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Q02821

- IMA1_YEAST

UniProt

Q02821 - IMA1_YEAST

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Protein

Importin subunit alpha

Gene
SRP1, KAP60, YNL189W, N1606
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.3 Publications

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
Complete GO annotation...

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
Complete GO annotation...

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.
Mutagenesisi145 – 1451E → K in SRP1-49; temperature-sensitive mutant; alteration in nucleolar and microtubule morphology.
Mutagenesisi219 – 2191P → Q in SRP1-1; temperature-sensitive mutant.
Mutagenesisi286 – 2861D → N in SRP1-3; temperature-sensitive mutant.
Mutagenesisi360 – 3601E → K in SRP1-2; temperature-sensitive mutant.
Mutagenesisi459 – 4591G → V in SRP1-54; temperature-sensitive mutant; reduced growth rate.

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 STS1.4 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.

Miscellaneous databases

EvolutionaryTraceiQ02821.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6565IBBAdd
BLAST
Repeati89 – 12234ARM 1; truncatedAdd
BLAST
Repeati123 – 16240ARM 2Add
BLAST
Repeati163 – 20442ARM 3Add
BLAST
Repeati205 – 25147ARM 4Add
BLAST
Repeati252 – 28837ARM 5Add
BLAST
Repeati289 – 33042ARM 6Add
BLAST
Repeati331 – 37242ARM 7Add
BLAST
Repeati373 – 41745ARM 8Add
BLAST
Repeati418 – 47154ARM 9Add
BLAST
Repeati472 – 50837ARM 10; atypicalAdd
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.
Contains 10 ARM repeats.
Contains 1 IBB domain.

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 138 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.

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

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