Cytoplasmic polyadenylation element-binding protein 1-B - Xenopus laevis (African clawed frog)

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Q52KN7 (CPE1B_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 46. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	568 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › centrosome By similarity. Membrane By similarity. Cytoplasm › cytoskeleton › spindle 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 process	Translation regulation mRNA processing
Cellular component	Cytoplasm Cytoskeleton Membrane
Domain	Repeat
Ligand	RNA-binding Zinc
Molecular function	Activator Repressor Ribonucleoprotein
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological_process	mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 568

568

Cytoplasmic polyadenylation element-binding protein 1-B

PRO_0000269258

Regions

Domain

313 – 410

RRM 1

Domain

432 – 513

RRM 2

Region

172 – 175

Necessary for interaction with microtubules and localization at the mitotic apparatus By similarity

Region

181 – 208

Necessary for degradation by the proteasome By similarity

Region

182 – 191

Necessary for interaction with microtubules and localization at the mitotic apparatus By similarity

Compositional bias

169 – 210

Ser-rich

Amino acid modifications

Modified residue

138

Phosphoserine; by cdk1 By similarity

Modified residue

174

Phosphoserine; by aurka By similarity

Modified residue

210

Phosphoserine; by cdk1 By similarity

Modified residue

248

Phosphoserine; by cdk1 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q52KN7 [UniParc].

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

568

62,632

        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

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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.
RefSeq	NP_001089420.1. NM_001095951.1.
UniGene	Xl.29059.
3D structure databases
ProteinModelPortal	Q52KN7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	734470.
KEGG	xla:734470.
Organism-specific databases
CTD	734470.
Xenbase	XB-GENE-6256188. cpeb1.
Phylogenomic databases
HOVERGEN	HBG079080.
KO	K02602.
Family and domain databases
Gene3D	3.30.70.330. 3 hits.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
SMART	SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CPE1B_XENLA

Accession

Primary (citable) accession number: Q52KN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	May 24, 2005
Last modified:	March 6, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents