XPO7_HUMAN - dbPTM
XPO7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XPO7_HUMAN
UniProt AC Q9UIA9
Protein Name Exportin-7
Gene Name XPO7
Organism Homo sapiens (Human).
Sequence Length 1087
Subcellular Localization Cytoplasm. Nucleus . Nucleus, nuclear pore complex . Shuttles between the nucleus and the cytoplasm.
Protein Description 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 MADHVQSLAQLENLCKQLYETTDTTTRLQAEKALVEFTNSPDCLSKCQLLLERGSSSYSQLLAATCLTKLVSRTNNPLPLEQRIDIRNYVLNYLATRPKLATFVTQALIQLYARITKLGWFDCQKDDYVFRNAITDVTRFLQDSVEYCIIGVTILSQLTNEINQADTTHPLTKHRKIASSFRDSSLFDIFTLSCNLLKQASGKNLNLNDESQHGLLMQLLKLTHNCLNFDFIGTSTDESSDDLCTVQIPTSWRSAFLDSSTLQLFFDLYHSIPPSFSPLVLSCLVQIASVRRSLFNNAERAKFLSHLVDGVKRILENPQSLSDPNNYHEFCRLLARLKSNYQLGELVKVENYPEVIRLIANFTVTSLQHWEFAPNSVHYLLSLWQRLAASVPYVKATEPHMLETYTPEVTKAYITSRLESVHIILRDGLEDPLEDTGLVQQQLDQLSTIGRCEYEKTCALLVQLFDQSAQSYQELLQSASASPMDIAVQEGRLTWLVYIIGAVIGGRVSFASTDEQDAMDGELVCRVLQLMNLTDSRLAQAGNEKLELAMLSFFEQFRKIYIGDQVQKSSKLYRRLSEVLGLNDETMVLSVFIGKIITNLKYWGRCEPITSKTLQLLNDLSIGYSSVRKLVKLSAVQFMLNNHTSEHFSFLGINNQSNLTDMRCRTTFYTALGRLLMVDLGEDEDQYEQFMLPLTAAFEAVAQMFSTNSFNEQEAKRTLVGLVRDLRGIAFAFNAKTSFMMLFEWIYPSYMPILQRAIELWYHDPACTTPVLKLMAELVHNRSQRLQFDVSSPNGILLFRETSKMITMYGNRILTLGEVPKDQVYALKLKGISICFSMLKAALSGSYVNFGVFRLYGDDALDNALQTFIKLLLSIPHSDLLDYPKLSQSYYSLLEVLTQDHMNFIASLEPHVIMYILSSISEGLTALDTMVCTGCCSCLDHIVTYLFKQLSRSTKKRTTPLNQESDRFLHIMQQHPEMIQQMLSTVLNIIIFEDCRNQWSMSRPLLGLILLNEKYFSDLRNSIVNSQPPEKQQAMHLCFENLMEGIERNLLTKNRDRFTQNLSAFRREVNDSMKNSTYGVNSNDMMS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MADHVQSLA
------CHHHHHHHH		27.2419413330
7Phosphorylation-MADHVQSLAQLENL
-CHHHHHHHHHHHHH		25.2825693802
19PhosphorylationENLCKQLYETTDTTT
HHHHHHHHHCCCHHH		14.5628152594
21PhosphorylationLCKQLYETTDTTTRL
HHHHHHHCCCHHHHH		19.2025072903
22PhosphorylationCKQLYETTDTTTRLQ
HHHHHHCCCHHHHHH		21.2925072903
24PhosphorylationQLYETTDTTTRLQAE
HHHHCCCHHHHHHHH		28.1625072903
25PhosphorylationLYETTDTTTRLQAEK
HHHCCCHHHHHHHHH		16.8425072903
26PhosphorylationYETTDTTTRLQAEKA
HHCCCHHHHHHHHHH		31.3225072903
32UbiquitinationTTRLQAEKALVEFTN
HHHHHHHHHHHHCCC		50.4629967540
40PhosphorylationALVEFTNSPDCLSKC
HHHHCCCCHHHHHHH		21.0325159151
46UbiquitinationNSPDCLSKCQLLLER
CCHHHHHHHHHHHHC		17.0429967540
58PhosphorylationLERGSSSYSQLLAAT
HHCCCCCHHHHHHHH		11.4622817900
69UbiquitinationLAATCLTKLVSRTNN
HHHHHHHHHHHCCCC		33.6622505724
70UbiquitinationAATCLTKLVSRTNNP
HHHHHHHHHHCCCCC		3.4022505724
144PhosphorylationVTRFLQDSVEYCIIG
HHHHHHHCHHHHHHH		12.14-
147PhosphorylationFLQDSVEYCIIGVTI
HHHHCHHHHHHHHHH		6.18-
167PhosphorylationNEINQADTTHPLTKH
HHHCCCCCCCCCHHH		29.98-
180PhosphorylationKHRKIASSFRDSSLF
HHHHHHHHCCCCCHH		18.45-
191PhosphorylationSSLFDIFTLSCNLLK
CCHHHHHHHHHHHHH		20.35-
203UbiquitinationLLKQASGKNLNLNDE
HHHHHCCCCCCCCCH		56.6229967540
223PhosphorylationLMQLLKLTHNCLNFD
HHHHHHHHHCCCCCC		14.9530576142
240PhosphorylationGTSTDESSDDLCTVQ
CCCCCCCCCCCEEEE		32.8530576142
245PhosphorylationESSDDLCTVQIPTSW
CCCCCCEEEECCCCH		23.8130576142
302AcetylationFNNAERAKFLSHLVD
CCHHHHHHHHHHHHH		53.7325953088
305PhosphorylationAERAKFLSHLVDGVK
HHHHHHHHHHHHHHH		20.2224961811
3122-HydroxyisobutyrylationSHLVDGVKRILENPQ
HHHHHHHHHHHHCCC		38.97-
312UbiquitinationSHLVDGVKRILENPQ
HHHHHHHHHHHHCCC		38.9724816145
313UbiquitinationHLVDGVKRILENPQS
HHHHHHHHHHHCCCC		36.0024816145
320PhosphorylationRILENPQSLSDPNNY
HHHHCCCCCCCCCCH		30.97-
321UbiquitinationILENPQSLSDPNNYH
HHHCCCCCCCCCCHH		5.9224816145
322UbiquitinationLENPQSLSDPNNYHE
HHCCCCCCCCCCHHH		57.1624816145
338UbiquitinationCRLLARLKSNYQLGE
HHHHHHHHHHCCCCC		30.9727667366
338AcetylationCRLLARLKSNYQLGE
HHHHHHHHHHCCCCC		30.9727452117
3382-HydroxyisobutyrylationCRLLARLKSNYQLGE
HHHHHHHHHHCCCCC		30.97-
339UbiquitinationRLLARLKSNYQLGEL
HHHHHHHHHCCCCCE		45.4127667366
339PhosphorylationRLLARLKSNYQLGEL
HHHHHHHHHCCCCCE		45.4120071362
347UbiquitinationNYQLGELVKVENYPE
HCCCCCEEEECCCHH		5.9327667366
348UbiquitinationYQLGELVKVENYPEV
CCCCCEEEECCCHHH		57.3627667366
348SumoylationYQLGELVKVENYPEV
CCCCCEEEECCCHHH		57.36-
348SumoylationYQLGELVKVENYPEV
CCCCCEEEECCCHHH		57.36-
390PhosphorylationLWQRLAASVPYVKAT
HHHHHHHCCCCEECC		20.3022985185
513PhosphorylationGRVSFASTDEQDAMD
CCCCCCCCCHHHCCC		39.8822210691
534PhosphorylationVLQLMNLTDSRLAQA
HHHHHCCCHHHHHHC		27.2422210691
546UbiquitinationAQAGNEKLELAMLSF
HHCCCHHHHHHHHHH		5.4932142685
5592-HydroxyisobutyrylationSFFEQFRKIYIGDQV
HHHHHHHHHHCCHHH		40.94-
561PhosphorylationFEQFRKIYIGDQVQK
HHHHHHHHCCHHHHH		11.2422817900
568AcetylationYIGDQVQKSSKLYRR
HCCHHHHHHHHHHHH		58.8125953088
568UbiquitinationYIGDQVQKSSKLYRR
HCCHHHHHHHHHHHH		58.8132142685
569PhosphorylationIGDQVQKSSKLYRRL
CCHHHHHHHHHHHHH		18.6628450419
570PhosphorylationGDQVQKSSKLYRRLS
CHHHHHHHHHHHHHH		33.4428450419
573PhosphorylationVQKSSKLYRRLSEVL
HHHHHHHHHHHHHHH		9.4520068231
577UbiquitinationSKLYRRLSEVLGLND
HHHHHHHHHHHCCCC		24.6932142685
590PhosphorylationNDETMVLSVFIGKII
CCHHHHHHHHHHHHH		11.99-
601AcetylationGKIITNLKYWGRCEP
HHHHHCCCCCCCCCC		40.8125038526
621PhosphorylationLQLLNDLSIGYSSVR
HHHHHHCCCCHHHHH		19.4820860994
624PhosphorylationLNDLSIGYSSVRKLV
HHHCCCCHHHHHHHH		8.9722817900
806UbiquitinationFRETSKMITMYGNRI
EEECCCEEEEECCEE		2.0033845483
807PhosphorylationRETSKMITMYGNRIL
EECCCEEEEECCEEE		10.8020071362
809PhosphorylationTSKMITMYGNRILTL
CCCEEEEECCEEEEE		11.5520071362
828UbiquitinationKDQVYALKLKGISIC
HHHEEEEECCCHHHH		39.7333845483
837UbiquitinationKGISICFSMLKAALS
CCHHHHHHHHHHHHC		20.8533845483
965PhosphorylationTTPLNQESDRFLHIM
CCCCCHHHHHHHHHH		25.0722617229
1017PhosphorylationLLNEKYFSDLRNSIV
HHCCHHHHHHHHHHH		32.4224719451
1020MethylationEKYFSDLRNSIVNSQ
CHHHHHHHHHHHHCC		39.58-
1053UbiquitinationIERNLLTKNRDRFTQ
HHHHHHHCCHHHHHH		50.37-
1063PhosphorylationDRFTQNLSAFRREVN
HHHHHHHHHHHHHHH		32.6724719451
1082PhosphorylationNSTYGVNSNDMMS--
HCCCCCCCCCCCC--		31.6223401153
1087PhosphorylationVNSNDMMS-------
CCCCCCCC-------		30.3628674419
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of XPO7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XPO7_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of XPO7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRN2_HUMANXRN2physical
22939629
SYCC_HUMANCARSphysical
22863883
DPYL2_HUMANDPYSL2physical
22863883
JMJD6_HUMANJMJD6physical
22863883
RANB3_HUMANRANBP3physical
22863883
SC24C_HUMANSEC24Cphysical
22863883
SF01_HUMANSF1physical
22863883
DSCR3_HUMANDSCR3physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of XPO7_HUMAN

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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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