IPO5_HUMAN
ID IPO5_HUMAN Reviewed; 1097 AA.
AC O00410; B4DZA0; O15257; Q5T578; Q86XC7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Importin-5;
DE Short=Imp5;
DE AltName: Full=Importin subunit beta-3;
DE AltName: Full=Karyopherin beta-3;
DE AltName: Full=Ran-binding protein 5;
DE Short=RanBP5;
GN Name=IPO5; Synonyms=KPNB3, RANBP5;
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] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Bone marrow;
RX PubMed=9114010; DOI=10.1073/pnas.94.9.4451;
RA Yaseen N.R., Blobel G.;
RT "Cloning and characterization of human karyopherin beta3.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4451-4456(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=9271386; DOI=10.1128/mcb.17.9.5087;
RA Deane R., Schaeffer W., Zimmermann H.-P., Mueller L., Goerlich D.,
RA Prehn S., Ponstingl H., Bischoff F.R.;
RT "Ran-binding protein 5 (RanBP5) is related to the nuclear transport factor
RT importin-beta but interacts differently with RanBP1.";
RL Mol. Cell. Biol. 17:5087-5096(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lung, and Testis;
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 PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [8]
RP FUNCTION, NUCLEAR LOCALIZATION SIGNAL RECOGNITION, AND INTERACTION WITH
RP RPL23A; RPS7 AND RPL5.
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, 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 [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=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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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 [18]
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 [19]
RP INTERACTION WITH CPEB3.
RX PubMed=22730302; DOI=10.1093/nar/gks598;
RA Chao H.W., Lai Y.T., Lu Y.L., Lin C.L., Mai W., Huang Y.S.;
RT "NMDAR signaling facilitates the IPO5-mediated nuclear import of CPEB3.";
RL Nucleic Acids Res. 40:8484-8498(2012).
RN [20]
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=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 [21]
RP REPEAT STRUCTURE.
RX PubMed=23541588; DOI=10.1016/j.jmb.2013.02.035;
RA Kobayashi J., Matsuura Y.;
RT "Structural basis for cell-cycle-dependent nuclear import mediated by the
RT karyopherin Kap121p.";
RL J. Mol. Biol. 425:1852-1868(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, 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 [23]
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 [24]
RP INTERACTION WITH STX3 (ISOFORM 3).
RX PubMed=29475951; DOI=10.1074/jbc.ra117.000874;
RA Giovannone A.J., Winterstein C., Bhattaram P., Reales E., Low S.H.,
RA Baggs J.E., Xu M., Lalli M.A., Hogenesch J.B., Weimbs T.;
RT "Soluble syntaxin 3 functions as a transcriptional regulator.";
RL J. Biol. Chem. 293:5478-5491(2018).
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals (NLS) in
CC cargo substrates. Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) through
CC binding to nucleoporin 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 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. The
CC directionality of nuclear import is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran between
CC the cytoplasm and nucleus (By similarity). Mediates the nuclear import
CC of ribosomal proteins RPL23A, RPS7 and RPL5 (PubMed:9687515,
CC PubMed:11682607). In vitro, mediates nuclear import of H2A, H2B, H3 and
CC H4 histones. Binds to CPEB3 and mediates its nuclear import following
CC neuronal stimulation (By similarity). In case of HIV-1 infection, binds
CC and mediates the nuclear import of HIV-1 Rev.
CC {ECO:0000250|UniProtKB:Q8BKC5, ECO:0000269|PubMed:11682607,
CC ECO:0000269|PubMed:9687515}.
CC -!- SUBUNIT: Interacts with RPS7 and RPL5 (PubMed:9687515). Interacts with
CC RPL23A (via BIB domain) (PubMed:9687515, PubMed:11682607). Interacts
CC with H2A, H2B, H3 and H4 histones (By similarity). Interacts with
CC CPEB3; this mediates CPEB3 nuclear import following neuronal
CC stimulation which enhances the interaction in a RAN-regulated manner
CC (PubMed:22730302). Interacts with AIFM2; this interaction likely
CC mediates the translocation of AIFM2 into the nucleus upon oxidative
CC stress. Interacts with STX3 (isoform 3) (PubMed:29475951). Interacts
CC with SRP19 (PubMed:11682607). {ECO:0000250|UniProtKB:Q8BKC5,
CC ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:29475951,
CC ECO:0000269|PubMed:9687515}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Rev.
CC {ECO:0000269|PubMed:16704975}.
CC -!- INTERACTION:
CC O00410; Q96AP0: ACD; NbExp=2; IntAct=EBI-356424, EBI-717666;
CC O00410; O95166: GABARAP; NbExp=6; IntAct=EBI-356424, EBI-712001;
CC O00410; Q9H0R8: GABARAPL1; NbExp=4; IntAct=EBI-356424, EBI-746969;
CC O00410; P60520: GABARAPL2; NbExp=5; IntAct=EBI-356424, EBI-720116;
CC O00410; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-356424, EBI-373144;
CC O00410; Q9BXW4: MAP1LC3C; NbExp=2; IntAct=EBI-356424, EBI-2603996;
CC O00410; P18124: RPL7; NbExp=4; IntAct=EBI-356424, EBI-350806;
CC O00410; PRO_0000037576 [P27958]; Xeno; NbExp=5; IntAct=EBI-356424, EBI-8753518;
CC O00410-3; P42858: HTT; NbExp=3; IntAct=EBI-9641587, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus.
CC Note=Nucleus; nuclear rim. Found particularly in the nuclear rim and
CC nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O00410-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00410-2; Sequence=VSP_037587;
CC Name=3;
CC IsoId=O00410-3; Sequence=VSP_037774;
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA70103.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 3]:
CC Sequence=CAA70103.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U72761; AAC51317.1; -; mRNA.
DR EMBL; Y08890; CAA70103.1; ALT_FRAME; mRNA.
DR EMBL; AK302812; BAG64012.1; -; mRNA.
DR EMBL; AL137120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471085; EAX08980.1; -; Genomic_DNA.
DR EMBL; BC001497; AAH01497.1; -; mRNA.
DR EMBL; BC019309; AAH19309.1; -; mRNA.
DR EMBL; BC045640; AAH45640.1; -; mRNA.
DR CCDS; CCDS31999.1; -. [O00410-1]
DR RefSeq; NP_002262.3; NM_002271.4. [O00410-1]
DR RefSeq; XP_005254109.1; XM_005254052.3. [O00410-3]
DR RefSeq; XP_005254110.1; XM_005254053.3. [O00410-3]
DR RefSeq; XP_011519389.1; XM_011521087.2. [O00410-3]
DR RefSeq; XP_011519390.1; XM_011521088.2. [O00410-3]
DR RefSeq; XP_011519391.1; XM_011521089.2. [O00410-3]
DR RefSeq; XP_011519392.1; XM_011521090.2. [O00410-3]
DR RefSeq; XP_016876051.1; XM_017020562.1. [O00410-3]
DR PDB; 6XTE; X-ray; 2.27 A; A=4-1097.
DR PDB; 6XU2; X-ray; 2.83 A; A=1-1097.
DR PDBsum; 6XTE; -.
DR PDBsum; 6XU2; -.
DR AlphaFoldDB; O00410; -.
DR SMR; O00410; -.
DR BioGRID; 110041; 257.
DR DIP; DIP-41042N; -.
DR IntAct; O00410; 95.
DR MINT; O00410; -.
DR STRING; 9606.ENSP00000261574; -.
DR ChEMBL; CHEMBL4295647; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; O00410; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00410; -.
DR MetOSite; O00410; -.
DR PhosphoSitePlus; O00410; -.
DR SwissPalm; O00410; -.
DR BioMuta; IPO5; -.
DR CPTAC; CPTAC-226; -.
DR EPD; O00410; -.
DR jPOST; O00410; -.
DR MassIVE; O00410; -.
DR MaxQB; O00410; -.
DR PaxDb; O00410; -.
DR PeptideAtlas; O00410; -.
DR PRIDE; O00410; -.
DR ProteomicsDB; 47872; -. [O00410-1]
DR ProteomicsDB; 47873; -. [O00410-2]
DR ProteomicsDB; 47874; -. [O00410-3]
DR Antibodypedia; 3967; 187 antibodies from 30 providers.
DR DNASU; 3843; -.
DR Ensembl; ENST00000261574.10; ENSP00000261574.5; ENSG00000065150.21. [O00410-3]
DR Ensembl; ENST00000357602.7; ENSP00000350219.3; ENSG00000065150.21. [O00410-1]
DR Ensembl; ENST00000490680.5; ENSP00000418393.1; ENSG00000065150.21. [O00410-1]
DR Ensembl; ENST00000651721.2; ENSP00000499125.1; ENSG00000065150.21. [O00410-1]
DR GeneID; 3843; -.
DR KEGG; hsa:3843; -.
DR MANE-Select; ENST00000651721.2; ENSP00000499125.1; NM_002271.6; NP_002262.4.
DR UCSC; uc001vne.4; human. [O00410-1]
DR CTD; 3843; -.
DR DisGeNET; 3843; -.
DR GeneCards; IPO5; -.
DR HGNC; HGNC:6402; IPO5.
DR HPA; ENSG00000065150; Tissue enhanced (testis).
DR MIM; 602008; gene.
DR neXtProt; NX_O00410; -.
DR OpenTargets; ENSG00000065150; -.
DR PharmGKB; PA30193; -.
DR VEuPathDB; HostDB:ENSG00000065150; -.
DR eggNOG; KOG2171; Eukaryota.
DR GeneTree; ENSGT00940000155502; -.
DR HOGENOM; CLU_003794_0_0_1; -.
DR InParanoid; O00410; -.
DR OrthoDB; 90499at2759; -.
DR PhylomeDB; O00410; -.
DR TreeFam; TF300344; -.
DR PathwayCommons; O00410; -.
DR Reactome; R-HSA-192905; vRNP Assembly.
DR SignaLink; O00410; -.
DR SIGNOR; O00410; -.
DR BioGRID-ORCS; 3843; 120 hits in 1082 CRISPR screens.
DR ChiTaRS; IPO5; human.
DR GeneWiki; RANBP5; -.
DR GenomeRNAi; 3843; -.
DR Pharos; O00410; Tbio.
DR PRO; PR:O00410; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; O00410; protein.
DR Bgee; ENSG00000065150; Expressed in sperm and 212 other tissues.
DR ExpressionAtlas; O00410; baseline and differential.
DR Genevisible; O00410; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
DR GO; GO:0061608; F:nuclear import signal receptor activity; ISS:UniProtKB.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; TAS:ProtInc.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ARUK-UCL.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006610; P:ribosomal 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; IPR000357; HEAT.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR InterPro; IPR041653; Importin_rep_4.
DR InterPro; IPR040928; Importin_rep_5.
DR InterPro; IPR041389; Importin_rep_6.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF02985; HEAT; 1.
DR Pfam; PF18808; Importin_rep_4; 1.
DR Pfam; PF18816; Importin_rep_5; 1.
DR Pfam; PF18829; Importin_rep_6; 1.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..1097
FT /note="Importin-5"
FT /id="PRO_0000120771"
FT REPEAT 5..38
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT DOMAIN 28..99
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 43..77
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 95..122
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 130..157
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 167..201
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 210..246
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 254..289
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 298..350
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 352..386
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 390..430
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 432..472
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 475..523
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 525..568
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 570..615
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 617..692
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 695..737
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 741..780
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 787..853
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 856..895
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 903..935
FT /note="HEAT 20"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 943..983
FT /note="HEAT 21"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 990..1021
FT /note="HEAT 22"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 1032..1067
FT /note="HEAT 23"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 1070..1093
FT /note="HEAT 24"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REGION 325..375
FT /note="Ran-GTP binding"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037587"
FT VAR_SEQ 1
FT /note="M -> MPEDQVGKLEATENTISAM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9271386"
FT /id="VSP_037774"
FT VARIANT 286
FT /note="L -> I (in dbSNP:rs1053814)"
FT /id="VAR_012029"
FT VARIANT 525
FT /note="E -> K (in dbSNP:rs632729)"
FT /id="VAR_012030"
FT VARIANT 549
FT /note="E -> K (in dbSNP:rs484770)"
FT /id="VAR_012031"
FT VARIANT 905
FT /note="Y -> C (in dbSNP:rs1804740)"
FT /id="VAR_012032"
FT VARIANT 969
FT /note="T -> I (in dbSNP:rs1804741)"
FT /id="VAR_012033"
FT CONFLICT 538
FT /note="L -> R (in Ref. 6; AAH45640)"
FT /evidence="ECO:0000305"
FT CONFLICT 826..827
FT /note="ES -> GT (in Ref. 1; AAC51317)"
FT /evidence="ECO:0000305"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 56..72
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 83..99
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 103..118
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:6XU2"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 165..169
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 188..202
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 248..254
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 255..266
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 298..313
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:6XU2"
FT HELIX 335..350
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 352..367
FT /evidence="ECO:0007829|PDB:6XTE"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6XU2"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 390..396
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 397..406
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 413..429
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 433..451
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 456..471
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 482..502
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 507..523
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 524..530
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 531..544
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 551..568
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 570..589
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 601..615
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 616..622
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 623..634
FT /evidence="ECO:0007829|PDB:6XTE"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:6XU2"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:6XTE"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 663..665
FT /evidence="ECO:0007829|PDB:6XTE"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 675..691
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 693..696
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 700..707
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 709..712
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 717..737
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 739..757
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 763..780
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 787..814
FT /evidence="ECO:0007829|PDB:6XTE"
FT STRAND 815..817
FT /evidence="ECO:0007829|PDB:6XU2"
FT HELIX 822..853
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 854..857
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 858..861
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 862..864
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 865..871
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 878..894
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 898..905
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 907..913
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 919..935
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 938..940
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 941..956
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 958..961
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 963..965
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 966..982
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 984..986
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 989..999
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 1006..1021
FT /evidence="ECO:0007829|PDB:6XTE"
FT STRAND 1022..1024
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 1026..1028
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 1030..1032
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 1035..1043
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 1044..1047
FT /evidence="ECO:0007829|PDB:6XTE"
FT TURN 1052..1054
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 1057..1068
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 1072..1080
FT /evidence="ECO:0007829|PDB:6XTE"
FT HELIX 1084..1096
FT /evidence="ECO:0007829|PDB:6XTE"
SQ SEQUENCE 1097 AA; 123630 MW; 1864AD23513F2DE1 CRC64;
MAAAAAEQQQ FYLLLGNLLS PDNVVRKQAE ETYENIPGQS KITFLLQAIR NTTAAEEARQ
MAAVLLRRLL SSAFDEVYPA LPSDVQTAIK SELLMIIQME TQSSMRKKVC DIAAELARNL
IDEDGNNQWP EGLKFLFDSV SSQNVGLREA ALHIFWNFPG IFGNQQQHYL DVIKRMLVQC
MQDQEHPSIR TLSARATAAF ILANEHNVAL FKHFADLLPG FLQAVNDSCY QNDDSVLKSL
VEIADTVPKY LRPHLEATLQ LSLKLCGDTS LNNMQRQLAL EVIVTLSETA AAMLRKHTNI
VAQTIPQMLA MMVDLEEDED WANADELEDD DFDSNAVAGE SALDRMACGL GGKLVLPMIK
EHIMQMLQNP DWKYRHAGLM ALSAIGEGCH QQMEGILNEI VNFVLLFLQD PHPRVRYAAC
NAVGQMATDF APGFQKKFHE KVIAALLQTM EDQGNQRVQA HAAAALINFT EDCPKSLLIP
YLDNLVKHLH SIMVLKLQEL IQKGTKLVLE QVVTSIASVA DTAEEKFVPY YDLFMPSLKH
IVENAVQKEL RLLRGKTIEC ISLIGLAVGK EKFMQDASDV MQLLLKTQTD FNDMEDDDPQ
ISYMISAWAR MCKILGKEFQ QYLPVVMGPL MKTASIKPEV ALLDTQDMEN MSDDDGWEFV
NLGDQQSFGI KTAGLEEKST ACQMLVCYAK ELKEGFVEYT EQVVKLMVPL LKFYFHDGVR
VAAAESMPLL LECARVRGPE YLTQMWHFMC DALIKAIGTE PDSDVLSEIM HSFAKCIEVM
GDGCLNNEHF EELGGILKAK LEEHFKNQEL RQVKRQDEDY DEQVEESLQD EDDNDVYILT
KVSDILHSIF SSYKEKVLPW FEQLLPLIVN LICPHRPWPD RQWGLCIFDD VIEHCSPASF
KYAEYFLRPM LQYVCDNSPE VRQAAAYGLG VMAQYGGDNY RPFCTEALPL LVRVIQSADS
KTKENVNATE NCISAVGKIM KFKPDCVNVE EVLPHWLSWL PLHEDKEEAV QTFNYLCDLI
ESNHPIVLGP NNTNLPKIFS IIAEGEMHEA IKHEDPCAKR LANVVRQVQT SGGLWTECIA
QLSPEQQAAI QELLNSA
