Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Exportin-7  

UniProtKB / Swiss-Prot ID :  XPO7_HUMAN

Gene Name (Synonyms) : 
XPO7, KIAA0745, RANBP16  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus (Probable). Nucleus, nuclear pore complex (Probable). Note=Shuttles between the nucleus and the cytoplasm (Probable). 

Protein Function :  Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO7 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. 

Protein Sequence MADHVQSLAQLENLCKQLYETTDTTTRLQAEKALVEFTNSPDCLSKCQLLLERGSSSYSQLLAATCLTKL...
Predicted Secondary Structure CCCHHHHHHHHHHHHHHHHCCCCHHHHHHHHHHHHHHHHCCCHHHHHHHHHCCCCCHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
398E -> D (in dbSNP:rs17856894). VAR_026526
835C -> Y (in dbSNP:rs17856895). VAR_026527
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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.---MADHVQ
---CCCHHH
27.24UniProtKB
Link-
58PhosphotyrosineGSSSYSQLL
CCCHHHHHH
11.46HPRD
Link-
58PhosphotyrosineGSSSYSQLL
CCCHHHHHH
11.46PhosphoELM
Link-
58PhosphotyrosineGSSSYSQLL
CCCHHHHHH
11.46Phosphositeplus
Link-
58Phosphotyrosine.GSSSYSQLL
CCCHHHHHH
11.46UniProtKB
Link-
348Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)GELVKVENY
HHEHCCCCH
57.36Phosphositeplus
Link-
561PhosphotyrosineFRKIYIGDQ
HHHHHHHHH
11.24Phosphositeplus
Link-
569PhosphoserineQVQKSSKLY
HHHHHHHHH
18.66HPRD
Link-
573PhosphotyrosineSSKLYRRLS
HHHHHHHHH
9.45HPRD
Link-
573PhosphotyrosineSSKLYRRLS
HHHHHHHHH
9.45Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
MK09_HUMANphysical interactionMINT-64910MINT16169070
Q96KE7_HUMANphysical interactionMINT-65233MINT16169070
NEMO_HUMANphysical interactionMINT-48232MINT14743216
NU153_HUMANphysical interactionEBI-286790
intact11024021
NU153_HUMANin vitroHPRD:05846HPRD11024021
XPOT_HUMANin vitroHPRD:05846HPRD11024021
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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.
Phosphorylation
ReferencePubMed
"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-58, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures