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Cytoplasmic polyadenylation element-binding protein 4 (CPE-BP4) (CPE-binding protein 4) (hCPEB-4)

 CPEB4_HUMAN             Reviewed;         729 AA.
Q17RY0; B7ZLQ7; Q7Z310; Q8N405; Q9C0J0;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
25-JUL-2006, sequence version 1.
25-APR-2018, entry version 103.
RecName: Full=Cytoplasmic polyadenylation element-binding protein 4;
Short=CPE-BP4;
Short=CPE-binding protein 4;
Short=hCPEB-4;
Name=CPEB4; Synonyms=KIAA1673;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Brain, and Lymphoma;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252; SER-255 AND
THR-326, AND 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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252; SER-255; SER-330
AND SER-332, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[7]
INTERACTION WITH TOB1.
PubMed=21336257; DOI=10.1038/emboj.2011.37;
Hosoda N., Funakoshi Y., Hirasawa M., Yamagishi R., Asano Y.,
Miyagawa R., Ogami K., Tsujimoto M., Hoshino S.;
"Anti-proliferative protein Tob negatively regulates CPEB3 target by
recruiting Caf1 deadenylase.";
EMBO J. 30:1311-1323(2011).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22138752; DOI=10.1038/nm.2540;
Ortiz-Zapater E., Pineda D., Martinez-Bosch N., Fernandez-Miranda G.,
Iglesias M., Alameda F., Moreno M., Eliscovich C., Eyras E.,
Real F.X., Mendez R., Navarro P.;
"Key contribution of CPEB4-mediated translational control to cancer
progression.";
Nat. Med. 18:83-90(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-99 AND SER-332,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-99 AND SER-137,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
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).
[12]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=27857118; DOI=10.1038/ncomms13418;
Perez-Guijarro E., Karras P., Cifdaloz M., Martinez-Herranz R.,
Canon E., Grana O., Horcajada-Reales C., Alonso-Curbelo D.,
Calvo T.G., Gomez-Lopez G., Bellora N., Riveiro-Falkenbach E.,
Ortiz-Romero P.L., Rodriguez-Peralto J.L., Maestre L., Roncador G.,
de Agustin Asensio J.C., Goding C.R., Eyras E., Megias D., Mendez R.,
Soengas M.S.;
"Lineage-specific roles of the cytoplasmic polyadenylation factor
CPEB4 in the regulation of melanoma drivers.";
Nat. Commun. 7:13418-13418(2016).
[13]
FUNCTION, STRUCTURE BY NMR OF 460-662 ALONE OR IN COMPLEX WITH RNA AND
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).
[14]
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 379-393.
PubMed=26349033; DOI=10.7554/eLife.10034;
Fung H.Y., Fu S.C., Brautigam C.A., Chook Y.M.;
"Structural determinants of nuclear export signal orientation in
binding to exportin CRM1.";
Elife 4:0-0(2015).
-!- FUNCTION: Sequence-specific RNA-binding protein that binds to the
cytoplasmic polyadenylation element (CPE), an uridine-rich
sequence element (consensus sequence 5'-UUUUUAU-3') within the
mRNA 3'-UTR (PubMed:24990967). RNA binding results in a clear
conformational change analogous to the Venus fly trap mechanism
(PubMed:24990967). Regulates activation of unfolded protein
response (UPR) in the process of adaptation to ER stress in liver,
by maintaining translation of CPE-regulated mRNAs in conditions in
which global protein synthesis is inhibited (By similarity).
Required for cell cycle progression, specifically for cytokinesis
and chromosomal segregation (PubMed:26398195). Plays a role as an
oncogene promoting tumor growth and progression by positively
regulating translation of t-plasminogen activator/PLAT
(PubMed:22138752). Stimulates proliferation of melanocytes
(PubMed:27857118). In contrast to CPEB1 and CPEB3, does not play
role in synaptic plasticity, learning and memory (By similarity).
{ECO:0000250|UniProtKB:Q7TN98, ECO:0000269|PubMed:22138752,
ECO:0000269|PubMed:24990967, ECO:0000269|PubMed:26398195,
ECO:0000269|PubMed:27857118}.
-!- SUBUNIT: Interacts with TOB1. {ECO:0000269|PubMed:21336257}.
-!- INTERACTION:
P50616:TOB1; NbExp=2; IntAct=EBI-2848203, EBI-723281;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7TN98}.
Cell projection, dendrite {ECO:0000250|UniProtKB:Q7TN98}. Cell
projection, dendritic spine {ECO:0000250|UniProtKB:Q7TN98}. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, axon
{ECO:0000250|UniProtKB:Q7TN98}. Cell projection, growth cone
{ECO:0000250|UniProtKB:Q7TN98}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q7TN98}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:Q7TN98}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q17RY0-1; Sequence=Displayed;
Name=2;
IsoId=Q17RY0-2; Sequence=VSP_022041;
Name=3;
IsoId=Q17RY0-3; Sequence=VSP_022040, VSP_022042;
-!- TISSUE SPECIFICITY: Expressed in pancreas in islets and ductal
cells (at protein level) (PubMed:22138752). Expressed in
melanocytes (PubMed:27857118). {ECO:0000269|PubMed:22138752,
ECO:0000269|PubMed:27857118}.
-!- DOMAIN: The 2 RRM domains and the C-terminal region mediate
interaction with CPE-containing RNA (PubMed:24990967). The
interdomain linker (564-579) 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 (By similarity). Unlike in
CPEB1, a continuous polar interface is formed between the 2 RRMs
(PubMed:24990967). {ECO:0000250|UniProtKB:Q9BZB8,
ECO:0000269|PubMed:24990967}.
-!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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EMBL; AB051460; BAB21764.1; -; mRNA.
EMBL; BX538213; CAD98072.1; -; mRNA.
EMBL; CH471062; EAW61392.1; -; Genomic_DNA.
EMBL; BC036899; AAH36899.1; -; mRNA.
EMBL; BC117150; AAI17151.1; -; mRNA.
EMBL; BC143958; AAI43959.1; -; mRNA.
CCDS; CCDS4390.1; -. [Q17RY0-1]
CCDS; CCDS78086.1; -. [Q17RY0-2]
CCDS; CCDS83044.1; -. [Q17RY0-3]
RefSeq; NP_001295118.1; NM_001308189.1. [Q17RY0-2]
RefSeq; NP_001295120.1; NM_001308191.1.
RefSeq; NP_001295121.1; NM_001308192.1.
RefSeq; NP_001295122.1; NM_001308193.1. [Q17RY0-3]
RefSeq; NP_085130.2; NM_030627.3. [Q17RY0-1]
UniGene; Hs.127126; -.
UniGene; Hs.127874; -.
PDB; 2MKI; NMR; -; A=460-662.
PDB; 2MKJ; NMR; -; A=460-662.
PDB; 5DIF; X-ray; 2.09 A; D=379-393.
PDBsum; 2MKI; -.
PDBsum; 2MKJ; -.
PDBsum; 5DIF; -.
ProteinModelPortal; Q17RY0; -.
SMR; Q17RY0; -.
BioGrid; 123228; 4.
IntAct; Q17RY0; 6.
MINT; Q17RY0; -.
STRING; 9606.ENSP00000265085; -.
iPTMnet; Q17RY0; -.
PhosphoSitePlus; Q17RY0; -.
BioMuta; CPEB4; -.
DMDM; 119368635; -.
MaxQB; Q17RY0; -.
PaxDb; Q17RY0; -.
PeptideAtlas; Q17RY0; -.
PRIDE; Q17RY0; -.
Ensembl; ENST00000265085; ENSP00000265085; ENSG00000113742. [Q17RY0-1]
Ensembl; ENST00000334035; ENSP00000334533; ENSG00000113742. [Q17RY0-2]
Ensembl; ENST00000517880; ENSP00000427990; ENSG00000113742. [Q17RY0-3]
GeneID; 80315; -.
KEGG; hsa:80315; -.
UCSC; uc003mcs.5; human. [Q17RY0-1]
CTD; 80315; -.
DisGeNET; 80315; -.
EuPathDB; HostDB:ENSG00000113742.12; -.
GeneCards; CPEB4; -.
HGNC; HGNC:21747; CPEB4.
HPA; HPA038394; -.
MIM; 610607; gene.
neXtProt; NX_Q17RY0; -.
OpenTargets; ENSG00000113742; -.
PharmGKB; PA134869176; -.
eggNOG; KOG0129; Eukaryota.
eggNOG; ENOG410Y1XZ; LUCA.
GeneTree; ENSGT00390000012886; -.
HOVERGEN; HBG058010; -.
InParanoid; Q17RY0; -.
KO; K02602; -.
OMA; CFPHQNG; -.
OrthoDB; EOG091G0AO9; -.
PhylomeDB; Q17RY0; -.
TreeFam; TF317658; -.
ChiTaRS; CPEB4; human.
GenomeRNAi; 80315; -.
PRO; PR:Q17RY0; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113742; -.
CleanEx; HS_CPEB4; -.
ExpressionAtlas; Q17RY0; baseline and differential.
Genevisible; Q17RY0; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
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:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
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:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
GO; GO:0000900; F:translation repressor activity, mRNA regulatory element binding; IBA:GO_Central.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
GO; GO:0036294; P:cellular response to decreased oxygen levels; ISS:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; IBA:GO_Central.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
Gene3D; 3.30.40.130; -; 1.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR032296; CEBP_ZZ.
InterPro; IPR038446; CEBP_ZZ_sf.
InterPro; IPR034819; CPEB.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR12566; PTHR12566; 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;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Endoplasmic reticulum;
Membrane; Metal-binding; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Repeat; RNA-binding; Synapse; Zinc.
CHAIN 1 729 Cytoplasmic polyadenylation element-
binding protein 4.
/FTId=PRO_0000269264.
DOMAIN 472 563 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 580 662 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 1 375 Low complexity region. {ECO:0000305}.
REGION 541 543 RNA-binding. {ECO:0000244|PDB:5DIF}.
COMPBIAS 232 246 His-rich.
COMPBIAS 302 311 Poly-Gly.
METAL 667 667 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 675 675 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 684 684 Zinc 2. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 689 689 Zinc 2. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 694 694 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 697 697 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 702 702 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9BZB8}.
METAL 710 710 Zinc 2; via pros nitrogen.
{ECO:0000250|UniProtKB:Q9BZB8}.
SITE 473 473 RNA-binding. {ECO:0000244|PDB:5DIF}.
SITE 561 561 Important for the positionning of RRM1
relative to RRM2.
{ECO:0000269|PubMed:24990967}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 326 326 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 382 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022040.
VAR_SEQ 403 419 Missing (in isoform 2).
{ECO:0000303|PubMed:11214970,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_022041.
VAR_SEQ 404 428 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022042.
CONFLICT 228 228 P -> L (in Ref. 2; CAD98072).
{ECO:0000305}.
HELIX 384 391 {ECO:0000244|PDB:5DIF}.
STRAND 472 477 {ECO:0000244|PDB:2MKI}.
HELIX 485 491 {ECO:0000244|PDB:2MKI}.
HELIX 492 495 {ECO:0000244|PDB:2MKI}.
STRAND 499 501 {ECO:0000244|PDB:2MKI}.
TURN 507 509 {ECO:0000244|PDB:2MKJ}.
STRAND 514 516 {ECO:0000244|PDB:2MKI}.
STRAND 518 521 {ECO:0000244|PDB:2MKI}.
HELIX 527 533 {ECO:0000244|PDB:2MKI}.
STRAND 534 538 {ECO:0000244|PDB:2MKI}.
STRAND 541 544 {ECO:0000244|PDB:2MKI}.
STRAND 556 560 {ECO:0000244|PDB:2MKI}.
STRAND 563 572 {ECO:0000244|PDB:2MKI}.
STRAND 580 586 {ECO:0000244|PDB:2MKI}.
STRAND 589 591 {ECO:0000244|PDB:2MKJ}.
HELIX 593 603 {ECO:0000244|PDB:2MKI}.
STRAND 607 615 {ECO:0000244|PDB:2MKI}.
TURN 616 619 {ECO:0000244|PDB:2MKI}.
STRAND 620 631 {ECO:0000244|PDB:2MKI}.
HELIX 632 638 {ECO:0000244|PDB:2MKI}.
STRAND 639 643 {ECO:0000244|PDB:2MKI}.
STRAND 645 648 {ECO:0000244|PDB:2MKJ}.
STRAND 651 653 {ECO:0000244|PDB:2MKJ}.
STRAND 656 659 {ECO:0000244|PDB:2MKI}.
SEQUENCE 729 AA; 80152 MW; B71AAB0650E8CB13 CRC64;
MGDYGFGVLV QSNTGNKSAF PVRFHPHLQP PHHHQNATPS PAAFINNNTA ANGSSAGSAW
LFPAPATHNI QDEILGSEKA KSQQQEQQDP LEKQQLSPSP GQEAGILPET EKAKSEENQG
DNSSENGNGK EKIRIESPVL TGFDYQEATG LGTSTQPLTS SASSLTGFSN WSAAIAPSSS
TIINEDASFF HQGGVPAASA NNGALLFQNF PHHVSPGFGG SFSPQIGPLS QHHPHHPHFQ
HHHSQHQQQR RSPASPHPPP FTHRNAAFNQ LPHLANNLNK PPSPWSSYQS PSPTPSSSWS
PGGGGYGGWG GSQGRDHRRG LNGGITPLNS ISPLKKNFAS NHIQLQKYAR PSSAFAPKSW
MEDSLNRADN IFPFPDRPRT FDMHSLESSL IDIMRAENDT IKGRLNYSYP GSDSSLLINA
RTYGRRRGQS SLFPMEDGFL DDGRGDQPLH SGLGSPHCFS HQNGERVERY SRKVFVGGLP
PDIDEDEITA SFRRFGPLIV DWPHKAESKS YFPPKGYAFL LFQDESSVQA LIDACIEEDG
KLYLCVSSPT IKDKPVQIRP WNLSDSDFVM DGSQPLDPRK TIFVGGVPRP LRAVELAMIM
DRLYGGVCYA GIDTDPELKY PKGAGRVAFS NQQSYIAAIS ARFVQLQHGE IDKRVEVKPY
VLDDQLCDEC QGARCGGKFA PFFCANVTCL QYYCEYCWAA IHSRAGREFH KPLVKEGGDR
PRHISFRWN


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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
EIAAB09046 Cpeb3,CPE-binding protein 3,CPE-BP3,Cytoplasmic polyadenylation element-binding protein 3,Kiaa0940,mCPEB-3,Mouse,Mus musculus
EIAAB09048 Cpeb4,CPE-binding protein 4,CPE-BP4,Cytoplasmic polyadenylation element-binding protein 4,Kiaa1673,mCPEB-4,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 0.1 mg
4687 (NT) Cytoplasmic polyadenylation element-binding protein 1 0.5 mg
EIAAB09041 Cpeb,Cpeb1,CPE-binding protein 1,CPE-BP1,Cytoplasmic polyadenylation element-binding protein 1,mCPEB,mCPEB-1,Mouse,Mus musculus
EIAAB09042 CPEB,Cpeb1,CPEB-1,CPE-binding protein 1,CPE-BP1,Cytoplasmic polyadenylation element-binding protein 1,Rat,Rattus norvegicus
CPEB1_RAT Rat ELISA Kit FOR Cytoplasmic polyadenylation element-binding protein 1 96T
CPLX2 CPEB4 Gene cytoplasmic polyadenylation element binding protein 4
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
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
CPEB4 CPEB2 Gene cytoplasmic polyadenylation element binding protein 2
CSB-EL005888HU Human Cytoplasmic polyadenylation element-binding protein 2(CPEB2) ELISA kit 96T
CSB-EL005890MO Mouse Cytoplasmic polyadenylation element-binding protein 4(CPEB4) ELISA kit 96T


 

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