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Eukaryotic translation initiation factor 4E type 2 (eIF-4E type 2) (eIF4E type 2) (Eukaryotic translation initiation factor 4E homologous protein) (Eukaryotic translation initiation factor 4E-like 3) (eIF4E-like protein 4E-LP) (mRNA cap-binding protein 4EHP) (h4EHP) (mRNA cap-binding protein type 3)

 IF4E2_HUMAN             Reviewed;         245 AA.
O60573; B8ZZJ9; O75349;
11-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
25-OCT-2017, entry version 156.
RecName: Full=Eukaryotic translation initiation factor 4E type 2;
Short=eIF-4E type 2;
Short=eIF4E type 2;
AltName: Full=Eukaryotic translation initiation factor 4E homologous protein;
AltName: Full=Eukaryotic translation initiation factor 4E-like 3;
AltName: Full=eIF4E-like protein 4E-LP;
AltName: Full=mRNA cap-binding protein 4EHP;
Short=h4EHP {ECO:0000303|PubMed:17368478};
AltName: Full=mRNA cap-binding protein type 3;
Name=EIF4E2; Synonyms=EIF4EL3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, 3D-STRUCTURE
MODELING, AND MUTAGENESIS.
TISSUE=Follicular cell;
PubMed=9582349; DOI=10.1074/jbc.273.21.13104;
Rom E., Kim H.C., Gingras A.-C., Marcotrigiano J., Favre D., Olsen H.,
Burley S.K., Sonenberg N.;
"Cloning and characterization of 4EHP, a novel mammalian eIF4E-related
cap-binding protein.";
J. Biol. Chem. 273:13104-13109(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH EIF4EBP1;
EIF4EBP2 AND EIF4EBP3.
TISSUE=Mammary gland;
PubMed=15153109; DOI=10.1111/j.1432-1033.2004.04149.x;
Joshi B., Cameron A., Jagus R.;
"Characterization of mammalian eIF4E-family members.";
Eur. J. Biochem. 271:2189-2203(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
Wang Y.-X., Chen S.-J., Chen Z.;
"Identification of genes expressed in human CD34(+) hematopoietic
stem/progenitor cells by expressed sequence tags and efficient full-
length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
[4]
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).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle, Urinary bladder, and Uterus;
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).
[7]
UBIQUITINATION BY ARIH1.
PubMed=14623119; DOI=10.1016/S0014-5793(03)01235-3;
Tan N.G., Ardley H.C., Scott G.B., Rose S.A., Markham A.F.,
Robinson P.A.;
"Human homologue of ariadne promotes the ubiquitylation of translation
initiation factor 4E homologous protein, 4EHP.";
FEBS Lett. 554:501-504(2003).
[8]
ISGYLATION AT LYS-134 AND LYS-222.
PubMed=17289916; DOI=10.1101/gad.1521607;
Okumura F., Zou W., Zhang D.E.;
"ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-
binding activity of 4EHP.";
Genes Dev. 21:255-260(2007).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-134, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
FUNCTION, AND IDENTIFICATION IN THE 4EHP-GYF2 COMPLEX.
PubMed=22751931; DOI=10.1128/MCB.00455-12;
Morita M., Ler L.W., Fabian M.R., Siddiqui N., Mullin M.,
Henderson V.C., Alain T., Fonseca B.D., Karashchuk G., Bennett C.F.,
Kabuta T., Higashi S., Larsson O., Topisirovic I., Smith R.J.,
Gingras A.C., Sonenberg N.;
"A novel 4EHP-GIGYF2 translational repressor complex is essential for
mammalian development.";
Mol. Cell. Biol. 32:3585-3593(2012).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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]
FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF LYS-121; LYS-130; LYS-134
AND LYS-222.
