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Overview

Uniprot IDP55060
Protein NameExportin-2
Gene NameCSE1L
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
158 RTAHSLFKRYRHEFK
17 TLTEYLKKTLDPDPA
83 IVEDEPNKICEADRV
840 VSGNVEKKICAVGIT

Function

Export receptor for importin-alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus binds cooperatively to importin-alpha 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 importin-alpha from the export receptor. CSE1L/XPO2 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 MELSDANLQT 20 LTEYLKKTLD 30 PDPAIRRPAE 40 KFLESVEGNQ 50 NYPLLLLTLL 60 EKSQDNVIKV 70 CASVTFKNYI 80 KRNWRIVEDE 90 PNKICEADRV 100 AIKANIVHLM 110 LSSPEQIQKQ 120 LSDAISIIGR 130 EDFPQKWPDL 140 LTEMVNRFQS 150 GDFHVINGVL 160 RTAHSLFKRY 170 RHEFKSNELW 180 TEIKLVLDAF 190 ALPLTNLFKA 200 TIELCSTHAN 210 DASALRILFS 220 SLILISKLFY 230 SLNFQDLPEF 240 FEDNMETWMN 250 NFHTLLTLDN 260 KLLQTDDEEE 270 AGLLELLKSQ 280 ICDNAALYAQ 290 KYDEEFQRYL 300 PRFVTAIWNL 310 LVTTGQEVKY 320 DLLVSNAIQF 330 LASVCERPHY 340 KNLFEDQNTL 350 TSICEKVIVP 360 NMEFRAADEE 370 AFEDNSEEYI 380 RRDLEGSDID 390 TRRRAACDLV 400 RGLCKFFEGP 410 VTGIFSGYVN 420 SMLQEYAKNP 430 SVNWKHKDAA 440 IYLVTSLASK 450 AQTQKHGITQ 460 ANELVNLTEF 470 FVNHILPDLK 480 SANVNEFPVL 490 KADGIKYIMI 500 FRNQVPKEHL 510 LVSIPLLINH 520 LQAESIVVHT 530 YAAHALERLF 540 TMRGPNNATL 550 FTAAEIAPFV 560 EILLTNLFKA 570 LTLPGSSENE 580 YIMKAIMRSF 590 SLLQEAIIPY 600 IPTLITQLTQ 610 KLLAVSKNPS 620 KPHFNHYMFE 630 AICLSIRITC 640 KANPAAVVNF 650 EEALFLVFTE 660 ILQNDVQEFI 670 PYVFQVMSLL 680 LETHKNDIPS 690 SYMALFPHLL 700 QPVLWERTGN 710 IPALVRLLQA 720 FLERGSNTIA 730 SAAADKIPGL 740 LGVFQKLIAS 750 KANDHQGFYL 760 LNSIIEHMPP 770 ESVDQYRKQI 780 FILLFQRLQN 790 SKTTKFIKSF 800 LVFINLYCIK 810 YGALALQEIF 820 DGIQPKMFGM 830 VLEKIIIPEI 840 QKVSGNVEKK 850 ICAVGITKLL 860 TECPPMMDTE 870 YTKLWTPLLQ 880 SLIGLFELPE 890 DDTIPDEEHF 900 IDIEDTPGYQ 910 TAFSQLAFAG 920 KKEHDPVGQM 930 VNNPKIHLAQ 940 SLHKLSTACP 950 GRVPSMVSTS 960 LNAEALQYLQ 970 GYLQAASVTL L

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0005654 nucleoplasm
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] 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.

[2] 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.

[3] 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.