Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
RAN (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
RAN a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The RAN protein is also involved in control of DNA synthesis and cell cycle progression. Nuclear localization of RAN requires the presence of regulator of chromosome condensation 1 (RCC1). Mutations in RAN disrupt DNA synthesis. It is likely that RAN interacts with several other proteins. RAN regulates formation and organization of the microtubule network independently of its role in the nucleus-cytosol exchange of macromolecules. RAN could be a key signaling molecule regulating microtubule polymerization during mitosis. RCC1 generates a high local concentration of RAN-GTP around chromatin which, in turn, induces the local nucleation of microtubules. Involved in chromatin condensation and control of cell cycle Note: This description may include information from UniProtKB.
Protein type: Nuclear export; G protein, monomeric; Motility/polarity/chemotaxis; G protein, monomeric, Ran; Nuclear receptor co-regulator; G protein
Cellular Component: nucleoplasm; cytoplasm; melanosome; nuclear pore; cytosol; chromatin
Molecular Function: GTPase activity; protein binding; GTP binding; androgen receptor binding; transcription coactivator activity; chromatin binding
Biological Process: mitosis; mitotic spindle organization and biogenesis; viral reproduction; positive regulation of protein binding; small GTPase mediated signal transduction; positive regulation of transcription, DNA-dependent; androgen receptor signaling pathway; gene expression; viral infectious cycle; protein export from nucleus; signal transduction; 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
Select Structure to View Below

RAN

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Source  |  NURSA  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


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

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

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 2 K23-u VGDGGTGktTFVKRH
0 1 T24-p GDGGTGktTFVKRHL
0 1 T32-p TFVKRHLtGEFEkky
0 2 K37-a HLtGEFEkkyVATLG
0 12 K37-u HLtGEFEkkyVATLG
0 32 K38-u LtGEFEkkyVATLGV
0 8 Y39-p tGEFEkkyVATLGVE
0 12 K60-a HTNRGPIkFNVWDTA
0 6 K60-u HTNRGPIkFNVWDTA
0 8 K71-a WDTAGQEkFGGLRDG
0 68 K71-u WDTAGQEkFGGLRDG
0 2 K99-a VTSRVTYkNVPNWHR
0 12 K99-u VTSRVTYkNVPNWHR
0 10 K123-u PIVLCGNkVDIkDRK
0 12 K127-u CGNkVDIkDRKVKAk
0 18 K134-u kDRKVKAksIVFHRk
2 8 S135-p DRKVKAksIVFHRkk
0 9 K141-u ksIVFHRkkNLQyyD
0 36 K142-u sIVFHRkkNLQyyDI
0 62 Y146-p HRkkNLQyyDISAkS
0 480 Y147-p RkkNLQyyDISAkSN
0 2 K152-u QyyDISAkSNyNFEk
0 156 Y155-p DISAkSNyNFEkPFL
1 7 K159-a kSNyNFEkPFLWLAR
0 48 K159-u kSNyNFEkPFLWLAR
0 4 K167-u PFLWLARkLIGDPNL
  mouse

 
K23-u VGDGGTGkTTFVKRH
T24 GDGGTGkTTFVKRHL
T32 TFVKRHLTGEFEKKY
K37 HLTGEFEKKYVATLG
K37 HLTGEFEKKYVATLG
K38 LTGEFEKKYVATLGV
Y39 TGEFEKKYVATLGVE
K60 HTNRGPIKFNVWDTA
K60-u HTNRGPIkFNVWDTA
K71 WDTAGQEKFGGLRDG
K71-u WDTAGQEkFGGLRDG
K99 VTSRVTYKNVPNWHR
K99-u VTSRVTYkNVPNWHR
K123-u PIVLCGNkVDIkDRK
K127-u CGNkVDIkDRKVKAk
K134-u kDRKVKAksIVFHRK
S135-p DRKVKAksIVFHRKk
K141 ksIVFHRKkNLQyyD
K142-u sIVFHRKkNLQyyDI
Y146-p HRKkNLQyyDISAkS
Y147-p RKkNLQyyDISAkSN
K152-u QyyDISAkSNyNFEk
Y155-p DISAkSNyNFEkPFL
K159 kSNyNFEKPFLWLAR
K159-u kSNyNFEkPFLWLAR
K167 PFLWLARKLIGDPNL
  rat

 
K23 VGDGGTGKTTFVKRH
T24 GDGGTGKTTFVKRHL
T32 TFVKRHLTGEFEKKY
K37 HLTGEFEKKYVATLG
K37 HLTGEFEKKYVATLG
K38 LTGEFEKKYVATLGV
Y39 TGEFEKKYVATLGVE
K60 HTNRGPIKFNVWDTA
K60 HTNRGPIKFNVWDTA
K71 WDTAGQEKFGGLRDG
K71 WDTAGQEKFGGLRDG
K99 VTSRVTYKNVPNWHR
K99 VTSRVTYKNVPNWHR
K123 PIVLCGNKVDIKDRK
K127 CGNKVDIKDRKVKAK
K134 KDRKVKAKSIVFHRK
S135 DRKVKAKSIVFHRKK
K141 KSIVFHRKKNLQYYD
K142 SIVFHRKKNLQYYDI
Y146 HRKKNLQYYDISAKS
Y147 RKKNLQYYDISAKSN
K152 QYYDISAKSNYNFEK
Y155 DISAKSNYNFEKPFL
K159 KSNYNFEKPFLWLAR
K159 KSNYNFEKPFLWLAR
K167 PFLWLARKLIGDPNL
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.