Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 114 (02 Dec 2020)
Sequence version 2 (09 Feb 2010)
Previous versions | rss
Add a publicationFeedback
Protein

Cytoplasmic polyadenylation element-binding protein 1-A

Gene

cpeb1-a

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi517Zinc 1By similarity1
Metal bindingi520Zinc 1By similarity1
Metal bindingi529Zinc 2By similarity1
Metal bindingi534Zinc 2By similarity1
Metal bindingi539Zinc 1By similarity1
Metal bindingi542Zinc 1By similarity1
Metal bindingi547Zinc 2By similarity1
Metal bindingi555Zinc 2By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Repressor, Ribonucleoprotein, RNA-binding
Biological processmRNA processing, Translation regulation
LigandMetal-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cytoplasmic polyadenylation element-binding protein 1-A
Short name:
CPE-BP1-A
Short name:
CPE-binding protein 1-A
Short name:
CPEB-1-A
Alternative name(s):
58 kDa CPE-binding protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cpeb1-a
Synonyms:cpeb
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiXenopus laevis (African clawed frog)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri8355 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-946172, cpeb1.L

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi138S → A: Abolishes degradation by the proteasome; when associated with A-210 and A-248. 1 Publication1
Mutagenesisi174 – 180SRSILDS → ARSILDA: Abolishes phosphorylation and CPE-containing mRNA cytoplasmic polyadenylation and oocyte maturation. 1 Publication7
Mutagenesisi174 – 180SRSILDS → DRSILD: Does not abolish interaction with cpsf2 and CPE-containing mRNA cytoplasmic polyadenylation and oocyte maturation. 1 Publication7
Mutagenesisi174S → A: Abolishes phosphorylation and CPE-containing mRNA cytoplasmic polyadenylation and oocyte maturation. Diminishes the interaction with cpsf2 and papd4/gld2. 2 Publications1
Mutagenesisi174S → D: Stimulates premature CPE-dependent polyadenylation and translation in primary oocytes. Does not diminishes the interaction with cpsf and papd4/gld2. 2 Publications1
Mutagenesisi210S → A: Abolishes degradation by the proteasome; when associated with A-138 and A-248. 1 Publication1
Mutagenesisi248S → A: Abolishes degradation by the proteasome; when associated with A-138 and A-210. 1 Publication1
Mutagenesisi529C → A: Abolishes RNA-binding. 1 Publication1
Mutagenesisi539C → A: Abolishes RNA-binding. 1 Publication1
Mutagenesisi547H → A: Abolishes RNA-binding. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002692571 – 568Cytoplasmic polyadenylation element-binding protein 1-AAdd BLAST568

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei138Phosphoserine; by cdk11 Publication1
Modified residuei174Phosphoserine; by aurka4 Publications1
Modified residuei210Phosphoserine; by cdk11 Publication1
Modified residuei248Phosphoserine; by cdk11 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 aplp1.5 Publications
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.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q91572

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q91572

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed uniformly in growing oocytes (stage I to IV) and distributed at the animal pole in fully-grown oocytes (stages V and VI) (at protein level). During early oocyte maturation its expression remains constant and then declines drastically during late oocyte maturation between 4 hours and 6 hours after the germinal vesicle breakdown (GVBD) (at protein level). Expressed during early oogenesis until stage III, remains constant through stage V oocytes, decreases slightly in stage VI oocytes, and then remains constant throughout oocyte maturation.3 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

After fertilization, expressed at the animal pole in embryo, blastomeres and blastula stage (at protein level).1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
100614, 6 interactors

Database of interacting proteins

More...
DIPi
DIP-30935N

Protein interaction database and analysis system

More...
IntActi
Q91572, 7 interactors

Molecular INTeraction database

More...
MINTi
Q91572

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q91572

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini313 – 410RRM 1PROSITE-ProRule annotationAdd BLAST98
Domaini432 – 513RRM 2PROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni172 – 175Necessary for interaction with microtubules and localization at the mitotic apparatus4
Regioni181 – 208Necessary for degradation by the proteasomeAdd BLAST28
Regioni182 – 191Necessary for interaction with microtubules and localization at the mitotic apparatus10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi169 – 210Ser-richAdd BLAST42

