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Overview

Uniprot ID	P52292
Protein Name	Importin subunit alpha-1
Gene Name	KPNA2
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
108	RKLLSREKQPPIDNI
22	HRFKNKGKDSTEMRR
43	VELRKAKKDDQMLKR

Function

Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1 (PubMed:28991411, PubMed:32130408, PubMed:7604027, PubMed:7754385). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (PubMed:28991411, PubMed:32130408, PubMed:7604027, PubMed:7754385). 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 (PubMed:7604027, PubMed:7754385). 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. Mediator of PR-DUB complex component BAP1 nuclear import; acts redundantly with KPNA1 and Transportin-1/TNPO1 (PubMed:35446349)

Protein Sequence

10 MSTNENANTP 20 AARLHRFKNK 30 GKDSTEMRRR 40 RIEVNVELRK 50 AKKDDQMLKR 60 RNVSSFPDDA 70 TSPLQENRNN 80 QGTVNWSVDD 90 IVKGINSSNV 100 ENQLQATQAA 110 RKLLSREKQP 120 PIDNIIRAGL 130 IPKFVSFLGR 140 TDCSPIQFES 150 AWALTNIASG 160 TSEQTKAVVD 170 GGAIPAFISL 180 LASPHAHISE 190 QAVWALGNIA 200 GDGSVFRDLV 210 IKYGAVDPLL 220 ALLAVPDMSS 230 LACGYLRNLT 240 WTLSNLCRNK 250 NPAPPIDAVE 260 QILPTLVRLL 270 HHDDPEVLAD 280 TCWAISYLTD 290 GPNERIGMVV 300 KTGVVPQLVK 310 LLGASELPIV 320 TPALRAIGNI 330 VTGTDEQTQV 340 VIDAGALAVF 350 PSLLTNPKTN 360 IQKEATWTMS 370 NITAGRQDQI 380 QQVVNHGLVP 390 FLVSVLSKAD 400 FKTQKEAVWA 410 VTNYTSGGTV 420 EQIVYLVHCG 430 IIEPLMNLLT 440 AKDTKIILVI 450 LDAISNIFQA 460 AEKLGETEKL 470 SIMIEECGGL 480 DKIEALQNHE 490 NESVYKASLS 500 LIEKYFSVEE 510 EEDQNVVPET 520 TSEGYTFQVQ DGAPGTFNF

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0005789	endoplasmic reticulum membrane
Cellular Component	GO:0000139	Golgi membrane
Cellular Component	GO:0043657	host cell
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0042564	NLS-dependent protein nuclear import complex
Cellular Component	GO:0031965	nuclear membrane
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Molecular Function	GO:0042826	histone deacetylase binding
Molecular Function	GO:0061608	nuclear import signal receptor activity
Molecular Function	GO:0008139	nuclear localization sequence binding
Molecular Function	GO:0003723	RNA binding
Biological Process	GO:0006259	DNA metabolic process
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:0032481	positive regulation of type I interferon production
Biological Process	GO:1903902	positive regulation of viral life cycle
Biological Process	GO:0006606	protein import into nucleus
Biological Process	GO:0000018	regulation of DNA recombination

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] 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.