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Protein

CUGBP Elav-like family member 1-A

Gene

cugbp1-a

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

Functioni

RNA-binding protein implicated in the regulation of several post-transcriptional events. May be involved in pre-mRNA alternative splicing, mRNA translation activation and stability (By similarity). Mediates the rapid and sequence-specific cytoplasmic deadenylation of EDEN-containing maternal mRNAs following fertilization. Binds to AU-rich sequences (AREs) of jun mRNA. Binds to the embryonic deadenylation element (EDEN) motif localized in the 3'-UTR of maternal mRNAs. Binds to RNA containing several repeats of the consensus sequence 5'-UGU-3'. EDEN-dependent deadenylation is enhanced by the presence of an additional cis element composed of three AUU repeats.By similarity5 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
CUGBP Elav-like family member 1-A
Short name:
CELF-1A
Alternative name(s):
Bruno-like protein 2-A
CUG triplet repeat RNA-binding protein 1-A
Short name:
CUG-BP1-A
CUG-BP- and ETR-3-like factor 1-A
Embryo deadenylation element-binding protein A
Short name:
EDEN-BP-A
RNA-binding protein BRUNOL-2-A
p53/p55
Gene namesi
Name:cugbp1-a
Synonyms:celf1-a
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-854043. celf1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002951861 – 489CUGBP Elav-like family member 1-AAdd BLAST489

Post-translational modificationi

Phosphorylated during oocyte maturation and dephosphorylated following egg activation. Dephosphorylation is calcium dependent and correlates with the increase in the activity of EDEN-dependent deadenylation.1 Publication

Keywords - PTMi

Phosphoprotein

Expressioni

Developmental stagei

Expressed in egg and embryo (at protein level).1 Publication

Interactioni

Subunit structurei

Oligomer. Oligomerization is required for RNA-binding and EDEN-dependent deadenylation.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO57406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 99RRM 1PROSITE-ProRule annotationAdd BLAST84
Domaini108 – 188RRM 2PROSITE-ProRule annotationAdd BLAST81
Domaini404 – 482RRM 3PROSITE-ProRule annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni183 – 210Necessary for oligomerization and EDEN-dependent deadenylationAdd BLAST28

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi270 – 279Poly-Ala10
Compositional biasi291 – 312Ser-richAdd BLAST22

Domaini

The 2 N-terminal RRMs and a part of the linker region (between RRM2 and RRM3) are necessary for binding to EDEN of mos mRNA.

Sequence similaritiesi

Belongs to the CELF/BRUNOL family.Curated
Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG107646.
KOiK13207.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O57406-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGTMDHPDH PDPDSIKMFV GQVPRSWSEK ELRELFEQYG AVYEINVLRD
60 70 80 90 100
RSQNPPQSKG CCFITFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE
110 120 130 140 150
KNNAVEDRKL FIGMVSKNCN ENDIRAMFSP FGQIEECRIL RGPDGMSRGC
160 170 180 190 200
AFVTFTTRSM AQMAIKSMHQ AQTMEGCSSP IVVKFADTQK DKEQKRMTQQ
210 220 230 240 250
LQQQMQQLNA ASMWGNLTGL NSLAPQYLAL LQQTASSGNL NSLSGLHPMG
260 270 280 290 300
AEYGTGMTSG LNAIQLQNLA ALAAAASAAQ NTPSAGAALT SSSSPLSILT
310 320 330 340 350
SSGSSPSSNN SSINTMASLG ALQTLAGATA GLNVNSLAGM AAFNGGLGSS
360 370 380 390 400
LSNGTGSTME ALSQAYSGIQ QYAAAALPSL YNQSLLSQQG LGAAGSQKEG
410 420 430 440 450
PEGANLFIYH LPQEFGDQDL LQMFMPFGNV VSSKVFIDKQ TNLSKCFGFV
460 470 480
SYDNPVSAQA AIQSMNGFQI GMKRLKVQLK RSKNDSKPY
Length:489
Mass (Da):52,424
Last modified:June 1, 1998 - v1
Checksum:iE077504D3385DCC8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003923 mRNA. Translation: AAC41243.1.
BC108574 mRNA. Translation: AAI08575.1.
RefSeqiNP_001084196.1. NM_001090727.1.
UniGeneiXl.25921.

Genome annotation databases

GeneIDi399360.
KEGGixla:399360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003923 mRNA. Translation: AAC41243.1.
BC108574 mRNA. Translation: AAI08575.1.
RefSeqiNP_001084196.1. NM_001090727.1.
UniGeneiXl.25921.

3D structure databases

ProteinModelPortaliO57406.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi399360.
KEGGixla:399360.

Organism-specific databases

CTDi399360.
XenbaseiXB-GENE-854043. celf1.

Phylogenomic databases

HOVERGENiHBG107646.
KOiK13207.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCEL1A_XENLA
AccessioniPrimary (citable) accession number: O57406
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: June 1, 1998
Last modified: November 2, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. 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.