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Overview

Uniprot IDP52294
Protein NameImportin subunit alpha-5
Gene NameKPNA1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
17 RLKSYKNKSLNPDEM
46 KREEQLFKRRNVATA

Function

Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1 (PubMed:27713473, PubMed:7892216, PubMed:8692858). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (PubMed:27713473, PubMed:7892216, PubMed:8692858). 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:27713473, PubMed:7892216). 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 (PubMed:7892216). 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 (PubMed:7892216). Mediator of PR-DUB complex component BAP1 nuclear import; acts redundantly with KPNA2 and Transportin-1/TNPO1 (PubMed:35446349)

Protein Sequence

10 MTTPGKENFR 20 LKSYKNKSLN 30 PDEMRRRREE 40 EGLQLRKQKR 50 EEQLFKRRNV 60 ATAEEETEEE 70 VMSDGGFHEA 80 QISNMEMAPG 90 GVITSDMIEM 100 IFSKSPEQQL 110 SATQKFRKLL 120 SKEPNPPIDE 130 VISTPGVVAR 140 FVEFLKRKEN 150 CTLQFESAWV 160 LTNIASGNSL 170 QTRIVIQAGA 180 VPIFIELLSS 190 EFEDVQEQAV 200 WALGNIAGDS 210 TMCRDYVLDC 220 NILPPLLQLF 230 SKQNRLTMTR 240 NAVWALSNLC 250 RGKSPPPEFA 260 KVSPCLNVLS 270 WLLFVSDTDV 280 LADACWALSY 290 LSDGPNDKIQ 300 AVIDAGVCRR 310 LVELLMHNDY 320 KVVSPALRAV 330 GNIVTGDDIQ 340 TQVILNCSAL 350 QSLLHLLSSP 360 KESIKKEACW 370 TISNITAGNR 380 AQIQTVIDAN 390 IFPALISILQ 400 TAEFRTRKEA 410 AWAITNATSG 420 GSAEQIKYLV 430 ELGCIKPLCD 440 LLTVMDSKIV 450 QVALNGLENI 460 LRLGEQEAKR 470 NGTGINPYCA 480 LIEEAYGLDK 490 IEFLQSHENQ 500 EIYQKAFDLI 510 EHYFGTEDED 520 SSIAPQVDLN 530 QQQYIFQQCE APMEGFQL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0030425 dendrite
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0042564 NLS-dependent protein nuclear import complex
Cellular Component GO:0005643 nuclear pore
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0014069 postsynaptic density
Molecular Function GO:0061608 nuclear import signal receptor activity
Molecular Function GO:0008139 nuclear localization sequence binding
Biological Process GO:0006607 NLS-bearing protein import into nucleus
Biological Process GO:0099527 postsynapse to nucleus signaling pathway
Biological Process GO:0000018 regulation of DNA recombination

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 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.

[4] 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.