ID TNPO1_HUMAN Reviewed; 898 AA. AC Q92973; B4DVC6; Q92957; Q92975; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 2. DT 27-MAR-2024, entry version 232. DE RecName: Full=Transportin-1; DE AltName: Full=Importin beta-2; DE AltName: Full=Karyopherin beta-2; DE AltName: Full=M9 region interaction protein; DE Short=MIP; GN Name=TNPO1; Synonyms=KPNB2, MIP1, TRN; 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). RX PubMed=8808633; DOI=10.1016/s0092-8674(00)80173-7; RA Pollard V.W., Michael W.M., Nakielny S., Siomi M.C., Wang F., Dreyfuss G.; RT "A novel receptor-mediated nuclear protein import pathway."; RL Cell 86:985-994(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Liver; RX PubMed=9144189; DOI=10.1073/pnas.94.10.5055; RA Bonifaci N., Moroianu J., Radu A., Blobel G.; RT "Karyopherin beta2 mediates nuclear import of a mRNA binding protein."; RL Proc. Natl. Acad. Sci. U.S.A. 94:5055-5060(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Fridell R.A., Thorne L.W., Benson R.E., Cullen B.R.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 FUNCTION. RX PubMed=8986607; DOI=10.1006/excr.1996.0369; RA Nakielny S., Siomi M.C., Siomi H., Michael W.M., Pollard V., Dreyfuss G.; RT "Transportin: nuclear transport receptor of a novel nuclear protein import RT pathway."; RL Exp. Cell Res. 229:261-266(1996). RN [8] RP INTERACTION WITH RAN. RX PubMed=9351834; DOI=10.1093/emboj/16.21.6535; RA Izaurralde E., Kutay U., von Kobbe C., Mattaj I.W., Goerlich D.; RT "The asymmetric distribution of the constituents of the Ran system is RT essential for transport into and out of the nucleus."; RL EMBO J. 16:6535-6547(1997). RN [9] RP SUBUNIT. RX PubMed=9428644; DOI=10.1016/s0014-5793(97)01467-1; RA Bischoff F.R., Goerlich D.; RT "RanBP1 is crucial for the release of RanGTP from importin beta-related RT nuclear transport factors."; RL FEBS Lett. 419:249-254(1997). RN [10] RP INTERACTION WITH HNRNPDL. RX PubMed=9524220; DOI=10.1016/s0167-4781(97)00223-6; RA Doi A., Shiosaka T., Takaoka Y., Yanagisawa K., Fujita S.; RT "Molecular cloning of the cDNA encoding A + U-rich element RNA binding RT factor."; RL Biochim. Biophys. Acta 1396:51-56(1998). RN [11] RP FUNCTION, AND INTERACTION WITH 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 [12] 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 [13] RP INTERACTION WITH HIV-1 REV, AND FUNCTION. 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 [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP INTERACTION WITH SNAI1 AND SNAI2. RX PubMed=19386897; DOI=10.1242/jcs.041749; RA Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.; RT "Characterization of Snail nuclear import pathways as representatives of RT C2H2 zinc finger transcription factors."; RL J. Cell Sci. 122:1452-1460(2009). RN [16] RP FUNCTION, AND INTERACTION WITH ADAR. RX PubMed=19124606; DOI=10.1128/mcb.01519-08; RA Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P., RA Jantsch M.F.; RT "RNA-regulated interaction of transportin-1 and exportin-5 with the double- RT stranded RNA-binding domain regulates nucleocytoplasmic shuttling of RT ADAR1."; RL Mol. Cell. Biol. 29:1487-1497(2009). 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 MET-1 (ISOFORM 2), AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [19] RP FUNCTION, INTERACTION WITH ADAR, AND MUTAGENESIS OF TRP-468 AND TRP-738. RX PubMed=24753571; DOI=10.1073/pnas.1323698111; RA Barraud P., Banerjee S., Mohamed W.I., Jantsch M.F., Allain F.H.; RT "A bimodular nuclear localization signal assembled via an extended double- RT stranded RNA-binding domain acts as an RNA-sensing signal for transportin RT 1."; RL Proc. Natl. Acad. Sci. U.S.A. 111:E1852-E1861(2014). RN [20] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH RAN, AND REPEAT RP STRUCTURE. RX PubMed=10353245; DOI=10.1038/20375; RA Chook Y.M., Blobel G.; RT "Structure of the nuclear transport complex karyopherin-beta2-Ran x RT GppNHp."; RL Nature 399:230-237(1999). CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport CC receptor. Serves as receptor for nuclear localization signals (NLS) in CC cargo substrates (PubMed:24753571). May 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). Involved in nuclear import CC of M9-containing proteins. In vitro, binds directly to the M9 region of CC the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and CC mediates their nuclear import. Involved in hnRNP A1/A2 nuclear export. CC Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 CC (PubMed:11682607). In vitro, mediates nuclear import of H2A, H2B, H3 CC and H4 histones (By similarity). In vitro, mediates nuclear import of CC SRP19 (PubMed:11682607). Mediates nuclear import of ADAR/ADAR1 isoform CC 1 and isoform 5 in a RanGTP-dependent manner (PubMed:19124606, CC PubMed:24753571). {ECO:0000250|UniProtKB:Q8BFY9, CC ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:19124606, CC ECO:0000269|PubMed:24753571, ECO:0000269|PubMed:8986607, CC ECO:0000269|PubMed:9687515}. CC -!- FUNCTION: (Microbial infection) In case of HIV-1 infection, binds and CC mediates the nuclear import of HIV-1 Rev. CC {ECO:0000269|PubMed:16704975}. CC -!- SUBUNIT: Identified in a complex that contains TNPO1, RAN and RANBP1 CC (PubMed:9428644). Binds HNRPA1, HNRPA2, HNRNPDL, RPS7, RPL5 and RAN. CC Interacts with H2A, H2B, H3 and H4 histones (By similarity). Interacts CC with isoform 1 and isoform 5 of ADAR/ADAR1 (via DRBM 3 domain) CC (PubMed:19124606, PubMed:24753571). Interacts with SNAI1 (via zinc CC fingers); the interaction mediates SNAI1 nuclear import CC (PubMed:19386897). Interacts with SNAI2 (via zinc fingers) CC (PubMed:19386897). Interacts with RPL23A (via BIB domain) and SRP19; CC this interaction is involved in RPL23A and SRP19 import into the CC nucleus (PubMed:11682607). {ECO:0000250|UniProtKB:Q8BFY9, CC ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:19124606, CC ECO:0000269|PubMed:19386897, ECO:0000269|PubMed:24753571, CC ECO:0000269|PubMed:9524220, ECO:0000269|PubMed:9687515}. CC -!- SUBUNIT: (Microbial infection) Binds to HIV-1 Rev. CC {ECO:0000269|PubMed:16704975}. CC -!- INTERACTION: CC Q92973; P62993: GRB2; NbExp=2; IntAct=EBI-286693, EBI-401755; CC Q92973; P09651-2: HNRNPA1; NbExp=2; IntAct=EBI-286693, EBI-352677; CC Q92973; P52272: HNRNPM; NbExp=3; IntAct=EBI-286693, EBI-486809; CC Q92973-2; P35637: FUS; NbExp=2; IntAct=EBI-11022821, EBI-400434; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q92973-1; Sequence=Displayed; CC Name=2; CC IsoId=Q92973-2; Sequence=VSP_038028; CC Name=3; CC IsoId=Q92973-3; Sequence=VSP_038029; CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-2 CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC50723.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH40340.1; 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; U70322; AAC50723.1; ALT_INIT; mRNA. DR EMBL; U72069; AAB58254.1; -; mRNA. DR EMBL; U72395; AAB68948.1; -; mRNA. DR EMBL; AK301021; BAG62638.1; -; mRNA. DR EMBL; BC040340; AAH40340.1; ALT_INIT; mRNA. DR CCDS; CCDS4016.1; -. [Q92973-2] DR CCDS; CCDS43329.1; -. [Q92973-1] DR CCDS; CCDS93732.1; -. [Q92973-3] DR RefSeq; NP_002261.3; NM_002270.3. [Q92973-1] DR RefSeq; NP_694858.1; NM_153188.2. [Q92973-2] DR RefSeq; XP_005248557.1; XM_005248500.2. DR PDB; 1QBK; X-ray; 3.00 A; B=9-898. DR PDB; 2H4M; X-ray; 3.05 A; A/B=376-898, A/B=9-343. DR PDB; 2OT8; X-ray; 3.10 A; A/B=9-331, A/B=375-898. DR PDB; 2QMR; X-ray; 3.00 A; A/B/C/D=9-898. DR PDB; 2Z5J; X-ray; 3.40 A; A=9-898. DR PDB; 2Z5K; X-ray; 2.60 A; A=9-898. DR PDB; 2Z5M; X-ray; 3.00 A; A=9-898. DR PDB; 2Z5N; X-ray; 3.20 A; A=9-898. DR PDB; 2Z5O; X-ray; 3.20 A; A=9-898. DR PDB; 4FDD; X-ray; 2.30 A; A=9-331, A=375-898. DR PDB; 4FQ3; X-ray; 3.00 A; A=9-898. DR PDB; 4JLQ; X-ray; 3.05 A; A=9-331, A=375-898. DR PDB; 4OO6; X-ray; 2.70 A; A=375-898, A=9-331. DR PDB; 5J3V; X-ray; 3.05 A; A/B=9-331, A/B=375-898. DR PDB; 5TQC; X-ray; 3.00 A; A=9-343, A=375-898. DR PDB; 5YVG; X-ray; 4.05 A; A/B=9-344, A/B=376-898. DR PDB; 5YVH; X-ray; 3.15 A; A=9-344, A=376-898. DR PDB; 5YVI; X-ray; 2.90 A; A=9-344, A=376-898. DR PDB; 7CYL; X-ray; 2.70 A; A=9-344, A=376-898. DR PDB; 7VPW; X-ray; 3.76 A; A=8-344, A=376-898. DR PDB; 8SGH; EM; 3.17 A; A=8-898. DR PDBsum; 1QBK; -. DR PDBsum; 2H4M; -. DR PDBsum; 2OT8; -. DR PDBsum; 2QMR; -. DR PDBsum; 2Z5J; -. DR PDBsum; 2Z5K; -. DR PDBsum; 2Z5M; -. DR PDBsum; 2Z5N; -. DR PDBsum; 2Z5O; -. DR PDBsum; 4FDD; -. DR PDBsum; 4FQ3; -. DR PDBsum; 4JLQ; -. DR PDBsum; 4OO6; -. DR PDBsum; 5J3V; -. DR PDBsum; 5TQC; -. DR PDBsum; 5YVG; -. DR PDBsum; 5YVH; -. DR PDBsum; 5YVI; -. DR PDBsum; 7CYL; -. DR PDBsum; 7VPW; -. DR PDBsum; 8SGH; -. DR AlphaFoldDB; Q92973; -. DR EMDB; EMD-40455; -. DR SMR; Q92973; -. DR BioGRID; 110040; 293. DR DIP; DIP-29335N; -. DR IntAct; Q92973; 73. DR MINT; Q92973; -. DR STRING; 9606.ENSP00000336712; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyGen; Q92973; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q92973; -. DR MetOSite; Q92973; -. DR PhosphoSitePlus; Q92973; -. DR SwissPalm; Q92973; -. DR BioMuta; TNPO1; -. DR DMDM; 259016171; -. DR EPD; Q92973; -. DR jPOST; Q92973; -. DR MassIVE; Q92973; -. DR MaxQB; Q92973; -. DR PaxDb; 9606-ENSP00000336712; -. DR PeptideAtlas; Q92973; -. DR ProteomicsDB; 75635; -. [Q92973-1] DR ProteomicsDB; 75636; -. [Q92973-2] DR ProteomicsDB; 75637; -. [Q92973-3] DR Pumba; Q92973; -. DR Antibodypedia; 4275; 318 antibodies from 30 providers. DR DNASU; 3842; -. DR Ensembl; ENST00000337273.10; ENSP00000336712.5; ENSG00000083312.19. [Q92973-1] DR Ensembl; ENST00000506351.6; ENSP00000425118.2; ENSG00000083312.19. [Q92973-2] DR Ensembl; ENST00000523768.5; ENSP00000428899.1; ENSG00000083312.19. [Q92973-3] DR GeneID; 3842; -. DR KEGG; hsa:3842; -. DR MANE-Select; ENST00000337273.10; ENSP00000336712.5; NM_002270.4; NP_002261.3. DR UCSC; uc003kci.5; human. [Q92973-1] DR AGR; HGNC:6401; -. DR CTD; 3842; -. DR DisGeNET; 3842; -. DR GeneCards; TNPO1; -. DR HGNC; HGNC:6401; TNPO1. DR HPA; ENSG00000083312; Low tissue specificity. DR MIM; 602901; gene. DR neXtProt; NX_Q92973; -. DR OpenTargets; ENSG00000083312; -. DR PharmGKB; PA30192; -. DR VEuPathDB; HostDB:ENSG00000083312; -. DR eggNOG; KOG2023; Eukaryota. DR GeneTree; ENSGT00940000155389; -. DR HOGENOM; CLU_008136_0_0_1; -. DR InParanoid; Q92973; -. DR OMA; XYMLQRT; -. DR OrthoDB; 276400at2759; -. DR PhylomeDB; Q92973; -. DR TreeFam; TF300825; -. DR PathwayCommons; Q92973; -. DR Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA. DR Reactome; R-HSA-5620924; Intraflagellar transport. DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation. DR SignaLink; Q92973; -. DR SIGNOR; Q92973; -. DR BioGRID-ORCS; 3842; 235 hits in 1184 CRISPR screens. DR ChiTaRS; TNPO1; human. DR EvolutionaryTrace; Q92973; -. DR GeneWiki; Transportin_1; -. DR GenomeRNAi; 3842; -. DR Pharos; Q92973; Tbio. DR PRO; PR:Q92973; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q92973; Protein. DR Bgee; ENSG00000083312; Expressed in corpus epididymis and 215 other cell types or tissues. DR ExpressionAtlas; Q92973; baseline and differential. DR GO; GO:0005929; C:cilium; TAS:Reactome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central. DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro. DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB. DR DisProt; DP01457; -. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2. DR IDEAL; IID00094; -. 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 PANTHER; PTHR10527; IMPORTIN BETA; 1. DR PANTHER; PTHR10527:SF21; TRANSPORTIN-1; 1. DR Pfam; PF02985; HEAT; 1. DR Pfam; PF13513; HEAT_EZ; 1. DR Pfam; PF03810; IBN_N; 1. DR SMART; SM00913; IBN_N; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50166; IMPORTIN_B_NT; 1. DR Genevisible; Q92973; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Host-virus interaction; Nucleus; Protein transport; Reference proteome; KW Repeat; Transport. FT CHAIN 1..898 FT /note="Transportin-1" FT /id="PRO_0000120765" FT REPEAT 19..46 FT /note="HEAT 1" FT /evidence="ECO:0000269|PubMed:10353245" FT DOMAIN 41..109 FT /note="Importin N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115" FT REPEAT 51..89 FT /note="HEAT 2" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 98..131 FT /note="HEAT 3" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 137..174 FT /note="HEAT 4" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 181..211 FT /note="HEAT 5" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 224..251 FT /note="HEAT 6" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 263..290 FT /note="HEAT 7" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 306..397 FT /note="HEAT 8" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 405..433 FT /note="HEAT 9" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 445..472 FT /note="HEAT 10" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 486..519 FT /note="HEAT 11" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 527..560 FT /note="HEAT 12" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 568..606 FT /note="HEAT 13" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 614..665 FT /note="HEAT 14" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 676..707 FT /note="HEAT 15" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 715..748 FT /note="HEAT 16" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 756..791 FT /note="HEAT 17" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 799..832 FT /note="HEAT 18" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 841..872 FT /note="HEAT 19" FT /evidence="ECO:0000269|PubMed:10353245" FT REPEAT 875..895 FT /note="HEAT 20" FT /evidence="ECO:0000269|PubMed:10353245" FT REGION 347..374 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 359..374 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 468 FT /note="Important for interaction with cargo nuclear FT localization signals" FT /evidence="ECO:0000269|PubMed:24753571" FT SITE 738 FT /note="Important for interaction with cargo nuclear FT localization signals" FT /evidence="ECO:0000269|PubMed:24753571" FT VAR_SEQ 1..9 FT /note="MVWDRQTKM -> M (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9144189, ECO:0000303|Ref.3" FT /id="VSP_038028" FT VAR_SEQ 69..118 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038029" FT MUTAGEN 468 FT /note="W->A: Abolishes interaction with the ADAR nuclear FT localization signal. Abolishes ADAR nuclear import." FT /evidence="ECO:0000269|PubMed:24753571" FT MUTAGEN 738 FT /note="W->A: Abolishes interaction with the ADAR nuclear FT localization signal. Abolishes ADAR nuclear import." FT /evidence="ECO:0000269|PubMed:24753571" FT CONFLICT 104 FT /note="L -> S (in Ref. 3; AAB68948)" FT /evidence="ECO:0000305" FT CONFLICT 225 FT /note="I -> T (in Ref. 1; AAC50723)" FT /evidence="ECO:0000305" FT CONFLICT 669 FT /note="Q -> L (in Ref. 3; AAB68948)" FT /evidence="ECO:0000305" FT CONFLICT 880 FT /note="F -> L (in Ref. 4; BAG62638)" FT /evidence="ECO:0000305" FT HELIX 17..30 FT /evidence="ECO:0007829|PDB:4FDD" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:2H4M" FT HELIX 35..48 FT /evidence="ECO:0007829|PDB:4FDD" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:2QMR" FT HELIX 52..63 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 70..83 FT /evidence="ECO:0007829|PDB:4FDD" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 93..104 FT /evidence="ECO:0007829|PDB:4FDD" FT TURN 105..108 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 112..128 FT /evidence="ECO:0007829|PDB:4FDD" FT TURN 129..133 FT /evidence="ECO:0007829|PDB:4FDD" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:4FQ3" FT HELIX 137..145 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:1QBK" FT HELIX 150..167 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 170..173 FT /evidence="ECO:0007829|PDB:4FDD" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 180..187 FT /evidence="ECO:0007829|PDB:4FDD" FT TURN 188..192 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 196..207 FT /evidence="ECO:0007829|PDB:4FDD" FT TURN 208..213 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 215..218 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 221..232 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 237..253 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 255..258 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 262..273 FT /evidence="ECO:0007829|PDB:4FDD" FT STRAND 275..277 FT /evidence="ECO:0007829|PDB:2OT8" FT HELIX 278..291 FT /evidence="ECO:0007829|PDB:4FDD" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:2Z5K" FT HELIX 297..301 FT /evidence="ECO:0007829|PDB:4FDD" FT TURN 302..304 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 305..315 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 320..327 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 340..342 FT /evidence="ECO:0007829|PDB:1QBK" FT HELIX 367..370 FT /evidence="ECO:0007829|PDB:1QBK" FT HELIX 372..379 FT /evidence="ECO:0007829|PDB:8SGH" FT HELIX 383..398 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 399..402 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 403..414 FT /evidence="ECO:0007829|PDB:4FDD" FT STRAND 416..418 FT /evidence="ECO:0007829|PDB:1QBK" FT HELIX 419..431 FT /evidence="ECO:0007829|PDB:4FDD" FT TURN 432..436 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 437..440 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 441..443 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 444..454 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 460..472 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 474..479 FT /evidence="ECO:0007829|PDB:4FDD" FT TURN 482..485 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 486..497 FT /evidence="ECO:0007829|PDB:4FDD" FT STRAND 498..500 FT /evidence="ECO:0007829|PDB:1QBK" FT HELIX 502..519 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 520..526 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 527..540 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 543..560 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 561..564 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 567..583 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 591..605 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 606..612 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 613..636 FT /evidence="ECO:0007829|PDB:4FDD" FT TURN 638..640 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 647..663 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 664..667 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 668..672 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 676..683 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 689..705 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 707..709 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 711..713 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 714..723 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 727..729 FT /evidence="ECO:0007829|PDB:4OO6" FT HELIX 730..747 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 748..755 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 756..766 FT /evidence="ECO:0007829|PDB:4FDD" FT STRAND 768..770 FT /evidence="ECO:0007829|PDB:5TQC" FT HELIX 773..789 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 791..794 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 795..797 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 798..810 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 816..831 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 833..835 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 837..839 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 840..848 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 855..880 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 881..883 FT /evidence="ECO:0007829|PDB:4FDD" FT HELIX 886..894 FT /evidence="ECO:0007829|PDB:4FDD" FT MOD_RES Q92973-2:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" SQ SEQUENCE 898 AA; 102355 MW; 7B880D9E7CA6798F CRC64; MVWDRQTKME YEWKPDEQGL QQILQLLKES QSPDTTIQRT VQQKLEQLNQ YPDFNNYLIF VLTKLKSEDE PTRSLSGLIL KNNVKAHFQN FPNGVTDFIK SECLNNIGDS SPLIRATVGI LITTIASKGE LQNWPDLLPK LCSLLDSEDY NTCEGAFGAL QKICEDSAEI LDSDVLDRPL NIMIPKFLQF FKHSSPKIRS HAVACVNQFI ISRTQALMLH IDSFIENLFA LAGDEEPEVR KNVCRALVML LEVRMDRLLP HMHNIVEYML QRTQDQDENV ALEACEFWLT LAEQPICKDV LVRHLPKLIP VLVNGMKYSD IDIILLKGDV EEDETIPDSE QDIRPRFHRS RTVAQQHDED GIEEEDDDDD EIDDDDTISD WNLRKCSAAA LDVLANVYRD ELLPHILPLL KELLFHHEWV VKESGILVLG AIAEGCMQGM IPYLPELIPH LIQCLSDKKA LVRSITCWTL SRYAHWVVSQ PPDTYLKPLM TELLKRILDS NKRVQEAACS AFATLEEEAC TELVPYLAYI LDTLVFAFSK YQHKNLLILY DAIGTLADSV GHHLNKPEYI QMLMPPLIQK WNMLKDEDKD LFPLLECLSS VATALQSGFL PYCEPVYQRC VNLVQKTLAQ AMLNNAQPDQ YEAPDKDFMI VALDLLSGLA EGLGGNIEQL VARSNILTLM YQCMQDKMPE VRQSSFALLG DLTKACFQHV KPCIADFMPI LGTNLNPEFI SVCNNATWAI GEISIQMGIE MQPYIPMVLH QLVEIINRPN TPKTLLENTA ITIGRLGYVC PQEVAPMLQQ FIRPWCTSLR NIRDNEEKDS AFRGICTMIS VNPSGVIQDF IFFCDAVASW INPKDDLRDM FCKILHGFKN QVGDENWRRF SDQFPLPLKE RLAAFYGV //