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Cytoplasmic polyadenylation element-binding protein 2 (CPE-BP2) (CPE-binding protein 2) (mCPEB-2)

 CPEB2_MOUSE             Reviewed;         521 AA.
Q812E0;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
25-OCT-2017, entry version 106.
RecName: Full=Cytoplasmic polyadenylation element-binding protein 2;
Short=CPE-BP2;
Short=CPE-binding protein 2;
Short=mCPEB-2;
Name=Cpeb2;
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, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=12672660; DOI=10.1095/biolreprod.103.015677;
Kurihara Y., Tokuriki M., Myojin R., Hori T., Kuroiwa A., Matsuda Y.,
Sakurai T., Kimura M., Hecht N.B., Uesugi S.;
"CPEB2, a novel putative translational regulator in mouse haploid germ
cells.";
Biol. Reprod. 69:261-268(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[3]
TISSUE SPECIFICITY, AND ABSENCE OF 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).
[4]
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Liver, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May play a role in translational regulation of stored
mRNAs in transcriptionally inactive haploid spermatids. Binds to
poly(U) RNA oligomers (PubMed:12672660). Required for cell cycle
progression, specifically for the transition from metaphase to
anaphase (By similarity). {ECO:0000250|UniProtKB:Q7Z5Q1,
ECO:0000269|PubMed:12672660}.
-!- SUBUNIT: Interacts with PAPD4/GLD2. {ECO:0000269|PubMed:17927953}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12672660}.
-!- TISSUE SPECIFICITY: Expressed in embryo, cerebellum, salivary
gland, thymus, heart, liver, lung, spleen, kidney, intestine,
ovary and round spermatids. Weakly expressed in granular cells of
dentate gyrus and the pyramidal cells of CA3 and CA1 of the
hippocampus. {ECO:0000269|PubMed:12672660,
ECO:0000269|PubMed:12871996}.
-!- INDUCTION: Not induced by kainate. {ECO:0000269|PubMed:12871996}.
-!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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EMBL; AB100307; BAC57076.1; -; mRNA.
EMBL; BC107349; AAI07350.1; -; mRNA.
EMBL; BC107350; AAI07351.1; -; mRNA.
UniGene; Mm.7233; -.
ProteinModelPortal; Q812E0; -.
SMR; Q812E0; -.
iPTMnet; Q812E0; -.
PhosphoSitePlus; Q812E0; -.
MaxQB; Q812E0; -.
PRIDE; Q812E0; -.
MGI; MGI:2442640; Cpeb2.
HOGENOM; HOG000290661; -.
HOVERGEN; HBG058010; -.
InParanoid; Q812E0; -.
PhylomeDB; Q812E0; -.
ChiTaRS; Cpeb2; mouse.
PRO; PR:Q812E0; -.
Proteomes; UP000000589; Unplaced.
Genevisible; Q812E0; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005844; C:polysome; IDA:MGI.
GO; GO:0045202; C:synapse; IBA:GO_Central.
GO; GO:0005095; F:GTPase inhibitor activity; ISS:UniProtKB.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
GO; GO:0008187; F:poly-pyrimidine tract binding; IDA:MGI.
GO; GO:0043023; F:ribosomal large subunit binding; ISS:UniProtKB.
GO; GO:0043024; F:ribosomal small subunit binding; ISS:UniProtKB.
GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; ISO: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:0071243; P:cellular response to arsenic-containing substance; 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:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; IDA:UniProtKB.
GO; GO:1900248; P:negative regulation of cytoplasmic translational elongation; ISS:UniProtKB.
GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0045900; P:negative regulation of translational elongation; IGI:MGI.
InterPro; IPR032296; CEBP_ZZ.
InterPro; IPR034819; CPEB.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR12566; PTHR12566; 3.
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;
Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome;
Repeat; RNA-binding; Translation regulation.
CHAIN 1 521 Cytoplasmic polyadenylation element-
binding protein 2.
/FTId=PRO_0000269260.
DOMAIN 264 355 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 372 454 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
SEQUENCE 521 AA; 58442 MW; 88B0D73942770A17 CRC64;
MNLPQQQPPA AAPQQPQSRR SPVSPQLQQQ HQAAAAAFLQ QRNSYNHHQP LLKQSPWSNH
QNSGWGTASM SWGAMHGRDH RRSGNMGIPG TMNQISPLKK PFSGNVIAPP KFTRSTPSLT
PKSWIEDNVF RTDNNSNTLL PLQVRSSLQL PAWGSDSLQD SWCTAAGTSR IDQDRSRMYD
SLNMHSLENS LIDIMRAEHD PLKGRLSYPH PGTDNLLMLN GRSSLFPIDD SLLDDGHSDQ
VGVLNSPTCY SAHQNGERIE RFSRKVFVGG LPPDIDEDEI TASFRRFGPL VVDWPHKAES
KSYFPPKGYA FLLFQEESSV QALIDACIEE DGKLYLCVSS PTIKDKPVQI RPWNLSDSDF
VMDGSQPLDP RKTIFVGGVP RPLRAVELAM IMDRLYGGVC YAGIDTDPEL KYPKGAGRVA
FSNQQSYIAA ISARFVQLQH GDIDKRVEVK PYVLDDQMCD ECQGARCGGK FAPFFCANVT
CLQYYCEFCW ANIHSRAGRE FHKPLVKEGA DRPRQIHFRW N


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