PubMed=25624349; DOI=10.1128/MCB.01152-14;
von Stechow L., Typas D., Carreras Puigvert J., Oort L., Siddappa R.,
Pines A., Vrieling H., van de Water B., Mullenders L.H., Danen E.H.;
"The E3 ubiquitin ligase ARIH1 protects against genotoxic stress by
initiating a 4EHP-mediated mRNA translation arrest.";
Mol. Cell. Biol. 35:1254-1268(2015).
[15]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 45-234 IN COMPLEX WITH MRNA
CAP ANALOGS AND EIF4EBP1, INTERACTION WITH EIF4EBP1, AND FUNCTION.
PubMed=17368478; DOI=10.1016/j.jmb.2007.02.019;
Rosettani P., Knapp S., Vismara M.-G., Rusconi L., Cameron A.D.;
"Structures of the human eIF4E homologous protein, h4EHP, in its
m7GTP-bound and unliganded forms.";
J. Mol. Biol. 368:691-705(2007).
-!- FUNCTION: Recognizes and binds the 7-methylguanosine-containing
mRNA cap during an early step in the initiation (PubMed:9582349,
PubMed:17368478, PubMed:25624349). Acts as a repressor of
translation initiation (PubMed:22751931). In contrast to EIF4E, it
is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting
that it acts by competing with EIF4E and block assembly of eIF4F
at the cap (By similarity). {ECO:0000250|UniProtKB:Q8BMB3,
ECO:0000269|PubMed:17368478, ECO:0000269|PubMed:22751931,
ECO:0000269|PubMed:25624349, ECO:0000269|PubMed:9582349}.
-!- SUBUNIT: Interacts with EIF4EBP1, EIF4EBP2 and EIF4EBP3
(PubMed:15153109, PubMed:17368478). Does not interact with eIF4G
(EIF4G1, EIF4G2 or EIF4G3) (By similarity). Component of the 4EHP-
GYF2 complex, at least composed of EIF4E2, GIGYF2 and ZNF598
(PubMed:22751931). Interacts with GIGYF2 (via the 4EHP-binding
motif); the interaction is direct (PubMed:22751931).
{ECO:0000250|UniProtKB:Q8BMB3, ECO:0000269|PubMed:15153109,
ECO:0000269|PubMed:17368478, ECO:0000269|PubMed:22751931}.
-!- INTERACTION:
Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-398610, EBI-10173507;
Q08117:AES; NbExp=3; IntAct=EBI-398610, EBI-717810;
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-398610, EBI-10187270;
Q9H257:CARD9; NbExp=3; IntAct=EBI-398610, EBI-751319;
Q01850:CDR2; NbExp=3; IntAct=EBI-398610, EBI-1181367;
Q9NRA8:EIF4ENIF1; NbExp=3; IntAct=EBI-398610, EBI-301024;
Q99814:EPAS1; NbExp=2; IntAct=EBI-398610, EBI-447470;
Q8IX15-3:HOMEZ; NbExp=3; IntAct=EBI-398610, EBI-10172004;
A1A4E9:KRT13; NbExp=3; IntAct=EBI-398610, EBI-10171552;
P08727:KRT19; NbExp=3; IntAct=EBI-398610, EBI-742756;
Q15323:KRT31; NbExp=3; IntAct=EBI-398610, EBI-948001;
Q6A162:KRT40; NbExp=3; IntAct=EBI-398610, EBI-10171697;
P60370:KRTAP10-5; NbExp=3; IntAct=EBI-398610, EBI-10172150;
P60410:KRTAP10-8; NbExp=3; IntAct=EBI-398610, EBI-10171774;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-398610, EBI-10172052;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-398610, EBI-741037;
Q9Y5V3:MAGED1; NbExp=3; IntAct=EBI-398610, EBI-716006;
Q9UPY8:MAPRE3; NbExp=3; IntAct=EBI-398610, EBI-726739;
Q8TD10:MIPOL1; NbExp=3; IntAct=EBI-398610, EBI-2548751;
P15173:MYOG; NbExp=3; IntAct=EBI-398610, EBI-3906629;
Q7Z6G3-2:NECAB2; NbExp=3; IntAct=EBI-398610, EBI-10172876;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-398610, EBI-945833;
Q9GZV8:PRDM14; NbExp=3; IntAct=EBI-398610, EBI-3957793;
Q04864:REL; NbExp=3; IntAct=EBI-398610, EBI-307352;
Q96R06:SPAG5; NbExp=3; IntAct=EBI-398610, EBI-413317;
Q8NA61:SPERT; NbExp=3; IntAct=EBI-398610, EBI-741724;
O43597:SPRY2; NbExp=3; IntAct=EBI-398610, EBI-742487;
O75478:TADA2A; NbExp=3; IntAct=EBI-398610, EBI-742268;
P15884:TCF4; NbExp=3; IntAct=EBI-398610, EBI-533224;
O75069-4:TMCC2; NbExp=3; IntAct=EBI-398610, EBI-10177480;
P14373:TRIM27; NbExp=3; IntAct=EBI-398610, EBI-719493;
Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-398610, EBI-2130429;
Q5T124:UBXN11; NbExp=3; IntAct=EBI-398610, EBI-746004;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-398610, EBI-739895;
Q70EL1:USP54; NbExp=3; IntAct=EBI-398610, EBI-946185;
Q96C00:ZBTB9; NbExp=3; IntAct=EBI-398610, EBI-395708;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O60573-1; Sequence=Displayed;
Name=2;
IsoId=O60573-2; Sequence=VSP_054783, VSP_054784;
Note=No experimental confirmation available.;
-!- PTM: Ubiquitinated by ARIH1 (PubMed:14623119, PubMed:25624349).
The consequences of ubiquitination are however unclear: according
to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-
binding and protein translation arrest (PubMed:25624349).
According to another report ubiquitination leads to its subsequent
degradation (PubMed:14623119). {ECO:0000269|PubMed:14623119,
ECO:0000269|PubMed:25624349}.
-!- PTM: ISGylation enhances its cap structure-binding activity and
translation-inhibition activity. {ECO:0000269|PubMed:17289916}.
-!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
{ECO:0000305}.
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EMBL; AF047695; AAC18565.1; -; mRNA.
EMBL; AF068117; AAC19374.1; -; mRNA.
EMBL; AF038957; AAC39871.1; -; mRNA.
EMBL; AC073254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471063; EAW71008.1; -; Genomic_DNA.
EMBL; BC005392; AAH05392.1; -; mRNA.
EMBL; BC005874; AAH05874.1; -; mRNA.
EMBL; BC021226; AAH21226.1; -; mRNA.
EMBL; BC021690; AAH21690.1; -; mRNA.
CCDS; CCDS2496.1; -. [O60573-1]
CCDS; CCDS63159.1; -. [O60573-2]
RefSeq; NP_001263265.1; NM_001276336.1. [O60573-2]
RefSeq; NP_004837.1; NM_004846.3. [O60573-1]
UniGene; Hs.292026; -.
PDB; 2JGB; X-ray; 1.70 A; A=45-234.
PDB; 2JGC; X-ray; 2.40 A; A=45-234.
PDB; 5NVK; X-ray; 2.90 A; A/C/E/G=52-234.
PDB; 5NVL; X-ray; 2.30 A; A/C=52-234.
PDB; 5NVM; X-ray; 2.00 A; A/C=52-234.
PDB; 5NVN; X-ray; 1.90 A; A/C=52-234.
PDBsum; 2JGB; -.
PDBsum; 2JGC; -.
PDBsum; 5NVK; -.
PDBsum; 5NVL; -.
PDBsum; 5NVM; -.
PDBsum; 5NVN; -.
ProteinModelPortal; O60573; -.
SMR; O60573; -.
BioGrid; 114856; 145.
DIP; DIP-32578N; -.
IntAct; O60573; 53.
MINT; MINT-1440115; -.
STRING; 9606.ENSP00000258416; -.
iPTMnet; O60573; -.
PhosphoSitePlus; O60573; -.
EPD; O60573; -.
PaxDb; O60573; -.
PeptideAtlas; O60573; -.
PRIDE; O60573; -.
Ensembl; ENST00000258416; ENSP00000258416; ENSG00000135930. [O60573-1]
Ensembl; ENST00000409098; ENSP00000386996; ENSG00000135930. [O60573-2]
GeneID; 9470; -.
KEGG; hsa:9470; -.
UCSC; uc002vtb.3; human. [O60573-1]
CTD; 9470; -.
DisGeNET; 9470; -.
EuPathDB; HostDB:ENSG00000135930.13; -.
GeneCards; EIF4E2; -.
HGNC; HGNC:3293; EIF4E2.
HPA; HPA019253; -.
MIM; 605895; gene.
neXtProt; NX_O60573; -.
OpenTargets; ENSG00000135930; -.
PharmGKB; PA27720; -.
eggNOG; KOG1669; Eukaryota.
eggNOG; COG5053; LUCA.
GeneTree; ENSGT00520000055549; -.
HOGENOM; HOG000186751; -.
HOVERGEN; HBG107087; -.
InParanoid; O60573; -.
KO; K03259; -.
OMA; WEDPLNI; -.
OrthoDB; EOG091G0IEX; -.
PhylomeDB; O60573; -.
TreeFam; TF101529; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
ChiTaRS; EIF4E2; human.
EvolutionaryTrace; O60573; -.
GeneWiki; EIF4E2; -.
GenomeRNAi; 9470; -.
PRO; PR:O60573; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000135930; -.
CleanEx; HS_EIF4E2; -.
ExpressionAtlas; O60573; baseline and differential.
Genevisible; O60573; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000339; F:RNA cap binding; TAS:ProtInc.
GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc.
GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0017148; P:negative regulation of translation; IMP:MGI.
Gene3D; 3.30.760.10; -; 1.
InterPro; IPR023398; TIF_eIF4e-like.
InterPro; IPR001040; TIF_eIF_4E.
InterPro; IPR019770; TIF_eIF_4E_CS.
PANTHER; PTHR11960; PTHR11960; 1.
Pfam; PF01652; IF4E; 1.
SUPFAM; SSF55418; SSF55418; 1.
PROSITE; PS00813; IF4E; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Initiation factor; Isopeptide bond; Phosphoprotein;
Protein biosynthesis; Reference proteome; RNA-binding;
Translation regulation; Ubl conjugation.
CHAIN 1 245 Eukaryotic translation initiation factor
4E type 2.
/FTId=PRO_0000193664.
REGION 54 57 EIF4EBP1/2/3 binding.
REGION 78 79 7-methylguanosine-containing mRNA cap
binding. {ECO:0000250}.
REGION 95 99 EIF4EBP1/2/3 binding.
REGION 124 125 7-methylguanosine-containing mRNA cap
binding.
REGION 150 157 EIF4EBP1/2/3 binding.
REGION 174 179 7-methylguanosine-containing mRNA cap
binding.
REGION 222 224 7-methylguanosine-containing mRNA cap
binding. {ECO:0000250}.
BINDING 110 110 7-methylguanosine-containing mRNA cap.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 134 134 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 134 134 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15);
alternate. {ECO:0000269|PubMed:17289916}.
CROSSLNK 222 222 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
{ECO:0000269|PubMed:17289916}.
VAR_SEQ 223 234 MPGRLGPQRLLF -> DNSSFRNTKITL (in isoform
2). {ECO:0000305}.
/FTId=VSP_054783.
VAR_SEQ 235 245 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_054784.
MUTAGEN 63 63 W->A: Unable to bind capped mRNA.
{ECO:0000269|PubMed:9582349}.
MUTAGEN 95 95 W->A: Ability to bind capped mRNA reduced
to 40% of wild-type.
{ECO:0000269|PubMed:9582349}.
