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Entry version 148 (12 Aug 2020)
Sequence version 1 (01 Jun 2001)
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Protein

Exosome complex component RRP46

Gene

Exosc5

Organism
Mus musculus (Mouse)
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>
-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

Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes (By similarity).By similarity

<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 functionRNA-binding
Biological processrRNA processing

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-429958, mRNA decay by 3' to 5' exoribonuclease
R-MMU-450385, Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-MMU-450513, Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA
R-MMU-450604, KSRP (KHSRP) binds and destabilizes mRNA
R-MMU-6791226, Major pathway of rRNA processing in the nucleolus and cytosol

<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:
Exosome complex component RRP46
Alternative name(s):
Exosome component 5
Ribosomal RNA-processing protein 46
<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:Exosc5
Synonyms:D7Wsu180e, Rrp46
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:107889, Exosc5

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

<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_00001399761 – 235Exosome complex component RRP46Add BLAST235

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 residuei20PhosphoserineCombined sources1
Modified residuei23PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9CRA8

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9CRA8

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9CRA8

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

More...
PaxDbi
Q9CRA8

PeptideAtlas

More...
PeptideAtlasi
Q9CRA8

PRoteomics IDEntifications database

More...
PRIDEi
Q9CRA8

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9CRA8

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9CRA8

<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
ENSMUSG00000061286, Expressed in testis and 266 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9CRA8, MM

<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 RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure.

Interacts with EXOSC1.

Interacts with GTPBP1 (By similarity).

Interacts with ZC3HAV1 (By similarity).

Interacts with DDX17 only in the presence of ZC3HAV1 in an RNA-independent manner (By similarity).

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
205707, 2 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-594, Nuclear exosome complex, Dis3-Exosc10 variant
CPX-595, Nucleolar exosome complex, Exosc10 variant
CPX-596, Cytoplasmic exosome complex, Dis3l variant
CPX-598, Exosome complex, Dis3 variant
CPX-601, Cytoplasmic exosome complex, Dis3l-Exosc10 variant

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q9CRA8

Protein interaction database and analysis system

More...
IntActi
Q9CRA8, 3 interactors

Molecular INTeraction database

More...
MINTi
Q9CRA8

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000078580

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q9CRA8, protein

<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
Q9CRA8

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

<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 RNase PH family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1069, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153348

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_063514_2_3_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9CRA8

KEGG Orthology (KO)

More...
KOi
K12590

Identification of Orthologs from Complete Genome Data

More...
OMAi
CNYRPKA

Database of Orthologous Groups

More...
OrthoDBi
1129417at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9CRA8

TreeFam database of animal gene trees

More...
TreeFami
TF315920

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.230.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001247, ExoRNase_PH_dom1
IPR015847, ExoRNase_PH_dom2
IPR036345, ExoRNase_PH_dom2_sf
IPR027408, PNPase/RNase_PH_dom_sf
IPR020568, Ribosomal_S5_D2-typ_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01138, RNase_PH, 1 hit
PF03725, RNase_PH_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54211, SSF54211, 1 hit
SSF55666, SSF55666, 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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q9CRA8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEGAKRADAN LLTDTGTESS PRSPVCSLRH FACEQNLLSR PDGSASFLQG
60 70 80 90 100
DTSVLAGVYG PAEVKVSKEI FNKATLEVIL RPKIGLPGVA EKSRERLVRN
110 120 130 140 150
TCEAVVLGAL HPRTSITVVL QVVSDAGSLL ACCLNAACMA LVDAGVPMRA
160 170 180 190 200
LFCGVTCALD SDGNLVLDPT TKQEKEARAI LTFALDSAEQ KLLMSTTKGL
210 220 230
YSDAELQQCL AAAQAASQHI FRFYRESLQR RYSKS
Length:235
Mass (Da):25,194
Last modified:June 1, 2001 - v1
<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:i08752915141CF65D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0U1RPX0A0A0U1RPX0_MOUSE
Exosome complex component RRP46
Exosc5
84Annotation score:

Annotation score:1 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>
A0A0U1RPC2A0A0U1RPC2_MOUSE
Exosome complex component RRP46
Exosc5
128Annotation score:

Annotation score:1 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 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 conflicti11L → V in AAH34358 (PubMed:15489334).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
AK007372 mRNA Translation: BAB24993.1
AK006475 mRNA Translation: BAB24607.1
BC034358 mRNA Translation: AAH34358.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS20990.1

NCBI Reference Sequences

More...
RefSeqi
NP_613052.1, NM_138586.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000079634; ENSMUSP00000078580; ENSMUSG00000061286
ENSMUST00000206561; ENSMUSP00000145948; ENSMUSG00000061286

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
27998

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:27998

UCSC genome browser

More...
UCSCi
uc009fti.2, mouse

<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
AK007372 mRNA Translation: BAB24993.1
AK006475 mRNA Translation: BAB24607.1
BC034358 mRNA Translation: AAH34358.1
CCDSiCCDS20990.1
RefSeqiNP_613052.1, NM_138586.3

3D structure databases

SMRiQ9CRA8
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi205707, 2 interactors
ComplexPortaliCPX-594, Nuclear exosome complex, Dis3-Exosc10 variant
CPX-595, Nucleolar exosome complex, Exosc10 variant
CPX-596, Cytoplasmic exosome complex, Dis3l variant
CPX-598, Exosome complex, Dis3 variant
CPX-601, Cytoplasmic exosome complex, Dis3l-Exosc10 variant
CORUMiQ9CRA8
IntActiQ9CRA8, 3 interactors
MINTiQ9CRA8
STRINGi10090.ENSMUSP00000078580

PTM databases

iPTMnetiQ9CRA8
PhosphoSitePlusiQ9CRA8

Proteomic databases

EPDiQ9CRA8
jPOSTiQ9CRA8
MaxQBiQ9CRA8
PaxDbiQ9CRA8
PeptideAtlasiQ9CRA8
PRIDEiQ9CRA8

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
30775, 189 antibodies

Genome annotation databases

EnsembliENSMUST00000079634; ENSMUSP00000078580; ENSMUSG00000061286
ENSMUST00000206561; ENSMUSP00000145948; ENSMUSG00000061286
GeneIDi27998
KEGGimmu:27998
UCSCiuc009fti.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
56915
MGIiMGI:107889, Exosc5

Phylogenomic databases

eggNOGiKOG1069, Eukaryota
GeneTreeiENSGT00940000153348
HOGENOMiCLU_063514_2_3_1
InParanoidiQ9CRA8
KOiK12590
OMAiCNYRPKA
OrthoDBi1129417at2759
PhylomeDBiQ9CRA8
TreeFamiTF315920

Enzyme and pathway databases

ReactomeiR-MMU-429958, mRNA decay by 3' to 5' exoribonuclease
R-MMU-450385, Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-MMU-450513, Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA
R-MMU-450604, KSRP (KHSRP) binds and destabilizes mRNA
R-MMU-6791226, Major pathway of rRNA processing in the nucleolus and cytosol

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
27998, 6 hits in 16 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Exosc5, mouse

Protein Ontology

More...
PROi
PR:Q9CRA8
RNActiQ9CRA8, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000061286, Expressed in testis and 266 other tissues
GenevisibleiQ9CRA8, MM

Family and domain databases

Gene3Di3.30.230.70, 1 hit
InterProiView protein in InterPro
IPR001247, ExoRNase_PH_dom1
IPR015847, ExoRNase_PH_dom2
IPR036345, ExoRNase_PH_dom2_sf
IPR027408, PNPase/RNase_PH_dom_sf
IPR020568, Ribosomal_S5_D2-typ_fold
PfamiView protein in Pfam
PF01138, RNase_PH, 1 hit
PF03725, RNase_PH_C, 1 hit
SUPFAMiSSF54211, SSF54211, 1 hit
SSF55666, SSF55666, 1 hit

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 nameiEXOS5_MOUSE
<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: Q9CRA8
Secondary accession number(s): Q8K1J2
<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: July 11, 2002
Last sequence update: June 1, 2001
Last modified: August 12, 2020
This is version 148 of the entry and version 1 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

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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