UniProt ID | RAN_DROME | |
---|---|---|
UniProt AC | Q9VZ23 | |
Protein Name | GTP-binding nuclear protein Ran | |
Gene Name | Ran {ECO:0000312|FlyBase:FBgn0020255} | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 216 | |
Subcellular Localization | Nucleus . Nucleus envelope . Cytoplasm . Cytoplasm, cytoskeleton, spindle . Localizes around the microtubule spindle during mitosis. | |
Protein Description | GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis (By similarity). GTP-bound Ran modulates both spindle and nuclear envelope assembly, supporting a role during mitosis. [PubMed: 12121620] | |
Protein Sequence | MAQEGQDIPTFKCVLVGDGGTGKTTFVKRHMTGEFEKKYVATLGVEVHPLIFHTNRGAIRFNVWDTAGQEKFGGLRDGYYIQGQCAVIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLVGDPNLEFVAMPALLPPEVKMDKDWQAQIERDLQEAQATALPDEDEEL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
71 | Acetylation | WDTAGQEKFGGLRDG EECCCCCCCCCCCCC | 41.23 | 21791702 | |
99 | Acetylation | VTSRVTYKNVPNWHR CCCCCEECCCCCHHH | 41.94 | 21791702 | |
135 | Phosphorylation | DRKVKAKSIVFHRKK CCEEECEEEEEEECC | 28.92 | 19429919 | |
191 | Acetylation | PPEVKMDKDWQAQIE CCCCCCCHHHHHHHH | 58.32 | 21791702 | |
207 | Phosphorylation | DLQEAQATALPDEDE HHHHHHHHCCCCCCC | 19.35 | 21082442 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of RAN_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAN_DROME !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of RAN_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
KPYK_DROME | PyK | physical | 14605208 | |
CH36_DROME | Cp36 | physical | 14605208 | |
SUB_DROME | sub | genetic | 22100918 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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