Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ran-binding protein 3  

UniProtKB / Swiss-Prot ID :  RANB3_HUMAN

Gene Name (Synonyms) : 
RANBP3  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein Function :  Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF- beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export. 

Protein Sequence MADLANEEKPAIAPPVFVFQKDKGQKSPAEQKNLSDSGEEPRGEAEAPHHGTGHPESAGEHALEPPAPAG...
Predicted Secondary Structure CCCCCCCCCCCCCCEEEEECCCCCCCCCCHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
314A -> V (in dbSNP:rs10417885). VAR_051303
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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
Predicted 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.---MADLAN
---CCCCCC
22.11UniProtKB
Link-
21N6-acetyllysineFVFQKDKGQ
EEECCCCCC
50.36HPRD
Link-
21N6-acetyllysineFVFQKDKGQ
EEECCCCCC
50.36Phosphositeplus
Link-
21N6-acetyllysine.FVFQKDKGQ
EEECCCCCC
50.36UniProtKB
Link-
27PhosphoserineKGQKSPAEQ
CCCCCCCHH
22.81HPRD
Link-
27PhosphoserineKGQKSPAEQ
CCCCCCCHH
22.81Phosphositeplus
Link-
57PhosphoserineGHPESAGEH
CCCCCCCCC
46.13HPRD
Link-
96PhosphoserineLAGRSAGGS
HHHHHCCCC
30.28HPRD
Link-
96PhosphoserineLAGRSAGGS
HHHHHCCCC
30.28PhosphoELM
Link-
96PhosphoserineLAGRSAGGS
HHHHHCCCC
30.28Phosphositeplus
Link-
96PhosphoserineLAGRSAGGS
HHHHHCCCC
30.28SysPTM
Link-
96Phosphoserine.LAGRSAGGS
HHHHHCCCC
30.28UniProtKB
Link-
100PhosphoserineSAGGSSPEG
HCCCCCCCC
41.63HPRD
Link-
100PhosphoserineSAGGSSPEG
HCCCCCCCC
41.63PhosphoELM
Link-
100PhosphoserineSAGGSSPEG
HCCCCCCCC
41.63Phosphositeplus
Link-
100PhosphoserineSAGGSSPEG
HCCCCCCCC
41.63SysPTM
Link-
100Phosphoserine.SAGGSSPEG
HCCCCCCCC
41.63UniProtKB
Link-
101PhosphoserineAGGSSPEGG
CCCCCCCCC
30.19HPRD
Link-
101PhosphoserineAGGSSPEGG
CCCCCCCCC
30.19PhosphoELM
Link-
101PhosphoserineAGGSSPEGG
CCCCCCCCC
30.19Phosphositeplus
Link-
101PhosphoserineAGGSSPEGG
CCCCCCCCC
30.19SysPTM
Link-
101Phosphoserine.AGGSSPEGG
CCCCCCCCC
30.19UniProtKB
Link-
108PhosphoserineGGEDSDRED
CCCCCCCCC
33.98HPRD
Link-
108PhosphoserineGGEDSDRED
CCCCCCCCC
33.98PhosphoELM
Link-
108PhosphoserineGGEDSDRED
CCCCCCCCC
33.98Phosphositeplus
Link-
108PhosphoserineGGEDSDRED
CCCCCCCCC
33.98SysPTM
Link-
108Phosphoserine.GGEDSDRED
CCCCCCCCC
33.98UniProtKB
Link-
115PhosphotyrosineEDGNYCPPV
CCCCCCCCC
16.32HPRD
Link-
115PhosphotyrosineEDGNYCPPV
CCCCCCCCC
16.32Phosphositeplus
Link-
115PhosphotyrosineEDGNYCPPV
CCCCCCCCC
16.32SysPTM
Link-
124PhosphothreonineKRERTSSLT
CCCCCCCCC
20.22HPRD
Link-
124PhosphothreonineKRERTSSLT
CCCCCCCCC
20.22PhosphoELM
Link-
124PhosphothreonineKRERTSSLT
CCCCCCCCC
20.22Phosphositeplus
Link-
124PhosphothreonineKRERTSSLT
CCCCCCCCC
20.22SysPTM
Link-
124Phosphothreonine.KRERTSSLT
CCCCCCCCC
20.22UniProtKB
Link-
125PhosphoserineRERTSSLTQ
CCCCCCCCC
29.57HPRD
Link-
125PhosphoserineRERTSSLTQ
CCCCCCCCC
29.57PhosphoELM
Link-
125PhosphoserineRERTSSLTQ
CCCCCCCCC
29.57Phosphositeplus
Link-
125Phosphoserine.RERTSSLTQ
CCCCCCCCC
29.57UniProtKB
Link-
126PhosphoserineERTSSLTQF
CCCCCCCCC
34.52HPRD
Link-
126PhosphoserineERTSSLTQF
CCCCCCCCC
34.52PhosphoELM
Link-
126PhosphoserineERTSSLTQF
CCCCCCCCC
34.52Phosphositeplus
Link-
126PhosphoserineERTSSLTQF
CCCCCCCCC
34.52SysPTM
Link-
126Phosphoserine.ERTSSLTQF
CCCCCCCCC
34.52UniProtKB
Link-
128PhosphothreonineTSSLTQFPP
CCCCCCCCC
30.06HPRD
Link-
128PhosphothreonineTSSLTQFPP
CCCCCCCCC
30.06PhosphoELM
Link-
128PhosphothreonineTSSLTQFPP
CCCCCCCCC
30.06Phosphositeplus
Link-
128PhosphothreonineTSSLTQFPP
CCCCCCCCC
30.06SysPTM
Link-
133PhosphoserineQFPPSQSEE
CCCCCCCCC
46.72HPRD
Link-
133PhosphoserineQFPPSQSEE
CCCCCCCCC
46.72PhosphoELM
Link-
133PhosphoserineQFPPSQSEE
CCCCCCCCC
46.72Phosphositeplus
Link-
133Phosphoserine.QFPPSQSEE
CCCCCCCCC
46.72UniProtKB
Link-
186PhosphoserinePKALSQTVP
CCCCCCCCC
28.76HPRD
Link-
211PhosphoserineVPAASPDTA
CCCCCCHHC
25.97HPRD
Link-
211PhosphoserineVPAASPDTA
CCCCCCHHC
25.97PhosphoELM
Link-
211PhosphoserineVPAASPDTA
CCCCCCHHC
25.97Phosphositeplus
Link-
211Phosphoserine.VPAASPDTA
CCCCCCHHC
25.97UniProtKB
Link-
214PhosphothreonineASPDTAAWR
CCCHHCCCC
22.97HPRD
Link-
214Phosphothreonine.ASPDTAAWR
CCCHHCCCC
22.97UniProtKB
Link-
219PhosphoserineAAWRSPSEA
CCCCCCCHH
23.29HPRD
Link-
219PhosphoserineAAWRSPSEA
CCCCCCCHH
23.29Phosphositeplus
Link-
289PhosphoserineAGHPSADTP
CCCCCCCCC
32.85HPRD
Link-
328PhosphoserineGQNMSERVL
CCCCCCCCC
29.78HPRD
Link-
333PhosphoserineERVLSPPKL
CCCCCCCCC
35.98HPRD
Link-
333PhosphoserineERVLSPPKL
CCCCCCCCC
35.98PhosphoELM
Link-
333PhosphoserineERVLSPPKL
CCCCCCCCC
35.98Phosphositeplus
Link-
333PhosphoserineERVLSPPKL
CCCCCCCCC
35.98SysPTM
Link-
333Phosphoserine.ERVLSPPKL
CCCCCCCCC
35.98UniProtKB
Link-
353PhosphoserineAAAESGSES
CCCCCCCCC
42.78HPRD
Link-
353PhosphoserineAAAESGSES
CCCCCCCCC
42.78PhosphoELM
Link-
353PhosphoserineAAAESGSES
CCCCCCCCC
42.78Phosphositeplus
Link-
353PhosphoserineAAAESGSES
CCCCCCCCC
42.78SysPTM
Link-
353Phosphoserine.AAAESGSES
CCCCCCCCC
42.78UniProtKB
Link-
355PhosphoserineAESGSESSS
CCCCCCCCC
43.51HPRD
Link-
355PhosphoserineAESGSESSS
CCCCCCCCC
43.51PhosphoELM
Link-
355PhosphoserineAESGSESSS
CCCCCCCCC
43.51Phosphositeplus
Link-
