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Cytoplasmic polyadenylation element-binding protein 3 (CPE-BP3) (CPE-binding protein 3) (hCPEB-3)

 CPEB3_HUMAN             Reviewed;         698 AA.
Q8NE35; Q5T389; Q9NQJ7; Q9Y2E9;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
22-NOV-2017, entry version 127.
RecName: Full=Cytoplasmic polyadenylation element-binding protein 3;
Short=CPE-BP3;
Short=CPE-binding protein 3;
Short=hCPEB-3;
Name=CPEB3; Synonyms=KIAA0940;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
TRP-324.
TISSUE=Testis;
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).
[4]
RIBOZYME-ENCODING INTRON.
PubMed=16990549; DOI=10.1126/science.1129308;
Salehi-Ashtiani K., Luptak A., Litovchick A., Szostak J.W.;
"A genomewide search for ribozymes reveals an HDV-like sequence in the
human CPEB3 gene.";
Science 313:1788-1792(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, 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).
[6]
ROLE OF RIBOZYME POLYMORPHISM IN MEMORY.
PubMed=19503753; DOI=10.3389/neuro.08.004.2009;
Vogler C., Spalek K., Aerni A., Demougin P., Mueller A., Huynh K.D.,
Papassotiropoulos A., de Quervain D.J.;
"CPEB3 is associated with human episodic memory.";
Front. Behav. Neurosci. 3:4-4(2009).
[7]
FUNCTION, INTERACTION WITH STAT5B, AND SUBCELLULAR LOCATION.
PubMed=20639532; DOI=10.1093/nar/gkq634;
Peng S.C., Lai Y.T., Huang H.Y., Huang H.D., Huang Y.S.;
"A novel role of CPEB3 in regulating EGFR gene transcription via
association with Stat5b in neurons.";
Nucleic Acids Res. 38:7446-7457(2010).
[8]
FUNCTION, AND INTERACTION WITH TOB1.
PubMed=21336257; DOI=10.1038/emboj.2011.37;
Hosoda N., Funakoshi Y., Hirasawa M., Yamagishi R., Asano Y.,
Miyagawa R., Ogami K., Tsujimoto M., Hoshino S.;
"Anti-proliferative protein Tob negatively regulates CPEB3 target by
recruiting Caf1 deadenylase.";
EMBO J. 30:1311-1323(2011).
[9]
INTERACTION WITH IPO5 AND XPO1, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF LEU-349 AND LEU-353.
PubMed=22730302; DOI=10.1093/nar/gks598;
Chao H.W., Lai Y.T., Lu Y.L., Lin C.L., Mai W., Huang Y.S.;
"NMDAR signaling facilitates the IPO5-mediated nuclear import of
CPEB3.";
Nucleic Acids Res. 40:8484-8498(2012).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[11]
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).
[12]
SITES IMPORTANT FOR BINDING RNA, AND MUTAGENESIS OF ARG-441; PHE-444;
GLY-446; ARG-463; ASP-470; LYS-474; SER-479; PHE-488 AND ARG-528.
PubMed=24343026; DOI=10.1093/nar/gkt1299;
Chen Y.C., Sargsyan K., Wright J.D., Huang Y.S., Lim C.;
"Identifying RNA-binding residues based on evolutionary conserved
structural and energetic features.";
Nucleic Acids Res. 42:E15-E15(2014).
[13]
FUNCTION.
PubMed=26398195; DOI=10.1371/journal.pone.0138794;
Giangarra V., Igea A., Castellazzi C.L., Bava F.A., Mendez R.;
"Global analysis of CPEBs reveals sequential and non-redundant
functions in mitotic cell cycle.";
PLoS ONE 10:E0138794-E0138794(2015).
[14]
STRUCTURE BY NMR OF 440-540.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RNA binding domain in cytoplasmic
polyadenylation element binding protein 3.";
Submitted (OCT-2006) to the PDB data bank.
[15]
STRUCTURE BY NMR OF 440-540.
PubMed=25066254; DOI=10.1002/prot.24651;
Tsuda K., Kuwasako K., Nagata T., Takahashi M., Kigawa T.,
Kobayashi N., Guentert P., Shirouzu M., Yokoyama S., Muto Y.;
"Novel RNA recognition motif domain in the cytoplasmic polyadenylation
element binding protein 3.";
Proteins 82:2879-2886(2014).
-!- FUNCTION: Sequence-specific RNA-binding protein which acts as a
translational repressor in the basal unstimulated state but,
following neuronal stimulation, acts as a translational activator
(By similarity). In contrast to CPEB1, does not bind to the
cytoplasmic polyadenylation element (CPE), a uridine-rich sequence
element within the mRNA 3'-UTR, but binds to a U-rich loop within
a stem-loop structure (By similarity). Required for the
consolidation and maintenance of hippocampal-based long term
memory (By similarity). In the basal state, binds to the mRNA 3'-
UTR of the glutamate receptors GRIA2/GLUR2 mRNA and negatively
regulates their translation (By similarity). Also represses the
translation of DLG4, GRIN1, GRIN2A and GRIN2B (By similarity).
When activated, acts as a translational activator of GRIA1 and
GRIA2 (By similarity). In the basal state, suppresses SUMO2
translation but activates it following neuronal stimulation (By
similarity). Binds to the 3'-UTR of TRPV1 mRNA and represses TRPV1
translation which is required to maintain normal thermoception (By
similarity). Binds actin mRNA, leading to actin translational
repression in the basal state and to translational activation
following neuronal stimulation (By similarity). Negatively
regulates target mRNA levels by binding to TOB1 which recruits
CNOT7/CAF1 to a ternary complex and this leads to target mRNA
deadenylation and decay (PubMed:21336257). In addition to its role
in translation, binds to and inhibits the transcriptional
activation activity of STAT5B without affecting its dimerization
or DNA-binding activity. This, in turn, represses transcription of
the STAT5B target gene EGFR which has been shown to play a role in
enhancing learning and memory performance (PubMed:20639532). In
contrast to CPEB1, CPEB2 and CPEB4, not required for cell cycle
progression (PubMed:26398195). {ECO:0000250|UniProtKB:Q7TN99,
ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:21336257,
ECO:0000269|PubMed:26398195}.
-!- SUBUNIT: Following synaptic activity, forms amyloid-like oligomers
(By similarity). Aggregation requires an intact actin cytoskeleton
(By similarity). Interacts with STAT5B; this inhibits STAT5B-
mediated transcriptional activation (PubMed:20639532). Interacts
with E3 ubiquitin-protein ligase NEURL1; this leads to
monoubiquitination and activation of CPEB3 (By similarity).
Interacts with CAPN2; this leads to cleavage of CPEB3 (By
similarity). Interacts (via C-terminal RNA-binding region) with
TOB1; TOB1 also binds CNOT7/CAF1 and recruits it to CPEB3 to form
a ternary complex (PubMed:21336257). Interacts with SUMO-
conjugating enzyme UBC9 (By similarity). Interacts with IPO5; the
interaction is enhanced in a RAN-regulated manner following
neuronal stimulation and mediates CPEB3 nuclear import
(PubMed:22730302). Interacts with exportin XPO1/CRM1
(PubMed:22730302). {ECO:0000250|UniProtKB:Q7TN99,
ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:21336257,
ECO:0000269|PubMed:22730302}.
-!- INTERACTION:
P50616:TOB1; NbExp=7; IntAct=EBI-8596191, EBI-723281;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20639532,
ECO:0000269|PubMed:22730302}. Nucleus
{ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:22730302}. Cell
junction, synapse {ECO:0000250|UniProtKB:Q7TN99}. Cell projection,
dendrite {ECO:0000250|UniProtKB:Q7TN99}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000250|UniProtKB:Q7TN99}. Note=Predominantly cytoplasmic in
unstimulated neurons but translocates to the nucleus following
neuronal stimulation (PubMed:20639532, PubMed:22730302). Nuclear
import is mediated by importin IPO5 (By similarity).
{ECO:0000250|UniProtKB:Q7TN99, ECO:0000269|PubMed:20639532,
ECO:0000269|PubMed:22730302}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8NE35-1; Sequence=Displayed;
Name=2;
IsoId=Q8NE35-2; Sequence=VSP_022034, VSP_022035;
-!- DOMAIN: The N-terminal Gln-rich region is required for the
formation of amyloid-like oligomers and for the stability of long-
term potentiation and spatial memory.
{ECO:0000250|UniProtKB:Q7TN99}.
-!- PTM: Activated by NEURL1-mediated monoubiquitination, resulting in
the growth of new dendritic spines and increased levels of GRIA1
and GRIA2. NEURL1-mediated monoubiquitination facilitates synaptic
plasticity and hippocampal-dependent memory storage.
{ECO:0000250|UniProtKB:Q7TN99}.
-!- PTM: Under basal unstimulated conditions when CPEB3 is mainly
unaggregated, sumoylated and acts as a translational repressor.
Following neuronal stimulation, becomes desumoylated and
aggregated which is required for the translation of mRNA targets
and for dendritic filopodia formation.
{ECO:0000250|UniProtKB:Q7TN99}.
-!- PTM: Following neuronal stimulation, cleaved by CAPN2 which
abolishes its translational repressor activity, leading to
translation of CPEB3 target mRNAs. {ECO:0000250|UniProtKB:Q7TN99}.
-!- PTM: Phosphorylation is enhanced by neuronal stimulation.
{ECO:0000250|UniProtKB:Q7TN99}.
-!- MISCELLANEOUS: The CPEB3 gene contains an intron-encoded self-
cleaving ribozyme which is structurally and biochemically related
to human hepatitis delta virus ribozymes and which may play a role
in the regulation of CPEB3 translation (PubMed:16990549). A
polymorphism in the ribozyme sequence which influences cleavage
activity of the ribozyme may play a role in episodic memory with
carriers of a rare C allele-containing ribozyme showing
significantly poorer memory recall performance than T allele
carriers (PubMed:19503753). {ECO:0000269|PubMed:16990549,
ECO:0000269|PubMed:19503753}.
-!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA76784.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Tenacious memory
- Issue 185 of November 2016;
URL="https://web.expasy.org/spotlight/back_issues/185/";
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EMBL; AB023157; BAA76784.2; ALT_INIT; mRNA.
EMBL; AL158040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL365398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC036444; AAH36444.1; -; mRNA.
CCDS; CCDS31246.1; -. [Q8NE35-1]
CCDS; CCDS53553.1; -. [Q8NE35-2]
RefSeq; NP_001171608.1; NM_001178137.1. [Q8NE35-2]
RefSeq; NP_055727.3; NM_014912.4. [Q8NE35-1]
RefSeq; XP_005269687.1; XM_005269630.4. [Q8NE35-2]
UniGene; Hs.131683; -.
UniGene; Hs.701732; -.
PDB; 2DNL; NMR; -; A=440-540.
PDB; 2RUG; NMR; -; A=440-540.
PDBsum; 2DNL; -.
PDBsum; 2RUG; -.
ProteinModelPortal; Q8NE35; -.
SMR; Q8NE35; -.
BioGrid; 116521; 3.
IntAct; Q8NE35; 7.
STRING; 9606.ENSP00000265997; -.
iPTMnet; Q8NE35; -.
PhosphoSitePlus; Q8NE35; -.
BioMuta; CPEB3; -.
DMDM; 119368633; -.
MaxQB; Q8NE35; -.
PaxDb; Q8NE35; -.
PeptideAtlas; Q8NE35; -.
PRIDE; Q8NE35; -.
DNASU; 22849; -.
Ensembl; ENST00000265997; ENSP00000265997; ENSG00000107864. [Q8NE35-1]
Ensembl; ENST00000412050; ENSP00000398310; ENSG00000107864. [Q8NE35-2]
Ensembl; ENST00000614585; ENSP00000482128; ENSG00000107864. [Q8NE35-1]
GeneID; 22849; -.
KEGG; hsa:22849; -.
UCSC; uc001khv.3; human. [Q8NE35-1]
CTD; 22849; -.
DisGeNET; 22849; -.
EuPathDB; HostDB:ENSG00000107864.14; -.
GeneCards; CPEB3; -.
HGNC; HGNC:21746; CPEB3.
MIM; 610606; gene.
neXtProt; NX_Q8NE35; -.
OpenTargets; ENSG00000107864; -.
PharmGKB; PA134903478; -.
eggNOG; KOG0129; Eukaryota.
eggNOG; ENOG410Y1XZ; LUCA.
GeneTree; ENSGT00390000012886; -.
HOGENOM; HOG000290660; -.
HOVERGEN; HBG058010; -.
InParanoid; Q8NE35; -.
KO; K02602; -.
OMA; GHQPIMT; -.
OrthoDB; EOG091G0AO9; -.
PhylomeDB; Q8NE35; -.
TreeFam; TF317658; -.
ChiTaRS; CPEB3; human.
EvolutionaryTrace; Q8NE35; -.
GenomeRNAi; 22849; -.
PRO; PR:Q8NE35; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107864; -.
CleanEx; HS_CPEB3; -.
ExpressionAtlas; Q8NE35; baseline and differential.
Genevisible; Q8NE35; HS.
GO; GO:0097440; C:apical dendrite; ISS:UniProtKB.
GO; GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
GO; GO:0008135; F:translation factor activity, RNA binding; IDA:UniProtKB.
GO; GO:0000900; F:translation repressor activity, nucleic acid binding; ISS:UniProtKB.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; IBA:GO_Central.
GO; GO:1900248; P:negative regulation of cytoplasmic translational elongation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:UniProtKB.
GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS:UniProtKB.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:UniProtKB.
GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
InterPro; IPR032296; CEBP_ZZ.
InterPro; IPR034819; CPEB.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR12566; PTHR12566; 1.
Pfam; PF16366; CEBP_ZZ; 1.
Pfam; PF16367; RRM_7; 1.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Amyloid; Cell junction;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Membrane; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Reference proteome; Repeat; Repressor;
RNA-binding; Synapse; Translation regulation; Ubl conjugation.
CHAIN 1 698 Cytoplasmic polyadenylation element-
binding protein 3.
/FTId=PRO_0000269261.
DOMAIN 441 532 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 549 631 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 13 27 Gln-rich.
COMPBIAS 26 200 Pro-rich.
COMPBIAS 170 238 Ala-rich.
SITE 441 442 Cleavage; by CAPN2.
{ECO:0000250|UniProtKB:Q7TN99}.
SITE 444 444 Required for RNA-binding activity.
{ECO:0000269|PubMed:24343026}.
SITE 488 488 Required for RNA-binding activity.
{ECO:0000269|PubMed:24343026}.
MOD_RES 192 192 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TN99}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TN99}.
MOD_RES 308 308 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q7TN99}.
VAR_SEQ 366 388 Missing (in isoform 2).
{ECO:0000303|PubMed:10231032}.
/FTId=VSP_022034.
VAR_SEQ 408 408 N -> SRSSLFPFED (in isoform 2).
{ECO:0000303|PubMed:10231032}.
/FTId=VSP_022035.
VARIANT 324 324 R -> W (in dbSNP:rs17853616).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_029776.
MUTAGEN 349 349 L->A: Abolishes nuclear export; when
associated with A-353.
{ECO:0000269|PubMed:22730302}.
MUTAGEN 353 353 L->A: Abolishes nuclear export; when
associated with A-349.
{ECO:0000269|PubMed:22730302}.
MUTAGEN 441 441 R->A: Does not impair RNA binding.
{ECO:0000269|PubMed:24343026}.
MUTAGEN 444 444 F->A,N: Abolishes RNA binding.
{ECO:0000269|PubMed:24343026}.
MUTAGEN 444 444 F->Y: Does not impair RNA binding.
{ECO:0000269|PubMed:24343026}.
MUTAGEN 446 446 G->A: Does not impair RNA binding.
{ECO:0000269|PubMed:24343026}.
MUTAGEN 463 463 R->A: Does not impair RNA binding.
{ECO:0000269|PubMed:24343026}.
MUTAGEN 470 470 D->A: Does not impair RNA binding.
{ECO:0000269|PubMed:24343026}.
MUTAGEN 474 474 K->A: Does not impair RNA binding.
{ECO:0000269|PubMed:24343026}.
MUTAGEN 479 479 S->A: Does not impair RNA binding.
{ECO:0000269|PubMed:24343026}.
MUTAGEN 488 488 F->A: Reduced RNA binding.
{ECO:0000269|PubMed:24343026}.
MUTAGEN 488 488 F->Y: Does not impair RNA binding.
{ECO:0000269|PubMed:24343026}.
MUTAGEN 528 528 R->A: Does not impair RNA binding.
{ECO:0000269|PubMed:24343026}.
CONFLICT 519 519 Missing (in Ref. 3; AAH36444).
{ECO:0000305}.
STRAND 443 446 {ECO:0000244|PDB:2DNL}.
HELIX 454 460 {ECO:0000244|PDB:2DNL}.
TURN 461 464 {ECO:0000244|PDB:2DNL}.
STRAND 467 470 {ECO:0000244|PDB:2RUG}.
STRAND 474 477 {ECO:0000244|PDB:2DNL}.
STRAND 478 481 {ECO:0000244|PDB:2RUG}.
STRAND 485 489 {ECO:0000244|PDB:2DNL}.
HELIX 494 503 {ECO:0000244|PDB:2DNL}.
STRAND 504 507 {ECO:0000244|PDB:2DNL}.
STRAND 510 515 {ECO:0000244|PDB:2DNL}.
STRAND 518 520 {ECO:0000244|PDB:2DNL}.
STRAND 522 528 {ECO:0000244|PDB:2DNL}.
SEQUENCE 698 AA; 76014 MW; 0E67DCB7F8A40C96 CRC64;
MQDDLLMDKS KTQPQPQQQQ RQQQQPQPES SVSEAPSTPL SSETPKPEEN SAVPALSPAA
APPAPNGPDK MQMESPLLPG LSFHQPPQQP PPPQEPAAPG ASLSPSFGST WSTGTTNAVE
DSFFQGITPV NGTMLFQNFP HHVNPVFGGT FSPQIGLAQT QHHQQPPPPA PAPQPAQPAQ
PPQAQPPQQR RSPASPSQAP YAQRSAAAAY GHQPIMTSKP SSSSAVAAAA AAAAASSASS
SWNTHQSVNA AWSAPSNPWG GLQAGRDPRR AVGVGVGVGV GVPSPLNPIS PLKKPFSSNV
IAPPKFPRAA PLTSKSWMED NAFRTDNGNN LLPFQDRSRP YDTFNLHSLE NSLMDMIRTD
HEPLKGKHYP PSGPPMSFAD IMWRNHFAGR MGINFHHPGT DNIMALNNAF LDDSHGDQAL
SSGLSSPTRC QNGERVERYS RKVFVGGLPP DIDEDEITAS FRRFGPLVVD WPHKAESKSY
FPPKGYAFLL FQEESSVQAL IDACLEEDGK LYLCVSSPTI KDKPVQIRPW NLSDSDFVMD
GSQPLDPRKT IFVGGVPRPL RAVELAMIMD RLYGGVCYAG IDTDPELKYP KGAGRVAFSN
QQSYIAAISA RFVQLQHNDI DKRVEVKPYV LDDQMCDECQ GTRCGGKFAP FFCANVTCLQ
YYCEYCWASI HSRAGREFHK PLVKEGGDRP RHVPFRWS


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