
RA Wu L., Belasco J.G.;
RT "Micro-RNA regulation of the mammalian lin-28 gene during neuronal
RT differentiation of embryonal carcinoma cells.";
RL Mol. Cell. Biol. 25:9198-9208(2005).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH
RP EIF3S2, AND MUTAGENESIS OF GLY-42; 44-CYS--PHE-47; MET-81; ARG-85; GLY-119;
RP PRO-124; 138-ARG-CYS-139 AND CYS-142.
RX PubMed=17473174; DOI=10.1101/gad.415007;
RA Polesskaya A., Cuvellier S., Naguibneva I., Duquet A., Moss E.G.,
RA Harel-Bellan A.;
RT "Lin-28 binds IGF-2 mRNA and participates in skeletal myogenesis by
RT increasing translation efficiency.";
RL Genes Dev. 21:1125-1138(2007).
RN [10]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=18604195; DOI=10.1038/ncb1759;
RA Rybak A., Fuchs H., Smirnova L., Brandt C., Pohl E.E., Nitsch R.,
RA Wulczyn F.G.;
RT "A feedback loop comprising lin-28 and let-7 controls pre-let-7 maturation
RT during neural stem-cell commitment.";
RL Nat. Cell Biol. 10:987-993(2008).
RN [11]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=18566191; DOI=10.1261/rna.1155108;
RA Newman M.A., Thomson J.M., Hammond S.M.;
RT "Lin-28 interaction with the Let-7 precursor loop mediates regulated
RT microRNA processing.";
RL RNA 14:1539-1549(2008).
RN [12]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=18292307; DOI=10.1126/science.1154040;
RA Viswanathan S.R., Daley G.Q., Gregory R.I.;
RT "Selective blockade of microRNA processing by Lin28.";
RL Science 320:97-100(2008).
RN [13]
RP FUNCTION IN MAINTENANCE OF EMBRYONIC STEM CELL PLURIPOTENCY.
RX PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
RA Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H., Han J.,
RA Kim V.N.;
RT "TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through pre-
RT microRNA uridylation.";
RL Cell 138:696-708(2009).
RN [14]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=23102813; DOI=10.1016/j.cell.2012.10.019;
RA Cho J., Chang H., Kwon S.C., Kim B., Kim Y., Choe J., Ha M., Kim Y.K.,
RA Kim V.N.;
RT "LIN28A is a suppressor of ER-associated translation in embryonic stem
RT cells.";
RL Cell 151:765-777(2012).
RN [15]
RP FUNCTION.
RX PubMed=24209617; DOI=10.1016/j.cell.2013.09.059;
RA Shyh-Chang N., Zhu H., Yvanka de Soysa T., Shinoda G., Seligson M.T.,
RA Tsanov K.M., Nguyen L., Asara J.M., Cantley L.C., Daley G.Q.;
RT "Lin28 enhances tissue repair by reprogramming cellular metabolism.";
RL Cell 155:778-792(2013).
RN [16]
RP FUNCTION.
RX PubMed=26045559; DOI=10.1074/jbc.m115.665521;
RA O'Day E., Le M.T., Imai S., Tan S.M., Kirchner R., Arthanari H.,
RA Hofmann O., Wagner G., Lieberman J.;
RT "An RNA-binding Protein, Lin28, Recognizes and Remodels G-quartets in the
RT MicroRNAs (miRNAs) and mRNAs It Regulates.";
RL J. Biol. Chem. 290:17909-17922(2015).
RN [17]
RP FUNCTION, INTERACTION WITH TUT4, RNA-BINDING, DOMAIN, AND MUTAGENESIS OF
RP 139-CYS--CYS-142 AND 161-CYS--CYS-164.
RX PubMed=28671666; DOI=10.1038/nsmb.3428;
RA Faehnle C.R., Walleshauser J., Joshua-Tor L.;
RT "Multi-domain utilization by TUT4 and TUT7 in control of let-7
RT biogenesis.";
RL Nat. Struct. Mol. Biol. 24:658-665(2017).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 31-187 IN COMPLEX WITH LET-7 RNA
RP PRECURSORS, DOMAINS, AND SUBUNIT.
RX PubMed=22078496; DOI=10.1016/j.cell.2011.10.020;
RA Nam Y., Chen C., Gregory R.I., Chou J.J., Sliz P.;
RT "Molecular basis for interaction of let-7 microRNAs with Lin28.";
RL Cell 147:1080-1091(2011).
CC -!- FUNCTION: RNA-binding protein that inhibits processing of pre-let-7
CC miRNAs and regulates translation of mRNAs that control developmental
CC timing, pluripotency and metabolism (PubMed:17473174, PubMed:18604195,
CC PubMed:18566191, PubMed:18292307, PubMed:19703396, PubMed:23102813,
CC PubMed:24209617). Seems to recognize a common structural G-quartet (G4)
CC feature in its miRNA and mRNA targets (PubMed:26045559). 'Translational
CC enhancer' that drives specific mRNAs to polysomes and increases the
CC efficiency of protein synthesis. Its association with the translational
CC machinery and target mRNAs results in an increased number of initiation
CC events per molecule of mRNA and, indirectly, in mRNA stabilization.
CC Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its
CC own mRNA. Essential for skeletal muscle differentiation program through
CC the translational up-regulation of IGF2 expression (PubMed:17473174).
CC Suppressor of microRNA (miRNA) biogenesis, including that of let-7,
CC miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors
CC (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA
CC terminal loop, and recruits TUT4 and TUT7 uridylyltransferaseS. This
CC results in the terminal uridylation of target pre-miRNAs. Uridylated
CC pre-miRNAs fail to be processed by Dicer and undergo degradation. The
CC repression of let-7 expression is required for normal development and
CC contributes to maintain the pluripotent state by preventing let-7-
CC mediated differentiation of embryonic stem cells (PubMed:19703396,
CC PubMed:28671666). Localized to the periendoplasmic reticulum area,
CC binds to a large number of spliced mRNAs and inhibits the translation
CC of mRNAs destined for the ER, reducing the synthesis of transmembrane
CC proteins, ER or Golgi lumen proteins, and secretory proteins
CC (PubMed:23102813). Binds to and enhances the translation of mRNAs for
CC several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing
CC glycolysis and oxidative phosphorylation. Which, with the let-7
CC repression may enhance tissue repair in adult tissue (PubMed:24209617).
CC {ECO:0000269|PubMed:17473174, ECO:0000269|PubMed:18292307,
CC ECO:0000269|PubMed:18566191, ECO:0000269|PubMed:18604195,
CC ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:23102813,
CC ECO:0000269|PubMed:24209617, ECO:0000269|PubMed:26045559,
CC ECO:0000269|PubMed:28671666}.
CC -!- SUBUNIT: Monomer (PubMed:22078496). During skeletal muscle
CC differentiation, associated with translation initiation complexes in
CC the polysomal compartment (By similarity). Directly interacts with
CC EIF3S2 (PubMed:17473174). Interacts with NCL in an RNA-dependent manner
CC (By similarity). Interacts with TUT4 in the presence of pre-let-7 RNA
CC (PubMed:28671666). {ECO:0000250, ECO:0000250|UniProtKB:Q9H9Z2,
CC ECO:0000269|PubMed:17473174, ECO:0000269|PubMed:22078496,
CC ECO:0000269|PubMed:28671666}.
CC -!- INTERACTION:
CC Q8K3Y3; Q8CI75: Dis3l2; NbExp=2; IntAct=EBI-11109197, EBI-16045218;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12798299,
CC ECO:0000269|PubMed:17473174}. Rough endoplasmic reticulum
CC {ECO:0000269|PubMed:23102813}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:Q9H9Z2}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:17473174}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:17473174}. Note=Predominantly cytoplasmic
CC (PubMed:12798299). In the cytoplasm, localizes to peri-endoplasmic
CC reticulum regions and detected in the microsomal fraction derived from
CC rough endoplasmic reticulum (RER) following subcellular fractionation.
CC May be bound to the cytosolic surface of RER on which ER-associated
CC mRNAs are translated (PubMed:23102813). Shuttle from the nucleus to the
CC cytoplasm requires RNA-binding (PubMed:17473174). Nucleolar
CC localization observed in 10-15% of the nuclei in differentiated
CC myotubes (PubMed:17473174). {ECO:0000269|PubMed:12798299,
CC ECO:0000269|PubMed:17473174, ECO:0000269|PubMed:23102813}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic stem cells (ES cells),
CC spermatagonia and testis. Expressed in numerous epithelial tissues
CC including the epithelia of the small intestine, the intralobular duct
CC epithelium of the mammary gland and the epithelia of Henle's loop in
CC the kidney and in the collecting duct (at protein level). Also
CC expressed in the myocardium and skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:12798299,
CC ECO:0000269|PubMed:14643679, ECO:0000269|PubMed:15722555}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed throughout the whole embryo at
CC 6.5 dpc, including the embryonic and extraembryonic ectoderm and
CC endoderm (at protein level). Subsequently expressed in the ectoderm,
CC endoderm and mesoderm at 7.5 dpc (at protein level). At 9.5 dpc,
CC expressed in epithelia covering the first branchial arch and the
CC coelomic cavity, the myocardium of the developing heart, the
CC neuroepithelium and some extraembryonic tissues such as the visceral
CC yolk sac (at protein level). Expression persists in a variety of
CC epithelial tissues at 10.5 dpc. At 15.5 dpc, expression is lost in
CC bronchial epithelium and becomes weaker in neuroepithelium, while
CC increasing in the myotome of somites, the foregut epithelium,
CC stratified epithelium and some kidney tubules (at protein level). At
CC 17.5 dpc, expression persists in the myocardium and in the epithelium
CC covering the body surface and skeletal muscles (at protein level).
CC Expression is reduced during differentiation of ES cells. In adult
CC primary myoblasts, barely detectable during proliferation, but
CC dramatically up-regulated during terminal differentiation. Induced as
CC early as 24 hours after differentiation signal and remains high as late
CC as 7 days of differentiation. Little expression in resting muscle, but
CC strongly up-regulated during regeneration of skeletal muscle fibers.
CC Expression decreases when regeneration is histologically and
CC functionally complete. {ECO:0000269|PubMed:12798299,
CC ECO:0000269|PubMed:14643679, ECO:0000269|PubMed:15722555,
CC ECO:0000269|PubMed:17473174}.
CC -!- INDUCTION: Negatively regulated by the microRNA miR-125b in response to
CC retinoic acid. {ECO:0000269|PubMed:15003116,
CC ECO:0000269|PubMed:16227573}.
CC -!- DOMAIN: The CSD domain is required for function in muscle
CC differentiation. {ECO:0000269|PubMed:22078496}.
CC -!- DOMAIN: The CCHC zinc fingers interact with the GGAG motif at the 3'
CC end of let-7 miRNAs precursors, more generally they bind the 5'-NGNNG-
CC 3' consensus motif with micromolar affinity. The CSD domain recognizes
CC the loop at the 5' end. The flexible linker allows accommodating
CC variable sequences and lengths among let-7 family members.
CC {ECO:0000269|PubMed:22078496, ECO:0000269|PubMed:28671666}.
CC -!- MISCELLANEOUS: Reactivation of LIN28A expression enhances tissue repair
CC in some adult tissues by reprogramming cellular bioenergetics. Improves
CC hair regrowth by promoting anagen in hair follicle and accelerates
CC regrowth of cartilage, bone and mesenchyme after ear and digit
CC injuries. {ECO:0000269|PubMed:24209617}.
