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Importin subunit beta-1 (Importin-90) (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97)

 IMB1_HUMAN              Reviewed;         876 AA.
Q14974; B7ZAV6; D3DTT3; Q14637; Q53XN2; Q96J27;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-MAY-2002, sequence version 2.
28-MAR-2018, entry version 199.
RecName: Full=Importin subunit beta-1;
AltName: Full=Importin-90;
AltName: Full=Karyopherin subunit beta-1;
AltName: Full=Nuclear factor p97;
AltName: Full=Pore targeting complex 97 kDa subunit;
Short=PTAC97;
Name=KPNB1; Synonyms=NTF97;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
TISSUE=Brain;
PubMed=7615630; DOI=10.1083/jcb.130.2.265;
Chi N.C., Adam E.J.H., Adam S.A.;
"Sequence and characterization of cytoplasmic nuclear protein import
factor p97.";
J. Cell Biol. 130:265-274(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7627554; DOI=10.1016/S0960-9822(95)00079-0;
Goerlich D., Kostka S., Kraft R., Dingwall C., Laskey R.A.,
Hartmann E., Prehn S.;
"Two different subunits of importin cooperate to recognize nuclear
localization signals and bind them to the nuclear envelope.";
Curr. Biol. 5:383-392(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PARTIAL PROTEIN SEQUENCE, AND INTERACTION WITH AN IMPORTIN ALPHA
SUBUNIT.
PubMed=8617227;
Weis K., Ryder U., Lamond A.I.;
"The conserved amino-terminal domain of hSRP1 alpha is essential for
nuclear protein import.";
EMBO J. 15:1818-1825(1996).
[9]
PROTEIN SEQUENCE OF 1-9; 55-62 AND 192-206, ACETYLATION AT MET-1, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAY-2005) to UniProtKB.
[10]
RAN-GTP AND ALPHA SUBUNIT BINDING SITES.
PubMed=8692944; DOI=10.1073/pnas.93.14.7059;
Moroianu J., Blobel G., Radu A.;
"Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta
heterodimer by displacing alpha from an overlapping binding site on
beta.";
Proc. Natl. Acad. Sci. U.S.A. 93:7059-7062(1996).
[11]
INTERACTION WITH HIV-1 REV AND TAT.
PubMed=9405152; DOI=10.1006/jmbi.1997.1420;
Henderson B.R., Percipalle P.;
"Interactions between HIV Rev and nuclear import and export factors:
the Rev nuclear localisation signal mediates specific binding to human
importin-beta.";
J. Mol. Biol. 274:693-707(1997).
[12]
INTERACTION WITH SNUPN.
PubMed=9670026; DOI=10.1093/emboj/17.14.4114;
Huber J., Cronshagen U., Kadokura M., Marshallsay C., Wada T.,
Sekine M., Luehrmann R.;
"Snurportin1, an m3G-cap-specific nuclear import receptor with a novel
domain structure.";
EMBO J. 17:4114-4126(1998).
[13]
FUNCTION, AND INTERACTION WITH RPL23A; RPS7; RPL5 AND IPO7.
PubMed=9687515; DOI=10.1093/emboj/17.15.4491;
Jaekel S., Goerlich D.;
"Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import
of ribosomal proteins in mammalian cells.";
EMBO J. 17:4491-4502(1998).
[14]
FUNCTION, AND INTERACTION WITH H1 HISTONE AND IPO7.
PubMed=10228156; DOI=10.1093/emboj/18.9.2411;
Jaekel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K.,
Doenecke D., Goerlich D.;
"The importin beta/importin 7 heterodimer is a functional nuclear
import receptor for histone H1.";
EMBO J. 18:2411-2423(1999).
[15]
IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, AND INTERACTION WITH
IPO7; SNUPN AND XPO1.
PubMed=10209022; DOI=10.1083/jcb.145.2.255;
Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U.,
Hartmann E., Luehrmann R., Goerlich D.;
"CRM1-mediated recycling of snurportin 1 to the cytoplasm.";
J. Cell Biol. 145:255-264(1999).
[16]
INTERACTION WITH HIV-1 REV.
PubMed=9891055; DOI=10.1128/MCB.19.2.1210;
Truant R., Cullen B.R.;
"The arginine-rich domains present in human immunodeficiency virus
type 1 Tat and Rev function as direct importin beta-dependent nuclear
localization signals.";
Mol. Cell. Biol. 19:1210-1217(1999).
[17]
INTERACTION WITH HTLV-1 REX.
PubMed=9891056; DOI=10.1128/MCB.19.2.1218;
Palmeri D., Malim M.H.;
"Importin beta can mediate the nuclear import of an arginine-rich
nuclear localization signal in the absence of importin alpha.";
Mol. Cell. Biol. 19:1218-1225(1999).
[18]
INTERACTION WITH NUMA1.
PubMed=11229403;
Wiese C., Wilde A., Moore M.S., Adam S.A., Merdes A., Zheng Y.;
"Role of importin-beta in coupling Ran to downstream targets in
microtubule assembly.";
Science 291:653-656(2001).
[19]
IDENTIFICATION IN AN IMPORT SNRNP COMPLEX.
PubMed=12095920; DOI=10.1093/hmg/11.15.1785;
Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.;
"SMN, the spinal muscular atrophy protein, forms a pre-import snRNP
complex with snurportin1 and importin beta.";
Hum. Mol. Genet. 11:1785-1795(2002).
[20]
INTERACTION WITH PRKCI, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11891849; DOI=10.1002/jcb.10101.abs;
White W.O., Seibenhener M.L., Wooten M.W.;
"Phosphorylation of tyrosine 256 facilitates nuclear import of
atypical protein kinase C.";
J. Cell. Biochem. 85:42-53(2002).
[21]
INTERACTION WITH SRY.
PubMed=12764225; DOI=10.1073/pnas.1137864100;
Harley V.R., Layfield S., Mitchell C.L., Forwood J.K., John A.P.,
Briggs L.J., McDowall S.G., Jans D.A.;
"Defective importin beta recognition and nuclear import of the sex-
determining factor SRY are associated with XY sex-reversing
mutations.";
Proc. Natl. Acad. Sci. U.S.A. 100:7045-7050(2003).
[22]
INTERACTION WITH SRY.
PubMed=15297880; DOI=10.1038/sj.emboj.7600352;
Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N.,
Aldrian-Herrada G., Poulat F., Berta P., Benkirane M.,
Boizet-Bonhoure B.;
"Regulation of human SRY subcellular distribution by its
acetylation/deacetylation.";
EMBO J. 23:3336-3345(2004).
[23]
INTERACTION WITH HRSV PROTEIN M.
PubMed=16171404; DOI=10.1021/bi050701e;
Ghildyal R., Ho A., Wagstaff K.M., Dias M.M., Barton C.L., Jans P.,
Bardin P.G., Jans D.A.;
"Nuclear import of the respiratory syncytial virus matrix protein is
mediated by importin beta1 independent of importin alpha.";
Biochemistry 44:12887-12895(2005).
[24]
INTERACTION WITH SNAI1.
PubMed=15836774; DOI=10.1111/j.1365-2443.2005.00850.x;
Yamasaki H., Sekimoto T., Ohkubo T., Douchi T., Nagata Y., Ozawa M.,
Yoneda Y.;
"Zinc finger domain of Snail functions as a nuclear localization
signal for importin beta-mediated nuclear import pathway.";
Genes Cells 10:455-464(2005).
[25]
INTERACTION WITH HRSV PROTEIN M2-1.
PubMed=15629770; DOI=10.1016/j.virol.2004.10.031;
Reimers K., Buchholz K., Werchau H.;
"Respiratory syncytial virus M2-1 protein induces the activation of
nuclear factor kappa B.";
Virology 331:260-268(2005).
[26]
INTERACTION WITH HIV-1 REV.
PubMed=16704975; DOI=10.1074/jbc.M602189200;
Arnold M., Nath A., Hauber J., Kehlenbach R.H.;
"Multiple importins function as nuclear transport receptors for the
Rev protein of human immunodeficiency virus type 1.";
J. Biol. Chem. 281:20883-20890(2006).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[30]
FUNCTION, AND INTERACTION WITH SNAI1 AND SNAI2.
PubMed=19386897; DOI=10.1242/jcs.041749;
Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.;
"Characterization of Snail nuclear import pathways as representatives
of C2H2 zinc finger transcription factors.";
J. Cell Sci. 122:1452-1460(2009).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211; LYS-835 AND LYS-867,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[32]
INTERACTION WITH KPNA7.
PubMed=20701745; DOI=10.1186/1471-2121-11-63;
Kelley J.B., Talley A.M., Spencer A., Gioeli D., Paschal B.M.;
"Karyopherin alpha7 (KPNA7), a divergent member of the importin alpha
family of nuclear import receptors.";
BMC Cell Biol. 11:63-63(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
INTERACTION WITH DCAF8.
PubMed=22500989; DOI=10.1016/j.febslet.2012.02.053;
Wu F., Wang S., Xing J., Li M., Zheng C.;
"Characterization of nuclear import and export signals determining the
subcellular localization of WD repeat-containing protein 42A
(WDR42A).";
FEBS Lett. 586:1079-1085(2012).
[35]
INTERACTION WITH SLC35G1 AND STIM1.
PubMed=22084111; DOI=10.1073/pnas.1117231108;
Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.;
"POST, partner of stromal interaction molecule 1 (STIM1), targets
STIM1 to multiple transporters.";
Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[37]
ADP-RIBOSYLATION, AND INTERACTION WITH PARP16.
PubMed=22701565; DOI=10.1371/journal.pone.0037352;
Di Paola S., Micaroni M., Di Tullio G., Buccione R., Di Girolamo M.;
"PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-
ribosyltransferase that interacts with, and modifies karyopherin-
beta1.";
PLoS ONE 7:E37352-E37352(2012).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[42]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-459 IN COMPLEX WITH RAN,
AND REPEAT STRUCTURE.
PubMed=10367892; DOI=10.1016/S0092-8674(00)80774-6;
Vetter I.R., Arndt A., Kutay U., Goerlich D., Wittinghofer A.;
"Structural view of the Ran-Importin beta interaction at 2.3 A
resolution.";
Cell 97:635-646(1999).
[43]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH KPNA2, AND
REPEAT STRUCTURE.
PubMed=10353244; DOI=10.1038/20367;
Cingolani G., Petosa C., Weis K., Muller C.W.;
"Structure of importin-beta bound to the IBB domain of importin-
alpha.";
Nature 399:221-229(1999).
[44]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 3-442, AND MUTAGENESIS OF
ILE-178.
PubMed=10929717; DOI=10.1016/S0092-8674(00)00014-3;
Bayliss R., Littlewood T., Stewart M.;
"Structural basis for the interaction between FxFG nucleoporin repeats
and importin-beta in nuclear trafficking.";
Cell 102:99-108(2000).
[45]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-485.
PubMed=12504010; DOI=10.1016/S1097-2765(02)00727-X;
Cingolani G., Bednenko J., Gillespie M.T., Gerace L.;
"Molecular basis for the recognition of a nonclassical nuclear
localization signal by importin beta.";
Mol. Cell 10:1345-1353(2002).
[46]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH SNUPN, AND
INTERACTION WITH SNUPN.
PubMed=18187419; DOI=10.1074/jbc.M709093200;
Mitrousis G., Olia A.S., Walker-Kopp N., Cingolani G.;
"Molecular basis for the recognition of snurportin 1 by importin
beta.";
J. Biol. Chem. 283:7877-7884(2008).
[47]
X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH SNUPN, AND
INTERACTION WITH SNUPN.
PubMed=20476751; DOI=10.1021/bi100292y;
Bhardwaj A., Cingolani G.;
"Conformational selection in the recognition of the snurportin
importin beta binding domain by importin beta.";
Biochemistry 49:5042-5047(2010).
[48]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH SNAI1,
INTERACTION WITH SNAI1, AND FUNCTION.
PubMed=24699649; DOI=10.1107/S1399004714000972;
Choi S., Yamashita E., Yasuhara N., Song J., Son S.Y., Won Y.H.,
Hong H.R., Shin Y.S., Sekimoto T., Park I.Y., Yoneda Y., Lee S.J.;
"Structural basis for the selective nuclear import of the C2H2 zinc-
finger protein Snail by importin beta.";
Acta Crystallogr. D 70:1050-1060(2014).
-!- 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.
{ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:11891849,
ECO:0000269|PubMed:19386897, ECO:0000269|PubMed:24699649,
ECO:0000269|PubMed:9687515}.
-!- SUBUNIT: Forms a complex with an importin alpha subunit
(PubMed:8617227, PubMed:8692944). Forms a heterodimer with IPO7.
Interacts with IPO7, SNUPN, RPL23A and XPO1. The KPNB1/IPO7
heterodimer interacts with H1 histone. Interacts with H2A, H2B, H3
and H4 histones (By similarity). Component of an import snRNP
complex composed of KPNB1, SNUPN, SMN1 and ZNF259. Component of a
nuclear export receptor complex composed of KPNB1, Ran, SNUPN and
XPO1. Binds to HIV-1 Rev and Tat. Interacts with HTLV-1 Rex.
Interacts with SRY. Interacts with PRKCI/atypical protein kinase C
iota. Interacts with human respiratory syncytial virus (HRSV)
protein M. Interacts with KPNA7. Interacts with SNAI1 (via zinc
fingers) and SNAI2 (via zinc fingers). Interacts with SLC35G1 and
STIM1. Interacts with DCAF8. Interacts with RAN (By similarity).
Interacts with NUMA1 (via C-terminus); this interaction is
inhibited by RanGTP (PubMed:11229403).
{ECO:0000250|UniProtKB:P70168, ECO:0000269|PubMed:10209022,
ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:11229403,
ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:12095920,
ECO:0000269|PubMed:12764225, ECO:0000269|PubMed:15297880,
ECO:0000269|PubMed:15629770, ECO:0000269|PubMed:15836774,
ECO:0000269|PubMed:16171404, ECO:0000269|PubMed:16704975,
ECO:0000269|PubMed:19386897, ECO:0000269|PubMed:20701745,
ECO:0000269|PubMed:22084111, ECO:0000269|PubMed:22500989,
ECO:0000269|PubMed:22701565, ECO:0000269|PubMed:24699649,
ECO:0000269|PubMed:8617227, ECO:0000269|PubMed:9405152,
ECO:0000269|PubMed:9670026, ECO:0000269|PubMed:9687515,
ECO:0000269|PubMed:9891055, ECO:0000269|PubMed:9891056}.
-!- INTERACTION:
Q9WMX2:- (xeno); NbExp=2; IntAct=EBI-286758, EBI-710918;
P04626:ERBB2; NbExp=14; IntAct=EBI-286758, EBI-641062;
P52294:KPNA1; NbExp=2; IntAct=EBI-286758, EBI-358383;
P52292:KPNA2; NbExp=5; IntAct=EBI-286758, EBI-349938;
O00505:KPNA3; NbExp=2; IntAct=EBI-286758, EBI-358297;
O00629:KPNA4; NbExp=4; IntAct=EBI-286758, EBI-396343;
O60684:KPNA6; NbExp=2; IntAct=EBI-286758, EBI-359923;
A9QM74:KPNA7; NbExp=2; IntAct=EBI-286758, EBI-13942676;
P03101:L1 (xeno); NbExp=2; IntAct=EBI-286758, EBI-7362698;
P03107:L2 (xeno); NbExp=2; IntAct=EBI-286758, EBI-7362531;
Q8K4J6:Mkl1 (xeno); NbExp=2; IntAct=EBI-286758, EBI-8291665;
P52298-1:NCBP2; NbExp=2; IntAct=EBI-15488647, EBI-15798444;
P14907:NSP1 (xeno); NbExp=2; IntAct=EBI-286758, EBI-12265;
P51178:PLCD1; NbExp=4; IntAct=EBI-286758, EBI-4405387;
P04620:rev (xeno); NbExp=3; IntAct=EBI-286758, EBI-10687101;
Q16637:SMN2; NbExp=2; IntAct=EBI-15488647, EBI-395421;
Q16637-3:SMN2; NbExp=5; IntAct=EBI-286758, EBI-395447;
O75940:SMNDC1; NbExp=2; IntAct=EBI-286758, EBI-1052641;
O92837:VP3 (xeno); NbExp=2; IntAct=EBI-286758, EBI-7196689;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891849}.
Nucleus envelope {ECO:0000269|PubMed:11891849}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14974-1; Sequence=Displayed;
Name=2;
IsoId=Q14974-2; Sequence=VSP_054612;
Note=No experimental confirmation available.;
-!- PTM: Mono-ADP-ribosylated by PARP16.
-!- SIMILARITY: Belongs to the importin beta family. Importin beta-1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L39793; AAA82869.1; -; Genomic_DNA.
EMBL; L38951; AAC41763.1; -; mRNA.
EMBL; BT009797; AAP88799.1; -; mRNA.
EMBL; AK316421; BAH14792.1; -; mRNA.
EMBL; AC015674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC025682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94807.1; -; Genomic_DNA.
EMBL; CH471109; EAW94808.1; -; Genomic_DNA.
EMBL; CH471109; EAW94810.1; -; Genomic_DNA.
EMBL; BC003572; AAH03572.1; -; mRNA.
EMBL; BC024045; AAH24045.1; -; mRNA.
EMBL; BC036703; AAH36703.1; -; mRNA.
CCDS; CCDS11513.1; -. [Q14974-1]
CCDS; CCDS62228.1; -. [Q14974-2]
PIR; I52907; I52907.
RefSeq; NP_001263382.1; NM_001276453.1. [Q14974-2]
RefSeq; NP_002256.2; NM_002265.5. [Q14974-1]
UniGene; Hs.532793; -.
PDB; 1F59; X-ray; 2.80 A; A/B=1-442.
PDB; 1IBR; X-ray; 2.30 A; B/D=1-462.
PDB; 1M5N; X-ray; 2.90 A; S=1-485.
PDB; 1O6O; X-ray; 2.80 A; A/B/C=1-442.
PDB; 1O6P; X-ray; 2.80 A; A/B=1-442.
PDB; 1QGK; X-ray; 2.50 A; A=1-876.
PDB; 1QGR; X-ray; 2.30 A; A=1-876.
PDB; 2P8Q; X-ray; 2.35 A; A=1-876.
PDB; 2Q5D; X-ray; 3.20 A; A/B=1-876.
PDB; 2QNA; X-ray; 2.84 A; A=127-875.
PDB; 3LWW; X-ray; 3.15 A; A/C=1-876.
PDB; 3W5K; X-ray; 2.60 A; A=1-876.
PDBsum; 1F59; -.
PDBsum; 1IBR; -.
PDBsum; 1M5N; -.
PDBsum; 1O6O; -.
PDBsum; 1O6P; -.
PDBsum; 1QGK; -.
PDBsum; 1QGR; -.
PDBsum; 2P8Q; -.
PDBsum; 2Q5D; -.
PDBsum; 2QNA; -.
PDBsum; 3LWW; -.
PDBsum; 3W5K; -.
ProteinModelPortal; Q14974; -.
SMR; Q14974; -.
BioGrid; 110035; 265.
CORUM; Q14974; -.
DIP; DIP-6204N; -.
IntAct; Q14974; 170.
MINT; Q14974; -.
STRING; 9606.ENSP00000290158; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; Q14974; -.
PhosphoSitePlus; Q14974; -.
SwissPalm; Q14974; -.
DMDM; 20981701; -.
EPD; Q14974; -.
MaxQB; Q14974; -.
PaxDb; Q14974; -.
PeptideAtlas; Q14974; -.
PRIDE; Q14974; -.
TopDownProteomics; Q14974-1; -. [Q14974-1]
DNASU; 3837; -.
Ensembl; ENST00000290158; ENSP00000290158; ENSG00000108424. [Q14974-1]
Ensembl; ENST00000535458; ENSP00000438253; ENSG00000108424. [Q14974-2]
Ensembl; ENST00000540627; ENSP00000438964; ENSG00000108424. [Q14974-2]
GeneID; 3837; -.
KEGG; hsa:3837; -.
UCSC; uc002ilt.3; human. [Q14974-1]
CTD; 3837; -.
DisGeNET; 3837; -.
EuPathDB; HostDB:ENSG00000108424.9; -.
GeneCards; KPNB1; -.
HGNC; HGNC:6400; KPNB1.
HPA; CAB034449; -.
HPA; HPA029878; -.
HPA; HPA050302; -.
MIM; 602738; gene.
neXtProt; NX_Q14974; -.
OpenTargets; ENSG00000108424; -.
PharmGKB; PA30191; -.
eggNOG; KOG1241; Eukaryota.
eggNOG; COG5215; LUCA.
GeneTree; ENSGT00550000074898; -.
HOGENOM; HOG000204108; -.
HOVERGEN; HBG002369; -.
InParanoid; Q14974; -.
KO; K14293; -.
OMA; KNHLTSK; -.
OrthoDB; EOG091G01XQ; -.
PhylomeDB; Q14974; -.
TreeFam; TF105655; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
Reactome; R-HSA-180746; Nuclear import of Rev protein.
Reactome; R-HSA-211227; Activation of DNA fragmentation factor.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; Q14974; -.
SIGNOR; Q14974; -.
ChiTaRS; KPNB1; human.
EvolutionaryTrace; Q14974; -.
GeneWiki; KPNB1; -.
GenomeRNAi; 3837; -.
PRO; PR:Q14974; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108424; -.
CleanEx; HS_KPNB1; -.
ExpressionAtlas; Q14974; baseline and differential.
Genevisible; Q14974; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0034399; C:nuclear periphery; IBA:GO_Central.
GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
GO; GO:0008139; F:nuclear localization sequence binding; TAS:ProtInc.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0008565; F:protein transporter activity; IBA:GO_Central.
GO; GO:0008536; F:Ran GTPase binding; IEA:InterPro.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0006309; P:apoptotic DNA fragmentation; TAS:Reactome.
GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB.
GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:UniProtKB.
GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IMP:UniProtKB.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
GO; GO:0019054; P:modulation by virus of host process; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; TAS:ProtInc.
GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
GO; GO:0000060; P:protein import into nucleus, translocation; TAS:ProtInc.
GO; GO:0031291; P:Ran protein signal transduction; IMP:UniProtKB.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; TAS:Reactome.
GO; GO:0006610; P:ribosomal protein import into nucleus; IDA:UniProtKB.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR021133; HEAT_type_2.
InterPro; IPR001494; Importin-beta_N.
Pfam; PF03810; IBN_N; 1.
SMART; SM00185; ARM; 3.
SMART; SM00913; IBN_N; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50077; HEAT_REPEAT; 1.
PROSITE; PS50166; IMPORTIN_B_NT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
Complete proteome; Cytoplasm; Direct protein sequencing;
Host-virus interaction; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; Repeat; Transport.
CHAIN 1 876 Importin subunit beta-1.
/FTId=PRO_0000120745.
REPEAT 2 31 HEAT 1. {ECO:0000269|PubMed:10353244,
ECO:0000269|PubMed:10367892}.
DOMAIN 21 101 Importin N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00115}.
REPEAT 33 65 HEAT 2. {ECO:0000269|PubMed:10353244,
ECO:0000269|PubMed:10367892}.
REPEAT 85 123 HEAT 3. {ECO:0000269|PubMed:10353244,
ECO:0000269|PubMed:10367892}.
REPEAT 129 160 HEAT 4. {ECO:0000269|PubMed:10353244,
ECO:0000269|PubMed:10367892}.
REPEAT 170 202 HEAT 5. {ECO:0000269|PubMed:10353244,
ECO:0000269|PubMed:10367892}.
REPEAT 212 247 HEAT 6. {ECO:0000269|PubMed:10353244,
ECO:0000269|PubMed:10367892}.
REPEAT 253 302 HEAT 7. {ECO:0000269|PubMed:10353244,
ECO:0000269|PubMed:10367892}.
REPEAT 314 360 HEAT 8. {ECO:0000269|PubMed:10353244,
ECO:0000269|PubMed:10367892}.
REPEAT 364 394 HEAT 9. {ECO:0000269|PubMed:10353244,
ECO:0000269|PubMed:10367892}.
REPEAT 402 438 HEAT 10. {ECO:0000269|PubMed:10353244,
ECO:0000269|PubMed:10367892}.
REPEAT 449 485 HEAT 11. {ECO:0000269|PubMed:10353244}.
REPEAT 500 537 HEAT 12. {ECO:0000269|PubMed:10353244}.
REPEAT 544 592 HEAT 13. {ECO:0000269|PubMed:10353244}.
REPEAT 600 639 HEAT 14. {ECO:0000269|PubMed:10353244}.
REPEAT 644 681 HEAT 15. {ECO:0000269|PubMed:10353244}.
REPEAT 686 724 HEAT 16. {ECO:0000269|PubMed:10353244}.
REPEAT 732 776 HEAT 17. {ECO:0000269|PubMed:10353244}.
REPEAT 786 829 HEAT 18. {ECO:0000269|PubMed:10353244}.
REPEAT 831 873 HEAT 19. {ECO:0000269|PubMed:10353244}.
REGION 329 342 IAB-binding.
REGION 334 419 Ran-GTP binding.
COMPBIAS 337 341 Poly-Asp.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.9}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 211 211 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 835 835 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 867 867 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 145 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054612.
MUTAGEN 178 178 I->A: Largely reduced binding to FxFG
repeats and reduced nuclear import.
{ECO:0000269|PubMed:10929717}.
MUTAGEN 178 178 I->F,D: Loss of binding to FxFG repeats
and reduced nuclear import.
{ECO:0000269|PubMed:10929717}.
CONFLICT 97 97 Q -> H (in Ref. 1; AAA82869).
{ECO:0000305}.
CONFLICT 200 200 N -> NA (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 863 863 T -> R (in Ref. 1; AAA82869).
{ECO:0000305}.
HELIX 3 9 {ECO:0000244|PDB:1IBR}.
HELIX 15 45 {ECO:0000244|PDB:1IBR}.
HELIX 51 65 {ECO:0000244|PDB:1IBR}.
HELIX 70 81 {ECO:0000244|PDB:1IBR}.
HELIX 85 98 {ECO:0000244|PDB:1IBR}.
TURN 99 101 {ECO:0000244|PDB:1QGR}.
STRAND 104 106 {ECO:0000244|PDB:1IBR}.
HELIX 109 120 {ECO:0000244|PDB:1IBR}.
HELIX 121 123 {ECO:0000244|PDB:1IBR}.
HELIX 129 138 {ECO:0000244|PDB:1IBR}.
HELIX 144 160 {ECO:0000244|PDB:1IBR}.
HELIX 163 165 {ECO:0000244|PDB:1IBR}.
HELIX 167 169 {ECO:0000244|PDB:1IBR}.
HELIX 170 181 {ECO:0000244|PDB:1IBR}.
HELIX 188 201 {ECO:0000244|PDB:1IBR}.
TURN 202 205 {ECO:0000244|PDB:1IBR}.
HELIX 206 209 {ECO:0000244|PDB:1IBR}.
HELIX 212 225 {ECO:0000244|PDB:1IBR}.
STRAND 228 230 {ECO:0000244|PDB:3LWW}.
HELIX 231 247 {ECO:0000244|PDB:1IBR}.
HELIX 249 251 {ECO:0000244|PDB:1IBR}.
TURN 253 259 {ECO:0000244|PDB:1IBR}.
HELIX 260 269 {ECO:0000244|PDB:1IBR}.
HELIX 273 297 {ECO:0000244|PDB:1IBR}.
STRAND 303 305 {ECO:0000244|PDB:1IBR}.
HELIX 314 329 {ECO:0000244|PDB:1IBR}.
HELIX 330 332 {ECO:0000244|PDB:1QGK}.
STRAND 335 337 {ECO:0000244|PDB:1O6P}.
HELIX 344 358 {ECO:0000244|PDB:1IBR}.
TURN 359 362 {ECO:0000244|PDB:1IBR}.
HELIX 363 374 {ECO:0000244|PDB:1IBR}.
HELIX 380 392 {ECO:0000244|PDB:1IBR}.
STRAND 394 397 {ECO:0000244|PDB:1IBR}.
TURN 399 402 {ECO:0000244|PDB:1IBR}.
TURN 404 408 {ECO:0000244|PDB:1IBR}.
HELIX 409 415 {ECO:0000244|PDB:1IBR}.
HELIX 416 418 {ECO:0000244|PDB:1IBR}.
HELIX 422 438 {ECO:0000244|PDB:1IBR}.
HELIX 439 442 {ECO:0000244|PDB:1IBR}.
TURN 446 448 {ECO:0000244|PDB:1IBR}.
HELIX 449 457 {ECO:0000244|PDB:1IBR}.
HELIX 464 483 {ECO:0000244|PDB:1QGR}.
STRAND 487 493 {ECO:0000244|PDB:2P8Q}.
TURN 500 502 {ECO:0000244|PDB:1QGR}.
HELIX 503 513 {ECO:0000244|PDB:1QGR}.
TURN 517 520 {ECO:0000244|PDB:2P8Q}.
HELIX 521 523 {ECO:0000244|PDB:2P8Q}.
HELIX 524 537 {ECO:0000244|PDB:1QGR}.
HELIX 541 543 {ECO:0000244|PDB:2P8Q}.
HELIX 544 562 {ECO:0000244|PDB:1QGR}.
TURN 563 566 {ECO:0000244|PDB:1QGR}.
HELIX 573 592 {ECO:0000244|PDB:1QGR}.
STRAND 593 595 {ECO:0000244|PDB:3LWW}.
HELIX 597 601 {ECO:0000244|PDB:1QGR}.
HELIX 604 614 {ECO:0000244|PDB:1QGR}.
STRAND 619 622 {ECO:0000244|PDB:2P8Q}.
HELIX 623 639 {ECO:0000244|PDB:1QGR}.
HELIX 640 646 {ECO:0000244|PDB:1QGR}.
HELIX 647 660 {ECO:0000244|PDB:1QGR}.
HELIX 664 681 {ECO:0000244|PDB:1QGR}.
HELIX 682 685 {ECO:0000244|PDB:1QGR}.
HELIX 686 700 {ECO:0000244|PDB:1QGR}.
STRAND 703 705 {ECO:0000244|PDB:2P8Q}.
HELIX 707 709 {ECO:0000244|PDB:1QGR}.
HELIX 710 724 {ECO:0000244|PDB:1QGR}.
HELIX 725 731 {ECO:0000244|PDB:1QGR}.
HELIX 732 743 {ECO:0000244|PDB:1QGR}.
HELIX 752 777 {ECO:0000244|PDB:1QGR}.
STRAND 779 782 {ECO:0000244|PDB:1QGR}.
HELIX 785 789 {ECO:0000244|PDB:1QGR}.
HELIX 791 793 {ECO:0000244|PDB:1QGR}.
HELIX 794 805 {ECO:0000244|PDB:1QGR}.
HELIX 812 829 {ECO:0000244|PDB:1QGR}.
HELIX 832 838 {ECO:0000244|PDB:1QGR}.
HELIX 841 852 {ECO:0000244|PDB:1QGR}.
HELIX 856 873 {ECO:0000244|PDB:1QGR}.
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


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20-372-60249 karyopherin (importin) beta 1 (KPNB1) - Mouse monoclonal anti-human KPNB1 antibody; Karyopherin subunit beta-1; Nuclear factor P97; Importin 90 Monoclonal 0.1 mg
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15-288-21448A AP-3 complex subunit beta-2 - Adapter-related protein complex 3 beta-2 subunit; Beta3B-adaptin; Adaptor protein complex AP-3 beta-2 subunit; AP-3 complex beta-2 subunit; Clathrin assembly protein comp 0.05 mg
15-288-21448A AP-3 complex subunit beta-2 - Adapter-related protein complex 3 beta-2 subunit; Beta3B-adaptin; Adaptor protein complex AP-3 beta-2 subunit; AP-3 complex beta-2 subunit; Clathrin assembly protein comp 0.1 mg
EIAAB29611 Homo sapiens,Human,PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAFAH subunit beta,PAF-AH subunit beta,PAFAH1B2,PAFAHB,Platelet-activating factor acetylhydrolase IB subunit beta
EIAAB29614 Bos taurus,Bovine,PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAFAH subunit beta,PAF-AH subunit beta,PAFAH1B2,PAFAHB,Platelet-activating factor acetylhydrolase IB subunit beta
EIAAB29612 Mouse,Mus musculus,PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAFAH subunit beta,PAF-AH subunit beta,Pafah1b2,Pafahb,Platelet-activating factor acetylhydrolase IB subunit beta
EIAAB29613 Chicken,Gallus gallus,PAF acetylhydrolase 30 kDa subunit,PAF-AH 30 kDa subunit,PAFAH subunit beta,PAF-AH subunit beta,PAFAH1B2,PAFAHB,Platelet-activating factor acetylhydrolase IB subunit beta,RCJMB04
15-288-22423F Platelet-activating factor acetylhydrolase IB subunit beta - EC 3.1.1.47; PAF acetylhydrolase 30 kDa subunit; PAF-AH 30 kDa subunit; PAF-AH subunit beta; PAFAH subunit beta Polyclonal 0.05 mg
15-288-22423F Platelet-activating factor acetylhydrolase IB subunit beta - EC 3.1.1.47; PAF acetylhydrolase 30 kDa subunit; PAF-AH 30 kDa subunit; PAF-AH subunit beta; PAFAH subunit beta Polyclonal 0.1 mg
15-288-22444 Importin alpha-2 subunit - Karyopherin alpha-2 subunit; SRP1-alpha; RAG cohort protein 1 Polyclonal 0.1 mg
15-288-22444 Importin alpha-2 subunit - Karyopherin alpha-2 subunit; SRP1-alpha; RAG cohort protein 1 Polyclonal 0.05 mg
EIAAB27111 CAAT box DNA-binding protein subunit B,HAP3,Homo sapiens,Human,NFYB,NF-YB,Nuclear transcription factor Y subunit B,Nuclear transcription factor Y subunit beta
10-288-22444F Importin alpha-2 subunit - Karyopherin alpha-2 subunit; SRP1-alpha; RAG cohort protein 1 0.1 mg
10-288-22444F Importin alpha-2 subunit - Karyopherin alpha-2 subunit; SRP1-alpha; RAG cohort protein 1 0.05 mg
EIAAB32876 11S regulator complex subunit beta,Activator of multicatalytic protease subunit 2,Homo sapiens,Human,PA28b,PA28beta,Proteasome activator 28 subunit beta,Proteasome activator complex subunit 2,PSME2,RE
EIAAB32777 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,Psmb8,Rat,Rattus norvegicus
EIAAB27108 CAAT box DNA-binding protein subunit B,Mouse,Mus musculus,Nfyb,NF-YB,Nuclear transcription factor Y subunit B,Nuclear transcription factor Y subunit beta
EIAAB27110 Bos taurus,Bovine,CAAT box DNA-binding protein subunit B,NFYB,NF-YB,Nuclear transcription factor Y subunit B,Nuclear transcription factor Y subunit beta
EIAAB30507 Cbfb,CBF-beta,Core-binding factor subunit beta,Mouse,Mus musculus,PEA2-beta,Pebp2b,PEBP2-beta,Pebpb2,Polyomavirus enhancer-binding protein 2 beta subunit,SL3_AKV core-binding factor beta subunit,SL3-3
EIAAB32873 11S regulator complex subunit beta,Activator of multicatalytic protease subunit 2,PA28b,PA28beta,Proteasome activator 28 subunit beta,Proteasome activator complex subunit 2,Psme2,Rat,Rattus norvegicus
EIAAB32875 11S regulator complex subunit beta,Activator of multicatalytic protease subunit 2,Mouse,Mus musculus,PA28b,Pa28b1,PA28beta,Proteasome activator 28 subunit beta,Proteasome activator complex subunit 2,P
10-288-22423F Platelet-activating factor acetylhydrolase IB subunit beta - EC 3.1.1.47; PAF acetylhydrolase 30 kDa subunit; PAF-AH 30 kDa subunit; PAF-AH subunit beta; PAFAH subunit beta 0.05 mg
10-288-22423F Platelet-activating factor acetylhydrolase IB subunit beta - EC 3.1.1.47; PAF acetylhydrolase 30 kDa subunit; PAF-AH 30 kDa subunit; PAF-AH subunit beta; PAFAH subunit beta 0.1 mg
EIAAB32773 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Pig,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,PSMB8,Sus scrofa


 

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