XPO4_HUMAN - dbPTM
XPO4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XPO4_HUMAN
UniProt AC Q9C0E2
Protein Name Exportin-4
Gene Name XPO4
Organism Homo sapiens (Human).
Sequence Length 1151
Subcellular Localization Cytoplasm . Nucleus . 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. XPO4 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 MMAAALGPPEVIAQLENAAKVLMAPPSMVNNEQRQHAEHIFLSFRKSKSPFAVCKHILETSKVDYVLFQAATAIMEAVVREWILLEKGSIESLRTFLLTYVLQRPNLQKYVREQILLAVAVIVKRGSLDKSIDCKSIFHEVSQLISSGNPTVQTLACSILTALLSEFSSSSKTSNIGLSMEFHGNCKRVFQEEDLRQIFMLTVEVLQEFSRRENLNAQMSSVFQRYLALANQVLSWNFLPPNLGRHYIAMFESSQNVLLKPTESWRETLLDSRVMELFFTVHRKIREDSDMAQDSLQCLAQLASLHGPIFPDEGSQVDYLAHFIEGLLNTINGIEIEDSEAVGISSIISNLITVFPRNVLTAIPSELFSSFVNCLTHLTCSFGRSAALEEVLDKDDMVYMEAYDKLLESWLTLVQDDKHFHKGFFTQHAVQVFNSYIQCHLAAPDGTRNLTANGVASREEEEISELQEDDRDQFSDQLASVGMLGRIAAEHCIPLLTSLLEERVTRLHGQLQRHQQQLLASPGSSTVDNKMLDDLYEDIHWLILVTGYLLADDTQGETPLIPPEIMEYSIKHSSEVDINTTLQILGSPGEKASSIPGYNRTDSVIRLLSAILRVSEVESRAIRADLTHLLSPQMGKDIVWFLKRWAKTYLLVDEKLYDQISLPFSTAFGADTEGSQWIIGYLLQKVISNLSVWSSEQDLANDTVQLLVTLVERRERANLVIQCENWWNLAKQFASRSPPLNFLSSPVQRTLMKALVLGGFAHMDTETKQQYWTEVLQPLQQRFLRVINQENFQQMCQQEEVKQEITATLEALCGIAEATQIDNVAILFNFLMDFLTNCIGLMEVYKNTPETVNLIIEVFVEVAHKQICYLGESKAMNLYEACLTLLQVYSKNNLGRQRIDVTAEEEQYQDLLLIMELLTNLLSKEFIDFSDTDEVFRGHEPGQAANRSVSAADVVLYGVNLILPLMSQDLLKFPTLCNQYYKLITFICEIFPEKIPQLPEDLFKSLMYSLELGMTSMSSEVCQLCLEALTPLAEQCAKAQETDSPLFLATRHFLKLVFDMLVLQKHNTEMTTAAGEAFYTLVCLHQAEYSELVETLLSSQQDPVIYQRLADAFNKLTASSTPPTLDRKQKMAFLKSLEEFMANVGGLLCVK
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
23SulfoxidationENAAKVLMAPPSMVN
HHHHHHHCCCHHHCC		6.1921406390
27PhosphorylationKVLMAPPSMVNNEQR
HHHCCCHHHCCHHHH		34.0125907765
43PhosphorylationHAEHIFLSFRKSKSP
HHHHHHHHHHCCCCH		16.5625907765
95PhosphorylationGSIESLRTFLLTYVL
CCHHHHHHHHHHHHH		24.7524719451
100PhosphorylationLRTFLLTYVLQRPNL
HHHHHHHHHHHCCCH		10.1124719451
247PhosphorylationPPNLGRHYIAMFESS
CCCCCCHHEEEEECC		6.76-
262PhosphorylationQNVLLKPTESWRETL
CCEEECCCHHHHHHH		40.85-
264PhosphorylationVLLKPTESWRETLLD
EEECCCHHHHHHHHH		33.63-
353UbiquitinationSIISNLITVFPRNVL
HHHHHHHHHCCHHHH		21.1821890473
367UbiquitinationLTAIPSELFSSFVNC
HHHCCHHHHHHHHHH		6.2321890473
385PhosphorylationLTCSFGRSAALEEVL
HHHHHCCHHHHHHHC		20.48-
399PhosphorylationLDKDDMVYMEAYDKL
CCCCCCHHHHHHHHH		5.21-
403PhosphorylationDMVYMEAYDKLLESW
CCHHHHHHHHHHHHH		10.58-
457PhosphorylationLTANGVASREEEEIS
CCCCCCCCCCHHHHH		37.5128102081
464PhosphorylationSREEEEISELQEDDR
CCCHHHHHHHCCCCH		35.2227362937
464UbiquitinationSREEEEISELQEDDR
CCCHHHHHHHCCCCH		35.2221890473
468UbiquitinationEEISELQEDDRDQFS
HHHHHHCCCCHHHHH		74.6121890473
475PhosphorylationEDDRDQFSDQLASVG
CCCHHHHHHHHHHHH		20.8622210691
492GlutathionylationGRIAAEHCIPLLTSL
HHHHHHHHHHHHHHH		2.2922555962
498PhosphorylationHCIPLLTSLLEERVT
HHHHHHHHHHHHHHH		30.8126437602
521PhosphorylationHQQQLLASPGSSTVD
HHHHHHCCCCCCHHC		29.7529255136
524PhosphorylationQLLASPGSSTVDNKM
HHHCCCCCCHHCCHH		26.6430266825
525PhosphorylationLLASPGSSTVDNKML
HHCCCCCCHHCCHHH		38.0630266825
526PhosphorylationLASPGSSTVDNKMLD
HCCCCCCHHCCHHHH		33.3130266825
569PhosphorylationPPEIMEYSIKHSSEV
CHHHHHHCCCCCCCC		16.3224719451
569UbiquitinationPPEIMEYSIKHSSEV
CHHHHHHCCCCCCCC		16.3221890473
587PhosphorylationTTLQILGSPGEKASS
CCEEECCCCCCCCCC		26.7025159151
594PhosphorylationSPGEKASSIPGYNRT
CCCCCCCCCCCCCCH		37.3521712546
598PhosphorylationKASSIPGYNRTDSVI
CCCCCCCCCCHHHHH		8.9821712546
603PhosphorylationPGYNRTDSVIRLLSA
CCCCCHHHHHHHHHH		20.8721712546
615PhosphorylationLSAILRVSEVESRAI
HHHHHHHHHHHHHHH		29.5027134283
619PhosphorylationLRVSEVESRAIRADL
HHHHHHHHHHHHHHH		31.9927134283
636UbiquitinationLLSPQMGKDIVWFLK
HHCHHCCHHHHHHHH		38.65-
643UbiquitinationKDIVWFLKRWAKTYL
HHHHHHHHHHHHHEE		36.1021890473
648PhosphorylationFLKRWAKTYLLVDEK
HHHHHHHHEEEECHH		16.2021406692
649PhosphorylationLKRWAKTYLLVDEKL
HHHHHHHEEEECHHH		9.4221406692
948PhosphorylationPGQAANRSVSAADVV
CCCCCCCCCCHHHHH		21.8922210691
950PhosphorylationQAANRSVSAADVVLY
CCCCCCCCHHHHHHH		20.9822210691
957PhosphorylationSAADVVLYGVNLILP
CHHHHHHHHHHHHHH		13.8622210691
967PhosphorylationNLILPLMSQDLLKFP
HHHHHHCCHHHHCCH		28.3822210691
1121PhosphorylationNKLTASSTPPTLDRK
HHHHCCCCCCCCCHH		30.6929083192
1124PhosphorylationTASSTPPTLDRKQKM
HCCCCCCCCCHHHHH		42.3629083192
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 XPO4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XPO4_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 XPO4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF5A1_HUMANEIF5Aphysical
10944119
ZHX1_HUMANZHX1physical
22939629
THADA_HUMANTHADAphysical
27173435
LST8_HUMANMLST8physical
27173435
MTOR_HUMANMTORphysical
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 XPO4_HUMAN

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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-521, AND MASSSPECTROMETRY.
"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-464, AND MASSSPECTROMETRY.
"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 SER-464 AND SER-521, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASSSPECTROMETRY.

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