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Overview

Uniprot IDQ9UIA9
Protein NameExportin-7
Gene NameXPO7
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
568 YIGDQVQKSSKLYRR

Function

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

10 MADHVQSLAQ 20 LENLCKQLYE 30 TTDTTTRLQA 40 EKALVEFTNS 50 PDCLSKCQLL 60 LERGSSSYSQ 70 LLAATCLTKL 80 VSRTNNPLPL 90 EQRIDIRNYV 100 LNYLATRPKL 110 ATFVTQALIQ 120 LYARITKLGW 130 FDCQKDDYVF 140 RNAITDVTRF 150 LQDSVEYCII 160 GVTILSQLTN 170 EINQADTTHP 180 LTKHRKIASS 190 FRDSSLFDIF 200 TLSCNLLKQA 210 SGKNLNLNDE 220 SQHGLLMQLL 230 KLTHNCLNFD 240 FIGTSTDESS 250 DDLCTVQIPT 260 SWRSAFLDSS 270 TLQLFFDLYH 280 SIPPSFSPLV 290 LSCLVQIASV 300 RRSLFNNAER 310 AKFLSHLVDG 320 VKRILENPQS 330 LSDPNNYHEF 340 CRLLARLKSN 350 YQLGELVKVE 360 NYPEVIRLIA 370 NFTVTSLQHW 380 EFAPNSVHYL 390 LSLWQRLAAS 400 VPYVKATEPH 410 MLETYTPEVT 420 KAYITSRLES 430 VHIILRDGLE 440 DPLEDTGLVQ 450 QQLDQLSTIG 460 RCEYEKTCAL 470 LVQLFDQSAQ 480 SYQELLQSAS 490 ASPMDIAVQE 500 GRLTWLVYII 510 GAVIGGRVSF 520 ASTDEQDAMD 530 GELVCRVLQL 540 MNLTDSRLAQ 550 AGNEKLELAM 560 LSFFEQFRKI 570 YIGDQVQKSS 580 KLYRRLSEVL 590 GLNDETMVLS 600 VFIGKIITNL 610 KYWGRCEPIT 620 SKTLQLLNDL 630 SIGYSSVRKL 640 VKLSAVQFML 650 NNHTSEHFSF 660 LGINNQSNLT 670 DMRCRTTFYT 680 ALGRLLMVDL 690 GEDEDQYEQF 700 MLPLTAAFEA 710 VAQMFSTNSF 720 NEQEAKRTLV 730 GLVRDLRGIA 740 FAFNAKTSFM 750 MLFEWIYPSY 760 MPILQRAIEL 770 WYHDPACTTP 780 VLKLMAELVH 790 NRSQRLQFDV 800 SSPNGILLFR 810 ETSKMITMYG 820 NRILTLGEVP 830 KDQVYALKLK 840 GISICFSMLK 850 AALSGSYVNF 860 GVFRLYGDDA 870 LDNALQTFIK 880 LLLSIPHSDL 890 LDYPKLSQSY 900 YSLLEVLTQD 910 HMNFIASLEP 920 HVIMYILSSI 930 SEGLTALDTM 940 VCTGCCSCLD 950 HIVTYLFKQL 960 SRSTKKRTTP 970 LNQESDRFLH 980 IMQQHPEMIQ 990 QMLSTVLNII 1000 IFEDCRNQWS 1010 MSRPLLGLIL 1020 LNEKYFSDLR 1030 NSIVNSQPPE 1040 KQQAMHLCFE 1050 NLMEGIERNL 1060 LTKNRDRFTQ 1070 NLSAFRREVN 1080 DSMKNSTYGV NSNDMMS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005643 nuclear pore
Cellular Component GO:0005634 nucleus
Molecular Function GO:0005049 nuclear export signal receptor activity
Molecular Function GO:0031267 small GTPase binding
Biological Process GO:0006611 protein export from nucleus

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.