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Overview

Uniprot IDO60684
Protein NameImportin subunit alpha-7
Gene NameKPNA6
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
18 NYRMKSYKNNALNPE
49 KREQQLFKRRNVELI
9 ETMASPGKDNYRMKS

Function

Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import 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 METMASPGKD 20 NYRMKSYKNN 30 ALNPEEMRRR 40 REEEGIQLRK 50 QKREQQLFKR 60 RNVELINEEA 70 AMFDSLLMDS 80 YVSSTTGESV 90 ITREMVEMLF 100 SDDSDLQLAT 110 TQKFRKLLSK 120 EPSPPIDEVI 130 NTPRVVDRFV 140 EFLKRNENCT 150 LQFEAAWALT 160 NIASGTSQQT 170 KIVIEAGAVP 180 IFIELLNSDF 190 EDVQEQAVWA 200 LGNIAGDSSV 210 CRDYVLNCSI 220 LNPLLTLLTK 230 STRLTMTRNA 240 VWALSNLCRG 250 KNPPPEFAKV 260 SPCLPVLSRL 270 LFSSDSDLLA 280 DACWALSYLS 290 DGPNEKIQAV 300 IDSGVCRRLV 310 ELLMHNDYKV 320 ASPALRAVGN 330 IVTGDDIQTQ 340 VILNCSALPC 350 LLHLLSSPKE 360 SIRKEACWTI 370 SNITAGNRAQ 380 IQAVIDANIF 390 PVLIEILQKA 400 EFRTRKEAAW 410 AITNATSGGT 420 PEQIRYLVSL 430 GCIKPLCDLL 440 TVMDSKIVQV 450 ALNGLENILR 460 LGEQEGKRSG 470 SGVNPYCGLI 480 EEAYGLDKIE 490 FLQSHENQEI 500 YQKAFDLIEH 510 YFGVEDDDSS 520 LAPQVDETQQ 530 QFIFQQPEAP MEGFQL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0043657 host cell
Cellular Component GO:0016020 membrane
Cellular Component GO:0042564 NLS-dependent protein nuclear import complex
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0061608 nuclear import signal receptor activity
Molecular Function GO:0008139 nuclear localization sequence binding
Biological Process GO:0075506 entry of viral genome into host nucleus through nuclear pore complex via importin
Biological Process GO:0006607 NLS-bearing protein import into nucleus
Biological Process GO:1903902 positive regulation of viral life cycle

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] 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.

[5] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[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.