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 10  

UniProtKB / Swiss-Prot ID :  RBP10_HUMAN

Gene Name (Synonyms) : 
RANBP10, KIAA1464  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytosol. Nucleus. Note=Predominantly cytoplasmic. 

Protein Function :  Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase (By similarity). May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen- induced transactivation. In contrast to RANBP9, does not interact with Sos and does not activate the Ras pathway. 

Protein Sequence MAAATADPGAGNPQPGDSSGGGAGGGLPSPGEQELSRRLQRLYPAVNQQETPLPRSWSPKDKYNYIGLSQ...
Predicted Secondary Structure  -
Protein Variant -
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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
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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.---MAAATA
---
13.05UniProtKB
Link-
293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QASIKNRQK
43.51Phosphositeplus
Link-
350PhosphoserineSEVRSLSSR
37.47Phosphositeplus
Link-
352PhosphoserineVRSLSSRSP
25.59Phosphositeplus
Link-
353PhosphoserineRSLSSRSPK
41.91Phosphositeplus
Link-
355PhosphoserineLSSRSPKSQ
38.33Phosphositeplus
Link-
357Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SRSPKSQDS
63.09Phosphositeplus
Link-
358PhosphoserineRSPKSQDSY
42.47Phosphositeplus
Link-
361PhosphoserineKSQDSYPGS
26.11HPRD
Link-
361PhosphoserineKSQDSYPGS
26.11PhosphoELM
Link-
361PhosphoserineKSQDSYPGS
26.11Phosphositeplus
Link-
361Phosphoserine.KSQDSYPGS
26.11UniProtKB
Link-
362PhosphotyrosineSQDSYPGSP
21.65HPRD
Link-
362Phosphotyrosine.SQDSYPGSP
21.65UniProtKB
Link-
365PhosphoserineSYPGSPSLS
13.55HPRD
Link-
365PhosphoserineSYPGSPSLS
13.55PhosphoELM
Link-
365PhosphoserineSYPGSPSLS
13.55Phosphositeplus
Link-
365Phosphoserine.SYPGSPSLS
13.55UniProtKB
Link-
367PhosphoserinePGSPSLSPR
43.08HPRD
Link-
367PhosphoserinePGSPSLSPR
43.08Phosphositeplus
Link-
369PhosphoserineSPSLSPRHG
24.99HPRD
Link-
369PhosphoserineSPSLSPRHG
24.99PhosphoELM
Link-
369PhosphoserineSPSLSPRHG
24.99Phosphositeplus
Link-
369Phosphoserine.SPSLSPRHG
24.99UniProtKB
Link-
486PhosphothreonineEDLQTDESS
49.37Phosphositeplus
Link-
489PhosphoserineQTDESSMDD
33.50HPRD
Link-
489PhosphoserineQTDESSMDD
33.50Phosphositeplus
Link-
490PhosphoserineTDESSMDDR
24.96Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RANB9_HUMANENSP00000316589STRING
RANB9_HUMANENSP00000316589STRING
RANB9_HUMANENSP00000316589STRING
RANB9_HUMANENSP00000316589STRING
RANB9_HUMANENSP00000316589STRING
RANB9_HUMANENSP00000316589STRING
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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 TYR-362; SER-365 AND SER-369, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-361; SER-365 ANDSER-369, 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 TYR-362; SER-365 AND SER-369, AND MASSSPECTROMETRY.
"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-365 AND SER-369, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures