RAN
entrez
5901
canonical
uniprot
P62826
canonical
ensembl
ENSG00000132341
resolver
ensp
ENSP00000376176
resolver
ensp
ENSP00000441210
resolver
ensp
ENSP00000446215
resolver
ensp
ENSP00000527585
resolver
ensp
ENSP00000527587
resolver
enst
ENST00000392369
resolver
enst
ENST00000541630
resolver
enst
ENST00000543796
resolver
enst
ENST00000857526
resolver
enst
ENST00000857528
resolver
genesymbol
RAN
resolver
genesymbol_syn
ARA24
resolver
hgnc
HGNC:9846
resolver
uniprot
A8K3Z8
resolver
uniprot
B4DV51
resolver
uniprot
F6VP10
resolver
uniprot
P17080
resolver
uniprot
P28746
resolver
uniprot
P28747
resolver
uniprot
Q6IPB2
resolver
uniprot
Q86V08
resolver
uniprot
Q8NI90
resolver
uniprot
Q9CSP3
resolver
uniprot
Q9CWI7
resolver
uniprot
Q9CZA2
resolver
uniprot
Q9UDJ5
resolver
uniprot
Q9UEU9
resolver
uniprot_entry
B4DV51_HUMAN
resolver
uniprot_entry
F6VP10_HUMAN
resolver
uniprot_entry
RAN_HUMAN
resolver
uniprot_sec
A8K3Z8
resolver
uniprot_sec
P17080
resolver
uniprot_sec
P28746
resolver
uniprot_sec
P28747
resolver
uniprot_sec
Q6IPB2
resolver
uniprot_sec
Q86V08
resolver
uniprot_sec
Q8NI90
resolver
uniprot_sec
Q9CSP3
resolver
uniprot_sec
Q9CWI7
resolver
uniprot_sec
Q9CZA2
resolver
uniprot_sec
Q9UDJ5
resolver
uniprot_sec
Q9UEU9
resolver
amino_acid_sequence
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs (PubMed:10400640, PubMed:17209048, PubMed:26272610, PubMed:27306458, PubMed:8276887, PubMed:8636225, PubMed:8692944, PubMed:8896452, PubMed:9351834, PubMed:9428644, PubMed:9822603). Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis (PubMed:11336674, PubMed:26272610, PubMed:29040603, PubMed:7819259, PubMed:8636225, PubMed:8692944, PubMed:8896452, PubMed:9351834, PubMed:9428644, PubMed:9822603). 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 (PubMed:8896452, PubMed:9351834, PubMed:9428644). 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 (PubMed:20485264). RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation (PubMed:10408446, PubMed:29040603). Required for normal progress through mitosis (PubMed:12194828, PubMed:29040603, PubMed:8421051). 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 (PubMed:18591255). Acts as a negative regulator of the kinase activity of VRK1 and VRK2 (PubMed:18617507). Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases (PubMed:10400640). {ECO:0000269|PubMed:10400640, ECO:0000269|PubMed:10408446, ECO:0000269|PubMed:11336674, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:20485264, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:27306458, ECO:0000269|PubMed:29040603, ECO:0000269|PubMed:7819259, ECO:0000269|PubMed:8276887, ECO:0000269|PubMed:8421051, ECO:0000269|PubMed:8636225, ECO:0000269|PubMed:8692944, ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9351834, ECO:0000269|PubMed:9428644, ECO:0000269|PubMed:9822603, ECO:0000305|PubMed:26272610}.
uniprot
proteins
mass_dalton
24423
uniprot
proteins
mutagenesis
MUTAGEN 19; /note="G->V: Blocks DNA replication; when associated with L-69."; /evidence="ECO:0000269|PubMed:8421051"; MUTAGEN 24; /note="T->L: Has low binding affinity for GTP and GDP. Almost completely abolishes interaction with BIRC5."; /evidence="ECO:0000269|PubMed:18591255"; MUTAGEN 24; /note="T->N: Has low binding affinity for GTP and GDP. Decreases nuclear import of proteins and RNA. Stabilizes the interaction with RCC1. No effect on nuclear location during interphase. Loss of activity in triggering microtubule assembly at mitotic chromosomes."; /evidence="ECO:0000269|PubMed:10408446, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:7819259, ECO:0000269|PubMed:8636225, ECO:0000269|PubMed:9351834"; MUTAGEN 25; /note="T->A: Minor effect on the interaction with the alpha phosphate group of bound GTP."; /evidence="ECO:0000269|PubMed:26272610"; MUTAGEN 37; /note="K->Q: Mimics acetylation; enhances the nuclear export of RELA/p65."; /evidence="ECO:0000269|PubMed:31075303"; MUTAGEN 37; /note="K->R: Decreased acetylation."; /evidence="ECO:0000269|PubMed:31075303"; MUTAGEN 39; /note="Y->A: Abolishes steric hindrance that traps the essential Q-69 in an unreactive position, and causes slow GTP hydrolysis in wild-type. Loss of one hydrogen bond with the gamma phosphate group of bound GTP."; /evidence="ECO:0000269|PubMed:26272610"; MUTAGEN 69; /note="Q->L: Strongly decreased GTPase activity. Probably locked in the GTP-bound form. Loss of interaction with NUTF2. Decreases nuclear location and leads to cytoplasmic location during interphase. Loss of function in importin-mediated protein nuclear import. High activity in triggering microtubule assembly at mitotic chromosomes. Blocks DNA replication; when associated with V-19."; /evidence="ECO:0000269|PubMed:10408446, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:7819259, ECO:0000269|PubMed:8421051, ECO:0000269|PubMed:8636225, ECO:0000269|PubMed:9351834, ECO:0000269|PubMed:9822603"; MUTAGEN 69; /note="Q->N: Unable to hydrolyze GTP. Increases binding to BIRC5 and promotes exaggerated spindle formation."; /evidence="ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:23878195, ECO:0000269|PubMed:24915079"; MUTAGEN 70; /note="E->A: Strongly decreases the relase of bound GDP."; /evidence="ECO:0000269|PubMed:11336674"; MUTAGEN 76; /note="R->E: Probable loss of interaction with NUTF2. Loss of transport to the nucleus."; /evidence="ECO:0000269|PubMed:9822603"; MUTAGEN 134; /note="K->Q: Loss of normal mitotic chromosome segregation and defective mitotic spindle orientation."; /evidence="ECO:0000269|PubMed:29040603"; MUTAGEN 134; /note="K->R: Loss of normal mitotic chromosome segregation and formation of sister chromatid bridges."; /evidence="ECO:0000269|PubMed:29040603"; MUTAGEN 211..216; /note="Missing: No effect on GTPase activity. Abolishes interaction with RANBP1."; /evidence="ECO:0000269|PubMed:7891706
uniprot
proteins
post_translational_modification
PTM: Acetylation by KAT5 at Lys-134 is increased during mitosis, impairs RANGRF binding and enhances RCC1 binding (PubMed:29040603). Acetylation at Lys-37 enhances the association with nuclear export components (PubMed:31075303). Deacetylation of Lys-37 by SIRT7 regulates the nuclear export of NF-kappa-B subunit RELA/p65 (PubMed:31075303). {ECO:0000269|PubMed:29040603, ECO:0000269|PubMed:31075303}.
uniprot
proteins
protein_family
Ran family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10078529
uniprot
proteins
pubmed
10209022
uniprot
proteins
pubmed
10353245
uniprot
proteins
pubmed
10367892
uniprot
proteins
pubmed
10400640
uniprot
proteins
pubmed
10408446
uniprot
proteins
pubmed
10679025
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
11336674
uniprot
proteins
pubmed
11425870
uniprot
proteins
pubmed
11571268
uniprot
proteins
pubmed
11832950
uniprot
proteins
pubmed
12194828
uniprot
proteins
pubmed
12808100
uniprot
proteins
pubmed
14500717
uniprot
proteins
pubmed
14612415
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14684163
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15574331
uniprot
proteins
pubmed
16428860
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
17209048
uniprot
proteins
pubmed
18266911
uniprot
proteins
pubmed
1855255
uniprot
proteins
pubmed
18591255
uniprot
proteins
pubmed
18611384
uniprot
proteins
pubmed
18617507
uniprot
proteins
pubmed
19389996
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19505478
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
1961752
uniprot
proteins
pubmed
19753112
uniprot
proteins
pubmed
20485264
uniprot
proteins
pubmed
2108320
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23878195
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24449914
uniprot
proteins
pubmed
24915079
uniprot
proteins
pubmed
25331866
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26272610
uniprot
proteins
pubmed
26304119
uniprot
proteins
pubmed
26349033
uniprot
proteins
pubmed
27306458
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28282025
uniprot
proteins
pubmed
29040603
uniprot
proteins
pubmed
29130391
uniprot
proteins
pubmed
31075303
uniprot
proteins
pubmed
7819259
uniprot
proteins
pubmed
7885480
uniprot
proteins
pubmed
7891706
uniprot
proteins
pubmed
8276887
uniprot
proteins
pubmed
8421051
uniprot
proteins
pubmed
8636225
uniprot
proteins
pubmed
8692944
uniprot
proteins
pubmed
8896452
uniprot
proteins
pubmed
9323133
uniprot
proteins
pubmed
9351834
uniprot
proteins
pubmed
9428644
uniprot
proteins
pubmed
9822603
uniprot
proteins
pubmed
9837918
uniprot
proteins
sequence_length
216
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:1961752, ECO:0000269|PubMed:19753112, ECO:0000269|PubMed:31075303, ECO:0000269|PubMed:8421051, ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9351834, ECO:0000269|PubMed:9822603}. Nucleus envelope {ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9822603}. Cytoplasm, cytosol {ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:8276887}. Cytoplasm {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:9822603}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Predominantly nuclear during interphase (PubMed:10679025, PubMed:12194828, PubMed:8421051). Becomes dispersed throughout the cytoplasm during mitosis (PubMed:12194828, PubMed:8421051). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:8421051}.
uniprot
proteins