IMB1_HUMAN

Source: hRBCD ; ID: IPI00001639
PM19886704
PM23856902
Marked as 'Non-membrane protein'
Confidence: medium (present in either hRBCD or BSc_CH or PM22954596) Search PubMed for
(RBC AND this entry)
Gene names: KPNB1 , NTF97
Protein names and data: IMB1_HUMAN , Importin subunit beta-1 , Importin-90; Karyopherin subunit beta-1; Nuclear factor p97; Pore targeting complex 97 kDa subunit; PTAC97 Lenght: 876 a.a.
Mass: 97170 Da
fasta formatted sequence
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. Acting autonomously, serves itself as NLS receptor. 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. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with IPO7 mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Imports SNAI1 and PRKCI into the nucleus.
Cellular location: Cytoplasm. Nucleus envelope.

Database cross-references

UniProt: Q14974
Ensembl: ENST00000290158
MIM: 602738
neXtProt: NX_Q14974
Antibodypedia: Q14974 (may not find the protein thus also not any antibody)
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