Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  GTP-binding nuclear protein Ran  

UniProtKB / Swiss-Prot ID :  RAN_HUMAN

Gene Name (Synonyms) : 
RAN, ARA24 OK/SW-cl.81  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Cytoplasm. Melanosome. Note=Predominantly nuclear during interphase (By similarity). Becomes dispersed throughout the cytoplasm during mitosis. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. 

Protein Function :  GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). 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. Transactivation decreases as the poly-Gln length within AR increases. 

Protein Sequence MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQE...
Predicted Secondary Structure CCCCCCCCCEEEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCEEEEEEEEEECCEEEEEEEEECCCCH...
Protein Variant
LocationDescription
95R -> I (in dbSNP:rs11546488). VAR_051900
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAQGE
---CCCCCC
14.43UniProtKB
Link-
23Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GGTGKTTFV
CCCCHHHHH
44.20Phosphositeplus
Link
37N6-acetyllysineGEFEKKYVA
CCCCCCCCC
55.51HPRD
Link
37N6-acetyllysineGEFEKKYVA
CCCCCCCCC
55.51Phosphositeplus
Link
38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EFEKKYVAT
CCCCCCCCC
37.45Phosphositeplus
Link
60Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RGPIKFNVW
CEEEEEEEE
33.74Phosphositeplus
Link
60N6-acetyllysineRGPIKFNVW
CEEEEEEEE
33.74HPRD
Link
60N6-acetyllysineRGPIKFNVW
CEEEEEEEE
33.74Phosphositeplus
Link
60N6-acetyllysine.RGPIKFNVW
CEEEEEEEE
33.74UniProtKB
Link
71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AGQEKFGGL
CCCHHHHHH
41.23Phosphositeplus
Link
71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AGQEKFGGL
CCCHHHHHH
41.23SysPTM
Link
71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).AGQEKFGGL
CCCHHHHHH
41.23UniProtKB
Link
71N6-acetyllysineAGQEKFGGL
CCCHHHHHH
41.23HPRD
Link
71N6-acetyllysineAGQEKFGGL
CCCHHHHHH
41.23Phosphositeplus
Link
71N6-acetyllysine.AGQEKFGGL
CCCHHHHHH
41.23UniProtKB
Link
99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RVTYKNVPN
HHHHHHHHH
41.94Phosphositeplus
Link
99N6-acetyllysineRVTYKNVPN
HHHHHHHHH
41.94HPRD
Link
99N6-acetyllysineRVTYKNVPN
HHHHHHHHH
41.94Phosphositeplus
Link
99N6-acetyllysine.RVTYKNVPN
HHHHHHHHH
41.94UniProtKB
Link
112S-nitrosocysteineLVRVCENIP
HHHHCCCCE
2.02dbSNO
Link
112S-nitrosocysteineLVRVCENIP
HHHHCCCCE
2.02HPRD
Link
112S-nitrosocysteineLVRVCENIP
HHHHCCCCE
2.02SysPTM
Link
120S-nitrosocysteinePIVLCGNKV
EEEEEECCC
3.80dbSNO
Link
120S-nitrosocysteinePIVLCGNKV
EEEEEECCC
3.80HPRD
Link
120S-nitrosocysteinePIVLCGNKV
EEEEEECCC
3.80SysPTM
Link
134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KVKAKSIVF
CHHHHHHHH
34.69Phosphositeplus
Link
135PhosphoserineVKAKSIVFH
HHHHHHHHH
28.92HPRD
Link
135PhosphoserineVKAKSIVFH
HHHHHHHHH
28.92Phosphositeplus
Link
142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FHRKKNLQY
HHHHCCCCE
63.95Phosphositeplus
Link
146PhosphotyrosineKNLQYYDIS
CCCCEEEEE
13.28HPRD
Link
146PhosphotyrosineKNLQYYDIS
CCCCEEEEE
13.28Phosphositeplus
Link
147PhosphotyrosineNLQYYDISA
CCCEEEEEE
8.21HPRD
Link
147PhosphotyrosineNLQYYDISA
CCCEEEEEE
8.21PhosphoELM
Link
147PhosphotyrosineNLQYYDISA
CCCEEEEEE
8.21Phosphositeplus
Link
147Phosphotyrosine.NLQYYDISA
CCCEEEEEE
8.21UniProtKB
Link
152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DISAKSNYN
EEEECCCCC
32.23Phosphositeplus
Link
155PhosphotyrosineAKSNYNFEK
ECCCCCHHH
28.46HPRD
Link
155PhosphotyrosineAKSNYNFEK
ECCCCCHHH
28.46PhosphoELM
Link
155PhosphotyrosineAKSNYNFEK
ECCCCCHHH
28.46Phosphositeplus
Link
155Phosphotyrosine.AKSNYNFEK
ECCCCCHHH
28.46UniProtKB
Link
159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YNFEKPFLW
CCHHHHHHH
36.61Phosphositeplus
Link
159N6-acetyllysineYNFEKPFLW
CCHHHHHHH
36.61HPRD
Link
159N6-acetyllysineYNFEKPFLW
CCHHHHHHH
