Full text data of TNPO1
TNPO1
(KPNB2, MIP1, TRN)
[Confidence: low (only semi-automatic identification from reviews)]
Transportin-1 (Importin beta-2; Karyopherin beta-2; M9 region interaction protein; MIP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transportin-1 (Importin beta-2; Karyopherin beta-2; M9 region interaction protein; MIP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q92973
ID TNPO1_HUMAN Reviewed; 898 AA.
AC Q92973; B4DVC6; Q92957; Q92975;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 144.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA 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
RT project: 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.,
RA Dreyfuss G.;
RT "Transportin: nuclear transport receptor of a novel nuclear protein
RT import pathway.";
RL Exp. Cell Res. 229:261-266(1996).
RN [8]
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 [9]
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
RT of ribosomal proteins in mammalian cells.";
RL EMBO J. 17:4491-4502(1998).
RN [10]
RP FUNCTION, AND INTERACTION WITH SRP19.
RX PubMed=11682607;
RA Dean K.A., von Ahsen O., Goerlich D., Fried H.M.;
RT "Signal recognition particle protein 19 is imported into the nucleus
RT by importin 8 (RanBP8) and transportin.";
RL J. Cell Sci. 114:3479-3485(2001).
RN [11]
RP INTERACTION WITH HIV-1 REV.
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
RT Rev protein of human immunodeficiency virus type 1.";
RL J. Biol. Chem. 281:20883-20890(2006).
RN [12]
RP IDENTIFICATION 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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
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
RT of C2H2 zinc finger transcription factors.";
RL J. Cell Sci. 122:1452-1460(2009).
RN [14]
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
RT double-stranded RNA-binding domain regulates nucleocytoplasmic
RT shuttling of ADAR1.";
RL Mol. Cell. Biol. 29:1487-1497(2009).
RN [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH RAN.
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
CC (NLS) in cargo substrates. Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC)
CC through binding to nucleoporin and the complex is subsequently
CC translocated through the pore by an energy requiring, Ran-
CC dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC binds to the importin, the importin/substrate complex dissociates
CC and importin is re-exported from the nucleus to the cytoplasm
CC where GTP hydrolysis releases Ran. The directionality of nuclear
CC import is thought to be conferred by an asymmetric distribution of
CC the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus (By similarity). Involved in nuclear import of M9-
CC containing proteins. In vitro, binds directly to the M9 region of
CC the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2
CC and mediates their nuclear import. Appears also to be involved in
CC hnRNP A1/A2 nuclear export. Mediates the nuclear import of
CC ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like
CC import receptor binding (BIB) domain of RPL23A. In vitro, mediates
CC nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. In case
CC of HIV-1 infection, binds and mediates the nuclear import of HIV-1
CC Rev. Mediates nuclear import of ADAR/ADAR1 (isoform 5) in a
CC RanGTP-dependent manner.
CC -!- SUBUNIT: Binds HNRPA1, HNRPA2, HNRNPDL, RPL23A, RPS7, RPL5, RAN
CC and SRP19. Interacts with H2A, H2B, H3 and H4 histones. Binds to
CC HIV-1 Rev. Interacts with isoform 5 of ADAR/ADAR1 (via DRBM 3
CC domain). Interacts with SNAI1 (via zinc fingers); the interaction
CC mediates SNAI1 nuclear import. Interacts with SNAI2 (via zinc
CC fingers).
CC -!- INTERACTION:
CC P62993:GRB2; NbExp=2; IntAct=EBI-286693, EBI-401755;
CC P62826:RAN; NbExp=2; IntAct=EBI-286693, EBI-286642;
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.
CC -!- SIMILARITY: Contains 8 HEAT repeats.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50723.1; Type=Erroneous initiation;
CC Sequence=AAH40340.1; Type=Erroneous initiation;
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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 RefSeq; NP_002261.3; NM_002270.3.
DR RefSeq; NP_694858.1; NM_153188.2.
DR RefSeq; XP_005248557.1; XM_005248500.1.
DR UniGene; Hs.482497; -.
DR PDB; 1QBK; X-ray; 3.00 A; B=9-898.
DR PDB; 2H4M; X-ray; 3.05 A; A/B=9-898.
DR PDB; 2OT8; X-ray; 3.10 A; A/B=9-890.
DR PDB; 2QMR; X-ray; 3.00 A; A/B/C/D=9-898.
DR PDB; 2Z5J; X-ray; 3.40 A; A=9-890.
DR PDB; 2Z5K; X-ray; 2.60 A; A=9-890.
DR PDB; 2Z5M; X-ray; 3.00 A; A=9-890.
DR PDB; 2Z5N; X-ray; 3.20 A; A=9-890.
DR PDB; 2Z5O; X-ray; 3.20 A; A=9-890.
DR PDB; 4FDD; X-ray; 2.30 A; A=9-898.
DR PDB; 4FQ3; X-ray; 3.00 A; A=9-898.
DR PDB; 4JLQ; X-ray; 3.04 A; A=9-898.
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 ProteinModelPortal; Q92973; -.
DR SMR; Q92973; 11-897.
DR DIP; DIP-29335N; -.
DR IntAct; Q92973; 18.
DR MINT; MINT-94165; -.
DR STRING; 9606.ENSP00000336712; -.
DR PhosphoSite; Q92973; -.
DR DMDM; 259016171; -.
DR PaxDb; Q92973; -.
DR PRIDE; Q92973; -.
DR DNASU; 3842; -.
DR Ensembl; ENST00000337273; ENSP00000336712; ENSG00000083312.
DR Ensembl; ENST00000454282; ENSP00000398524; ENSG00000083312.
DR Ensembl; ENST00000506351; ENSP00000425118; ENSG00000083312.
DR Ensembl; ENST00000523768; ENSP00000428899; ENSG00000083312.
DR GeneID; 3842; -.
DR KEGG; hsa:3842; -.
DR UCSC; uc003kcg.4; human.
DR CTD; 3842; -.
DR GeneCards; GC05P072148; -.
DR HGNC; HGNC:6401; TNPO1.
DR HPA; CAB016325; -.
DR MIM; 602901; gene.
DR neXtProt; NX_Q92973; -.
DR PharmGKB; PA30192; -.
DR eggNOG; COG5215; -.
DR HOGENOM; HOG000203940; -.
DR HOVERGEN; HBG058963; -.
DR InParanoid; Q92973; -.
DR OMA; EEDIKPR; -.
DR OrthoDB; EOG7XM2X0; -.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; TNPO1; human.
DR EvolutionaryTrace; Q92973; -.
DR GeneWiki; Transportin_1; -.
DR GenomeRNAi; 3842; -.
DR NextBio; 15119; -.
DR PRO; PR:Q92973; -.
DR ArrayExpress; Q92973; -.
DR Bgee; Q92973; -.
DR CleanEx; HS_TNPO1; -.
DR Genevestigator; Q92973; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0008139; F:nuclear localization sequence binding; TAS:ProtInc.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0000060; P:protein import into nucleus, translocation; TAS:ProtInc.
DR Gene3D; 1.25.10.10; -; 2.
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; PS50077; HEAT_REPEAT; FALSE_NEG.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Host-virus interaction; Nucleus; Polymorphism; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1 898 Transportin-1.
FT /FTId=PRO_0000120765.
FT DOMAIN 41 109 Importin N-terminal.
FT REPEAT 132 169 HEAT 1.
FT REPEAT 178 215 HEAT 2.
FT REPEAT 219 256 HEAT 3.
FT REPEAT 401 438 HEAT 4.
FT REPEAT 442 479 HEAT 5.
FT REPEAT 484 521 HEAT 6.
FT REPEAT 568 607 HEAT 7.
FT REPEAT 671 708 HEAT 8.
FT COMPBIAS 358 376 Asp/Glu-rich (acidic).
FT VAR_SEQ 1 9 MVWDRQTKM -> M (in isoform 2).
FT /FTId=VSP_038028.
FT VAR_SEQ 69 118 Missing (in isoform 3).
FT /FTId=VSP_038029.
FT VARIANT 34 34 D -> E (in dbSNP:rs25661).
FT /FTId=VAR_014455.
FT CONFLICT 104 104 L -> S (in Ref. 3; AAB68948).
FT CONFLICT 225 225 I -> T (in Ref. 1; AAC50723).
FT CONFLICT 669 669 Q -> L (in Ref. 3; AAB68948).
FT CONFLICT 880 880 F -> L (in Ref. 4; BAG62638).
FT HELIX 17 30
FT STRAND 31 33
FT HELIX 35 48
FT STRAND 49 51
FT HELIX 52 63
FT HELIX 70 83
FT TURN 84 86
FT HELIX 88 90
FT HELIX 93 104
FT TURN 105 108
FT HELIX 112 128
FT TURN 129 133
FT STRAND 134 136
FT HELIX 137 145
FT HELIX 147 149
FT HELIX 150 167
FT HELIX 170 173
FT STRAND 175 178
FT HELIX 180 187
FT TURN 188 192
FT HELIX 196 207
FT TURN 208 213
FT HELIX 215 218
FT HELIX 221 232
FT HELIX 237 253
FT HELIX 255 258
FT HELIX 259 261
FT HELIX 262 273
FT STRAND 275 277
FT HELIX 278 291
FT STRAND 294 296
FT HELIX 297 301
FT TURN 302 304
FT HELIX 305 315
FT HELIX 320 327
FT HELIX 340 342
FT HELIX 367 370
FT HELIX 383 398
FT HELIX 399 402
FT HELIX 403 414
FT STRAND 416 418
FT HELIX 419 431
FT TURN 432 436
FT HELIX 437 440
FT HELIX 441 443
FT HELIX 444 454
FT HELIX 460 472
FT HELIX 474 479
FT TURN 482 485
FT HELIX 486 497
FT STRAND 498 500
FT HELIX 502 519
FT HELIX 520 526
FT HELIX 527 540
FT HELIX 543 560
FT HELIX 561 564
FT HELIX 567 583
FT HELIX 591 605
FT HELIX 606 612
FT HELIX 613 636
FT TURN 638 640
FT HELIX 647 663
FT HELIX 664 667
FT HELIX 668 672
FT HELIX 676 683
FT HELIX 689 705
FT HELIX 707 709
FT HELIX 711 713
FT HELIX 714 723
FT HELIX 727 729
FT HELIX 730 747
FT HELIX 748 755
FT HELIX 756 766
FT STRAND 768 770
FT HELIX 773 789
FT HELIX 791 794
FT HELIX 795 797
FT HELIX 798 810
FT HELIX 816 831
FT HELIX 833 835
FT HELIX 837 839
FT HELIX 840 848
FT HELIX 855 880
FT HELIX 881 883
FT HELIX 886 894
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
//
ID TNPO1_HUMAN Reviewed; 898 AA.
AC Q92973; B4DVC6; Q92957; Q92975;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 144.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA 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
RT project: 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.,
RA Dreyfuss G.;
RT "Transportin: nuclear transport receptor of a novel nuclear protein
RT import pathway.";
RL Exp. Cell Res. 229:261-266(1996).
RN [8]
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 [9]
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
RT of ribosomal proteins in mammalian cells.";
RL EMBO J. 17:4491-4502(1998).
RN [10]
RP FUNCTION, AND INTERACTION WITH SRP19.
RX PubMed=11682607;
RA Dean K.A., von Ahsen O., Goerlich D., Fried H.M.;
RT "Signal recognition particle protein 19 is imported into the nucleus
RT by importin 8 (RanBP8) and transportin.";
RL J. Cell Sci. 114:3479-3485(2001).
RN [11]
RP INTERACTION WITH HIV-1 REV.
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
RT Rev protein of human immunodeficiency virus type 1.";
RL J. Biol. Chem. 281:20883-20890(2006).
RN [12]
RP IDENTIFICATION 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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
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
RT of C2H2 zinc finger transcription factors.";
RL J. Cell Sci. 122:1452-1460(2009).
RN [14]
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
RT double-stranded RNA-binding domain regulates nucleocytoplasmic
RT shuttling of ADAR1.";
RL Mol. Cell. Biol. 29:1487-1497(2009).
RN [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH RAN.
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
CC (NLS) in cargo substrates. Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC)
CC through binding to nucleoporin and the complex is subsequently
CC translocated through the pore by an energy requiring, Ran-
CC dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC binds to the importin, the importin/substrate complex dissociates
CC and importin is re-exported from the nucleus to the cytoplasm
CC where GTP hydrolysis releases Ran. The directionality of nuclear
CC import is thought to be conferred by an asymmetric distribution of
CC the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus (By similarity). Involved in nuclear import of M9-
CC containing proteins. In vitro, binds directly to the M9 region of
CC the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2
CC and mediates their nuclear import. Appears also to be involved in
CC hnRNP A1/A2 nuclear export. Mediates the nuclear import of
CC ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like
CC import receptor binding (BIB) domain of RPL23A. In vitro, mediates
CC nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. In case
CC of HIV-1 infection, binds and mediates the nuclear import of HIV-1
CC Rev. Mediates nuclear import of ADAR/ADAR1 (isoform 5) in a
CC RanGTP-dependent manner.
CC -!- SUBUNIT: Binds HNRPA1, HNRPA2, HNRNPDL, RPL23A, RPS7, RPL5, RAN
CC and SRP19. Interacts with H2A, H2B, H3 and H4 histones. Binds to
CC HIV-1 Rev. Interacts with isoform 5 of ADAR/ADAR1 (via DRBM 3
CC domain). Interacts with SNAI1 (via zinc fingers); the interaction
CC mediates SNAI1 nuclear import. Interacts with SNAI2 (via zinc
CC fingers).
CC -!- INTERACTION:
CC P62993:GRB2; NbExp=2; IntAct=EBI-286693, EBI-401755;
CC P62826:RAN; NbExp=2; IntAct=EBI-286693, EBI-286642;
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.
CC -!- SIMILARITY: Contains 8 HEAT repeats.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50723.1; Type=Erroneous initiation;
CC Sequence=AAH40340.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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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 RefSeq; NP_002261.3; NM_002270.3.
DR RefSeq; NP_694858.1; NM_153188.2.
DR RefSeq; XP_005248557.1; XM_005248500.1.
DR UniGene; Hs.482497; -.
DR PDB; 1QBK; X-ray; 3.00 A; B=9-898.
DR PDB; 2H4M; X-ray; 3.05 A; A/B=9-898.
DR PDB; 2OT8; X-ray; 3.10 A; A/B=9-890.
DR PDB; 2QMR; X-ray; 3.00 A; A/B/C/D=9-898.
DR PDB; 2Z5J; X-ray; 3.40 A; A=9-890.
DR PDB; 2Z5K; X-ray; 2.60 A; A=9-890.
DR PDB; 2Z5M; X-ray; 3.00 A; A=9-890.
DR PDB; 2Z5N; X-ray; 3.20 A; A=9-890.
DR PDB; 2Z5O; X-ray; 3.20 A; A=9-890.
DR PDB; 4FDD; X-ray; 2.30 A; A=9-898.
DR PDB; 4FQ3; X-ray; 3.00 A; A=9-898.
DR PDB; 4JLQ; X-ray; 3.04 A; A=9-898.
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 ProteinModelPortal; Q92973; -.
DR SMR; Q92973; 11-897.
DR DIP; DIP-29335N; -.
DR IntAct; Q92973; 18.
DR MINT; MINT-94165; -.
DR STRING; 9606.ENSP00000336712; -.
DR PhosphoSite; Q92973; -.
DR DMDM; 259016171; -.
DR PaxDb; Q92973; -.
DR PRIDE; Q92973; -.
DR DNASU; 3842; -.
DR Ensembl; ENST00000337273; ENSP00000336712; ENSG00000083312.
DR Ensembl; ENST00000454282; ENSP00000398524; ENSG00000083312.
DR Ensembl; ENST00000506351; ENSP00000425118; ENSG00000083312.
DR Ensembl; ENST00000523768; ENSP00000428899; ENSG00000083312.
DR GeneID; 3842; -.
DR KEGG; hsa:3842; -.
DR UCSC; uc003kcg.4; human.
DR CTD; 3842; -.
DR GeneCards; GC05P072148; -.
DR HGNC; HGNC:6401; TNPO1.
DR HPA; CAB016325; -.
DR MIM; 602901; gene.
DR neXtProt; NX_Q92973; -.
DR PharmGKB; PA30192; -.
DR eggNOG; COG5215; -.
DR HOGENOM; HOG000203940; -.
DR HOVERGEN; HBG058963; -.
DR InParanoid; Q92973; -.
DR OMA; EEDIKPR; -.
DR OrthoDB; EOG7XM2X0; -.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; TNPO1; human.
DR EvolutionaryTrace; Q92973; -.
DR GeneWiki; Transportin_1; -.
DR GenomeRNAi; 3842; -.
DR NextBio; 15119; -.
DR PRO; PR:Q92973; -.
DR ArrayExpress; Q92973; -.
DR Bgee; Q92973; -.
DR CleanEx; HS_TNPO1; -.
DR Genevestigator; Q92973; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0008139; F:nuclear localization sequence binding; TAS:ProtInc.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0000060; P:protein import into nucleus, translocation; TAS:ProtInc.
DR Gene3D; 1.25.10.10; -; 2.
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; PS50077; HEAT_REPEAT; FALSE_NEG.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Host-virus interaction; Nucleus; Polymorphism; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1 898 Transportin-1.
FT /FTId=PRO_0000120765.
FT DOMAIN 41 109 Importin N-terminal.
FT REPEAT 132 169 HEAT 1.
FT REPEAT 178 215 HEAT 2.
FT REPEAT 219 256 HEAT 3.
FT REPEAT 401 438 HEAT 4.
FT REPEAT 442 479 HEAT 5.
FT REPEAT 484 521 HEAT 6.
FT REPEAT 568 607 HEAT 7.
FT REPEAT 671 708 HEAT 8.
FT COMPBIAS 358 376 Asp/Glu-rich (acidic).
FT VAR_SEQ 1 9 MVWDRQTKM -> M (in isoform 2).
FT /FTId=VSP_038028.
FT VAR_SEQ 69 118 Missing (in isoform 3).
FT /FTId=VSP_038029.
FT VARIANT 34 34 D -> E (in dbSNP:rs25661).
FT /FTId=VAR_014455.
FT CONFLICT 104 104 L -> S (in Ref. 3; AAB68948).
FT CONFLICT 225 225 I -> T (in Ref. 1; AAC50723).
FT CONFLICT 669 669 Q -> L (in Ref. 3; AAB68948).
FT CONFLICT 880 880 F -> L (in Ref. 4; BAG62638).
FT HELIX 17 30
FT STRAND 31 33
FT HELIX 35 48
FT STRAND 49 51
FT HELIX 52 63
FT HELIX 70 83
FT TURN 84 86
FT HELIX 88 90
FT HELIX 93 104
FT TURN 105 108
FT HELIX 112 128
FT TURN 129 133
FT STRAND 134 136
FT HELIX 137 145
FT HELIX 147 149
FT HELIX 150 167
FT HELIX 170 173
FT STRAND 175 178
FT HELIX 180 187
FT TURN 188 192
FT HELIX 196 207
FT TURN 208 213
FT HELIX 215 218
FT HELIX 221 232
FT HELIX 237 253
FT HELIX 255 258
FT HELIX 259 261
FT HELIX 262 273
FT STRAND 275 277
FT HELIX 278 291
FT STRAND 294 296
FT HELIX 297 301
FT TURN 302 304
FT HELIX 305 315
FT HELIX 320 327
FT HELIX 340 342
FT HELIX 367 370
FT HELIX 383 398
FT HELIX 399 402
FT HELIX 403 414
FT STRAND 416 418
FT HELIX 419 431
FT TURN 432 436
FT HELIX 437 440
FT HELIX 441 443
FT HELIX 444 454
FT HELIX 460 472
FT HELIX 474 479
FT TURN 482 485
FT HELIX 486 497
FT STRAND 498 500
FT HELIX 502 519
FT HELIX 520 526
FT HELIX 527 540
FT HELIX 543 560
FT HELIX 561 564
FT HELIX 567 583
FT HELIX 591 605
FT HELIX 606 612
FT HELIX 613 636
FT TURN 638 640
FT HELIX 647 663
FT HELIX 664 667
FT HELIX 668 672
FT HELIX 676 683
FT HELIX 689 705
FT HELIX 707 709
FT HELIX 711 713
FT HELIX 714 723
FT HELIX 727 729
FT HELIX 730 747
FT HELIX 748 755
FT HELIX 756 766
FT STRAND 768 770
FT HELIX 773 789
FT HELIX 791 794
FT HELIX 795 797
FT HELIX 798 810
FT HELIX 816 831
FT HELIX 833 835
FT HELIX 837 839
FT HELIX 840 848
FT HELIX 855 880
FT HELIX 881 883
FT HELIX 886 894
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
//
MIM
602901
*RECORD*
*FIELD* NO
602901
*FIELD* TI
*602901 TRANSPORTIN 1; TNPO1
;;TRANSPORTIN;;
KARYOPHERIN BETA-2; KPNB2;;
M9-INTERACTING PROTEIN; MIP1;;
read moreIMPORTIN BETA-2
*FIELD* TX
CLONING
Targeting of most nuclear proteins to the cell nucleus is initiated by
interaction between the protein's nuclear localization signal (NLS) and
the importin, or karyopherin, receptor complex. An importin heterodimer
recognizes the NLS protein in the cytoplasm via its alpha subunit and,
via its beta subunit, docks the complex to a subset of peptide
repeat-containing proteins known as nucleoporins. See importin beta-1
(KPNB1; 602738). Michael et al. (1995) determined that the C terminus of
HNRNPA1 (164017) contains a 38-amino acid domain, termed M9, that
confers bidirectional transport across the nuclear envelope. Pollard et
al. (1996) found that M9-mediated nuclear import occurs by a novel
pathway independent of the importin-mediated NLS pathway. Using a yeast
2-hybrid system, they identified a HeLa cell cDNA encoding a protein
that interacts with an M9-containing sequence. The predicted 890-amino
acid protein was designated M9-interacting protein (MIP1), or
transportin. Transportin contains 2 leucine zipper motifs and a 19-amino
acid highly acidic domain, and has an estimated pI of 4.6. Pollard et
al. (1996) demonstrated that transportin mediated the nuclear import of
M9-bearing proteins.
Bonifaci et al. (1997) isolated cDNAs encoding transportin, which they
designated karyopherin beta-2, or KPNB2. They reported that the
predicted protein sequence is 34% identical to that of the yeast
beta-karyopherin Kap104p. Using overlay blots, Bonifaci et al. (1997)
demonstrated that KPNB2 also functions as a docking factor that binds to
peptide repeat-containing nucleoporins. In an assay using permeabilized
HeLa cells, KPNB2 inhibited KPNB1-mediated import of an NLS-containing
substrate and KPNB1 inhibited KPNB2-mediated import of recombinant
HNRNPA1. These results led Bonifaci et al. (1997) to suggest that the
distinct KPNB1- and KPNB2-mediated nuclear import pathways merge at
least partially at the level of docking to nucleoporins.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the KPNB2
gene to chromosome 5 (TMAP WI-13973).
BIOCHEMICAL FEATURES
- Crystal Structure
Lee et al. (2003) showed the crystal structure of importin-beta
complexed with the active form of SREBP2 (600481). Importin-beta uses
characteristic long helices like a pair of chopsticks to interact with
an SREBP2 dimer. Importin-beta changes its conformation to reveal a
pseudo-2-fold symmetry on its surface structure so that it can
accommodate a symmetric dimer molecule.
*FIELD* RF
1. Bonifaci, N.; Moroianu, J.; Radu, A.; Blobel, G.: Karyopherin
beta-2 mediates nuclear import of a mRNA binding protein. Proc. Nat.
Acad. Sci. 94: 5055-5060, 1997.
2. Lee, S. J.; Sekimoto, T.; Yamashita, E.; Nagoshi, E.; Nakagawa,
A.; Imamoto, N.; Yoshimura, M.; Sakai, H.; Chong, K. T.; Tsukihara,
T.; Yoneda, Y.: The structure of importin-beta bound to SREBP-2:
nuclear import of a transcription factor. Science 302: 1571-1575,
2003.
3. Michael, W. M.; Choi, M.; Dreyfuss, G.: A nuclear export signal
in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein
export pathway. Cell 83: 415-422, 1995.
4. Pollard, V. W.; Michael, W. M.; Nakielny, S.; Siomi, M. C.; Wang,
F.; Dreyfuss, G.: A novel receptor-mediated nuclear protein import
pathway. Cell 86: 985-994, 1996.
*FIELD* CN
Ada Hamosh - updated: 12/3/2003
Carol A. Bocchini - updated: 10/12/2001
*FIELD* CD
Rebekah S. Rasooly: 7/29/1998
*FIELD* ED
wwang: 08/27/2008
mgross: 4/7/2006
alopez: 3/8/2005
alopez: 12/8/2003
terry: 12/3/2003
carol: 10/12/2001
alopez: 8/27/1998
psherman: 8/17/1998
alopez: 7/29/1998
*RECORD*
*FIELD* NO
602901
*FIELD* TI
*602901 TRANSPORTIN 1; TNPO1
;;TRANSPORTIN;;
KARYOPHERIN BETA-2; KPNB2;;
M9-INTERACTING PROTEIN; MIP1;;
read moreIMPORTIN BETA-2
*FIELD* TX
CLONING
Targeting of most nuclear proteins to the cell nucleus is initiated by
interaction between the protein's nuclear localization signal (NLS) and
the importin, or karyopherin, receptor complex. An importin heterodimer
recognizes the NLS protein in the cytoplasm via its alpha subunit and,
via its beta subunit, docks the complex to a subset of peptide
repeat-containing proteins known as nucleoporins. See importin beta-1
(KPNB1; 602738). Michael et al. (1995) determined that the C terminus of
HNRNPA1 (164017) contains a 38-amino acid domain, termed M9, that
confers bidirectional transport across the nuclear envelope. Pollard et
al. (1996) found that M9-mediated nuclear import occurs by a novel
pathway independent of the importin-mediated NLS pathway. Using a yeast
2-hybrid system, they identified a HeLa cell cDNA encoding a protein
that interacts with an M9-containing sequence. The predicted 890-amino
acid protein was designated M9-interacting protein (MIP1), or
transportin. Transportin contains 2 leucine zipper motifs and a 19-amino
acid highly acidic domain, and has an estimated pI of 4.6. Pollard et
al. (1996) demonstrated that transportin mediated the nuclear import of
M9-bearing proteins.
Bonifaci et al. (1997) isolated cDNAs encoding transportin, which they
designated karyopherin beta-2, or KPNB2. They reported that the
predicted protein sequence is 34% identical to that of the yeast
beta-karyopherin Kap104p. Using overlay blots, Bonifaci et al. (1997)
demonstrated that KPNB2 also functions as a docking factor that binds to
peptide repeat-containing nucleoporins. In an assay using permeabilized
HeLa cells, KPNB2 inhibited KPNB1-mediated import of an NLS-containing
substrate and KPNB1 inhibited KPNB2-mediated import of recombinant
HNRNPA1. These results led Bonifaci et al. (1997) to suggest that the
distinct KPNB1- and KPNB2-mediated nuclear import pathways merge at
least partially at the level of docking to nucleoporins.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the KPNB2
gene to chromosome 5 (TMAP WI-13973).
BIOCHEMICAL FEATURES
- Crystal Structure
Lee et al. (2003) showed the crystal structure of importin-beta
complexed with the active form of SREBP2 (600481). Importin-beta uses
characteristic long helices like a pair of chopsticks to interact with
an SREBP2 dimer. Importin-beta changes its conformation to reveal a
pseudo-2-fold symmetry on its surface structure so that it can
accommodate a symmetric dimer molecule.
*FIELD* RF
1. Bonifaci, N.; Moroianu, J.; Radu, A.; Blobel, G.: Karyopherin
beta-2 mediates nuclear import of a mRNA binding protein. Proc. Nat.
Acad. Sci. 94: 5055-5060, 1997.
2. Lee, S. J.; Sekimoto, T.; Yamashita, E.; Nagoshi, E.; Nakagawa,
A.; Imamoto, N.; Yoshimura, M.; Sakai, H.; Chong, K. T.; Tsukihara,
T.; Yoneda, Y.: The structure of importin-beta bound to SREBP-2:
nuclear import of a transcription factor. Science 302: 1571-1575,
2003.
3. Michael, W. M.; Choi, M.; Dreyfuss, G.: A nuclear export signal
in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein
export pathway. Cell 83: 415-422, 1995.
4. Pollard, V. W.; Michael, W. M.; Nakielny, S.; Siomi, M. C.; Wang,
F.; Dreyfuss, G.: A novel receptor-mediated nuclear protein import
pathway. Cell 86: 985-994, 1996.
*FIELD* CN
Ada Hamosh - updated: 12/3/2003
Carol A. Bocchini - updated: 10/12/2001
*FIELD* CD
Rebekah S. Rasooly: 7/29/1998
*FIELD* ED
wwang: 08/27/2008
mgross: 4/7/2006
alopez: 3/8/2005
alopez: 12/8/2003
terry: 12/3/2003
carol: 10/12/2001
alopez: 8/27/1998
psherman: 8/17/1998
alopez: 7/29/1998