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P52292

- IMA1_HUMAN

UniProt

P52292 - IMA1_HUMAN

Protein

Importin subunit alpha-1

Gene

KPNA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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.

    GO - Molecular functioni

    1. histone deacetylase binding Source: BHF-UCL
    2. nuclear localization sequence binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein transporter activity Source: InterPro

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. DNA metabolic process Source: ProtInc
    3. mitotic G2 phase Source: ProtInc
    4. NLS-bearing protein import into nucleus Source: UniProtKB
    5. regulation of DNA recombination Source: ProtInc
    6. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    SignaLinkiP52292.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Importin subunit alpha-1
    Alternative name(s):
    Karyopherin subunit alpha-2
    RAG cohort protein 1
    SRP1-alpha
    Gene namesi
    Name:KPNA2
    Synonyms:RCH1, SRP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:6395. KPNA2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30186.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 529528Importin subunit alpha-1PRO_0000120722Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine4 Publications
    Modified residuei62 – 621Phosphoserine5 Publications
    Modified residuei490 – 4901Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP52292.
    PaxDbiP52292.
    PeptideAtlasiP52292.
    PRIDEiP52292.

    2D gel databases

    SWISS-2DPAGEP52292.

    PTM databases

    PhosphoSiteiP52292.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously.

    Gene expression databases

    ArrayExpressiP52292.
    BgeeiP52292.
    CleanExiHS_KPNA2.
    GenevestigatoriP52292.

    Organism-specific databases

    HPAiCAB015460.
    HPA041270.

    Interactioni

    Subunit structurei

    Heterodimer; with KPNB1. Interacts with ANP32E By similarity. Component of a complex containing CSE1L, RAN and KPNA2. Interacts directly with CSE1L. Interacts with HIV-1 Vpr and PLAG1. Interacts with APEX1 (via N-terminus). Interacts with FRG1 (via N-terminus). Interacts with ARL4A, CTNNBL1 and NBN. Interacts with SNAI1 (via zinc fingers) and SNAI2 (via zinc fingers).By similarity12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA1P383983EBI-349938,EBI-349905
    JUNP054122EBI-349938,EBI-852823
    L1P031013EBI-349938,EBI-7362698From a different organism.
    L2P031073EBI-349938,EBI-7362531From a different organism.
    npm2Q6GQG62EBI-349938,EBI-8469111From a different organism.
    RECQLP460632EBI-349938,EBI-2823728
    S100A2P290345EBI-349938,EBI-752230
    S100A6P067033EBI-349938,EBI-352877
    SUN2Q9UH993EBI-349938,EBI-1044964

    Protein-protein interaction databases

    BioGridi110036. 131 interactions.
    DIPiDIP-6205N.
    IntActiP52292. 73 interactions.
    MINTiMINT-94121.
    STRINGi9606.ENSP00000332455.

    Structurei

    Secondary structure

    1
    529
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 163
    Turni18 – 214
    Helixi30 – 4819
    Helixi78 – 858
    Helixi90 – 10415
    Beta strandi106 – 1083
    Helixi112 – 1176
    Helixi120 – 12910
    Helixi134 – 14714
    Helixi152 – 1609
    Helixi163 – 1708
    Helixi176 – 19015
    Helixi194 – 2029
    Helixi206 – 2116
    Helixi218 – 2203
    Helixi223 – 23614
    Helixi246 – 25914
    Helixi265 – 27915
    Helixi283 – 2919
    Helixi295 – 3017
    Helixi307 – 32014
    Helixi325 – 3339
    Helixi336 – 3449
    Helixi349 – 36214
    Helixi367 – 3759
    Helixi379 – 38810
    Helixi391 – 40717
    Helixi410 – 4189
    Helixi422 – 4276
    Helixi428 – 4303
    Helixi434 – 45320
    Helixi457 – 46610
    Helixi469 – 4757
    Helixi476 – 4783
    Helixi482 – 49514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EFXX-ray3.00C204-212[»]
    1QGKX-ray2.50B11-54[»]
    1QGRX-ray2.30B28-54[»]
    3FEXX-ray3.55C70-529[»]
    3FEYX-ray2.20C70-529[»]
    4E4VX-ray2.53A/B70-529[»]
    ProteinModelPortaliP52292.
    SMRiP52292. Positions 11-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52292.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 6059IBBPROSITE-ProRule annotationAdd
    BLAST
    Repeati71 – 11141ARM 1; truncatedAdd
    BLAST
    Repeati112 – 15140ARM 2Add
    BLAST
    Repeati152 – 19342ARM 3Add
    BLAST
    Repeati200 – 24445ARM 4Add
    BLAST
    Repeati246 – 28237ARM 5Add
    BLAST
    Repeati283 – 32240ARM 6Add
    BLAST
    Repeati325 – 36440ARM 7Add
    BLAST
    Repeati367 – 40943ARM 8Add
    BLAST
    Repeati410 – 45647ARM 9Add
    BLAST
    Repeati457 – 49640ARM 10; atypicalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni142 – 23897NLS binding site (major)By similarityAdd
    BLAST
    Regioni315 – 40389NLS binding site (minor)By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi45 – 5410Nuclear localization signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi28 – 314Poly-Arg
    Compositional biasi499 – 5024Poly-Glu

    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.
    InParanoidiP52292.
    KOiK15043.
    OMAiNETEKLC.
    PhylomeDBiP52292.
    TreeFamiTF101178.

    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. 5 hits.
    PS51214. IBB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P52292-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTNENANTP AARLHRFKNK GKDSTEMRRR RIEVNVELRK AKKDDQMLKR    50
    RNVSSFPDDA TSPLQENRNN QGTVNWSVDD IVKGINSSNV ENQLQATQAA 100
    RKLLSREKQP PIDNIIRAGL IPKFVSFLGR TDCSPIQFES AWALTNIASG 150
    TSEQTKAVVD GGAIPAFISL LASPHAHISE QAVWALGNIA GDGSVFRDLV 200
    IKYGAVDPLL ALLAVPDMSS LACGYLRNLT WTLSNLCRNK NPAPPIDAVE 250
    QILPTLVRLL HHDDPEVLAD TCWAISYLTD GPNERIGMVV KTGVVPQLVK 300
    LLGASELPIV TPALRAIGNI VTGTDEQTQV VIDAGALAVF PSLLTNPKTN 350
    IQKEATWTMS NITAGRQDQI QQVVNHGLVP FLVSVLSKAD FKTQKEAVWA 400
    VTNYTSGGTV EQIVYLVHCG IIEPLMNLLT AKDTKIILVI LDAISNIFQA 450
    AEKLGETEKL SIMIEECGGL DKIEALQNHE NESVYKASLS LIEKYFSVEE 500
    EEDQNVVPET TSEGYTFQVQ DGAPGTFNF 529
    Length:529
    Mass (Da):57,862
    Last modified:October 1, 1996 - v1
    Checksum:iB0F94A0475B80EED
    GO

    Mass spectrometryi

    Molecular mass is 57861.92 Da from positions 1 - 529. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti157 – 1571A → V.2 Publications
    Corresponds to variant rs17850032 [ dbSNP | Ensembl ].
    VAR_067625
    Natural varianti165 – 1651P → R.1 Publication
    Corresponds to variant rs11545989 [ dbSNP | Ensembl ].
    VAR_013137
    Natural varianti365 – 3651G → S.
    Corresponds to variant rs1059558 [ dbSNP | Ensembl ].
    VAR_067626
    Natural varianti430 – 4301T → P.
    Corresponds to variant rs1059538 [ dbSNP | Ensembl ].
    VAR_014453
    Natural varianti453 – 4531K → N.2 Publications
    Corresponds to variant rs17850031 [ dbSNP | Ensembl ].
    VAR_067627

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28386 mRNA. Translation: AAA69957.1.
    AJ303086 Genomic DNA. Translation: CAC83080.1.
    BT006665 mRNA. Translation: AAP35311.1.
    CH471099 Genomic DNA. Translation: EAW89041.1.
    BC005978 mRNA. Translation: AAH05978.1.
    BC146905 mRNA. Translation: AAI46906.1.
    U09559 mRNA. Translation: AAA65700.1.
    CCDSiCCDS32713.1.
    PIRiA56516.
    RefSeqiNP_002257.1. NM_002266.2.
    UniGeneiHs.594238.

    Genome annotation databases

    GeneIDi3838.
    KEGGihsa:3838.
    UCSCiuc002jgk.3. human.

    Polymorphism databases

    DMDMi1708480.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28386 mRNA. Translation: AAA69957.1 .
    AJ303086 Genomic DNA. Translation: CAC83080.1 .
    BT006665 mRNA. Translation: AAP35311.1 .
    CH471099 Genomic DNA. Translation: EAW89041.1 .
    BC005978 mRNA. Translation: AAH05978.1 .
    BC146905 mRNA. Translation: AAI46906.1 .
    U09559 mRNA. Translation: AAA65700.1 .
    CCDSi CCDS32713.1.
    PIRi A56516.
    RefSeqi NP_002257.1. NM_002266.2.
    UniGenei Hs.594238.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EFX X-ray 3.00 C 204-212 [» ]
    1QGK X-ray 2.50 B 11-54 [» ]
    1QGR X-ray 2.30 B 28-54 [» ]
    3FEX X-ray 3.55 C 70-529 [» ]
    3FEY X-ray 2.20 C 70-529 [» ]
    4E4V X-ray 2.53 A/B 70-529 [» ]
    ProteinModelPortali P52292.
    SMRi P52292. Positions 11-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110036. 131 interactions.
    DIPi DIP-6205N.
    IntActi P52292. 73 interactions.
    MINTi MINT-94121.
    STRINGi 9606.ENSP00000332455.

    Chemistry

    BindingDBi P52292.
    ChEMBLi CHEMBL1741187.

    PTM databases

    PhosphoSitei P52292.

    Polymorphism databases

    DMDMi 1708480.

    2D gel databases

    SWISS-2DPAGE P52292.

    Proteomic databases

    MaxQBi P52292.
    PaxDbi P52292.
    PeptideAtlasi P52292.
    PRIDEi P52292.

    Protocols and materials databases

    DNASUi 3838.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3838.
    KEGGi hsa:3838.
    UCSCi uc002jgk.3. human.

    Organism-specific databases

    CTDi 3838.
    GeneCardsi GC17P066031.
    HGNCi HGNC:6395. KPNA2.
    HPAi CAB015460.
    HPA041270.
    MIMi 600685. gene.
    neXtProti NX_P52292.
    PharmGKBi PA30186.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5064.
    HOGENOMi HOG000167616.
    HOVERGENi HBG001846.
    InParanoidi P52292.
    KOi K15043.
    OMAi NETEKLC.
    PhylomeDBi P52292.
    TreeFami TF101178.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    SignaLinki P52292.

    Miscellaneous databases

    ChiTaRSi KPNA2. human.
    EvolutionaryTracei P52292.
    GeneWikii Karyopherin_alpha_2.
    GenomeRNAii 3838.
    NextBioi 15087.
    PROi P52292.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52292.
    Bgeei P52292.
    CleanExi HS_KPNA2.
    Genevestigatori P52292.

    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. 5 hits.
    PS51214. IBB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences."
      Weis K., Mattaj I.W., Lamond A.I.
      Science 268:1049-1053(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Genomic structure of karyopherin alpha2 (KPNA2) within a low-copy repeat on chromosome 17q23-q24 and mutation analysis in patients with Russell-Silver syndrome."
      Doerr S., Schlicker M., Hansmann I.
      Hum. Genet. 109:479-486(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-165.
    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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-157 AND ASN-453.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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], VARIANTS VAL-157 AND ASN-453.
      Tissue: Bone marrow and Testis.
    6. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13; 69-101; 107-117; 239-258; 292-315; 354-388 AND 487-494, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    7. "Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein."
      Cuomo C.A., Kirch S.A., Gyuris J., Brent R., Oettinger M.A.
      Proc. Natl. Acad. Sci. U.S.A. 91:6156-6160(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-529.
      Tissue: Cervix carcinoma.
    8. "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: SUBUNIT, SUBCELLULAR LOCATION.
    9. "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: DOMAIN IBB.
    10. "Export of importin-alpha from the nucleus is mediated by a specific nuclear transport factor."
      Kutay U., Bischoff F.R., Kostka S., Kraft R., Goerlich D.
      Cell 90:1061-1071(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH RAN AND CSE1L.
    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. "Determination of the functional domain organization of the importin alpha nuclear import factor."
      Herold A., Truant R., Wiegand H., Cullen B.R.
      J. Cell Biol. 143:309-318(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XPO2/CSE1L.
    13. "ARL4, an ARF-like protein that is developmentally regulated and localized to nuclei and nucleoli."
      Lin C.Y., Huang P.H., Liao W.L., Cheng H.J., Huang C.F., Kuo J.C., Patton W.A., Massenburg D., Moss J., Lee F.J.
      J. Biol. Chem. 275:37815-37823(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARL4A.
    14. "Identification of a karyopherin alpha 2 recognition site in PLAG1, which functions as a nuclear localization signal."
      Braem C.V., Kas K., Meyen E., Debiec-Rychter M., Van De Ven W.J.M., Voz M.L.
      J. Biol. Chem. 277:19673-19678(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLAG1.
    15. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
      Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
      Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    16. "Importin KPNA2 is required for proper nuclear localization and multiple functions of NBS1."
      Tseng S.-F., Chang C.-Y., Wu K.-J., Teng S.-C.
      J. Biol. Chem. 280:39594-39600(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NBN.
    17. "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.
    18. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "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.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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.
    25. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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.
    29. "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.
    30. "Facioscapulohumeral muscular dystrophy region gene 1 is a dynamic RNA-associated and actin-bundling protein."
      Sun C.Y., van Koningsbruggen S., Long S.W., Straasheijm K., Klooster R., Jones T.I., Bellini M., Levesque L., Brieher W.M., van der Maarel S.M., Jones P.L.
      J. Mol. Biol. 411:397-416(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FRG1.
    31. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "Structure of importin-beta bound to the IBB domain of importin-alpha."
      Cingolani G., Petosa C., Weis K., Muller C.W.
      Nature 399:221-229(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 11-54.

    Entry informationi

    Entry nameiIMA1_HUMAN
    AccessioniPrimary (citable) accession number: P52292
    Secondary accession number(s): B9EJD6, Q53YE3, Q9BRU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 173 of the entry and version 1 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. 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