Search Results

Overview

Uniprot IDQ14974
Protein NameImportin subunit beta-1
Gene NameKPNB1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
183 AIIQGMRKEEPSNNV
68 IKNSLTSKDPDIKAQ
73 TSKDPDIKAQYQQRW
835 AFGKDVLKLVEARPM
867 TLATWATKELRKLKN

Function

Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor (PubMed:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649, PubMed:7615630, PubMed:9687515). Acting autonomously, serves itself as NLS receptor (PubMed:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649, PubMed:7615630, PubMed:9687515). 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:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649, PubMed:7615630, PubMed:9687515). 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:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649, PubMed:7615630, PubMed:9687515). 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:10228156, PubMed:11682607, PubMed:11891849, PubMed:19386897, PubMed:24699649, PubMed:7615630, PubMed:9687515). Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 (PubMed:11682607, PubMed:9687515). In association with IPO7, mediates the nuclear import of H1 histone (PubMed:10228156). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones (By similarity). Imports MRTFA, SNAI1 and PRKCI into the nucleus (PubMed:11891849, PubMed:19386897, PubMed:20818336, PubMed:24699649)

Protein Sequence

10 MELITILEKT 20 VSPDRLELEA 30 AQKFLERAAV 40 ENLPTFLVEL 50 SRVLANPGNS 60 QVARVAAGLQ 70 IKNSLTSKDP 80 DIKAQYQQRW 90 LAIDANARRE 100 VKNYVLQTLG 110 TETYRPSSAS 120 QCVAGIACAE 130 IPVNQWPELI 140 PQLVANVTNP 150 NSTEHMKEST 160 LEAIGYICQD 170 IDPEQLQDKS 180 NEILTAIIQG 190 MRKEEPSNNV 200 KLAATNALLN 210 SLEFTKANFD 220 KESERHFIMQ 230 VVCEATQCPD 240 TRVRVAALQN 250 LVKIMSLYYQ 260 YMETYMGPAL 270 FAITIEAMKS 280 DIDEVALQGI 290 EFWSNVCDEE 300 MDLAIEASEA 310 AEQGRPPEHT 320 SKFYAKGALQ 330 YLVPILTQTL 340 TKQDENDDDD 350 DWNPCKAAGV 360 CLMLLATCCE 370 DDIVPHVLPF 380 IKEHIKNPDW 390 RYRDAAVMAF 400 GCILEGPEPS 410 QLKPLVIQAM 420 PTLIELMKDP 430 SVVVRDTAAW 440 TVGRICELLP 450 EAAINDVYLA 460 PLLQCLIEGL 470 SAEPRVASNV 480 CWAFSSLAEA 490 AYEAADVADD 500 QEEPATYCLS 510 SSFELIVQKL 520 LETTDRPDGH 530 QNNLRSSAYE 540 SLMEIVKNSA 550 KDCYPAVQKT 560 TLVIMERLQQ 570 VLQMESHIQS 580 TSDRIQFNDL 590 QSLLCATLQN 600 VLRKVQHQDA 610 LQISDVVMAS 620 LLRMFQSTAG 630 SGGVQEDALM 640 AVSTLVEVLG 650 GEFLKYMEAF 660 KPFLGIGLKN 670 YAEYQVCLAA 680 VGLVGDLCRA 690 LQSNIIPFCD 700 EVMQLLLENL 710 GNENVHRSVK 720 PQILSVFGDI 730 ALAIGGEFKK 740 YLEVVLNTLQ 750 QASQAQVDKS 760 DYDMVDYLNE 770 LRESCLEAYT 780 GIVQGLKGDQ 790 ENVHPDVMLV 800 QPRVEFILSF 810 IDHIAGDEDH 820 TDGVVACAAG 830 LIGDLCTAFG 840 KDVLKLVEAR 850 PMIHELLTEG 860 RRSKTNKAKT 870 LATWATKELR KLKNQA

Gene Ontology

Classification GO ID Description
Biological Process GO:0006404 RNA import into nucleus
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0010494 cytoplasmic stress granule
Cellular Component GO:0005829 cytosol
Cellular Component GO:0071782 endoplasmic reticulum tubular network
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0016020 membrane
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0031965 nuclear membrane
Cellular Component GO:0005643 nuclear pore
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0035580 specific granule lumen
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0051879 Hsp90 protein binding
Molecular Function GO:0061676 importin-alpha family protein binding
Molecular Function GO:0061608 nuclear import signal receptor activity
Molecular Function GO:0008139 nuclear localization sequence binding
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0031267 small GTPase binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0030953 astral microtubule organization
Biological Process GO:0040001 establishment of mitotic spindle localization
Biological Process GO:0007079 mitotic chromosome movement towards spindle pole
Biological Process GO:0007080 mitotic metaphase chromosome alignment
Biological Process GO:0090307 mitotic spindle assembly
Biological Process GO:0006607 NLS-bearing protein import into nucleus
Biological Process GO:0045542 positive regulation of cholesterol biosynthetic process
Biological Process GO:0006606 protein import into nucleus
Biological Process GO:0045540 regulation of cholesterol biosynthetic process
Biological Process GO:0006610 ribosomal protein import into nucleus

Reference

[1] 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.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[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.