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Q52KN7 (CPE1B_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic polyadenylation element-binding protein 1-B

Short name=CPE-BP1-B
Short name=CPE-binding protein 1-B
Short name=CPEB-1-B
Gene names
Name:cpeb1-b
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length568 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation and early development. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. In the absence of phosphorylation and in association with tacc3/maskin, also acts as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation. Requires zinc for RNA binding. Involved in the cell cycle progression from S phase into M phase By similarity.

Subunit structure

Found in a complex with cpeb1, tacc3/maskin and eif4e; dissolution of this complex results in the binding of eif4e to eif4g and the translational activation of CPE-containing mRNAs. Found in a complex with cpeb1, cpsf1, the cytoplasmic poly(A) polymerase papd4/gld2 and sympk. Found in a mRNP complex with cpeb1, a guanine exchange factor xgef and mos mRNA. Interacts with cpsf1, papd4/gld2, tacc3/maskin, microtubules, sympk and xgef. Component of a ribonucleoprotein (RNP) complex, at least composed of cpeb1, lsm14b/rap55b, ddx6/Xp54, ybx2/frgy2, pat1/P100, eif4enif1/4E-T and eif4e1b. Interaction with ybx2/frgy2 is RNA-dependent. May interact with aplp1. Interaction with cpsf1 increases during meiotic maturation and is not mediated through RNA. Interaction with xgef is necessary for its early activating phosphorylation status By similarity.

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Membrane By similarity. Cytoplasmcytoskeletonspindle pole By similarity. Note: During mitosis localizes with tacc3/maskin and CPE-containing mRNAs to both spindle poles. Membrane-associated. Colocalizes with members of the polyadenylation and translation complex factors (cpsf, aplp1, tacc3/maskin, aurka, etc.), including CPE-containing RNAs By similarity.

Domain

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

Post-translational modification

Ser-174 phosphorylation by aurka in immature oocytes is essential to trigger CPE-containing mRNA cytoplasmic polyadenylation and translation activation and the subsequent signaling events that result in meiotic progression. Ser-174 phosphorylation recruits the cleavage and polyadenylation specificity factor (cpsf1) into an active cytoplasmic polyadenylation complex. Ser-174 phosphorylation increases its affinity for cpsf1 and papd4/gld2. Heavily phosphorylated by CDK1 on serines late during oocyte maturation. Ser-210 phosphorylation is sufficient to target cpeb1 for degradation. Ser-174 phosphorylation oscillates with the cell cycle (phosphorylated at M phase, but not at S phase) and is necessary for S phase to M phase progression. Phosphorylation at Ser-174 may be promoted by aplp1 By similarity.

Ubiquitinated. Requires a PEST box and the proteasome pathway for destruction during oocyte maturation. Ser-210 phosphorylation triggers its destruction, an event important to allow the transition from metaphase I to metaphase II and cytokinesis in the early embryo By similarity.

Sequence similarities

Belongs to the RRM CPEB family.

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processmRNA processing
Translation regulation
   Cellular componentCytoplasm
Cytoskeleton
Membrane
   DomainRepeat
   LigandMetal-binding
RNA-binding
Zinc
   Molecular functionActivator
Repressor
Ribonucleoprotein
   PTMPhosphoprotein
Ubl conjugation
Gene Ontology (GO)
   Biological_processcellular response to amino acid stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of cytoplasmic translation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmRNA 3'-UTR AU-rich region binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

translation repressor activity, nucleic acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 568568Cytoplasmic polyadenylation element-binding protein 1-B
PRO_0000269258

Regions

Domain313 – 41098RRM 1
Domain432 – 51382RRM 2
Region172 – 1754Necessary for interaction with microtubules and localization at the mitotic apparatus By similarity
Region181 – 20828Necessary for degradation by the proteasome By similarity
Region182 – 19110Necessary for interaction with microtubules and localization at the mitotic apparatus By similarity
Compositional bias169 – 21042Ser-rich

Sites

Metal binding5171Zinc 1 By similarity
Metal binding5201Zinc 1 By similarity
Metal binding5291Zinc 2 By similarity
Metal binding5341Zinc 2 By similarity
Metal binding5391Zinc 1 By similarity
Metal binding5421Zinc 1 By similarity
Metal binding5471Zinc 2 By similarity
Metal binding5551Zinc 2 By similarity

Amino acid modifications

Modified residue1381Phosphoserine; by cdk1 By similarity
Modified residue1741Phosphoserine; by aurka By similarity
Modified residue2101Phosphoserine; by cdk1 By similarity
Modified residue2481Phosphoserine; by cdk1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q52KN7 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: 109829643720D8F2

FASTA56862,632
        10         20         30         40         50         60 
MAFPLKDDLG RAKDCWGCSS DTPALSTCSN ADIFRRINAM LDNSLDFTGV CTTPNTKGKC 

        70         80         90        100        110        120 
EHLQDYPDTE GAAASRMLFS TSHEPLPRGL PDTNDLCLGL QSLSLTGWDR PWSTQDSEAG 

       130        140        150        160        170        180 
GQSSTPTAAQ SVFSMLNSPM GKPSPLGFLP LDPIGSDLVE KYPTHLLRSS RFDSRSILDS 

       190        200        210        220        230        240 
RSSSPSDSDT SGFSSGSDHL SDLISSLRIS PPLPFLPLGS GISRDPLRLG VGSRLDQDHA 

       250        260        270        280        290        300 
ALAAATASPL GITKRWPGTS VWPSWDLLDS ADDPFSIERE ARLHRQAAAV NEATCTWSGQ 

       310        320        330        340        350        360 
LPPRNYKNPV YSCKVFLGGV PWDITETGLI NTFRVFGALS VEWPGKDGKH PRCPPKGNMP 

       370        380        390        400        410        420 
KGYVYLVFES EKSVRALLQA CTQDLLSQDG LSEHYFKMSS RRMRCKEVQV IPWVLADSNF 

       430        440        450        460        470        480 
VRSPSQRLDP SKTVFVGALH GMLNAEALAS IMNDLFGGVV YAGIDTDKHK YPIGSGRVTF 

       490        500        510        520        530        540 
NNQRSYLKAV SAAFVEIKTA KFTKKVQIDP YLEDSVCQVC NAQPGPFFCR DQVCFKYFCR 

       550        560 
SCWHWQHSME ILRHHRPLMR NQKSRDSS 

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Oocyte.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC094261 mRNA. Translation: AAH94261.1.
RefSeqNP_001089420.1. NM_001095951.1.
UniGeneXl.29059.

3D structure databases

ProteinModelPortalQ52KN7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID734470.
KEGGxla:734470.

Organism-specific databases

CTD734470.
XenbaseXB-GENE-6256188. cpeb1.

Phylogenomic databases

HOVERGENHBG079080.
KOK02602.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCPE1B_XENLA
AccessionPrimary (citable) accession number: Q52KN7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 24, 2005
Last modified: January 22, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families