CPEB1_HUMAN
ID CPEB1_HUMAN Reviewed; 566 AA.
AC Q9BZB8; B7Z6C6; Q86W46; Q8IV41; Q9BZB7; Q9H8V5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 1;
DE Short=CPE-BP1;
DE Short=CPE-binding protein 1;
DE Short=h-CPEB;
DE Short=hCPEB-1;
GN Name=CPEB1; Synonyms=CPEB;
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 [MRNA] (ISOFORMS 1 AND 2), RNA-BINDING, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain, and Ovary;
RX PubMed=11223249; DOI=10.1016/s0378-1119(00)00588-6;
RA Welk J.F., Charlesworth A., Smith G.D., MacNicol A.M.;
RT "Identification and characterization of the gene encoding human cytoplasmic
RT polyadenylation element binding protein.";
RL Gene 263:113-120(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Pericardium, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Melanoma;
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 [5]
RP FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15966895; DOI=10.1111/j.1365-2443.2005.00870.x;
RA Sasayama T., Marumoto T., Kunitoku N., Zhang D., Tamaki N., Kohmura E.,
RA Saya H., Hirota T.;
RT "Over-expression of Aurora-A targets cytoplasmic polyadenylation element
RT binding protein and promotes mRNA polyadenylation of Cdk1 and cyclin B1.";
RL Genes Cells 10:627-638(2005).
RN [6]
RP FUNCTION, ALTERNATIVE SPLICING, MUTAGENESIS OF THR-172; PHE-314 AND
RP HIS-545, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15731006; DOI=10.1242/jcs.01692;
RA Wilczynska A., Aigueperse C., Kress M., Dautry F., Weil D.;
RT "The translational regulator CPEB1 provides a link between dcp1 bodies and
RT stress granules.";
RL J. Cell Sci. 118:981-992(2005).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18923137; DOI=10.1091/mbc.e08-09-0904;
RA Ernoult-Lange M., Wilczynska A., Harper M., Aigueperse C., Dautry F.,
RA Kress M., Weil D.;
RT "Nucleocytoplasmic traffic of CPEB1 and accumulation in Crm1 nucleolar
RT bodies.";
RL Mol. Biol. Cell 20:176-187(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
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 [11]
RP STRUCTURE BY NMR OF 504-566 IN COMPLEX WITH ZINC, AND DOMAIN.
RX PubMed=23500490; DOI=10.1016/j.jmb.2013.03.009;
RA Merkel D.J., Wells S.B., Hilburn B.C., Elazzouzi F., Perez-Alvarado G.C.,
RA Lee B.M.;
RT "The C-Terminal region of cytoplasmic polyadenylation element binding
RT protein is a ZZ domain with potential for protein-protein interactions.";
RL J. Mol. Biol. 425:2015-2026(2013).
RN [12]
RP FUNCTION, STRUCTURE BY NMR OF 294-566 ALONE OR IN COMPLEX WITH RNA AND IN
RP COMPLEX WITH ZINC, AND DOMAIN.
RX PubMed=24990967; DOI=10.1101/gad.241133.114;
RA Afroz T., Skrisovska L., Belloc E., Guillen-Boixet J., Mendez R.,
RA Allain F.H.;
RT "A fly trap mechanism provides sequence-specific RNA recognition by CPEB
RT proteins.";
RL Genes Dev. 28:1498-1514(2014).
RN [13]
RP INTERACTION WITH TENT4B, AND SUBCELLULAR LOCATION.
RX PubMed=28383716; DOI=10.1093/nar/gkx239;
RA Shin J., Paek K.Y., Ivshina M., Stackpole E.E., Richter J.D.;
RT "Essential role for non-canonical poly(A) polymerase GLD4 in cytoplasmic
RT polyadenylation and carbohydrate metabolism.";
RL Nucleic Acids Res. 45:6793-6804(2017).
RN [14]
RP STRUCTURE BY NMR OF 206-213.
RX PubMed=26456073; DOI=10.1038/srep14990;
RA Schelhorn C., Martin-Malpartida P., Sunol D., Macias M.J.;
RT "Structural Analysis of the Pin1-CPEB1 interaction and its potential role
RT in CPEB1 degradation.";
RL Sci. Rep. 5:14990-14990(2015).
