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Entry version 129 (16 Oct 2019)
Sequence version 1 (01 Mar 2003)
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Protein

Radical S-adenosyl methionine domain-containing protein 2

Gene

Rsad2

Organism
Mus musculus (Mouse)
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

Interferon-inducible iron-sulfur (4FE-4S) cluster-binding antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Can inhibit a wide range of viruses, including west Nile virus (WNV), dengue virus, sindbis virus, influenza A virus, sendai virus and vesicular stomatitis virus (VSV). Displays antiviral activity against influenza A virus by inhibiting the budding of the virus from the plasma membrane by disturbing the lipid rafts. This is accomplished, at least in part, through binding and inhibition of the enzyme farnesyl diphosphate synthase (FPPS), which is essential for the biosynthesis of isoprenoid-derived lipids. Promotes TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating Lys-63'-linked ubiquitination of IRAK1. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins.4 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

[4Fe-4S] clusterCombined sources1 PublicationNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.Combined sources1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi84Iron-sulfur (4Fe-4S-S-AdoMet)Combined sources1 Publication1
Metal bindingi88Iron-sulfur (4Fe-4S-S-AdoMet)Combined sources1 Publication1
Metal bindingi91Iron-sulfur (4Fe-4S-S-AdoMet)Combined sources1 Publication1

<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

Biological processAntiviral defense, Immunity, Innate immunity
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

<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_and_taxonomy_section">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:
Radical S-adenosyl methionine domain-containing protein 2
Alternative name(s):
Viperin
Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Rsad2Imported
Synonyms:Vig1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 12

Organism-specific databases

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

More...
MGIi
MGI:1929628 Rsad2

<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

Endoplasmic reticulum, Lipid droplet, Membrane

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003095841 – 362Radical S-adenosyl methionine domain-containing protein 2Add BLAST362

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q8CBB9

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

More...
PaxDbi
Q8CBB9

PRoteomics IDEntifications database

More...
PRIDEi
Q8CBB9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8CBB9

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

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PhosphoSitePlusi
Q8CBB9

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q8CBB9

<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 at higher levels in atherosclerotic arteries than in normal arteries.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By interferon type I, type II and LPS. Induced by infection with Vesicular stomatitis virus and pseudorabies virus in dendritic cells, presumably through type I interferon pathway.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000020641 Expressed in 192 organ(s), highest expression level in blood

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q8CBB9 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8CBB9 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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

Interacts with FPPS (By similarity).

Interacts (via C-terminus) with VAPA/VAP33 (via C-terminus) and inhibits its interaction with hepatitis virus C (HCV) protein NS5A.

Interacts with HADHB (By similarity).

Interacts with IRAK1 and TRAF6.

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
208378, 5 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000020970

<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

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q8CBB9

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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 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 N-terminal region (1-43) is necessary for its localization to the endoplasmic reticulum membrane and lipid droplet.

<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 radical SAM superfamily. RSAD2 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IGZE Eukaryota
ENOG410XQM5 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000013670

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8CBB9

KEGG Orthology (KO)

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KOi
K15045

Identification of Orthologs from Complete Genome Data

More...
OMAi
CWLRATF

Database of Orthologous Groups

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OrthoDBi
1098093at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8CBB9

TreeFam database of animal gene trees

More...
TreeFami
TF300085

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785 Aldolase_TIM
IPR006638 Elp3/MiaB/NifB
IPR007197 rSAM

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04055 Radical_SAM, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00729 Elp3, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 1 potential isoform that is computationally mapped.Show allAlign All

Q8CBB9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGMLVPTALA ARLLSLFQQQ LGSLWSGLAI LFCWLRIALG WLDPGKEQPQ
60 70 80 90 100
VRGEPEDTQE TQEDGNSTQP TTPVSVNYHF TRQCNYKCGF CFHTAKTSFV
110 120 130 140 150
LPLEEAKRGL LLLKQAGLEK INFSGGEPFL QDRGEYLGKL VRFCKEELAL
160 170 180 190 200
PSVSIVSNGS LIRERWFKDY GEYLDILAIS CDSFDEQVNA LIGRGQGKKN
210 220 230 240 250
HVENLQKLRR WCRDYKVAFK INSVINRFNV DEDMNEHIKA LSPVRWKVFQ
260 270 280 290 300
CLLIEGENSG EDALREAERF LISNEEFETF LERHKEVSCL VPESNQKMKD
310 320 330 340 350
SYLILDEYMR FLNCTGGRKD PSKSILDVGV EEAIKFSGFD EKMFLKRGGK
360
YVWSKADLKL DW
Length:362
Mass (Da):41,524
Last modified:March 1, 2003 - 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:iF56F0BBEC9F20E50
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RJ49D6RJ49_MOUSE
Radical S-adenosyl methionine domai...
Rsad2
187Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAE29281 differs from that shown. Reason: Erroneous termination. Truncated C-terminus.Curated