MUTAGEN 121 121 K->R: Does not affect ubiquitination by
ARIH1; when associated with R-130; R-134
and R-222. {ECO:0000269|PubMed:25624349}.
MUTAGEN 124 126 WED->FAA: Unable to bind capped mRNA.
{ECO:0000269|PubMed:9582349}.
MUTAGEN 124 124 W->A: Ability to bind capped mRNA reduced
to less than 10% of wild-type.
{ECO:0000269|PubMed:9582349}.
MUTAGEN 124 124 W->F: Ability to bind capped mRNA reduced
to 13% of wild-type.
{ECO:0000269|PubMed:9582349}.
MUTAGEN 125 125 E->A: Ability to bind capped mRNA reduced
to less than 10% of wild-type.
{ECO:0000269|PubMed:9582349}.
MUTAGEN 126 126 D->A: Slight reduction in ability to bind
capped mRNA.
{ECO:0000269|PubMed:9582349}.
MUTAGEN 130 130 K->R: Does not affect ubiquitination by
ARIH1; when associated with R-121; R-134
and R-222. {ECO:0000269|PubMed:25624349}.
MUTAGEN 134 134 K->R: Does not affect ubiquitination by
ARIH1; when associated with R-121; R-130
and R-222. {ECO:0000269|PubMed:25624349}.
MUTAGEN 135 135 W->A: Unable to bind capped mRNA.
{ECO:0000269|PubMed:9582349}.
MUTAGEN 148 148 W->A: Unable to bind capped mRNA.
{ECO:0000269|PubMed:9582349}.
MUTAGEN 183 183 W->A: Ability to bind capped mRNA reduced
to less than 10% of wild-type.
{ECO:0000269|PubMed:9582349}.
MUTAGEN 183 183 W->F: Unable to bind capped mRNA.
{ECO:0000269|PubMed:9582349}.
MUTAGEN 222 222 K->R: Does not affect ubiquitination by
ARIH1; when associated with R-121; R-130
and R-134. {ECO:0000269|PubMed:25624349}.
CONFLICT 1 27 MNNKFDALKDDDSGDHDQNEENSTQKD -> MMTVGTMIRM
KKTAHRKI (in Ref. 3; AAC39871).
{ECO:0000305}.
STRAND 55 67 {ECO:0000244|PDB:2JGB}.
HELIX 75 81 {ECO:0000244|PDB:2JGB}.
STRAND 82 90 {ECO:0000244|PDB:2JGB}.
HELIX 91 98 {ECO:0000244|PDB:2JGB}.
HELIX 104 106 {ECO:0000244|PDB:2JGB}.
STRAND 109 117 {ECO:0000244|PDB:2JGB}.
TURN 127 131 {ECO:0000244|PDB:2JGB}.
STRAND 133 139 {ECO:0000244|PDB:2JGB}.
HELIX 144 156 {ECO:0000244|PDB:2JGB}.
STRAND 166 173 {ECO:0000244|PDB:2JGB}.
STRAND 178 185 {ECO:0000244|PDB:2JGB}.
HELIX 190 203 {ECO:0000244|PDB:2JGB}.
STRAND 212 216 {ECO:0000244|PDB:2JGB}.
HELIX 217 222 {ECO:0000244|PDB:2JGB}.
SEQUENCE 245 AA; 28362 MW; 3D3075BFA48B3C12 CRC64;
MNNKFDALKD DDSGDHDQNE ENSTQKDGEK EKTERDKNQS SSKRKAVVPG PAEHPLQYNY
TFWYSRRTPG RPTSSQSYEQ NIKQIGTFAS VEQFWRFYSH MVRPGDLTGH SDFHLFKEGI
KPMWEDDANK NGGKWIIRLR KGLASRCWEN LILAMLGEQF MVGEEICGAV VSVRFQEDII
SIWNKTASDQ ATTARIRDTL RRVLNLPPNT IMEYKTHTDS IKMPGRLGPQ RLLFQNLWKP
RLNVP


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