RN [15]
RP VARIANTS GLU-8 DEL AND ILE-233.
RX PubMed=26063658; DOI=10.1093/brain/awv155;
RA Verdura E., Herve D., Scharrer E., del Mar Amador M., Guyant-Marechal L.,
RA Philippi A., Corlobe A., Bergametti F., Gazal S., Prieto-Morin C.,
RA Beaufort N., Le Bail B., Viakhireva I., Dichgans M., Chabriat H.,
RA Haffner C., Tournier-Lasserve E.;
RT "Heterozygous HTRA1 mutations are associated with autosomal dominant
RT cerebral small vessel disease.";
RL Brain 138:2347-2358(2015).
CC -!- FUNCTION: Sequence-specific RNA-binding protein that regulates mRNA
CC cytoplasmic polyadenylation and translation initiation during oocyte
CC maturation, early development and at postsynapse sites of neurons.
CC Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich
CC sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-
CC UTR. RNA binding results in a clear conformational change analogous to
CC the Venus fly trap mechanism (PubMed:24990967). In absence of
CC phosphorylation and in association with TACC3 is also involved as a
CC repressor of translation of CPE-containing mRNA; a repression that is
CC relieved by phosphorylation or degradation (By similarity). Involved in
CC the transport of CPE-containing mRNA to dendrites; those mRNAs may be
CC transported to dendrites in a translationally dormant form and
CC translationally activated at synapses (By similarity). Its interaction
CC with APLP1 promotes local CPE-containing mRNA polyadenylation and
CC translation activation (By similarity). Induces the assembly of stress
CC granules in the absence of stress. Required for cell cycle progression,
CC specifically for prophase entry (PubMed:26398195).
CC {ECO:0000250|UniProtKB:P70166, ECO:0000269|PubMed:15731006,
CC ECO:0000269|PubMed:15966895, ECO:0000269|PubMed:24990967,
CC ECO:0000269|PubMed:26398195}.
CC -!- SUBUNIT: Interacts with kinesin, dynein, APLP1, APLP2, TENT2/GLD2 and
CC APP. Both phosphorylated and non phosphorylated forms interact with
CC APLP1 (By similarity). Interacts with TENT4B; the interaction is
CC required for TENT4B-mediated translational control (PubMed:28383716).
CC {ECO:0000250|UniProtKB:P70166, ECO:0000269|PubMed:28383716}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18923137,
CC ECO:0000269|PubMed:28383716}. Nucleus {ECO:0000269|PubMed:18923137}.
CC Cytoplasm, P-body. Cytoplasmic granule. Synapse. Membrane. Postsynaptic
CC density {ECO:0000250}. Cell projection, dendrite {ECO:0000250}.
CC Note=Continuously shuttling between nucleus and cytoplasm
CC (PubMed:18923137). Also found in stress granules. Recruited to stress
CC granules (SGs) upon arsenite treatment. In dendrites (By similarity).
CC Localizes in synaptosomes at dendritic synapses of neurons (By
CC similarity). Strongly enriched in postsynaptic density (PSD) fractions
CC (By similarity). Transported into dendrites in a microtubule-dependent
CC fashion and colocalizes in mRNA-containing particles with TACC3, dynein
CC and kinesin (By similarity). Membrane-associated (By similarity).
CC Colocalizes at excitatory synapses with members of the polyadenylation
CC and translation complex factors (CPSF, APLP1, TACC3, AURKA, SYP, etc.)
CC including CPE-containing RNAs (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:18923137}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=hCPEB long, hCPEBg;
CC IsoId=Q9BZB8-1; Sequence=Displayed;
CC Name=2; Synonyms=hCPEB short, hCPEBs;
CC IsoId=Q9BZB8-2; Sequence=VSP_022027;
CC Name=3;
CC IsoId=Q9BZB8-3; Sequence=VSP_022028, VSP_022029;
CC Name=4;
CC IsoId=Q9BZB8-4; Sequence=VSP_022027, VSP_022029;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in immature oocytes, ovary,
CC brain and heart. Isoform 2 is expressed in brain and heart. Isoform 3
CC and isoform 4 are expressed in brain. Expressed in breast tumors and
CC several tumor cell lines. {ECO:0000269|PubMed:11223249,
CC ECO:0000269|PubMed:15731006, ECO:0000269|PubMed:15966895}.
CC -!- DOMAIN: The 2 RRM domains and the C-terminal region mediate interaction
CC with CPE-containing RNA (PubMed:24990967). The interdomain linker (411-
CC 429) acts as a hinge to fix the relative orientation of the 2 RRMs
CC (PubMed:24990967). The ZZ domain (509-566) coordinates 2 Zn ions and is
CC probably implicated in mediating interactions with other proteins in
CC addition to increasing the affinity of the RRMs for the CPEs
CC (PubMed:23500490, PubMed:24990967). A continuous hydrophobic interface
CC is formed between the 2 RRMs (PubMed:24990967).
CC {ECO:0000269|PubMed:23500490, ECO:0000269|PubMed:24990967}.
CC -!- PTM: Phosphorylated on serine/threonine residues by AURKA within
CC positions 166 and 197. Phosphorylation and dephosphorylation on Thr-172
CC regulates cytoplasmic polyadenylation and translation of CPE-containing
CC mRNAs. Phosphorylation on Thr-172 by AURKA and CAMK2A activates CPEB1.
CC Phosphorylation on Thr-172 may be promoted by APLP1. Phosphorylation
CC increases binding to RNA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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DR EMBL; AF329402; AAK01239.1; -; mRNA.
DR EMBL; AF329403; AAK01240.1; -; mRNA.
DR EMBL; AK023265; BAB14496.1; -; mRNA.
DR EMBL; AK300105; BAH13212.1; -; mRNA.
DR EMBL; CH471188; EAW62449.1; -; Genomic_DNA.
DR EMBL; BC035348; AAH35348.1; -; mRNA.
DR EMBL; BC050629; AAH50629.1; -; mRNA.
DR CCDS; CCDS42072.2; -. [Q9BZB8-2]
DR CCDS; CCDS45329.2; -. [Q9BZB8-3]
DR CCDS; CCDS45330.2; -. [Q9BZB8-4]
DR RefSeq; NP_001073001.1; NM_001079533.1. [Q9BZB8-2]
DR RefSeq; NP_001073002.1; NM_001079534.1. [Q9BZB8-4]
DR RefSeq; NP_001073003.1; NM_001079535.1. [Q9BZB8-4]
DR RefSeq; NP_001275748.1; NM_001288819.1. [Q9BZB8-4]
DR RefSeq; NP_085097.3; NM_030594.4. [Q9BZB8-3]
DR PDB; 2M13; NMR; -; A=504-566.
DR PDB; 2MKE; NMR; -; A=506-566.
DR PDB; 2MKH; NMR; -; A=294-514.
DR PDB; 2MKK; NMR; -; A=294-510.
DR PDB; 2N1O; NMR; -; B=206-213.
DR PDBsum; 2M13; -.
DR PDBsum; 2MKE; -.
DR PDBsum; 2MKH; -.
DR PDBsum; 2MKK; -.
DR PDBsum; 2N1O; -.
DR AlphaFoldDB; Q9BZB8; -.
DR BMRB; Q9BZB8; -.
DR SMR; Q9BZB8; -.
DR BioGRID; 122202; 139.
DR IntAct; Q9BZB8; 131.
DR STRING; 9606.ENSP00000477715; -.
DR iPTMnet; Q9BZB8; -.
DR PhosphoSitePlus; Q9BZB8; -.
DR BioMuta; CPEB1; -.
DR DMDM; 74762720; -.
DR MassIVE; Q9BZB8; -.
DR MaxQB; Q9BZB8; -.
DR PaxDb; Q9BZB8; -.
DR PeptideAtlas; Q9BZB8; -.
DR PRIDE; Q9BZB8; -.
DR ProteomicsDB; 79800; -. [Q9BZB8-1]
DR ProteomicsDB; 79801; -. [Q9BZB8-2]
DR ProteomicsDB; 79802; -. [Q9BZB8-3]
DR ProteomicsDB; 79803; -. [Q9BZB8-4]
DR Antibodypedia; 28086; 305 antibodies from 39 providers.
DR DNASU; 64506; -.
