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Cytoplasmic polyadenylation element-binding protein 1 (CPE-BP1) (CPE-binding protein 1) (mCPEB) (mCPEB-1)

 CPEB1_MOUSE             Reviewed;         561 AA.
P70166; Q8C5P9;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 129.
RecName: Full=Cytoplasmic polyadenylation element-binding protein 1;
Short=CPE-BP1;
Short=CPE-binding protein 1;
Short=mCPEB;
Short=mCPEB-1;
Name=Cpeb1; Synonyms=Cpeb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING, AND TISSUE SPECIFICITY.
TISSUE=Ovary;
PubMed=8962099; DOI=10.1073/pnas.93.25.14602;
Gebauer F., Richter J.D.;
"Mouse cytoplasmic polyadenylation element binding protein: an
evolutionarily conserved protein that interacts with the cytoplasmic
polyadenylation elements of c-mos mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 93:14602-14607(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 422-561.
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
RNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9856468; DOI=10.1016/S0896-6273(00)80630-3;
Wu L., Wells D., Tay J., Mendis D., Abbott M.-A., Barnitt A.,
Quinlan E., Heynen A., Fallon J.R., Richter J.D.;
"CPEB-mediated cytoplasmic polyadenylation and the regulation of
experience-dependent translation of alpha-CaMKII mRNA at synapses.";
Neuron 21:1129-1139(1998).
[4]
FUNCTION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=11526086;
Hodgman R., Tay J., Mendez R., Richter J.D.;
"CPEB phosphorylation and cytoplasmic polyadenylation are catalyzed by
the kinase IAK1/Eg2 in maturing mouse oocytes.";
Development 128:2815-2822(2001).
[5]
FUNCTION, PHOSPHORYLATION AT THR-171 BY AURKA MUTAGENESIS OF THR-171,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11980711; DOI=10.1093/emboj/21.9.2139;
Huang Y.-S., Jung M.-Y., Sarkissian M., Richter J.D.;
"N-methyl-D-aspartate receptor signaling results in Aurora kinase-
catalyzed CPEB phosphorylation and alpha CaMKII mRNA polyadenylation
at synapses.";
EMBO J. 21:2139-2148(2002).
[6]
FUNCTION, INTERACTION WITH DYNEIN AND KINESIN, RNA-BINDING, AND
SUBCELLULAR LOCATION.
PubMed=12629046; DOI=10.1101/gad.1053003;
Huang Y.-S., Carson J.H., Barbarese E., Richter J.D.;
"Facilitation of dendritic mRNA transport by CPEB.";
Genes Dev. 17:638-653(2003).
[7]
PHOSPHORYLATION AT THR-171 BY AURKA, DEPHOSPHORYLATION AT THR-171 BY
PP1, MUTAGENESIS OF THR-171, AND DEVELOPMENTAL STAGE.
PubMed=12815066; DOI=10.1101/gad.1071403;
Tay J., Hodgman R., Sarkissian M., Richter J.D.;
"Regulated CPEB phosphorylation during meiotic progression suggests a
mechanism for temporal control of maternal mRNA translation.";
Genes Dev. 17:1457-1462(2003).
[8]
TISSUE SPECIFICITY, AND ABSENCE OF KAINATE INDUCTION.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=12871996; DOI=10.1073/pnas.1133424100;
Theis M., Si K., Kandel E.R.;
"Two previously undescribed members of the mouse CPEB family of genes
and their inducible expression in the principal cell layers of the
hippocampus.";
Proc. Natl. Acad. Sci. U.S.A. 100:9602-9607(2003).
[9]
PHOSPHORYLATION AT THR-171 BY CAMK2A, MUTAGENESIS OF THR-171, AND
SUBCELLULAR LOCATION.
PubMed=15175389; DOI=10.1523/JNEUROSCI.0854-04.2004;
Atkins C.M., Nozaki N., Shigeri Y., Soderling T.R.;
"Cytoplasmic polyadenylation element binding protein-dependent protein
synthesis is regulated by calcium/calmodulin-dependent protein kinase
II.";
J. Neurosci. 24:5193-5201(2004).
[10]
PHOSPHORYLATION AT THR-171 BY CAMK2A, AND DEPHOSPHORYLATION AT
THR-171.