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 conflicti15S → R in BAE31578 (PubMed:16141072).Curated1
Sequence conflicti15S → R in BAE30379 (PubMed:16141072).Curated1
Sequence conflicti15S → R in BAE29807 (PubMed:16141072).Curated1
Sequence conflicti15S → R in BAE29764 (PubMed:16141072).Curated1
Sequence conflicti26S → C in BAE30676 (PubMed:16141072).Curated1
Sequence conflicti26S → G in BAE31898 (PubMed:16141072).Curated1
Sequence conflicti26S → G in BAE31903 (PubMed:16141072).Curated1
Sequence conflicti52R → P in BAE30920 (PubMed:16141072).Curated1
Sequence conflicti55P → L in AAF60314 (PubMed:11038379).Curated1
Sequence conflicti55P → L in CAJ18585 (Ref. 3) Curated1
Sequence conflicti55P → L in AAH57868 (PubMed:15489334).Curated1
Sequence conflicti55P → L in AAL50054 (PubMed:11752458).Curated1
Sequence conflicti57D → E in AAF60314 (PubMed:11038379).Curated1
Sequence conflicti57D → E in CAJ18585 (Ref. 3) Curated1
Sequence conflicti57D → E in AAH57868 (PubMed:15489334).Curated1
Sequence conflicti57D → E in AAL50054 (PubMed:11752458).Curated1
Sequence conflicti70P → R in AAF60314 (PubMed:11038379).Curated1
Sequence conflicti70P → R in CAJ18585 (Ref. 3) Curated1
Sequence conflicti70P → R in AAH57868 (PubMed:15489334).Curated1
Sequence conflicti70P → R in AAL50054 (PubMed:11752458).Curated1
Sequence conflicti73P → T in BAE31898 (PubMed:16141072).Curated1
Sequence conflicti94T → K in BAE30826 (PubMed:16141072).Curated1
Sequence conflicti94T → K in BAE32092 (PubMed:16141072).Curated1
Sequence conflicti125G → E in BAE29848 (PubMed:16141072).Curated1
Sequence conflicti148L → Q in BAE31064 (PubMed:16141072).Curated1
Sequence conflicti149A → S in BAE30826 (PubMed:16141072).Curated1
Sequence conflicti163R → Q in AAF60314 (PubMed:11038379).Curated1
Sequence conflicti163R → Q in AAL50054 (PubMed:11752458).Curated1
Sequence conflicti211W → R in BAE31565 (PubMed:16141072).Curated1
Sequence conflicti211W → R in BAE31383 (PubMed:16141072).Curated1
Sequence conflicti211W → R in BAE30737 (PubMed:16141072).Curated1
Sequence conflicti241L → Q in BAE31898 (PubMed:16141072).Curated1
Sequence conflicti241L → Q in BAE31903 (PubMed:16141072).Curated1
Sequence conflicti247K → E in BAE30673 (PubMed:16141072).Curated1
Sequence conflicti247K → E in BAE30203 (PubMed:16141072).Curated1
Sequence conflicti262D → G in BAE30726 (PubMed:16141072).Curated1
Sequence conflicti270F → L in BAE31348 (PubMed:16141072).Curated1
Sequence conflicti273S → G in BAE31064 (PubMed:16141072).Curated1
Sequence conflicti339F → Y in BAE30676 (PubMed:16141072).Curated1
Sequence conflicti339F → Y in BAE30787 (PubMed:16141072).Curated1
Sequence conflicti339F → Y in BAE30790 (PubMed:16141072).Curated1
Sequence conflicti339F → Y in BAE30920 (PubMed:16141072).Curated1
Sequence conflicti339F → Y in BAE30927 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF236064 mRNA Translation: AAF60314.2
