ID IMB1_HUMAN Reviewed; 876 AA. AC Q14974; Q14637; Q96J27; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2002, sequence version 2. DT 20-MAR-2007, entry version 75. DE Importin beta-1 subunit (Karyopherin beta-1 subunit) (Nuclear factor DE P97) (Importin 90). GN Name=KPNB1; Synonyms=NTF97; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RC TISSUE=Brain; RX MEDLINE=95340629; PubMed=7615630; DOI=10.1083/jcb.130.2.265; RA Chi N.C., Adam E.J.H., Adam S.A.; RT "Sequence and characterization of cytoplasmic nuclear protein import RT factor p97."; RL J. Cell Biol. 130:265-274(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=95353691; PubMed=7627554; DOI=10.1016/S0960-9822(95)00079-0; RA Goerlich D., Kostka S., Kraft R., Dingwall C., Laskey R.A., RA Hartmann E., Prehn S.; RT "Two different subunits of importin cooperate to recognize nuclear RT localization signals and bind them to the nuclear envelope."; RL Curr. Biol. 5:383-392(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PARTIAL PROTEIN SEQUENCE, AND INTERACTION WITH AN IMPORTIN ALPHA RP SUBUNIT. RX MEDLINE=96203102; PubMed=8617227; RA Weis K., Ryder U., Lamond A.I.; RT "The conserved amino-terminal domain of hSRP1 alpha is essential for RT nuclear protein import."; RL EMBO J. 15:1818-1825(1996). RN [5] RP PROTEIN SEQUENCE OF 1-9; 55-62 AND 192-206, ACETYLATION AT MET-1, AND RP MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Unpublished observations (MAY-2005). RN [6] RP RAN-GTP AND ALPHA SUBUNIT BINDING SITES. RX MEDLINE=96293475; PubMed=8692944; DOI=10.1073/pnas.93.14.7059; RA Moroianu J., Blobel G., Radu A.; RT "Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta RT heterodimer by displacing alpha from an overlapping binding site on RT beta."; RL Proc. Natl. Acad. Sci. U.S.A. 93:7059-7062(1996). RN [7] RP INTERACTION WITH HIV-1 REV AND TAT. RX PubMed=9405152; DOI=10.1006/jmbi.1997.1420; RA Henderson B.R., Percipalle P.; RT "Interactions between HIV Rev and nuclear import and export factors: RT the Rev nuclear localisation signal mediates specific binding to human RT importin-beta."; RL J. Mol. Biol. 274:693-707(1997). RN [8] RP INTERACTION WITH SNUPN. RX MEDLINE=98336200; PubMed=9670026; DOI=10.1093/emboj/17.14.4114; RA Huber J., Cronshagen U., Kadokura M., Marshallsay C., Wada T., RA Sekine M., Luehrmann R.; RT "Snurportin1, an m3G-cap-specific nuclear import receptor with a novel RT domain structure."; RL EMBO J. 17:4114-4126(1998). RN [9] RP FUNCTION, AND INTERACTION WITH RPL23A; RPS7; RPL5 AND IPO7. RX MEDLINE=98353472; PubMed=9687515; DOI=10.1093/emboj/17.15.4491; RA Jaekel S., Goerlich D.; RT "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import RT of ribosomal proteins in mammalian cells."; RL EMBO J. 17:4491-4502(1998). RN [10] RP FUNCTION, AND INTERACTION WITH H1 HISTONE AND IPO7. RX MEDLINE=99246267; PubMed=10228156; DOI=10.1093/emboj/18.9.2411; RA Jaekel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K., RA Doenecke D., Goerlich D.; RT "The importin beta/importin 7 heterodimer is a functional nuclear RT import receptor for histone H1."; RL EMBO J. 18:2411-2423(1999). RN [11] RP IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, AND INTERACTION WITH RP IPO7; SNUPN AND XPO1. RX MEDLINE=99225511; PubMed=10209022; DOI=10.1083/jcb.145.2.255; RA Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U., RA Hartmann E., Luehrmann R., Goerlich D.; RT "CRM1-mediated recycling of snurportin 1 to the cytoplasm."; RL J. Cell Biol. 145:255-264(1999). RN [12] RP INTERACTION WITH HIV-1 REV. RX PubMed=9891055; RA Truant R., Cullen B.R.; RT "The arginine-rich domains present in human immunodeficiency virus RT type 1 Tat and Rev function as direct importin beta-dependent nuclear RT localization signals."; RL Mol. Cell. Biol. 19:1210-1217(1999). RN [13] RP INTERACTION WITH HTLV-1 REX. RX PubMed=9891056; RA Palmeri D., Malim M.H.; RT "Importin beta can mediate the nuclear import of an arginine-rich RT nuclear localization signal in the absence of importin alpha."; RL Mol. Cell. Biol. 19:1218-1225(1999). RN [14] RP IDENTIFICATION IN AN IMPORT SNRNP COMPLEX. RX MEDLINE=22090571; PubMed=12095920; DOI=10.1093/hmg/11.15.1785; RA Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.; RT "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP RT complex with snurportin1 and importin beta."; RL Hum. Mol. Genet. 11:1785-1795(2002). RN [15] RP INTERACTION WITH SRY. RX PubMed=12764225; DOI=10.1073/pnas.1137864100; RA Harley V.R., Layfield S., Mitchell C.L., Forwood J.K., John A.P., RA Briggs L.J., McDowall S.G., Jans D.A.; RT "Defective importin beta recognition and nuclear import of the sex- RT determining factor SRY are associated with XY sex-reversing RT mutations."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7045-7050(2003). RN [16] RP INTERACTION WITH SRY. RX PubMed=15297880; DOI=10.1038/sj.emboj.7600352; RA Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N., RA Aldrian-Herrada G., Poulat F., Berta P., Benkirane M., RA Boizet-Bonhoure B.; RT "Regulation of human SRY subcellular distribution by its RT acetylation/deacetylation."; RL EMBO J. 23:3336-3345(2004). RN [17] RP INTERACTION WITH HIV-1 REV. RX PubMed=16704975; DOI=10.1074/jbc.M602189200; RA Arnold M., Nath A., Hauber J., Kehlenbach R.H.; RT "Multiple importins function as nuclear transport receptors for the RT Rev protein of human immunodeficiency virus type 1."; RL J. Biol. Chem. 281:20883-20890(2006). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-459. RX PubMed=10367892; DOI=10.1016/S0092-8674(00)80774-6; RA Vetter I.R., Arndt A., Kutay U., Goerlich D., Wittinghofer A.; RT "Structural view of the Ran-Importin beta interaction at 2.3 A RT resolution."; RL Cell 97:635-646(1999). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 3-442, AND MUTAGENESIS OF RP ILE-178. RX PubMed=10929717; DOI=10.1016/S0092-8674(00)00014-3; RA Bayliss R., Littlewood T., Stewart M.; RT "Structural basis for the interaction between FxFG nucleoporin repeats RT and importin-beta in nuclear trafficking."; RL Cell 102:99-108(2000). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-485. RX MEDLINE=22394015; PubMed=12504010; DOI=10.1016/S1097-2765(02)00727-X; RA Cingolani G., Bednenko J., Gillespie M.T., Gerace L.; RT "Molecular basis for the recognition of a nonclassical nuclear RT localization signal by importin beta."; RL Mol. Cell 10:1345-1353(2002). CC -!- FUNCTION: Functions in nuclear protein import, either in CC association with an adapter protein, like an importin-alpha CC subunit, which binds to nuclear localization signals (NLS) in CC cargo substrates, or by acting as autonomous nuclear transport CC receptor. Acting autonomously, serves itself as NLS receptor. CC Docking of the importin/substrate complex to the nuclear pore CC complex (NPC) is mediated by KPNB1 through binding to nucleoporin CC FxFG repeats and the complex is subsequently translocated through CC the pore by an energy requiring, Ran-dependent mechanism. At the CC nucleoplasmic side of the NPC, Ran binds to importin-beta and the CC three components separate and importin-alpha and -beta are re- CC exported from the nucleus to the cytoplasm where GTP hydrolysis CC releases Ran from importin. The directionality of nuclear import CC is thought to be conferred by an asymmetric distribution of the CC GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. CC Mediates autonomously the nuclear import of ribosomal proteins CC RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor CC binding (BIB) domain of RPL23A. In association with IPO7 mediates CC the nuclear import of H1 histone. In vitro, mediates nuclear CC import of H2A, H2B, H3 and H4 histones. In case of HIV-1 CC infection, binds and mediates the nuclear import of HIV-1 Rev. CC -!- SUBUNIT: Forms a complex with an importin alpha subunit. Forms an CC heterodimer with IPO7. Interacts with IPO7, SNUPN, RPL23A and CC XPO1. The KPNB1/IPO7 heterodimer interacts with H1 histone. CC Interacts with H2A, H2B, H3 and H4 histones (By similarity). CC Component of an import snRNP complex composed of KPNB1, SNUPN, CC SMN1 and ZNF259. Component of a nuclear export receptor complex CC composed of KPNB1, Ran, SNUPN and XPO1. Binds to HIV-1 Rev and CC Tat. Interacts with HTLV-1 Rex. Interacts with SRY. CC -!- INTERACTION: CC Q16637-3:SMN1; NbExp=2; IntAct=EBI-286758, EBI-395447; CC O75940:SMNDC1; NbExp=1; IntAct=EBI-286758, EBI-464921; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus; nuclear envelope. CC -!- SIMILARITY: Belongs to the importin beta family. CC -!- SIMILARITY: Contains 8 HEAT repeats. CC -!- SIMILARITY: Contains 1 importin N-terminal domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L39793; AAA82869.1; -; Genomic_DNA. DR EMBL; L38951; AAC41763.1; -; mRNA. DR EMBL; BC003572; AAH03572.1; -; mRNA. DR EMBL; BC024045; AAH24045.1; -; mRNA. DR EMBL; BC036703; AAH36703.1; -; mRNA. DR PIR; I52907; I52907. DR UniGene; Hs.532793; -. DR UniGene; Hs.649829; -. DR PDB; 1F59; X-ray; A/B=1-442. DR PDB; 1IBR; X-ray; B/D=1-462. DR PDB; 1M5N; X-ray; S=1-485. DR PDB; 1O6O; X-ray; A/B/C=1-442. DR PDB; 1O6P; X-ray; A/B=1-442. DR PDB; 1QGK; X-ray; A=1-876. DR PDB; 1QGR; X-ray; A=1-876. DR DIP; DIP:6204N; -. DR IntAct; Q14974; -. DR Ensembl; ENSG00000108424; Homo sapiens. DR KEGG; hsa:3837; -. DR H-InvDB; HIX0013923; -. DR HGNC; HGNC:6400; KPNB1. DR MIM; 602738; gene. DR Reactome; REACT_6167.2; Influenza Infection. DR LinkHub; Q14974; -. DR ArrayExpress; Q14974; -. DR GermOnline; ENSG00000108424; Homo sapiens. DR RZPD-ProtExp; I0321; -. DR RZPD-ProtExp; IOH4406; -. DR RZPD-ProtExp; RZPDo839H1165; -. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc. DR GO; GO:0008139; F:nuclear localization sequence binding; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc. DR GO; GO:0006607; P:NLS-bearing substrate import into nucleus; TAS:ProtInc. DR GO; GO:0000060; P:protein import into nucleus, translocation; TAS:ProtInc. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR000357; HEAT. DR InterPro; IPR001494; Importinb_N. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF00514; Arm; 1. DR Pfam; PF02985; HEAT; 2. DR Pfam; PF03810; IBN_N; 1. DR PROSITE; PS50077; HEAT_REPEAT; 1. DR PROSITE; PS50166; IMPORTIN_B_NT; 1. KW 3D-structure; Acetylation; Direct protein sequencing; KW Host-virus interaction; Nuclear protein; Protein transport; Repeat; KW Transport. FT CHAIN 1 876 Importin beta-1 subunit. FT /FTId=PRO_0000120745. FT DOMAIN 21 101 Importin N-terminal. FT REPEAT 124 163 HEAT 1. FT REPEAT 168 207 HEAT 2. FT REPEAT 213 250 HEAT 3. FT REPEAT 317 357 HEAT 4. FT REPEAT 362 399 HEAT 5. FT REPEAT 404 441 HEAT 6. FT REPEAT 602 641 HEAT 7. FT REPEAT 687 726 HEAT 8. FT REGION 329 342 IAB-binding. FT REGION 334 419 Ran-GTP binding. FT COMPBIAS 337 341 Poly-Asp. FT MOD_RES 1 1 N-acetylmethionine. FT MUTAGEN 178 178 I->A: Largely reduced binding to FxFG FT repeats and reduced nuclear import. FT MUTAGEN 178 178 I->F,D: Loss of binding to FxFG repeats FT and reduced nuclear import. FT CONFLICT 97 97 Q -> H (in Ref. 1). FT CONFLICT 200 200 N -> NA (in Ref. 4). FT CONFLICT 863 863 T -> R (in Ref. 1). FT HELIX 3 9 FT HELIX 15 45 FT HELIX 51 65 FT HELIX 70 81 FT HELIX 85 98 FT STRAND 104 106 FT HELIX 109 120 FT HELIX 121 123 FT HELIX 129 138 FT HELIX 144 160 FT HELIX 163 165 FT HELIX 167 169 FT HELIX 170 181 FT HELIX 188 201 FT TURN 202 205 FT HELIX 206 209 FT HELIX 212 225 FT HELIX 231 247 FT HELIX 249 251 FT TURN 253 259 FT HELIX 260 269 FT HELIX 273 297 FT STRAND 303 305 FT HELIX 314 329 FT HELIX 344 358 FT TURN 359 362 FT HELIX 363 374 FT HELIX 380 392 FT STRAND 394 397 FT TURN 399 402 FT TURN 404 408 FT HELIX 409 415 FT HELIX 416 418 FT HELIX 422 438 FT HELIX 439 442 FT TURN 446 448 FT HELIX 449 457 FT HELIX 464 483 FT TURN 500 502 FT HELIX 503 513 FT HELIX 524 537 FT HELIX 544 562 FT TURN 563 566 FT HELIX 573 592 FT HELIX 597 601 FT HELIX 604 614 FT HELIX 623 639 FT HELIX 640 646 FT HELIX 647 660 FT HELIX 664 681 FT HELIX 682 685 FT HELIX 686 700 FT HELIX 707 709 FT HELIX 710 724 FT HELIX 725 731 FT HELIX 732 743 FT HELIX 752 777 FT STRAND 779 782 FT HELIX 785 789 FT HELIX 791 793 FT HELIX 794 805 FT HELIX 812 829 FT HELIX 832 838 FT HELIX 841 852 FT HELIX 856 873 SQ SEQUENCE 876 AA; 97170 MW; F3BB8B73E7E51639 CRC64; MELITILEKT VSPDRLELEA AQKFLERAAV ENLPTFLVEL SRVLANPGNS QVARVAAGLQ IKNSLTSKDP DIKAQYQQRW LAIDANARRE VKNYVLQTLG TETYRPSSAS QCVAGIACAE IPVNQWPELI PQLVANVTNP NSTEHMKEST LEAIGYICQD IDPEQLQDKS NEILTAIIQG MRKEEPSNNV KLAATNALLN SLEFTKANFD KESERHFIMQ VVCEATQCPD TRVRVAALQN LVKIMSLYYQ YMETYMGPAL FAITIEAMKS DIDEVALQGI EFWSNVCDEE MDLAIEASEA AEQGRPPEHT SKFYAKGALQ YLVPILTQTL TKQDENDDDD DWNPCKAAGV CLMLLATCCE DDIVPHVLPF IKEHIKNPDW RYRDAAVMAF GCILEGPEPS QLKPLVIQAM PTLIELMKDP SVVVRDTAAW TVGRICELLP EAAINDVYLA PLLQCLIEGL SAEPRVASNV CWAFSSLAEA AYEAADVADD QEEPATYCLS SSFELIVQKL LETTDRPDGH QNNLRSSAYE SLMEIVKNSA KDCYPAVQKT TLVIMERLQQ VLQMESHIQS TSDRIQFNDL QSLLCATLQN VLRKVQHQDA LQISDVVMAS LLRMFQSTAG SGGVQEDALM AVSTLVEVLG GEFLKYMEAF KPFLGIGLKN YAEYQVCLAA VGLVGDLCRA LQSNIIPFCD EVMQLLLENL GNENVHRSVK PQILSVFGDI ALAIGGEFKK YLEVVLNTLQ QASQAQVDKS DYDMVDYLNE LRESCLEAYT GIVQGLKGDQ ENVHPDVMLV QPRVEFILSF IDHIAGDEDH TDGVVACAAG LIGDLCTAFG KDVLKLVEAR PMIHELLTEG RRSKTNKAKT LATWATKELR KLKNQA //