PubMed=15944388; DOI=10.1523/JNEUROSCI.5051-04.2005;
Atkins C.M., Davare M.A., Oh M.C., Derkach V., Soderling T.R.;
"Bidirectional regulation of cytoplasmic polyadenylation element-
binding protein phosphorylation by Ca2+/calmodulin-dependent protein
kinase II and protein phosphatase 1 during hippocampal long-term
potentiation.";
J. Neurosci. 25:5604-5610(2005).
[11]
INTERACTION WITH APLP1; APLP2 AND APP, PHOSPHORYLATION, AND
SUBCELLULAR LOCATION.
PubMed=16314516; DOI=10.1128/MCB.25.24.10930-10939.2005;
Cao Q., Huang Y.-S., Kan M.-C., Richter J.D.;
"Amyloid precursor proteins anchor CPEB to membranes and promote
polyadenylation-induced translation.";
Mol. Cell. Biol. 25:10930-10939(2005).
[12]
INTERACTION WITH NGDN.
PubMed=16705177; DOI=10.1128/MCB.02470-05;
Jung M.-Y., Lorenz L., Richter J.D.;
"Translational control by neuroguidin, a eukaryotic initiation factor
4E and CPEB binding protein.";
Mol. Cell. Biol. 26:4277-4287(2006).
[13]
INTERACTION WITH PAPD4.
PubMed=17927953; DOI=10.1016/j.bbrc.2007.09.096;
Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T.,
Kimura M., Kashiwabara S., Baba T.;
"Disruption of mouse poly(A) polymerase mGLD-2 does not alter
polyadenylation status in oocytes and somatic cells.";
Biochem. Biophys. Res. Commun. 364:14-19(2007).
-!- FUNCTION: Sequence-specific RNA-binding protein that regulates
mRNA cytoplasmic polyadenylation and translation initiation during
oocyte maturation, early development and at postsynapse sites of
neurons. Binds to the cytoplasmic polyadenylation element (CPE),
an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-
3') within the 3'-UTR of mRNAs. In absence of phosphorylation and
in association with TACC3 is also involved as a repressor of
translation of CPE-containing mRNA; a repression that is relieved
by phosphorylation or degradation (By similarity). Involved in the
transport of CPE-containing mRNA to dendrites; those mRNAs may be
transported to dendrites in a translationally dormant form and
translationally activated at synapses. Its interaction with APLP1
promotes local CPE-containing mRNA polyadenylation and translation
activation. Induces the assembly of stress granules in the absence
of stress (By similarity). Required for cell cycle progression,
specifically for prophase entry (By similarity).
{ECO:0000250|UniProtKB:Q9BZB8, ECO:0000269|PubMed:11526086,
ECO:0000269|PubMed:11980711, ECO:0000269|PubMed:12629046}.
-!- SUBUNIT: Interacts with kinesin, dynein, APLP1, APLP2, PAPD4/GLD2
and APP. Both phosphorylated and non phosphorylated forms interact
with APLP1. {ECO:0000269|PubMed:12629046,
ECO:0000269|PubMed:16314516, ECO:0000269|PubMed:16705177,
ECO:0000269|PubMed:17927953}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction,
synapse {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}.
Cytoplasmic granule {ECO:0000250}. Membrane {ECO:0000250}. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000250}. Note=Localizes in synaptosomes at dendritic
synapses of neurons. Strongly enriched in postsynaptic density
(PSD) fractions. Transported into dendrites in a microtubule-
dependent fashion and colocalizes in mRNA-containing particles
with TACC3, dynein and kinesin. Membrane-associated. Colocalizes
at excitatory synapses with members of the polyadenylation and
translation complex factors (CPSF, APLP1, TACC3, AURKA, SYP, etc.)
including CPE-containing RNAs. In P-bodies and stress granules (By
similarity). Recruited to stress granules (SGs) upon arsenite
treatment (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in hippocampus, cerebral cortex and
oocytes (at protein level). Expressed in brain, heart, kidney,
lung and ovary and testis. Weakly expressed in granular cells of
dentate gyrus and the pyramidal cells of CA3 and CA1 of the
hippocampus. {ECO:0000269|PubMed:11526086,
ECO:0000269|PubMed:11980711, ECO:0000269|PubMed:12871996,
ECO:0000269|PubMed:8962099, ECO:0000269|PubMed:9856468}.
-!- DEVELOPMENTAL STAGE: Expressed in embryonic ovaries at 14.5, 16.5
and 18.5 dpc (at protein level). {ECO:0000269|PubMed:12815066}.
-!- INDUCTION: Not induced by kainate.
-!- DOMAIN: The 2 RRM domains and the C-terminal region mediate
interaction with CPE-containing RNA. The interdomain linker (411-
429) acts as a hinge to fix the relative orientation of the 2
RRMs. The ZZ domain (509-566) coordinates 2 Zn ions and is
probably implicated in mediating interactions with other proteins
in addition to increasing the affinity of the RRMs for the CPEs. A
continuous hydrophobic interface is formed between the 2 RRM.
{ECO:0000250|UniProtKB:Q9BZB8}.
-!- PTM: Phosphorylated on serine/threonine residues by AURKA within
positions 165 and 196 (By similarity). Phosphorylation and
dephosphorylation on Thr-171 regulates cytoplasmic polyadenylation
and translation of CPE-containing mRNAs. Phosphorylation on Thr-
171 by AURKA in embryonic ovaries at 16.5 dpc (mostly pachytene
oocytes) activates CPEB1. Not phosphorylated on Thr-171 in
embryonic ovaries between 18.5 dpc (diplotene oocytes) and
metaphase I. Dephosphorylation on Thr-171 by PP1 in embryonic
ovaries at 18.5 dpc (mostly diplotene oocytes) inactivates CPEB1.
In maturing oocytes, re-phosphorylation on Thr-171 by AURKA
reactivates CPEB1. Phosphorylation on Thr-171 by CAMK2A in
depolarized hippocampal neurons activates CPEB1. Dephosphorylation
on Thr-171 (indirectly by PP1) in hippocampal neurons inactivates
CPEB1. Phosphorylation on Thr-171 may be promoted by APLP1.
Phosphorylation increases binding to RNA. {ECO:0000250,
ECO:0000269|PubMed:11526086, ECO:0000269|PubMed:11980711,
ECO:0000269|PubMed:12815066, ECO:0000269|PubMed:15175389,
ECO:0000269|PubMed:15944388, ECO:0000269|PubMed:16314516}.
-!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y08260; CAA69588.1; -; mRNA.
EMBL; AK077799; BAC37017.1; -; mRNA.
CCDS; CCDS40007.1; -.
RefSeq; NP_001239454.1; NM_001252525.1.
RefSeq; NP_001239455.1; NM_001252526.1.
RefSeq; NP_031781.1; NM_007755.5.
UniGene; Mm.273122; -.
ProteinModelPortal; P70166; -.
SMR; P70166; -.
BioGrid; 198856; 4.
DIP; DIP-41380N; -.
IntAct; P70166; 1.
MINT; MINT-261117; -.
STRING; 10090.ENSMUSP00000137079; -.
iPTMnet; P70166; -.
PhosphoSitePlus; P70166; -.
MaxQB; P70166; -.
PaxDb; P70166; -.
PRIDE; P70166; -.
Ensembl; ENSMUST00000098331; ENSMUSP00000095936; ENSMUSG00000025586.
GeneID; 12877; -.
KEGG; mmu:12877; -.
UCSC; uc009ibw.2; mouse.
CTD; 64506; -.
MGI; MGI:108442; Cpeb1.
eggNOG; ENOG410KDT8; Eukaryota.
eggNOG; ENOG410YBXF; LUCA.
GeneTree; ENSGT00390000012886; -.
