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Protein Page:
RAN (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RAN a small GTPase belonging to the RAS superfamily that regulates the nucleo-cytoplasmic traffic through the nuclear pore complex, the condensation of chromatin, spindle assembly and cytokinesis, as well as the organization of non-centrosomal microtubules. A major regulator of mitosis and a potential therapeutic target in cancers expressing higher Ras/MEK/ERK and PI3K/Akt/mTORC1 activities. Required for the import of protein into and RNA export from the nucleus. Cycles between the nucleus and cytoplasm in this process. The Ran guanine nucleotide-exchange factor (RanGEF) is nuclear, promoting the GTP-bound state, while the Ran GTPase activating protein (RanGAP) is cytoplasmic, promoting GDP-bound state. RanGDP is imported into the nucleus by nuclear transport factor-2 (NUTF2), where RanGEF catalyses nucleotide exchange and generates RanGTP. RanGTP then binds to transport factors, such as KPNB1 and CAS, and is exported to the cytoplasm, where RanGAP stimulates GTP hydrolysis. Regulates microtubule polymerization during mitosis; micritubule localization of RAN requires the presence of regulator of chromosome condensation 1 (RCC1), a Ran-GEF. RCC1 generates a high local concentration of RAN-GTP around chromatin which, in turn, induces the local nucleation of microtubules. Regulates the formation and organization of the microtubule network independently of its role in the nucleus-cytosol exchange of macromolecules. GTP-Ran interacts with survivin at S and M phases of the cell cycle. Ran-survivin complexes play 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. Interacts with TERT following the tyrosine phosphorylation of TERT induced by H2O2, inducing nuclear export of TERT. Interacts with MAD2L2. Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis. Note: This description may include information from UniProtKB.
Protein type: G protein; Motility/polarity/chemotaxis; G protein, monomeric; Nuclear export; Nuclear receptor co-regulator; G protein, monomeric, Ran; Cell cycle regulation
Cellular Component: nucleoplasm; membrane; cytoplasm; melanosome; nuclear pore; cytosol; nucleus; chromatin
Molecular Function: GTPase activity; protein domain specific binding; protein binding; androgen receptor binding; GTP binding; transcription coactivator activity; chromatin binding
Biological Process: ribosomal small subunit export from nucleus; mitosis; viral reproduction; positive regulation of protein binding; positive regulation of transcription, DNA-dependent; viral infectious cycle; signal transduction; ribosomal large subunit export from nucleus; mitotic spindle organization and biogenesis; GTP catabolic process; small GTPase mediated signal transduction; androgen receptor signaling pathway; gene expression; protein export from nucleus; DNA metabolic process
Reference #:  P62826 (UniProtKB)
Alt. Names/Synonyms: Androgen receptor-associated protein 24; ARA24; Gsp1; GTP-binding nuclear protein Ran; GTPase Ran; guanosine triphosphatase Ran; member RAS oncogene family; OK/SW-cl.81; RAN; RAN, member RAS oncogene family; RanGTPase; Ras-like protein TC4; Ras-related nuclear protein; TC4
Gene Symbols: RAN
Molecular weight: 24,423 Da
Basal Isoelectric point: 7.01  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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RAN

Protein Structure Not Found.


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Sites Implicated In
cell cycle regulation: S135‑p
intracellular localization: S135‑p
molecular association, regulation: S135‑p

Modification Sites and Domains Show Modification Legend
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Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T21-p VLVGDGGtGkttFVk
0 2 K23-ub VGDGGtGkttFVkRH
0 1 K23-sc VGDGGtGkttFVkRH
0 1 T24-p GDGGtGkttFVkRHL
0 1 T25-p DGGtGkttFVkRHLt
0 1 K28-ub tGkttFVkRHLtGEF
0 2 T32-p tFVkRHLtGEFEkky
0 2 K37-ac HLtGEFEkkyVATLG
0 12 K37-ub HLtGEFEkkyVATLG
0 1 K37-sc HLtGEFEkkyVATLG
0 32 K38-ub LtGEFEkkyVATLGV
0 25 Y39-p tGEFEkkyVATLGVE
0 13 K60-ac HTNRGPIkFNVWDTA
0 6 K60-ub HTNRGPIkFNVWDTA
0 9 K71-ac WDTAGQEkFGGLRDG
0 68 K71-ub WDTAGQEkFGGLRDG
0 3 K99-ac VTSRVTYkNVPNWHR
0 12 K99-ub VTSRVTYkNVPNWHR
0 1 K99-sc VTSRVTYkNVPNWHR
0 10 K123-ub PIVLCGNkVDIkDRk
0 12 K127-ub CGNkVDIkDRkVKAk
0 1 K127-sc CGNkVDIkDRkVKAk
0 1 K130-ub kVDIkDRkVKAksIV
0 18 K134-ub kDRkVKAksIVFHRk
2 13 S135-p DRkVKAksIVFHRkk
0 9 K141-ub ksIVFHRkkNLQyyD
0 36 K142-ub sIVFHRkkNLQyyDI
0 64 Y146-p HRkkNLQyyDIsAkS
0 474 Y147-p RkkNLQyyDIsAkSN
0 1 S150-p NLQyyDIsAkSNyNF
0 1 K152-ac QyyDIsAkSNyNFEk
0 2 K152-ub QyyDIsAkSNyNFEk
0 1 K152-sc QyyDIsAkSNyNFEk
0 168 Y155-p DIsAkSNyNFEkPFL
0 8 K159-ac kSNyNFEkPFLWLAR
0 48 K159-ub kSNyNFEkPFLWLAR
0 4 K167-ub PFLWLARkLIGDPNL
  mouse

 
T21 VLVGDGGTGkTTFVK
K23-ub VGDGGTGkTTFVKRH
K23 VGDGGTGKTTFVKRH
T24 GDGGTGkTTFVKRHL
T25 DGGTGkTTFVKRHLT
K28 TGkTTFVKRHLTGEF
T32 TFVKRHLTGEFEKKY
K37 HLTGEFEKKYVATLG
K37 HLTGEFEKKYVATLG
K37 HLTGEFEKKYVATLG
K38 LTGEFEKKYVATLGV
Y39 TGEFEKKYVATLGVE
K60-ac HTNRGPIkFNVWDTA
K60-ub HTNRGPIkFNVWDTA
K71-ac WDTAGQEkFGGLRDG
K71-ub WDTAGQEkFGGLRDG
K99 VTSRVTYKNVPNWHR
K99-ub VTSRVTYkNVPNWHR
K99 VTSRVTYKNVPNWHR
K123-ub PIVLCGNkVDIkDRK
K127-ub CGNkVDIkDRKVKAk
K127 CGNkVDIKDRKVKAk
K130 kVDIkDRKVKAksIV
K134-ub kDRKVKAksIVFHRK
S135-p DRKVKAksIVFHRKk
K141 ksIVFHRKkNLQyyD
K142-ub sIVFHRKkNLQyyDI
Y146-p HRKkNLQyyDISAkS
Y147-p RKkNLQyyDISAkSN
S150 NLQyyDISAkSNyNF
K152 QyyDISAKSNyNFEk
K152-ub QyyDISAkSNyNFEk
K152 QyyDISAKSNyNFEk
Y155-p DISAkSNyNFEkPFL
K159-ac kSNyNFEkPFLWLAR
K159-ub kSNyNFEkPFLWLAR
K167 PFLWLARKLIGDPNL
  rat

 
T21 VLVGDGGTGKTTFVK
K23 VGDGGTGKTTFVKRH
K23 VGDGGTGKTTFVKRH
T24 GDGGTGKTTFVKRHL
T25 DGGTGKTTFVKRHLT
K28 TGKTTFVKRHLTGEF
T32 TFVKRHLTGEFEkKY
K37-ac HLTGEFEkKYVATLG
K37 HLTGEFEKKYVATLG
K37 HLTGEFEKKYVATLG
K38 LTGEFEkKYVATLGV
Y39 TGEFEkKYVATLGVE
K60-ac HTNRGPIkFNVWDTA
K60 HTNRGPIKFNVWDTA
K71 WDTAGQEKFGGLRDG
K71 WDTAGQEKFGGLRDG
K99-ac VTSRVTYkNVPNWHR
K99 VTSRVTYKNVPNWHR
K99 VTSRVTYKNVPNWHR
K123 PIVLCGNKVDIKDRK
K127 CGNKVDIKDRKVKAK
K127 CGNKVDIKDRKVKAK
K130 KVDIKDRKVKAKsIV
K134 KDRKVKAKsIVFHRK
S135-p DRKVKAKsIVFHRKK
K141 KsIVFHRKKNLQYYD
K142 sIVFHRKKNLQYYDI
Y146 HRKKNLQYYDISAkS
Y147 RKKNLQYYDISAkSN
S150 NLQYYDISAkSNYNF
K152-ac QYYDISAkSNYNFEk
K152 QYYDISAKSNYNFEk
K152 QYYDISAKSNYNFEk
Y155 DISAkSNYNFEkPFL
K159-ac kSNYNFEkPFLWLAR
K159 kSNYNFEKPFLWLAR
K167 PFLWLARKLIGDPNL
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