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 151 (02 Jun 2021)
Sequence version 2 (03 Oct 2012)
Previous versions | rss
Add a publicationFeedback
Protein

Nuclear cap-binding protein subunit 2

Gene

ncbp-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score:

Annotation score:4 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>
-Protein inferred from homologyi <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

Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing and RNA-mediated gene silencing (RNAi). The CBC complex is involved in miRNA-mediated RNA interference and is required for primary microRNAs (miRNAs) processing. In the CBC complex, ncbp-2 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires ncbp-1 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure (By similarity).

By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei17mRNA capBy similarity1
Binding sitei40mRNA capBy 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

  • RNA cap binding Source: GO_Central

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 functionRNA-binding
Biological processmRNA processing, mRNA splicing, RNA-mediated gene silencing

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-111367, SLBP independent Processing of Histone Pre-mRNAs
R-CEL-113418, Formation of the Early Elongation Complex
R-CEL-159227, Transport of the SLBP independent Mature mRNA
R-CEL-159230, Transport of the SLBP Dependant Mature mRNA
R-CEL-159231, Transport of Mature mRNA Derived from an Intronless Transcript
R-CEL-159236, Transport of Mature mRNA derived from an Intron-Containing Transcript
R-CEL-674695, RNA Polymerase II Pre-transcription Events
R-CEL-6803529, FGFR2 alternative splicing
R-CEL-6807505, RNA polymerase II transcribes snRNA genes
R-CEL-72086, mRNA Capping
R-CEL-72163, mRNA Splicing - Major Pathway
R-CEL-72165, mRNA Splicing - Minor Pathway
R-CEL-72187, mRNA 3'-end processing
R-CEL-73856, RNA Polymerase II Transcription Termination
R-CEL-77588, SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs
R-CEL-77595, Processing of Intronless Pre-mRNAs
R-CEL-975956, Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-CEL-975957, Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

<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:
Nuclear cap-binding protein subunit 2
Alternative name(s):
20 kDa nuclear cap-binding protein
NCBP 20 kDa subunit
Short name:
CBP20
<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:ncbp-2
Synonyms:cbp-20
ORF Names:F26A3.2
<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>OrganismiCaenorhabditis elegans
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001940 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome I

Organism-specific databases

WormBase

More...
WormBasei
F26A3.2a ; CE46329 ; WBGene00009141 ; ncbp-2
F26A3.2b ; CE46444 ; WBGene00009141 ; ncbp-2
F26A3.2c ; CE46506 ; WBGene00009141 ; ncbp-2

<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

Nucleus

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Lethality in 98.7% of embryos.1 Publication

<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_00003852571 – 158Nuclear cap-binding protein subunit 2Add BLAST158

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q93594

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q93594

PeptideAtlas

More...
PeptideAtlasi
Q93594

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00009141, Expressed in multi-cellular organism and 5 other tissues

<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

Component of the nuclear cap-binding complex (CBC), a heterodimer composed of ncbp-1 and ncbp-2 that interacts with m7GpppG-capped RNA.

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
49734, 3 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-957, Nuclear cap-binding complex

STRING: functional protein association networks

More...
STRINGi
6239.F26A3.2a

<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
Q93594

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>Domaini37 – 115RRMPROSITE-ProRule annotationAdd BLAST79

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>Regioni109 – 113mRNA cap-bindingBy similarity5
Regioni120 – 124mRNA cap-bindingBy similarity5
Regioni123 – 158DisorderedSequence analysisAdd BLAST36
Regioni130 – 131mRNA cap-bindingBy similarity2

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi125 – 144Basic and acidic residuesSequence analysisAdd BLAST20

<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 NCBP2 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0121, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000003197

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_070952_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q93594

Identification of Orthologs from Complete Genome Data

More...
OMAi
AENCMRY

Database of Orthologous Groups

More...
OrthoDBi
1421503at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12240, RRM_NCBP2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.70.330, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027157, NCBP2
IPR034148, NCBP2_RRM
IPR012677, Nucleotide-bd_a/b_plait_sf
IPR035979, RBD_domain_sf
IPR000504, RRM_dom

The PANTHER Classification System

More...
PANTHERi
PTHR18847, PTHR18847, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00076, RRM_1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00360, RRM, 1 hit

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, 1 hit

<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>Sequences (3)i

<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.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform a (identifier: Q93594-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MVFDPRTLDN PKEISAYRDQ RYQGTVRDQE TALRTSCTLY VGNLSYYTKE
60 70 80 90 100
DQVYELFGRA GDVRRVIMGL DRFKKTPCGF CFVEYYTRED AELALQNISN
110 120 130 140 150
TRMDDRVIRA DWDAGFIEGR QYGRGKHGGQ VRDEYRKDYD PERGGYNRAI

AQKGGDRQ
Length:158
Mass (Da):18,438
Last modified:October 3, 2012 - 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:i18AB5D6FF8131E50
GO
Isoform b (identifier: Q93594-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: Missing.

Show »
Length:91
Mass (Da):10,587
Checksum:i6D43BF7B715F680D
GO
Isoform c (identifier: Q93594-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: Missing.

Show »
Length:56
Mass (Da):6,487
Checksum:i0AE9ECFB8FEA1322
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0442111 – 102Missing in isoform c. CuratedAdd BLAST102
Alternative sequenceiVSP_0442101 – 67Missing in isoform b. CuratedAdd BLAST67

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
Z78419 Genomic DNA Translation: CCD31067.1
Z78419 Genomic DNA Translation: CCD31068.1
Z78419 Genomic DNA Translation: CCD31069.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T21382

NCBI Reference Sequences

More...
RefSeqi
NP_001250552.1, NM_001263623.1
NP_001250553.1, NM_001263624.1 [Q93594-2]
NP_001250554.1, NM_001263625.1 [Q93594-3]

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
F26A3.2a.1; F26A3.2a.1; WBGene00009141 [Q93594-1]
F26A3.2a.2; F26A3.2a.2; WBGene00009141 [Q93594-1]
F26A3.2b.1; F26A3.2b.1; WBGene00009141 [Q93594-2]
F26A3.2b.2; F26A3.2b.2; WBGene00009141 [Q93594-2]
F26A3.2c.1; F26A3.2c.1; WBGene00009141 [Q93594-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
184953

UCSC genome browser

More...
UCSCi
F26A3.2, c. elegans [Q93594-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
Z78419 Genomic DNA Translation: CCD31067.1
Z78419 Genomic DNA Translation: CCD31068.1
Z78419 Genomic DNA Translation: CCD31069.1
PIRiT21382
RefSeqiNP_001250552.1, NM_001263623.1
NP_001250553.1, NM_001263624.1 [Q93594-2]
NP_001250554.1, NM_001263625.1 [Q93594-3]

3D structure databases

SMRiQ93594
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi49734, 3 interactors
ComplexPortaliCPX-957, Nuclear cap-binding complex
STRINGi6239.F26A3.2a

Proteomic databases

EPDiQ93594
PaxDbiQ93594
PeptideAtlasiQ93594

Genome annotation databases

EnsemblMetazoaiF26A3.2a.1; F26A3.2a.1; WBGene00009141 [Q93594-1]
F26A3.2a.2; F26A3.2a.2; WBGene00009141 [Q93594-1]
F26A3.2b.1; F26A3.2b.1; WBGene00009141 [Q93594-2]
F26A3.2b.2; F26A3.2b.2; WBGene00009141 [Q93594-2]
F26A3.2c.1; F26A3.2c.1; WBGene00009141 [Q93594-3]
GeneIDi184953
UCSCiF26A3.2, c. elegans [Q93594-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
184953
WormBaseiF26A3.2a ; CE46329 ; WBGene00009141 ; ncbp-2
F26A3.2b ; CE46444 ; WBGene00009141 ; ncbp-2
F26A3.2c ; CE46506 ; WBGene00009141 ; ncbp-2

Phylogenomic databases

eggNOGiKOG0121, Eukaryota
GeneTreeiENSGT00390000003197
HOGENOMiCLU_070952_2_1_1
InParanoidiQ93594
OMAiAENCMRY
OrthoDBi1421503at2759

Enzyme and pathway databases

ReactomeiR-CEL-111367, SLBP independent Processing of Histone Pre-mRNAs
R-CEL-113418, Formation of the Early Elongation Complex
R-CEL-159227, Transport of the SLBP independent Mature mRNA
R-CEL-159230, Transport of the SLBP Dependant Mature mRNA
R-CEL-159231, Transport of Mature mRNA Derived from an Intronless Transcript
R-CEL-159236, Transport of Mature mRNA derived from an Intron-Containing Transcript
R-CEL-674695, RNA Polymerase II Pre-transcription Events
R-CEL-6803529, FGFR2 alternative splicing
R-CEL-6807505, RNA polymerase II transcribes snRNA genes
R-CEL-72086, mRNA Capping
R-CEL-72163, mRNA Splicing - Major Pathway
R-CEL-72165, mRNA Splicing - Minor Pathway
R-CEL-72187, mRNA 3'-end processing
R-CEL-73856, RNA Polymerase II Transcription Termination
R-CEL-77588, SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs
R-CEL-77595, Processing of Intronless Pre-mRNAs
R-CEL-975956, Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-CEL-975957, Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q93594

Gene expression databases

BgeeiWBGene00009141, Expressed in multi-cellular organism and 5 other tissues

Family and domain databases

CDDicd12240, RRM_NCBP2, 1 hit
Gene3Di3.30.70.330, 1 hit
InterProiView protein in InterPro
IPR027157, NCBP2
IPR034148, NCBP2_RRM
IPR012677, Nucleotide-bd_a/b_plait_sf
IPR035979, RBD_domain_sf
IPR000504, RRM_dom
PANTHERiPTHR18847, PTHR18847, 1 hit
PfamiView protein in Pfam
PF00076, RRM_1, 1 hit
SMARTiView protein in SMART
SM00360, RRM, 1 hit
SUPFAMiSSF54928, SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50102, RRM, 1 hit

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 nameiNCBP2_CAEEL
<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: Q93594
Secondary accession number(s): G3MU41, G3MU42, G3MU43
<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: September 22, 2009
Last sequence update: October 3, 2012
Last modified: June 2, 2021
This is version 151 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 programCaenorhabditis annotation project

<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

Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. 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