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Protein

Cytoplasmic polyadenylation element-binding protein 1

Gene

CPEB1

Organism
Homo sapiens (Human)
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 mRNA 3'-UTR. 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.By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi515Zinc 11 Publication1
Metal bindingi518Zinc 11 Publication1
Metal bindingi527Zinc 21 Publication1
Metal bindingi532Zinc 21 Publication1
Metal bindingi537Zinc 11 Publication1
Metal bindingi540Zinc 11 Publication1
Metal bindingi545Zinc 21 Publication1
Metal bindingi553Zinc 21 Publication1

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
  • mRNA processing Source: UniProtKB-KW
  • negative regulation of cytoplasmic translation Source: UniProtKB
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:
h-CPEB
Short name:
hCPEB-1
Gene namesi
Name:CPEB1
Synonyms:CPEB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:21744. CPEB1.

Subcellular locationi

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

  • Note: 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi172T → A: Does not affect its localization. 1 Publication1
Mutagenesisi172T → D: Does not affect its localization. 1 Publication1
Mutagenesisi314F → A: Abolishes stress granule assembly and correct localization in dcp1 bodies. 1 Publication1
Mutagenesisi545H → A: Abolishes stress granule assembly and correct localization in dcp1 bodies. 1 Publication1

Organism-specific databases

DisGeNETi64506.
OpenTargetsiENSG00000214575.
ENSG00000277445.
PharmGKBiPA134929879.

Polymorphism and mutation databases

BioMutaiCPEB1.
DMDMi74762720.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002692511 – 566Cytoplasmic polyadenylation element-binding protein 1Add BLAST566

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43PhosphoserineCombined sources1
Modified residuei172Phosphothreonine; by AURKA and CAMK2ABy similarity1

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BZB8.
PaxDbiQ9BZB8.
PeptideAtlasiQ9BZB8.
PRIDEiQ9BZB8.

PTM databases

iPTMnetiQ9BZB8.
PhosphoSitePlusiQ9BZB8.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiENSG00000214575.
CleanExiHS_CPEB1.
ExpressionAtlasiQ9BZB8. baseline and differential.
GenevisibleiQ9BZB8. HS.

Organism-specific databases

HPAiHPA044113.

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

BioGridi122202. 12 interactors.
IntActiQ9BZB8. 3 interactors.
STRINGi9606.ENSP00000457881.

Structurei

Secondary structure

1566
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi294 – 296Combined sources3
Beta strandi309 – 316Combined sources8
Helixi324 – 331Combined sources8
Helixi332 – 334Combined sources3
Beta strandi337 – 340Combined sources4
Turni342 – 345Combined sources4
Beta strandi361 – 366Combined sources6
Helixi370 – 376Combined sources7
Beta strandi379 – 384Combined sources6
Beta strandi387 – 389Combined sources3
Beta strandi391 – 394Combined sources4
Beta strandi399 – 401Combined sources3
Beta strandi406 – 412Combined sources7
Helixi413 – 415Combined sources3
Beta strandi417 – 420Combined sources4
Beta strandi431 – 436Combined sources6
Helixi443 – 453Combined sources11
Beta strandi458 – 462Combined sources5
Beta strandi466 – 470Combined sources5
Beta strandi472 – 477Combined sources6
Beta strandi479 – 481Combined sources3
Helixi482 – 490Combined sources9
Beta strandi492 – 496Combined sources5
Beta strandi501 – 507Combined sources7
Turni508 – 510Combined sources3
Turni516 – 518Combined sources3
Beta strandi524 – 527Combined sources4
Turni530 – 532Combined sources3
Beta strandi534 – 536Combined sources3
Helixi538 – 545Combined sources8
Helixi548 – 550Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M13NMR-A504-566[»]
2MKENMR-A506-566[»]
2MKHNMR-A294-514[»]
2MKKNMR-A294-510[»]
2N1ONMR-B206-213[»]
ProteinModelPortaliQ9BZB8.
SMRiQ9BZB8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini311 – 408RRM 1PROSITE-ProRule annotationAdd BLAST98
Domaini430 – 511RRM 2PROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni330 – 566Necessary for stress granule assembly and correct localization in dcp1 bodiesAdd BLAST237

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi178 – 217Ser-richAdd BLAST40

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

eggNOGiENOG410ITXD. Eukaryota.
ENOG410YBXF. LUCA.
GeneTreeiENSGT00390000012886.
HOGENOMiHOG000290661.
HOVERGENiHBG079080.
InParanoidiQ9BZB8.
KOiK02602.
PhylomeDBiQ9BZB8.
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]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BZB8-1) [UniParc]FASTAAdd to basket
Also known as: hCPEB long, hCPEBg

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALSLEEEAG RIKDCWDNQE APALSTCSNA NIFRRINAIL DNSLDFSRVC
60 70 80 90 100
TTPINRGIHD HLPDFQDSEE TVTSRMLFPT SAQESSRGLP DANDLCLGLQ
110 120 130 140 150
SLSLTGWDRP WSTQDSDSSA QSSTHSVLSM LHNPLGNVLG KPPLSFLPLD
160 170 180 190 200
PLGSDLVDKF PAPSVRGSRL DTRPILDSRS SSPSDSDTSG FSSGSDHLSD
210 220 230 240 250
LISSLRISPP LPFLSLSGGG PRDPLKMGVG SRMDQEQAAL AAVTPSPTSA
260 270 280 290 300
SKRWPGASVW PSWDLLEAPK DPFSIEREAR LHRQAAAVNE ATCTWSGQLP
310 320 330 340 350
PRNYKNPIYS CKVFLGGVPW DITEAGLVNT FRVFGSLSVE WPGKDGKHPR
360 370 380 390 400
CPPKGNMPKG YVYLVFELEK SVRSLLQACS HDPLSPDGLS EYYFKMSSRR
410 420 430 440 450
MRCKEVQVIP WVLADSNFVR SPSQRLDPSR TVFVGALHGM LNAEALAAIL
460 470 480 490 500
NDLFGGVVYA GIDTDKHKYP IGSGRVTFNN QRSYLKAVSA AFVEIKTTKF
510 520 530 540 550
TKKVQIDPYL EDSLCHICSS QPGPFFCRDQ VCFKYFCRSC WHWRHSMEGL
560
RHHSPLMRNQ KNRDSS
Length:566
Mass (Da):62,595
Last modified:June 1, 2001 - v1
Checksum:i9E41E5B0EC69DA87
GO
Isoform 2 (identifier: Q9BZB8-2) [UniParc]FASTAAdd to basket
Also known as: hCPEB short, hCPEBs

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: Missing.

Show »
Length:491
Mass (Da):54,162
Checksum:i561A40FEBD482262
GO
Isoform 3 (identifier: Q9BZB8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MALSL → MAFPL
     354-358: Missing.

Show »
Length:561
Mass (Da):62,111
Checksum:iDCE6E16D700DD14E
GO
Isoform 4 (identifier: Q9BZB8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: Missing.
     354-358: Missing.

Show »
Length:486
Mass (Da):53,635
Checksum:i19FA96CE00D0B9FE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti446L → Q in BAB14496 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0763878Missing .1
Natural variantiVAR_076388233M → I.1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0220271 – 75Missing in isoform 2 and isoform 4. 3 PublicationsAdd BLAST75
Alternative sequenceiVSP_0220281 – 5MALSL → MAFPL in isoform 3. 1 Publication5
Alternative sequenceiVSP_022029354 – 358Missing in isoform 3 and isoform 4. 2 Publications5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF329402 mRNA. Translation: AAK01239.1.
AF329403 mRNA. Translation: AAK01240.1.
AK023265 mRNA. Translation: BAB14496.1.
AK300105 mRNA. Translation: BAH13212.1.
CH471188 Genomic DNA. Translation: EAW62449.1.
BC035348 mRNA. Translation: AAH35348.1.
BC050629 mRNA. Translation: AAH50629.1.
CCDSiCCDS42072.2. [Q9BZB8-2]
CCDS45329.2. [Q9BZB8-3]
CCDS45330.2. [Q9BZB8-4]
RefSeqiNP_001073001.1. NM_001079533.1. [Q9BZB8-2]
NP_001073002.1. NM_001079534.1. [Q9BZB8-4]
NP_001073003.1. NM_001079535.1. [Q9BZB8-4]
NP_001275748.1. NM_001288819.1. [Q9BZB8-4]
NP_085097.3. NM_030594.4. [Q9BZB8-3]
UniGeneiHs.459132.
Hs.547988.

