CPEB3_HUMAN
ID CPEB3_HUMAN Reviewed; 698 AA.
AC Q8NE35; Q5T389; Q9NQJ7; Q9Y2E9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 3;
DE Short=CPE-BP3;
DE Short=CPE-binding protein 3;
DE Short=hCPEB-3;
GN Name=CPEB3; Synonyms=KIAA0940;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TRP-324.
RC TISSUE=Testis;
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 RIBOZYME-ENCODING INTRON.
RX PubMed=16990549; DOI=10.1126/science.1129308;
RA Salehi-Ashtiani K., Luptak A., Litovchick A., Szostak J.W.;
RT "A genomewide search for ribozymes reveals an HDV-like sequence in the
RT human CPEB3 gene.";
RL Science 313:1788-1792(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, 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 [6]
RP ROLE OF RIBOZYME POLYMORPHISM IN MEMORY.
RX PubMed=19503753; DOI=10.3389/neuro.08.004.2009;
RA Vogler C., Spalek K., Aerni A., Demougin P., Mueller A., Huynh K.D.,
RA Papassotiropoulos A., de Quervain D.J.;
RT "CPEB3 is associated with human episodic memory.";
RL Front. Behav. Neurosci. 3:4-4(2009).
RN [7]
RP FUNCTION, INTERACTION WITH STAT5B, AND SUBCELLULAR LOCATION.
RX PubMed=20639532; DOI=10.1093/nar/gkq634;
RA Peng S.C., Lai Y.T., Huang H.Y., Huang H.D., Huang Y.S.;
RT "A novel role of CPEB3 in regulating EGFR gene transcription via
RT association with Stat5b in neurons.";
RL Nucleic Acids Res. 38:7446-7457(2010).
RN [8]
RP FUNCTION, AND INTERACTION WITH TOB1.
RX PubMed=21336257; DOI=10.1038/emboj.2011.37;
RA Hosoda N., Funakoshi Y., Hirasawa M., Yamagishi R., Asano Y., Miyagawa R.,
RA Ogami K., Tsujimoto M., Hoshino S.;
RT "Anti-proliferative protein Tob negatively regulates CPEB3 target by
RT recruiting Caf1 deadenylase.";
RL EMBO J. 30:1311-1323(2011).
RN [9]
RP INTERACTION WITH IPO5 AND XPO1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LEU-349 AND LEU-353.
RX PubMed=22730302; DOI=10.1093/nar/gks598;
RA Chao H.W., Lai Y.T., Lu Y.L., Lin C.L., Mai W., Huang Y.S.;
RT "NMDAR signaling facilitates the IPO5-mediated nuclear import of CPEB3.";
RL Nucleic Acids Res. 40:8484-8498(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
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 [12]
RP SITES IMPORTANT FOR BINDING RNA, AND MUTAGENESIS OF ARG-441; PHE-444;
RP GLY-446; ARG-463; ASP-470; LYS-474; SER-479; PHE-488 AND ARG-528.
RX PubMed=24343026; DOI=10.1093/nar/gkt1299;
RA Chen Y.C., Sargsyan K., Wright J.D., Huang Y.S., Lim C.;
RT "Identifying RNA-binding residues based on evolutionary conserved
RT structural and energetic features.";
RL Nucleic Acids Res. 42:E15-E15(2014).
RN [13]
RP FUNCTION.
RX PubMed=26398195; DOI=10.1371/journal.pone.0138794;
RA Giangarra V., Igea A., Castellazzi C.L., Bava F.A., Mendez R.;
RT "Global analysis of CPEBs reveals sequential and non-redundant functions in
RT mitotic cell cycle.";
RL PLoS ONE 10:E0138794-E0138794(2015).
RN [14]
RP STRUCTURE BY NMR OF 440-540.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in cytoplasmic polyadenylation
RT element binding protein 3.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [15]
RP STRUCTURE BY NMR OF 440-540.
RX PubMed=25066254; DOI=10.1002/prot.24651;
RA Tsuda K., Kuwasako K., Nagata T., Takahashi M., Kigawa T., Kobayashi N.,
RA Guentert P., Shirouzu M., Yokoyama S., Muto Y.;
RT "Novel RNA recognition motif domain in the cytoplasmic polyadenylation
RT element binding protein 3.";
RL Proteins 82:2879-2886(2014).
CC -!- FUNCTION: Sequence-specific RNA-binding protein which acts as a
CC translational repressor in the basal unstimulated state but, following
CC neuronal stimulation, acts as a translational activator (By
CC similarity). In contrast to CPEB1, does not bind to the cytoplasmic
CC polyadenylation element (CPE), a uridine-rich sequence element within
CC the mRNA 3'-UTR, but binds to a U-rich loop within a stem-loop
CC structure (By similarity). Required for the consolidation and
CC maintenance of hippocampal-based long term memory (By similarity). In
CC the basal state, binds to the mRNA 3'-UTR of the glutamate receptors
CC GRIA2/GLUR2 mRNA and negatively regulates their translation (By
CC similarity). Also represses the translation of DLG4, GRIN1, GRIN2A and
CC GRIN2B (By similarity). When activated, acts as a translational
CC activator of GRIA1 and GRIA2 (By similarity). In the basal state,
CC suppresses SUMO2 translation but activates it following neuronal
CC stimulation (By similarity). Binds to the 3'-UTR of TRPV1 mRNA and
CC represses TRPV1 translation which is required to maintain normal
CC thermoception (By similarity). Binds actin mRNA, leading to actin
CC translational repression in the basal state and to translational
CC activation following neuronal stimulation (By similarity). Negatively
CC regulates target mRNA levels by binding to TOB1 which recruits
CC CNOT7/CAF1 to a ternary complex and this leads to target mRNA
CC deadenylation and decay (PubMed:21336257). In addition to its role in
CC translation, binds to and inhibits the transcriptional activation
CC activity of STAT5B without affecting its dimerization or DNA-binding
CC activity. This, in turn, represses transcription of the STAT5B target
CC gene EGFR which has been shown to play a role in enhancing learning and
CC memory performance (PubMed:20639532). In contrast to CPEB1, CPEB2 and
CC CPEB4, not required for cell cycle progression (PubMed:26398195).
CC {ECO:0000250|UniProtKB:Q7TN99, ECO:0000269|PubMed:20639532,
CC ECO:0000269|PubMed:21336257, ECO:0000269|PubMed:26398195}.
CC -!- SUBUNIT: Following synaptic activity, forms amyloid-like oligomers (By
CC similarity). Aggregation requires an intact actin cytoskeleton (By
CC similarity). Interacts with STAT5B; this inhibits STAT5B-mediated
CC transcriptional activation (PubMed:20639532). Interacts with E3
CC ubiquitin-protein ligase NEURL1; this leads to monoubiquitination and
CC activation of CPEB3 (By similarity). Interacts with CAPN2; this leads
CC to cleavage of CPEB3 (By similarity). Interacts (via C-terminal RNA-
CC binding region) with TOB1; TOB1 also binds CNOT7/CAF1 and recruits it
CC to CPEB3 to form a ternary complex (PubMed:21336257). Interacts with
CC SUMO-conjugating enzyme UBC9 (By similarity). Interacts with IPO5; the
CC interaction is enhanced in a RAN-regulated manner following neuronal
CC stimulation and mediates CPEB3 nuclear import (PubMed:22730302).
CC Interacts with exportin XPO1/CRM1 (PubMed:22730302).
CC {ECO:0000250|UniProtKB:Q7TN99, ECO:0000269|PubMed:20639532,
CC ECO:0000269|PubMed:21336257, ECO:0000269|PubMed:22730302}.
CC -!- INTERACTION:
CC Q8NE35; P50616: TOB1; NbExp=7; IntAct=EBI-8596191, EBI-723281;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20639532,
CC ECO:0000269|PubMed:22730302}. Nucleus {ECO:0000269|PubMed:20639532,
CC ECO:0000269|PubMed:22730302}. Synapse {ECO:0000250|UniProtKB:Q7TN99}.
CC Cell projection, dendrite {ECO:0000250|UniProtKB:Q7TN99}. Postsynaptic
CC density {ECO:0000250|UniProtKB:Q7TN99}. Note=Predominantly cytoplasmic
CC in unstimulated neurons but translocates to the nucleus following
CC neuronal stimulation (PubMed:20639532, PubMed:22730302). Nuclear import
CC is mediated by importin IPO5 (By similarity).
CC {ECO:0000250|UniProtKB:Q7TN99, ECO:0000269|PubMed:20639532,
CC ECO:0000269|PubMed:22730302}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NE35-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NE35-2; Sequence=VSP_022034, VSP_022035;
CC -!- DOMAIN: The N-terminal Gln-rich region is required for the formation of
CC amyloid-like oligomers and for the stability of long-term potentiation
CC and spatial memory. {ECO:0000250|UniProtKB:Q7TN99}.
CC -!- PTM: Activated by NEURL1-mediated monoubiquitination, resulting in the
CC growth of new dendritic spines and increased levels of GRIA1 and GRIA2.
CC NEURL1-mediated monoubiquitination facilitates synaptic plasticity and
CC hippocampal-dependent memory storage. {ECO:0000250|UniProtKB:Q7TN99}.
CC -!- PTM: Under basal unstimulated conditions when CPEB3 is mainly
CC unaggregated, sumoylated and acts as a translational repressor.
CC Following neuronal stimulation, becomes desumoylated and aggregated
CC which is required for the translation of mRNA targets and for dendritic
CC filopodia formation. {ECO:0000250|UniProtKB:Q7TN99}.
CC -!- PTM: Following neuronal stimulation, cleaved by CAPN2 which abolishes
CC its translational repressor activity, leading to translation of CPEB3
CC target mRNAs. {ECO:0000250|UniProtKB:Q7TN99}.
CC -!- PTM: Phosphorylation is enhanced by neuronal stimulation.
CC {ECO:0000250|UniProtKB:Q7TN99}.
CC -!- MISCELLANEOUS: The CPEB3 gene contains an intron-encoded self-cleaving
CC ribozyme which is structurally and biochemically related to human
CC hepatitis delta virus ribozymes and which may play a role in the
CC regulation of CPEB3 translation (PubMed:16990549). A polymorphism in
CC the ribozyme sequence which influences cleavage activity of the
CC ribozyme may play a role in episodic memory with carriers of a rare C
CC allele-containing ribozyme showing significantly poorer memory recall
CC performance than T allele carriers (PubMed:19503753).
CC {ECO:0000269|PubMed:16990549, ECO:0000269|PubMed:19503753}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76784.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Tenacious memory - Issue 185
CC of November 2016;
CC URL="https://web.expasy.org/spotlight/back_issues/185/";
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DR EMBL; AB023157; BAA76784.2; ALT_INIT; mRNA.
DR EMBL; AL158040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036444; AAH36444.1; -; mRNA.
DR CCDS; CCDS31246.1; -. [Q8NE35-1]
DR CCDS; CCDS53553.1; -. [Q8NE35-2]
DR RefSeq; NP_001171608.1; NM_001178137.1. [Q8NE35-2]
DR RefSeq; NP_055727.3; NM_014912.4. [Q8NE35-1]
DR RefSeq; XP_005269687.1; XM_005269630.4. [Q8NE35-2]
DR PDB; 2DNL; NMR; -; A=440-540.
DR PDB; 2RUG; NMR; -; A=440-540.
DR PDBsum; 2DNL; -.
DR PDBsum; 2RUG; -.
DR AlphaFoldDB; Q8NE35; -.
DR SMR; Q8NE35; -.
DR BioGRID; 116521; 6.
DR IntAct; Q8NE35; 9.
DR MINT; Q8NE35; -.
DR STRING; 9606.ENSP00000482128; -.
DR iPTMnet; Q8NE35; -.
DR PhosphoSitePlus; Q8NE35; -.
DR BioMuta; CPEB3; -.
DR DMDM; 119368633; -.
DR EPD; Q8NE35; -.
DR jPOST; Q8NE35; -.
DR MassIVE; Q8NE35; -.
DR MaxQB; Q8NE35; -.
DR PaxDb; Q8NE35; -.
DR PeptideAtlas; Q8NE35; -.
DR PRIDE; Q8NE35; -.
DR ProteomicsDB; 73124; -. [Q8NE35-1]
DR ProteomicsDB; 73125; -. [Q8NE35-2]
DR Antibodypedia; 30391; 121 antibodies from 19 providers.
DR DNASU; 22849; -.
DR Ensembl; ENST00000265997.5; ENSP00000265997.4; ENSG00000107864.15. [Q8NE35-1]
DR Ensembl; ENST00000412050.8; ENSP00000398310.2; ENSG00000107864.15. [Q8NE35-2]
DR Ensembl; ENST00000614585.4; ENSP00000482128.1; ENSG00000107864.15. [Q8NE35-1]
DR GeneID; 22849; -.
DR KEGG; hsa:22849; -.
DR MANE-Select; ENST00000265997.5; ENSP00000265997.4; NM_014912.5; NP_055727.3.
DR UCSC; uc001khv.3; human. [Q8NE35-1]
DR CTD; 22849; -.
DR DisGeNET; 22849; -.
DR GeneCards; CPEB3; -.
DR HGNC; HGNC:21746; CPEB3.
DR HPA; ENSG00000107864; Tissue enhanced (liver).
DR MIM; 610606; gene.
DR neXtProt; NX_Q8NE35; -.
DR OpenTargets; ENSG00000107864; -.
DR PharmGKB; PA134903478; -.
DR VEuPathDB; HostDB:ENSG00000107864; -.
DR eggNOG; KOG0129; Eukaryota.
DR GeneTree; ENSGT00940000158949; -.
DR HOGENOM; CLU_014948_2_1_1; -.
DR InParanoid; Q8NE35; -.
DR OMA; CWAAIHA; -.
DR OrthoDB; 1075356at2759; -.
DR PhylomeDB; Q8NE35; -.
DR TreeFam; TF317658; -.
DR PathwayCommons; Q8NE35; -.
DR SignaLink; Q8NE35; -.
DR BioGRID-ORCS; 22849; 12 hits in 1068 CRISPR screens.
DR ChiTaRS; CPEB3; human.
DR EvolutionaryTrace; Q8NE35; -.
DR GenomeRNAi; 22849; -.
DR Pharos; Q8NE35; Tbio.
DR PRO; PR:Q8NE35; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8NE35; protein.
DR Bgee; ENSG00000107864; Expressed in buccal mucosa cell and 169 other tissues.
DR ExpressionAtlas; Q8NE35; baseline and differential.
DR Genevisible; Q8NE35; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; ISS:UniProtKB.
DR GO; GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IDA:HPA.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, RNA binding; IDA:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IBA:GO_Central.
DR GO; GO:1900248; P:negative regulation of cytoplasmic translational elongation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.640.40; -; 1.
DR InterPro; IPR032296; CEBP_ZZ.
DR InterPro; IPR038446; CEBP_ZZ_sf.
DR InterPro; IPR034819; CPEB.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR12566; PTHR12566; 1.
DR Pfam; PF16366; CEBP_ZZ; 1.
DR Pfam; PF16367; RRM_7; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Amyloid; Cell projection;
KW Cytoplasm; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; RNA-binding; Synapse; Translation regulation;
KW Ubl conjugation.
FT CHAIN 1..698
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 3"
FT /id="PRO_0000269261"
FT DOMAIN 441..532
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 549..631
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..189
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 441..442
FT /note="Cleavage; by CAPN2"
FT /evidence="ECO:0000250|UniProtKB:Q7TN99"
FT SITE 444
FT /note="Required for RNA-binding activity"
FT /evidence="ECO:0000269|PubMed:24343026"
FT SITE 488
FT /note="Required for RNA-binding activity"
FT /evidence="ECO:0000269|PubMed:24343026"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TN99"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TN99"
FT MOD_RES 308
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q7TN99"
FT VAR_SEQ 366..388
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_022034"
FT VAR_SEQ 408
FT /note="N -> SRSSLFPFED (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_022035"
FT VARIANT 324
FT /note="R -> W (in dbSNP:rs17853616)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029776"
FT MUTAGEN 349
FT /note="L->A: Abolishes nuclear export; when associated with
FT A-353."
FT /evidence="ECO:0000269|PubMed:22730302"
FT MUTAGEN 353
FT /note="L->A: Abolishes nuclear export; when associated with
FT A-349."
FT /evidence="ECO:0000269|PubMed:22730302"
FT MUTAGEN 441
FT /note="R->A: Does not impair RNA binding."
FT /evidence="ECO:0000269|PubMed:24343026"
FT MUTAGEN 444
FT /note="F->A,N: Abolishes RNA binding."
FT /evidence="ECO:0000269|PubMed:24343026"
FT MUTAGEN 444
FT /note="F->Y: Does not impair RNA binding."
FT /evidence="ECO:0000269|PubMed:24343026"
FT MUTAGEN 446
FT /note="G->A: Does not impair RNA binding."
FT /evidence="ECO:0000269|PubMed:24343026"
FT MUTAGEN 463
FT /note="R->A: Does not impair RNA binding."
FT /evidence="ECO:0000269|PubMed:24343026"
FT MUTAGEN 470
FT /note="D->A: Does not impair RNA binding."
FT /evidence="ECO:0000269|PubMed:24343026"
FT MUTAGEN 474
FT /note="K->A: Does not impair RNA binding."
FT /evidence="ECO:0000269|PubMed:24343026"
FT MUTAGEN 479
FT /note="S->A: Does not impair RNA binding."
FT /evidence="ECO:0000269|PubMed:24343026"
FT MUTAGEN 488
FT /note="F->A: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:24343026"
FT MUTAGEN 488
FT /note="F->Y: Does not impair RNA binding."
FT /evidence="ECO:0000269|PubMed:24343026"
FT MUTAGEN 528
FT /note="R->A: Does not impair RNA binding."
FT /evidence="ECO:0000269|PubMed:24343026"
FT CONFLICT 519
FT /note="Missing (in Ref. 3; AAH36444)"
FT /evidence="ECO:0000305"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:2DNL"
FT HELIX 454..460
FT /evidence="ECO:0007829|PDB:2DNL"
FT TURN 461..464
FT /evidence="ECO:0007829|PDB:2DNL"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:2RUG"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:2DNL"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:2RUG"
FT STRAND 485..489
FT /evidence="ECO:0007829|PDB:2DNL"
FT HELIX 494..503
FT /evidence="ECO:0007829|PDB:2DNL"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:2DNL"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:2DNL"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:2DNL"
FT STRAND 522..528
FT /evidence="ECO:0007829|PDB:2DNL"
SQ 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
