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Q14974

- IMB1_HUMAN

UniProt

Q14974 - IMB1_HUMAN

Protein

Importin subunit beta-1

Gene

KPNB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (15 May 2002)
      Previous versions | rss
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    Functioni

    Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats 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 importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. 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. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with IPO7 mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Imports SNAI1 and PRKCI into the nucleus.4 Publications

    GO - Molecular functioni

    1. enzyme binding Source: UniProt
    2. nuclear localization sequence binding Source: ProtInc
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein domain specific binding Source: UniProtKB
    6. protein transporter activity Source: Ensembl
    7. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. apoptotic DNA fragmentation Source: Reactome
    2. apoptotic process Source: Reactome
    3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    4. cytokine-mediated signaling pathway Source: Reactome
    5. intracellular transport of virus Source: Reactome
    6. NLS-bearing protein import into nucleus Source: ProtInc
    7. protein import into nucleus Source: MGI
    8. protein import into nucleus, translocation Source: ProtInc
    9. ribosomal protein import into nucleus Source: UniProtKB
    10. small molecule metabolic process Source: Reactome
    11. viral life cycle Source: Reactome
    12. viral process Source: Reactome

    Keywords - Biological processi

    Host-virus interaction, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_13462. Activation of DNA fragmentation factor.
    REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
    REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
    REACT_9395. Nuclear import of Rev protein.
    SignaLinkiQ14974.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Importin subunit beta-1
    Alternative name(s):
    Importin-90
    Karyopherin subunit beta-1
    Nuclear factor p97
    Pore targeting complex 97 kDa subunit
    Short name:
    PTAC97
    Gene namesi
    Name:KPNB1
    Synonyms:NTF97
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:6400. KPNB1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus envelope 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. endoplasmic reticulum tubular network Source: UniProt
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB
    6. nuclear envelope Source: UniProt
    7. nuclear membrane Source: HPA
    8. nuclear pore Source: ProtInc
    9. nucleoplasm Source: Reactome
    10. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi178 – 1781I → A: Largely reduced binding to FxFG repeats and reduced nuclear import. 1 Publication
    Mutagenesisi178 – 1781I → F or D: Loss of binding to FxFG repeats and reduced nuclear import. 1 Publication

    Organism-specific databases

    PharmGKBiPA30191.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 876876Importin subunit beta-1PRO_0000120745Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei12 – 121Phosphoserine1 Publication
    Cross-linki206 – 206Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei211 – 2111N6-acetyllysine; alternate1 Publication
    Cross-linki211 – 211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
    Modified residuei835 – 8351N6-acetyllysine1 Publication
    Modified residuei867 – 8671N6-acetyllysine1 Publication

    Post-translational modificationi

    Mono-ADP-ribosylated by PARP16.

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ14974.
    PaxDbiQ14974.
    PeptideAtlasiQ14974.
    PRIDEiQ14974.

    PTM databases

    PhosphoSiteiQ14974.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14974.
    BgeeiQ14974.
    CleanExiHS_KPNB1.
    GenevestigatoriQ14974.

    Organism-specific databases

    HPAiCAB034449.
    HPA029878.
    HPA050302.

    Interactioni

    Subunit structurei

    Forms a complex with an importin alpha subunit. Forms a heterodimer with IPO7. Interacts with IPO7, SNUPN, RPL23A and XPO1. The KPNB1/IPO7 heterodimer interacts with H1 histone. Interacts with H2A, H2B, H3 and H4 histones By similarity. Component of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259. Component of a nuclear export receptor complex composed of KPNB1, Ran, SNUPN and XPO1. Binds to HIV-1 Rev and Tat. Interacts with HTLV-1 Rex. Interacts with SRY. Interacts with PRKCI/atypical protein kinase C iota. Interacts with human respiratory syncytial virus (HRSV) protein M. Interacts with KPNA7. Interacts with SNAI1 (via zinc fingers) and SNAI2 (via zinc fingers). Interacts with SLC35G1 and STIM1.By similarity20 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERBB2P0462614EBI-286758,EBI-641062
    L1P031012EBI-286758,EBI-7362698From a different organism.
    L2P031072EBI-286758,EBI-7362531From a different organism.
    Mkl1Q8K4J65EBI-286758,EBI-8291665From a different organism.
    NSP1P149072EBI-286758,EBI-12265From a different organism.
    SMN2Q16637-35EBI-286758,EBI-395447
    SMNDC1O759402EBI-286758,EBI-1052641

    Protein-protein interaction databases

    BioGridi110035. 134 interactions.
    DIPiDIP-6204N.
    IntActiQ14974. 54 interactions.
    MINTiMINT-94095.
    STRINGi9606.ENSP00000290158.

    Structurei

    Secondary structure

    1
    876
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 97
    Helixi15 – 4531
    Helixi51 – 6515
    Helixi70 – 8112
    Helixi85 – 9814
    Turni99 – 1013
    Beta strandi104 – 1063
    Helixi109 – 12012
    Helixi121 – 1233
    Helixi129 – 13810
    Helixi144 – 16017
    Helixi163 – 1653
    Helixi167 – 1693
    Helixi170 – 18112
    Helixi188 – 20114
    Turni202 – 2054
    Helixi206 – 2094
    Helixi212 – 22514
    Beta strandi228 – 2303
    Helixi231 – 24717
    Helixi249 – 2513
    Turni253 – 2597
    Helixi260 – 26910
    Helixi273 – 29725
    Beta strandi303 – 3053
    Helixi314 – 32916
    Helixi330 – 3323
    Beta strandi335 – 3373
    Helixi344 – 35815
    Turni359 – 3624
    Helixi363 – 37412
    Helixi380 – 39213
    Beta strandi394 – 3974
    Turni399 – 4024
    Turni404 – 4085
    Helixi409 – 4157
    Helixi416 – 4183
    Helixi422 – 43817
    Helixi439 – 4424
    Turni446 – 4483
    Helixi449 – 4579
    Helixi464 – 48320
    Beta strandi487 – 4937
    Turni500 – 5023
    Helixi503 – 51311
    Turni517 – 5204
    Helixi521 – 5233
    Helixi524 – 53714
    Helixi541 – 5433
    Helixi544 – 56219
    Turni563 – 5664
    Helixi573 – 59220
    Beta strandi593 – 5953
    Helixi597 – 6015
    Helixi604 – 61411
    Beta strandi619 – 6224
    Helixi623 – 63917
    Helixi640 – 6467
    Helixi647 – 66014
    Helixi664 – 68118
    Helixi682 – 6854
    Helixi686 – 70015
    Beta strandi703 – 7053
    Helixi707 – 7093
    Helixi710 – 72415
    Helixi725 – 7317
    Helixi732 – 74312
    Helixi752 – 77726
    Beta strandi779 – 7824
    Helixi785 – 7895
    Helixi791 – 7933
    Helixi794 – 80512
    Helixi812 – 82918
    Helixi832 – 8387
    Helixi841 – 85212
    Helixi856 – 87318

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F59X-ray2.80A/B1-442[»]
    1IBRX-ray2.30B/D1-462[»]
    1M5NX-ray2.90S1-485[»]
    1O6OX-ray2.80A/B/C1-442[»]
    1O6PX-ray2.80A/B1-442[»]
    1QGKX-ray2.50A1-876[»]
    1QGRX-ray2.30A1-876[»]
    2P8QX-ray2.35A1-876[»]
    2Q5DX-ray3.20A/B1-876[»]
    2QNAX-ray2.84A127-875[»]
    3LWWX-ray3.15A/C1-876[»]
    3W5KX-ray2.60A1-876[»]
    ProteinModelPortaliQ14974.
    SMRiQ14974. Positions 1-873.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14974.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 10181Importin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Repeati124 – 16340HEAT 1Add
    BLAST
    Repeati168 – 20740HEAT 2Add
    BLAST
    Repeati213 – 25038HEAT 3Add
    BLAST
    Repeati317 – 35741HEAT 4Add
    BLAST
    Repeati362 – 39938HEAT 5Add
    BLAST
    Repeati404 – 44138HEAT 6Add
    BLAST
    Repeati602 – 64140HEAT 7Add
    BLAST
    Repeati687 – 72640HEAT 8Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni329 – 34214IAB-bindingAdd
    BLAST
    Regioni334 – 41986Ran-GTP bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi337 – 3415Poly-Asp

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5215.
    HOGENOMiHOG000204108.
    HOVERGENiHBG002369.
    InParanoidiQ14974.
    KOiK14293.
    OMAiGLTIMGM.
    OrthoDBiEOG7GN2KZ.
    PhylomeDBiQ14974.
    TreeFamiTF105655.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR021133. HEAT_type_2.
    IPR001494. Importin-beta_N.
    IPR027140. KPNB1.
    [Graphical view]
    PANTHERiPTHR10527:SF1. PTHR10527:SF1. 1 hit.
    PfamiPF00514. Arm. 1 hit.
    PF03810. IBN_N. 1 hit.
    [Graphical view]
    SMARTiSM00913. IBN_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS50077. HEAT_REPEAT. 1 hit.
    PS50166. IMPORTIN_B_NT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14974-1) [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

    MELITILEKT VSPDRLELEA AQKFLERAAV ENLPTFLVEL SRVLANPGNS    50
    QVARVAAGLQ IKNSLTSKDP DIKAQYQQRW LAIDANARRE VKNYVLQTLG 100
    TETYRPSSAS QCVAGIACAE IPVNQWPELI PQLVANVTNP NSTEHMKEST 150
    LEAIGYICQD IDPEQLQDKS NEILTAIIQG MRKEEPSNNV KLAATNALLN 200
    SLEFTKANFD KESERHFIMQ VVCEATQCPD TRVRVAALQN LVKIMSLYYQ 250
    YMETYMGPAL FAITIEAMKS DIDEVALQGI EFWSNVCDEE MDLAIEASEA 300
    AEQGRPPEHT SKFYAKGALQ YLVPILTQTL TKQDENDDDD DWNPCKAAGV 350
    CLMLLATCCE DDIVPHVLPF IKEHIKNPDW RYRDAAVMAF GCILEGPEPS 400
    QLKPLVIQAM PTLIELMKDP SVVVRDTAAW TVGRICELLP EAAINDVYLA 450
    PLLQCLIEGL SAEPRVASNV CWAFSSLAEA AYEAADVADD QEEPATYCLS 500
    SSFELIVQKL LETTDRPDGH QNNLRSSAYE SLMEIVKNSA KDCYPAVQKT 550
    TLVIMERLQQ VLQMESHIQS TSDRIQFNDL QSLLCATLQN VLRKVQHQDA 600
    LQISDVVMAS LLRMFQSTAG SGGVQEDALM AVSTLVEVLG GEFLKYMEAF 650
    KPFLGIGLKN YAEYQVCLAA VGLVGDLCRA LQSNIIPFCD EVMQLLLENL 700
    GNENVHRSVK PQILSVFGDI ALAIGGEFKK YLEVVLNTLQ QASQAQVDKS 750
    DYDMVDYLNE LRESCLEAYT GIVQGLKGDQ ENVHPDVMLV QPRVEFILSF 800
    IDHIAGDEDH TDGVVACAAG LIGDLCTAFG KDVLKLVEAR PMIHELLTEG 850
    RRSKTNKAKT LATWATKELR KLKNQA 876
    Length:876
    Mass (Da):97,170
    Last modified:May 15, 2002 - v2
    Checksum:iF3BB8B73E7E51639
    GO
    Isoform 2 (identifier: Q14974-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-145: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:731
    Mass (Da):81,179
    Checksum:i03F6C311DF096541
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971Q → H in AAA82869. (PubMed:7615630)Curated
    Sequence conflicti200 – 2001N → NA AA sequence (PubMed:8617227)Curated
    Sequence conflicti863 – 8631T → R in AAA82869. (PubMed:7615630)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 145145Missing in isoform 2. 1 PublicationVSP_054612Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L39793 Genomic DNA. Translation: AAA82869.1.
    L38951 mRNA. Translation: AAC41763.1.
    BT009797 mRNA. Translation: AAP88799.1.
    AK316421 mRNA. Translation: BAH14792.1.
    AC015674 Genomic DNA. No translation available.
    AC025682 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94807.1.
    CH471109 Genomic DNA. Translation: EAW94808.1.
    CH471109 Genomic DNA. Translation: EAW94810.1.
    BC003572 mRNA. Translation: AAH03572.1.
    BC024045 mRNA. Translation: AAH24045.1.
    BC036703 mRNA. Translation: AAH36703.1.
    CCDSiCCDS11513.1. [Q14974-1]
    CCDS62228.1. [Q14974-2]
    PIRiI52907.
    RefSeqiNP_001263382.1. NM_001276453.1. [Q14974-2]
    NP_002256.2. NM_002265.5. [Q14974-1]
    UniGeneiHs.532793.

    Genome annotation databases

    EnsembliENST00000290158; ENSP00000290158; ENSG00000108424. [Q14974-1]
    ENST00000535458; ENSP00000438253; ENSG00000108424. [Q14974-2]
    ENST00000540627; ENSP00000438964; ENSG00000108424. [Q14974-2]
    GeneIDi3837.
    KEGGihsa:3837.
    UCSCiuc002ilt.2. human. [Q14974-1]

    Polymorphism databases

    DMDMi20981701.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L39793 Genomic DNA. Translation: AAA82869.1 .
    L38951 mRNA. Translation: AAC41763.1 .
    BT009797 mRNA. Translation: AAP88799.1 .
    AK316421 mRNA. Translation: BAH14792.1 .
    AC015674 Genomic DNA. No translation available.
    AC025682 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94807.1 .
    CH471109 Genomic DNA. Translation: EAW94808.1 .
    CH471109 Genomic DNA. Translation: EAW94810.1 .
    BC003572 mRNA. Translation: AAH03572.1 .
    BC024045 mRNA. Translation: AAH24045.1 .
    BC036703 mRNA. Translation: AAH36703.1 .
    CCDSi CCDS11513.1. [Q14974-1 ]
    CCDS62228.1. [Q14974-2 ]
    PIRi I52907.
    RefSeqi NP_001263382.1. NM_001276453.1. [Q14974-2 ]
    NP_002256.2. NM_002265.5. [Q14974-1 ]
    UniGenei Hs.532793.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F59 X-ray 2.80 A/B 1-442 [» ]
    1IBR X-ray 2.30 B/D 1-462 [» ]
    1M5N X-ray 2.90 S 1-485 [» ]
    1O6O X-ray 2.80 A/B/C 1-442 [» ]
    1O6P X-ray 2.80 A/B 1-442 [» ]
    1QGK X-ray 2.50 A 1-876 [» ]
    1QGR X-ray 2.30 A 1-876 [» ]
    2P8Q X-ray 2.35 A 1-876 [» ]
    2Q5D X-ray 3.20 A/B 1-876 [» ]
    2QNA X-ray 2.84 A 127-875 [» ]
    3LWW X-ray 3.15 A/C 1-876 [» ]
    3W5K X-ray 2.60 A 1-876 [» ]
    ProteinModelPortali Q14974.
    SMRi Q14974. Positions 1-873.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110035. 134 interactions.
    DIPi DIP-6204N.
    IntActi Q14974. 54 interactions.
    MINTi MINT-94095.
    STRINGi 9606.ENSP00000290158.

    PTM databases

    PhosphoSitei Q14974.

    Polymorphism databases

    DMDMi 20981701.

    Proteomic databases

    MaxQBi Q14974.
    PaxDbi Q14974.
    PeptideAtlasi Q14974.
    PRIDEi Q14974.

    Protocols and materials databases

    DNASUi 3837.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290158 ; ENSP00000290158 ; ENSG00000108424 . [Q14974-1 ]
    ENST00000535458 ; ENSP00000438253 ; ENSG00000108424 . [Q14974-2 ]
    ENST00000540627 ; ENSP00000438964 ; ENSG00000108424 . [Q14974-2 ]
    GeneIDi 3837.
    KEGGi hsa:3837.
    UCSCi uc002ilt.2. human. [Q14974-1 ]

    Organism-specific databases

    CTDi 3837.
    GeneCardsi GC17P045727.
    HGNCi HGNC:6400. KPNB1.
    HPAi CAB034449.
    HPA029878.
    HPA050302.
    MIMi 602738. gene.
    neXtProti NX_Q14974.
    PharmGKBi PA30191.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5215.
    HOGENOMi HOG000204108.
    HOVERGENi HBG002369.
    InParanoidi Q14974.
    KOi K14293.
    OMAi GLTIMGM.
    OrthoDBi EOG7GN2KZ.
    PhylomeDBi Q14974.
    TreeFami TF105655.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_13462. Activation of DNA fragmentation factor.
    REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
    REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
    REACT_9395. Nuclear import of Rev protein.
    SignaLinki Q14974.

    Miscellaneous databases

    ChiTaRSi KPNB1. human.
    EvolutionaryTracei Q14974.
    GeneWikii KPNB1.
    GenomeRNAii 3837.
    NextBioi 15083.
    PROi Q14974.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14974.
    Bgeei Q14974.
    CleanExi HS_KPNB1.
    Genevestigatori Q14974.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR021133. HEAT_type_2.
    IPR001494. Importin-beta_N.
    IPR027140. KPNB1.
    [Graphical view ]
    PANTHERi PTHR10527:SF1. PTHR10527:SF1. 1 hit.
    Pfami PF00514. Arm. 1 hit.
    PF03810. IBN_N. 1 hit.
    [Graphical view ]
    SMARTi SM00913. IBN_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50077. HEAT_REPEAT. 1 hit.
    PS50166. IMPORTIN_B_NT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and characterization of cytoplasmic nuclear protein import factor p97."
      Chi N.C., Adam E.J.H., Adam S.A.
      J. Cell Biol. 130:265-274(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
      Tissue: Brain.
    2. "Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope."
      Goerlich D., Kostka S., Kraft R., Dingwall C., Laskey R.A., Hartmann E., Prehn S.
      Curr. Biol. 5:383-392(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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 2).
      Tissue: Testis.
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 and Eye.
    8. "The conserved amino-terminal domain of hSRP1 alpha is essential for nuclear protein import."
      Weis K., Ryder U., Lamond A.I.
      EMBO J. 15:1818-1825(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH AN IMPORTIN ALPHA SUBUNIT.
    9. Bienvenut W.V.
      Submitted (MAY-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-9; 55-62 AND 192-206, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    10. "Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta."
      Moroianu J., Blobel G., Radu A.
      Proc. Natl. Acad. Sci. U.S.A. 93:7059-7062(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: RAN-GTP AND ALPHA SUBUNIT BINDING SITES.
    11. "Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta."
      Henderson B.R., Percipalle P.
      J. Mol. Biol. 274:693-707(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 REV AND TAT.
    12. "Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure."
      Huber J., Cronshagen U., Kadokura M., Marshallsay C., Wada T., Sekine M., Luehrmann R.
      EMBO J. 17:4114-4126(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNUPN.
    13. "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; RPL5 AND IPO7.
    14. "The importin beta/importin 7 heterodimer is a functional nuclear import receptor for histone H1."
      Jaekel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K., Doenecke D., Goerlich D.
      EMBO J. 18:2411-2423(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH H1 HISTONE AND IPO7.
    15. Cited for: IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, INTERACTION WITH IPO7; SNUPN AND XPO1.
    16. "The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals."
      Truant R., Cullen B.R.
      Mol. Cell. Biol. 19:1210-1217(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 REV.
    17. "Importin beta can mediate the nuclear import of an arginine-rich nuclear localization signal in the absence of importin alpha."
      Palmeri D., Malim M.H.
      Mol. Cell. Biol. 19:1218-1225(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 REX.
    18. "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta."
      Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.
      Hum. Mol. Genet. 11:1785-1795(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN AN IMPORT SNRNP COMPLEX.
    19. "Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C."
      White W.O., Seibenhener M.L., Wooten M.W.
      J. Cell. Biochem. 85:42-53(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKCI, FUNCTION, SUBCELLULAR LOCATION.
    20. "Defective importin beta recognition and nuclear import of the sex-determining factor SRY are associated with XY sex-reversing mutations."
      Harley V.R., Layfield S., Mitchell C.L., Forwood J.K., John A.P., Briggs L.J., McDowall S.G., Jans D.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:7045-7050(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRY.
    21. "Regulation of human SRY subcellular distribution by its acetylation/deacetylation."
      Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N., Aldrian-Herrada G., Poulat F., Berta P., Benkirane M., Boizet-Bonhoure B.
      EMBO J. 23:3336-3345(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRY.
    22. "Nuclear import of the respiratory syncytial virus matrix protein is mediated by importin beta1 independent of importin alpha."
      Ghildyal R., Ho A., Wagstaff K.M., Dias M.M., Barton C.L., Jans P., Bardin P.G., Jans D.A.
      Biochemistry 44:12887-12895(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HRSV PROTEIN M.
    23. "Zinc finger domain of Snail functions as a nuclear localization signal for importin beta-mediated nuclear import pathway."
      Yamasaki H., Sekimoto T., Ohkubo T., Douchi T., Nagata Y., Ozawa M., Yoneda Y.
      Genes Cells 10:455-464(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNAI1.
    24. "Respiratory syncytial virus M2-1 protein induces the activation of nuclear factor kappa B."
      Reimers K., Buchholz K., Werchau H.
      Virology 331:260-268(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HRSV PROTEIN M2-1.
    25. "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.
    26. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-206 AND LYS-211.
      Tissue: Mammary cancer.
    27. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "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: FUNCTION, INTERACTION WITH SNAI1 AND SNAI2.
    31. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211; LYS-835 AND LYS-867, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "Karyopherin alpha7 (KPNA7), a divergent member of the importin alpha family of nuclear import receptors."
      Kelley J.B., Talley A.M., Spencer A., Gioeli D., Paschal B.M.
      BMC Cell Biol. 11:63-63(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KPNA7.
    33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to multiple transporters."
      Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.
      Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC35G1 AND STIM1.
    35. "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].
    36. "PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-beta1."
      Di Paola S., Micaroni M., Di Tullio G., Buccione R., Di Girolamo M.
      PLoS ONE 7:E37352-E37352(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ADP-RIBOSYLATION, INTERACTION WITH PARP16.
    37. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. "Structural view of the Ran-Importin beta interaction at 2.3 A resolution."
      Vetter I.R., Arndt A., Kutay U., Goerlich D., Wittinghofer A.
      Cell 97:635-646(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-459.
    39. "Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking."
      Bayliss R., Littlewood T., Stewart M.
      Cell 102:99-108(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 3-442, MUTAGENESIS OF ILE-178.
    40. "Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta."
      Cingolani G., Bednenko J., Gillespie M.T., Gerace L.
      Mol. Cell 10:1345-1353(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-485.

    Entry informationi

    Entry nameiIMB1_HUMAN
    AccessioniPrimary (citable) accession number: Q14974
    Secondary accession number(s): B7ZAV6
    , D3DTT3, Q14637, Q53XN2, Q96J27
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 15, 2002
    Last modified: October 1, 2014
    This is version 162 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3