Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Cytoplasmic polyadenylation element-binding protein 1 (CPE-BP1) (CPE-binding protein 1) (h-CPEB) (hCPEB-1)

 CPEB1_HUMAN             Reviewed;         566 AA.
Q9BZB8; B7Z6C6; Q86W46; Q8IV41; Q9BZB7; Q9H8V5;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 135.
RecName: Full=Cytoplasmic polyadenylation element-binding protein 1;
Short=CPE-BP1;
Short=CPE-binding protein 1;
Short=h-CPEB;
Short=hCPEB-1;
Name=CPEB1; Synonyms=CPEB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), RNA-BINDING, AND TISSUE
SPECIFICITY.
TISSUE=Brain, and Ovary;
PubMed=11223249; DOI=10.1016/S0378-1119(00)00588-6;
Welk J.F., Charlesworth A., Smith G.D., MacNicol A.M.;
"Identification and characterization of the gene encoding human
cytoplasmic polyadenylation element binding protein.";
Gene 263:113-120(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Pericardium, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
TISSUE=Brain, and Melanoma;
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).
[5]
FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=15966895; DOI=10.1111/j.1365-2443.2005.00870.x;
Sasayama T., Marumoto T., Kunitoku N., Zhang D., Tamaki N.,
Kohmura E., Saya H., Hirota T.;
"Over-expression of Aurora-A targets cytoplasmic polyadenylation
element binding protein and promotes mRNA polyadenylation of Cdk1 and
cyclin B1.";
Genes Cells 10:627-638(2005).
[6]
FUNCTION, ALTERNATIVE SPLICING, MUTAGENESIS OF THR-172; PHE-314 AND
HIS-545, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15731006; DOI=10.1242/jcs.01692;
Wilczynska A., Aigueperse C., Kress M., Dautry F., Weil D.;
"The translational regulator CPEB1 provides a link between dcp1 bodies
and stress granules.";
J. Cell Sci. 118:981-992(2005).
[7]
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).
[8]
SUBCELLULAR LOCATION.
PubMed=18923137; DOI=10.1091/mbc.E08-09-0904;
Ernoult-Lange M., Wilczynska A., Harper M., Aigueperse C., Dautry F.,
Kress M., Weil D.;
"Nucleocytoplasmic traffic of CPEB1 and accumulation in Crm1 nucleolar
bodies.";
Mol. Biol. Cell 20:176-187(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
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).
[11]
STRUCTURE BY NMR OF 504-566 IN COMPLEX WITH ZINC, AND DOMAIN.
PubMed=23500490; DOI=10.1016/j.jmb.2013.03.009;
Merkel D.J., Wells S.B., Hilburn B.C., Elazzouzi F.,
Perez-Alvarado G.C., Lee B.M.;
"The C-Terminal region of cytoplasmic polyadenylation element binding
protein is a ZZ domain with potential for protein-protein
interactions.";
J. Mol. Biol. 425:2015-2026(2013).
[12]
FUNCTION, STRUCTURE BY NMR OF 294-566 ALONE OR IN COMPLEX WITH RNA AND
IN COMPLEX WITH ZINC, AND DOMAIN.
PubMed=24990967; DOI=10.1101/gad.241133.114;
Afroz T., Skrisovska L., Belloc E., Guillen-Boixet J., Mendez R.,
Allain F.H.;
"A fly trap mechanism provides sequence-specific RNA recognition by
CPEB proteins.";
Genes Dev. 28:1498-1514(2014).
[13]
STRUCTURE BY NMR OF 206-213.
PubMed=26456073; DOI=10.1038/srep14990;
Schelhorn C., Martin-Malpartida P., Sunol D., Macias M.J.;
"Structural Analysis of the Pin1-CPEB1 interaction and its potential
role in CPEB1 degradation.";
Sci. Rep. 5:14990-14990(2015).
[14]
VARIANTS GLU-8 DEL AND ILE-233.
PubMed=26063658; DOI=10.1093/brain/awv155;
Verdura E., Herve D., Scharrer E., del Mar Amador M.,
Guyant-Marechal L., Philippi A., Corlobe A., Bergametti F., Gazal S.,
Prieto-Morin C., Beaufort N., Le Bail B., Viakhireva I., Dichgans M.,
Chabriat H., Haffner C., Tournier-Lasserve E.;
"Heterozygous HTRA1 mutations are associated with autosomal dominant
cerebral small vessel disease.";
Brain 138:2347-2358(2015).
-!- 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 mRNA 3'-UTR. RNA binding results in a clear
conformational change analogous to the Venus fly trap mechanism
(PubMed:24990967). 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 (By similarity). Its
interaction with APLP1 promotes local CPE-containing mRNA
polyadenylation and translation activation (By similarity).
Induces the assembly of stress granules in the absence of stress.
Required for cell cycle progression, specifically for prophase
entry (PubMed:26398195). {ECO:0000250|UniProtKB:P70166,
ECO:0000269|PubMed:15731006, ECO:0000269|PubMed:15966895,
ECO:0000269|PubMed:24990967, ECO:0000269|PubMed:26398195}.
-!- SUBUNIT: Interacts with kinesin, dynein, APLP1, APLP2, PAPD4/GLD2
and APP. Both phosphorylated and non phosphorylated forms interact
with APLP1 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18923137}.
Nucleus {ECO:0000269|PubMed:18923137}. Cytoplasm, P-body.
Cytoplasmic granule. Cell junction, synapse. Membrane. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000250}. Cell projection, dendrite {ECO:0000250}.
Note=Continuously shuttling between nucleus and cytoplasm
(PubMed:18923137). Also found in stress granules. Recruited to
stress granules (SGs) upon arsenite treatment. In dendrites (By
similarity). Localizes in synaptosomes at dendritic synapses of
neurons (By similarity). Strongly enriched in postsynaptic density
(PSD) fractions (By similarity). Transported into dendrites in a
microtubule-dependent fashion and colocalizes in mRNA-containing
particles with TACC3, dynein and kinesin (By similarity).
Membrane-associated (By similarity). Colocalizes at excitatory
synapses with members of the polyadenylation and translation
complex factors (CPSF, APLP1, TACC3, AURKA, SYP, etc.) including
CPE-containing RNAs (By similarity). {ECO:0000250,
ECO:0000269|PubMed:18923137}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=hCPEB long, hCPEBg;
IsoId=Q9BZB8-1; Sequence=Displayed;
Name=2; Synonyms=hCPEB short, hCPEBs;
IsoId=Q9BZB8-2; Sequence=VSP_022027;
Name=3;
IsoId=Q9BZB8-3; Sequence=VSP_022028, VSP_022029;
Name=4;
IsoId=Q9BZB8-4; Sequence=VSP_022027, VSP_022029;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed in immature oocytes,
ovary, brain and heart. Isoform 2 is expressed in brain and heart.
Isoform 3 and isoform 4 are expressed in brain. Expressed in
breast tumors and several tumor cell lines.
{ECO:0000269|PubMed:11223249, ECO:0000269|PubMed:15731006,
ECO:0000269|PubMed:15966895}.
-!- DOMAIN: The 2 RRM domains and the C-terminal region mediate
interaction with CPE-containing RNA (PubMed:24990967). The
interdomain linker (411-429) acts as a hinge to fix the relative
orientation of the 2 RRMs (PubMed:24990967). 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 (PubMed:23500490,
PubMed:24990967). A continuous hydrophobic interface is formed
between the 2 RRMs (PubMed:24990967).
{ECO:0000269|PubMed:23500490, ECO:0000269|PubMed:24990967}.
-!- PTM: Phosphorylated on serine/threonine residues by AURKA within
positions 166 and 197. Phosphorylation and dephosphorylation on
Thr-172 regulates cytoplasmic polyadenylation and translation of
CPE-containing mRNAs. Phosphorylation on Thr-172 by AURKA and
CAMK2A activates CPEB1. Phosphorylation on Thr-172 may be promoted
by APLP1. Phosphorylation increases binding to RNA (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF329402; AAK01239.1; -; mRNA.
EMBL; AF329403; AAK01240.1; -; mRNA.
EMBL; AK023265; BAB14496.1; -; mRNA.
EMBL; AK300105; BAH13212.1; -; mRNA.
EMBL; CH471188; EAW62449.1; -; Genomic_DNA.
EMBL; BC035348; AAH35348.1; -; mRNA.
EMBL; BC050629; AAH50629.1; -; mRNA.
CCDS; CCDS42072.2; -. [Q9BZB8-2]
CCDS; CCDS45329.2; -. [Q9BZB8-3]
CCDS; CCDS45330.2; -. [Q9BZB8-4]
RefSeq; NP_001073001.1; NM_001079533.1. [Q9BZB8-2]
RefSeq; NP_001073002.1; NM_001079534.1. [Q9BZB8-4]
RefSeq; NP_001073003.1; NM_001079535.1. [Q9BZB8-4]
RefSeq; NP_001275748.1; NM_001288819.1. [Q9BZB8-4]
RefSeq; NP_085097.3; NM_030594.4. [Q9BZB8-3]
UniGene; Hs.459132; -.
UniGene; Hs.547988; -.
PDB; 2M13; NMR; -; A=504-566.
PDB; 2MKE; NMR; -; A=506-566.
PDB; 2MKH; NMR; -; A=294-514.
PDB; 2MKK; NMR; -; A=294-510.
PDB; 2N1O; NMR; -; B=206-213.
PDBsum; 2M13; -.
PDBsum; 2MKE; -.
PDBsum; 2MKH; -.
PDBsum; 2MKK; -.
PDBsum; 2N1O; -.
ProteinModelPortal; Q9BZB8; -.
SMR; Q9BZB8; -.
BioGrid; 122202; 12.
IntAct; Q9BZB8; 3.
STRING; 9606.ENSP00000457881; -.
iPTMnet; Q9BZB8; -.
PhosphoSitePlus; Q9BZB8; -.
BioMuta; CPEB1; -.
DMDM; 74762720; -.
MaxQB; Q9BZB8; -.
PaxDb; Q9BZB8; -.
PeptideAtlas; Q9BZB8; -.
PRIDE; Q9BZB8; -.
DNASU; 64506; -.
Ensembl; ENST00000611163; ENSP00000483857; ENSG00000214575. [Q9BZB8-4]
Ensembl; ENST00000615198; ENSP00000477715; ENSG00000214575. [Q9BZB8-3]
Ensembl; ENST00000616775; ENSP00000482116; ENSG00000277445. [Q9BZB8-2]
Ensembl; ENST00000617462; ENSP00000477557; ENSG00000214575. [Q9BZB8-4]
Ensembl; ENST00000617522; ENSP00000481009; ENSG00000214575. [Q9BZB8-4]
Ensembl; ENST00000618449; ENSP00000483590; ENSG00000214575. [Q9BZB8-2]
Ensembl; ENST00000619696; ENSP00000482965; ENSG00000277445. [Q9BZB8-4]
Ensembl; ENST00000620182; ENSP00000484549; ENSG00000214575. [Q9BZB8-4]
Ensembl; ENST00000620212; ENSP00000478558; ENSG00000277445. [Q9BZB8-4]
Ensembl; ENST00000631674; ENSP00000488352; ENSG00000277445. [Q9BZB8-4]
Ensembl; ENST00000632526; ENSP00000487757; ENSG00000277445. [Q9BZB8-4]
GeneID; 64506; -.
KEGG; hsa:64506; -.
UCSC; uc002biq.4; human. [Q9BZB8-1]
CTD; 64506; -.
DisGeNET; 64506; -.
EuPathDB; HostDB:ENSG00000214575.9; -.
GeneCards; CPEB1; -.
HGNC; HGNC:21744; CPEB1.
HPA; HPA040396; -.
MIM; 607342; gene.
neXtProt; NX_Q9BZB8; -.
OpenTargets; ENSG00000214575; -.
PharmGKB; PA134929879; -.
eggNOG; ENOG410ITXD; Eukaryota.
eggNOG; ENOG410YBXF; LUCA.
GeneTree; ENSGT00390000012886; -.
HOGENOM; HOG000290661; -.
HOVERGEN; HBG079080; -.
InParanoid; Q9BZB8; -.
KO; K02602; -.
PhylomeDB; Q9BZB8; -.
TreeFam; TF317658; -.
GeneWiki; CPEB1; -.
GenomeRNAi; 64506; -.
PRO; PR:Q9BZB8; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000214575; -.
CleanEx; HS_CPEB1; -.
ExpressionAtlas; Q9BZB8; baseline and differential.
Genevisible; Q9BZB8; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
GO; GO:0000900; F:translation repressor activity, nucleic acid binding; ISS:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
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.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Cell junction;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Membrane; Metal-binding; mRNA processing; Nucleus; Phosphoprotein;
Polymorphism; Postsynaptic cell membrane; Reference proteome; Repeat;
Repressor; Ribonucleoprotein; RNA-binding; Synapse;
Translation regulation; Zinc.
CHAIN 1 566 Cytoplasmic polyadenylation element-
binding protein 1.
/FTId=PRO_0000269251.
DOMAIN 311 408 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 430 511 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 330 566 Necessary for stress granule assembly and
correct localization in dcp1 bodies.
COMPBIAS 178 217 Ser-rich.
METAL 515 515 Zinc 1. {ECO:0000244|PDB:2M13,
ECO:0000244|PDB:2MKE,
ECO:0000269|PubMed:23500490}.
METAL 518 518 Zinc 1. {ECO:0000244|PDB:2M13,
ECO:0000244|PDB:2MKE,
ECO:0000269|PubMed:23500490}.
METAL 527 527 Zinc 2. {ECO:0000244|PDB:2M13,
ECO:0000244|PDB:2MKE,
ECO:0000269|PubMed:23500490}.
METAL 532 532 Zinc 2. {ECO:0000244|PDB:2M13,
ECO:0000244|PDB:2MKE,
ECO:0000269|PubMed:23500490}.
METAL 537 537 Zinc 1. {ECO:0000244|PDB:2M13,
ECO:0000244|PDB:2MKE,
ECO:0000269|PubMed:23500490}.
METAL 540 540 Zinc 1. {ECO:0000244|PDB:2M13,
ECO:0000244|PDB:2MKE,
ECO:0000269|PubMed:23500490}.
METAL 545 545 Zinc 2; via tele nitrogen.
{ECO:0000244|PDB:2M13,
ECO:0000244|PDB:2MKE,
ECO:0000269|PubMed:23500490}.
METAL 553 553 Zinc 2; via pros nitrogen.
{ECO:0000244|PDB:2M13,
ECO:0000244|PDB:2MKE,
ECO:0000269|PubMed:23500490}.
SITE 411 411 Important for the positionning of RRM1
relative to RRM2.
{ECO:0000269|PubMed:24990967}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 172 172 Phosphothreonine; by AURKA and CAMK2A.
{ECO:0000250|UniProtKB:P70166}.
VAR_SEQ 1 75 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:11223249,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_022027.
VAR_SEQ 1 5 MALSL -> MAFPL (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022028.
VAR_SEQ 354 358 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_022029.
VARIANT 8 8 Missing.
/FTId=VAR_076387.
VARIANT 233 233 M -> I. {ECO:0000269|PubMed:26063658}.
/FTId=VAR_076388.
MUTAGEN 172 172 T->A: Does not affect its localization.
{ECO:0000269|PubMed:15731006}.
MUTAGEN 172 172 T->D: Does not affect its localization.
{ECO:0000269|PubMed:15731006}.
MUTAGEN 314 314 F->A: Abolishes stress granule assembly
and correct localization in dcp1 bodies.
{ECO:0000269|PubMed:15731006}.
MUTAGEN 545 545 H->A: Abolishes stress granule assembly
and correct localization in dcp1 bodies.
{ECO:0000269|PubMed:15731006}.
CONFLICT 446 446 L -> Q (in Ref. 2; BAB14496).
{ECO:0000305}.
STRAND 294 296 {ECO:0000244|PDB:2MKH}.
STRAND 309 316 {ECO:0000244|PDB:2MKH}.
HELIX 324 331 {ECO:0000244|PDB:2MKH}.
HELIX 332 334 {ECO:0000244|PDB:2MKH}.
STRAND 337 340 {ECO:0000244|PDB:2MKH}.
TURN 342 345 {ECO:0000244|PDB:2MKH}.
STRAND 361 366 {ECO:0000244|PDB:2MKH}.
HELIX 370 376 {ECO:0000244|PDB:2MKH}.
STRAND 379 384 {ECO:0000244|PDB:2MKH}.
STRAND 387 389 {ECO:0000244|PDB:2MKH}.
STRAND 391 394 {ECO:0000244|PDB:2MKH}.
STRAND 399 401 {ECO:0000244|PDB:2MKH}.
STRAND 406 412 {ECO:0000244|PDB:2MKH}.
HELIX 413 415 {ECO:0000244|PDB:2MKH}.
STRAND 417 420 {ECO:0000244|PDB:2MKH}.
STRAND 431 436 {ECO:0000244|PDB:2MKH}.
HELIX 443 453 {ECO:0000244|PDB:2MKH}.
STRAND 458 462 {ECO:0000244|PDB:2MKH}.
STRAND 466 470 {ECO:0000244|PDB:2MKK}.
STRAND 472 477 {ECO:0000244|PDB:2MKH}.
STRAND 479 481 {ECO:0000244|PDB:2MKH}.
HELIX 482 490 {ECO:0000244|PDB:2MKH}.
STRAND 492 496 {ECO:0000244|PDB:2MKH}.
STRAND 501 507 {ECO:0000244|PDB:2MKH}.
TURN 508 510 {ECO:0000244|PDB:2M13}.
TURN 516 518 {ECO:0000244|PDB:2M13}.
STRAND 524 527 {ECO:0000244|PDB:2M13}.
TURN 530 532 {ECO:0000244|PDB:2M13}.
STRAND 534 536 {ECO:0000244|PDB:2M13}.
HELIX 538 545 {ECO:0000244|PDB:2M13}.
HELIX 548 550 {ECO:0000244|PDB:2MKE}.
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


Related products :

Catalog number Product name Quantity
EIAAB09043 CPEB,CPEB1,CPE-binding protein 1,CPE-BP1,Cytoplasmic polyadenylation element-binding protein 1,h-CEBP,hCPEB-1,Homo sapiens,Human
EIAAB09042 CPEB,Cpeb1,CPEB-1,CPE-binding protein 1,CPE-BP1,Cytoplasmic polyadenylation element-binding protein 1,Rat,Rattus norvegicus
29-521 CPEB2 is highly similar to cytoplasmic polyadenylation element binding protein (CPEB), an mRNA-binding protein that regulates cytoplasmic polyadenylation of mRNA as a trans factor in oogenesis and spe 0.1 mg
29-520 CPEB2 is highly similar to cytoplasmic polyadenylation element binding protein (CPEB), an mRNA-binding protein that regulates cytoplasmic polyadenylation of mRNA as a trans factor in oogenesis and spe 0.05 mg
29-519 CPEB2 is highly similar to cytoplasmic polyadenylation element binding protein (CPEB), an mRNA-binding protein that regulates cytoplasmic polyadenylation of mRNA as a trans factor in oogenesis and spe 0.05 mg
EIAAB09044 CPEB2,CPE-binding protein 2,CPE-BP2,Cytoplasmic polyadenylation element-binding protein 2,hCPEB-2,Homo sapiens,Human
EIAAB09049 CPEB4,CPE-binding protein 4,CPE-BP4,Cytoplasmic polyadenylation element-binding protein 4,hCPEB-4,Homo sapiens,Human,KIAA1673
EIAAB09047 CPEB3,CPE-binding protein 3,CPE-BP3,Cytoplasmic polyadenylation element-binding protein 3,hCPEB-3,Homo sapiens,Human,KIAA0940
EIAAB09041 Cpeb,Cpeb1,CPE-binding protein 1,CPE-BP1,Cytoplasmic polyadenylation element-binding protein 1,mCPEB,mCPEB-1,Mouse,Mus musculus
EIAAB09048 Cpeb4,CPE-binding protein 4,CPE-BP4,Cytoplasmic polyadenylation element-binding protein 4,Kiaa1673,mCPEB-4,Mouse,Mus musculus
EIAAB09046 Cpeb3,CPE-binding protein 3,CPE-BP3,Cytoplasmic polyadenylation element-binding protein 3,Kiaa0940,mCPEB-3,Mouse,Mus musculus
EIAAB09045 Cpeb2,CPE-binding protein 2,CPE-BP2,Cytoplasmic polyadenylation element-binding protein 2,mCPEB-2,Mouse,Mus musculus
4687 (NT) Cytoplasmic polyadenylation element-binding protein 1 0.5 mg
4687 (NT) Cytoplasmic polyadenylation element-binding protein 1 0.1 mg
CPEB1_RAT Rat ELISA Kit FOR Cytoplasmic polyadenylation element-binding protein 1 96T
CPEB4 CPEB2 Gene cytoplasmic polyadenylation element binding protein 2
CPLX2 CPEB4 Gene cytoplasmic polyadenylation element binding protein 4
CPLX1 CPEB3 Gene cytoplasmic polyadenylation element binding protein 3
CPEB1_MOUSE Mouse ELISA Kit FOR Cytoplasmic polyadenylation element-binding protein 1 96T
CSB-EL005887RA Rat Cytoplasmic polyadenylation element-binding protein 1(CPEB1) ELISA kit 96T
CPEB3 CPEB1 Gene cytoplasmic polyadenylation element binding protein 1
CPEB2_MOUSE Mouse ELISA Kit FOR Cytoplasmic polyadenylation element-binding protein 2 96T
E0933h Mouse ELISA Kit FOR Cytoplasmic polyadenylation element-binding protein 3 96T
CSB-EL005888MO Mouse Cytoplasmic polyadenylation element-binding protein 2(CPEB2) ELISA kit 96T
CSB-EL005890HU Human Cytoplasmic polyadenylation element-binding protein 4(CPEB4) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur