RAN_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAN_RAT
• UniProt AC: P62828
• Protein Name: GTP-binding nuclear protein Ran
• Gene Name: Ran
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 216
• Subcellular Localization: Nucleus . Nucleus envelope . Cytoplasm, cytosol . Cytoplasm . Melanosome . Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). Identified by mass spectrometry in melanosome fractions fro
• 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. 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..
• Protein Sequence: MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL

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
2	Acetylation	------MAAQGEPQV ------CCCCCCCEE	14.43	-
23	Acetylation	VGDGGTGKTTFVKRH EECCCCCCEEEEEEC	44.20	22902405
24	Phosphorylation	GDGGTGKTTFVKRHL ECCCCCCEEEEEECC	27.15	-
28	Acetylation	TGKTTFVKRHLTGEF CCCEEEEEECCCCCC	29.88	22902405
37	Acetylation	HLTGEFEKKYVATLG CCCCCCCEEEEEEEE	55.51	22902405
60	Acetylation	HTNRGPIKFNVWDTA ECCCCCEEEEEEECC	33.74	22902405
71	Acetylation	WDTAGQEKFGGLRDG EECCCCCCCCCCCCC	41.23	-
71	Ubiquitination	WDTAGQEKFGGLRDG EECCCCCCCCCCCCC	41.23	-
99	Acetylation	VTSRVTYKNVPNWHR CCCCCEECCCCCHHH	41.94	22902405
134	Acetylation	KDRKVKAKSIVFHRK CCCEEECEEEEEEEC	34.69	22902405
135	Phosphorylation	DRKVKAKSIVFHRKK CCEEECEEEEEEECC	28.92	25403869
142	Ubiquitination	SIVFHRKKNLQYYDI EEEEEECCCCEEEEC	63.95	-
152	Acetylation	QYYDISAKSNYNFEK EEEECCCCCCCCCCC	32.23	22902405
159	Acetylation	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	22902405
159	Succinylation	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	-
159	Succinylation	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	-

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

Oops, there are no upstream regulatory protein records of RAN_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
37	K	Acetylation	Acetylation at Lys-37 enhances the association with nuclear export components.	-
37	K	Acetylation	Deacetylation of Lys-37 by SIRT7 regulates the nuclear export of NF-kappa-B subunit RELA/p65.	-
134	K	Acetylation	Acetylation by KAT5 at Lys-134 is increased during mitosis, impairs RANGRF binding and enhances RCC1 binding.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RAN_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of RAN_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.