Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Exportin-6  

UniProtKB / Swiss-Prot ID :  XPO6_HUMAN

Gene Name (Synonyms) : 
XPO6, KIAA0370, RANBP20  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm. 

Protein Function :  Mediates the nuclear export of actin and profilin-actin complexes in somatic cells. 

Protein Sequence MASEEASLRALESLMTEFFHDCTTNERKREIEELLNNFAQQIGAWRFCLYFLSSTRNDYVMMYSLTVFEN...
Predicted Secondary Structure CCCHHHHHHHHHHHHHHHHCCCCCCHHHHHHHHHHHHHHCCCCHHHHHHHHHHCCCCHHHHHHHHHHHHH...
Protein Variant
LocationDescription
1029V -> L (in dbSNP:rs14672). VAR_048961
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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
199PhosphoserineWDKHSVTAA
HCCCCCEEE
27.23HPRD
Link-
199PhosphoserineWDKHSVTAA
HCCCCCEEE
27.23Phosphositeplus
Link-
199PhosphoserineWDKHSVTAA
HCCCCCEEE
27.23SysPTM
Link-
199Phosphoserine.WDKHSVTAA
HCCCCCEEE
27.23UniProtKB
Link-
201PhosphothreonineKHSVTAATP
CCCCEEECC
17.37HPRD
Link-
201PhosphothreonineKHSVTAATP
CCCCEEECC
17.37Phosphositeplus
Link-
201PhosphothreonineKHSVTAATP
CCCCEEECC
17.37SysPTM
Link-
201Phosphothreonine.KHSVTAATP
CCCCEEECC
17.37UniProtKB
Link-
204PhosphothreonineVTAATPPPS
CEEECCCCC
33.59HPRD
Link-
204PhosphothreonineVTAATPPPS
CEEECCCCC
33.59PhosphoELM
Link-
204PhosphothreonineVTAATPPPS
CEEECCCCC
33.59Phosphositeplus
Link-
204PhosphothreonineVTAATPPPS
CEEECCCCC
33.59SysPTM
Link-
204Phosphothreonine.VTAATPPPS
CEEECCCCC
33.59UniProtKB
Link-
208PhosphoserineTPPPSPTSG
CCCCCCCCC
46.73HPRD
Link-
208PhosphoserineTPPPSPTSG
CCCCCCCCC
46.73PhosphoELM
Link-
208PhosphoserineTPPPSPTSG
CCCCCCCCC
46.73Phosphositeplus
Link-
208Phosphoserine.TPPPSPTSG
CCCCCCCCC
46.73UniProtKB
Link-
210PhosphothreoninePPSPTSGES
CCCCCCCHH
54.42HPRD
Link-
210PhosphothreoninePPSPTSGES
CCCCCCCHH
54.42PhosphoELM
Link-
210PhosphothreoninePPSPTSGES
CCCCCCCHH
54.42Phosphositeplus
Link-
210PhosphothreoninePPSPTSGES
CCCCCCCHH
54.42SysPTM
Link-
210Phosphothreonine.PPSPTSGES
CCCCCCCHH
54.42UniProtKB
Link-
211PhosphoserinePSPTSGESG
CCCCCCHHH
43.90HPRD
Link-
211PhosphoserinePSPTSGESG
CCCCCCHHH
43.90PhosphoELM
Link-
214PhosphoserineTSGESGDLL
CCCHHHHHH
40.92HPRD
Link-
214PhosphoserineTSGESGDLL
CCCHHHHHH
40.92PhosphoELM
Link-
214PhosphoserineTSGESGDLL
CCCHHHHHH
40.92Phosphositeplus
Link-
214Phosphoserine.TSGESGDLL
CCCHHHHHH
40.92UniProtKB
Link-
219PhosphoserineGDLLSNLLQ
HHHHHHHHC
32.50Phosphositeplus
Link-
224PhosphoserineNLLQSPSSA
HHHCCCCHH
27.07HPRD
Link-
224PhosphoserineNLLQSPSSA
HHHCCCCHH
27.07PhosphoELM
Link-
224PhosphoserineNLLQSPSSA
HHHCCCCHH
27.07Phosphositeplus
Link-
224PhosphoserineNLLQSPSSA
HHHCCCCHH
27.07SysPTM
Link-
224Phosphoserine.NLLQSPSSA
HHHCCCCHH
27.07UniProtKB
Link-
357Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AHTVKSRLE
HHHHHHHHH
30.89Phosphositeplus
Link-
766Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YRNLKPSAV
HHHCCCCCC
40.24Phosphositeplus
Link-
961PhosphoserineTVLASVQRG
HHHHHHHHC
18.02HPRD
Link-
961PhosphoserineTVLASVQRG
HHHHHHHHC
18.02Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NUP62_HUMANphysical interactionEBI-754264
intact16189514
ACTB_HUMANin vitroHPRD:10525HPRD14592989
EGFR_HUMANin vitroHPRD:10525HPRD14592989
PROF1_HUMANin vitroHPRD:10525HPRD14592989
VASP_HUMANin vitroHPRD:10525HPRD14592989
DIAP1_HUMANin vitroHPRD:10525HPRD14592989
PROF1_HUMANENSP00000302790STRING
ACTB_HUMANENSP00000302790STRING
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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
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204 AND SER-208, ANDMASS 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-199; THR-201; THR-204AND SER-224, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204; THR-204; SER-208AND SER-214, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204; THR-210 ANDSER-224, AND MASS SPECTROMETRY.
"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 THR-204; THR-210 ANDSER-224, 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