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Protein

Importin subunit beta-3

Gene

PSE1

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

Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for classical and arginine/glycine-rich nuclear localization signals (cNLS and rg-NLS) in cargo substrates (PubMed:15367670). Its predominant cargo substrate seems to be ribosomal proteins and ribosome biogenesis trans- and cis-acting factors (PubMed:9182759, PubMed:9321403, PubMed:15367670). Required for nuclear transport of YAP1, NOP1 and SOF1 (PubMed:11274141, PubMed:15367670). Mediates the nuclear import of histones H3 and H4 (PubMed:11694505). Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:11423015). At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo (PubMed:9321403). The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11423015).5 Publications1 Publication
Plays a role in protein secretion.1 Publication

GO - Molecular functioni

  1. nuclear localization sequence binding Source: SGD
  2. protein transporter activity Source: SGD

GO - Biological processi

  1. mRNA export from nucleus Source: SGD
  2. protein import into nucleus Source: SGD
  3. regulation of mitosis Source: SGD
  4. regulation of protein desumoylation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32972-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit beta-3Curated
Alternative name(s):
Karyopherin subunit beta-3Curated
Karyopherin-1211 Publication
Protein secretion enhancer 11 Publication
Gene namesi
Name:PSE11 Publication
Synonyms:KAP1211 Publication
Ordered Locus Names:YMR308CImported
ORF Names:YM9952.10C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYMR308c.
SGDiS000004925. PSE1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10891088Importin subunit beta-3PRO_0000120774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei830 – 8301Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP32337.
PaxDbiP32337.
PeptideAtlasiP32337.

Expressioni

Gene expression databases

GenevestigatoriP32337.

Interactioni

Subunit structurei

Interacts with Ran (GSP1); interacts specifically with the GTP-bound form of Ran (GTP-Ran), protecting it from GTP hydrolysis and nucleotide exchange (PubMed:9321403). Interacts with RPL25; this interaction is dissociated by binding to Ran-GTP (PubMed:9321403). Interacts with YAP1; this interaction is dissociated by binding to Ran-GTP (PubMed:11274141). Interacts with NOP1; via its rg-NLS (PubMed:15367670). Interacts with SOF1; via its cNLS (PubMed:15367670). Interacts with histones H3 and H4; via their NLS (PubMed:11694505). Interacts with ABF1 (PubMed:15522095).4 Publications

Protein-protein interaction databases

BioGridi35488. 154 interactions.
DIPiDIP-1533N.
IntActiP32337. 73 interactions.
MINTiMINT-390897.
STRINGi4932.YMR308C.

Structurei

Secondary structure

1
1089
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1813Combined sources
Helixi25 – 3713Combined sources
Turni41 – 433Combined sources
Helixi44 – 5714Combined sources
Helixi61 – 7717Combined sources
Helixi91 – 933Combined sources
Helixi96 – 11116Combined sources
Helixi116 – 12712Combined sources
Helixi138 – 14912Combined sources
Helixi153 – 16513Combined sources
Helixi168 – 1725Combined sources
Helixi175 – 18511Combined sources
Helixi191 – 20717Combined sources
Helixi210 – 2156Combined sources
Helixi217 – 2193Combined sources
Helixi220 – 2267Combined sources
Helixi228 – 2325Combined sources
Helixi236 – 25217Combined sources
Helixi254 – 2607Combined sources
Helixi261 – 27313Combined sources
Helixi279 – 29517Combined sources
Helixi297 – 3015Combined sources
Helixi304 – 31815Combined sources
Helixi329 – 3324Combined sources
Helixi343 – 35917Combined sources
Helixi361 – 37616Combined sources
Helixi381 – 39414Combined sources
Turni395 – 3984Combined sources
Helixi399 – 4024Combined sources
Helixi406 – 4138Combined sources
Helixi414 – 4185Combined sources
Helixi422 – 43817Combined sources
Turni439 – 4413Combined sources
Helixi442 – 45817Combined sources
Helixi465 – 48016Combined sources
Helixi484 – 4874Combined sources
Helixi488 – 4903Combined sources
Helixi491 – 50212Combined sources
Helixi507 – 52418Combined sources
Helixi525 – 5317Combined sources
Helixi532 – 54413Combined sources
Helixi551 – 56818Combined sources
Helixi570 – 5734Combined sources
Turni574 – 5763Combined sources
Helixi577 – 58812Combined sources
Helixi597 – 61317Combined sources
Helixi614 – 6207Combined sources
Helixi621 – 63212Combined sources
Beta strandi638 – 6414Combined sources
Beta strandi646 – 6483Combined sources
Helixi649 – 6513Combined sources
Beta strandi655 – 66814Combined sources
Helixi669 – 68921Combined sources
Helixi690 – 6934Combined sources
Helixi694 – 70310Combined sources
Helixi705 – 7095Combined sources
Helixi715 – 73420Combined sources
Helixi742 – 75716Combined sources
Turni758 – 7603Combined sources
Helixi764 – 78118Combined sources
Helixi788 – 80922Combined sources
Helixi829 – 84921Combined sources
Turni850 – 8534Combined sources
Helixi854 – 8574Combined sources
Helixi858 – 8603Combined sources
Helixi861 – 8688Combined sources
Helixi873 – 88715Combined sources
Helixi891 – 8933Combined sources
Helixi895 – 90915Combined sources
Helixi914 – 93017Combined sources
Turni933 – 9353Combined sources
Helixi936 – 94914Combined sources
Helixi958 – 9603Combined sources
Helixi961 – 97717Combined sources
Turni978 – 9803Combined sources
Helixi987 – 9937Combined sources
Helixi1002 – 101312Combined sources
Helixi1029 – 104113Combined sources
Helixi1053 – 106210Combined sources
Helixi1066 – 10716Combined sources
Helixi1072 – 10754Combined sources
Helixi1078 – 10858Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP32337.
SMRiP32337. Positions 133-549.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati6 – 3934HEAT 11 PublicationAdd
BLAST
Repeati44 – 7835HEAT 21 PublicationAdd
BLAST
Repeati96 – 12934HEAT 31 PublicationAdd
BLAST
Repeati138 – 16528HEAT 41 PublicationAdd
BLAST
Repeati175 – 20733HEAT 51 PublicationAdd
BLAST
Repeati216 – 25237HEAT 61 PublicationAdd
BLAST
Repeati260 – 29536HEAT 71 PublicationAdd
BLAST
Repeati304 – 35956HEAT 81 PublicationAdd
BLAST
Repeati361 – 39535HEAT 91 PublicationAdd
BLAST
Repeati399 – 43941HEAT 101 PublicationAdd
BLAST
Repeati441 – 48141HEAT 111 PublicationAdd
BLAST
Repeati484 – 52441HEAT 121 PublicationAdd
BLAST
Repeati526 – 56843HEAT 131 PublicationAdd
BLAST
Repeati571 – 61343HEAT 141 PublicationAdd
BLAST
Repeati615 – 68975HEAT 151 PublicationAdd
BLAST
Repeati692 – 73544HEAT 161 PublicationAdd
BLAST
Repeati742 – 78140HEAT 171 PublicationAdd
BLAST
Repeati788 – 84962HEAT 181 PublicationAdd
BLAST
Repeati852 – 89039HEAT 191 PublicationAdd
BLAST
Repeati898 – 93033HEAT 201 PublicationAdd
BLAST
Repeati938 – 97841HEAT 211 PublicationAdd
BLAST
Repeati986 – 101732HEAT 221 PublicationAdd
BLAST
Repeati1028 – 106336HEAT 231 PublicationAdd
BLAST
Repeati1066 – 108924HEAT 241 PublicationAdd
BLAST

Sequence similaritiesi

Contains 24 HEAT repeats.1 Publication

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG249123.
GeneTreeiENSGT00550000074773.
HOGENOMiHOG000209725.
InParanoidiP32337.
OMAiCDMEIAN.
OrthoDBiEOG7WX0HQ.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSALPEEVNR TLLQIVQAFA SPDNQIRSVA EKALSEEWIT ENNIEYLLTF
60 70 80 90 100
LAEQAAFSQD TTVAALSAVL FRKLALKAPP SSKLMIMSKN ITHIRKEVLA
110 120 130 140 150
QIRSSLLKGF LSERADSIRH KLSDAIAECV QDDLPAWPEL LQALIESLKS
160 170 180 190 200
GNPNFRESSF RILTTVPYLI TAVDINSILP IFQSGFTDAS DNVKIAAVTA
210 220 230 240 250
FVGYFKQLPK SEWSKLGILL PSLLNSLPRF LDDGKDDALA SVFESLIELV
260 270 280 290 300
ELAPKLFKDM FDQIIQFTDM VIKNKDLEPP ARTTALELLT VFSENAPQMC
310 320 330 340 350
KSNQNYGQTL VMVTLIMMTE VSIDDDDAAE WIESDDTDDE EEVTYDHARQ
360 370 380 390 400
ALDRVALKLG GEYLAAPLFQ YLQQMITSTE WRERFAAMMA LSSAAEGCAD
410 420 430 440 450
VLIGEIPKIL DMVIPLINDP HPRVQYGCCN VLGQISTDFS PFIQRTAHDR
460 470 480 490 500
ILPALISKLT SECTSRVQTH AAAALVNFSE FASKDILEPY LDSLLTNLLV
510 520 530 540 550
LLQSNKLYVQ EQALTTIAFI AEAAKNKFIK YYDTLMPLLL NVLKVNNKDN
560 570 580 590 600
SVLKGKCMEC ATLIGFAVGK EKFHEHSQEL ISILVALQNS DIDEDDALRS
610 620 630 640 650
YLEQSWSRIC RILGDDFVPL LPIVIPPLLI TAKATQDVGL IEEEEAANFQ
660 670 680 690 700
QYPDWDVVQV QGKHIAIHTS VLDDKVSAME LLQSYATLLR GQFAVYVKEV
710 720 730 740 750
MEEIALPSLD FYLHDGVRAA GATLIPILLS CLLAATGTQN EELVLLWHKA
760 770 780 790 800
SSKLIGGLMS EPMPEITQVY HNSLVNGIKV MGDNCLSEDQ LAAFTKGVSA
810 820 830 840 850
NLTDTYERMQ DRHGDGDEYN ENIDEEEDFT DEDLLDEINK SIAAVLKTTN
860 870 880 890 900
GHYLKNLENI WPMINTFLLD NEPILVIFAL VVIGDLIQYG GEQTASMKNA
910 920 930 940 950
FIPKVTECLI SPDARIRQAA SYIIGVCAQY APSTYADVCI PTLDTLVQIV
960 970 980 990 1000
DFPGSKLEEN RSSTENASAA IAKILYAYNS NIPNVDTYTA NWFKTLPTIT
1010 1020 1030 1040 1050
DKEAASFNYQ FLSQLIENNS PIVCAQSNIS AVVDSVIQAL NERSLTEREG
1060 1070 1080
QTVISSVKKL LGFLPSSDAM AIFNRYPADI MEKVHKWFA
Length:1,089
Mass (Da):121,031
Last modified:October 1, 1996 - v2
Checksum:i9C5F7FB5B8824C37
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651A → S in CAA77639 (PubMed:1522152).Curated
Sequence conflicti65 – 651A → S in AAA10665 (PubMed:1522152).Curated
Sequence conflicti1077 – 10771P → A in CAA77639 (PubMed:1522152).Curated
Sequence conflicti1077 – 10771P → A in AAA10665 (PubMed:1522152).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11538 Genomic DNA. Translation: CAA77639.1.
S45357 Genomic DNA. Translation: AAA10665.1.
Z49212 Genomic DNA. Translation: CAA89141.1.
BK006946 Genomic DNA. Translation: DAA10209.1.
PIRiS53978.
RefSeqiNP_014039.1. NM_001182819.1.

Genome annotation databases

EnsemblFungiiYMR308C; YMR308C; YMR308C.
GeneIDi855356.
KEGGisce:YMR308C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11538 Genomic DNA. Translation: CAA77639.1.
S45357 Genomic DNA. Translation: AAA10665.1.
Z49212 Genomic DNA. Translation: CAA89141.1.
BK006946 Genomic DNA. Translation: DAA10209.1.
PIRiS53978.
RefSeqiNP_014039.1. NM_001182819.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP32337.
SMRiP32337. Positions 133-549.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35488. 154 interactions.
DIPiDIP-1533N.
IntActiP32337. 73 interactions.
MINTiMINT-390897.
STRINGi4932.YMR308C.

Proteomic databases

MaxQBiP32337.
PaxDbiP32337.
PeptideAtlasiP32337.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR308C; YMR308C; YMR308C.
GeneIDi855356.
KEGGisce:YMR308C.

Organism-specific databases

CYGDiYMR308c.
SGDiS000004925. PSE1.

Phylogenomic databases

eggNOGiNOG249123.
GeneTreeiENSGT00550000074773.
HOGENOMiHOG000209725.
InParanoidiP32337.
OMAiCDMEIAN.
OrthoDBiEOG7WX0HQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-32972-MONOMER.

Miscellaneous databases

NextBioi979118.

Gene expression databases

GenevestigatoriP32337.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], FUNCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "A distinct nuclear import pathway used by ribosomal proteins."
    Rout M.P., Blobel G., Aitchison J.D.
    Cell 89:715-725(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Yrb4p, a yeast ran-GTP-binding protein involved in import of ribosomal protein L25 into the nucleus."
    Schlenstedt G., Smirnova E., Deane R., Solsbacher J., Kutay U., Goerlich D., Ponstingl H., Bischoff F.R.
    EMBO J. 16:6237-6249(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GSP1 AND RPL25.
  6. "Importin/karyopherin protein family members required for mRNA export from the nucleus."
    Seedorf M., Silver P.A.
    Proc. Natl. Acad. Sci. U.S.A. 94:8590-8595(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Importin-beta-like nuclear transport receptors."
    Stroem A.C., Weis K.
    Genome Biol. 2:REVIEWS3008.1-REVIEWS3008.9(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  8. "Nuclear import of the yeast AP-1-like transcription factor Yap1p is mediated by transport receptor Pse1p, and this import step is not affected by oxidative stress."
    Isoyama T., Murayama A., Nomoto A., Kuge S.
    J. Biol. Chem. 276:21863-21869(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YAP1.
  9. "Pathways mediating the nuclear import of histones H3 and H4 in yeast."
    Mosammaparast N., Guo Y., Shabanowitz J., Hunt D.F., Pemberton L.F.
    J. Biol. Chem. 277:862-868(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HISTONES H3 AND H4.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "Characterization of karyopherin cargoes reveals unique mechanisms of Kap121p-mediated nuclear import."
    Leslie D.M., Zhang W., Timney B.L., Chait B.T., Rout M.P., Wozniak R.W., Aitchison J.D.
    Mol. Cell. Biol. 24:8487-8503(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NOP1 AND SOF1.
  12. "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.
  13. "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].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. "Structural basis for cell-cycle-dependent nuclear import mediated by the karyopherin Kap121p."
    Kobayashi J., Matsuura Y.
    J. Mol. Biol. 425:1852-1868(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-1089 IN COMPLEXES WITH STE11; PHO4; NUP53 AND GSP1, REPEAT STRUCTURE.

Entry informationi

Entry nameiIMB3_YEAST
AccessioniPrimary (citable) accession number: P32337
Secondary accession number(s): D6W0D5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 15500 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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: 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.