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Overview

Uniprot IDQ9HAV4
Protein NameExportin-5
Gene NameXPO5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1140 LLNPSLQKVADKRRK
1144 SLQKVADKRRKDQFK
1180 KNLPSLFKKTKPMLE
1181 NLPSLFKKTKPMLET

Function

Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. 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, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to 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. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi). Mediates nuclear export of isoform 5 of ADAR/ADAR1 in a RanGTP-dependent manner

Protein Sequence

10 MAMDQVNALC 20 EQLVKAVTVM 30 MDPNSTQRYR 40 LEALKFCEEF 50 KEKCPICVPC 60 GLRLAEKTQV 70 AIVRHFGLQI 80 LEHVVKFRWN 90 GMSRLEKVYL 100 KNSVMELIAN 110 GTLNILEEEN 120 HIKDALSRIV 130 VEMIKREWPQ 140 HWPDMLIELD 150 TLSKQGETQT 160 ELVMFILLRL 170 AEDVVTFQTL 180 PPQRRRDIQQ 190 TLTQNMERIF 200 SFLLNTLQEN 210 VNKYQQVKTD 220 TSQESKAQAN 230 CRVGVAALNT 240 LAGYIDWVSM 250 SHITAENCKL 260 LEILCLLLNE 270 QELQLGAAEC 280 LLIAVSRKGK 290 LEDRKPLMVL 300 FGDVAMHYIL 310 SAAQTADGGG 320 LVEKHYVFLK 330 RLCQVLCALG 340 NQLCALLGAD 350 SDVETPSNFG 360 KYLESFLAFT 370 THPSQFLRSS 380 TQMTWGALFR 390 HEILSRDPLL 400 LAIIPKYLRA 410 SMTNLVKMGF 420 PSKTDSPSCE 430 YSRFDFDSDE 440 DFNAFFNSSR 450 AQQGEVMRLA 460 CRLDPKTSFQ 470 MAGEWLKYQL 480 STFLDAGSVN 490 SCSAVGTGEG 500 SLCSVFSPSF 510 VQWEAMTLFL 520 ESVITQMFRT 530 LNREEIPVND 540 GIELLQMVLN 550 FDTKDPLILS 560 CVLTNVSALF 570 PFVTYRPEFL 580 PQVFSKLFSS 590 VTFETVEESK 600 APRTRAVRNV 610 RRHACSSIIK 620 MCRDYPQLVL 630 PNFDMLYNHV 640 KQLLSNELLL 650 TQMEKCALME 660 ALVLISNQFK 670 NYERQKVFLE 680 ELMAPVASIW 690 LSQDMHRVLS 700 DVDAFIAYVG 710 TDQKSCDPGL 720 EDPCGLNRAR 730 MSFCVYSILG 740 VVKRTCWPTD 750 LEEAKAGGFV 760 VGYTSSGNPI 770 FRNPCTEQIL 780 KLLDNLLALI 790 RTHNTLYAPE 800 MLAKMAEPFT 810 KALDMLDAEK 820 SAILGLPQPL 830 LELNDSPVFK 840 TVLERMQRFF 850 STLYENCFHI 860 LGKAGPSMQQ 870 DFYTVEDLAT 880 QLLSSAFVNL 890 NNIPDYRLRP 900 MLRVFVKPLV 910 LFCPPEHYEA 920 LVSPILGPLF 930 TYLHMRLSQK 940 WQVINQRSLL 950 CGEDEAADEN 960 PESQEMLEEQ 970 LVRMLTREVM 980 DLITVCCVSK 990 KGADHSSAPP 1000 ADGDDEEMMA 1010 TEVTPSAMAE 1020 LTDLGKCLMK 1030 HEDVCTALLI 1040 TAFNSLAWKD 1050 TLSCQRTTSQ 1060 LCWPLLKQVL 1070 SGTLLADAVT 1080 WLFTSVLKGL 1090 QMHGQHDGCM 1100 ASLVHLAFQI 1110 YEALRPRYLE 1120 IRAVMEQIPE 1130 IQKDSLDQFD 1140 CKLLNPSLQK 1150 VADKRRKDQF 1160 KRLIAGCIGK 1170 PLGEQFRKEV 1180 HIKNLPSLFK 1190 KTKPMLETEV 1200 LDNDGGGLAT IFEP

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0016442 RISC complex
Cellular Component GO:0042565 RNA nuclear export complex
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0005049 nuclear export signal receptor activity
Molecular Function GO:0070883 pre-miRNA binding
Molecular Function GO:1905172 RISC complex binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0031267 small GTPase binding
Molecular Function GO:0000049 tRNA binding
Biological Process GO:0010586 miRNA metabolic process
Biological Process GO:0035281 pre-miRNA export from nucleus
Biological Process GO:0006611 protein export from nucleus
Biological Process GO:0006405 RNA export from nucleus

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] 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.

[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.