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Protein

Importin subunit alpha

Gene

SRP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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 similarity3 Publications

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

GO - Molecular functioni

  • disordered domain specific binding Source: CAFA
  • nuclear import signal receptor activity Source: InterPro
  • nuclear localization sequence binding Source: GO_Central
  • protein transporter activity Source: SGD

GO - Biological processi

  • NLS-bearing protein import into nucleus Source: GO_Central
  • proteasome localization Source: SGD
  • protein import into nucleus Source: SGD
  • protein targeting to membrane Source: SGD

Keywordsi

Biological processProtein 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
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL189W
SGDiS000005133 SRP1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi116S → F in SRP1-31; temperature-sensitive mutant; reduced growth rate and chromosome loss. 1 Publication1
Mutagenesisi145E → K in SRP1-49; temperature-sensitive mutant; alteration in nucleolar and microtubule morphology. 1 Publication1
Mutagenesisi219P → Q in SRP1-1; temperature-sensitive mutant. 1 Publication1
Mutagenesisi286D → N in SRP1-3; temperature-sensitive mutant. 1 Publication1
Mutagenesisi360E → K in SRP1-2; temperature-sensitive mutant. 1 Publication1
Mutagenesisi459G → V in SRP1-54; temperature-sensitive mutant; reduced growth rate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001207441 – 542Importin subunit alphaAdd BLAST542

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ02821
PaxDbiQ02821
PRIDEiQ02821

PTM databases

iPTMnetiQ02821

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
P052212EBI-1797,EBI-7261813From Xenopus laevis.
ACTBP607093EBI-1797,EBI-353944From Homo sapiens.
ACTG1P632613EBI-1797,EBI-351292From Homo sapiens.
ALAS1P131963EBI-1797,EBI-3905054From Homo sapiens.
ARL6IP1Q150413EBI-1797,EBI-714543From Homo sapiens.
BLMHQ138673EBI-1797,EBI-718504From Homo sapiens.
CALCOCO2Q131373EBI-1797,EBI-739580From Homo sapiens.
CAMK2DQ13557-83EBI-1797,EBI-11534483From a different organism.
CBC2Q0892010EBI-1797,EBI-33556
CBSP355203EBI-1797,EBI-740135From Homo sapiens.
CDC73Q066976EBI-1797,EBI-29913
CSE1P333072EBI-1797,EBI-5168
DAZAP2Q150383EBI-1797,EBI-724310From Homo sapiens.
DIS3Q081623EBI-1797,EBI-1740
EAF7P539116EBI-1797,EBI-28927
EFT2P323242EBI-1797,EBI-6333
GAL11P196592EBI-1797,EBI-7305
hCG_2043597Q96A103EBI-1797,EBI-10486892From Homo sapiens.
HEH2Q032817EBI-1797,EBI-22131
HSC82P151082EBI-1797,EBI-8666
KAP95Q0614226EBI-1797,EBI-9145
KCTD4Q8WVF53EBI-1797,EBI-741463From Homo sapiens.
MBIPQ9NS733EBI-1797,EBI-741953From Homo sapiens.
MBIPQ9NS73-53EBI-1797,EBI-10182361From a different organism.
MX1P205913EBI-1797,EBI-929476From Homo sapiens.
NECAB2Q7Z6G3-23EBI-1797,EBI-10172876From a different organism.
NMNAT1Q9HAN93EBI-1797,EBI-3917542From Homo sapiens.
NOP56Q124603EBI-1797,EBI-17148
NOP58Q124993EBI-1797,EBI-12126
NOP7P532618EBI-1797,EBI-13145
NUP1P206768EBI-1797,EBI-12392
NUP2P3249912EBI-1797,EBI-12401
NUP60P3970511EBI-1797,EBI-20731
OGG1P533974EBI-1797,EBI-12494
PAICSP222343EBI-1797,EBI-712261From Homo sapiens.
PCT1P132594EBI-1797,EBI-5254
RAD53P222166EBI-1797,EBI-17843
RCO1Q047793EBI-1797,EBI-28153
RRP43P253592EBI-1797,EBI-1773
RRP6Q121494EBI-1797,EBI-1782
RTT103Q055433EBI-1797,EBI-35018
SIN3P225793EBI-1797,EBI-17160
SPT2P068433EBI-1797,EBI-17914
SRC1Q037075EBI-1797,EBI-18064
STO1P3416011EBI-1797,EBI-745
THAP1Q9NVV93EBI-1797,EBI-741515From Homo sapiens.
THO2P535524EBI-1797,EBI-15475
TRIM38O006353EBI-1797,EBI-2130415From Homo sapiens.
ULP1Q027244EBI-1797,EBI-20050
URB2P471083EBI-1797,EBI-25492
UTP14Q045002EBI-1797,EBI-27917
YHC1Q059002EBI-1797,EBI-754
YNG2P388063EBI-1797,EBI-24622
ZBTB32A0A0C4DGF13EBI-1797,EBI-10188476From Homo sapiens.

GO - Molecular functioni

  • disordered domain specific binding Source: CAFA

Protein-protein interaction databases

BioGridi35644, 395 interactors
DIPiDIP-728N
ELMiQ02821
IntActiQ02821, 180 interactors
MINTiQ02821
STRINGi4932.YNL189W

Structurei

Secondary structure

1542
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 17Combined sources3
Helixi89 – 96Combined sources8
Beta strandi97 – 99Combined sources3
Helixi101 – 114Combined sources14
Beta strandi118 – 120Combined sources3
Helixi123 – 128Combined sources6
Helixi132 – 137Combined sources6
Beta strandi140 – 143Combined sources4
Helixi145 – 158Combined sources14
Helixi163 – 171Combined sources9
Helixi175 – 184Combined sources10
Helixi187 – 201Combined sources15
Helixi205 – 213Combined sources9
Helixi217 – 222Combined sources6
Helixi223 – 225Combined sources3
Helixi229 – 243Combined sources15
Beta strandi246 – 248Combined sources3
Helixi252 – 255Combined sources4
Helixi256 – 258Combined sources3
Helixi259 – 265Combined sources7
Helixi271 – 285Combined sources15
Beta strandi286 – 288Combined sources3
Helixi289 – 297Combined sources9
Helixi301 – 306Combined sources6
Helixi307 – 309Combined sources3
Helixi313 – 326Combined sources14
Helixi331 – 339Combined sources9
Helixi342 – 349Combined sources8
Helixi355 – 368Combined sources14
Helixi373 – 381Combined sources9
Helixi385 – 394Combined sources10
Helixi397 – 413Combined sources17
Turni414 – 416Combined sources3
Helixi419 – 426Combined sources8
Helixi430 – 436Combined sources7
Turni437 – 439Combined sources3
Helixi442 – 466Combined sources25
Helixi472 – 479Combined sources8
Helixi482 – 487Combined sources6
Helixi488 – 491Combined sources4
Beta strandi492 – 494Combined sources3
Helixi495 – 508Combined sources14
Beta strandi509 – 511Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4PVZX-ray2.50A/B88-509[»]
4XZRX-ray2.25B88-509[»]
5H2WX-ray2.50A/C88-510[»]
5H2XX-ray2.20A88-510[»]
5T94X-ray2.63B1-542[»]
ProteinModelPortaliQ02821
SMRiQ02821
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02821

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 65IBBPROSITE-ProRule annotationAdd BLAST65
Repeati89 – 122ARM 1; truncatedPROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati123 – 162ARM 2PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati163 – 204ARM 3PROSITE-ProRule annotation1 PublicationAdd BLAST42
Repeati205 – 251ARM 4PROSITE-ProRule annotation1 PublicationAdd BLAST47
Repeati252 – 288ARM 5PROSITE-ProRule annotation1 PublicationAdd BLAST37
Repeati289 – 330ARM 6PROSITE-ProRule annotation1 PublicationAdd BLAST42
Repeati331 – 372ARM 7PROSITE-ProRule annotation1 PublicationAdd BLAST42
Repeati373 – 417ARM 8PROSITE-ProRule annotation1 PublicationAdd BLAST45
Repeati418 – 471ARM 9PROSITE-ProRule annotation1 PublicationAdd BLAST54
Repeati472 – 508ARM 10; atypicalPROSITE-ProRule annotation1 PublicationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni209 – 335NLS binding site 1Add BLAST127
Regioni419 – 505NLS binding site 2Add BLAST87

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

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00760000119094
HOGENOMiHOG000167616
InParanoidiQ02821
OMAiPYAITIE
OrthoDBiEOG092C1PRY

Family and domain databases

Gene3Di1.20.5.690, 1 hit
1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR032413 Arm_3
IPR000225 Armadillo
IPR002652 Importin-a_IBB
IPR036975 Importin-a_IBB_sf
IPR024931 Importing_su_alpha
PfamiView protein in Pfam
PF00514 Arm, 8 hits
PF16186 Arm_3, 1 hit
PF01749 IBB, 1 hit
PIRSFiPIRSF005673 Importin_alpha, 1 hit
SMARTiView protein in SMART
SM00185 ARM, 8 hits
SUPFAMiSSF48371 SSF48371, 1 hit
PROSITEiView protein in PROSITE
PS50176 ARM_REPEAT, 2 hits
PS51214 IBB, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiIMA1_YEAST
AccessioniPrimary (citable) accession number: Q02821
Secondary accession number(s): D6W0Z8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 25, 2018
This is version 173 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health