XPO6_HUMAN - dbPTM
XPO6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XPO6_HUMAN
UniProt AC Q96QU8
Protein Name Exportin-6
Gene Name XPO6
Organism Homo sapiens (Human).
Sequence Length 1125
Subcellular Localization Nucleus. Cytoplasm. Shuttles between the nucleus and the cytoplasm.
Protein Description Mediates the nuclear export of actin and profilin-actin complexes in somatic cells..
Protein Sequence MASEEASLRALESLMTEFFHDCTTNERKREIEELLNNFAQQIGAWRFCLYFLSSTRNDYVMMYSLTVFENLINKMWLGVPSQDKMEIRSCLPKLLLAHHKTLPYFIRNKLCKVIVDIGRQDWPMFYHDFFTNILQLIQSPVTTPLGLIMLKTTSEELACPREDLSVARKEELRKLLLDQVQTVLGLLTGILETVWDKHSVTAATPPPSPTSGESGDLLSNLLQSPSSAKLLNQPIPILDVESEYICSLALECLAHLFSWIPLSASITPSLLTTIFHFARFGCDIRARKMASVNGSSQNCVSGQERGRLGVLAMSCINELMSKNCVPMEFEEYLLRMFQQTFYLLQKITKDNNAHTVKSRLEELDESYIEKFTDFLRLFVSVHLRRIESYSQFPVVEFLTLLFKYTFHQPTHEGYFSCLDIWTLFLDYLTSKIKSRLGDKEAVLNRYEDALVLLLTEVLNRIQFRYNQAQLEELDDETLDDDQQTEWQRYLRQSLEVVAKVMELLPTHAFSTLFPVLQDNLEVYLGLQQFIVTSGSGHRLNITAENDCRRLHCSLRDLSSLLQAVGRLAEYFIGDVFAARFNDALTVVERLVKVTLYGSQIKLYNIETAVPSVLKPDLIDVHAQSLAALQAYSHWLAQYCSEVHRQNTQQFVTLISTTMDAITPLISTKVQDKLLLSACHLLVSLATTVRPVFLISIPAVQKVFNRITDASALRLVDKAQVLVCRALSNILLLPWPNLPENEQQWPVRSINHASLISALSRDYRNLKPSAVAPQRKMPLDDTKLIIHQTLSVLEDIVENISGESTKSRQICYQSLQESVQVSLALFPAFIHQSDVTDEMLSFFLTLFRGLRVQMGVPFTEQIIQTFLNMFTREQLAESILHEGSTGCRVVEKFLKILQVVVQEPGQVFKPFLPSIIALCMEQVYPIIAERPSPDVKAELFELLFRTLHHNWRYFFKSTVLASVQRGIAEEQMENEPQFSAIMQAFGQSFLQPDIHLFKQNLFYLETLNTKQKLYHKKIFRTAMLFQFVNVLLQVLVHKSHDLLQEEIGIAIYNMASVDFDGFFAAFLPEFLTSCDGVDANQKSVLGRNFKMDRDLPSFTQNVHRLVNDLRYYRLCNDSLPPGTVKL
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------MASEEASLR
------CCCHHHHHH		36.6322223895
79UbiquitinationINKMWLGVPSQDKME
HHHHCCCCCCCCHHH		3.7429967540
93AcetylationEIRSCLPKLLLAHHK
HHHHHHHHHHHHHHC		38.5325953088
93UbiquitinationEIRSCLPKLLLAHHK
HHHHHHHHHHHHHHC		38.5329967540
152PhosphorylationLGLIMLKTTSEELAC
CCEEEEECCCHHHCC		31.43-
153PhosphorylationGLIMLKTTSEELACP
CEEEEECCCHHHCCC		32.33-
154PhosphorylationLIMLKTTSEELACPR
EEEEECCCHHHCCCH		34.01-
175UbiquitinationRKEELRKLLLDQVQT
CHHHHHHHHHHHHHH		4.6727667366
183UbiquitinationLLDQVQTVLGLLTGI
HHHHHHHHHHHHHHH		1.9222817900
190PhosphorylationVLGLLTGILETVWDK
HHHHHHHHHHHHHHH		2.3732142685
194PhosphorylationLTGILETVWDKHSVT
HHHHHHHHHHHCCCC		4.5532142685
199PhosphorylationETVWDKHSVTAATPP
HHHHHHCCCCCCCCC		27.2329255136
201PhosphorylationVWDKHSVTAATPPPS
HHHHCCCCCCCCCCC		17.3729255136
204PhosphorylationKHSVTAATPPPSPTS
HCCCCCCCCCCCCCC		33.5929255136
208PhosphorylationTAATPPPSPTSGESG
CCCCCCCCCCCCCCC		46.7329255136
210PhosphorylationATPPPSPTSGESGDL
CCCCCCCCCCCCCCH		54.4229255136
211PhosphorylationTPPPSPTSGESGDLL
CCCCCCCCCCCCCHH		43.9029255136
214PhosphorylationPSPTSGESGDLLSNL
CCCCCCCCCCHHHHH		40.9229255136
219PhosphorylationGESGDLLSNLLQSPS
CCCCCHHHHHHCCCC		32.5029255136
224PhosphorylationLLSNLLQSPSSAKLL
HHHHHHCCCCHHHHH		27.0730278072
226PhosphorylationSNLLQSPSSAKLLNQ
HHHHCCCCHHHHHCC		48.4530278072
227PhosphorylationNLLQSPSSAKLLNQP
HHHCCCCHHHHHCCC		32.5730278072
274UbiquitinationTPSLLTTIFHFARFG
CHHHHHHHHHHHHHC		1.81-
275UbiquitinationPSLLTTIFHFARFGC
HHHHHHHHHHHHHCC		3.4927667366
283UbiquitinationHFARFGCDIRARKMA
HHHHHCCCCCCHHHH		33.5122817900
288UbiquitinationGCDIRARKMASVNGS
CCCCCCHHHHHCCCC		37.52-
296PhosphorylationMASVNGSSQNCVSGQ
HHHCCCCCCCCCCCC		27.15-
305MethylationNCVSGQERGRLGVLA
CCCCCCCCCHHHHHH		27.87-
307MethylationVSGQERGRLGVLAMS
CCCCCCCHHHHHHHH		34.19-
314PhosphorylationRLGVLAMSCINELMS
HHHHHHHHHHHHHHH		13.2625072903
321PhosphorylationSCINELMSKNCVPME
HHHHHHHHCCCCCCC		33.0825072903
332PhosphorylationVPMEFEEYLLRMFQQ
CCCCHHHHHHHHHHH		12.1125332170
335UbiquitinationEFEEYLLRMFQQTFY
CHHHHHHHHHHHHHH		22.6727667366
340PhosphorylationLLRMFQQTFYLLQKI
HHHHHHHHHHHHHHH		11.9425332170
342PhosphorylationRMFQQTFYLLQKITK
HHHHHHHHHHHHHHC		15.1925332170
343UbiquitinationMFQQTFYLLQKITKD
HHHHHHHHHHHHHCC		3.4021906983
343UbiquitinationMFQQTFYLLQKITKD
HHHHHHHHHHHHHCC		3.4022817900
349UbiquitinationYLLQKITKDNNAHTV
HHHHHHHCCCCCHHH		63.0327667366
356UbiquitinationKDNNAHTVKSRLEEL
CCCCCHHHHHHHHHH		3.6829901268
357UbiquitinationDNNAHTVKSRLEELD
CCCCHHHHHHHHHHC		30.8922817900
370UbiquitinationLDESYIEKFTDFLRL
HCHHHHHHHHHHHHH		43.9629901268
421UbiquitinationYFSCLDIWTLFLDYL
CCHHHHHHHHHHHHH		6.1622817900
542PhosphorylationSGHRLNITAENDCRR
CCCCEEEECCCHHHH		27.1825841592
558PhosphorylationHCSLRDLSSLLQAVG
CCCHHHHHHHHHHHH		24.1921712546
585PhosphorylationARFNDALTVVERLVK
HHHHHHHHHHHHHHH		24.99-
592UbiquitinationTVVERLVKVTLYGSQ
HHHHHHHHHEEECCE		33.8122817900
647PhosphorylationSEVHRQNTQQFVTLI
HHHHHHCHHHHHHHH		18.53-
652PhosphorylationQNTQQFVTLISTTMD
HCHHHHHHHHHHHHH		21.4720071362
655PhosphorylationQQFVTLISTTMDAIT
HHHHHHHHHHHHHHH		22.42-
657PhosphorylationFVTLISTTMDAITPL
HHHHHHHHHHHHHHH		13.2820071362
662PhosphorylationSTTMDAITPLISTKV
HHHHHHHHHHHCHHH		17.4820071362
666PhosphorylationDAITPLISTKVQDKL
HHHHHHHCHHHHHHH		29.8324719451
692UbiquitinationATTVRPVFLISIPAV
HHCCCCEEEEHHHHH		5.7822817900
703UbiquitinationIPAVQKVFNRITDAS
HHHHHHHHHHCCCHH		7.01-
717UbiquitinationSALRLVDKAQVLVCR
HHHHHCCHHHHHHHH		32.99-
752UbiquitinationPVRSINHASLISALS
CCCCCCHHHHHHHHH		11.0922817900
752UbiquitinationPVRSINHASLISALS
CCCCCCHHHHHHHHH		11.0921906983
766UbiquitinationSRDYRNLKPSAVAPQ
HCCHHCCCCCCCCCC		40.2421906983
781PhosphorylationRKMPLDDTKLIIHQT
CCCCCCCCHHHHHHH		27.67-
788PhosphorylationTKLIIHQTLSVLEDI
CHHHHHHHHHHHHHH		13.56-
804PhosphorylationENISGESTKSRQICY
HHCCCCCHHHHHHHH		28.83-
891UbiquitinationTGCRVVEKFLKILQV
CHHHHHHHHHHHHHH		44.37-
956PhosphorylationNWRYFFKSTVLASVQ
CHHHHHHHHHHHHHH		20.7020068231
957PhosphorylationWRYFFKSTVLASVQR
HHHHHHHHHHHHHHH		21.8220068231
961PhosphorylationFKSTVLASVQRGIAE
HHHHHHHHHHHCCCH		18.0220068231
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 XPO6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XPO6_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 XPO6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUP62_HUMANNUP62physical
16189514
VASP_HUMANVASPphysical
14592989
RAN_HUMANRANphysical
14592989
ACTS_HUMANACTA1physical
14592989
PROF1_HUMANPFN1physical
14592989
DIAP1_HUMANDIAPH1physical
14592989
ENAH_HUMANENAHphysical
14592989
NUP62_HUMANNUP62physical
25416956
NUP62_HUMANNUP62physical
21516116
MTOR_HUMANMTORphysical
27173435
THADA_HUMANTHADAphysical
27173435
LST8_HUMANMLST8physical
27173435
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 XPO6_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory