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Details on Person UniProt:P49792 RANBP2
| Class:Id | ReferenceGeneProduct:62874 |
|---|---|
| _chainChangeLog | chain:1-3224 added on Sat February 7 2015 |
| _displayName | UniProt:P49792 RANBP2 |
| _timestamp | 2024-11-03 20:07:17 |
| chain | chain:1-3224 |
| checksum | 4CD9A3D5E77183FB |
| comment | FUNCTION E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). 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). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). 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).PATHWAY Protein modification; protein sumoylation.SUBUNIT Part of the nuclear pore complex (PubMed:11839768, PubMed:20386726, PubMed:23353830, PubMed:7603572). Forms a complex with NXT1, NXF1 and RANGAP1 (PubMed:14729961). Forms a tight complex with RANBP1 and UBE2I (PubMed:10078529, PubMed:15388847, PubMed:15826666). Interacts with SUMO1 but not SUMO2 (PubMed:10078529, PubMed:15388847, PubMed:15826666). Interacts with PRKN (PubMed:16332688). Interacts with sumoylated RANGAP1 (PubMed:10078529, PubMed:15378033, PubMed:15826666). Interacts with CDCA8 (PubMed:19413330). Interacts with PML (isoform PML-4) (PubMed:22155184). Interacts with BICD2 (PubMed:20386726). Interacts with MCM3AP isoform GANP (PubMed:20005110). Interacts with COX11 (PubMed:34400285). Interacts with synaptic plasticity regulator PANTS (By similarity).SUBUNIT (Microbial infection) Interacts with HIV-1 Vpu protein; this interaction allows Vpu to down-regulate BLM sumoylation.INTERACTION Detected in diffuse and discrete intranuclear foci (PubMed:11839768). Cytoplasmic filaments (PubMed:7775481).DOMAIN 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.DOMAIN 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.PTM Polyubiquitinated by PRKN, which leads to proteasomal degradation.PTM 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.DISEASE The disease is caused by variants 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).DISEASE A chromosomal aberration involving RANBP2 is a cause of chromosome 8p11 myeloproliferative syndrome. Translocation t(2;8)(q12;p11) with FGFR1. Chromosome 8p11 myeloproliferative syndrome is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia.SIMILARITY Belongs to the RanBP2 E3 ligase family.CAUTION Despite the presence of a PPIase cyclophilin-type domain, it has probably no peptidyl-prolyl cis-trans isomerase activity. |
| description | recommendedName: E3 SUMO-protein ligase RanBP2 ecNumber evidence="8 10 12 16 23"2.3.2.- alternativeName: 358 kDa nucleoporin alternativeName: Nuclear pore complex protein Nup358 alternativeName: Nucleoporin Nup358 alternativeName: Ran-binding protein 2 shortName: RanBP2 alternativeName: p270 |
| geneName | RANBP2 NUP358 |
| identifier | P49792 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Chromosomal rearrangement Disulfide bond Isopeptide bond Membrane Metal-binding Methylation mRNA transport Nuclear pore complex Nucleus Phosphoprotein Protein transport Proteomics identification Reference proteome Repeat RNA-binding TPR repeat Transferase Translocation Transport Ubl conjugation Ubl conjugation pathway Zinc Zinc-finger |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | RANBP2 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8993856] ENSEMBL:ENSG00000153201 RANBP2 [Homo sapiens] |
| secondaryIdentifier | RBP2_HUMAN Q13074 Q15280 Q53TE2 Q59FH7 |
| sequenceLength | 3224 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:157703] RANBP2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:2993756] RANBP2 [nuclear envelope] [Homo sapiens] [EntityWithAccessionedSequence:4551599] monoSUMO1-K2592,K2650,K2723-RANBP2 [nuclear envelope] [Homo sapiens] [EntityWithAccessionedSequence:4551720] polySUMO2-K2652,K2725-RANBP2 [nuclear envelope] [Homo sapiens] [EntityWithAccessionedSequence:9702002] RANBP2(1-867)-ALK(1058-1620) fusion [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:9718443] RANBP2(1-867)-p-7Y-ALK(1058-1620) fusion [cytosol] [Homo sapiens] |
| (referenceSequence) | [GroupModifiedResidue:4551621] sumoylated lysine (polySUMO2 [nucleoplasm]) at 2725 [GroupModifiedResidue:4551634] sumoylated lysine (monoSUMO1 [nucleoplasm]) at 2723 [GroupModifiedResidue:4551670] sumoylated lysine (monoSUMO1 [nucleoplasm]) at 2592 [GroupModifiedResidue:4551688] sumoylated lysine (monoSUMO1 [nucleoplasm]) at 2650 [GroupModifiedResidue:4551703] sumoylated lysine (polySUMO2 [nucleoplasm]) at 2652 |
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No pathways have been reviewed or authored by UniProt:P49792 RANBP2 (62874)
