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Protein

E3 SUMO-protein ligase RanBP2

Gene

RANBP2

Organism
Homo sapiens (Human)
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 (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:22194619, PubMed:15931224). 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 (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830).1 Publication10 Publications

Caution

Despite the presence of a PPIase cyclophilin-type domain, it has probably no peptidyl-prolyl cis-trans isomerase activity.2 Publications

<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 ‘Function’ 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 fingeri1351 – 1381RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1415 – 1444RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1479 – 1508RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1543 – 1572RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1606 – 1635RanBP2-type 5PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1665 – 1694RanBP2-type 6PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1724 – 1753RanBP2-type 7PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1781 – 1810RanBP2-type 8PROSITE-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

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Reactomei
R-HSA-1169408 ISG15 antiviral mechanism
R-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-HSA-159227 Transport of the SLBP independent Mature mRNA
R-HSA-159230 Transport of the SLBP Dependant Mature mRNA
R-HSA-159231 Transport of Mature mRNA Derived from an Intronless Transcript
R-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-HSA-165054 Rev-mediated nuclear export of HIV RNA
R-HSA-168271 Transport of Ribonucleoproteins into the Host Nucleus
R-HSA-168276 NS1 Mediated Effects on Host Pathways
R-HSA-168325 Viral Messenger RNA Synthesis
R-HSA-168333 NEP/NS2 Interacts with the Cellular Export Machinery
R-HSA-170822 Regulation of Glucokinase by Glucokinase Regulatory Protein
R-HSA-180746 Nuclear import of Rev protein
R-HSA-180910 Vpr-mediated nuclear import of PICs
R-HSA-191859 snRNP Assembly
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-3301854 Nuclear Pore Complex (NPC) Disassembly
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-4085377 SUMOylation of SUMOylation proteins
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-4570464 SUMOylation of RNA binding proteins
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-5578749 Transcriptional regulation by small RNAs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6784531 tRNA processing in the nucleus
R-HSA-68877 Mitotic Prometaphase

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

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UniPathwayi
UPA00886

Protein family/group databases

Transport Classification Database

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TCDBi
1.I.1.1.3 the eukaryotic nuclear pore complex (e-npc) family

<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.-5 Publications)
Alternative name(s):
358 kDa nucleoporin
Nuclear pore complex protein Nup358
Nucleoporin Nup358
Ran-binding protein 2
Short name:
RanBP2
p270
<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
Synonyms:NUP358
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000153201.15

Human Gene Nomenclature Database

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HGNCi
HGNC:9848 RANBP2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601181 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P49792

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Encephalopathy, acute, infection-induced, 3 (IIAE3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. Mutations in the RANBP2 gene predispose to IIAE3, but by themselves are insufficient to make the phenotype fully penetrant; additional genetic and environmental factors are required (PubMed:19118815).1 Publication
Disease descriptionA rapidly progressive encephalopathy manifesting in susceptible individuals with seizures and coma. It can occur within days in otherwise healthy children after common viral infections such as influenza and parainfluenza, without evidence of viral infection of the brain or inflammatory cell infiltration. Brain T2-weighted magnetic resonance imaging reveals characteristic symmetric lesions present in the thalami, pons and brainstem.
See also OMIM:608033
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_054997585T → M in IIAE3. 1 PublicationCorresponds to variant dbSNP:rs121434502EnsemblClinVar.1
Natural variantiVAR_054998653T → I in IIAE3. 1 PublicationCorresponds to variant dbSNP:rs121434503EnsemblClinVar.1
Natural variantiVAR_054999656I → V in IIAE3. 1 PublicationCorresponds to variant dbSNP:rs121434504EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2632V → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication1
Mutagenesisi2634I → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication1
Mutagenesisi2635V → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication1
Mutagenesisi2640P → A: No effect on SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2645K → A: No effect on SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2651L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2652K → A: No effect on SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2653L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2654P → A: Impairs SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2655P → A: No effect on SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2656T → A: Impairs SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2657F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2658F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2659C → S or A: Impairs SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2676D → A: Impairs SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2677F → A: Impairs SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2689Y → A: Impairs SUMO E3 ligase activity. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
5903

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
RANBP2

MalaCards human disease database

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MalaCardsi
RANBP2
MIMi608033 phenotype

Open Targets

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OpenTargetsi
ENSG00000153201

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
263524 Acute necrotizing encephalopathy of childhood
88619 Familial acute necrotizing encephalopathy
178342 Inflammatory myofibroblastic tumor

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34209

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RANBP2

Domain mapping of disease mutations (DMDM)

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DMDMi
83305554

<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_00002049131 – 3224E3 SUMO-protein ligase RanBP2Add BLAST3224

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 residuei19PhosphothreonineCombined sources1
Modified residuei21PhosphoserineCombined sources1
Modified residuei779PhosphothreonineCombined sources1
Modified residuei781PhosphoserineCombined sources1
Modified residuei788PhosphoserineBy similarity1
Modified residuei837PhosphoserineCombined sources1
Modified residuei945Asymmetric dimethylarginineCombined sources1
Modified residuei948PhosphoserineCombined sources1
Modified residuei955PhosphoserineCombined sources1
Modified residuei1016Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei1016Omega-N-methylarginine; alternateCombined sources1
Modified residuei1098PhosphothreonineCombined sources1
Modified residuei1103PhosphoserineCombined sources1
Modified residuei1107PhosphoserineCombined sources1
Modified residuei1110PhosphoserineCombined sources1
Modified residuei1144PhosphothreonineCombined sources1
Modified residuei1160PhosphoserineCombined sources1
Modified residuei1249PhosphoserineCombined sources1
<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-linki1350Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1396PhosphothreonineCombined sources1
Modified residuei1412PhosphothreonineCombined sources1
Cross-linki1414Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1443PhosphoserineCombined sources1
Modified residuei1450PhosphoserineCombined sources1
Modified residuei1456PhosphoserineCombined sources1
Modified residuei1509PhosphoserineCombined sources1
Modified residuei1520PhosphoserineCombined sources1
Modified residuei1573PhosphoserineCombined sources1
Cross-linki1596Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1605Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki1605Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki1655Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki1664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki1714Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1723Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki1723Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei1833PhosphoserineCombined sources1
Modified residuei1835PhosphoserineCombined sources1
Modified residuei1869PhosphoserineCombined sources1
Modified residuei1871PhosphoserineCombined sources1
Modified residuei1977N6-acetyllysineBy similarity1
Modified residuei2005PhosphothreonineBy similarity1
Modified residuei2008PhosphoserineBy similarity1
Cross-linki2022Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei2153PhosphothreonineBy similarity1
Modified residuei2246PhosphoserineBy similarity1
Modified residuei2251PhosphoserineBy similarity1
Modified residuei2270PhosphoserineCombined sources1
Modified residuei2280PhosphoserineBy similarity1
Modified residuei2290PhosphoserineBy similarity1
Modified residuei2293PhosphothreonineBy similarity1
Modified residuei2297PhosphoserineBy similarity1
Modified residuei2462PhosphoserineBy similarity1
Modified residuei2493PhosphoserineBy similarity1
Modified residuei2510PhosphoserineBy similarity1
Cross-linki2522Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei2526PhosphoserineCombined sources1
Cross-linki2592Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki2594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki2594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki2612Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei2613PhosphothreonineCombined sources1
Modified residuei2666PhosphotyrosineCombined sources1
Modified residuei2668PhosphoserineCombined sources1
Modified residuei2741PhosphoserineCombined sources1
Modified residuei2743PhosphothreonineCombined sources1
Cross-linki2792Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei2805PhosphoserineCombined sources1
Cross-linki2815Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei2900PhosphoserineCombined sources1
Modified residuei3207PhosphoserineCombined sources1

<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.1 Publication
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.By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P49792

MaxQB - The MaxQuant DataBase

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MaxQBi
P49792

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

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PaxDbi
P49792

PeptideAtlas

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PeptideAtlasi
P49792

PRoteomics IDEntifications database

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PRIDEi
P49792

ProteomicsDB human proteome resource

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ProteomicsDBi
56121

2D gel databases

USC-OGP 2-DE database

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OGPi
P49792

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P49792

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

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PhosphoSitePlusi
P49792

SwissPalm database of S-palmitoylation events

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SwissPalmi
P49792

<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

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Bgeei
ENSG00000153201 Expressed in 245 organ(s), highest expression level in biceps brachii

CleanEx database of gene expression profiles

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CleanExi
HS_RANBP2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P49792 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P49792 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB034063
HPA018437
HPA023960
HPA049497
HPA051675
HPA067564

<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 (PubMed:14729961). Forms a tight complex with RANBP1 and UBE2I (PubMed:15388847, PubMed:10078529, PubMed:15826666). Interacts with SUMO1 but not SUMO2 (PubMed:15388847, PubMed:10078529, PubMed:15826666). Interacts with PRKN (PubMed:16332688). Interacts with sumoylated RANGAP1 (PubMed:15378033, PubMed:10078529, PubMed:15826666). Interacts with CDCA8 (PubMed:19413330). Interacts with PML (isoform PML-4) (PubMed:22155184). Interacts with BICD2 (PubMed:20386726).8 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111839, 159 interactors

Database of interacting proteins

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DIPi
DIP-37654N

Protein interaction database and analysis system

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IntActi
P49792, 69 interactors

Molecular INTeraction database

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MINTi
P49792

STRING: functional protein association networks

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STRINGi
9606.ENSP00000283195

<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

13224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P49792

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

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SMRi
P49792

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P49792

<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 1PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati60 – 93TPR 2PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati94 – 128TPR 3PROSITE-ProRule annotation1 PublicationAdd BLAST35
Repeati165 – 201TPR 4PROSITE-ProRule annotation1 PublicationAdd BLAST37
Repeati287 – 319TPR 5PROSITE-ProRule annotation1 PublicationAdd BLAST33
Repeati583 – 616TPR 6PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati648 – 681TPR 7PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati1001 – 10021Curated2
Repeati1101 – 11022Curated2
Repeati1142 – 11433Curated2
<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>Domaini1171 – 1307RanBD1 1PROSITE-ProRule annotationAdd BLAST137
Repeati1459 – 14604Curated2
Repeati1523 – 15245Curated2
Repeati1586 – 15876Curated2
Repeati1852 – 18537Curated2
Repeati1861 – 18628Curated2
Repeati1900 – 19019Curated2
Repeati1938 – 193910Curated2
Repeati1961 – 196211Curated2
Domaini2012 – 2148RanBD1 2PROSITE-ProRule annotationAdd BLAST137
Repeati2260 – 226112Curated2
Domaini2309 – 2445RanBD1 3PROSITE-ProRule annotationAdd BLAST137
Repeati2516 – 251713Curated2
Repeati2535 – 253614Curated2
Repeati2545 – 254615Curated2
Repeati2633 – 268511 PublicationAdd BLAST53
Repeati2711 – 276121 PublicationAdd BLAST51
Repeati2840 – 284116Curated2
Repeati2842 – 284317Curated2
Repeati2863 – 286418Curated2
Repeati2880 – 288119Curated2
Domaini2911 – 3046RanBD1 4PROSITE-ProRule annotationAdd BLAST136
Domaini3067 – 3223PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST157
Repeati3106 – 310720Curated2
Repeati3189 – 319021Curated2
Repeati3205 – 320622Curated2

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>Regioni1001 – 320622 X 2 AA repeats of F-GCuratedAdd BLAST2206
Regioni2147 – 2287Interaction with BICD21 PublicationAdd BLAST141
Regioni2631 – 2635Interaction with sumoylated RANGAP15
Regioni2633 – 27612 X 50 AA approximate repeatsAdd BLAST129
Regioni2633 – 2710Required for E3 SUMO-ligase activityAdd BLAST78
Regioni2633 – 2685Interaction with UBE2IAdd BLAST53
Regioni2686 – 2761Interaction with SUMO11 PublicationAdd BLAST76

<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) (PubMed:23353830). Only about half of the residues that surround the PPIA active site cleft are conserved.1 Publication

<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 fingeri1351 – 1381RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1415 – 1444RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1479 – 1508RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1543 – 1572RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1606 – 1635RanBP2-type 5PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1665 – 1694RanBP2-type 6PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1724 – 1753RanBP2-type 7PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1781 – 1810RanBP2-type 8PROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Repeat, TPR repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0864 Eukaryota
KOG0865 Eukaryota
COG0652 LUCA
COG5171 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154389

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000089994

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG092361

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P49792

KEGG Orthology (KO)

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KOi
K12172

Identification of Orthologs from Complete Genome Data

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OMAi
EGMFTKK

Database of Orthologous Groups

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OrthoDBi
EOG091G0BGL

Database for complete collections of gene phylogenies

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PhylomeDBi
P49792

TreeFam database of animal gene trees

More...
TreeFami
TF314797

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
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

More...
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

More...
Pfami
View protein in Pfam
PF12185 IR1-M, 2 hits
PF00160 Pro_isomerase, 1 hit
PF00638 Ran_BP1, 4 hits
PF00641 zf-RanBP, 8 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

More...
SMARTi
View protein in SMART
SM00160 RanBD, 4 hits
SM00028 TPR, 1 hit
SM00547 ZnF_RBZ, 8 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48452 SSF48452, 1 hit
SSF50891 SSF50891, 1 hit
SSF90209 SSF90209, 7 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00170 CSA_PPIASE_1, 1 hit
PS50072 CSA_PPIASE_2, 1 hit
PS50196 RANBD1, 4 hits
PS50005 TPR, 1 hit
PS50293 TPR_REGION, 1 hit
PS01358 ZF_RANBP2_1, 8 hits
PS50199 ZF_RANBP2_2, 8 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>.<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

P49792-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRRSKADVER YIASVQGSTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC
60 70 80 90 100
TYINVQERDP KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI
110 120 130 140 150
AELLCKNDVT DGRAKYWLER AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL
160 170 180 190 200
FDLIQSELYV RPDDVHVNIR LVEVYRSTKR LKDAVAHCHE AERNIALRSS
210 220 230 240 250
LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA NLMLLTLSTR
260 270 280 290 300
DVQESRELLQ SFDSALQSVK SLGGNDELSA TFLEMKGHFY MHAGSLLLKM
310 320 330 340 350
GQHSSNVQWR ALSELAALCY LIAFQVPRPK IKLIKGEAGQ NLLEMMACDR
360 370 380 390 400
LSQSGHMLLN LSRGKQDFLK EIVETFANKS GQSALYDALF SSQSPKDTSF
410 420 430 440 450
LGSDDIGNID VREPELEDLT RYDVGAIRAH NGSLQHLTWL GLQWNSLPAL
460 470 480 490 500
PGIRKWLKQL FHHLPHETSR LETNAPESIC ILDLEVFLLG VVYTSHLQLK
510 520 530 540 550
EKCNSHHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH RKAVPGNVAK
560 570 580 590 600
LRLLVQHEIN TLRAQEKHGL QPALLVHWAE CLQKTGSGLN SFYDQREYIG
610 620 630 640 650
RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA
660 670 680 690 700
HITFAILDAV NGNIEDAVTA FESIKSVVSY WNLALIFHRK AEDIENDALS
710 720 730 740 750
PEEQEECKNY LRKTRDYLIK IIDDSDSNLS VVKKLPVPLE SVKEMLNSVM
760 770 780 790 800
QELEDYSEGG PLYKNGSLRN ADSEIKHSTP SPTRYSLSPS KSYKYSPKTP
810 820 830 840 850
PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSSNSASPHR WPTENYGPDS
860 870 880 890 900
VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
910 920 930 940 950
PVYGMNRLPP QQHIYAYPQQ MHTPPVQSSS ACMFSQEMYG PPALRFESPA
960 970 980 990 1000
TGILSPRGDD YFNYNVQQTS TNPPLPEPGY FTKPPIAAHA SRSAESKTIE
1010 1020 1030 1040 1050
FGKTNFVQPM PGEGLRPSLP TQAHTTQPTP FKFNSNFKSN DGDFTFSSPQ
1060 1070 1080 1090 1100
VVTQPPPAAY SNSESLLGLL TSDKPLQGDG YSGAKPIPGG QTIGPRNTFN
1110 1120 1130 1140 1150
FGSKNVSGIS FTENMGSSQQ KNSGFRRSDD MFTFHGPGKS VFGTPTLETA
1160 1170 1180 1190 1200
NKNHETDGGS AHGDDDDDGP HFEPVVPLPD KIEVKTGEED EEEFFCNRAK
1210 1220 1230 1240 1250
LFRFDVESKE WKERGIGNVK ILRHKTSGKI RLLMRREQVL KICANHYISP
1260 1270 1280 1290 1300
DMKLTPNAGS DRSFVWHALD YADELPKPEQ LAIRFKTPEE AALFKCKFEE
1310 1320 1330 1340 1350
AQSILKAPGT NVAMASNQAV RIVKEPTSHD NKDICKSDAG NLNFEFQVAK
1360 1370 1380 1390 1400
KEGSWWHCNS CSLKNASTAK KCVSCQNLNP SNKELVGPPL AETVFTPKTS
1410 1420 1430 1440 1450
PENVQDRFAL VTPKKEGHWD CSICLVRNEP TVSRCIACQN TKSANKSGSS
1460 1470 1480 1490 1500
FVHQASFKFG QGDLPKPINS DFRSVFSTKE GQWDCSACLV QNEGSSTKCA
1510 1520 1530 1540 1550
ACQNPRKQSL PATSIPTPAS FKFGTSETSK TLKSGFEDMF AKKEGQWDCS
1560 1570 1580 1590 1600
SCLVRNEANA TRCVACQNPD KPSPSTSVPA PASFKFGTSE TSKAPKSGFE
1610 1620 1630 1640 1650
GMFTKKEGQW DCSVCLVRNE ASATKCIACQ NPGKQNQTTS AVSTPASSET
1660 1670 1680 1690 1700
SKAPKSGFEG MFTKKEGQWD CSVCLVRNEA SATKCIACQN PGKQNQTTSA
1710 1720 1730 1740 1750
VSTPASSETS KAPKSGFEGM FTKKEGQWDC SVCLVRNEAS ATKCIACQCP
1760 1770 1780 1790 1800
SKQNQTTAIS TPASSEISKA PKSGFEGMFI RKGQWDCSVC CVQNESSSLK
1810 1820 1830 1840 1850
CVACDASKPT HKPIAEAPSA FTLGSEMKLH DSSGSQVGTG FKSNFSEKAS
1860 1870 1880 1890 1900
KFGNTEQGFK FGHVDQENSP SFMFQGSSNT EFKSTKEGFS IPVSADGFKF
1910 1920 1930 1940 1950
GISEPGNQEK KSEKPLENGT GFQAQDISGQ KNGRGVIFGQ TSSTFTFADL
1960 1970 1980 1990 2000
AKSTSGEGFQ FGKKDPNFKG FSGAGEKLFS SQYGKMANKA NTSGDFEKDD
2010 2020 2030 2040 2050
DAYKTEDSDD IHFEPVVQMP EKVELVTGEE DEKVLYSQRV KLFRFDAEVS
2060 2070 2080 2090 2100
QWKERGLGNL KILKNEVNGK LRMLMRREQV LKVCANHWIT TTMNLKPLSG
2110 2120 2130 2140 2150
SDRAWMWLAS DFSDGDAKLE QLAAKFKTPE LAEEFKQKFE ECQRLLLDIP
2160 2170 2180 2190 2200
LQTPHKLVDT GRAAKLIQRA EEMKSGLKDF KTFLTNDQTK VTEEENKGSG
2210 2220 2230 2240 2250
TGAAGASDTT IKPNPENTGP TLEWDNYDLR EDALDDSVSS SSVHASPLAS
2260 2270 2280 2290 2300
SPVRKNLFRF GESTTGFNFS FKSALSPSKS PAKLNQSGTS VGTDEESDVT
2310 2320 2330 2340 2350
QEEERDGQYF EPVVPLPDLV EVSSGEENEQ VVFSHRAKLY RYDKDVGQWK
2360 2370 2380 2390 2400
ERGIGDIKIL QNYDNKQVRI VMRRDQVLKL CANHRITPDM TLQNMKGTER
2410 2420 2430 2440 2450
VWLWTACDFA DGERKVEHLA VRFKLQDVAD SFKKIFDEAK TAQEKDSLIT
2460 2470 2480 2490 2500
PHVSRSSTPR ESPCGKIAVA VLEETTRERT DVIQGDDVAD ATSEVEVSST
2510 2520 2530 2540 2550
SETTPKAVVS PPKFVFGSES VKSIFSSEKS KPFAFGNSSA TGSLFGFSFN
2560 2570 2580 2590 2600
APLKSNNSET SSVAQSGSES KVEPKKCELS KNSDIEQSSD SKVKNLFASF
2610 2620 2630 2640 2650
PTEESSINYT FKTPEKAKEK KKPEDSPSDD DVLIVYELTP TAEQKALATK
2660 2670 2680 2690 2700
LKLPPTFFCY KNRPDYVSEE EEDDEDFETA VKKLNGKLYL DGSEKCRPLE
2710 2720 2730 2740 2750
ENTADNEKEC IIVWEKKPTV EEKAKADTLK LPPTFFCGVC SDTDEDNGNG
2760 2770 2780 2790 2800
EDFQSELQKV QEAQKSQTEE ITSTTDSVYT GGTEVMVPSF CKSEEPDSIT
2810 2820 2830 2840 2850
KSISSPSVSS ETMDKPVDLS TRKEIDTDST SQGESKIVSF GFGSSTGLSF
2860 2870 2880 2890 2900
ADLASSNSGD FAFGSKDKNF QWANTGAAVF GTQSVGTQSA GKVGEDEDGS
2910 2920 2930 2940 2950
DEEVVHNEDI HFEPIVSLPE VEVKSGEEDE EILFKERAKL YRWDRDVSQW
2960 2970 2980 2990 3000
KERGVGDIKI LWHTMKNYYR ILMRRDQVFK VCANHVITKT MELKPLNVSN
3010 3020 3030 3040 3050
NALVWTASDY ADGEAKVEQL AVRFKTKEVA DCFKKTFEEC QQNLMKLQKG
3060 3070 3080 3090 3100
HVSLAAELSK ETNPVVFFDV CADGEPLGRI TMELFSNIVP RTAENFRALC
3110 3120 3130 3140 3150
TGEKGFGFKN SIFHRVIPDF VCQGGDITKH DGTGGQSIYG DKFEDENFDV
3160 3170 3180 3190 3200
KHTGPGLLSM ANQGQNTNNS QFVITLKKAE HLDFKHVVFG FVKDGMDTVK
3210 3220
KIESFGSPKG SVCRRITITE CGQI
Length:3,224
Mass (Da):358,199
Last modified:December 6, 2005 - 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:i4CD9A3D5E77183FB
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
F8WBP7F8WBP7_HUMAN
E3 SUMO-protein ligase RanBP2
RANBP2
51Annotation 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 conflicti777H → R in AAC41758 (PubMed:7775481).Curated1
Sequence conflicti2207S → A in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2210T → P in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2216E → V in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2436F → C in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2475T → P in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2531K → N in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2545F → C (PubMed:7724562).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029765548V → L. Corresponds to variant dbSNP:rs1057954Ensembl.1
Natural variantiVAR_029766580E → K. Corresponds to variant dbSNP:rs1057956EnsemblClinVar.1
Natural variantiVAR_029767581C → Y. Corresponds to variant dbSNP:rs1057957Ensembl.1
Natural variantiVAR_054997585T → M in IIAE3. 1 PublicationCorresponds to variant dbSNP:rs121434502EnsemblClinVar.1
Natural variantiVAR_054998653T → I in IIAE3. 1 PublicationCorresponds to variant dbSNP:rs121434503EnsemblClinVar.1
Natural variantiVAR_054999656I → V in IIAE3. 1 PublicationCorresponds to variant dbSNP:rs121434504EnsemblClinVar.1
Natural variantiVAR_050575725S → G. Corresponds to variant dbSNP:rs17414315EnsemblClinVar.1
Natural variantiVAR_023939784R → K1 PublicationCorresponds to variant dbSNP:rs2912838EnsemblClinVar.1
Natural variantiVAR_0297681870P → L. Corresponds to variant dbSNP:rs2889846Ensembl.1
Natural variantiVAR_0148861892P → A. Corresponds to variant dbSNP:rs12770Ensembl.1
Natural variantiVAR_0505761892P → R. Corresponds to variant dbSNP:rs12770Ensembl.1

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
L41840 Genomic DNA Translation: AAC41758.1
D42063 mRNA Translation: BAA07662.1
AC010095 Genomic DNA Translation: AAY14984.1
AB209483 mRNA Translation: BAD92720.1
U19248 mRNA Translation: AAA85838.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2079.1

Protein sequence database of the Protein Information Resource

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PIRi
S58884

NCBI Reference Sequences

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RefSeqi
NP_006258.3, NM_006267.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.199561
Hs.715056

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000283195; ENSP00000283195; ENSG00000153201

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5903

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5903

UCSC genome browser

More...
UCSCi
uc002tem.4 human

Keywords - Coding sequence diversityi

Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L41840 Genomic DNA Translation: AAC41758.1
D42063 mRNA Translation: BAA07662.1
AC010095 Genomic DNA Translation: AAY14984.1
AB209483 mRNA Translation: BAD92720.1
U19248 mRNA Translation: AAA85838.1
CCDSiCCDS2079.1
PIRiS58884
RefSeqiNP_006258.3, NM_006267.4
UniGeneiHs.199561
Hs.715056

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RRPX-ray2.96B/D1171-1304[»]
1XKENMR-A2028-2154[»]
1Z5SX-ray3.01D2631-2711[»]
2LASNMR-B2705-2717[»]
3UINX-ray2.60D2629-2695[»]
3UIOX-ray2.60D2631-2695[»]
3UIPX-ray2.29D2631-2695[»]
4GA0X-ray1.15A1-145[»]
4I9YX-ray1.75A/B/C/D/E/F3062-3224[»]
4L6EX-ray2.50A2907-3050[»]
4LQWX-ray1.95A/B3057-3224[»]
5CLLX-ray2.45B/D1155-1321[»]
5CLQX-ray3.20B/D1155-1321[»]
ProteinModelPortaliP49792
SMRiP49792
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111839, 159 interactors
DIPiDIP-37654N
IntActiP49792, 69 interactors
MINTiP49792
STRINGi9606.ENSP00000283195

Protein family/group databases

TCDBi1.I.1.1.3 the eukaryotic nuclear pore complex (e-npc) family

PTM databases

iPTMnetiP49792
PhosphoSitePlusiP49792
SwissPalmiP49792

Polymorphism and mutation databases

BioMutaiRANBP2
DMDMi83305554

2D gel databases

OGPiP49792

Proteomic databases

EPDiP49792
MaxQBiP49792
PaxDbiP49792
PeptideAtlasiP49792
PRIDEiP49792
ProteomicsDBi56121

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000283195; ENSP00000283195; ENSG00000153201
GeneIDi5903
KEGGihsa:5903
UCSCiuc002tem.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5903
DisGeNETi5903
EuPathDBiHostDB:ENSG00000153201.15

GeneCards: human genes, protein and diseases

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GeneCardsi
RANBP2
GeneReviewsiRANBP2

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0002358
HGNCiHGNC:9848 RANBP2
HPAiCAB034063
HPA018437
HPA023960
HPA049497
HPA051675
HPA067564
MalaCardsiRANBP2
MIMi601181 gene
608033 phenotype
neXtProtiNX_P49792
OpenTargetsiENSG00000153201
Orphaneti263524 Acute necrotizing encephalopathy of childhood
88619 Familial acute necrotizing encephalopathy
178342 Inflammatory myofibroblastic tumor
PharmGKBiPA34209

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG0864 Eukaryota
KOG0865 Eukaryota
COG0652 LUCA
COG5171 LUCA
GeneTreeiENSGT00940000154389
HOGENOMiHOG000089994
HOVERGENiHBG092361
InParanoidiP49792
KOiK12172
OMAiEGMFTKK
OrthoDBiEOG091G0BGL
PhylomeDBiP49792
TreeFamiTF314797

Enzyme and pathway databases

UniPathwayi
UPA00886

ReactomeiR-HSA-1169408 ISG15 antiviral mechanism
R-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-HSA-159227 Transport of the SLBP independent Mature mRNA
R-HSA-159230 Transport of the SLBP Dependant Mature mRNA
R-HSA-159231 Transport of Mature mRNA Derived from an Intronless Transcript
R-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-HSA-165054 Rev-mediated nuclear export of HIV RNA
R-HSA-168271 Transport of Ribonucleoproteins into the Host Nucleus
R-HSA-168276 NS1 Mediated Effects on Host Pathways
R-HSA-168325 Viral Messenger RNA Synthesis
R-HSA-168333 NEP/NS2 Interacts with the Cellular Export Machinery
R-HSA-170822 Regulation of Glucokinase by Glucokinase Regulatory Protein
R-HSA-180746 Nuclear import of Rev protein
R-HSA-180910 Vpr-mediated nuclear import of PICs
R-HSA-191859 snRNP Assembly
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-3301854 Nuclear Pore Complex (NPC) Disassembly
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-4085377 SUMOylation of SUMOylation proteins
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-4570464 SUMOylation of RNA binding proteins
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-5578749 Transcriptional regulation by small RNAs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6784531 tRNA processing in the nucleus
R-HSA-68877 Mitotic Prometaphase

Miscellaneous databases

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

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ChiTaRSi
RANBP2 human
EvolutionaryTraceiP49792

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
RANBP2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
5903

Protein Ontology

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PROi
PR:P49792

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000153201 Expressed in 245 organ(s), highest expression level in biceps brachii
CleanExiHS_RANBP2
ExpressionAtlasiP49792 baseline and differential
GenevisibleiP49792 HS

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, 8 hits
PRINTSiPR00153 CSAPPISMRASE
SMARTiView protein in SMART
SM00160 RanBD, 4 hits
SM00028 TPR, 1 hit
SM00547 ZnF_RBZ, 8 hits
SUPFAMiSSF48452 SSF48452, 1 hit
SSF50891 SSF50891, 1 hit
SSF90209 SSF90209, 7 hits
PROSITEiView protein in PROSITE
PS00170 CSA_PPIASE_1, 1 hit
PS50072 CSA_PPIASE_2, 1 hit
PS50196 RANBD1, 4 hits
PS50005 TPR, 1 hit
PS50293 TPR_REGION, 1 hit
PS01358 ZF_RANBP2_1, 8 hits
PS50199 ZF_RANBP2_2, 8 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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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 nameiRBP2_HUMAN
<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: P49792
Secondary accession number(s): Q13074
, Q15280, Q53TE2, Q59FH7
<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: October 1, 1996
Last sequence update: December 6, 2005
Last modified: December 5, 2018
This is version 214 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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