CC -!- SIMILARITY: Belongs to the lin-28 family. {ECO:0000305}.
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DR EMBL; AF521097; AAM77749.1; -; mRNA.
DR EMBL; BC068304; AAH68304.1; -; mRNA.
DR CCDS; CCDS18761.1; -.
DR RefSeq; NP_665832.1; NM_145833.1.
DR PDB; 3TRZ; X-ray; 2.90 A; A/B/C/D/E/F=31-187.
DR PDB; 3TS0; X-ray; 2.76 A; A/B=33-187.
DR PDB; 3TS2; X-ray; 2.01 A; A/B=31-187.
DR PDBsum; 3TRZ; -.
DR PDBsum; 3TS0; -.
DR PDBsum; 3TS2; -.
DR AlphaFoldDB; Q8K3Y3; -.
DR SMR; Q8K3Y3; -.
DR BioGRID; 219943; 10.
DR DIP; DIP-48573N; -.
DR IntAct; Q8K3Y3; 17.
DR STRING; 10090.ENSMUSP00000050488; -.
DR BindingDB; Q8K3Y3; -.
DR ChEMBL; CHEMBL4295897; -.
DR iPTMnet; Q8K3Y3; -.
DR PhosphoSitePlus; Q8K3Y3; -.
DR MaxQB; Q8K3Y3; -.
DR PaxDb; Q8K3Y3; -.
DR PeptideAtlas; Q8K3Y3; -.
DR PRIDE; Q8K3Y3; -.
DR ProteomicsDB; 292109; -.
DR Antibodypedia; 30634; 736 antibodies from 43 providers.
DR DNASU; 83557; -.
DR Ensembl; ENSMUST00000051674; ENSMUSP00000050488; ENSMUSG00000050966.
DR GeneID; 83557; -.
DR KEGG; mmu:83557; -.
DR UCSC; uc008vdw.1; mouse.
DR CTD; 79727; -.
DR MGI; MGI:1890546; Lin28a.
DR VEuPathDB; HostDB:ENSMUSG00000050966; -.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00940000153295; -.
DR HOGENOM; CLU_089169_4_0_1; -.
DR InParanoid; Q8K3Y3; -.
DR OMA; ANCPVKT; -.
DR OrthoDB; 1604809at2759; -.
DR PhylomeDB; Q8K3Y3; -.
DR TreeFam; TF316240; -.
DR BioGRID-ORCS; 83557; 1 hit in 75 CRISPR screens.
DR PRO; PR:Q8K3Y3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8K3Y3; protein.
DR Bgee; ENSMUSG00000050966; Expressed in primitive streak and 75 other tissues.
DR ExpressionAtlas; Q8K3Y3; baseline and differential.
DR Genevisible; Q8K3Y3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0002151; F:G-quadruplex RNA binding; IDA:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:1905538; F:polysome binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IDA:UniProtKB.
DR GO; GO:0031369; F:translation initiation factor binding; IPI:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IMP:BHF-UCL.
DR GO; GO:0007281; P:germ cell development; IMP:MGI.
DR GO; GO:0010587; P:miRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; IDA:MGI.
DR GO; GO:0045686; P:negative regulation of glial cell differentiation; IDA:MGI.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:1901724; P:positive regulation of cell proliferation involved in kidney development; IMP:BHF-UCL.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:1903800; P:positive regulation of miRNA maturation; IDA:BHF-UCL.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IDA:BHF-UCL.
DR GO; GO:0045727; P:positive regulation of translation; IDA:MGI.
DR GO; GO:0031054; P:pre-miRNA processing; IDA:MGI.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; IGI:MGI.
DR GO; GO:0071076; P:RNA 3' uridylation; IDA:CACAO.
DR GO; GO:0031123; P:RNA 3'-end processing; ISO:MGI.
DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; ISO:MGI.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00313; CSD; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR PRINTS; PR00050; COLDSHOCK.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS51857; CSD_2; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Endoplasmic reticulum; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW RNA-mediated gene silencing; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Z2"
FT CHAIN 2..209
FT /note="Protein lin-28 homolog A"
FT /id="PRO_0000253788"
FT DOMAIN 39..112
FT /note="CSD"
FT ZN_FING 137..154
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 159..176
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..136
FT /note="Flexible linker"
FT REGION 177..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Z2"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Z2"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Z2"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Z2"
FT MUTAGEN 42
FT /note="G->S: Erroneous subcellular location. No positive
FT effect on terminal myogenic differentiation."
FT /evidence="ECO:0000269|PubMed:17473174"
FT MUTAGEN 44..47
FT /note="Missing: Erroneous subcellular location. No positive
FT effect on terminal myogenic differentiation."
FT /evidence="ECO:0000269|PubMed:17473174"
FT MUTAGEN 81
FT /note="M->I: Erroneous subcellular location; when
FT associated with Q-85. No positive effect on terminal
FT myogenic differentiation; when associated with Q-85."
FT /evidence="ECO:0000269|PubMed:17473174"
FT MUTAGEN 85
FT /note="R->Q: Erroneous subcellular location; when
FT associated with I-81. No positive effect on terminal
FT myogenic differentiation; when associated with I-81."
FT /evidence="ECO:0000269|PubMed:17473174"
FT MUTAGEN 119
FT /note="G->R: Erroneous subcellular location; when
FT associated with S-124. No positive effect on terminal
FT myogenic differentiation; when associated with S-124."
FT /evidence="ECO:0000269|PubMed:17473174"
FT MUTAGEN 124
FT /note="P->S: Erroneous subcellular location; when
FT associated with R-119. No positive effect on terminal
FT myogenic differentiation; when associated with R-119."
FT /evidence="ECO:0000269|PubMed:17473174"
FT MUTAGEN 138..139
FT /note="Missing: No effect on subcellular location; when
FT associated with S-142. Normal terminal myogenic
FT differentiation; when associated with S-142."
FT /evidence="ECO:0000269|PubMed:17473174"
FT MUTAGEN 139..142
FT /note="CYNC->AYNA: Disrupts 5'-GGAG-3' motif interaction.
FT Disrupts oligoU-addition to pre-miRNA pre-let-7 by TUT4."
FT /evidence="ECO:0000269|PubMed:28671666"
FT MUTAGEN 142
FT /note="C->S: No effect on subcellular location; when
FT associated with 44-C--F-47. Normal terminal myogenic
FT differentiation; when associated with 44-C--F-47."
FT /evidence="ECO:0000269|PubMed:17473174"
FT MUTAGEN 161..164
FT /note="CHFC->AHFA: Disrupts 5'-GGAG-3' motif interaction.
FT Binds miRNA but not TUT4."
FT /evidence="ECO:0000269|PubMed:28671666"
FT CONFLICT 194
FT /note="E -> D (in Ref. 3; AAH68304)"
FT /evidence="ECO:0000305"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:3TS2"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:3TS2"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:3TS2"
FT STRAND 64..75
FT /evidence="ECO:0007829|PDB:3TS2"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3TS2"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:3TS2"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:3TS2"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:3TS2"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3TS2"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3TS0"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:3TS2"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3TS2"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:3TS2"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3TS2"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:3TS2"
SQ SEQUENCE 209 AA; 22720 MW; 4BD14DCAF13CD659 CRC64;
MGSVSNQQFA GGCAKAAEKA PEEAPPDAAR AADEPQLLHG AGICKWFNVR MGFGFLSMTA
RAGVALDPPV DVFVHQSKLH MEGFRSLKEG EAVEFTFKKS AKGLESIRVT GPGGVFCIGS
ERRPKGKNMQ KRRSKGDRCY NCGGLDHHAK ECKLPPQPKK CHFCQSINHM VASCPLKAQQ
GPSSQGKPAY FREEEEEIHS PALLPEAQN