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RRM CPEB family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
1075356at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12723, RRM1_CPEB1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.40.130, 1 hit
3.30.70.330, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR032292, CEBP1_N
IPR032296, CEBP_ZZ
IPR038446, CEBP_ZZ_sf
IPR034819, CPEB
IPR034977, CPEB1_RRM1
IPR012677, Nucleotide-bd_a/b_plait_sf
IPR035979, RBD_domain_sf
IPR000504, RRM_dom

The PANTHER Classification System

More...
PANTHERi
PTHR12566, PTHR12566, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16368, CEBP1_N, 1 hit
PF16366, CEBP_ZZ, 1 hit
PF16367, RRM_7, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00360, RRM, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54928, SSF54928, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50102, RRM, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q91572-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAFPLKDDLG RAKDCWGCPS DTPALSTCSN ADIFRRINAM LDNSLDFTGV
60 70 80 90 100
CTTPNTKGKC EHLQDYQDTE GPAASRMLFS TSHEPLPRGL PDTNDLCLGL
110 120 130 140 150
QSLSLTGWDR PWSTQDSEAG GHSSTPTAAQ SVFSMLNSPM GKPSPLGFLT
160 170 180 190 200
FDPIGSDLME KYPTPLLRSS RLDSRSILDS RSSSPSDSDT SGFSSGSDHL
210 220 230 240 250
SDLISSLRIS PPLPFLPLGG GVSRDPLKLG IGSRLDQDHA ALAAATVSPL
260 270 280 290 300
GITKGWPSTS VWPSWDLLDS AEDPFSIERE ARLHRQAAAV NEATCTWSGQ
310 320 330 340 350
LPPRNYKNPV YSCKVFLGGV PWDITETGLI NTFRVFGALS VEWPGKDGKH
360 370 380 390 400
PRCPPKGNMP KGYVYLVFES EKSVRALLQA CSQDLLSQDG 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):62,605
Last modified:February 9, 2010 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEF812949F5B4DE54
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti19P → S in AAI70313 (Ref. 2) Curated1
Sequence conflicti214P → H in AAA80483 (PubMed:7954828).Curated1
Sequence conflicti404R → A in AAA80483 (PubMed:7954828).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U14169 mRNA Translation: AAA80483.1
BC170313 mRNA Translation: AAI70313.1
BC170341 mRNA Translation: AAI70341.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A55377

NCBI Reference Sequences

More...
RefSeqi
NP_001084072.1, NM_001090603.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
399289

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:399289

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14169 mRNA Translation: AAA80483.1
BC170313 mRNA Translation: AAI70313.1
BC170341 mRNA Translation: AAI70341.1
PIRiA55377
RefSeqiNP_001084072.1, NM_001090603.1

3D structure databases

SMRiQ91572
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi100614, 6 interactors
DIPiDIP-30935N
IntActiQ91572, 7 interactors
MINTiQ91572

PTM databases

iPTMnetiQ91572

Proteomic databases

PRIDEiQ91572

Genome annotation databases

GeneIDi399289
KEGGixla:399289

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
399289
XenbaseiXB-GENE-946172, cpeb1.L

Phylogenomic databases

OrthoDBi1075356at2759

Family and domain databases

CDDicd12723, RRM1_CPEB1, 1 hit
Gene3Di3.30.40.130, 1 hit
3.30.70.330, 2 hits
InterProiView protein in InterPro
IPR032292, CEBP1_N
IPR032296, CEBP_ZZ
IPR038446, CEBP_ZZ_sf
IPR034819, CPEB
IPR034977, CPEB1_RRM1
IPR012677, Nucleotide-bd_a/b_plait_sf
IPR035979, RBD_domain_sf
IPR000504, RRM_dom
PANTHERiPTHR12566, PTHR12566, 1 hit
PfamiView protein in Pfam
PF16368, CEBP1_N, 1 hit
PF16366, CEBP_ZZ, 1 hit
PF16367, RRM_7, 1 hit
SMARTiView protein in SMART
SM00360, RRM, 2 hits
SUPFAMiSSF54928, SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50102, RRM, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCPE1A_XENLA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q91572
Secondary accession number(s): B7ZRW6, B7ZRZ4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: February 9, 2010
Last modified: December 2, 2020
This is version 114 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again