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P32337 (IMB3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Importin subunit beta-3
Alternative name(s):
Karyopherin subunit beta-3
Karyopherin-121
Protein secretion enhancer 1
Gene names
Name:PSE1
Synonyms:KAP121
Ordered Locus Names:YMR308C
ORF Names:YM9952.10C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1089 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the nuclear import of ribosomal proteins. Binds to nucleoporins and the GTP-bound form of GSP1 (Ran).

Plays a role in protein secretion.

Subunit structure

Interacts with ABF1. Ref.5

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Miscellaneous

Present with 15500 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the importin beta family.

Contains 9 HEAT repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 10891088Importin subunit beta-3
PRO_0000120774

Regions

Repeat6 – 4338HEAT 1
Repeat135 – 17238HEAT 2
Repeat174 – 21037HEAT 3
Repeat404 – 44138HEAT 4
Repeat446 – 48439HEAT 5
Repeat489 – 52638HEAT 6
Repeat530 – 57041HEAT 7
Repeat719 – 75638HEAT 8
Repeat896 – 93338HEAT 9

Amino acid modifications

Modified residue21N-acetylserine Ref.7
Modified residue8301Phosphothreonine Ref.6

Experimental info

Sequence conflict651A → S in CAA77639. Ref.1
Sequence conflict651A → S in AAA10665. Ref.1
Sequence conflict10771P → A in CAA77639. Ref.1
Sequence conflict10771P → A in AAA10665. Ref.1

Secondary structure

........................................................................................................................................ 1089
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32337 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 9C5F7FB5B8824C37

FASTA1,089121,031
        10         20         30         40         50         60 
MSALPEEVNR TLLQIVQAFA SPDNQIRSVA EKALSEEWIT ENNIEYLLTF LAEQAAFSQD 

        70         80         90        100        110        120 
TTVAALSAVL FRKLALKAPP SSKLMIMSKN ITHIRKEVLA QIRSSLLKGF LSERADSIRH 

       130        140        150        160        170        180 
KLSDAIAECV QDDLPAWPEL LQALIESLKS GNPNFRESSF RILTTVPYLI TAVDINSILP 

       190        200        210        220        230        240 
IFQSGFTDAS DNVKIAAVTA FVGYFKQLPK SEWSKLGILL PSLLNSLPRF LDDGKDDALA 

       250        260        270        280        290        300 
SVFESLIELV ELAPKLFKDM FDQIIQFTDM VIKNKDLEPP ARTTALELLT VFSENAPQMC 

       310        320        330        340        350        360 
KSNQNYGQTL VMVTLIMMTE VSIDDDDAAE WIESDDTDDE EEVTYDHARQ ALDRVALKLG 

       370        380        390        400        410        420 
GEYLAAPLFQ YLQQMITSTE WRERFAAMMA LSSAAEGCAD VLIGEIPKIL DMVIPLINDP 

       430        440        450        460        470        480 
HPRVQYGCCN VLGQISTDFS PFIQRTAHDR ILPALISKLT SECTSRVQTH AAAALVNFSE 

       490        500        510        520        530        540 
FASKDILEPY LDSLLTNLLV LLQSNKLYVQ EQALTTIAFI AEAAKNKFIK YYDTLMPLLL 

       550        560        570        580        590        600 
NVLKVNNKDN SVLKGKCMEC ATLIGFAVGK EKFHEHSQEL ISILVALQNS DIDEDDALRS 

       610        620        630        640        650        660 
YLEQSWSRIC RILGDDFVPL LPIVIPPLLI TAKATQDVGL IEEEEAANFQ QYPDWDVVQV 

       670        680        690        700        710        720 
QGKHIAIHTS VLDDKVSAME LLQSYATLLR GQFAVYVKEV MEEIALPSLD FYLHDGVRAA 

       730        740        750        760        770        780 
GATLIPILLS CLLAATGTQN EELVLLWHKA SSKLIGGLMS EPMPEITQVY HNSLVNGIKV 

       790        800        810        820        830        840 
MGDNCLSEDQ LAAFTKGVSA NLTDTYERMQ DRHGDGDEYN ENIDEEEDFT DEDLLDEINK 

       850        860        870        880        890        900 
SIAAVLKTTN GHYLKNLENI WPMINTFLLD NEPILVIFAL VVIGDLIQYG GEQTASMKNA 

       910        920        930        940        950        960 
FIPKVTECLI SPDARIRQAA SYIIGVCAQY APSTYADVCI PTLDTLVQIV DFPGSKLEEN 

       970        980        990       1000       1010       1020 
RSSTENASAA IAKILYAYNS NIPNVDTYTA NWFKTLPTIT DKEAASFNYQ FLSQLIENNS 

      1030       1040       1050       1060       1070       1080 
PIVCAQSNIS AVVDSVIQAL NERSLTEREG QTVISSVKKL LGFLPSSDAM AIFNRYPADI 


MEKVHKWFA 

« Hide

References

« Hide 'large scale' references
[1]"Screening and identification of a gene, PSE-1, that affects protein secretion in Saccharomyces cerevisiae."
Chow T.Y.-K., Ash J.J., Dignard D., Thomas D.Y.
J. Cell Sci. 101:709-719(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"Functional and physical interactions between autonomously replicating sequence-binding factor 1 and the nuclear transport machinery."
Loch C.M., Mosammaparast N., Miyake T., Pemberton L.F., Li R.
Traffic 5:925-935(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ABF1.
[6]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-830, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11538 Genomic DNA. Translation: CAA77639.1.
S45357 Genomic DNA. Translation: AAA10665.1.
Z49212 Genomic DNA. Translation: CAA89141.1.
BK006946 Genomic DNA. Translation: DAA10209.1.
PIRS53978.
RefSeqNP_014039.1. NM_001182819.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3W3TX-ray2.90A1-1089[»]
3W3UX-ray2.60A1-1089[»]
3W3VX-ray3.20A1-1089[»]
3W3WX-ray2.20A1-1089[»]
3W3XX-ray2.90A1-1089[»]
3W3YX-ray2.80A1-1089[»]
3W3ZX-ray2.70A1-1089[»]
ProteinModelPortalP32337.
SMRP32337. Positions 133-549.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35488. 152 interactions.
DIPDIP-1533N.
IntActP32337. 73 interactions.
MINTMINT-390897.
STRING4932.YMR308C.

Proteomic databases

PaxDbP32337.
PeptideAtlasP32337.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR308C; YMR308C; YMR308C.
GeneID855356.
KEGGsce:YMR308C.

Organism-specific databases

CYGDYMR308c.
SGDS000004925. PSE1.

Phylogenomic databases

eggNOGNOG249123.
GeneTreeENSGT00550000074773.
HOGENOMHOG000209725.
OMANCNLPRI.
OrthoDBEOG7WX0HQ.

Enzyme and pathway databases

BioCycYEAST:G3O-32972-MONOMER.

Gene expression databases

GenevestigatorP32337.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

NextBio979118.

Entry information

Entry nameIMB3_YEAST
AccessionPrimary (citable) accession number: P32337
Secondary accession number(s): D6W0D5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references