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Protein

Cytoplasmic polyadenylation element-binding protein 1

Gene

Cpeb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi514 – 5141Zinc 1By similarity
Metal bindingi517 – 5171Zinc 1By similarity
Metal bindingi526 – 5261Zinc 2By similarity
Metal bindingi531 – 5311Zinc 2By similarity
Metal bindingi536 – 5361Zinc 1By similarity
Metal bindingi539 – 5391Zinc 1By similarity
Metal bindingi544 – 5441Zinc 2By similarity
Metal bindingi552 – 5521Zinc 2By similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to amino acid stimulus Source: UniProtKB
  • cellular response to hypoxia Source: UniProtKB
  • cellular response to insulin stimulus Source: UniProtKB
  • cellular response to lipopolysaccharide Source: RGD
  • mRNA processing Source: UniProtKB-KW
  • mRNA transport Source: RGD
  • negative regulation of cell proliferation Source: RGD
  • negative regulation of cytoplasmic translation Source: UniProtKB
  • negative regulation of translation Source: RGD
  • positive regulation of cell migration Source: RGD
  • positive regulation of neuron projection development Source: RGD
  • positive regulation of nitric-oxide synthase biosynthetic process Source: RGD
  • positive regulation of translation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

mRNA processing, Translation regulation

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic polyadenylation element-binding protein 1
Short name:
CPE-BP1
Short name:
CPE-binding protein 1
Short name:
CPEB
Short name:
CPEB-1
Gene namesi
Name:Cpeb1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1310421. Cpeb1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell junctionsynapse By similarity
  • CytoplasmP-body By similarity
  • Cytoplasmic granule By similarity
  • Membrane By similarity
  • Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity

  • Note: Localizes in synaptosomes at dendritic synapses of neurons. Strongly enriched in postsynaptic density fractions. 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). In P-bodies and stress granules (By similarity). Recruited to stress granules (SGs) upon arsenite treatment (By similarity).By similarity

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • centrosome Source: RGD
  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB-SubCell
  • growth cone Source: RGD
  • neuronal cell body Source: RGD
  • nucleoplasm Source: Ensembl
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: RGD
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Postsynaptic cell membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Cytoplasmic polyadenylation element-binding protein 1PRO_0000269254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphoserineBy similarity
Modified residuei171 – 1711Phosphothreonine; by AURKA and CAMK2ABy similarity

Post-translational modificationi

Phosphorylated on serine/threonine residues by AURKA within positions 165 and 196. Phosphorylation and dephosphorylation on Thr-171 regulates cytoplasmic polyadenylation and translation of CPE-containing mRNAs. Phosphorylation on Thr-171 by AURKA and CAMK2A activates CPEB1. Phosphorylation on Thr-171 may be promoted by APLP1. Phosphorylation increases binding to RNA (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0C279.
PRIDEiP0C279.

PTM databases

iPTMnetiP0C279.
PhosphoSiteiP0C279.

Expressioni

Tissue specificityi

Expressed in hippocampus and cerebral cortex (at protein level). Expressed in hippocampus (dentate gyrus and CA1-CA4 regions), cerebellum (Purkinje cells), cortex, visual cortex (layers 1 and 2), mesencephalon, diencephalon and brain stem.1 Publication

Gene expression databases

ExpressionAtlasiP0C279. baseline and differential.
GenevisibleiP0C279. RN.

Interactioni

Subunit structurei

Interacts with kinesin, dynein, APLP1, APLP2, PAPD4/GLD2 and APP. Both phosphorylated and non phosphorylated forms interact with APLP1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026009.

Structurei

3D structure databases

ProteinModelPortaliP0C279.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini310 – 40798RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini429 – 51082RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni329 – 561233Necessary for stress granule assembly and correct localization in dcp1 bodiesBy similarityAdd
BLAST

Domaini

The 2 RRM domains and the C-terminal region mediate interaction with CPE-containing RNA.By similarity

Sequence similaritiesi

Belongs to the RRM CPEB family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410KDT8. Eukaryota.
ENOG410YBXF. LUCA.
GeneTreeiENSGT00390000012886.
HOGENOMiHOG000290661.
HOVERGENiHBG079080.
InParanoidiP0C279.
KOiK02602.
PhylomeDBiP0C279.
TreeFamiTF317658.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR032292. CEBP1_N.
IPR032296. CEBP_ZZ.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF16368. CEBP1_N. 1 hit.
PF16366. CEBP_ZZ. 1 hit.
PF16367. RRM_7. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C279-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFSLEEESG RIKDCWDNQE VPALSTCSNA NIFRRINAIL DDSLDFSKVC
60 70 80 90 100
TTPINRGIHD QLPDFQDSEE AITSRMLFPT SAQESPRGLP DANGLCLGLQ
110 120 130 140 150
SLSLTGWDRP WSTQDSDSSA QSNTQSVLSM LQNPLGNVLG KTPLSFLSLD
160 170 180 190 200
PLGSDLDKFP APSVRGSRLD TRPILDSRSS SPSDSDTSGF SSGSDHLSDL
210 220 230 240 250
ISSLRISPPL PFLSMTGNGP RDPLKMGVGS RMDQEQAALA AVAPSPTSAP
260 270 280 290 300
KRWPGTSVWP SWDLLGAPKD PFSIEREARL HRQAAAVNEA TCTWSGQLPP
310 320 330 340 350
RNYKNPIYSC KVFLGGVPWD ITEAGLVNTF RVFGSLSVEW PGKDGKHPRC
360 370 380 390 400
PPKGNMPKGY VYLVFELEKS VRALLQACSH DPLSPDGLSE YYFKMSSRRM
410 420 430 440 450
RCKEVQVIPW VLADSNFVWS PSQRLDPSRT VFVGALHGML NAEALAAILN
460 470 480 490 500
DLFGGVVYAG IDTDKHKYPI GSGRVTFNNQ RSYLKAVTAA FVEIKTTKFT
510 520 530 540 550
KKVQIDPYLE DSLCLICSSQ PGPFFCRDQV CFKYFCRSCW HWRHSMEGLR
560
HHSPLMRNQK N
Length:561
Mass (Da):62,062
Last modified:December 12, 2006 - v1
Checksum:iAF890EA7A263FC5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03000812 Genomic DNA. No translation available.
AABR03000839 Genomic DNA. No translation available.
RefSeqiNP_001099746.1. NM_001106276.1.
UniGeneiRn.224485.

Genome annotation databases

EnsembliENSRNOT00000026009; ENSRNOP00000026009; ENSRNOG00000019161.
GeneIDi293056.
KEGGirno:293056.
UCSCiRGD:1310421. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03000812 Genomic DNA. No translation available.
AABR03000839 Genomic DNA. No translation available.
RefSeqiNP_001099746.1. NM_001106276.1.
UniGeneiRn.224485.

3D structure databases

ProteinModelPortaliP0C279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026009.

PTM databases

iPTMnetiP0C279.
PhosphoSiteiP0C279.

Proteomic databases

PaxDbiP0C279.
PRIDEiP0C279.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026009; ENSRNOP00000026009; ENSRNOG00000019161.
GeneIDi293056.
KEGGirno:293056.
UCSCiRGD:1310421. rat.

Organism-specific databases

CTDi64506.
RGDi1310421. Cpeb1.

Phylogenomic databases

eggNOGiENOG410KDT8. Eukaryota.
ENOG410YBXF. LUCA.
GeneTreeiENSGT00390000012886.
HOGENOMiHOG000290661.
HOVERGENiHBG079080.
InParanoidiP0C279.
KOiK02602.
PhylomeDBiP0C279.
TreeFamiTF317658.

Miscellaneous databases

NextBioi635273.
PROiP0C279.

Gene expression databases

ExpressionAtlasiP0C279. baseline and differential.
GenevisibleiP0C279. RN.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR032292. CEBP1_N.
IPR032296. CEBP_ZZ.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF16368. CEBP1_N. 1 hit.
PF16366. CEBP_ZZ. 1 hit.
PF16367. RRM_7. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses."
    Wu L., Wells D., Tay J., Mendis D., Abbott M.-A., Barnitt A., Quinlan E., Heynen A., Fallon J.R., Richter J.D.
    Neuron 21:1129-1139(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCPEB1_RAT
AccessioniPrimary (citable) accession number: P0C279
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: May 11, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.