RAN_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAN_MOUSE
• UniProt AC: P62827
• Protein Name: GTP-binding nuclear protein Ran
• Gene Name: Ran
• Organism: Mus musculus (Mouse).
• 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	Ubiquitination	VGDGGTGKTTFVKRH EECCCCCCEEEEEEC	44.20	-
23	Acetylation	VGDGGTGKTTFVKRH EECCCCCCEEEEEEC	44.20	23806337
23	Succinylation	VGDGGTGKTTFVKRH EECCCCCCEEEEEEC	44.20	23806337
24	Phosphorylation	GDGGTGKTTFVKRHL ECCCCCCEEEEEECC	27.15	-
28	Acetylation	TGKTTFVKRHLTGEF CCCEEEEEECCCCCC	29.88	22826441
32	Phosphorylation	TFVKRHLTGEFEKKY EEEEECCCCCCCEEE	28.65	24899341
37	Acetylation	HLTGEFEKKYVATLG CCCCCCCEEEEEEEE	55.51	22826441
60	Ubiquitination	HTNRGPIKFNVWDTA ECCCCCEEEEEEECC	33.74	22790023
60	Acetylation	HTNRGPIKFNVWDTA ECCCCCEEEEEEECC	33.74	23806337
71	Ubiquitination	WDTAGQEKFGGLRDG EECCCCCCCCCCCCC	41.23	22790023
71	Acetylation	WDTAGQEKFGGLRDG EECCCCCCCCCCCCC	41.23	23806337
99	Acetylation	VTSRVTYKNVPNWHR CCCCCEECCCCCHHH	41.94	23806337
99	Ubiquitination	VTSRVTYKNVPNWHR CCCCCEECCCCCHHH	41.94	27667366
99	Malonylation	VTSRVTYKNVPNWHR CCCCCEECCCCCHHH	41.94	26320211
112	S-nitrosocysteine	HRDLVRVCENIPIVL HHHHHHHHCCCCEEE	2.02	-
112	S-nitrosylation	HRDLVRVCENIPIVL HHHHHHHHCCCCEEE	2.02	24926564
120	Glutathionylation	ENIPIVLCGNKVDIK CCCCEEECCCCCCCC	3.80	24333276
120	S-nitrosylation	ENIPIVLCGNKVDIK CCCCEEECCCCCCCC	3.80	22588120
123	Ubiquitination	PIVLCGNKVDIKDRK CEEECCCCCCCCCCE	26.94	-
123	Acetylation	PIVLCGNKVDIKDRK CEEECCCCCCCCCCE	26.94	22826441
127	Ubiquitination	CGNKVDIKDRKVKAK CCCCCCCCCCEEECE	47.20	22790023
134	Acetylation	KDRKVKAKSIVFHRK CCCEEECEEEEEEEC	34.69	23806337
134	Ubiquitination	KDRKVKAKSIVFHRK CCCEEECEEEEEEEC	34.69	-
134	Malonylation	KDRKVKAKSIVFHRK CCCEEECEEEEEEEC	34.69	26320211
134	Succinylation	KDRKVKAKSIVFHRK CCCEEECEEEEEEEC	34.69	-
135	Phosphorylation	DRKVKAKSIVFHRKK CCEEECEEEEEEECC	28.92	26824392
142	Acetylation	SIVFHRKKNLQYYDI EEEEEECCCCEEEEC	63.95	23806337
142	Succinylation	SIVFHRKKNLQYYDI EEEEEECCCCEEEEC	63.95	-
142	Ubiquitination	SIVFHRKKNLQYYDI EEEEEECCCCEEEEC	63.95	-
142	Malonylation	SIVFHRKKNLQYYDI EEEEEECCCCEEEEC	63.95	26320211
146	Phosphorylation	HRKKNLQYYDISAKS EECCCCEEEECCCCC	13.28	22499769
147	Phosphorylation	RKKNLQYYDISAKSN ECCCCEEEECCCCCC	8.21	20116462
150	Phosphorylation	NLQYYDISAKSNYNF CCEEEECCCCCCCCC	27.09	28066266
152	Acetylation	QYYDISAKSNYNFEK EEEECCCCCCCCCCC	32.23	23236377
152	Ubiquitination	QYYDISAKSNYNFEK EEEECCCCCCCCCCC	32.23	22790023
155	Phosphorylation	DISAKSNYNFEKPFL ECCCCCCCCCCCHHH	28.46	18563927
159	Acetylation	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	23806337
159	Succinylation	KSNYNFEKPFLWLAR CCCCCCCCHHHHHHH	36.61	23806337
159	Ubiquitination	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_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RAN_MOUSE !!

Drug and Disease Associations

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