AK036373 mRNA Translation: BAC29401.1
AK150069 mRNA Translation: BAE29281.1 Sequence problems.
AK150406 mRNA Translation: BAE29532.1
AK150425 mRNA Translation: BAE29548.1
AK150525 mRNA Translation: BAE29636.1
AK150616 mRNA Translation: BAE29706.1
AK150684 mRNA Translation: BAE29764.1
AK150731 mRNA Translation: BAE29807.1
AK150767 mRNA Translation: BAE29833.1
AK150783 mRNA Translation: BAE29848.1
AK150788 mRNA Translation: BAE29852.1
AK150812 mRNA Translation: BAE29875.1
AK150835 mRNA Translation: BAE29895.1
AK151140 mRNA Translation: BAE30147.1
AK151185 mRNA Translation: BAE30184.1
AK151191 mRNA Translation: BAE30188.1
AK151206 mRNA Translation: BAE30203.1
AK151286 mRNA Translation: BAE30271.1
AK151308 mRNA Translation: BAE30290.1
AK151339 mRNA Translation: BAE30317.1
AK151389 mRNA Translation: BAE30360.1
AK151410 mRNA Translation: BAE30375.1
AK151412 mRNA Translation: BAE30377.1
AK151414 mRNA Translation: BAE30379.1
AK151476 mRNA Translation: BAE30431.1
AK151502 mRNA Translation: BAE30453.1
AK151538 mRNA Translation: BAE30485.1
AK151767 mRNA Translation: BAE30673.1
AK151770 mRNA Translation: BAE30676.1
AK151825 mRNA Translation: BAE30722.1
AK151833 mRNA Translation: BAE30726.1
AK151846 mRNA Translation: BAE30737.1
AK151906 mRNA Translation: BAE30787.1
AK151909 mRNA Translation: BAE30790.1
AK151940 mRNA Translation: BAE30816.1
AK151954 mRNA Translation: BAE30826.1
AK151971 mRNA Translation: BAE30840.1
AK152050 mRNA Translation: BAE30906.1
AK152065 mRNA Translation: BAE30920.1
AK152075 mRNA Translation: BAE30927.1
AK152235 mRNA Translation: BAE31060.1
AK152239 mRNA Translation: BAE31062.1
AK152241 mRNA Translation: BAE31064.1
AK152310 mRNA Translation: BAE31116.1
AK152354 mRNA Translation: BAE31146.1
AK152493 mRNA Translation: BAE31264.1
AK152600 mRNA Translation: BAE31348.1
AK152601 mRNA Translation: BAE31349.1
AK152631 mRNA Translation: BAE31374.1
AK152644 mRNA Translation: BAE31383.1
AK152664 mRNA Translation: BAE31399.1
AK152796 mRNA Translation: BAE31501.1
AK152861 mRNA Translation: BAE31552.1
AK152880 mRNA Translation: BAE31565.1
AK152895 mRNA Translation: BAE31578.1
AK152934 mRNA Translation: BAE31608.1
AK152962 mRNA Translation: BAE31625.1
AK153003 mRNA Translation: BAE31643.1
AK153024 mRNA Translation: BAE31658.1
AK153062 mRNA Translation: BAE31688.1
AK153077 mRNA Translation: BAE31702.1
AK153078 mRNA Translation: BAE31703.1
AK153232 mRNA Translation: BAE31825.1
AK153234 mRNA Translation: BAE31827.1
AK153306 mRNA Translation: BAE31887.1
AK153318 mRNA Translation: BAE31898.1
AK153324 mRNA Translation: BAE31903.1
AK153435 mRNA Translation: BAE31992.1
AK153556 mRNA Translation: BAE32092.1
AK159147 mRNA Translation: BAE34854.1
CT010378 mRNA Translation: CAJ18585.1
BC057868 mRNA Translation: AAH57868.1
AF442152 mRNA Translation: AAL50054.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS25848.1

