IPO9_HUMAN
ID IPO9_HUMAN Reviewed; 1041 AA.
AC Q96P70; B1ASV5; Q8N1Y1; Q8N3I2; Q8NCG9; Q96SU6; Q9NW01; Q9P0A8; Q9ULM8;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Importin-9 {ECO:0000303|PubMed:30855230};
DE Short=Imp9 {ECO:0000303|PubMed:11823430};
DE AltName: Full=Ran-binding protein 9;
DE Short=RanBP9;
GN Name=IPO9 {ECO:0000303|PubMed:30855230, ECO:0000312|HGNC:HGNC:19425};
GN Synonyms=IMP9 {ECO:0000303|PubMed:11823430},
GN KIAA1192 {ECO:0000303|PubMed:10574461}, RANBP9; ORFNames=HSPC273;
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 [MRNA], FUNCTION, AND INTERACTION WITH RPS7; RPL18A;
RP RPL4 AND RPL6.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-276 AND 358-1041.
RC TISSUE=Amygdala;
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 PROTEIN SEQUENCE OF 2-22; 400-427 AND 908-916, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1041.
RC TISSUE=Placenta;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 632-1041.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 767-1041.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 780-1041.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [10]
RP INTERACTION WITH PPP2R1A AND PPP2R1B.
RX PubMed=12670497; DOI=10.1016/s0006-291x(03)00434-0;
RA Lubert E.J., Sarge K.D.;
RT "Interaction between protein phosphatase 2A and members of the importin
RT beta superfamily.";
RL Biochem. Biophys. Res. Commun. 303:908-913(2003).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH AKIRIN2.
RX PubMed=34711951; DOI=10.1038/s41586-021-04035-8;
RA de Almeida M., Hinterndorfer M., Brunner H., Grishkovskaya I., Singh K.,
RA Schleiffer A., Jude J., Deswal S., Kalis R., Vunjak M., Lendl T., Imre R.,
RA Roitinger E., Neumann T., Kandolf S., Schutzbier M., Mechtler K.,
RA Versteeg G.A., Haselbach D., Zuber J.;
RT "AKIRIN2 controls the nuclear import of proteasomes in vertebrates.";
RL Nature 599:491-496(2021).
RN [17] {ECO:0007744|PDB:6N1Z}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH HISTONE H2A AND H2B,
RP FUNCTION, AND SUBUNIT.
RX PubMed=30855230; DOI=10.7554/elife.43630;
RA Padavannil A., Sarkar P., Kim S.J., Cagatay T., Jiou J., Brautigam C.A.,
RA Tomchick D.R., Sali A., D'Arcy S., Chook Y.M.;
RT "Importin-9 wraps around the H2A-H2B core to act as nuclear importer and
RT histone chaperone.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Nuclear transport receptor that mediates nuclear import of
CC proteins, such as histones, proteasome and actin (PubMed:11823430,
CC PubMed:34711951, PubMed:30855230). Serves as receptor for nuclear
CC localization signals (NLS) in cargo substrates (PubMed:11823430). Is
CC thought to mediate docking of the importin/substrate complex to the
CC nuclear pore complex (NPC) through binding to nucleoporin and the
CC complex is subsequently translocated through the pore by an energy
CC requiring, Ran-dependent mechanism (PubMed:11823430). At the
CC nucleoplasmic side of the NPC, Ran binds to the importin, the
CC importin/substrate complex dissociates and importin is re-exported from
CC the nucleus to the cytoplasm where GTP hydrolysis releases Ran
CC (PubMed:11823430). The directionality of nuclear import is thought to
CC be conferred by an asymmetric distribution of the GTP- and GDP-bound
CC forms of Ran between the cytoplasm and nucleus (PubMed:11823430).
CC Mediates the import of pre-assembled proteasomes into the nucleus;
CC AKIRIN2 acts as a molecular bridge between IPO9 and the proteasome
CC complex (PubMed:11823430, PubMed:34711951). Mediates the nuclear import
CC of histones H2A, H2B, H4 and H4 (PubMed:11823430, PubMed:30855230). In
CC addition to nuclear import, also acts as a chaperone for histones by
CC preventing inappropriate non-nucleosomal interactions
CC (PubMed:30855230). Mediates the nuclear import of actin (By
CC similarity). {ECO:0000250|UniProtKB:Q91YE6,
CC ECO:0000269|PubMed:11823430, ECO:0000269|PubMed:30855230,
CC ECO:0000269|PubMed:34711951}.
CC -!- SUBUNIT: Interacts with histones H2A, H2B, H3 and H4 (PubMed:11823430,
CC PubMed:30855230). The binding is coupled to RanGTP cycles
CC (PubMed:11823430). Interacts with AKIRIN2; promoting association with
CC pre-assembled proteasomes (PubMed:34711951). Associates with pre-
CC assembled proteasomes; interaction is indirect and mediated via
CC interaction with AKIRIN2 (PubMed:34711951). Interacts with PPP2R1A and
CC PPP2R1B (PubMed:12670497). {ECO:0000269|PubMed:11823430,
CC ECO:0000269|PubMed:12670497, ECO:0000269|PubMed:30855230,
CC ECO:0000269|PubMed:34711951}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11823430}. Nucleus
CC {ECO:0000269|PubMed:11823430}.
CC -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28951.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA86506.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91588.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB55181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC11173.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AF410465; AAL01416.1; -; mRNA.
DR EMBL; AL645504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK001264; BAA91588.1; ALT_INIT; mRNA.
DR EMBL; AK027532; BAB55181.1; ALT_INIT; mRNA.
DR EMBL; AK074740; BAC11173.1; ALT_INIT; mRNA.
DR EMBL; AK094603; BAC04383.1; ALT_SEQ; mRNA.
DR EMBL; CH471067; EAW91376.1; -; Genomic_DNA.
DR EMBL; BC003604; AAH03604.2; -; mRNA.
DR EMBL; AF161391; AAF28951.1; ALT_FRAME; mRNA.
DR EMBL; AL834323; CAD38991.1; -; mRNA.
DR EMBL; AB033018; BAA86506.1; ALT_INIT; mRNA.
DR CCDS; CCDS1415.1; -.
DR RefSeq; NP_060555.2; NM_018085.4.
DR PDB; 6N1Z; X-ray; 2.70 A; A/D=1-1041.
DR PDBsum; 6N1Z; -.
DR AlphaFoldDB; Q96P70; -.
DR SMR; Q96P70; -.
DR BioGRID; 120830; 168.
DR IntAct; Q96P70; 70.
DR MINT; Q96P70; -.
DR STRING; 9606.ENSP00000354742; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q96P70; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96P70; -.
DR MetOSite; Q96P70; -.
DR PhosphoSitePlus; Q96P70; -.
DR SwissPalm; Q96P70; -.
DR BioMuta; IPO9; -.
DR DMDM; 41688593; -.
DR EPD; Q96P70; -.
DR jPOST; Q96P70; -.
DR MassIVE; Q96P70; -.
DR MaxQB; Q96P70; -.
DR PaxDb; Q96P70; -.
DR PeptideAtlas; Q96P70; -.
DR PRIDE; Q96P70; -.
DR ProteomicsDB; 77644; -.
DR Antibodypedia; 34514; 169 antibodies from 29 providers.
DR DNASU; 55705; -.
DR Ensembl; ENST00000361565.9; ENSP00000354742.4; ENSG00000198700.10.
DR GeneID; 55705; -.
DR KEGG; hsa:55705; -.
DR MANE-Select; ENST00000361565.9; ENSP00000354742.4; NM_018085.5; NP_060555.2.
DR UCSC; uc001gwz.4; human.
DR CTD; 55705; -.
DR DisGeNET; 55705; -.
DR GeneCards; IPO9; -.
DR HGNC; HGNC:19425; IPO9.
DR HPA; ENSG00000198700; Low tissue specificity.
DR neXtProt; NX_Q96P70; -.
DR OpenTargets; ENSG00000198700; -.
DR PharmGKB; PA134930111; -.
DR VEuPathDB; HostDB:ENSG00000198700; -.
DR eggNOG; KOG2274; Eukaryota.
DR GeneTree; ENSGT00390000008224; -.
DR HOGENOM; CLU_008920_0_0_1; -.
DR InParanoid; Q96P70; -.
DR OMA; CLRAPPV; -.
DR OrthoDB; 546100at2759; -.
DR PhylomeDB; Q96P70; -.
DR TreeFam; TF323706; -.
DR PathwayCommons; Q96P70; -.
DR SignaLink; Q96P70; -.
DR BioGRID-ORCS; 55705; 478 hits in 1096 CRISPR screens.
DR ChiTaRS; IPO9; human.
DR GeneWiki; IPO9; -.
DR GenomeRNAi; 55705; -.
DR Pharos; Q96P70; Tbio.
DR PRO; PR:Q96P70; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96P70; protein.
DR Bgee; ENSG00000198700; Expressed in nipple and 210 other tissues.
DR ExpressionAtlas; Q96P70; baseline and differential.
DR Genevisible; Q96P70; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; IDA:UniProtKB.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0031144; P:proteasome localization; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW Nucleus; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT CHAIN 2..1041
FT /note="Importin-9"
FT /id="PRO_0000120754"
FT DOMAIN 43..119
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REGION 936..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..966
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT CONFLICT 632
FT /note="E -> G (in Ref. 4; BAC11173)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="K -> R (in Ref. 4; BAC11173)"
FT /evidence="ECO:0000305"
FT CONFLICT 935
FT /note="R -> P (in Ref. 4; BAB55181)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="E -> G (in Ref. 4; BAC11173)"
FT /evidence="ECO:0000305"
FT HELIX 16..32
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 71..88
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 122..139
FT /evidence="ECO:0007829|PDB:6N1Z"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 160..174
FT /evidence="ECO:0007829|PDB:6N1Z"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 182..198
FT /evidence="ECO:0007829|PDB:6N1Z"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 205..228
FT /evidence="ECO:0007829|PDB:6N1Z"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:6N1Z"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 262..278
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:6N1Z"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 287..308
FT /evidence="ECO:0007829|PDB:6N1Z"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 329..344
FT /evidence="ECO:0007829|PDB:6N1Z"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 350..367
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 372..380
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 382..388
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 398..412
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 414..437
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 444..456
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 458..466
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 474..480
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 482..486
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 492..504
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 511..525
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 531..550
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 554..560
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 561..572
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 577..590
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 595..600
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 602..615
FT /evidence="ECO:0007829|PDB:6N1Z"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 620..634
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 637..656
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 659..661
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 666..680
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 687..691
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 693..703
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 707..723
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 725..730
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 739..750
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 757..760
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 763..773
FT /evidence="ECO:0007829|PDB:6N1Z"
FT STRAND 774..776
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 780..795
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 799..815
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 817..825
FT /evidence="ECO:0007829|PDB:6N1Z"
FT STRAND 831..833
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 835..844
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 847..849
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 853..872
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 876..879
FT /evidence="ECO:0007829|PDB:6N1Z"
FT STRAND 882..884
FT /evidence="ECO:0007829|PDB:6N1Z"
FT STRAND 891..893
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 898..902
FT /evidence="ECO:0007829|PDB:6N1Z"
FT STRAND 910..912
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 913..932
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 998..1001
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 1004..1016
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 1021..1025
FT /evidence="ECO:0007829|PDB:6N1Z"
FT HELIX 1030..1037
FT /evidence="ECO:0007829|PDB:6N1Z"
SQ SEQUENCE 1041 AA; 115963 MW; A1842C357AEDFD90 CRC64;
MAAAAAAGAA SGLPGPVAQG LKEALVDTLT GILSPVQEVR AAAEEQIKVL EVTEEFGVHL
AELTVDPQGA LAIRQLASVI LKQYVETHWC AQSEKFRPPE TTERAKIVIR ELLPNGLRES
ISKVRSSVAY AVSAIAHWDW PEAWPQLFNL LMEMLVSGDL NAVHGAMRVL TEFTREVTDT
QMPLVAPVIL PEMYKIFTMA EVYGIRTRSR AVEIFTTCAH MICNMEELEK GAAKVLIFPV
VQQFTEAFVQ ALQIPDGPTS DSGFKMEVLK AVTALVKNFP KHMVSSMQQI LPIVWNTLTE
SAAFYVRTEV NYTEEVEDPV DSDGEVLGFE NLVFSIFEFV HALLENSKFK STVKKALPEL
IYYIILYMQI TEEQIKVWTA NPQQFVEDED DDTFSYTVRI AAQDLLLAVA TDFQNESAAA
LAAAATRHLQ EAEQTKNSGT EHWWKIHEAC MLALGSVKAI ITDSVKNGRI HFDMHGFLTN
VILADLNLSV SPFLLGRALW AASRFTVAMS PELIQQFLQA TVSGLHETQP PSVRISAVRA
IWGYCDQLKV SESTHVLQPF LPSILDGLIH LAAQFSSEVL NLVMETLCIV CTVDPEFTAS
MESKICPFTI AIFLKYSNDP VVASLAQDIF KELSQIEACQ GPMQMRLIPT LVSIMQAPAD
KIPAGLCATA IDILTTVVRN TKPPLSQLLI CQAFPAVAQC TLHTDDNATM QNGGECLRAY
VSVTLEQVAQ WHDEQGHNGL WYVMQVVSQL LDPRTSEFTA AFVGRLVSTL ISKAGRELGE
NLDQILRAIL SKMQQAETLS VMQSLIMVFA HLVHTQLEPL LEFLCSLPGP TGKPALEFVM
AEWTSRQHLF YGQYEGKVSS VALCKLLQHG INADDKRLQD IRVKGEEIYS MDEGIRTRSK
SAKNPERWTN IPLLVKILKL IINELSNVME ANAARQATPA EWSQDDSNDM WEDQEEEEEE
EEDGLAGQLL SDILATSKYE EDYYEDDEED DPDALKDPLY QIDLQAYLTD FLCQFAQQPC
YIMFSGHLND NERRVLQTIG I
