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Q02821

- IMA1_YEAST

UniProt

Q02821 - IMA1_YEAST

Protein

Importin subunit alpha

Gene

SRP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein transporter activity Source: SGD

    GO - Biological processi

    1. protein import into nucleus Source: SGD
    2. protein targeting to membrane Source: SGD

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33200-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Importin subunit alpha
    Alternative name(s):
    Karyopherin subunit alpha
    Karyopherin-60
    Serine-rich RNA polymerase I suppressor protein
    Gene namesi
    Name:SRP1
    Synonyms:KAP60
    Ordered Locus Names:YNL189W
    ORF Names:N1606
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL189w.
    SGDiS000005133. SRP1.

    Subcellular locationi

    Cytoplasmperinuclear region
    Note: Mainly localized at the periphery of the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: SGD
    3. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi116 – 1161S → F in SRP1-31; temperature-sensitive mutant; reduced growth rate and chromosome loss. 1 Publication
    Mutagenesisi145 – 1451E → K in SRP1-49; temperature-sensitive mutant; alteration in nucleolar and microtubule morphology. 1 Publication
    Mutagenesisi219 – 2191P → Q in SRP1-1; temperature-sensitive mutant. 1 Publication
    Mutagenesisi286 – 2861D → N in SRP1-3; temperature-sensitive mutant. 1 Publication
    Mutagenesisi360 – 3601E → K in SRP1-2; temperature-sensitive mutant. 1 Publication
    Mutagenesisi459 – 4591G → V in SRP1-54; temperature-sensitive mutant; reduced growth rate. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 542542Importin subunit alphaPRO_0000120744Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ02821.
    PaxDbiQ02821.
    PeptideAtlasiQ02821.

    Expressioni

    Gene expression databases

    GenevestigatoriQ02821.

    Interactioni

    Subunit structurei

    Forms a complex with an importin beta subunit. In the nucleus, interacts with NUP2 which accelerate release of NLSs, NUP2 is subsequently displaced by CSE1:RanGTP which mediates re-export and recycling. Interacts with HEH2, SHE2, and STS1.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CBC2Q089203EBI-1797,EBI-33556
    CSE1P333072EBI-1797,EBI-5168
    KAP95Q061425EBI-1797,EBI-9145
    NUP2P324993EBI-1797,EBI-12401

    Protein-protein interaction databases

    BioGridi35644. 241 interactions.
    DIPiDIP-728N.
    IntActiQ02821. 134 interactions.
    MINTiMINT-386354.
    STRINGi4932.YNL189W.

    Structurei

    Secondary structure

    1
    542
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 173
    Helixi89 – 968
    Beta strandi97 – 993
    Helixi101 – 11414
    Beta strandi118 – 1203
    Helixi123 – 1286
    Helixi132 – 1376
    Helixi145 – 15814
    Helixi163 – 1719
    Helixi175 – 18410
    Helixi187 – 20115
    Helixi205 – 2139
    Helixi217 – 2226
    Helixi223 – 2253
    Helixi229 – 24315
    Beta strandi246 – 2483
    Helixi252 – 2554
    Helixi256 – 2583
    Helixi259 – 2657
    Helixi271 – 28515
    Helixi289 – 2979
    Helixi301 – 3066
    Helixi307 – 3093
    Helixi313 – 32614
    Helixi331 – 3399
    Helixi342 – 3498
    Helixi355 – 36814
    Helixi373 – 3819
    Helixi385 – 39410
    Helixi397 – 41317
    Turni414 – 4163
    Helixi419 – 4268
    Helixi430 – 4367
    Turni437 – 4393
    Helixi442 – 46625
    Helixi472 – 4798
    Helixi482 – 4876
    Helixi488 – 4914
    Beta strandi492 – 4943
    Helixi495 – 50814
    Beta strandi509 – 5113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BK5X-ray2.20A/B89-510[»]
    1BK6X-ray2.80A/B89-510[»]
    1EE4X-ray2.10A/B87-509[»]
    1EE5X-ray2.40A87-510[»]
    1UN0X-ray2.60A/B88-530[»]
    1WA5X-ray2.00B1-530[»]
    2C1TX-ray2.60A/B88-541[»]
    ProteinModelPortaliQ02821.
    SMRiQ02821. Positions 37-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02821.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6565IBBPROSITE-ProRule annotationAdd
    BLAST
    Repeati89 – 12234ARM 1; truncated1 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati123 – 16240ARM 21 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati163 – 20442ARM 31 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati205 – 25147ARM 41 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati252 – 28837ARM 51 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati289 – 33042ARM 61 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati331 – 37242ARM 71 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati373 – 41745ARM 81 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati418 – 47154ARM 91 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati472 – 50837ARM 10; atypical1 PublicationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni209 – 335127NLS binding site 1Add
    BLAST
    Regioni419 – 50587NLS binding site 2Add
    BLAST

    Domaini

    The 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.

    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.
    GeneTreeiENSGT00610000085856.
    HOGENOMiHOG000167616.
    OMAiCQQNEND.
    OrthoDBiEOG7DC2DF.

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

    Sequencei

    Sequence statusi: Complete.

    Q02821-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDNGTDSSTS KFVPEYRRTN FKNKGRFSAD ELRRRRDTQQ VELRKAKRDE    50
    ALAKRRNFIP PTDGADSDEE DESSVSADQQ FYSQLQQELP QMTQQLNSDD 100
    MQEQLSATVK FRQILSREHR PPIDVVIQAG VVPRLVEFMR ENQPEMLQLE 150
    AAWALTNIAS GTSAQTKVVV DADAVPLFIQ LLYTGSVEVK EQAIWALGNV 200
    AGDSTDYRDY VLQCNAMEPI LGLFNSNKPS LIRTATWTLS NLCRGKKPQP 250
    DWSVVSQALP TLAKLIYSMD TETLVDACWA ISYLSDGPQE AIQAVIDVRI 300
    PKRLVELLSH ESTLVQTPAL RAVGNIVTGN DLQTQVVINA GVLPALRLLL 350
    SSPKENIKKE ACWTISNITA GNTEQIQAVI DANLIPPLVK LLEVAEYKTK 400
    KEACWAISNA SSGGLQRPDI IRYLVSQGCI KPLCDLLEIA DNRIIEVTLD 450
    ALENILKMGE ADKEARGLNI NENADFIEKA GGMEKIFNCQ QNENDKIYEK 500
    AYKIIETYFG EEEDAVDETM APQNAGNTFG FGSNVNQQFN FN 542
    Length:542
    Mass (Da):60,441
    Last modified:July 1, 1993 - v1
    Checksum:i8D3A0CB76F2E7C00
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M75849 Genomic DNA. Translation: AAA35090.1.
    Z71465 Genomic DNA. Translation: CAA96083.1.
    BK006947 Genomic DNA. Translation: DAA10364.1.
    PIRiS30884.
    RefSeqiNP_014210.1. NM_001183027.1.

    Genome annotation databases

    EnsemblFungiiYNL189W; YNL189W; YNL189W.
    GeneIDi855532.
    KEGGisce:YNL189W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M75849 Genomic DNA. Translation: AAA35090.1 .
    Z71465 Genomic DNA. Translation: CAA96083.1 .
    BK006947 Genomic DNA. Translation: DAA10364.1 .
    PIRi S30884.
    RefSeqi NP_014210.1. NM_001183027.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BK5 X-ray 2.20 A/B 89-510 [» ]
    1BK6 X-ray 2.80 A/B 89-510 [» ]
    1EE4 X-ray 2.10 A/B 87-509 [» ]
    1EE5 X-ray 2.40 A 87-510 [» ]
    1UN0 X-ray 2.60 A/B 88-530 [» ]
    1WA5 X-ray 2.00 B 1-530 [» ]
    2C1T X-ray 2.60 A/B 88-541 [» ]
    ProteinModelPortali Q02821.
    SMRi Q02821. Positions 37-513.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35644. 241 interactions.
    DIPi DIP-728N.
    IntActi Q02821. 134 interactions.
    MINTi MINT-386354.
    STRINGi 4932.YNL189W.