NCBI Reference Sequences

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RefSeqi
NP_067359.2, NM_021384.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000020970; ENSMUSP00000020970; ENSMUSG00000020641

Database of genes from NCBI RefSeq genomes

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GeneIDi
58185

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:58185

UCSC genome browser

More...
UCSCi
uc007nfh.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
AF236064 mRNA Translation: AAF60314.2
AK036373 mRNA Translation: BAC29401.1
AK150069 mRNA Translation: BAE29281.1 Sequence problems.
AK150406 mRNA Translation: BAE29532.1
AK150425 mRNA Translation: BAE29548.1
AK150525 mRNA Translation: BAE29636.1
AK150616 mRNA Translation: BAE29706.1
AK150684 mRNA Translation: BAE29764.1
AK150731 mRNA Translation: BAE29807.1
AK150767 mRNA Translation: BAE29833.1
AK150783 mRNA Translation: BAE29848.1
AK150788 mRNA Translation: BAE29852.1
AK150812 mRNA Translation: BAE29875.1
AK150835 mRNA Translation: BAE29895.1
AK151140 mRNA Translation: BAE30147.1
AK151185 mRNA Translation: BAE30184.1
AK151191 mRNA Translation: BAE30188.1
AK151206 mRNA Translation: BAE30203.1
AK151286 mRNA Translation: BAE30271.1
AK151308 mRNA Translation: BAE30290.1
AK151339 mRNA Translation: BAE30317.1
AK151389 mRNA Translation: BAE30360.1
AK151410 mRNA Translation: BAE30375.1
AK151412 mRNA Translation: BAE30377.1
AK151414 mRNA Translation: BAE30379.1
AK151476 mRNA Translation: BAE30431.1
AK151502 mRNA Translation: BAE30453.1
AK151538 mRNA Translation: BAE30485.1
AK151767 mRNA Translation: BAE30673.1
AK151770 mRNA Translation: BAE30676.1
AK151825 mRNA Translation: BAE30722.1
AK151833 mRNA Translation: BAE30726.1
AK151846 mRNA Translation: BAE30737.1
AK151906 mRNA Translation: BAE30787.1
AK151909 mRNA Translation: BAE30790.1
AK151940 mRNA Translation: BAE30816.1
AK151954 mRNA Translation: BAE30826.1
AK151971 mRNA Translation: BAE30840.1
AK152050 mRNA Translation: BAE30906.1
AK152065 mRNA Translation: BAE30920.1
AK152075 mRNA Translation: BAE30927.1
AK152235 mRNA Translation: BAE31060.1
AK152239 mRNA Translation: BAE31062.1
AK152241 mRNA Translation: BAE31064.1
AK152310 mRNA Translation: BAE31116.1
AK152354 mRNA Translation: BAE31146.1
AK152493 mRNA Translation: BAE31264.1
AK152600 mRNA Translation: BAE31348.1
AK152601 mRNA Translation: BAE31349.1
AK152631 mRNA Translation: BAE31374.1
AK152644 mRNA Translation: BAE31383.1
AK152664 mRNA Translation: BAE31399.1
AK152796 mRNA Translation: BAE31501.1
AK152861 mRNA Translation: BAE31552.1
AK152880 mRNA Translation: BAE31565.1
AK152895 mRNA Translation: BAE31578.1
AK152934 mRNA Translation: BAE31608.1
AK152962 mRNA Translation: BAE31625.1
AK153003 mRNA Translation: BAE31643.1
AK153024 mRNA Translation: BAE31658.1
AK153062 mRNA Translation: BAE31688.1
AK153077 mRNA Translation: BAE31702.1
AK153078 mRNA Translation: BAE31703.1
AK153232 mRNA Translation: BAE31825.1
AK153234 mRNA Translation: BAE31827.1
AK153306 mRNA Translation: BAE31887.1
AK153318 mRNA Translation: BAE31898.1
AK153324 mRNA Translation: BAE31903.1
AK153435 mRNA Translation: BAE31992.1
AK153556 mRNA Translation: BAE32092.1
AK159147 mRNA Translation: BAE34854.1
CT010378 mRNA Translation: CAJ18585.1
BC057868 mRNA Translation: AAH57868.1
AF442152 mRNA Translation: AAL50054.1
CCDSiCCDS25848.1
RefSeqiNP_067359.2, NM_021384.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5VSLX-ray1.97A/B45-362[»]
5VSMX-ray1.70A/B45-362[»]
SMRiQ8CBB9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi208378, 5 interactors
STRINGi10090.ENSMUSP00000020970

PTM databases

iPTMnetiQ8CBB9
PhosphoSitePlusiQ8CBB9
SwissPalmiQ8CBB9

Proteomic databases

MaxQBiQ8CBB9
PaxDbiQ8CBB9
PRIDEiQ8CBB9

Genome annotation databases

EnsembliENSMUST00000020970; ENSMUSP00000020970; ENSMUSG00000020641
GeneIDi58185
KEGGimmu:58185
UCSCiuc007nfh.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
91543
MGIiMGI:1929628 Rsad2

Phylogenomic databases

eggNOGiENOG410IGZE Eukaryota
ENOG410XQM5 LUCA
GeneTreeiENSGT00390000013670
InParanoidiQ8CBB9
KOiK15045
OMAiCWLRATF
OrthoDBi1098093at2759
PhylomeDBiQ8CBB9
TreeFamiTF300085

Miscellaneous databases

Protein Ontology

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PROi
PR:Q8CBB9

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000020641 Expressed in 192 organ(s), highest expression level in blood
ExpressionAtlasiQ8CBB9 baseline and differential
GenevisibleiQ8CBB9 MM

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR006638 Elp3/MiaB/NifB
IPR007197 rSAM
PfamiView protein in Pfam
PF04055 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiRSAD2_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: Q8CBB9
Secondary accession number(s): Q3U5I6
, Q3U5T4, Q3U622, Q3U627, Q3U7I6, Q3U7M1, Q3U8F4, Q3U8U7, Q3U941, Q3U977, Q3U9E1, Q3U9J0, Q3U9J3, Q3UBW6, Q3UC07, Q3UDI0, Q6PEU4, Q8VHM2, Q9JHD4
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2003
Last modified: October 16, 2019
This is version 129 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

3D-structure, Complete proteome, Reference proteome

Documents

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