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Q52KN7

- CPE1B_XENLA

UniProt

Q52KN7 - CPE1B_XENLA

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Protein

Cytoplasmic polyadenylation element-binding protein 1-B

Gene

cpeb1-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi517 – 5171Zinc 1By similarity
Metal bindingi520 – 5201Zinc 1By similarity
Metal bindingi529 – 5291Zinc 2By similarity
Metal bindingi534 – 5341Zinc 2By similarity
Metal bindingi539 – 5391Zinc 1By similarity
Metal bindingi542 – 5421Zinc 1By similarity
Metal bindingi547 – 5471Zinc 2By similarity
Metal bindingi555 – 5551Zinc 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. mRNA 3'-UTR AU-rich region binding Source: UniProtKB
  3. nucleotide binding Source: InterPro
  4. translation repressor activity, nucleic acid binding Source: UniProtKB

GO - Biological processi

  1. cellular response to amino acid stimulus Source: UniProtKB
  2. cellular response to hypoxia Source: UniProtKB
  3. cellular response to insulin stimulus Source: UniProtKB
  4. mRNA processing Source: UniProtKB-KW
  5. 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-B
Short name:
CPE-BP1-B
Short name:
CPE-binding protein 1-B
Short name:
CPEB-1-B
Gene namesi
Name:cpeb1-b
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6256188. cpeb1.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. nucleus Source: UniProtKB
  5. ribonucleoprotein complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 568568Cytoplasmic polyadenylation element-binding protein 1-BPRO_0000269258Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei138 – 1381Phosphoserine; by cdk1By similarity
Modified residuei174 – 1741Phosphoserine; by aurkaBy similarity
Modified residuei210 – 2101Phosphoserine; by cdk1By similarity
Modified residuei248 – 2481Phosphoserine; by cdk1By similarity

Post-translational modificationi

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).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).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ52KN7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini313 – 41098RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini432 – 51382RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 1754Necessary for interaction with microtubules and localization at the mitotic apparatusBy similarity
Regioni181 – 20828Necessary for degradation by the proteasomeBy similarityAdd
BLAST
Regioni182 – 19110Necessary for interaction with microtubules and localization at the mitotic apparatusBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi169 – 21042Ser-richAdd
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

HOVERGENiHBG079080.
KOiK02602.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q52KN7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFPLKDDLG RAKDCWGCSS DTPALSTCSN ADIFRRINAM LDNSLDFTGV
60 70 80 90 100
CTTPNTKGKC EHLQDYPDTE GAAASRMLFS TSHEPLPRGL PDTNDLCLGL
110 120 130 140 150
QSLSLTGWDR PWSTQDSEAG GQSSTPTAAQ SVFSMLNSPM GKPSPLGFLP
160 170 180 190 200
LDPIGSDLVE KYPTHLLRSS RFDSRSILDS RSSSPSDSDT SGFSSGSDHL
210 220 230 240 250
SDLISSLRIS PPLPFLPLGS GISRDPLRLG VGSRLDQDHA ALAAATASPL
260 270 280 290 300
GITKRWPGTS VWPSWDLLDS ADDPFSIERE ARLHRQAAAV NEATCTWSGQ
310 320 330 340 350
LPPRNYKNPV YSCKVFLGGV PWDITETGLI NTFRVFGALS VEWPGKDGKH
360 370 380 390 400
PRCPPKGNMP KGYVYLVFES EKSVRALLQA CTQDLLSQDG LSEHYFKMSS
410 420 430 440 450
RRMRCKEVQV IPWVLADSNF VRSPSQRLDP SKTVFVGALH GMLNAEALAS
460 470 480 490 500
IMNDLFGGVV YAGIDTDKHK YPIGSGRVTF NNQRSYLKAV SAAFVEIKTA
510 520 530 540 550
KFTKKVQIDP YLEDSVCQVC NAQPGPFFCR DQVCFKYFCR SCWHWQHSME
560
ILRHHRPLMR NQKSRDSS
Length:568
Mass (Da):62,632
Last modified:May 24, 2005 - v1
Checksum:i109829643720D8F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC094261 mRNA. Translation: AAH94261.1.
RefSeqiNP_001089420.1. NM_001095951.1.
UniGeneiXl.29059.

Genome annotation databases

GeneIDi734470.
KEGGixla:734470.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC094261 mRNA. Translation: AAH94261.1 .
RefSeqi NP_001089420.1. NM_001095951.1.
UniGenei Xl.29059.

3D structure databases

ProteinModelPortali Q52KN7.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 734470.
KEGGi xla:734470.

Organism-specific databases

CTDi 734470.
Xenbasei XB-GENE-6256188. cpeb1.

Phylogenomic databases

HOVERGENi HBG079080.
KOi K02602.

Family and domain databases

Gene3Di 3.30.70.330. 3 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCPE1B_XENLA
AccessioniPrimary (citable) accession number: Q52KN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 24, 2005
Last modified: October 29, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3