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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: GTP-binding nuclear protein Ran

UniprotKB/SwissProt ID: RAN_HUMAN (P62826)

Gene Name: RAN

Synonyms: ARA24

Organism: Homo sapiens (Human).

Function: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Cytoplasm. Melanosome. Note=Predominantly nuclear during interphase (By similarity). Becomes dispersed throughout the cytoplasm during mitosis. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Network with metabolic pathway:
Kegg map ID Pathway Link
map03008Ribosome biogenesis in eukaryotes
map05166HTLV-I infection
map05169Epstein-Barr virus infection
map03013RNA transport
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR001806
IPR002041
IPR005225
IPR013753

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1I2M X-ray 1.76 A A/C1-216Link
1IBR X-ray 2.30 A A/C1-216Link
1K5D X-ray 2.70 A A/D/G/J1-216Link
1K5G X-ray 3.10 A A/D/G/J1-216Link
1QBK X-ray 3.00 A C1-216Link
1RRP X-ray 2.96 A A/C8-211Link
3CH5 X-ray 2.10 A A1-216Link
3EA5 X-ray 2.50 A A/C1-216Link
3GJ0 X-ray 1.48 A A/B2-216Link
3GJ3 X-ray 1.79 A A2-216Link
3GJ4 X-ray 2.15 A A/C2-216Link
3GJ5 X-ray 1.79 A A/C2-216Link
3GJ6 X-ray 2.70 A A2-216Link
3GJ7 X-ray 1.93 A A/C2-216Link
3GJ8 X-ray 1.82 A A/C2-216Link
3GJX X-ray 2.50 A C/F1-216Link
3NBY X-ray 3.42 A C/F5-180Link
3NBZ X-ray 2.80 A C/F5-180Link
3NC0 X-ray 2.90 A C/F5-180Link
3NC1 X-ray 3.35 A C1-180Link
3ZJY X-ray 3.60 A A/D/F1-180Link
4C0Q X-ray 3.42 A C/D2-216Link
4GMX X-ray 2.10 A A1-216Link
4GPT X-ray 2.22 A A1-216Link
4HAT X-ray 1.78 A A1-216Link
4HAU X-ray 2.00 A A1-216Link
4HAV X-ray 2.00 A A1-216Link
4HAW X-ray 1.90 A A1-216Link
4HAX X-ray 2.28 A A1-216Link
4HAY X-ray 2.30 A A1-216Link
4HAZ X-ray 1.90 A A1-216Link
4HB0 X-ray 2.20 A A1-216Link
4HB2 X-ray 1.80 A A1-216Link
4HB3 X-ray 2.80 A A1-216Link
4HB4 X-ray 2.05 A A1-216Link

The S-nitrosylation sites of RAN_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1112PNWHRDLVRV C ENIPIVLCGN HHHHHHHHHH C CCCEEEEEEC 2.02%HC0322178444-
2112PNWHRDLVRV C ENIPIVLCGN HHHHHHHHHH C CCCEEEEEEC 2.02%HC0318335467-
3112PNWHRDLVRV C ENIPIVLCGN HHHHHHHHHH C CCCEEEEEEC 2.02%HC0319366988-
4112PNWHRDLVRV C ENIPIVLCGN HHHHHHHHHH C CCCEEEEEEC 2.02%HC0319483679in vivo
5120RVCENIPIVL C GNKVDIKDRK HHCCCCEEEE E ECCCCCCCCC 3.80%HC0822178444-
6120RVCENIPIVL C GNKVDIKDRK HHCCCCEEEE E ECCCCCCCCC 3.80%HC0818335467-
7120RVCENIPIVL C GNKVDIKDRK HHCCCCEEEE E ECCCCCCCCC 3.80%HC0819366988-
8120RVCENIPIVL C GNKVDIKDRK HHCCCCEEEE E ECCCCCCCCC 3.80%HC0819483679in vivo