XPOT_HUMAN - dbPTM
XPOT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XPOT_HUMAN
UniProt AC O43592
Protein Name Exportin-T
Gene Name XPOT
Organism Homo sapiens (Human).
Sequence Length 962
Subcellular Localization Nucleus. Cytoplasm. Nuclear, once bound to tRNA and Ran the complex translocates to the cytoplasm. Shuttles between the nucleus and the cytoplasm.
Protein Description Mediates the nuclear export of aminoacylated tRNAs. In the nucleus binds to tRNA 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 tRNA from the export receptor. XPOT 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 MDEQALLGLNPNADSDFRQRALAYFEQLKISPDAWQVCAEALAQRTYSDDHVKFFCFQVLEHQVKYKYSELTTVQQQLIRETLISWLQAQMLNPQPEKTFIRNKAAQVFALLFVTEYLTKWPKFFFDILSVVDLNPRGVDLYLRILMAIDSELVDRDVVHTSEEARRNTLIKDTMREQCIPNLVESWYQILQNYQFTNSEVTCQCLEVVGAYVSWIDLSLIANDRFINMLLGHMSIEVLREEACDCLFEVVNKGMDPVDKMKLVESLCQVLQSAGFFSIDQEEDVDFLARFSKLVNGMGQSLIVSWSKLIKNGDIKNAQEALQAIETKVALMLQLLIHEDDDISSNIIGFCYDYLHILKQLTVLSDQQKANVEAIMLAVMKKLTYDEEYNFENEGEDEAMFVEYRKQLKLLLDRLAQVSPELLLASVRRVFSSTLQNWQTTRFMEVEVAIRLLYMLAEALPVSHGAHFSGDVSKASALQDMMRTLVTSGVSSYQHTSVTLEFFETVVRYEKFFTVEPQHIPCVLMAFLDHRGLRHSSAKVRSRTAYLFSRFVKSLNKQMNPFIEDILNRIQDLLELSPPENGHQSLLSSDDQLFIYETAGVLIVNSEYPAERKQALMRNLLTPLMEKFKILLEKLMLAQDEERQASLADCLNHAVGFASRTSKAFSNKQTVKQCGCSEVYLDCLQTFLPALSCPLQKDILRSGVRTFLHRMIICLEEEVLPFIPSASEHMLKDCEAKDLQEFIPLINQITAKFKIQVSPFLQQMFMPLLHAIFEVLLRPAEENDQSAALEKQMLRRSYFAFLQTVTGSGMSEVIANQGAENVERVLVTVIQGAVEYPDPIAQKTCFIILSKLVELWGGKDGPVGFADFVYKHIVPACFLAPLKQTFDLADAQTVLALSECAVTLKTIHLKRGPECVQYLQQEYLPSLQVAPEIIQEFCQALQQPDAKVFKNYLKVFFQRAKP
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
1Acetylation-------MDEQALLG
-------CCHHHHCC		13.2822223895
68PhosphorylationEHQVKYKYSELTTVQ
HHHHHHCHHCCHHHH		12.3220071362
69PhosphorylationHQVKYKYSELTTVQQ
HHHHHCHHCCHHHHH		23.2120071362
115PhosphorylationVFALLFVTEYLTKWP
HHHHHHHHHHHHCCC		16.1629083192
117PhosphorylationALLFVTEYLTKWPKF
HHHHHHHHHHCCCHH		15.4229083192
119PhosphorylationLFVTEYLTKWPKFFF
HHHHHHHHCCCHHHH		30.1129083192
147SulfoxidationDLYLRILMAIDSELV
HHHHHHHHHHCHHHC		2.6030846556
169PhosphorylationSEEARRNTLIKDTMR
CHHHHHCCCCHHHHH		28.2222210691
172UbiquitinationARRNTLIKDTMREQC
HHHCCCCHHHHHHHH		50.7027667366
260AcetylationKGMDPVDKMKLVESL
CCCCHHHHHHHHHHH		37.8626822725
311UbiquitinationVSWSKLIKNGDIKNA
HHHHHHHHCCCCCCH		66.3732142685
311MalonylationVSWSKLIKNGDIKNA
HHHHHHHHCCCCCCH		66.3726320211
316UbiquitinationLIKNGDIKNAQEALQ
HHHCCCCCCHHHHHH		51.4729967540
327PhosphorylationEALQAIETKVALMLQ
HHHHHHHHHHHHHHH		25.38-
362PhosphorylationLHILKQLTVLSDQQK
HHHHHHHHHCCHHHH		19.5324043423
365PhosphorylationLKQLTVLSDQQKANV
HHHHHHCCHHHHCHH		29.1024043423
409UbiquitinationVEYRKQLKLLLDRLA
HHHHHHHHHHHHHHH		34.3024816145
432PhosphorylationASVRRVFSSTLQNWQ
HHHHHHHHHHHCCCC		21.40-
553UbiquitinationYLFSRFVKSLNKQMN
HHHHHHHHHHHHHCC		46.6522817900
557UbiquitinationRFVKSLNKQMNPFIE
HHHHHHHHHCCHHHH		57.1021890473
622PhosphorylationALMRNLLTPLMEKFK
HHHHHHHHHHHHHHH		19.9728509920
6272-HydroxyisobutyrylationLLTPLMEKFKILLEK
HHHHHHHHHHHHHHH		37.68-
627AcetylationLLTPLMEKFKILLEK
HHHHHHHHHHHHHHH		37.6819608861
627UbiquitinationLLTPLMEKFKILLEK
HHHHHHHHHHHHHHH		37.6821890473
629UbiquitinationTPLMEKFKILLEKLM
HHHHHHHHHHHHHHH		43.4423000965
6342-HydroxyisobutyrylationKFKILLEKLMLAQDE
HHHHHHHHHHHCCCH		38.88-
634AcetylationKFKILLEKLMLAQDE
HHHHHHHHHHHCCCH		38.8819608861
634UbiquitinationKFKILLEKLMLAQDE
HHHHHHHHHHHCCCH		38.8823000965
636SulfoxidationKILLEKLMLAQDEER
HHHHHHHHHCCCHHH		4.2821406390
646PhosphorylationQDEERQASLADCLNH
CCHHHHHHHHHHHHH		18.7620068231
659PhosphorylationNHAVGFASRTSKAFS
HHHHHHHHHCCHHHC		33.5520068231
661PhosphorylationAVGFASRTSKAFSNK
HHHHHHHCCHHHCCC		31.8920068231
662PhosphorylationVGFASRTSKAFSNKQ
HHHHHHCCHHHCCCC		22.3720068231
663UbiquitinationGFASRTSKAFSNKQT
HHHHHCCHHHCCCCH		53.4927667366
668AcetylationTSKAFSNKQTVKQCG
CCHHHCCCCHHHHHC		46.2625953088
668UbiquitinationTSKAFSNKQTVKQCG
CCHHHCCCCHHHHHC		46.2627667366
737UbiquitinationMLKDCEAKDLQEFIP
HHHHCCCCCHHHHHH		36.3629967540
859UbiquitinationLVELWGGKDGPVGFA
HHHHHCCCCCCCCHH		56.42-
885PhosphorylationFLAPLKQTFDLADAQ
HHHCHHCCCCCCHHH		19.9628857561
893PhosphorylationFDLADAQTVLALSEC
CCCCHHHHHHHHHHH		21.1428857561
903PhosphorylationALSECAVTLKTIHLK
HHHHHHEEEHHHHHH		12.1928857561
950UbiquitinationQPDAKVFKNYLKVFF
CCCHHHHHHHHHHHH		47.9029967540
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 XPOT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XPOT_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 XPOT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APEX1_HUMANAPEX1physical
22863883
PAPS1_HUMANPAPSS1physical
22863883
GCSH_HUMANGCSHphysical
26344197
NAA40_HUMANNAA40physical
26344197
PSA3_HUMANPSMA3physical
26344197
PSA4_HUMANPSMA4physical
26344197
WDR11_HUMANWDR11physical
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 XPOT_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 MET-1, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-634, AND MASS SPECTROMETRY.

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