355PhosphoserineAESGSESSS
CCCCCCCCC
43.51SysPTM
Link-
355Phosphoserine.AESGSESSS
CCCCCCCCC
43.51UniProtKB
Link-
357PhosphoserineSGSESSSQE
CCCCCCCCC
36.67HPRD
Link-
357PhosphoserineSGSESSSQE
CCCCCCCCC
36.67PhosphoELM
Link-
357PhosphoserineSGSESSSQE
CCCCCCCCC
36.67Phosphositeplus
Link-
357PhosphoserineSGSESSSQE
CCCCCCCCC
36.67SysPTM
Link-
357Phosphoserine.SGSESSSQE
CCCCCCCCC
36.67UniProtKB
Link-
358PhosphoserineGSESSSQEA
CCCCCCCCC
31.80Phosphositeplus
Link-
359PhosphoserineSESSSQEAT
CCCCCCCCC
41.12HPRD
Link-
359PhosphoserineSESSSQEAT
CCCCCCCCC
41.12PhosphoELM
Link-
359PhosphoserineSESSSQEAT
CCCCCCCCC
41.12Phosphositeplus
Link-
359PhosphoserineSESSSQEAT
CCCCCCCCC
41.12SysPTM
Link-
359Phosphoserine.SESSSQEAT
CCCCCCCCC
41.12UniProtKB
Link-
363PhosphothreonineSQEATPEKE
CCCCCCCCC
31.09Phosphositeplus
Link-
413Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FVFDKTSQS
EEEECCCCC
38.31Phosphositeplus
Link
533PhosphoserineGAAPSNEED
CCCCCCCCC
52.74HPRD
Link-
533PhosphoserineGAAPSNEED
CCCCCCCCC
52.74Phosphositeplus
Link-
533Phosphoserine.GAAPSNEED
CCCCCCCCC
52.74UniProtKB
Link-
539PhosphoserineEEDDSDDDD
CCCCCCCCC
56.09HPRD
Link-
539PhosphoserineEEDDSDDDD
CCCCCCCCC
56.09PhosphoELM
Link-
539PhosphoserineEEDDSDDDD
CCCCCCCCC
56.09Phosphositeplus
Link-
539PhosphoserineEEDDSDDDD
CCCCCCCCC
56.09SysPTM
Link-
539Phosphoserine.EEDDSDDDD
CCCCCCCCC
56.09UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RAN_HUMANphysical interactionEBI-992712
intact11932251
RCC1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04508HPRD11932251
RAN_HUMANin vitro
in vivo
HPRD:04508HPRD9637251
XPO1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04508HPRD11425870
XPO1_HUMANENSP00000341483STRING
RAN_HUMANENSP00000341483STRING
RAN_HUMANENSP00000341483STRING
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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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-100; SER-101; SER-108; SER-125; SER-126;SER-211; THR-214; SER-533 AND SER-539, 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-21, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-133 ANDSER-359, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-101; SER-108;THR-124; SER-126; SER-333; SER-353; SER-355; SER-357; SER-359 ANDSER-539, AND MASS SPECTROMETRY.
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-100; SER-101; SER-108; SER-125; SER-126;SER-211; THR-214; SER-533 AND SER-539, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-100; SER-101 ANDSER-108, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures