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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: E3 SUMO-protein ligase RanBP2

UniprotKB/SwissProt ID: Q9ERU9 (Q9ERU9)

Gene Name: Ranbp2

Organism: Mus musculus (Mouse)

Function: 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. Inhibits EIF4E-dependent mRNA export. 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

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Nucleus membrane. Nucleus, nuclear pore complex. Nucleus envelope

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
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
IPR045255 RanBP1-like
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_rpt
IPR001876 Znf_RanBP2
IPR036443 Znf_RanBP2_sf

The S-nitrosylation sites of Q9ERU9

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 2951 IFHRVVPDFI C QGGDITKYNG