RAN_DROME - dbPTM
RAN_DROME - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
71AcetylationWDTAGQEKFGGLRDG
EECCCCCCCCCCCCC
41.2321791702
99AcetylationVTSRVTYKNVPNWHR
CCCCCEECCCCCHHH
41.9421791702
135PhosphorylationDRKVKAKSIVFHRKK
CCEEECEEEEEEECC
28.9219429919
191AcetylationPPEVKMDKDWQAQIE
CCCCCCCHHHHHHHH
58.3221791702
207PhosphorylationDLQEAQATALPDEDE
HHHHHHHHCCCCCCC
19.3521082442

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAN_DROME !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KPYK_DROMEPyKphysical
14605208
CH36_DROMECp36physical
14605208
SUB_DROMEsubgenetic
22100918

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAN_DROME

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Related Literatures of Post-Translational Modification

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