DR Ensembl; ENST00000611163.4; ENSP00000483857.1; ENSG00000214575.10. [Q9BZB8-4]
DR Ensembl; ENST00000615198.4; ENSP00000477715.1; ENSG00000214575.10. [Q9BZB8-3]
DR Ensembl; ENST00000616775.4; ENSP00000482116.1; ENSG00000277445.4. [Q9BZB8-2]
DR Ensembl; ENST00000617462.4; ENSP00000477557.1; ENSG00000214575.10. [Q9BZB8-4]
DR Ensembl; ENST00000617522.4; ENSP00000481009.1; ENSG00000214575.10. [Q9BZB8-4]
DR Ensembl; ENST00000618449.4; ENSP00000483590.1; ENSG00000214575.10. [Q9BZB8-2]
DR Ensembl; ENST00000619696.2; ENSP00000482965.2; ENSG00000277445.4. [Q9BZB8-4]
DR Ensembl; ENST00000620182.4; ENSP00000484549.1; ENSG00000214575.10. [Q9BZB8-4]
DR Ensembl; ENST00000620212.4; ENSP00000478558.1; ENSG00000277445.4. [Q9BZB8-4]
DR Ensembl; ENST00000631674.1; ENSP00000488352.1; ENSG00000277445.4. [Q9BZB8-4]
DR Ensembl; ENST00000632526.1; ENSP00000487757.1; ENSG00000277445.4. [Q9BZB8-4]
DR GeneID; 64506; -.
DR KEGG; hsa:64506; -.
DR UCSC; uc002biq.4; human. [Q9BZB8-1]
DR CTD; 64506; -.
DR DisGeNET; 64506; -.
DR GeneCards; CPEB1; -.
DR HGNC; HGNC:21744; CPEB1.
DR HPA; ENSG00000214575; Tissue enhanced (brain, testis).
DR MIM; 607342; gene.
DR neXtProt; NX_Q9BZB8; -.
DR OpenTargets; ENSG00000214575; -.
DR PharmGKB; PA134929879; -.
DR VEuPathDB; HostDB:ENSG00000214575; -.
DR eggNOG; KOG0129; Eukaryota.
DR GeneTree; ENSGT00940000155524; -.
DR HOGENOM; CLU_014948_1_1_1; -.
DR InParanoid; Q9BZB8; -.
DR OMA; CACEECH; -.
DR OrthoDB; 1075356at2759; -.
DR PhylomeDB; Q9BZB8; -.
DR TreeFam; TF317658; -.
DR PathwayCommons; Q9BZB8; -.
DR SignaLink; Q9BZB8; -.
DR BioGRID-ORCS; 64506; 18 hits in 1077 CRISPR screens.
DR ChiTaRS; CPEB1; human.
DR GeneWiki; CPEB1; -.
DR GenomeRNAi; 64506; -.
DR Pharos; Q9BZB8; Tbio.
DR PRO; PR:Q9BZB8; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9BZB8; protein.
DR Bgee; ENSG00000214575; Expressed in C1 segment of cervical spinal cord and 100 other tissues.
DR ExpressionAtlas; Q9BZB8; baseline and differential.
DR Genevisible; Q9BZB8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
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:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:UniProtKB.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; IDA:UniProtKB.
DR CDD; cd12723; RRM1_CPEB1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.640.40; -; 1.
DR InterPro; IPR032292; CEBP1_N.
DR InterPro; IPR032296; CEBP_ZZ.
DR InterPro; IPR038446; CEBP_ZZ_sf.
DR InterPro; IPR034819; CPEB.
DR InterPro; IPR034977; CPEB1_RRM1.
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; PF16368; CEBP1_N; 1.
DR Pfam; PF16366; CEBP_ZZ; 1.
DR Pfam; PF16367; RRM_7; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cell projection; Cytoplasm;
KW Membrane; Metal-binding; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Ribonucleoprotein; RNA-binding;
KW Synapse; Translation regulation; Zinc.
FT CHAIN 1..566
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 1"
FT /id="PRO_0000269251"
FT DOMAIN 311..408
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 430..511
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 162..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..566
FT /note="Necessary for stress granule assembly and correct
FT localization in dcp1 bodies"
FT COMPBIAS 174..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23500490,
FT ECO:0007744|PDB:2M13, ECO:0007744|PDB:2MKE"
FT BINDING 518
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23500490,
FT ECO:0007744|PDB:2M13, ECO:0007744|PDB:2MKE"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23500490,
FT ECO:0007744|PDB:2M13, ECO:0007744|PDB:2MKE"
FT BINDING 532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23500490,
FT ECO:0007744|PDB:2M13, ECO:0007744|PDB:2MKE"
FT BINDING 537
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23500490,
FT ECO:0007744|PDB:2M13, ECO:0007744|PDB:2MKE"
FT BINDING 540
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23500490,
FT ECO:0007744|PDB:2M13, ECO:0007744|PDB:2MKE"
FT BINDING 545
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23500490,
FT ECO:0007744|PDB:2M13, ECO:0007744|PDB:2MKE"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23500490,
FT ECO:0007744|PDB:2M13, ECO:0007744|PDB:2MKE"
FT SITE 411
FT /note="Important for the positionning of RRM1 relative to
FT RRM2"
FT /evidence="ECO:0000269|PubMed:24990967"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 172
FT /note="Phosphothreonine; by AURKA and CAMK2A"
FT /evidence="ECO:0000250|UniProtKB:P70166"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11223249,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_022027"
FT VAR_SEQ 1..5
FT /note="MALSL -> MAFPL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022028"
FT VAR_SEQ 354..358
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_022029"
FT VARIANT 8
FT /note="Missing"
FT /id="VAR_076387"
FT VARIANT 233
FT /note="M -> I"
FT /evidence="ECO:0000269|PubMed:26063658"
FT /id="VAR_076388"
FT MUTAGEN 172
FT /note="T->A: Does not affect its localization."
FT /evidence="ECO:0000269|PubMed:15731006"
FT MUTAGEN 172
FT /note="T->D: Does not affect its localization."
FT /evidence="ECO:0000269|PubMed:15731006"
FT MUTAGEN 314
FT /note="F->A: Abolishes stress granule assembly and correct
FT localization in dcp1 bodies."
FT /evidence="ECO:0000269|PubMed:15731006"
FT MUTAGEN 545
FT /note="H->A: Abolishes stress granule assembly and correct
FT localization in dcp1 bodies."
FT /evidence="ECO:0000269|PubMed:15731006"
FT CONFLICT 446
FT /note="L -> Q (in Ref. 2; BAB14496)"
FT /evidence="ECO:0000305"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:2MKH"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:2MKH"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:2MKH"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:2MKH"
FT HELIX 370..376
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 406..412
FT /evidence="ECO:0007829|PDB:2MKH"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:2MKH"
FT HELIX 443..453
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:2MKK"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:2MKH"
FT HELIX 482..490
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:2MKH"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:2MKH"
FT TURN 508..510
FT /evidence="ECO:0007829|PDB:2M13"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:2M13"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:2M13"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:2M13"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:2M13"
FT HELIX 538..545
FT /evidence="ECO:0007829|PDB:2M13"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:2MKE"
SQ SEQUENCE 566 AA; 62595 MW; 9E41E5B0EC69DA87 CRC64;
MALSLEEEAG RIKDCWDNQE APALSTCSNA NIFRRINAIL DNSLDFSRVC TTPINRGIHD
HLPDFQDSEE TVTSRMLFPT SAQESSRGLP DANDLCLGLQ SLSLTGWDRP WSTQDSDSSA
QSSTHSVLSM LHNPLGNVLG KPPLSFLPLD PLGSDLVDKF PAPSVRGSRL DTRPILDSRS
SSPSDSDTSG FSSGSDHLSD LISSLRISPP LPFLSLSGGG PRDPLKMGVG SRMDQEQAAL
AAVTPSPTSA SKRWPGASVW PSWDLLEAPK DPFSIEREAR LHRQAAAVNE ATCTWSGQLP
PRNYKNPIYS CKVFLGGVPW DITEAGLVNT FRVFGSLSVE WPGKDGKHPR CPPKGNMPKG
YVYLVFELEK SVRSLLQACS HDPLSPDGLS EYYFKMSSRR MRCKEVQVIP WVLADSNFVR
SPSQRLDPSR TVFVGALHGM LNAEALAAIL NDLFGGVVYA GIDTDKHKYP IGSGRVTFNN
QRSYLKAVSA AFVEIKTTKF TKKVQIDPYL EDSLCHICSS QPGPFFCRDQ VCFKYFCRSC
WHWRHSMEGL RHHSPLMRNQ KNRDSS
