IMB1_HUMAN
ID IMB1_HUMAN Reviewed; 876 AA.
AC Q14974; B7ZAV6; D3DTT3; Q14637; Q53XN2; Q96J27;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Importin subunit beta-1;
DE AltName: Full=Importin-90;
DE AltName: Full=Karyopherin subunit beta-1;
DE AltName: Full=Nuclear factor p97;
DE AltName: Full=Pore targeting complex 97 kDa subunit;
DE Short=PTAC97;
GN Name=KPNB1; Synonyms=NTF97;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC TISSUE=Brain;
RX 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 factor
RT p97.";
RL J. Cell Biol. 130:265-274(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7627554; DOI=10.1016/s0960-9822(95)00079-0;
RA Goerlich D., Kostka S., Kraft R., Dingwall C., Laskey R.A., Hartmann E.,
RA 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] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, AND INTERACTION WITH AN IMPORTIN ALPHA SUBUNIT.
RX PubMed=8617227; DOI=10.1002/j.1460-2075.1996.tb00531.x;
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 [9]
RP PROTEIN SEQUENCE OF 1-9; 55-62 AND 192-206, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAY-2005) to UniProtKB.
RN [10]
RP RAN-GTP AND ALPHA SUBUNIT BINDING SITES.
RX 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 beta.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7059-7062(1996).
RN [11]
RP INTERACTION WITH HIV-1 REV AND TAT (MICROBIAL INFECTION).
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: the
RT Rev nuclear localisation signal mediates specific binding to human
RT importin-beta.";
RL J. Mol. Biol. 274:693-707(1997).
RN [12]
RP INTERACTION WITH SNUPN.
RX PubMed=9670026; DOI=10.1093/emboj/17.14.4114;
RA Huber J., Cronshagen U., Kadokura M., Marshallsay C., Wada T., Sekine M.,
RA 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 [13]
RP FUNCTION, AND INTERACTION WITH RPL23A; RPS7; RPL5 AND IPO7.
RX PubMed=9687515; DOI=10.1093/emboj/17.15.4491;
RA Jaekel S., Goerlich D.;
RT "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of
RT ribosomal proteins in mammalian cells.";
RL EMBO J. 17:4491-4502(1998).
RN [14]
RP FUNCTION, AND INTERACTION WITH H1 HISTONE AND IPO7.
RX PubMed=10228156; DOI=10.1093/emboj/18.9.2411;
RA Jaekel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K., Doenecke D.,
RA Goerlich D.;
RT "The importin beta/importin 7 heterodimer is a functional nuclear import
RT receptor for histone H1.";
RL EMBO J. 18:2411-2423(1999).
RN [15]
RP IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, AND INTERACTION WITH IPO7;
RP SNUPN AND XPO1.
RX 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 [16]
RP INTERACTION WITH HIV-1 REV.
RX PubMed=9891055; DOI=10.1128/mcb.19.2.1210;
RA Truant R., Cullen B.R.;
RT "The arginine-rich domains present in human immunodeficiency virus type 1
RT Tat and Rev function as direct importin beta-dependent nuclear localization
RT signals.";
RL Mol. Cell. Biol. 19:1210-1217(1999).
RN [17]
RP INTERACTION WITH HTLV-1 REX (MICROBIAL INFECTION).
RX PubMed=9891056; DOI=10.1128/mcb.19.2.1218;
RA Palmeri D., Malim M.H.;
RT "Importin beta can mediate the nuclear import of an arginine-rich nuclear
RT localization signal in the absence of importin alpha.";
RL Mol. Cell. Biol. 19:1218-1225(1999).
RN [18]
RP FUNCTION, AND INTERACTION WITH RPL23A AND SRP19.
RX PubMed=11682607; DOI=10.1242/jcs.114.19.3479;
RA Dean K.A., von Ahsen O., Goerlich D., Fried H.M.;
RT "Signal recognition particle protein 19 is imported into the nucleus by
RT importin 8 (RanBP8) and transportin.";
RL J. Cell Sci. 114:3479-3485(2001).
RN [19]
RP INTERACTION WITH NUMA1.
RX PubMed=11229403; DOI=10.1126/science.1057661;
RA Wiese C., Wilde A., Moore M.S., Adam S.A., Merdes A., Zheng Y.;
RT "Role of importin-beta in coupling Ran to downstream targets in microtubule
RT assembly.";
RL Science 291:653-656(2001).
RN [20]
RP IDENTIFICATION IN AN IMPORT SNRNP COMPLEX.
RX 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 complex
RT with snurportin1 and importin beta.";
RL Hum. Mol. Genet. 11:1785-1795(2002).
RN [21]
RP INTERACTION WITH PRKCI, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11891849; DOI=10.1002/jcb.10101.abs;
RA White W.O., Seibenhener M.L., Wooten M.W.;
RT "Phosphorylation of tyrosine 256 facilitates nuclear import of atypical
RT protein kinase C.";
RL J. Cell. Biochem. 85:42-53(2002).
RN [22]
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 mutations.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7045-7050(2003).
RN [23]
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., Boizet-Bonhoure B.;
RT "Regulation of human SRY subcellular distribution by its
RT acetylation/deacetylation.";
RL EMBO J. 23:3336-3345(2004).
RN [24]
RP INTERACTION WITH HRSV MATRIX PROTEIN (MICROBIAL INFECTION).
RX PubMed=16171404; DOI=10.1021/bi050701e;
RA Ghildyal R., Ho A., Wagstaff K.M., Dias M.M., Barton C.L., Jans P.,
RA Bardin P.G., Jans D.A.;
RT "Nuclear import of the respiratory syncytial virus matrix protein is
RT mediated by importin beta1 independent of importin alpha.";
RL Biochemistry 44:12887-12895(2005).
RN [25]
RP INTERACTION WITH SNAI1.
RX PubMed=15836774; DOI=10.1111/j.1365-2443.2005.00850.x;
RA Yamasaki H., Sekimoto T., Ohkubo T., Douchi T., Nagata Y., Ozawa M.,
RA Yoneda Y.;
RT "Zinc finger domain of Snail functions as a nuclear localization signal for
RT importin beta-mediated nuclear import pathway.";
RL Genes Cells 10:455-464(2005).
RN [26]
RP INTERACTION WITH HRSV PROTEIN M2-1 (MICROBIAL INFECTION).
RX PubMed=15629770; DOI=10.1016/j.virol.2004.10.031;
RA Reimers K., Buchholz K., Werchau H.;
RT "Respiratory syncytial virus M2-1 protein induces the activation of nuclear
RT factor kappa B.";
RL Virology 331:260-268(2005).
RN [27]
RP INTERACTION WITH HIV-1 REV (MICROBIAL INFECTION).
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 Rev
RT protein of human immunodeficiency virus type 1.";
RL J. Biol. Chem. 281:20883-20890(2006).
RN [28]
RP INTERACTION WITH ZBED1.
RX PubMed=17209048; DOI=10.1074/jbc.m607180200;
RA Yamashita D., Komori H., Higuchi Y., Yamaguchi T., Osumi T., Hirose F.;
RT "Human DNA replication-related element binding factor (hDREF) self-
RT association via hATC domain is necessary for its nuclear accumulation and
RT DNA binding.";
RL J. Biol. Chem. 282:7563-7575(2007).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [32]
RP FUNCTION, AND INTERACTION WITH SNAI1 AND SNAI2.
RX PubMed=19386897; DOI=10.1242/jcs.041749;
RA Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.;
RT "Characterization of Snail nuclear import pathways as representatives of
RT C2H2 zinc finger transcription factors.";
RL J. Cell Sci. 122:1452-1460(2009).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211; LYS-835 AND LYS-867, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [34]
RP INTERACTION WITH KPNA7.
RX PubMed=20701745; DOI=10.1186/1471-2121-11-63;
RA Kelley J.B., Talley A.M., Spencer A., Gioeli D., Paschal B.M.;
RT "Karyopherin alpha7 (KPNA7), a divergent member of the importin alpha
RT family of nuclear import receptors.";
RL BMC Cell Biol. 11:63-63(2010).
RN [35]
RP IDENTIFICATION IN COMPLEX WITH CRM1 AND VENEZUELAN EQUINE ENCEPHALITIS
RP VIRUS CAPSID PROTEIN (MICROBIAL INFECTION).
RX PubMed=20147401; DOI=10.1128/jvi.02554-09;
RA Atasheva S., Fish A., Fornerod M., Frolova E.I.;
RT "Venezuelan equine encephalitis virus capsid protein forms a tetrameric
RT complex with CRM1 and importin alpha/beta that obstructs nuclear pore
RT complex function.";
RL J. Virol. 84:4158-4171(2010).
RN [36]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [37]
RP INTERACTION WITH DCAF8.
RX PubMed=22500989; DOI=10.1016/j.febslet.2012.02.053;
RA Wu F., Wang S., Xing J., Li M., Zheng C.;
RT "Characterization of nuclear import and export signals determining the
RT subcellular localization of WD repeat-containing protein 42A (WDR42A).";
RL FEBS Lett. 586:1079-1085(2012).
RN [38]
RP INTERACTION WITH SLC35G1 AND STIM1.
RX PubMed=22084111; DOI=10.1073/pnas.1117231108;
RA Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.;
RT "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to
RT multiple transporters.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011).
RN [39]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [40]
RP ADP-RIBOSYLATION, AND INTERACTION WITH PARP16.
RX PubMed=22701565; DOI=10.1371/journal.pone.0037352;
RA Di Paola S., Micaroni M., Di Tullio G., Buccione R., Di Girolamo M.;
RT "PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-
RT ribosyltransferase that interacts with, and modifies karyopherin-beta1.";
RL PLoS ONE 7:E37352-E37352(2012).
RN [41]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [42]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [43]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [44]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-459 IN COMPLEX WITH RAN, AND
RP REPEAT STRUCTURE.
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 [46]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH KPNA2, AND REPEAT
RP STRUCTURE.
RX PubMed=10353244; DOI=10.1038/20367;
RA Cingolani G., Petosa C., Weis K., Muller C.W.;
RT "Structure of importin-beta bound to the IBB domain of importin-alpha.";
RL Nature 399:221-229(1999).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 3-442, AND MUTAGENESIS OF 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 and
RT importin-beta in nuclear trafficking.";
RL Cell 102:99-108(2000).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-485.
RX 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 localization
RT signal by importin beta.";
RL Mol. Cell 10:1345-1353(2002).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH SNUPN, AND
RP INTERACTION WITH SNUPN.
RX PubMed=18187419; DOI=10.1074/jbc.m709093200;
RA Mitrousis G., Olia A.S., Walker-Kopp N., Cingolani G.;
RT "Molecular basis for the recognition of snurportin 1 by importin beta.";
RL J. Biol. Chem. 283:7877-7884(2008).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH SNUPN, AND
RP INTERACTION WITH SNUPN.
RX PubMed=20476751; DOI=10.1021/bi100292y;
RA Bhardwaj A., Cingolani G.;
RT "Conformational selection in the recognition of the snurportin importin
RT beta binding domain by importin beta.";
RL Biochemistry 49:5042-5047(2010).
RN [51]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH SNAI1, INTERACTION
RP WITH SNAI1, AND FUNCTION.
RX PubMed=24699649; DOI=10.1107/s1399004714000972;
RA Choi S., Yamashita E., Yasuhara N., Song J., Son S.Y., Won Y.H., Hong H.R.,
RA Shin Y.S., Sekimoto T., Park I.Y., Yoneda Y., Lee S.J.;
RT "Structural basis for the selective nuclear import of the C2H2 zinc-finger
RT protein Snail by importin beta.";
RL Acta Crystallogr. D 70:1050-1060(2014).
CC -!- FUNCTION: Functions in nuclear protein import, either in association
CC with an adapter protein, like an importin-alpha subunit, which binds to
CC nuclear localization signals (NLS) in cargo substrates, or by acting as
CC autonomous nuclear transport receptor. Acting autonomously, serves
CC itself as NLS receptor. Docking of the importin/substrate complex to
CC the nuclear pore complex (NPC) is mediated by KPNB1 through binding to
CC nucleoporin FxFG repeats and the complex is subsequently translocated
CC through the pore by an energy requiring, Ran-dependent mechanism. At
CC the nucleoplasmic side of the NPC, Ran binds to importin-beta and the
CC three components separate and importin-alpha and -beta are re-exported
CC from the nucleus to the cytoplasm where GTP hydrolysis releases Ran
CC from importin. The directionality of nuclear import is thought to be
CC conferred by an asymmetric distribution of the GTP- and GDP-bound forms
CC of Ran between the cytoplasm and nucleus. Mediates autonomously the
CC nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5
CC (PubMed:11682607). In association with IPO7, mediates the nuclear
CC import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3
CC and H4 histones. In case of HIV-1 infection, binds and mediates the
CC nuclear import of HIV-1 Rev. Imports SNAI1 and PRKCI into the nucleus.
CC {ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:11682607,
CC ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:19386897,
CC ECO:0000269|PubMed:24699649, ECO:0000269|PubMed:9687515}.
CC -!- SUBUNIT: Forms a complex with an importin alpha subunit
CC (PubMed:8617227, PubMed:8692944). Interacts with XPO1
CC (PubMed:10209022). Forms a heterodimer with IPO7 (PubMed:9687515,
CC PubMed:10228156, PubMed:10209022). The KPNB1/IPO7 heterodimer interacts
CC with H1 histone (PubMed:10228156). Interacts with SNUPN
CC (PubMed:9670026, PubMed:10209022, PubMed:18187419, PubMed:20476751).
CC Interacts with H2A, H2B, H3 and H4 histones (By similarity). Component
CC of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259
CC (PubMed:12095920). Component of a nuclear export receptor complex
CC composed of KPNB1, Ran, SNUPN and XPO1 (PubMed:10209022,
CC PubMed:10367892). Interacts with SRY (PubMed:12764225,
CC PubMed:15297880). Interacts with PRKCI/atypical protein kinase C iota
CC (PubMed:11891849). Interacts with KPNA2 (PubMed:10353244). Interacts
CC with KPNA7 (PubMed:20701745). Interacts with SNAI1 (via zinc fingers)
CC and SNAI2 (via zinc fingers) (PubMed:15836774, PubMed:19386897,
CC PubMed:24699649). Interacts with SLC35G1 and STIM1 (PubMed:22084111).
CC Interacts with DCAF8 (PubMed:22500989). Interacts with RAN
CC (PubMed:10367892). Interacts with NUMA1 (via C-terminus); this
CC interaction is inhibited by RanGTP (PubMed:11229403). Interacts with
CC ZBED1/hDREF; required for nuclear import of ZBED1/hDREF
CC (PubMed:17209048). Interacts with SRP19 (PubMed:11682607). Interacts
CC with RPL23A (via BIB domain), RPS7 and RPL5 (PubMed:9687515,
CC PubMed:11682607). Interacts with PARP16 (PubMed:22701565).
CC {ECO:0000250|UniProtKB:P70168, ECO:0000269|PubMed:10209022,
CC ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:10353244,
CC ECO:0000269|PubMed:10367892, ECO:0000269|PubMed:11682607,
CC ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:12095920,
CC ECO:0000269|PubMed:12764225, ECO:0000269|PubMed:15297880,
CC ECO:0000269|PubMed:15836774, ECO:0000269|PubMed:17209048,
CC ECO:0000269|PubMed:18187419, ECO:0000269|PubMed:19386897,
CC ECO:0000269|PubMed:20476751, ECO:0000269|PubMed:20701745,
CC ECO:0000269|PubMed:22084111, ECO:0000269|PubMed:22500989,
CC ECO:0000269|PubMed:22701565, ECO:0000269|PubMed:24699649,
CC ECO:0000269|PubMed:8617227, ECO:0000269|PubMed:8692944,
CC ECO:0000269|PubMed:9670026, ECO:0000269|PubMed:9687515}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Rev and Tat.
CC {ECO:0000269|PubMed:16704975, ECO:0000269|PubMed:9405152,
CC ECO:0000269|PubMed:9891055}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Rex.
CC {ECO:0000269|PubMed:9891056}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human respiratory
CC syncytial virus (HRSV) matrix protein; this interaction mediates
CC nuclear import of the matrix protein early during infection.
CC {ECO:0000269|PubMed:15629770, ECO:0000269|PubMed:16171404}.
CC -!- SUBUNIT: (Microbial infection) Part of a tetrameric complex composed of
CC CRM1, importin alpha/beta dimer and the Venezuelan equine encephalitis
CC virus (VEEV) capsid; this complex blocks the receptor-mediated
CC transport through the nuclear pore. {ECO:0000269|PubMed:20147401}.
CC -!- INTERACTION:
CC Q14974; P04233: CD74; NbExp=2; IntAct=EBI-286758, EBI-2622890;
CC Q14974; Q9NRI5: DISC1; NbExp=2; IntAct=EBI-286758, EBI-529989;
CC Q14974; P04626: ERBB2; NbExp=14; IntAct=EBI-286758, EBI-641062;
CC Q14974; O95373: IPO7; NbExp=2; IntAct=EBI-286758, EBI-286735;
CC Q14974; P52294: KPNA1; NbExp=3; IntAct=EBI-286758, EBI-358383;
CC Q14974; P52292: KPNA2; NbExp=11; IntAct=EBI-286758, EBI-349938;
CC Q14974; O00505: KPNA3; NbExp=3; IntAct=EBI-286758, EBI-358297;
CC Q14974; O00629: KPNA4; NbExp=4; IntAct=EBI-286758, EBI-396343;
CC Q14974; O60684: KPNA6; NbExp=2; IntAct=EBI-286758, EBI-359923;
CC Q14974; A9QM74: KPNA7; NbExp=2; IntAct=EBI-286758, EBI-13942676;
CC Q14974; Q99558: MAP3K14; NbExp=2; IntAct=EBI-286758, EBI-358011;
CC Q14974; P49790: NUP153; NbExp=8; IntAct=EBI-286758, EBI-286779;
CC Q14974; Q15077: P2RY6; NbExp=4; IntAct=EBI-286758, EBI-10235794;
CC Q14974; Q6IQ23: PLEKHA7; NbExp=2; IntAct=EBI-286758, EBI-2125301;
CC Q14974; A8CG34: POM121C; NbExp=2; IntAct=EBI-286758, EBI-2880179;
CC Q14974; F5H1C8: SLC15A3; NbExp=2; IntAct=EBI-286758, EBI-21259559;
CC Q14974; Q16637-3: SMN2; NbExp=5; IntAct=EBI-286758, EBI-395447;
CC Q14974; O75940: SMNDC1; NbExp=2; IntAct=EBI-286758, EBI-1052641;
CC Q14974; Q9Y275: TNFSF13B; NbExp=2; IntAct=EBI-286758, EBI-519169;
CC Q14974; Q9H1C4: UNC93B1; NbExp=2; IntAct=EBI-286758, EBI-4401271;
CC Q14974; P03101: L1; Xeno; NbExp=2; IntAct=EBI-286758, EBI-7362698;
CC Q14974; P03107: L2; Xeno; NbExp=2; IntAct=EBI-286758, EBI-7362531;
CC Q14974; Q8K4J6: Mrtfa; Xeno; NbExp=2; IntAct=EBI-286758, EBI-8291665;
CC Q14974; P14907: NSP1; Xeno; NbExp=2; IntAct=EBI-286758, EBI-12265;
CC Q14974; B3CRR2: OTT_0753; Xeno; NbExp=2; IntAct=EBI-286758, EBI-26357571;
CC Q14974; P04620: rev; Xeno; NbExp=3; IntAct=EBI-286758, EBI-10687101;
CC Q14974; Q9WMX2; Xeno; NbExp=2; IntAct=EBI-286758, EBI-710918;
CC Q14974-1; P52292: KPNA2; NbExp=4; IntAct=EBI-15488647, EBI-349938;
CC Q14974-1; P52298-1: NCBP2; NbExp=2; IntAct=EBI-15488647, EBI-15798444;
CC Q14974-1; Q16637: SMN2; NbExp=2; IntAct=EBI-15488647, EBI-395421;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891849}. Nucleus
CC envelope {ECO:0000269|PubMed:11891849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14974-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14974-2; Sequence=VSP_054612;
CC -!- PTM: Mono-ADP-ribosylated by PARP16.
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-1
CC subfamily. {ECO:0000305}.
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DR EMBL; L39793; AAA82869.1; -; Genomic_DNA.
DR EMBL; L38951; AAC41763.1; -; mRNA.
DR EMBL; BT009797; AAP88799.1; -; mRNA.
DR EMBL; AK316421; BAH14792.1; -; mRNA.
DR EMBL; AC015674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94807.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94808.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94810.1; -; Genomic_DNA.
DR EMBL; BC003572; AAH03572.1; -; mRNA.
DR EMBL; BC024045; AAH24045.1; -; mRNA.
DR EMBL; BC036703; AAH36703.1; -; mRNA.
DR CCDS; CCDS11513.1; -. [Q14974-1]
DR CCDS; CCDS62228.1; -. [Q14974-2]
DR PIR; I52907; I52907.
DR RefSeq; NP_001263382.1; NM_001276453.1. [Q14974-2]
DR RefSeq; NP_002256.2; NM_002265.5. [Q14974-1]
DR PDB; 1F59; X-ray; 2.80 A; A/B=1-442.
DR PDB; 1IBR; X-ray; 2.30 A; B/D=1-462.
DR PDB; 1M5N; X-ray; 2.90 A; S=1-485.
DR PDB; 1O6O; X-ray; 2.80 A; A/B/C=1-442.
DR PDB; 1O6P; X-ray; 2.80 A; A/B=1-442.
DR PDB; 1QGK; X-ray; 2.50 A; A=1-876.
DR PDB; 1QGR; X-ray; 2.30 A; A=1-876.
DR PDB; 2P8Q; X-ray; 2.35 A; A=1-876.
DR PDB; 2Q5D; X-ray; 3.20 A; A/B=1-876.
DR PDB; 2QNA; X-ray; 2.84 A; A=127-875.
DR PDB; 3LWW; X-ray; 3.15 A; A/C=1-876.
DR PDB; 3W5K; X-ray; 2.60 A; A=1-876.
DR PDB; 6N88; EM; 6.20 A; B=1-876.
DR PDB; 6N89; EM; 7.50 A; A=1-876.
DR PDBsum; 1F59; -.
DR PDBsum; 1IBR; -.
DR PDBsum; 1M5N; -.
DR PDBsum; 1O6O; -.
DR PDBsum; 1O6P; -.
DR PDBsum; 1QGK; -.
DR PDBsum; 1QGR; -.
DR PDBsum; 2P8Q; -.
DR PDBsum; 2Q5D; -.
DR PDBsum; 2QNA; -.
DR PDBsum; 3LWW; -.
DR PDBsum; 3W5K; -.
DR PDBsum; 6N88; -.
DR PDBsum; 6N89; -.
DR AlphaFoldDB; Q14974; -.
DR SMR; Q14974; -.
DR BioGRID; 110035; 414.
DR ComplexPortal; CPX-1027; Importin complex, KPNA2 variant.
DR ComplexPortal; CPX-1032; Importin complex, Snurportin variant.
DR ComplexPortal; CPX-1055; Importin complex, KPNA1 variant.
DR ComplexPortal; CPX-1057; Importin complex, KPNA3 variant.
DR ComplexPortal; CPX-1060; Importin complex, KPNA4 variant.
DR ComplexPortal; CPX-1063; Importin complex, KPNA5 variant.
DR ComplexPortal; CPX-1064; Importin complex, KPNA6 variant.
DR ComplexPortal; CPX-1066; Importin complex, KPNA7 variant.
DR CORUM; Q14974; -.
DR DIP; DIP-6204N; -.
DR IntAct; Q14974; 253.
DR MINT; Q14974; -.
DR STRING; 9606.ENSP00000290158; -.
DR ChEMBL; CHEMBL1741199; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q14974; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14974; -.
DR MetOSite; Q14974; -.
DR PhosphoSitePlus; Q14974; -.
DR SwissPalm; Q14974; -.
DR BioMuta; KPNB1; -.
DR DMDM; 20981701; -.
DR EPD; Q14974; -.
DR jPOST; Q14974; -.
DR MassIVE; Q14974; -.
DR MaxQB; Q14974; -.
DR PaxDb; Q14974; -.
DR PeptideAtlas; Q14974; -.
DR PRIDE; Q14974; -.
DR ProteomicsDB; 60268; -. [Q14974-1]
DR ProteomicsDB; 7089; -.
DR TopDownProteomics; Q14974-1; -. [Q14974-1]
DR Antibodypedia; 17751; 300 antibodies from 41 providers.
DR DNASU; 3837; -.
DR Ensembl; ENST00000290158.9; ENSP00000290158.3; ENSG00000108424.11. [Q14974-1]
DR Ensembl; ENST00000535458.6; ENSP00000438253.2; ENSG00000108424.11. [Q14974-2]
DR Ensembl; ENST00000540627.5; ENSP00000438964.1; ENSG00000108424.11. [Q14974-2]
DR Ensembl; ENST00000583648.6; ENSP00000464042.2; ENSG00000108424.11. [Q14974-1]
DR GeneID; 3837; -.
DR KEGG; hsa:3837; -.
DR MANE-Select; ENST00000290158.9; ENSP00000290158.3; NM_002265.6; NP_002256.2.
DR UCSC; uc002ilt.3; human. [Q14974-1]
DR CTD; 3837; -.
DR DisGeNET; 3837; -.
DR GeneCards; KPNB1; -.
DR HGNC; HGNC:6400; KPNB1.
DR HPA; ENSG00000108424; Low tissue specificity.
DR MIM; 602738; gene.
DR neXtProt; NX_Q14974; -.
DR OpenTargets; ENSG00000108424; -.
DR PharmGKB; PA30191; -.
DR VEuPathDB; HostDB:ENSG00000108424; -.
DR eggNOG; KOG1241; Eukaryota.
DR GeneTree; ENSGT00550000074898; -.
DR HOGENOM; CLU_008296_1_0_1; -.
DR InParanoid; Q14974; -.
DR OMA; GRICDII; -.
DR OrthoDB; 769199at2759; -.
DR PhylomeDB; Q14974; -.
DR TreeFam; TF105655; -.
DR PathwayCommons; Q14974; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-HSA-9636249; Inhibition of nitric oxide production.
DR SignaLink; Q14974; -.
DR SIGNOR; Q14974; -.
DR BioGRID-ORCS; 3837; 810 hits in 1069 CRISPR screens.
DR ChiTaRS; KPNB1; human.
DR EvolutionaryTrace; Q14974; -.
DR GeneWiki; KPNB1; -.
DR GenomeRNAi; 3837; -.
DR Pharos; Q14974; Tbio.
DR PRO; PR:Q14974; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14974; protein.
DR Bgee; ENSG00000108424; Expressed in buccal mucosa cell and 213 other tissues.
DR ExpressionAtlas; Q14974; baseline and differential.
DR Genevisible; Q14974; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IPI:ComplexPortal.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0061676; F:importin-alpha family protein binding; IEA:Ensembl.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; TAS:ProtInc.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0031291; P:Ran protein signal transduction; IMP:GO_Central.
DR GO; GO:0006610; P:ribosomal protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0006404; P:RNA import into nucleus; IDA:ComplexPortal.
DR Gene3D; 1.25.10.10; -; 1.
DR IDEAL; IID00386; -.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00185; ARM; 3.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
KW Cytoplasm; Direct protein sequencing; Host-virus interaction; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..876
FT /note="Importin subunit beta-1"
FT /id="PRO_0000120745"
FT REPEAT 2..31
FT /note="HEAT 1"
FT /evidence="ECO:0000269|PubMed:10353244,
FT ECO:0000269|PubMed:10367892"
FT DOMAIN 21..101
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 33..65
FT /note="HEAT 2"
FT /evidence="ECO:0000269|PubMed:10353244,
FT ECO:0000269|PubMed:10367892"
FT REPEAT 85..123
FT /note="HEAT 3"
FT /evidence="ECO:0000269|PubMed:10353244,
FT ECO:0000269|PubMed:10367892"
FT REPEAT 129..160
FT /note="HEAT 4"
FT /evidence="ECO:0000269|PubMed:10353244,
FT ECO:0000269|PubMed:10367892"
FT REPEAT 170..202
FT /note="HEAT 5"
FT /evidence="ECO:0000269|PubMed:10353244,
FT ECO:0000269|PubMed:10367892"
FT REPEAT 212..247
FT /note="HEAT 6"
FT /evidence="ECO:0000269|PubMed:10353244,
FT ECO:0000269|PubMed:10367892"
FT REPEAT 253..302
FT /note="HEAT 7"
FT /evidence="ECO:0000269|PubMed:10353244,
FT ECO:0000269|PubMed:10367892"
FT REPEAT 314..360
FT /note="HEAT 8"
FT /evidence="ECO:0000269|PubMed:10353244,
FT ECO:0000269|PubMed:10367892"
FT REPEAT 364..394
FT /note="HEAT 9"
FT /evidence="ECO:0000269|PubMed:10353244,
FT ECO:0000269|PubMed:10367892"
FT REPEAT 402..438
FT /note="HEAT 10"
FT /evidence="ECO:0000269|PubMed:10353244,
FT ECO:0000269|PubMed:10367892"
FT REPEAT 449..485
FT /note="HEAT 11"
FT /evidence="ECO:0000269|PubMed:10353244"
FT REPEAT 500..537
FT /note="HEAT 12"
FT /evidence="ECO:0000269|PubMed:10353244"
FT REPEAT 544..592
FT /note="HEAT 13"
FT /evidence="ECO:0000269|PubMed:10353244"
FT REPEAT 600..639
FT /note="HEAT 14"
FT /evidence="ECO:0000269|PubMed:10353244"
FT REPEAT 644..681
FT /note="HEAT 15"
FT /evidence="ECO:0000269|PubMed:10353244"
FT REPEAT 686..724
FT /note="HEAT 16"
FT /evidence="ECO:0000269|PubMed:10353244"
FT REPEAT 732..776
FT /note="HEAT 17"
FT /evidence="ECO:0000269|PubMed:10353244"
FT REPEAT 786..829
FT /note="HEAT 18"
FT /evidence="ECO:0000269|PubMed:10353244"
FT REPEAT 831..873
FT /note="HEAT 19"
FT /evidence="ECO:0000269|PubMed:10353244"
FT REGION 286..462
FT /note="Essential for high affinity interaction with RPL23A"
FT /evidence="ECO:0000269|PubMed:9687515"
FT REGION 329..342
FT /note="IAB-binding"
FT REGION 334..419
FT /note="Ran-GTP binding"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 835
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 867
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..145
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054612"
FT MUTAGEN 178
FT /note="I->A: Largely reduced binding to FxFG repeats and
FT reduced nuclear import."
FT /evidence="ECO:0000269|PubMed:10929717"
FT MUTAGEN 178
FT /note="I->F,D: Loss of binding to FxFG repeats and reduced
FT nuclear import."
FT /evidence="ECO:0000269|PubMed:10929717"
FT CONFLICT 97
FT /note="Q -> H (in Ref. 1; AAA82869)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="N -> NA (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 863
FT /note="T -> R (in Ref. 1; AAA82869)"
FT /evidence="ECO:0000305"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 15..45
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:1IBR"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1QGR"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 170..181
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:1IBR"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:1IBR"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3LWW"
FT HELIX 231..247
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1IBR"
FT TURN 253..259
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 273..297
FT /evidence="ECO:0007829|PDB:1IBR"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 314..329
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1QGK"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1O6P"
FT HELIX 344..358
FT /evidence="ECO:0007829|PDB:1IBR"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 380..392
FT /evidence="ECO:0007829|PDB:1IBR"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:1IBR"
FT TURN 399..402
FT /evidence="ECO:0007829|PDB:1IBR"
FT TURN 404..408
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 409..415
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 422..438
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:1IBR"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 449..457
FT /evidence="ECO:0007829|PDB:1IBR"
FT HELIX 464..483
FT /evidence="ECO:0007829|PDB:1QGR"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:2P8Q"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 503..513
FT /evidence="ECO:0007829|PDB:1QGR"
FT TURN 517..520
FT /evidence="ECO:0007829|PDB:2P8Q"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:2P8Q"
FT HELIX 524..537
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:2P8Q"
FT HELIX 544..562
FT /evidence="ECO:0007829|PDB:1QGR"
FT TURN 563..566
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 573..592
FT /evidence="ECO:0007829|PDB:1QGR"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:3LWW"
FT HELIX 597..601
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 604..614
FT /evidence="ECO:0007829|PDB:1QGR"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:2P8Q"
FT HELIX 623..639
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 640..646
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 647..660
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 664..681
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 682..685
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 686..700
FT /evidence="ECO:0007829|PDB:1QGR"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:2P8Q"
FT HELIX 707..709
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 710..724
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 725..731
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 732..743
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 752..777
FT /evidence="ECO:0007829|PDB:1QGR"
FT STRAND 779..782
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 785..789
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 791..793
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 794..805
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 812..829
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 832..838
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 841..852
FT /evidence="ECO:0007829|PDB:1QGR"
FT HELIX 856..873
FT /evidence="ECO:0007829|PDB:1QGR"
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