Genome annotation databases

EnsembliENST00000611163; ENSP00000483857; ENSG00000214575. [Q9BZB8-4]
ENST00000615198; ENSP00000477715; ENSG00000214575. [Q9BZB8-3]
ENST00000616775; ENSP00000482116; ENSG00000277445. [Q9BZB8-2]
ENST00000617462; ENSP00000477557; ENSG00000214575. [Q9BZB8-4]
ENST00000617522; ENSP00000481009; ENSG00000214575. [Q9BZB8-4]
ENST00000618449; ENSP00000483590; ENSG00000214575. [Q9BZB8-2]
ENST00000619696; ENSP00000482965; ENSG00000277445. [Q9BZB8-4]
ENST00000620182; ENSP00000484549; ENSG00000214575. [Q9BZB8-4]
ENST00000620212; ENSP00000478558; ENSG00000277445. [Q9BZB8-4]
ENST00000631674; ENSP00000488352; ENSG00000277445. [Q9BZB8-4]
ENST00000632526; ENSP00000487757; ENSG00000277445. [Q9BZB8-4]
GeneIDi64506.
KEGGihsa:64506.
UCSCiuc002biq.4. human. [Q9BZB8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF329402 mRNA. Translation: AAK01239.1.
AF329403 mRNA. Translation: AAK01240.1.
AK023265 mRNA. Translation: BAB14496.1.
AK300105 mRNA. Translation: BAH13212.1.
CH471188 Genomic DNA. Translation: EAW62449.1.
BC035348 mRNA. Translation: AAH35348.1.
BC050629 mRNA. Translation: AAH50629.1.
CCDSiCCDS42072.2. [Q9BZB8-2]
CCDS45329.2. [Q9BZB8-3]
CCDS45330.2. [Q9BZB8-4]
RefSeqiNP_001073001.1. NM_001079533.1. [Q9BZB8-2]
NP_001073002.1. NM_001079534.1. [Q9BZB8-4]
NP_001073003.1. NM_001079535.1. [Q9BZB8-4]
NP_001275748.1. NM_001288819.1. [Q9BZB8-4]
NP_085097.3. NM_030594.4. [Q9BZB8-3]
UniGeneiHs.459132.
Hs.547988.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M13NMR-A504-566[»]
2MKENMR-A506-566[»]
2MKHNMR-A294-514[»]
2MKKNMR-A294-510[»]
2N1ONMR-B206-213[»]
ProteinModelPortaliQ9BZB8.
SMRiQ9BZB8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122202. 12 interactors.
IntActiQ9BZB8. 3 interactors.
STRINGi9606.ENSP00000457881.

PTM databases

iPTMnetiQ9BZB8.
PhosphoSitePlusiQ9BZB8.

Polymorphism and mutation databases

BioMutaiCPEB1.
DMDMi74762720.

Proteomic databases

MaxQBiQ9BZB8.
PaxDbiQ9BZB8.
PeptideAtlasiQ9BZB8.
PRIDEiQ9BZB8.

Protocols and materials databases

DNASUi64506.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000611163; ENSP00000483857; ENSG00000214575. [Q9BZB8-4]
ENST00000615198; ENSP00000477715; ENSG00000214575. [Q9BZB8-3]
ENST00000616775; ENSP00000482116; ENSG00000277445. [Q9BZB8-2]
ENST00000617462; ENSP00000477557; ENSG00000214575. [Q9BZB8-4]
ENST00000617522; ENSP00000481009; ENSG00000214575. [Q9BZB8-4]
ENST00000618449; ENSP00000483590; ENSG00000214575. [Q9BZB8-2]
ENST00000619696; ENSP00000482965; ENSG00000277445. [Q9BZB8-4]
ENST00000620182; ENSP00000484549; ENSG00000214575. [Q9BZB8-4]
ENST00000620212; ENSP00000478558; ENSG00000277445. [Q9BZB8-4]
ENST00000631674; ENSP00000488352; ENSG00000277445. [Q9BZB8-4]
ENST00000632526; ENSP00000487757; ENSG00000277445. [Q9BZB8-4]
GeneIDi64506.
KEGGihsa:64506.
UCSCiuc002biq.4. human. [Q9BZB8-1]

Organism-specific databases

CTDi64506.
DisGeNETi64506.
GeneCardsiCPEB1.
HGNCiHGNC:21744. CPEB1.
HPAiHPA044113.
MIMi607342. gene.
neXtProtiNX_Q9BZB8.
OpenTargetsiENSG00000214575.
ENSG00000277445.
PharmGKBiPA134929879.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITXD. Eukaryota.
ENOG410YBXF. LUCA.
GeneTreeiENSGT00390000012886.
HOGENOMiHOG000290661.
HOVERGENiHBG079080.
InParanoidiQ9BZB8.
KOiK02602.
PhylomeDBiQ9BZB8.
TreeFamiTF317658.

Miscellaneous databases

GeneWikiiCPEB1.
GenomeRNAii64506.
PROiQ9BZB8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000214575.
CleanExiHS_CPEB1.
ExpressionAtlasiQ9BZB8. baseline and differential.
GenevisibleiQ9BZB8. HS.

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]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCPEB1_HUMAN
AccessioniPrimary (citable) accession number: Q9BZB8
Secondary accession number(s): B7Z6C6
, Q86W46, Q8IV41, Q9BZB7, Q9H8V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.