Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q92973

- TNPO1_HUMAN

UniProt

Q92973 - TNPO1_HUMAN

Protein

Transportin-1

Gene

TNPO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (22 Sep 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus By similarity. Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Appears also to be involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Mediates nuclear import of ADAR/ADAR1 (isoform 5) in a RanGTP-dependent manner.By similarity4 Publications

    GO - Molecular functioni

    1. nuclear localization sequence binding Source: ProtInc
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA metabolic process Source: Reactome
    3. protein import into nucleus, translocation Source: ProtInc
    4. RNA metabolic process Source: Reactome
    5. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transportin-1
    Alternative name(s):
    Importin beta-2
    Karyopherin beta-2
    M9 region interaction protein
    Short name:
    MIP
    Gene namesi
    Name:TNPO1
    Synonyms:KPNB2, MIP1, TRN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6401. TNPO1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome
    3. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30192.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 898898Transportin-1PRO_0000120765Add
    BLAST

    Proteomic databases

    MaxQBiQ92973.
    PaxDbiQ92973.
    PRIDEiQ92973.

    PTM databases

    PhosphoSiteiQ92973.

    Expressioni

    Gene expression databases

    ArrayExpressiQ92973.
    BgeeiQ92973.
    CleanExiHS_TNPO1.
    GenevestigatoriQ92973.

    Organism-specific databases

    HPAiCAB016325.

    Interactioni

    Subunit structurei

    Binds HNRPA1, HNRPA2, HNRNPDL, RPL23A, RPS7, RPL5, RAN and SRP19. Interacts with H2A, H2B, H3 and H4 histones. Binds to HIV-1 Rev. Interacts with isoform 5 of ADAR/ADAR1 (via DRBM 3 domain). Interacts with SNAI1 (via zinc fingers); the interaction mediates SNAI1 nuclear import. Interacts with SNAI2 (via zinc fingers).6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GRB2P629932EBI-286693,EBI-401755
    RANP628262EBI-286693,EBI-286642

    Protein-protein interaction databases

    BioGridi110040. 41 interactions.
    DIPiDIP-29335N.
    IntActiQ92973. 18 interactions.
    MINTiMINT-94165.
    STRINGi9606.ENSP00000336712.

    Structurei

    Secondary structure

    1
    898
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 3014
    Beta strandi31 – 333
    Helixi35 – 4814
    Beta strandi49 – 513
    Helixi52 – 6312
    Helixi70 – 8314
    Turni84 – 863
    Helixi88 – 903
    Helixi93 – 10412
    Turni105 – 1084
    Helixi112 – 12817
    Turni129 – 1335
    Beta strandi134 – 1363
    Helixi137 – 1459
    Helixi147 – 1493
    Helixi150 – 16718
    Helixi170 – 1734
    Beta strandi175 – 1784
    Helixi180 – 1878
    Turni188 – 1925
    Helixi196 – 20712
    Turni208 – 2136
    Helixi215 – 2184
    Helixi221 – 23212
    Helixi237 – 25317
    Helixi255 – 2584
    Helixi259 – 2613
    Helixi262 – 27312
    Beta strandi275 – 2773
    Helixi278 – 29114
    Beta strandi294 – 2963
    Helixi297 – 3015
    Turni302 – 3043
    Helixi305 – 31511
    Helixi320 – 3278
    Helixi340 – 3423
    Helixi367 – 3704
    Helixi383 – 39816
    Helixi399 – 4024
    Helixi403 – 41412
    Beta strandi416 – 4183
    Helixi419 – 43113
    Turni432 – 4365
    Helixi437 – 4404
    Helixi441 – 4433
    Helixi444 – 45411
    Helixi460 – 47213
    Helixi474 – 4796
    Turni482 – 4854
    Helixi486 – 49712
    Beta strandi498 – 5003
    Helixi502 – 51918
    Helixi520 – 5267
    Helixi527 – 54014
    Helixi543 – 56018
    Helixi561 – 5644
    Helixi567 – 58317
    Helixi591 – 60515
    Helixi606 – 6127
    Helixi613 – 63624
    Turni638 – 6403
    Helixi647 – 66317
    Helixi664 – 6674
    Helixi668 – 6725
    Helixi676 – 6838
    Helixi689 – 70517
    Helixi707 – 7093
    Helixi711 – 7133
    Helixi714 – 72310
    Helixi727 – 7293
    Helixi730 – 74718
    Helixi748 – 7558
    Helixi756 – 76611
    Beta strandi768 – 7703
    Helixi773 – 78917
    Helixi791 – 7944
    Helixi795 – 7973
    Helixi798 – 81013
    Helixi816 – 83116
    Helixi833 – 8353
    Helixi837 – 8393
    Helixi840 – 8489
    Helixi855 – 88026
    Helixi881 – 8833
    Helixi886 – 8949

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QBKX-ray3.00B9-898[»]
    2H4MX-ray3.05A/B376-898[»]
    A/B9-343[»]
    2OT8X-ray3.10A/B9-331[»]
    A/B375-898[»]
    2QMRX-ray3.00A/B/C/D9-898[»]
    2Z5JX-ray3.40A9-898[»]
    2Z5KX-ray2.60A9-898[»]
    2Z5MX-ray3.00A9-898[»]
    2Z5NX-ray3.20A9-898[»]
    2Z5OX-ray3.20A9-898[»]
    4FDDX-ray2.30A9-331[»]
    A375-898[»]
    4FQ3X-ray3.00A9-898[»]
    4JLQX-ray3.05A9-331[»]
    A375-898[»]
    4OO6X-ray2.70A375-898[»]
    A9-331[»]
    ProteinModelPortaliQ92973.
    SMRiQ92973. Positions 11-897.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92973.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 10969Importin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Repeati132 – 16938HEAT 1Add
    BLAST
    Repeati178 – 21538HEAT 2Add
    BLAST
    Repeati219 – 25638HEAT 3Add
    BLAST
    Repeati401 – 43838HEAT 4Add
    BLAST
    Repeati442 – 47938HEAT 5Add
    BLAST
    Repeati484 – 52138HEAT 6Add
    BLAST
    Repeati568 – 60740HEAT 7Add
    BLAST
    Repeati671 – 70838HEAT 8Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi358 – 37619Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the importin beta family.Curated
    Contains 8 HEAT repeats.Curated
    Contains 1 importin N-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5215.
    HOGENOMiHOG000203940.
    HOVERGENiHBG058963.
    InParanoidiQ92973.
    OMAiEEDIKPR.
    OrthoDBiEOG7XM2X0.
    PhylomeDBiQ92973.
    TreeFamiTF300825.

    Family and domain databases

    Gene3Di1.25.10.10. 2 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR001494. Importin-beta_N.
    [Graphical view]
    PfamiPF03810. IBN_N. 1 hit.
    [Graphical view]
    SMARTiSM00913. IBN_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92973-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVWDRQTKME YEWKPDEQGL QQILQLLKES QSPDTTIQRT VQQKLEQLNQ    50
    YPDFNNYLIF VLTKLKSEDE PTRSLSGLIL KNNVKAHFQN FPNGVTDFIK 100
    SECLNNIGDS SPLIRATVGI LITTIASKGE LQNWPDLLPK LCSLLDSEDY 150
    NTCEGAFGAL QKICEDSAEI LDSDVLDRPL NIMIPKFLQF FKHSSPKIRS 200
    HAVACVNQFI ISRTQALMLH IDSFIENLFA LAGDEEPEVR KNVCRALVML 250
    LEVRMDRLLP HMHNIVEYML QRTQDQDENV ALEACEFWLT LAEQPICKDV 300
    LVRHLPKLIP VLVNGMKYSD IDIILLKGDV EEDETIPDSE QDIRPRFHRS 350
    RTVAQQHDED GIEEEDDDDD EIDDDDTISD WNLRKCSAAA LDVLANVYRD 400
    ELLPHILPLL KELLFHHEWV VKESGILVLG AIAEGCMQGM IPYLPELIPH 450
    LIQCLSDKKA LVRSITCWTL SRYAHWVVSQ PPDTYLKPLM TELLKRILDS 500
    NKRVQEAACS AFATLEEEAC TELVPYLAYI LDTLVFAFSK YQHKNLLILY 550
    DAIGTLADSV GHHLNKPEYI QMLMPPLIQK WNMLKDEDKD LFPLLECLSS 600
    VATALQSGFL PYCEPVYQRC VNLVQKTLAQ AMLNNAQPDQ YEAPDKDFMI 650
    VALDLLSGLA EGLGGNIEQL VARSNILTLM YQCMQDKMPE VRQSSFALLG 700
    DLTKACFQHV KPCIADFMPI LGTNLNPEFI SVCNNATWAI GEISIQMGIE 750
    MQPYIPMVLH QLVEIINRPN TPKTLLENTA ITIGRLGYVC PQEVAPMLQQ 800
    FIRPWCTSLR NIRDNEEKDS AFRGICTMIS VNPSGVIQDF IFFCDAVASW 850
    INPKDDLRDM FCKILHGFKN QVGDENWRRF SDQFPLPLKE RLAAFYGV 898
    Length:898
    Mass (Da):102,355
    Last modified:September 22, 2009 - v2
    Checksum:i7B880D9E7CA6798F
    GO
    Isoform 2 (identifier: Q92973-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-9: MVWDRQTKM → M

    Show »
    Length:890
    Mass (Da):101,310
    Checksum:i4762DB4895472D10
    GO
    Isoform 3 (identifier: Q92973-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         69-118: Missing.

    Show »
    Length:848
    Mass (Da):96,901
    Checksum:i6DF034D06DC572B4
    GO

    Sequence cautioni

    The sequence AAC50723.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH40340.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti104 – 1041L → S in AAB68948. 1 PublicationCurated
    Sequence conflicti225 – 2251I → T in AAC50723. (PubMed:8808633)Curated
    Sequence conflicti669 – 6691Q → L in AAB68948. 1 PublicationCurated
    Sequence conflicti880 – 8801F → L in BAG62638. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti34 – 341D → E.
    Corresponds to variant rs25661 [ dbSNP | Ensembl ].
    VAR_014455

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 99MVWDRQTKM → M in isoform 2. 2 PublicationsVSP_038028
    Alternative sequencei69 – 11850Missing in isoform 3. 1 PublicationVSP_038029Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70322 mRNA. Translation: AAC50723.1. Different initiation.
    U72069 mRNA. Translation: AAB58254.1.
    U72395 mRNA. Translation: AAB68948.1.
    AK301021 mRNA. Translation: BAG62638.1.
    BC040340 mRNA. Translation: AAH40340.1. Different initiation.
    CCDSiCCDS4016.1. [Q92973-2]
    CCDS43329.1. [Q92973-1]
    RefSeqiNP_002261.3. NM_002270.3. [Q92973-1]
    NP_694858.1. NM_153188.2. [Q92973-2]
    XP_005248557.1. XM_005248500.1. [Q92973-2]
    UniGeneiHs.482497.

    Genome annotation databases

    EnsembliENST00000337273; ENSP00000336712; ENSG00000083312. [Q92973-1]
    ENST00000506351; ENSP00000425118; ENSG00000083312. [Q92973-2]
    ENST00000523768; ENSP00000428899; ENSG00000083312. [Q92973-3]
    GeneIDi3842.
    KEGGihsa:3842.
    UCSCiuc003kcg.4. human. [Q92973-1]
    uc011csj.1. human. [Q92973-3]

    Polymorphism databases

    DMDMi259016171.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70322 mRNA. Translation: AAC50723.1 . Different initiation.
    U72069 mRNA. Translation: AAB58254.1 .
    U72395 mRNA. Translation: AAB68948.1 .
    AK301021 mRNA. Translation: BAG62638.1 .
    BC040340 mRNA. Translation: AAH40340.1 . Different initiation.
    CCDSi CCDS4016.1. [Q92973-2 ]
    CCDS43329.1. [Q92973-1 ]
    RefSeqi NP_002261.3. NM_002270.3. [Q92973-1 ]
    NP_694858.1. NM_153188.2. [Q92973-2 ]
    XP_005248557.1. XM_005248500.1. [Q92973-2 ]
    UniGenei Hs.482497.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QBK X-ray 3.00 B 9-898 [» ]
    2H4M X-ray 3.05 A/B 376-898 [» ]
    A/B 9-343 [» ]
    2OT8 X-ray 3.10 A/B 9-331 [» ]
    A/B 375-898 [» ]
    2QMR X-ray 3.00 A/B/C/D 9-898 [» ]
    2Z5J X-ray 3.40 A 9-898 [» ]
    2Z5K X-ray 2.60 A 9-898 [» ]
    2Z5M X-ray 3.00 A 9-898 [» ]
    2Z5N X-ray 3.20 A 9-898 [» ]
    2Z5O X-ray 3.20 A 9-898 [» ]
    4FDD X-ray 2.30 A 9-331 [» ]
    A 375-898 [» ]
    4FQ3 X-ray 3.00 A 9-898 [» ]
    4JLQ X-ray 3.05 A 9-331 [» ]
    A 375-898 [» ]
    4OO6 X-ray 2.70 A 375-898 [» ]
    A 9-331 [» ]
    ProteinModelPortali Q92973.
    SMRi Q92973. Positions 11-897.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110040. 41 interactions.
    DIPi DIP-29335N.
    IntActi Q92973. 18 interactions.
    MINTi MINT-94165.
    STRINGi 9606.ENSP00000336712.

    PTM databases

    PhosphoSitei Q92973.

    Polymorphism databases

    DMDMi 259016171.

    Proteomic databases

    MaxQBi Q92973.
    PaxDbi Q92973.
    PRIDEi Q92973.

    Protocols and materials databases

    DNASUi 3842.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337273 ; ENSP00000336712 ; ENSG00000083312 . [Q92973-1 ]
    ENST00000506351 ; ENSP00000425118 ; ENSG00000083312 . [Q92973-2 ]
    ENST00000523768 ; ENSP00000428899 ; ENSG00000083312 . [Q92973-3 ]
    GeneIDi 3842.
    KEGGi hsa:3842.
    UCSCi uc003kcg.4. human. [Q92973-1 ]
    uc011csj.1. human. [Q92973-3 ]

    Organism-specific databases

    CTDi 3842.
    GeneCardsi GC05P072148.
    HGNCi HGNC:6401. TNPO1.
    HPAi CAB016325.
    MIMi 602901. gene.
    neXtProti NX_Q92973.
    PharmGKBi PA30192.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5215.
    HOGENOMi HOG000203940.
    HOVERGENi HBG058963.
    InParanoidi Q92973.
    OMAi EEDIKPR.
    OrthoDBi EOG7XM2X0.
    PhylomeDBi Q92973.
    TreeFami TF300825.

    Enzyme and pathway databases

    Reactomei REACT_25064. Tristetraprolin (TTP) destabilizes mRNA.

    Miscellaneous databases

    ChiTaRSi TNPO1. human.
    EvolutionaryTracei Q92973.
    GeneWikii Transportin_1.
    GenomeRNAii 3842.
    NextBioi 15119.
    PROi Q92973.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92973.
    Bgeei Q92973.
    CleanExi HS_TNPO1.
    Genevestigatori Q92973.

    Family and domain databases

    Gene3Di 1.25.10.10. 2 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR001494. Importin-beta_N.
    [Graphical view ]
    Pfami PF03810. IBN_N. 1 hit.
    [Graphical view ]
    SMARTi SM00913. IBN_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50166. IMPORTIN_B_NT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel receptor-mediated nuclear protein import pathway."
      Pollard V.W., Michael W.M., Nakielny S., Siomi M.C., Wang F., Dreyfuss G.
      Cell 86:985-994(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Karyopherin beta2 mediates nuclear import of a mRNA binding protein."
      Bonifaci N., Moroianu J., Radu A., Blobel G.
      Proc. Natl. Acad. Sci. U.S.A. 94:5055-5060(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Liver.
    3. Fridell R.A., Thorne L.W., Benson R.E., Cullen B.R.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Spleen.
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    7. "Transportin: nuclear transport receptor of a novel nuclear protein import pathway."
      Nakielny S., Siomi M.C., Siomi H., Michael W.M., Pollard V., Dreyfuss G.
      Exp. Cell Res. 229:261-266(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Molecular cloning of the cDNA encoding A + U-rich element RNA binding factor."
      Doi A., Shiosaka T., Takaoka Y., Yanagisawa K., Fujita S.
      Biochim. Biophys. Acta 1396:51-56(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HNRNPDL.
    9. "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells."
      Jaekel S., Goerlich D.
      EMBO J. 17:4491-4502(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RPL23A; RPS7 AND RPL5.
    10. "Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin."
      Dean K.A., von Ahsen O., Goerlich D., Fried H.M.
      J. Cell Sci. 114:3479-3485(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SRP19.
    11. "Multiple importins function as nuclear transport receptors for the Rev protein of human immunodeficiency virus type 1."
      Arnold M., Nath A., Hauber J., Kehlenbach R.H.
      J. Biol. Chem. 281:20883-20890(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 REV.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Characterization of Snail nuclear import pathways as representatives of C2H2 zinc finger transcription factors."
      Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.
      J. Cell Sci. 122:1452-1460(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNAI1 AND SNAI2.
    14. "RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1."
      Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P., Jantsch M.F.
      Mol. Cell. Biol. 29:1487-1497(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ADAR.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp."
      Chook Y.M., Blobel G.
      Nature 399:230-237(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH RAN.

    Entry informationi

    Entry nameiTNPO1_HUMAN
    AccessioniPrimary (citable) accession number: Q92973
    Secondary accession number(s): B4DVC6, Q92957, Q92975
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3