HOVERGEN; HBG079080; -.
InParanoid; P70166; -.
KO; K02602; -.
TreeFam; TF317658; -.
ChiTaRS; Cpeb1; mouse.
PRO; PR:P70166; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000025586; -.
ExpressionAtlas; P70166; baseline and differential.
Genevisible; P70166; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0072687; C:meiotic spindle; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0045202; C:synapse; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:MGI.
GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
GO; GO:0000900; F:translation repressor activity, nucleic acid binding; IDA:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; IDA:UniProtKB.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
GO; GO:0006417; P:regulation of translation; IDA:MGI.
GO; GO:0007130; P:synaptonemal complex assembly; IMP:MGI.
CDD; cd12723; RRM1_CPEB1; 1.
InterPro; IPR032292; CEBP1_N.
InterPro; IPR032296; CEBP_ZZ.
InterPro; IPR034819; CPEB.
InterPro; IPR034977; CPEB1_RRM1.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR12566; PTHR12566; 1.
Pfam; PF16368; CEBP1_N; 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;
Activator; Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Membrane; Metal-binding; mRNA processing; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Repeat; Repressor;
Ribonucleoprotein; RNA-binding; Synapse; Translation regulation; Zinc.
CHAIN 1 561 Cytoplasmic polyadenylation element-
binding protein 1.
/FTId=PRO_0000269252.
DOMAIN 310 407 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 429 510 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 329 561 Necessary for stress granule assembly and
correct localization in dcp1 bodies.
{ECO:0000250}.
COMPBIAS 177 207 Ser-rich.
METAL 514 514 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 517 517 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 526 526 Zinc 2. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 531 531 Zinc 2. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 536 536 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 539 539 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 544 544 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9BZB8}.
METAL 552 552 Zinc 2; via pros nitrogen.
{ECO:0000250|UniProtKB:Q9BZB8}.
SITE 410 410 Important for the positionning of RRM1
relative to RRM2.
{ECO:0000250|UniProtKB:Q9BZB8}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BZB8}.
MOD_RES 171 171 Phosphothreonine; by AURKA and CAMK2A.
{ECO:0000269|PubMed:11980711,
ECO:0000269|PubMed:12815066,
ECO:0000269|PubMed:15175389,
ECO:0000269|PubMed:15944388}.
MUTAGEN 171 171 T->A: Inhibits CPE-containing cytoplasmic
polyadenylation and translation
activation. {ECO:0000269|PubMed:12815066,
ECO:0000269|PubMed:15175389}.
SEQUENCE 561 AA; 61917 MW; CB7958885AB13FF6 CRC64;
MAFSLEEAAG RIKDCWDNQE VPALSTCSNA NIFRRINAIL DDSLDFSKVC TTPINRGIHD
QLPDFQDSEE TVTSRMLFPT SAQESPRGLP DANGLCLGLQ SLSLTGWDRP WSTQDSDSSA
QSSTQSVLSM LQNPLGNVLG KAPLSFLSLD PLGSDLDKFP APSVRGSRLD TRPILDSRSS
SPSDSDTSGF SSGSDHLSDL ISSLRISPPL PFLSMTGNGP RDPLKMGVGS RMDQEQAALA
AVAPSPTSAP KRWPGASVWP SWDLLGAPKD PFSIEREARL HRQAAAVNEA TCTWSGQLPP
RNYKNPIYSC KVFLGGVPWD ITEAGLVNTF RVFGSLSVEW PGKDGKHPRC PPKGNMPKGY
VYLVFELEKS VRALLQACSH DPLSPDGLSE YYFKMSSRRM RCKEVQVIPW VLADSNFVWS
PSQRLDPSRT VFVGALHGML NAEALAAILN DLFGGVVYAG IDTDKHKYPI GSGRVTFNNQ
RSYLKAVTAA FVEIKTTKFT KKVQIDPYLE DSLCLICSSQ PGPFFCRDQV CFKYFCRSCW
HWRHSMEGLR HHSPLMRNQK N


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