36.61Phosphositeplus
Link
159N6-acetyllysine.YNFEKPFLW
CCHHHHHHH
36.61UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RANG_HUMANphysical interactionMINT-73242MINT12649209
NELF_HUMANphysical interactionMINT-63976MINT16169070
TNPO1_HUMANphysical interactionMINT-24902MINT10353245
K1377_HUMANphysical interactionMINT-63977MINT16169070
NTF2_HUMANphysical interactionDIP:10951EDIP9533885
ANDR_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
DIP:10649EDIP10400640
10400640
10400640
10400640
10400640
NTF2_HUMANphysical interactionDIP:44981EDIP9533885
NFL_HUMANphysical interactionEBI-737516
intact16169070
K1377_HUMANphysical interactionEBI-733094
intact16169070
TNPO1_HUMANdirect interaction
physical interaction
EBI-1027757
EBI-286729
intact10353245
11024021
RANG_HUMANphysical interaction
physical interaction
EBI-1032926
EBI-1032940
intact11832950
11832950
XPO7_HUMANphysical interactionEBI-286729
intact11024021
XPOT_HUMANphysical interactionEBI-286729
intact11024021
XPO2_HUMANphysical interactionEBI-286729
intact11024021
IPO7_HUMANphysical interactionEBI-286729
intact11024021
IMB1_HUMANphysical interactionEBI-286729
intact11024021
MBP_HUMANin vitro
in vivo
HPRD:03109HPRD12101123
PTMA_HUMANin vitroHPRD:03109HPRD11310559
RCC1_HUMANin vivoHPRD:03109HPRD10369786
12194828
ABL1_HUMANin vivoHPRD:03109HPRD11420673
ANDR_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03109HPRD10400640
RAN_HUMANin vitro
in vivo
HPRD:03109HPRD14684163
9637251
SMAD1_HUMANin vivoHPRD:03109HPRD15761153
SMAD2_HUMANin vivoHPRD:03109HPRD15761153
SMUF2_HUMANin vivoHPRD:03109HPRD15761153
TGFR1_HUMANin vivoHPRD:03109HPRD15761153
NELF_HUMANyeast 2-hybridHPRD:03109HPRD16169070
K1377_HUMANyeast 2-hybridHPRD:03109HPRD16169070
RANB9_HUMANENSP00000254675STRING
RANB9_HUMANENSP00000254675STRING
RANB9_HUMANENSP00000254675STRING
RANB9_HUMANENSP00000254675STRING
XPO1_HUMANENSP00000254675STRING
XPO1_HUMANENSP00000254675STRING
AAAS_HUMANENSP00000254675STRING
AAAS_HUMANENSP00000254675STRING
NTF2_HUMANENSP00000254675STRING
NTF2_HUMANENSP00000254675STRING
NUP88_HUMANENSP00000254675STRING
NUP88_HUMANENSP00000254675STRING
NU107_HUMANENSP00000254675STRING
NU107_HUMANENSP00000254675STRING
NU155_HUMANENSP00000254675STRING
NU155_HUMANENSP00000254675STRING
SH23A_HUMANENSP00000254675STRING
SH23A_HUMANENSP00000254675STRING
NUP37_HUMANENSP00000254675STRING
NUP37_HUMANENSP00000254675STRING
PO121_HUMANENSP00000254675STRING
PO121_HUMANENSP00000254675STRING
NUPL2_HUMANENSP00000254675STRING
NUPL2_HUMANENSP00000254675STRING
NU133_HUMANENSP00000254675STRING
NU133_HUMANENSP00000254675STRING
IMB3_HUMANENSP00000254675STRING
IMB3_HUMANENSP00000254675STRING
XPO2_HUMANENSP00000254675STRING
XPO2_HUMANENSP00000254675STRING
NU160_HUMANENSP00000254675STRING
NU160_HUMANENSP00000254675STRING
NUP54_HUMANENSP00000254675STRING
NUP54_HUMANENSP00000254675STRING
RBP2_HUMANENSP00000254675STRING
RBP2_HUMANENSP00000254675STRING
NU205_HUMANENSP00000254675STRING
NU205_HUMANENSP00000254675STRING
IMB1_HUMANENSP00000254675STRING
IMB1_HUMANENSP00000254675STRING
NUP53_HUMANENSP00000254675STRING
NUP53_HUMANENSP00000254675STRING
NUP93_HUMANENSP00000254675STRING
NUP93_HUMANENSP00000254675STRING
IPO11_HUMANENSP00000254675STRING
IPO11_HUMANENSP00000254675STRING
RANG_HUMANENSP00000254675STRING
RANG_HUMANENSP00000254675STRING
XPOT_HUMANENSP00000254675STRING
XPOT_HUMANENSP00000254675STRING
RANB3_HUMANENSP00000254675STRING
RANB3_HUMANENSP00000254675STRING
NUP43_HUMANENSP00000254675STRING
NUP43_HUMANENSP00000254675STRING
NUP50_HUMANENSP00000254675STRING
NUP50_HUMANENSP00000254675STRING
RAGP1_HUMANENSP00000254675STRING
RAGP1_HUMANENSP00000254675STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-71; LYS-99 ANDLYS-159, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147 AND TYR-155, ANDMASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-71, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures