UniProt ID | XPO1_HUMAN | |
---|---|---|
UniProt AC | O14980 | |
Protein Name | Exportin-1 | |
Gene Name | XPO1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 1071 | |
Subcellular Localization | Cytoplasm. Nucleus, nucleoplasm. Nucleus, Cajal body. Nucleus, nucleolus. Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm. | |
Protein Description | Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this 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. 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. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization.. | |
Protein Sequence | MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTEKLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKISTSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
20 | Phosphorylation | ARQLLDFSQKLDINL HHHHHCHHHHCCHHH | 26.52 | 29507054 | |
22 | Ubiquitination | QLLDFSQKLDINLLD HHHCHHHHCCHHHHH | 47.10 | - | |
34 | Glutathionylation | LLDNVVNCLYHGEGA HHHHHHHHHHCCCHH | 2.42 | 22555962 | |
45 | Sulfoxidation | GEGAQQRMAQEVLTH CCHHHHHHHHHHHHH | 3.82 | 21406390 | |
54 | Ubiquitination | QEVLTHLKEHPDAWT HHHHHHHHHCCCHHH | 46.50 | 21906983 | |
54 | Acetylation | QEVLTHLKEHPDAWT HHHHHHHHHCCCHHH | 46.50 | 25953088 | |
65 | Phosphorylation | DAWTRVDTILEFSQN CHHHHHHHHHHHHHH | 25.30 | 20068231 | |
70 | Phosphorylation | VDTILEFSQNMNTKY HHHHHHHHHHCCCCC | 15.98 | 20068231 | |
73 | Sulfoxidation | ILEFSQNMNTKYYGL HHHHHHHCCCCCHHH | 5.37 | 21406390 | |
88 | Ubiquitination | QILENVIKTRWKILP HHHHHHHHHCCEECC | 27.96 | - | |
89 | O-linked_Glycosylation | ILENVIKTRWKILPR HHHHHHHHCCEECCH | 30.55 | 23301498 | |
92 | Ubiquitination | NVIKTRWKILPRNQC HHHHHCCEECCHHHC | 30.95 | - | |
103 | 2-Hydroxyisobutyrylation | RNQCEGIKKYVVGLI HHHCCHHHHHHEEEE | 49.24 | - | |
103 | Acetylation | RNQCEGIKKYVVGLI HHHCCHHHHHHEEEE | 49.24 | 25953088 | |
105 | Phosphorylation | QCEGIKKYVVGLIIK HCCHHHHHHEEEEEE | 8.72 | 28152594 | |
122 | Ubiquitination | SDPTCVEKEKVYIGK CCCCCCCCCEEEEHH | 42.30 | - | |
122 | Acetylation | SDPTCVEKEKVYIGK CCCCCCCCCEEEEHH | 42.30 | 26051181 | |
124 | Ubiquitination | PTCVEKEKVYIGKLN CCCCCCCEEEEHHHH | 51.94 | - | |
124 | Acetylation | PTCVEKEKVYIGKLN CCCCCCCEEEEHHHH | 51.94 | 25953088 | |
144 | Acetylation | ILKQEWPKHWPTFIS HHHHHCCCCCCCHHH | 60.41 | 23954790 | |
144 | Ubiquitination | ILKQEWPKHWPTFIS HHHHHCCCCCCCHHH | 60.41 | 21906983 | |
164 | Glutathionylation | SRTSESLCQNNMVIL CCCCHHHHHCCCHHH | 5.91 | 22555962 | |
164 | S-nitrosylation | SRTSESLCQNNMVIL CCCCHHHHHCCCHHH | 5.91 | 2212679 | |
182 | Phosphorylation | SEEVFDFSSGQITQV CHHHHCCCCCCCEEC | 35.09 | 28348404 | |
183 | Phosphorylation | EEVFDFSSGQITQVK HHHHCCCCCCCEECC | 34.41 | 28348404 | |
187 | Phosphorylation | DFSSGQITQVKSKHL CCCCCCCEECCCHHH | 21.30 | 24173317 | |
190 | Ubiquitination | SGQITQVKSKHLKDS CCCCEECCCHHHCHH | 43.92 | 21906983 | |
190 | 2-Hydroxyisobutyrylation | SGQITQVKSKHLKDS CCCCEECCCHHHCHH | 43.92 | - | |
192 | Ubiquitination | QITQVKSKHLKDSMC CCEECCCHHHCHHHH | 47.44 | - | |
248 | Phosphorylation | IFETKLISTLIYKFL HHHHHHHHHHHHHHH | 27.83 | 21406692 | |
249 | Phosphorylation | FETKLISTLIYKFLN HHHHHHHHHHHHHHC | 15.35 | 21406692 | |
252 | Phosphorylation | KLISTLIYKFLNVPM HHHHHHHHHHHCCCC | 9.98 | 19835603 | |
264 | Phosphorylation | VPMFRNVSLKCLTEI CCCCCCCCHHHHHHH | 26.17 | 19835603 | |
297 | Sulfoxidation | TMMQLKQMLPLNTNI HHHHHHHHCCCCCCE | 3.88 | 28183972 | |
339 | Ubiquitination | EHDQLIEKRLNLRET HHHHHHHHHHCHHHH | 56.01 | - | |
339 | 2-Hydroxyisobutyrylation | EHDQLIEKRLNLRET HHHHHHHHHHCHHHH | 56.01 | - | |
339 | Acetylation | EHDQLIEKRLNLRET HHHHHHHHHHCHHHH | 56.01 | 27452117 | |
358 | Phosphorylation | LHYMLLVSEVEETEI HHHHHHHHCCCHHHH | 35.57 | 26074081 | |
363 | Phosphorylation | LVSEVEETEIFKICL HHHCCCHHHHHHHHH | 22.37 | 26074081 | |
372 | Phosphorylation | IFKICLEYWNHLAAE HHHHHHHHHHHHHHH | 9.88 | 26074081 | |
381 | Phosphorylation | NHLAAELYRESPFST HHHHHHHHHHCCCCC | 12.11 | 26074081 | |
384 | Phosphorylation | AAELYRESPFSTSAS HHHHHHHCCCCCCCC | 23.42 | 23927012 | |
387 | Phosphorylation | LYRESPFSTSASPLL HHHHCCCCCCCCCCC | 25.49 | 30266825 | |
388 | Phosphorylation | YRESPFSTSASPLLS HHHCCCCCCCCCCCC | 28.79 | 30266825 | |
389 | Phosphorylation | RESPFSTSASPLLSG HHCCCCCCCCCCCCC | 26.08 | 30266825 | |
391 | Phosphorylation | SPFSTSASPLLSGSQ CCCCCCCCCCCCCCC | 18.82 | 29255136 | |
395 | Phosphorylation | TSASPLLSGSQHFDV CCCCCCCCCCCCCCC | 44.04 | 30266825 | |
397 | Phosphorylation | ASPLLSGSQHFDVPP CCCCCCCCCCCCCCC | 19.67 | 17525332 | |
409 | Phosphorylation | VPPRRQLYLPMLFKV CCCCHHHHHHHHHHH | 10.62 | 21406692 | |
415 | Acetylation | LYLPMLFKVRLLMVS HHHHHHHHHHHHHHH | 23.60 | 25953088 | |
415 | Ubiquitination | LYLPMLFKVRLLMVS HHHHHHHHHHHHHHH | 23.60 | 21906983 | |
424 | Sulfoxidation | RLLMVSRMAKPEEVL HHHHHHCCCCCCEEE | 4.35 | 30846556 | |
426 | Ubiquitination | LMVSRMAKPEEVLVV HHHHCCCCCCEEEEE | 43.55 | 21906983 | |
445 | Sulfoxidation | GEVVREFMKDTDSIN CHHHHHHHCCCCCCC | 3.08 | 30846556 | |
446 | Acetylation | EVVREFMKDTDSINL HHHHHHHCCCCCCCH | 63.90 | 19608861 | |
446 | Ubiquitination | EVVREFMKDTDSINL HHHHHHHCCCCCCCH | 63.90 | 21890473 | |
446 | 2-Hydroxyisobutyrylation | EVVREFMKDTDSINL HHHHHHHCCCCCCCH | 63.90 | - | |
446 | Malonylation | EVVREFMKDTDSINL HHHHHHHCCCCCCCH | 63.90 | 26320211 | |
448 | Phosphorylation | VREFMKDTDSINLYK HHHHHCCCCCCCHHH | 26.57 | 30631047 | |
450 | Phosphorylation | EFMKDTDSINLYKNM HHHCCCCCCCHHHHH | 18.57 | 20873877 | |
454 | Phosphorylation | DTDSINLYKNMRETL CCCCCCHHHHHHHHH | 8.88 | - | |
455 | Acetylation | TDSINLYKNMRETLV CCCCCHHHHHHHHHH | 47.65 | 23954790 | |
455 | Ubiquitination | TDSINLYKNMRETLV CCCCCHHHHHHHHHH | 47.65 | 21890473 | |
455 | Malonylation | TDSINLYKNMRETLV CCCCCHHHHHHHHHH | 47.65 | 26320211 | |
460 | Phosphorylation | LYKNMRETLVYLTHL HHHHHHHHHHHHHCC | 15.91 | 24043423 | |
463 | Phosphorylation | NMRETLVYLTHLDYV HHHHHHHHHHCCHHC | 14.70 | 24043423 | |
465 | Phosphorylation | RETLVYLTHLDYVDT HHHHHHHHCCHHCCH | 11.60 | 24043423 | |
469 | Phosphorylation | VYLTHLDYVDTERIM HHHHCCHHCCHHHHH | 13.44 | 24043423 | |
472 | Phosphorylation | THLDYVDTERIMTEK HCCHHCCHHHHHHHH | 19.67 | 24043423 | |
479 | Ubiquitination | TERIMTEKLHNQVNG HHHHHHHHHHHCCCC | 45.97 | 21906983 | |
479 | Acetylation | TERIMTEKLHNQVNG HHHHHHHHHHHCCCC | 45.97 | 26051181 | |
514 | Acetylation | AMHEEDEKRFLVTVI CCCHHHHHHHHHHHH | 61.85 | 25953088 | |
519 | Phosphorylation | DEKRFLVTVIKDLLG HHHHHHHHHHHHHHH | 20.75 | 22067460 | |
528 | S-nitrosocysteine | IKDLLGLCEQKRGKD HHHHHHHHHHHCCCC | 5.03 | - | |
528 | S-nitrosylation | IKDLLGLCEQKRGKD HHHHHHHHHHHCCCC | 5.03 | 19483679 | |
531 | Acetylation | LLGLCEQKRGKDNKA HHHHHHHHCCCCCCE | 40.60 | 23749302 | |
531 | Ubiquitination | LLGLCEQKRGKDNKA HHHHHHHHCCCCCCE | 40.60 | - | |
531 | 2-Hydroxyisobutyrylation | LLGLCEQKRGKDNKA HHHHHHHHCCCCCCE | 40.60 | - | |
534 | Acetylation | LCEQKRGKDNKAIIA HHHHHCCCCCCEEHH | 63.26 | 25038526 | |
537 | Acetylation | QKRGKDNKAIIASNI HHCCCCCCEEHHHHH | 51.61 | 23954790 | |
545 | Sulfoxidation | AIIASNIMYIVGQYP EEHHHHHHHHHHCCH | 1.87 | 28183972 | |
560 | Acetylation | RFLRAHWKFLKTVVN HHHHHHHHHHHHHHH | 30.83 | 25953088 | |
563 | Ubiquitination | RAHWKFLKTVVNKLF HHHHHHHHHHHHHHH | 42.26 | - | |
563 | Acetylation | RAHWKFLKTVVNKLF HHHHHHHHHHHHHHH | 42.26 | 25953088 | |
568 | Acetylation | FLKTVVNKLFEFMHE HHHHHHHHHHHHHHH | 42.83 | 23954790 | |
590 | Ubiquitination | MACDTFIKIAQKCRR HCHHHHHHHHHHHHH | 28.00 | - | |
674 | Ubiquitination | SIIQQATKNVDILKD HHHHHHHCCCCCCCC | 58.97 | - | |
680 | Ubiquitination | TKNVDILKDPETVKQ HCCCCCCCCHHHHHH | 72.13 | - | |
680 | 2-Hydroxyisobutyrylation | TKNVDILKDPETVKQ HCCCCCCCCHHHHHH | 72.13 | - | |
680 | Acetylation | TKNVDILKDPETVKQ HCCCCCCCCHHHHHH | 72.13 | 26051181 | |
686 | Acetylation | LKDPETVKQLGSILK CCCHHHHHHHHHHHH | 47.42 | 23954790 | |
686 | Ubiquitination | LKDPETVKQLGSILK CCCHHHHHHHHHHHH | 47.42 | 21906983 | |
690 | Phosphorylation | ETVKQLGSILKTNVR HHHHHHHHHHHHCHH | 33.08 | 24719451 | |
693 | Acetylation | KQLGSILKTNVRACK HHHHHHHHHCHHHHH | 36.06 | 19608861 | |
693 | Ubiquitination | KQLGSILKTNVRACK HHHHHHHHHCHHHHH | 36.06 | 21906983 | |
694 | Phosphorylation | QLGSILKTNVRACKA HHHHHHHHCHHHHHH | 35.19 | - | |
700 | Ubiquitination | KTNVRACKAVGHPFV HHCHHHHHHHCCCHH | 45.16 | - | |
700 | Malonylation | KTNVRACKAVGHPFV HHCHHHHHHHCCCHH | 45.16 | 26320211 | |
700 | Acetylation | KTNVRACKAVGHPFV HHCHHHHHHHCCCHH | 45.16 | 25953088 | |
714 | Phosphorylation | VIQLGRIYLDMLNVY HHEECHHHHHHHHHH | 8.69 | 28152594 | |
757 | Acetylation | TVKRETLKLISGWVS HHCHHHHHHHHHHHH | 51.71 | 25953088 | |
757 | Ubiquitination | TVKRETLKLISGWVS HHCHHHHHHHHHHHH | 51.71 | 21890473 | |
757 | Malonylation | TVKRETLKLISGWVS HHCHHHHHHHHHHHH | 51.71 | 26320211 | |
760 | Phosphorylation | RETLKLISGWVSRSN HHHHHHHHHHHHCCC | 36.72 | 21406692 | |
764 | Phosphorylation | KLISGWVSRSNDPQM HHHHHHHHCCCCHHH | 24.39 | 20068231 | |
766 | Phosphorylation | ISGWVSRSNDPQMVA HHHHHHCCCCHHHHH | 37.77 | 21406692 | |
771 | Sulfoxidation | SRSNDPQMVAENFVP HCCCCHHHHHHHCCH | 3.62 | 28183972 | |
802 | Phosphorylation | AREPEVLSTMAIIVN CCCHHHHHHHHHHHH | 22.70 | - | |
804 | Sulfoxidation | EPEVLSTMAIIVNKL CHHHHHHHHHHHHHH | 1.96 | 21406390 | |
816 | Phosphorylation | NKLGGHITAEIPQIF HHHCCCCEECHHHHH | 16.74 | - | |
841 | Phosphorylation | INKDFEEYPEHRTNF HCCCHHHCCCHHCCH | 13.51 | - | |
877 | Phosphorylation | QFKLVLDSIIWAFKH HHHHHHHHHHHHHHH | 16.29 | 27794612 | |
1012 | Acetylation | NQDIPAFKEHLRDFL CCCCHHHHHHHHHHH | 46.46 | 26051181 | |
1030 | Phosphorylation | KEFAGEDTSDLFLEE HHHCCCCCHHHHHHH | 21.60 | 30266825 | |
1031 | Phosphorylation | EFAGEDTSDLFLEER HHCCCCCHHHHHHHH | 44.64 | 15574331 | |
1043 | Methylation | EEREIALRQADEEKH HHHHHHHHHHHHHHH | 22.18 | - | |
1055 | Phosphorylation | EKHKRQMSVPGIFNP HHHHHHCCCCCCCCH | 19.47 | 25159151 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of XPO1_HUMAN !! |
* 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 XPO1_HUMAN !! |
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. |
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Acetylation | |
Reference | PubMed |
"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-446; LYS-455 AND LYS-693,AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"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-391 AND SER-1031, ANDMASS SPECTROMETRY. | |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND MASSSPECTROMETRY. |