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P52294

- IMA5_HUMAN

UniProt

P52294 - IMA5_HUMAN

Protein

Importin subunit alpha-5

Gene

KPNA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. 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. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.

    GO - Molecular functioni

    1. nuclear localization sequence binding Source: ProtInc
    2. protein binding Source: UniProtKB
    3. protein transporter activity Source: InterPro

    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. positive regulation of protein import into nucleus Source: UniProtKB
    8. regulation of DNA recombination Source: ProtInc
    9. viral life cycle Source: Reactome
    10. 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_6248. Transport of Ribonucleoproteins into the Host Nucleus.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    SignaLinkiP52294.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Importin subunit alpha-5
    Alternative name(s):
    Karyopherin subunit alpha-1
    Nucleoprotein interactor 1
    Short name:
    NPI-1
    RAG cohort protein 2
    SRP1-beta
    Cleaved into the following chain:
    Gene namesi
    Name:KPNA1
    Synonyms:RCH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:6394. KPNA1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. dendrite Source: UniProtKB
    4. nuclear pore Source: ProtInc
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30185.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 538538Importin subunit alpha-5PRO_0000120719Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 538537Importin subunit alpha-5, N-terminally processedPRO_0000424491Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21N-acetylthreonine; in Importin subunit alpha-5, N-terminally processed1 Publication

    Post-translational modificationi

    Polyubiquitinated in the presence of RAG1 (in vitro).1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiP52294.
    PaxDbiP52294.
    PRIDEiP52294.

    PTM databases

    PhosphoSiteiP52294.

    Miscellaneous databases

    PMAP-CutDBP52294.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously.

    Gene expression databases

    ArrayExpressiP52294.
    BgeeiP52294.
    CleanExiHS_KPNA1.
    GenevestigatoriP52294.

    Organism-specific databases

    HPAiHPA053627.

    Interactioni

    Subunit structurei

    Heterodimer; with KPNB1. Interacts with ANP32E. Interacts with ZIC3 By similarity. Interacts with NSMF; the interaction occurs in a calcium-independent manner after synaptic NMDA receptor stimulation and is required for nuclear import of NSMF but is competed by CABP1 By similarity. Interacts with the nucleoprotein of influenza A viruses. Binds to HCMV (human cytomegalovirus) UL84, HIV-1 Vpr and to ebolavirus VP24. Interacts with APEX1 and RAG1. Interacts with CTNNBL1 (via its N-terminal). Interacts with AICDA (via its NLS). Interacts with SNAI1 (via zinc fingers).By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9WMX22EBI-358383,EBI-6863741From a different organism.
    DCAF8Q5TAQ92EBI-358383,EBI-740686
    GRM1Q132552EBI-358383,EBI-8527352

    Protein-protein interaction databases

    BioGridi110034. 62 interactions.
    DIPiDIP-29296N.
    IntActiP52294. 33 interactions.
    MINTiMINT-240027.
    STRINGi9606.ENSP00000343701.

    Structurei

    Secondary structure

    1
    538
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi85 – 928
    Helixi96 – 11116
    Beta strandi112 – 1154
    Helixi118 – 1225
    Helixi127 – 1359
    Helixi141 – 15515
    Helixi159 – 1679
    Helixi170 – 1778
    Helixi183 – 19715
    Helixi201 – 2099
    Helixi213 – 2197
    Helixi226 – 24015
    Beta strandi243 – 2453
    Helixi249 – 2513
    Helixi253 – 2553
    Helixi256 – 2627
    Helixi268 – 28114
    Beta strandi283 – 2853
    Helixi286 – 2949
    Turni295 – 2973
    Helixi298 – 3047
    Helixi310 – 32314
    Helixi328 – 3358
    Turni336 – 3383
    Helixi339 – 3468
    Helixi352 – 36514
    Helixi370 – 3789
    Helixi381 – 39111
    Helixi394 – 41017
    Helixi413 – 42210
    Helixi425 – 4306
    Helixi431 – 4333
    Helixi437 – 46024
    Beta strandi461 – 4633
    Helixi468 – 4769
    Helixi478 – 4858
    Helixi487 – 50418

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JDQX-ray2.20A/B66-512[»]
    3TJ3X-ray2.70A/B66-512[»]
    4B18X-ray2.52A66-512[»]
    ProteinModelPortaliP52294.
    SMRiP52294. Positions 10-509.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52294.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 5757IBBPROSITE-ProRule annotationAdd
    BLAST
    Repeati77 – 11741ARM 1; truncatedAdd
    BLAST
    Repeati118 – 16144ARM 2Add
    BLAST
    Repeati162 – 20645ARM 3Add
    BLAST
    Repeati207 – 24539ARM 4Add
    BLAST
    Repeati246 – 29045ARM 5Add
    BLAST
    Repeati291 – 33040ARM 6Add
    BLAST
    Repeati331 – 37242ARM 7Add
    BLAST
    Repeati373 – 41240ARM 8Add
    BLAST
    Repeati413 – 45745ARM 9Add
    BLAST
    Repeati460 – 50445ARM 10; atypicalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni149 – 24193NLS binding site (major)By similarityAdd
    BLAST
    Regioni245 – 437193Binding to RAG1Add
    BLAST
    Regioni318 – 40689NLS binding site (minor)By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi42 – 5110Nuclear localization signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi25 – 284Poly-Arg

    Domaini

    Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.1 Publication
    The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins By similarity.By similarity
    The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding By similarity.By similarity

    Sequence similaritiesi

    Belongs to the importin alpha family.Curated
    Contains 10 ARM repeats.PROSITE-ProRule annotation
    Contains 1 IBB domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5064.
    HOGENOMiHOG000167616.
    HOVERGENiHBG001846.
    InParanoidiP52294.
    KOiK15042.
    OMAiETEPNPP.
    OrthoDBiEOG7VHSWV.
    PhylomeDBiP52294.
    TreeFamiTF354205.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR002652. Importin-a_IBB.
    IPR024931. Importing_su_alpha.
    [Graphical view]
    PfamiPF00514. Arm. 8 hits.
    PF01749. IBB. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005673. Importin_alpha. 1 hit.
    SMARTiSM00185. ARM. 8 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS50176. ARM_REPEAT. 4 hits.
    PS51214. IBB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P52294-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTPGKENFR LKSYKNKSLN PDEMRRRREE EGLQLRKQKR EEQLFKRRNV    50
    ATAEEETEEE VMSDGGFHEA QISNMEMAPG GVITSDMIEM IFSKSPEQQL 100
    SATQKFRKLL SKEPNPPIDE VISTPGVVAR FVEFLKRKEN CTLQFESAWV 150
    LTNIASGNSL QTRIVIQAGA VPIFIELLSS EFEDVQEQAV WALGNIAGDS 200
    TMCRDYVLDC NILPPLLQLF SKQNRLTMTR NAVWALSNLC RGKSPPPEFA 250
    KVSPCLNVLS WLLFVSDTDV LADACWALSY LSDGPNDKIQ AVIDAGVCRR 300
    LVELLMHNDY KVVSPALRAV GNIVTGDDIQ TQVILNCSAL QSLLHLLSSP 350
    KESIKKEACW TISNITAGNR AQIQTVIDAN IFPALISILQ TAEFRTRKEA 400
    AWAITNATSG GSAEQIKYLV ELGCIKPLCD LLTVMDSKIV QVALNGLENI 450
    LRLGEQEAKR NGTGINPYCA LIEEAYGLDK IEFLQSHENQ EIYQKAFDLI 500
    EHYFGTEDED SSIAPQVDLN QQQYIFQQCE APMEGFQL 538
    Length:538
    Mass (Da):60,222
    Last modified:May 18, 2010 - v3
    Checksum:iE8407A3352D6051C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti142 – 1421T → S in AAC60648. (PubMed:7831767)Curated
    Sequence conflicti169 – 1691G → R in AAC60648. (PubMed:7831767)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti73 – 731S → N.4 Publications
    Corresponds to variant rs4678193 [ dbSNP | Ensembl ].
    VAR_050002

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S75295 mRNA. Translation: AAC60648.1.
    BT006959 mRNA. Translation: AAP35605.1.
    CR456743 mRNA. Translation: CAG33024.1.
    AC083798 Genomic DNA. No translation available.
    AC096861 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79482.1.
    CH471052 Genomic DNA. Translation: EAW79483.1.
    BC002374 mRNA. Translation: AAH02374.1.
    BC003009 mRNA. Translation: AAH03009.1.
    CCDSiCCDS3013.1.
    PIRiI59931.
    RefSeqiNP_002255.3. NM_002264.3.
    XP_005247494.1. XM_005247437.2.
    UniGeneiHs.161008.

    Genome annotation databases

    EnsembliENST00000344337; ENSP00000343701; ENSG00000114030.
    GeneIDi3836.
    KEGGihsa:3836.
    UCSCiuc003efb.1. human.

    Polymorphism databases

    DMDMi296439328.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S75295 mRNA. Translation: AAC60648.1 .
    BT006959 mRNA. Translation: AAP35605.1 .
    CR456743 mRNA. Translation: CAG33024.1 .
    AC083798 Genomic DNA. No translation available.
    AC096861 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79482.1 .
    CH471052 Genomic DNA. Translation: EAW79483.1 .
    BC002374 mRNA. Translation: AAH02374.1 .
    BC003009 mRNA. Translation: AAH03009.1 .
    CCDSi CCDS3013.1.
    PIRi I59931.
    RefSeqi NP_002255.3. NM_002264.3.
    XP_005247494.1. XM_005247437.2.
    UniGenei Hs.161008.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JDQ X-ray 2.20 A/B 66-512 [» ]
    3TJ3 X-ray 2.70 A/B 66-512 [» ]
    4B18 X-ray 2.52 A 66-512 [» ]
    ProteinModelPortali P52294.
    SMRi P52294. Positions 10-509.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110034. 62 interactions.
    DIPi DIP-29296N.
    IntActi P52294. 33 interactions.
    MINTi MINT-240027.
    STRINGi 9606.ENSP00000343701.

    PTM databases

    PhosphoSitei P52294.

    Polymorphism databases

    DMDMi 296439328.

    Proteomic databases

    MaxQBi P52294.
    PaxDbi P52294.
    PRIDEi P52294.

    Protocols and materials databases

    DNASUi 3836.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344337 ; ENSP00000343701 ; ENSG00000114030 .
    GeneIDi 3836.
    KEGGi hsa:3836.
    UCSCi uc003efb.1. human.

    Organism-specific databases

    CTDi 3836.
    GeneCardsi GC03M122140.
    HGNCi HGNC:6394. KPNA1.
    HPAi HPA053627.
    MIMi 600686. gene.
    neXtProti NX_P52294.
    PharmGKBi PA30185.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5064.
    HOGENOMi HOG000167616.
    HOVERGENi HBG001846.
    InParanoidi P52294.
    KOi K15042.
    OMAi ETEPNPP.
    OrthoDBi EOG7VHSWV.
    PhylomeDBi P52294.
    TreeFami TF354205.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_13462. Activation of DNA fragmentation factor.
    REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    SignaLinki P52294.

    Miscellaneous databases

    EvolutionaryTracei P52294.
    GeneWikii Karyopherin_alpha_1.
    GenomeRNAii 3836.
    NextBioi 15079.
    PMAP-CutDB P52294.
    PROi P52294.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52294.
    Bgeei P52294.
    CleanExi HS_KPNA1.
    Genevestigatori P52294.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR002652. Importin-a_IBB.
    IPR024931. Importing_su_alpha.
    [Graphical view ]
    Pfami PF00514. Arm. 8 hits.
    PF01749. IBB. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005673. Importin_alpha. 1 hit.
    SMARTi SM00185. ARM. 8 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50176. ARM_REPEAT. 4 hits.
    PS51214. IBB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NPI-1, the human homolog of SRP-1, interacts with influenza virus nucleoprotein."
      O'Neill R.E., Palese P.
      Virology 206:116-125(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-73.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-73.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-73.
    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], VARIANT ASN-73.
      Tissue: Lung.
    7. "RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1."
      Cortes P., Ye Z.-S., Baltimore D.
      Proc. Natl. Acad. Sci. U.S.A. 91:7633-7637(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAG1.
    8. "Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes."
      Moroianu J., Blobel G., Radu A.
      Proc. Natl. Acad. Sci. U.S.A. 92:2008-2011(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence."
      Moroianu J., Blobel G., Radu A.
      Proc. Natl. Acad. Sci. U.S.A. 93:6572-6576(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 481-495, DOMAINS IBB.
    10. "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins."
      Moroianu J., Hijikata M., Blobel G., Radu A.
      Proc. Natl. Acad. Sci. U.S.A. 92:6532-6536(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT.
    11. "Viral protein R regulates nuclear import of the HIV-1 pre-integration complex."
      Popov S., Rexach M., Zybarth G., Reiling N., Lee M.A., Ratner L., Lane C.M., Moore M.S., Blobel G., Bukrinsky M.
      EMBO J. 17:909-917(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 VPR.
    12. "A nonconventional nuclear localization signal within the UL84 protein of human cytomegalovirus mediates nuclear import via the importin alpha/beta pathway."
      Lischka P., Sorg G., Kann M., Winkler M., Stamminger T.
      J. Virol. 77:3734-3748(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCMV UL84.
    13. "Analysis of nuclear transport signals in the human apurinic/apyrimidinic endonuclease (APE1/Ref1)."
      Jackson E.B., Theriot C.A., Chattopadhyay R., Mitra S., Izumi T.
      Nucleic Acids Res. 33:3303-3312(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APEX1.
    14. "Ebola virus VP24 binds karyopherin alpha-1 and blocks STAT1 nuclear accumulation."
      Reid S.P., Leung L.W., Hartman A.L., Martinez O., Shaw M.L., Carbonnelle C., Volchkov V.E., Nichol S.T., Basler C.F.
      J. Virol. 80:5156-5167(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EBOLAVIRUS VP24.
    15. "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.
    16. "Karyopherin alpha 1 is a putative substrate of the RAG1 ubiquitin ligase."
      Simkus C., Makiya M., Jones J.M.
      Mol. Immunol. 46:1319-1325(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Importin alpha protein acts as a negative regulator for Snail protein nuclear import."
      Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.
      J. Biol. Chem. 286:15126-15131(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNAI1.
    19. "CTNNBL1 is a novel nuclear localization sequence-binding protein that recognizes RNA-splicing factors CDC5L and Prp31."
      Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.
      J. Biol. Chem. 286:17091-17102(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTNNBL1 AND AICDA.
    20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIMA5_HUMAN
    AccessioniPrimary (citable) accession number: P52294
    Secondary accession number(s): D3DN93, Q6IBQ9, Q9BQ56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 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 3
      Human chromosome 3: 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