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Overview

Uniprot IDO95373
Protein NameImportin-7
Gene NameIPO7
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1013 HESKMIEKHGGYKFS
314 VLYQYKEKQYMAPRV

Function

Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. 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. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 (PubMed:11682607). In association with KPNB1 mediates the nuclear import of H1 histone and the Ran-binding site of IPO7 is not required but synergizes with that of KPNB1 in importin/substrate complex dissociation. Promotes odontoblast differentiation via promoting nuclear translocation of DLX3, KLF4, SMAD2, thereby facilitating the transcription of target genes that play a role in odontoblast differentiation (By similarity). Facilitates BMP4-induced translocation of SMAD1 to the nucleus and recruitment to the MSX1 gene promoter, thereby promotes the expression of the odontogenic regulator MSX1 in dental mesenchymal cells (By similarity). Also promotes odontoblast differentiation by facilitating the nuclear translocation of HDAC6 and subsequent repression of RUNX2 expression (By similarity). Inhibits osteoblast differentiation by inhibiting nuclear translocation of RUNX2 and therefore inhibition of RUNX2 target gene transcription (By similarity). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones

Protein Sequence

10 MDPNTIIEAL 20 RGTMDPALRE 30 AAERQLNEAH 40 KSLNFVSTLL 50 QITMSEQLDL 60 PVRQAGVIYL 70 KNMITQYWPD 80 RETAPGDISP 90 YTIPEEDRHC 100 IRENIVEAII 110 HSPELIRVQL 120 TTCIHHIIKH 130 DYPSRWTAIV 140 DKIGFYLQSD 150 NSACWLGILL 160 CLYQLVKNYE 170 YKKPEERSPL 180 VAAMQHFLPV 190 LKDRFIQLLS 200 DQSDQSVLIQ 210 KQIFKIFYAL 220 VQYTLPLELI 230 NQQNLTEWIE 240 ILKTVVNRDV 250 PNETLQVEED 260 DRPELPWWKC 270 KKWALHILAR 280 LFERYGSPGN 290 VSKEYNEFAE 300 VFLKAFAVGV 310 QQVLLKVLYQ 320 YKEKQYMAPR 330 VLQQTLNYIN 340 QGVSHALTWK 350 NLKPHIQGII 360 QDVIFPLMCY 370 TDADEELWQE 380 DPYEYIRMKF 390 DVFEDFISPT 400 TAAQTLLFTA 410 CSKRKEVLQK 420 TMGFCYQILT 430 EPNADPRKKD 440 GALHMIGSLA 450 EILLKKKIYK 460 DQMEYMLQNH 470 VFPLFSSELG 480 YMRARACWVL 490 HYFCEVKFKS 500 DQNLQTALEL 510 TRRCLIDDRE 520 MPVKVEAAIA 530 LQVLISNQEK 540 AKEYITPFIR 550 PVMQALLHII 560 RETENDDLTN 570 VIQKMICEYS 580 EEVTPIAVEM 590 TQHLAMTFNQ 600 VIQTGPDEEG 610 SDDKAVTAMG 620 ILNTIDTLLS 630 VVEDHKEITQ 640 QLEGICLQVI 650 GTVLQQHVLE 660 FYEEIFSLAH 670 SLTCQQVSPQ 680 MWQLLPLVFE 690 VFQQDGFDYF 700 TDMMPLLHNY 710 VTVDTDTLLS 720 DTKYLEMIYS 730 MCKKVLTGVA 740 GEDAECHAAK 750 LLEVIILQCK 760 GRGIDQCIPL 770 FVEAALERLT 780 REVKTSELRT 790 MCLQVAIAAL 800 YYNPHLLLNT 810 LENLRFPNNV 820 EPVTNHFITQ 830 WLNDVDCFLG 840 LHDRKMCVLG 850 LCALIDMEQI 860 PQVLNQVSGQ 870 ILPAFILLFN 880 GLKRAYACHA 890 EHENDSDDDD 900 EAEDDDETEE 910 LGSDEDDIDE 920 DGQEYLEILA 930 KQAGEDGDDE 940 DWEEDDAEET 950 ALEGYSTIID 960 DEDNPVDEYQ 970 IFKAIFQTIQ 980 NRNPVWYQAL 990 THGLNEEQRK 1000 QLQDIATLAD 1010 QRRAAHESKM 1020 IEKHGGYKFS 1030 APVVPSSFNF GGPAPGMN

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016020 membrane
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0005643 nuclear pore
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0030695 GTPase regulator activity
Molecular Function GO:0042393 histone binding
Molecular Function GO:0061608 nuclear import signal receptor activity
Molecular Function GO:0046332 SMAD binding
Molecular Function GO:0031267 small GTPase binding
Biological Process GO:0045786 negative regulation of cell cycle
Biological Process GO:0045668 negative regulation of osteoblast differentiation
Biological Process GO:1901331 positive regulation of odontoblast differentiation
Biological Process GO:1900182 positive regulation of protein localization to nucleus
Biological Process GO:0006606 protein import into nucleus

Reference

[1] 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.

[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.