    Proteomic databases

    MaxQBi Q02821.
    PaxDbi Q02821.
    PeptideAtlasi Q02821.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL189W ; YNL189W ; YNL189W .
    GeneIDi 855532.
    KEGGi sce:YNL189W.

    Organism-specific databases

    CYGDi YNL189w.
    SGDi S000005133. SRP1.

    Phylogenomic databases

    eggNOGi COG5064.
    GeneTreei ENSGT00610000085856.
    HOGENOMi HOG000167616.
    OMAi CQQNEND.
    OrthoDBi EOG7DC2DF.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33200-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q02821.
    NextBioi 979583.
    PROi Q02821.

    Gene expression databases

    Genevestigatori Q02821.

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

    Publicationsi

    1. "Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae."
      Yano R., Oakes M., Yamaghishi M., Dodd J.A., Nomura M.
      Mol. Cell. Biol. 12:5640-5651(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is required for normal migration, division, and integrity of nuclei during mitosis."
      Kuessel P., Frasch M.
      Mol. Gen. Genet. 248:351-363(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: ATCC 200060 / W303.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Yeast Srp1p has homology to armadillo/plakoglobin/beta-catenin and participates in apparently multiple nuclear functions including the maintenance of the nucleolar structure."
      Yano R., Oakes M.L., Tabb M.M., Nomura M.
      Proc. Natl. Acad. Sci. U.S.A. 91:6880-6884(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    6. "Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes."
      Enenkel C., Blobel G., Rexach M.
      J. Biol. Chem. 270:16499-16502(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    7. "Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins."
      Rexach M., Blobel G.
      Cell 83:683-692(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOPORIN REPEAT BINDING REQUIREMENT.
    8. "Evidence for separable functions of Srp1p, the yeast homolog of importin alpha (Karyopherin alpha): role for Srp1p and Sts1p in protein degradation."
      Tabb M.M., Tongaonkar P., Vu L., Nomura M.
      Mol. Cell. Biol. 20:6062-6073(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH STS1.
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "Karyopherin-mediated import of integral inner nuclear membrane proteins."
      King M.C., Lusk C.P., Blobel G.
      Nature 442:1003-1007(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HEH2.
    11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    12. "Nuclear shuttling of She2p couples ASH1 mRNA localization to its translational repression by recruiting Loc1p and Puf6p."
      Shen Z., Paquin N., Forget A., Chartrand P.
      Mol. Biol. Cell 20:2265-2275(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHE2.
    13. Cited for: FUNCTION, INTERACTION WITH STS1.
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha."
      Conti E., Uy M., Leighton L., Blobel G., Kuriyan J.
      Cell 94:193-204(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 89-510.
    16. "Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha."
      Conti E., Kuriyan J.
      Structure 8:329-338(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 87-509 IN COMPLEX WITH NLS PEPTIDE.
    17. "Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import."
      Matsuura Y., Lange A., Harreman M.T., Corbett A.H., Stewart M.
      EMBO J. 22:5358-5369(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 88-530 IN COMPLEX WITH NUP2.
    18. "Structural basis for the assembly of a nuclear export complex."
      Matsuura Y., Stewart M.
      Nature 432:872-877(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-530 IN COMPLEX WITH CSE1 AND RANGTP.

    Entry informationi

    Entry nameiIMA1_YEAST
    AccessioniPrimary (citable) accession number: Q02821
    Secondary accession number(s): D6W0Z8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binds to nucleoporin FxFG but not GLFG repeat regions. Ran-GTP can disrupt the karyopherin heterodimer by binding to the beta subunit and releases both subunits from the docking site.
    Present with 2790 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3