TNPO1_HUMAN
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 03-AUG-2022, entry version 223.
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};
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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 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 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 AlphaFoldDB; Q92973; -.
DR SMR; Q92973; -.
DR BioGRID; 110040; 173.
DR DIP; DIP-29335N; -.
DR IntAct; Q92973; 69.
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; Q92973; -.
DR PeptideAtlas; Q92973; -.
DR PRIDE; Q92973; -.
DR ProteomicsDB; 75635; -. [Q92973-1]
DR ProteomicsDB; 75636; -. [Q92973-2]
DR ProteomicsDB; 75637; -. [Q92973-3]
DR Antibodypedia; 4275; 296 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 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; MFPLLEC; -.
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; 203 hits in 1098 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 213 other tissues.
DR ExpressionAtlas; Q92973; baseline and differential.
DR Genevisible; Q92973; HS.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
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; -; 2.
DR IDEAL; IID00094; -.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR PANTHER; PTHR10527; PTHR10527; 1.
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; 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 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
