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Entry version 161 (05 Jun 2019)
Sequence version 2 (27 Jul 2011)
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Protein

E3 SUMO-protein ligase RanBP2

Gene

Ranbp2

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

E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single-stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1 (By similarity). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity.By similarity

Caution

Despite the presence of a PPIase cyclophilin-type domain, it has probably no peptidyl-prolyl cis-trans isomerase activity.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1345 – 1375RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1410 – 1439RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1469 – 1498RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1494 – 1527RanBP2-type 4PROSITE-ProRule annotationAdd BLAST34
Zinc fingeri1558 – 1587RanBP2-type 5PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1617 – 1646RanBP2-type 6PROSITE-ProRule annotationAdd BLAST30

<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, Transferase
Biological processmRNA transport, Protein transport, Translocation, Transport, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-159227 Transport of the SLBP independent Mature mRNA
R-MMU-159230 Transport of the SLBP Dependant Mature mRNA
R-MMU-159231 Transport of Mature mRNA Derived from an Intronless Transcript
R-MMU-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-MMU-191859 snRNP Assembly
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins
R-MMU-3301854 Nuclear Pore Complex (NPC) Disassembly
R-MMU-3371453 Regulation of HSF1-mediated heat shock response
R-MMU-4085377 SUMOylation of SUMOylation proteins
R-MMU-4615885 SUMOylation of DNA replication proteins
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-68877 Mitotic Prometaphase

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00886

<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:
E3 SUMO-protein ligase RanBP2 (EC:2.3.2.-By similarity)
Alternative name(s):
Ran-binding protein 2
Short name:
RanBP2
<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:Ranbp2
<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 10

Organism-specific databases

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

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MGIi
MGI:894323 Ranbp2

<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

Membrane, Nuclear pore complex, 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002049141 – 3053E3 SUMO-protein ligase RanBP2Add BLAST3053

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 residuei21PhosphoserineCombined sources1
Modified residuei779PhosphothreonineBy similarity1
Modified residuei781PhosphoserineCombined sources1
Modified residuei788PhosphoserineCombined sources1
Modified residuei837PhosphoserineBy similarity1
Modified residuei944Asymmetric dimethylarginineBy similarity1
Modified residuei947PhosphoserineBy similarity1
Modified residuei954PhosphoserineCombined sources1
Modified residuei1015Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei1015Omega-N-methylarginine; alternateBy similarity1
Modified residuei1096PhosphothreonineBy similarity1
Modified residuei1101PhosphoserineCombined sources1
Modified residuei1138PhosphothreonineBy similarity1
Modified residuei1154PhosphoserineCombined sources1
Modified residuei1243PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki1344Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1407PhosphothreonineBy similarity1
Modified residuei1438PhosphoserineBy similarity1
Modified residuei1441PhosphoserineBy similarity1
Modified residuei1446PhosphoserineBy similarity1
Modified residuei1528PhosphoserineBy similarity1
Cross-linki1557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki1607Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1616Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1616Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei1670PhosphoserineBy similarity1
Modified residuei1706PhosphoserineBy similarity1
Modified residuei1814N6-acetyllysineCombined sources1
Modified residuei1842PhosphothreonineCombined sources1
Modified residuei1845PhosphoserineCombined sources1
Cross-linki1859Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1990PhosphothreonineCombined sources1
Modified residuei2083PhosphoserineCombined sources1
Modified residuei2088PhosphoserineCombined sources1
Modified residuei2107PhosphoserineCombined sources1
Modified residuei2117PhosphoserineCombined sources1
Modified residuei2127PhosphoserineCombined sources1
Modified residuei2130PhosphothreonineCombined sources1
Modified residuei2134PhosphoserineCombined sources1
Modified residuei2299PhosphoserineCombined sources1
Modified residuei2330PhosphoserineCombined sources1
Modified residuei2348PhosphoserineCombined sources1
Cross-linki2360Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2364PhosphoserineBy similarity1
Cross-linki2430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki2432Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki2432Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki2449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2450PhosphothreonineBy similarity1
Modified residuei2503PhosphotyrosineBy similarity1
Modified residuei2505PhosphoserineCombined sources1
Modified residuei2576PhosphoserineCombined sources1
Modified residuei2578PhosphothreonineCombined sources1
Cross-linki2627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2640PhosphoserineBy similarity1
Cross-linki2649Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2729PhosphoserineCombined sources1
Modified residuei3036PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Polyubiquitinated by PRKN, which leads to proteasomal degradation.By similarity
The inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9ERU9

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9ERU9

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9ERU9

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

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PaxDbi
Q9ERU9

PeptideAtlas

More...
PeptideAtlasi
Q9ERU9

PRoteomics IDEntifications database

More...
PRIDEi
Q9ERU9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9ERU9

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

More...
PhosphoSitePlusi
Q9ERU9

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q9ERU9

<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
ENSMUSG00000003226 Expressed in 274 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9ERU9 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

Forms a complex with NXT1, NXF1 and RANGAP1 (By similarity). Forms a tight complex with RANBP1 and UBE2I (By similarity). Interacts with SUMO1 but not SUMO2 (By similarity). Interacts with sumoylated RANGAP1 (By similarity). Interacts with CDCA8 (By similarity). Interacts with PML (By similarity). Interacts with BICD2 (By similarity). Interacts with PRKN (PubMed:16332688). Interacts with MCM3AP (By similarity).By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
PrknQ9WVS62EBI-643756,EBI-973635

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
202582, 85 interactors

Protein interaction database and analysis system

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IntActi
Q9ERU9, 91 interactors

Molecular INTeraction database

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MINTi
Q9ERU9

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000003310

<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

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SMRi
Q9ERU9

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati26 – 59TPR 1Add BLAST34
Repeati60 – 93TPR 2Add BLAST34
Repeati94 – 128TPR 3Add BLAST35
Repeati165 – 201TPR 4Add BLAST37
Repeati288 – 319TPR 5Add BLAST32
Repeati583 – 616TPR 6Add BLAST34
Repeati648 – 681TPR 7Add BLAST34
Repeati1000 – 10011By similarity2
Repeati1099 – 11002By similarity2
Repeati1117 – 11183Curated2
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">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>Domaini1165 – 1301RanBD1 1PROSITE-ProRule annotationAdd BLAST137
Repeati1449 – 14504By similarity2
Repeati1538 – 15395By similarity2
Repeati1696 – 16976By similarity2
Repeati1737 – 17387By similarity2
Repeati1775 – 17768By similarity2
Repeati1798 – 17999By similarity2
Domaini1849 – 1985RanBD1 2PROSITE-ProRule annotationAdd BLAST137
Repeati2097 – 209810By similarity2
Domaini2146 – 2282RanBD1 3PROSITE-ProRule annotationAdd BLAST137
Repeati2354 – 235511By similarity2
Repeati2373 – 237412By similarity2
Repeati2383 – 238413By similarity2
Repeati2470 – 25221Add BLAST53
Repeati2546 – 25962Add BLAST51
Repeati2674 – 267514By similarity2
Repeati2676 – 267715By similarity2
Repeati2697 – 269816By similarity2
Repeati2714 – 271517Curated2
Domaini2740 – 2875RanBD1 4PROSITE-ProRule annotationAdd BLAST136
Domaini2896 – 3052PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST157
Repeati2935 – 293618By similarity2
Repeati3018 – 301919By similarity2
Repeati3034 – 303520By similarity2

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>Regioni1000 – 303520 X 2 AA repeats of F-GCuratedAdd BLAST2036
Regioni1984 – 2124Interaction with BICD2By similarityAdd BLAST141
Regioni2468 – 2472Interaction with sumoylated RANGAP1By similarity5
Regioni2470 – 25962 X 50 AA approximate repeatsAdd BLAST127
Regioni2470 – 2545Required for E3 SUMO-ligase activityBy similarityAdd BLAST76
Regioni2470 – 2522Interaction with UBE2IBy similarityAdd BLAST53
Regioni2523 – 2596Interaction with SUMO1By similarityAdd BLAST74

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 biasi2074 – 2079Poly-Ser6
Compositional biasi2506 – 2509Poly-Glu4
Compositional biasi2638 – 2641Poly-Ser4

<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

Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited.Curated
The PPIase cyclophilin-type domain has high structural similarity with PPIA, but has extremely low and barely detectable proline isomerase activity (in vitro) (By similarity). Only about half of the residues that surround the PPIA active site cleft are conserved.By similarity

<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 RanBP2 E3 ligase family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1345 – 1375RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1410 – 1439RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1469 – 1498RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1494 – 1527RanBP2-type 4PROSITE-ProRule annotationAdd BLAST34
Zinc fingeri1558 – 1587RanBP2-type 5PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1617 – 1646RanBP2-type 6PROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Repeat, TPR repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0864 Eukaryota
KOG0865 Eukaryota
COG0652 LUCA
COG5171 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154389

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000089994

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9ERU9

KEGG Orthology (KO)

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KOi
K12172

Identification of Orthologs from Complete Genome Data

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OMAi
CIACQNP

Database of Orthologous Groups

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OrthoDBi
201737at2759

TreeFam database of animal gene trees

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TreeFami
TF314797

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.40.10, 1 hit
2.30.29.30, 4 hits
2.40.100.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029000 Cyclophilin-like_dom_sf
IPR020892 Cyclophilin-type_PPIase_CS
IPR002130 Cyclophilin-type_PPIase_dom
IPR022011 IR1-M
IPR011993 PH-like_dom_sf
IPR000156 Ran_bind_dom
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat
IPR001876 Znf_RanBP2
IPR036443 Znf_RanBP2_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF12185 IR1-M, 2 hits
PF00160 Pro_isomerase, 1 hit
PF00638 Ran_BP1, 4 hits
PF00641 zf-RanBP, 6 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00153 CSAPPISMRASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00160 RanBD, 4 hits
SM00028 TPR, 1 hit
SM00547 ZnF_RBZ, 6 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48452 SSF48452, 1 hit
SSF50891 SSF50891, 1 hit
SSF90209 SSF90209, 4 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00170 CSA_PPIASE_1, 1 hit
PS50072 CSA_PPIASE_2, 1 hit
PS50196 RANBD1, 4 hits
PS50005 TPR, 2 hits
PS50293 TPR_REGION, 1 hit
PS01358 ZF_RANBP2_1, 6 hits
PS50199 ZF_RANBP2_2, 6 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_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>Sequencei

<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.

Q9ERU9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRRSKADVER YIASVQGSAP SPREKSMKGF YFAKLYYEAK EYDLAKKYIS
60 70 80 90 100
TYINVQERDP KAHRFLGLLY EVEENIDKAV ECYKRSVELN PTQKDLVLKI
110 120 130 140 150
AELLCKNDVT DGRAKYWVER AAKLFPGSPA IYKLKEQLLD CKGEDGWNKL
160 170 180 190 200
FDLIQSELYA RPDDIHVNIR LVELYRSNKR LKDAVAHCHE ADRNTALRSS
210 220 230 240 250
LEWNLCVVQT LKEYLESLQC LDSDKSTWRA TNKDLLLAYA NLMLLTLSTR
260 270 280 290 300
DVQEGRELLE SFDSALQSVK SSVGGNDELS ATFLETKGHF YMHVGSLLLK
310 320 330 340 350
MGQQSDIQWR ALSELAALCY LVAFQVPRPK VKLIKGEAGQ NLLETMAHDR
360 370 380 390 400
LSQSGHMLLN LSRGKQDFLK EVVESFANKS GQSALCDALF SSQSSKERSF
410 420 430 440 450
LGNDDIGNLD GQVPDPDDLA RYDTGAVRAH NGSLQHLTWL GLQWNSLSTL
460 470 480 490 500
PAIRKWLKQL FHHLPQETSR LETNAPESIC ILDLEVFLLG VIYTSHLQLK
510 520 530 540 550
EKCNSHHTSY QPLCLPLPVC RQLCTERQKT WWDAVCTLIH RKALPGTSAK
560 570 580 590 600
LRLLVQREIN SLRGQEKHGL QPALLVHWAQ SLQKTGSSLN SFYDQREYIG
610 620 630 640 650
RSVHYWRKVL PLLKMIRKKN SIPEPIDPLF KHFHSVDIQA SEIGEYEEDA
660 670 680 690 700
HITFAILDAV NGNIEDAMTA FESIKNVVSY WNLALIFHRK AEDIENDALS
710 720 730 740 750
PEEQEECKNY LRKTRDYLIR ILDDSDSNTS VVQKLPVPLE SVKEMLNSVM
760 770 780 790 800
QELEDYSEGG TLYKNGCWRS ADSELKHSTP SPTKYSLSPS KSYKYSPKTP
810 820 830 840 850
PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSNNSASPHR WPAEPYGQDP
860 870 880 890 900
APDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
910 920 930 940 950
PVYGMNRLPP QQHIYAYSQQ MHTPPVQSSS ACMFSQEMYG PPLRFESPAT
960 970 980 990 1000
GILSPRGDDY FNYNVQQTST NPPLPEPGYF TKPPLVAHAS RSAESKVIEF
1010 1020 1030 1040 1050
GKSNFVQPMQ GEVIRPPLTT PAHTTQPTPF KFNSNFKSND GDFTFSSPQV
1060 1070 1080 1090 1100
VAQPPSTAYS NSESLLGLLT SDKPLQGDGY SGLKPISGQA SGSRNTFSFG
1110 1120 1130 1140 1150
SKNTLTENMG PNQQKNFGFH RSDDMFAFHG PGKSVFTTAA SELANKSHET
1160 1170 1180 1190 1200
DGGSAHGDEE DDGPHFEPVV PLPDKIEVKT GEEDEEEFFC NRAKLFRFDG
1210 1220 1230 1240 1250
ESKEWKERGI GNVKILRHKT SGKIRLLMRR EQVLKICANH YISPDMKLTP
1260 1270 1280 1290 1300
NAGSDRSFVW HALDYADELP KPEQLAIRFK TPEEAALFKC KFEEAQNILK
1310 1320 1330 1340 1350
ALGTNTSTAP NHTLRIVKES ATQDNKDICK ADGGNLNFEF QIVKKEGPYW
1360 1370 1380 1390 1400
NCNSCSFKNA ATAKKCVSCQ NTNPTSNKEL LGPPLVENGF APKTGLENAQ
1410 1420 1430 1440 1450
DRFATMTANK EGHWDCSVCL VRNEPTVSRC IACQNTKSAS SFVQTSFKFG
1460 1470 1480 1490 1500
QGDLPKSVDS DFRSVFSKKE GQWECSVCLV RNERSAKKCV ACENPGKQFK
1510 1520 1530 1540 1550
EWHCSLCSVK NEAHAIKCVA CNNPVTPSLS TAPPSFKFGT SEMSKPFRIG
1560 1570 1580 1590 1600
FEGMFAKKEG QWDCSLCFVR NEASATHCIA CQYPNKQNQP TSCVSAPASS
1610 1620 1630 1640 1650
ETSRSPKSGF EGLFPKKEGE WECAVCSVQN ESSSLKCVAC EASKPTHKPH
1660 1670 1680 1690 1700
EAPSAFTVGS KSQSNESAGS QVGTEFKSNF PEKNFKVGIS EQKFKFGHVD
1710 1720 1730 1740 1750
QEKTPSFAFQ GGSNTEFKSI KDGFSFCIPV SADGFKFGIQ EKGNQEKKSE
1760 1770 1780 1790 1800
KHLENDPSFQ AHDTSGQKNG SGVVFGQTSS TFTFADLAKS TSREGFQFGK
1810 1820 1830 1840 1850
KDPNFKGFSG AGEKLFSSQS GKVAEKANTS SDLEKDDDAY KTEDSDDIHF
1860 1870 1880 1890 1900
EPVVQMPEKV ELVTGEEDEK VLYSQRVKLF RFDAEISQWK ERGLGNLKIL
1910 1920 1930 1940 1950
KNEVNGKLRM LMRREQVLKV CANHWITTTM NLKPLSGSDR AWMWLASDFS
1960 1970 1980 1990 2000
DGDAKLEQLA AKFKTPELAE EFKQKFEECQ RLLLDIPLQT PHKLVDTGRA
2010 2020 2030 2040 2050
AKLIQRAEEM KSGLKDFKTF LTNDQVKVTD EENASSGADA PSASDTTAKQ
2060 2070 2080 2090 2100
NPDNTGPALE WDNYDLREDA LDDSVSSSSV HASPLASSPV RKNLFRFGES
2110 2120 2130 2140 2150
TTGFNFSFKS ALSPSKSPAK LNQSGASVGT DEESDVTQEE ERDGQYFEPV
2160 2170 2180 2190 2200
VPLPDLVEVS SGEENEQVVF SHRAKLYRYD KDVGQWKERG IGDIKILQNY
2210 2220 2230 2240 2250
DNKQVRIVMR RDQVLKLCAN HRITPDMTLQ TMKGTERVWV WTACDFADGE
2260 2270 2280 2290 2300
RKIEHLAVRF KLQDVADSFK KIFDEAKTAQ EKDSLITPHV SHLSTPRESP
2310 2320 2330 2340 2350
CGKIAIAVLE ETTRERTDLT QGDEVIDTTS EAGETSSTSE TTPKAVVSPP
2360 2370 2380 2390 2400
KFVFGSESVK SIFSSEKSKP FAFGNSSATG SLFGFSFNAP LKNSNSEMTS
2410 2420 2430 2440 2450
RVQSGSEGKV KPDKCELPQN SDIKQSSDGK VKNLSAFSKE NSSTSYTFKT
2460 2470 2480 2490 2500
PEKAQEKSKP EDLPSDNDIL IVYELTPTPE QKALAEKLLL PSTFFCYKNR
2510 2520 2530 2540 2550
PGYVSEEEED DEDYEMAVKK LNGKLYLDDS EKPLEENLAD NDKECVIVWE
2560 2570 2580 2590 2600
KKPTVEERAK ADTLKLPPTF FCGVCSDTDE DNGNGEDFQS ELRKVCEAQK
2610 2620 2630 2640 2650
SQNEKVTDRV GIEHIGETEV TNPVGCKSEE PDSDTKHSSS SPVSGTMDKP
2660 2670 2680 2690 2700
VDLSTRKETD MEFPSKGENK PVLFGFGSGT GLSFADLASS NSGDFAFGSK
2710 2720 2730 2740 2750
DKNFQWANTG AAVFGTQTTS KGGEDEDGSD EDVVHNEDIH FEPIVSLPEV
2760 2770 2780 2790 2800
EVKSGEEDEE VLFKERAKLY RWDRDVSQWK ERGIGDIKIL WHTMKKYYRI
2810 2820 2830 2840 2850
LMRRDQVFKV CANHVITKAM ELKPLNVSNN ALVWTASDYA DGEAKVEQLA
2860 2870 2880 2890 2900
VRFKTKEMTE SFKKKFEECQ QNIIKLQNGH TSLAAELSKD TNPVVFFDVC
2910 2920 2930 2940 2950
ADGEPLGRII MELFSNIVPQ TAENFRALCT GEKGFGFKNS IFHRVVPDFI
2960 2970 2980 2990 3000
CQGGDITKYN GTGGQSIYGD KFDDENFDLK HTGPGLLSMA NYGQNTNSSQ
3010 3020 3030 3040 3050
FFITLKKAEH LDFKHVVFGF VKDGMDTVRK IESFGSPKGS VSRRICITEC

GQL
Length:3,053
Mass (Da):341,121
Last modified:July 27, 2011 - 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:i62FD4249DEE466AE
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 conflicti213 – 222EYLESLQCLD → VGETYFSTVF in BAC31101 (PubMed:16141072).Curated10
Sequence conflicti985 – 1001LVAHA…VIEFG → IPGSRFKVSRIKGYRIWL in CAA60778 (PubMed:8603673).CuratedAdd BLAST17
Sequence conflicti1086 – 1089ISGQ → YLA in CAA60778 (PubMed:8603673).Curated4
Sequence conflicti1269L → F in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1273E → G in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1276A → S in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1280K → Q in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1293E → G in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1297N → D in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti1861E → D in CAA60778 (PubMed:8603673).Curated1
Sequence conflicti2868 – 2869EC → DS in AAG17403 (PubMed:11353387).Curated2

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
AF279458 Genomic DNA Translation: AAG17403.1
AC158593 Genomic DNA No translation available.
AK041932 mRNA Translation: BAC31101.1
X87337 mRNA Translation: CAA60778.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS23861.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S57968

NCBI Reference Sequences

More...
RefSeqi
NP_035370.2, NM_011240.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000003310; ENSMUSP00000003310; ENSMUSG00000003226

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
19386

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:19386

UCSC genome browser

More...
UCSCi
uc007fdd.1 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
AF279458 Genomic DNA Translation: AAG17403.1
AC158593 Genomic DNA No translation available.
AK041932 mRNA Translation: BAC31101.1
X87337 mRNA Translation: CAA60778.1
CCDSiCCDS23861.1
PIRiS57968
RefSeqiNP_035370.2, NM_011240.3

3D structure databases

SMRiQ9ERU9
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202582, 85 interactors
IntActiQ9ERU9, 91 interactors
MINTiQ9ERU9
STRINGi10090.ENSMUSP00000003310

PTM databases

iPTMnetiQ9ERU9
PhosphoSitePlusiQ9ERU9
SwissPalmiQ9ERU9

Proteomic databases

EPDiQ9ERU9
jPOSTiQ9ERU9
MaxQBiQ9ERU9
PaxDbiQ9ERU9
PeptideAtlasiQ9ERU9
PRIDEiQ9ERU9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003310; ENSMUSP00000003310; ENSMUSG00000003226
GeneIDi19386
KEGGimmu:19386
UCSCiuc007fdd.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5903
MGIiMGI:894323 Ranbp2

Phylogenomic databases

eggNOGiKOG0864 Eukaryota
KOG0865 Eukaryota
COG0652 LUCA
COG5171 LUCA
GeneTreeiENSGT00940000154389
HOGENOMiHOG000089994
InParanoidiQ9ERU9
KOiK12172
OMAiCIACQNP
OrthoDBi201737at2759
TreeFamiTF314797

Enzyme and pathway databases

UniPathwayiUPA00886
ReactomeiR-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-159227 Transport of the SLBP independent Mature mRNA
R-MMU-159230 Transport of the SLBP Dependant Mature mRNA
R-MMU-159231 Transport of Mature mRNA Derived from an Intronless Transcript
R-MMU-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-MMU-191859 snRNP Assembly
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins
R-MMU-3301854 Nuclear Pore Complex (NPC) Disassembly
R-MMU-3371453 Regulation of HSF1-mediated heat shock response
R-MMU-4085377 SUMOylation of SUMOylation proteins
R-MMU-4615885 SUMOylation of DNA replication proteins
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-68877 Mitotic Prometaphase

Miscellaneous databases

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

More...
ChiTaRSi
Ranbp2 mouse

Protein Ontology

More...
PROi
PR:Q9ERU9

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000003226 Expressed in 274 organ(s), highest expression level in liver
GenevisibleiQ9ERU9 MM

Family and domain databases

Gene3Di1.25.40.10, 1 hit
2.30.29.30, 4 hits
2.40.100.10, 1 hit
InterProiView protein in InterPro
IPR029000 Cyclophilin-like_dom_sf
IPR020892 Cyclophilin-type_PPIase_CS
IPR002130 Cyclophilin-type_PPIase_dom
IPR022011 IR1-M
IPR011993 PH-like_dom_sf
IPR000156 Ran_bind_dom
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat
IPR001876 Znf_RanBP2
IPR036443 Znf_RanBP2_sf
PfamiView protein in Pfam
PF12185 IR1-M, 2 hits
PF00160 Pro_isomerase, 1 hit
PF00638 Ran_BP1, 4 hits
PF00641 zf-RanBP, 6 hits
PRINTSiPR00153 CSAPPISMRASE
SMARTiView protein in SMART
SM00160 RanBD, 4 hits
SM00028 TPR, 1 hit
SM00547 ZnF_RBZ, 6 hits
SUPFAMiSSF48452 SSF48452, 1 hit
SSF50891 SSF50891, 1 hit
SSF90209 SSF90209, 4 hits
PROSITEiView protein in PROSITE
PS00170 CSA_PPIASE_1, 1 hit
PS50072 CSA_PPIASE_2, 1 hit
PS50196 RANBD1, 4 hits
PS50005 TPR, 2 hits
PS50293 TPR_REGION, 1 hit
PS01358 ZF_RANBP2_1, 6 hits
PS50199 ZF_RANBP2_2, 6 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiRBP2_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: Q9ERU9
Secondary accession number(s): E9QM01, Q61992, Q8C9K9
<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: December 6, 2005
Last sequence update: July 27, 2011
Last modified: June 5, 2019
This is version 161 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

Complete proteome, Reference proteome

Documents

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