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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. Required for cell cycle progression, specifically for prophase entry.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei410Important for the positionning of RRM1 relative to RRM2By similarity1
Metal bindingi514Zinc 1By similarity1
Metal bindingi517Zinc 1By similarity1
Metal bindingi526Zinc 2By similarity1
Metal bindingi531Zinc 2By similarity1
Metal bindingi536Zinc 1By similarity1
Metal bindingi539Zinc 1By similarity1
Metal bindingi544Zinc 2; via tele nitrogenBy similarity1
Metal bindingi552Zinc 2; via pros nitrogenBy similarity1

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
  • regulation of neuronal synaptic plasticity Source: RGD
  • regulation of translation Source: RGD
  • synaptonemal complex assembly Source: RGD

Keywordsi

Molecular functionActivator, Repressor, Ribonucleoprotein, RNA-binding
Biological processmRNA processing, Translation regulation
LigandMetal-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1310421. Cpeb1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002692541 – 561Cytoplasmic polyadenylation element-binding protein 1Add BLAST561

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43PhosphoserineBy similarity1
Modified residuei171Phosphothreonine; by AURKA and CAMK2ABy similarity1

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.
PhosphoSitePlusiP0C279.

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

BgeeiENSRNOG00000019161.
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.
SMRiP0C279.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini310 – 407RRM 1PROSITE-ProRule annotationAdd BLAST98
Domaini429 – 510RRM 2PROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni329 – 561Necessary for stress granule assembly and correct localization in dcp1 bodiesBy similarityAdd BLAST233

Domaini

The 2 RRM domains and the C-terminal region mediate interaction with CPE-containing RNA. The interdomain linker (411-429) acts as a hinge to fix the relative orientation of the 2 RRMs. 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. A continuous hydrophobic interface is formed between the 2 RRM.By similarity

Sequence similaritiesi

Belongs to the RRM CPEB family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

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

Family and domain databases

CDDicd12723. RRM1_CPEB1. 1 hit.
InterProiView protein in InterPro
IPR032292. CEBP1_N.
IPR032296. CEBP_ZZ.
IPR034819. CPEB.
IPR034977. CPEB1_RRM1.
IPR035979. RBD_domain_sf.
IPR000504. RRM_dom.
PANTHERiPTHR12566. PTHR12566. 1 hit.
PfamiView protein in Pfam
PF16368. CEBP1_N. 1 hit.
PF16366. CEBP_ZZ. 1 hit.
PF16367. RRM_7. 1 hit.
SMARTiView protein in SMART
SM00360. RRM. 2 hits.
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiView protein in PROSITE
PS50102. RRM. 2 hits.

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.

Similar proteinsi

Entry informationi

Entry nameiCPEB1_RAT
AccessioniPrimary (citable) accession number: P0C279
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: November 22, 2017
This is version 91 of the entry and version 1 of the sequence. See 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