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Protein

Importin subunit alpha

Gene

SRP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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).By similarity

GO - Molecular functioni

  1. protein transporter activity Source: SGD

GO - Biological processi

  1. proteasome localization Source: SGD
  2. protein import into nucleus Source: SGD
  3. 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 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNL189w.
EuPathDBiFungiDB:YNL189W.
SGDiS000005133. SRP1.

Subcellular locationi

  1. Cytoplasmperinuclear region

  2. 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. 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. 243 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 – 173Combined sources
Helixi89 – 968Combined sources
Beta strandi97 – 993Combined sources
Helixi101 – 11414Combined sources
Beta strandi118 – 1203Combined sources
Helixi123 – 1286Combined sources
Helixi132 – 1376Combined sources
Helixi145 – 15814Combined sources
Helixi163 – 1719Combined sources
Helixi175 – 18410Combined sources
Helixi187 – 20115Combined sources
Helixi205 – 2139Combined sources
Helixi217 – 2226Combined sources
Helixi223 – 2253Combined sources
Helixi229 – 24315Combined sources
Beta strandi246 – 2483Combined sources
Helixi252 – 2554Combined sources
Helixi256 – 2583Combined sources
Helixi259 – 2657Combined sources
Helixi271 – 28515Combined sources
Helixi289 – 2979Combined sources
Helixi301 – 3066Combined sources
Helixi307 – 3093Combined sources
Helixi313 – 32614Combined sources
Helixi331 – 3399Combined sources
Helixi342 – 3498Combined sources
Helixi355 – 36814Combined sources
Helixi373 – 3819Combined sources
Helixi385 – 39410Combined sources
Helixi397 – 41317Combined sources
Turni414 – 4163Combined sources
Helixi419 – 4268Combined sources
Helixi430 – 4367Combined sources
Turni437 – 4393Combined sources
Helixi442 – 46625Combined sources
Helixi472 – 4798Combined sources
Helixi482 – 4876Combined sources
Helixi488 – 4914Combined sources
Beta strandi492 – 4943Combined sources
Helixi495 – 50814Combined sources
Beta strandi509 – 5113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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; truncatedPROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati123 – 16240ARM 2PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati163 – 20442ARM 3PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati205 – 25147ARM 4PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati252 – 28837ARM 5PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati289 – 33042ARM 6PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati331 – 37242ARM 7PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati373 – 41745ARM 8PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati418 – 47154ARM 9PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati472 – 50837ARM 10; atypicalPROSITE-ProRule annotation1 PublicationAdd
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.
GeneTreeiENSGT00760000119094.
HOGENOMiHOG000167616.
InParanoidiQ02821.
OMAiGGMERIH.
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

        10         20         30         40         50
MDNGTDSSTS KFVPEYRRTN FKNKGRFSAD ELRRRRDTQQ VELRKAKRDE
60 70 80 90 100
ALAKRRNFIP PTDGADSDEE DESSVSADQQ FYSQLQQELP QMTQQLNSDD
110 120 130 140 150
MQEQLSATVK FRQILSREHR PPIDVVIQAG VVPRLVEFMR ENQPEMLQLE
160 170 180 190 200
AAWALTNIAS GTSAQTKVVV DADAVPLFIQ LLYTGSVEVK EQAIWALGNV
210 220 230 240 250
AGDSTDYRDY VLQCNAMEPI LGLFNSNKPS LIRTATWTLS NLCRGKKPQP
260 270 280 290 300
DWSVVSQALP TLAKLIYSMD TETLVDACWA ISYLSDGPQE AIQAVIDVRI
310 320 330 340 350
PKRLVELLSH ESTLVQTPAL RAVGNIVTGN DLQTQVVINA GVLPALRLLL
360 370 380 390 400
SSPKENIKKE ACWTISNITA GNTEQIQAVI DANLIPPLVK LLEVAEYKTK
410 420 430 440 450
KEACWAISNA SSGGLQRPDI IRYLVSQGCI KPLCDLLEIA DNRIIEVTLD
460 470 480 490 500
ALENILKMGE ADKEARGLNI NENADFIEKA GGMEKIFNCQ QNENDKIYEK
510 520 530 540
AYKIIETYFG EEEDAVDETM APQNAGNTFG FGSNVNQQFN FN
Length:542
Mass (Da):60,441
Last modified:July 1, 1993 - v1
Checksum:i8D3A0CB76F2E7C00
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi35644. 243 interactions.
DIPiDIP-728N.
IntActiQ02821. 134 interactions.
MINTiMINT-386354.
STRINGi4932.YNL189W.

Proteomic databases

MaxQBiQ02821.
PaxDbiQ02821.
PeptideAtlasiQ02821.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYNL189w.
EuPathDBiFungiDB:YNL189W.
SGDiS000005133. SRP1.

Phylogenomic databases

eggNOGiCOG5064.
GeneTreeiENSGT00760000119094.
HOGENOMiHOG000167616.
InParanoidiQ02821.
OMAiGGMERIH.
OrthoDBiEOG7DC2DF.

Enzyme and pathway databases

BioCyciYEAST:G3O-33200-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ02821.
NextBioi979583.
PROiQ02821.

Gene expression databases

GenevestigatoriQ02821.

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]
ProtoNetiSearch...

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: April 29, 2015
This is version 144 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.