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P23724

- PSB6_YEAST

UniProt

P23724 - PSB6_YEAST

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Protein
Proteasome subunit beta type-6
Gene
PRE7, PRS3, PTS1, YBL041W, YBL0407
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteasomal ubiquitin-independent protein catabolic process Source: SGD
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciYEAST:G3O-28942-MONOMER.
ReactomeiREACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189025. ER-Phagosome pathway.
REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_83036. Orc1 removal from chromatin.

Protein family/group databases

MEROPSiT01.A12.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-6 (EC:3.4.25.1)
Alternative name(s):
Multicatalytic endopeptidase complex subunit C5
Proteasome component C5
Gene namesi
Name:PRE7
Synonyms:PRS3, PTS1
Ordered Locus Names:YBL041W
ORF Names:YBL0407
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBL041w.
SGDiS000000137. PRE7.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: SGD
  2. nucleus Source: SGD
  3. proteasome core complex, beta-subunit complex Source: SGD
  4. proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1919
PRO_0000331489Add
BLAST
Chaini20 – 241222Proteasome subunit beta type-6
PRO_0000148042Add
BLAST

Proteomic databases

MaxQBiP23724.
PaxDbiP23724.
PeptideAtlasiP23724.

2D gel databases

UCD-2DPAGEP23724.

Expressioni

Gene expression databases

GenevestigatoriP23724.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.

Protein-protein interaction databases

BioGridi32656. 41 interactions.
DIPiDIP-2821N.
IntActiP23724. 16 interactions.
MINTiMINT-592611.
STRINGi4932.YBL041W.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 356
Beta strandi40 – 456
Beta strandi48 – 503
Beta strandi53 – 575
Beta strandi62 – 643
Beta strandi70 – 767
Helixi77 – 9721
Turni98 – 1003
Helixi105 – 11713
Turni118 – 1214
Beta strandi126 – 1338
Beta strandi139 – 1446
Beta strandi146 – 1483
Beta strandi150 – 15910
Helixi162 – 17211
Turni181 – 1855
Beta strandi186 – 1883
Helixi196 – 21318
Beta strandi214 – 2174
Beta strandi219 – 2279
Beta strandi230 – 2378

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20M/a20-240[»]
1G0UX-ray2.40L/Z1-241[»]
1G65X-ray2.25L/Z20-241[»]
1JD2X-ray3.00L/S20-241[»]
1RYPX-ray1.901/M20-241[»]
1VSYX-ray3.001/M20-241[»]
1Z7QX-ray3.22M/a20-241[»]
2F16X-ray2.80L/Z20-241[»]
2FAKX-ray2.80L/Z20-241[»]
2GPLX-ray2.81L/Z20-241[»]
2ZCYX-ray2.90L/Z1-241[»]
3BDMX-ray2.70L/Z1-241[»]
3D29X-ray2.60L/Z20-241[»]
3DY3X-ray2.81L/Z20-241[»]
3DY4X-ray2.80L/Z20-241[»]
3E47X-ray3.00L/Z20-241[»]
3GPJX-ray2.70L/Z20-241[»]
3GPTX-ray2.41L/Z20-241[»]
3GPWX-ray2.50L/Z20-241[»]
3HYEX-ray2.50L/Z20-241[»]
3L5QX-ray3.003/Q20-241[»]
3MG0X-ray2.68L/Z20-241[»]
3MG4X-ray3.11L/Z20-241[»]
3MG6X-ray2.60L/Z1-241[»]
3MG7X-ray2.78L/Z1-241[»]
3MG8X-ray2.59L/Z1-241[»]
3NZJX-ray2.40L/Z1-241[»]
3NZWX-ray2.50L/Z1-241[»]
3NZXX-ray2.70L/Z1-241[»]
3OEUX-ray2.60L/Z20-241[»]
3OEVX-ray2.85L/Z20-241[»]
3OKJX-ray2.70L/Z20-241[»]
3SDIX-ray2.65L/Z20-241[»]
3SDKX-ray2.70L/Z20-241[»]
3SHJX-ray2.80L/Z20-241[»]
3TDDX-ray2.70L/Z20-241[»]
3UN4X-ray3.40L/Z20-241[»]
3UN8X-ray2.70L/Z20-241[»]
4CR2electron microscopy7.7061-241[»]
4CR3electron microscopy9.3061-241[»]
4CR4electron microscopy8.8061-241[»]
4EU2X-ray2.511/M20-241[»]
4FZCX-ray2.80L/Z20-241[»]
4FZGX-ray3.00L/Z20-241[»]
4G4SX-ray2.49M20-241[»]
4GK7X-ray2.80L/Z20-241[»]
4HNPX-ray2.80L/Z20-241[»]
4HRCX-ray2.80L/Z20-241[»]
4HRDX-ray2.80L/Z20-241[»]
4INRX-ray2.70L/Z20-241[»]
4INTX-ray2.90L/Z20-241[»]
4INUX-ray3.10L/Z20-241[»]
4J70X-ray2.80L/Z20-241[»]
4JSQX-ray2.80L/Z20-241[»]
4JSUX-ray2.90L/Z20-241[»]
4JT0X-ray3.10L/Z20-241[»]
4LQIX-ray2.70L/Z20-241[»]
4NNNX-ray2.50L/Z20-241[»]
4NNWX-ray2.60L/Z20-241[»]
4NO1X-ray2.50L/Z20-241[»]
4NO6X-ray3.00L/Z20-241[»]
4NO8X-ray2.70L/Z20-241[»]
4NO9X-ray2.90L/Z20-241[»]
4QBYX-ray3.00L/Z20-241[»]
ProteinModelPortaliP23724.
SMRiP23724. Positions 20-241.

Miscellaneous databases

EvolutionaryTraceiP23724.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000075035.
HOGENOMiHOG000091081.
KOiK02732.
OMAiQCRAGGA.
OrthoDBiEOG7VMPGM.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P23724-1 [UniParc]FASTAAdd to Basket

« Hide

MATIASEYSS EASNTPIEHQ FNPYGDNGGT ILGIAGEDFA VLAGDTRNIT    50
DYSINSRYEP KVFDCGDNIV MSANGFAADG DALVKRFKNS VKWYHFDHND 100
KKLSINSAAR NIQHLLYGKR FFPYYVHTII AGLDEDGKGA VYSFDPVGSY 150
EREQCRAGGA AASLIMPFLD NQVNFKNQYE PGTNGKVKKP LKYLSVEEVI 200
KLVRDSFTSA TERHIQVGDG LEILIVTKDG VRKEFYELKR D 241
Length:241
Mass (Da):26,871
Last modified:November 1, 1991 - v1
Checksum:i770A4DF1DF0A0F0E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34777 Genomic DNA. Translation: AAA68908.1.
D00845 Genomic DNA. Translation: BAA00725.1.
X78214 Genomic DNA. Translation: CAA55053.1.
Z35802 Genomic DNA. Translation: CAA84861.1.
AY558462 Genomic DNA. Translation: AAS56788.1.
BK006936 Genomic DNA. Translation: DAA07077.1.
PIRiS42436.
RefSeqiNP_009512.1. NM_001178281.1.

Genome annotation databases

EnsemblFungiiYBL041W; YBL041W; YBL041W.
GeneIDi852239.
KEGGisce:YBL041W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34777 Genomic DNA. Translation: AAA68908.1 .
D00845 Genomic DNA. Translation: BAA00725.1 .
X78214 Genomic DNA. Translation: CAA55053.1 .
Z35802 Genomic DNA. Translation: CAA84861.1 .
AY558462 Genomic DNA. Translation: AAS56788.1 .
BK006936 Genomic DNA. Translation: DAA07077.1 .
PIRi S42436.
RefSeqi NP_009512.1. NM_001178281.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FNT X-ray 3.20 M/a 20-240 [» ]
1G0U X-ray 2.40 L/Z 1-241 [» ]
1G65 X-ray 2.25 L/Z 20-241 [» ]
1JD2 X-ray 3.00 L/S 20-241 [» ]
1RYP X-ray 1.90 1/M 20-241 [» ]
1VSY X-ray 3.00 1/M 20-241 [» ]
1Z7Q X-ray 3.22 M/a 20-241 [» ]
2F16 X-ray 2.80 L/Z 20-241 [» ]
2FAK X-ray 2.80 L/Z 20-241 [» ]
2GPL X-ray 2.81 L/Z 20-241 [» ]
2ZCY X-ray 2.90 L/Z 1-241 [» ]
3BDM X-ray 2.70 L/Z 1-241 [» ]
3D29 X-ray 2.60 L/Z 20-241 [» ]
3DY3 X-ray 2.81 L/Z 20-241 [» ]
3DY4 X-ray 2.80 L/Z 20-241 [» ]
3E47 X-ray 3.00 L/Z 20-241 [» ]
3GPJ X-ray 2.70 L/Z 20-241 [» ]
3GPT X-ray 2.41 L/Z 20-241 [» ]
3GPW X-ray 2.50 L/Z 20-241 [» ]
3HYE X-ray 2.50 L/Z 20-241 [» ]
3L5Q X-ray 3.00 3/Q 20-241 [» ]
3MG0 X-ray 2.68 L/Z 20-241 [» ]
3MG4 X-ray 3.11 L/Z 20-241 [» ]
3MG6 X-ray 2.60 L/Z 1-241 [» ]
3MG7 X-ray 2.78 L/Z 1-241 [» ]
3MG8 X-ray 2.59 L/Z 1-241 [» ]
3NZJ X-ray 2.40 L/Z 1-241 [» ]
3NZW X-ray 2.50 L/Z 1-241 [» ]
3NZX X-ray 2.70 L/Z 1-241 [» ]
3OEU X-ray 2.60 L/Z 20-241 [» ]
3OEV X-ray 2.85 L/Z 20-241 [» ]
3OKJ X-ray 2.70 L/Z 20-241 [» ]
3SDI X-ray 2.65 L/Z 20-241 [» ]
3SDK X-ray 2.70 L/Z 20-241 [» ]
3SHJ X-ray 2.80 L/Z 20-241 [» ]
3TDD X-ray 2.70 L/Z 20-241 [» ]
3UN4 X-ray 3.40 L/Z 20-241 [» ]
3UN8 X-ray 2.70 L/Z 20-241 [» ]
4CR2 electron microscopy 7.70 6 1-241 [» ]
4CR3 electron microscopy 9.30 6 1-241 [» ]
4CR4 electron microscopy 8.80 6 1-241 [» ]
4EU2 X-ray 2.51 1/M 20-241 [» ]
4FZC X-ray 2.80 L/Z 20-241 [» ]
4FZG X-ray 3.00 L/Z 20-241 [» ]
4G4S X-ray 2.49 M 20-241 [» ]
4GK7 X-ray 2.80 L/Z 20-241 [» ]
4HNP X-ray 2.80 L/Z 20-241 [» ]
4HRC X-ray 2.80 L/Z 20-241 [» ]
4HRD X-ray 2.80 L/Z 20-241 [» ]
4INR X-ray 2.70 L/Z 20-241 [» ]
4INT X-ray 2.90 L/Z 20-241 [» ]
4INU X-ray 3.10 L/Z 20-241 [» ]
4J70 X-ray 2.80 L/Z 20-241 [» ]
4JSQ X-ray 2.80 L/Z 20-241 [» ]
4JSU X-ray 2.90 L/Z 20-241 [» ]
4JT0 X-ray 3.10 L/Z 20-241 [» ]
4LQI X-ray 2.70 L/Z 20-241 [» ]
4NNN X-ray 2.50 L/Z 20-241 [» ]
4NNW X-ray 2.60 L/Z 20-241 [» ]
4NO1 X-ray 2.50 L/Z 20-241 [» ]
4NO6 X-ray 3.00 L/Z 20-241 [» ]
4NO8 X-ray 2.70 L/Z 20-241 [» ]
4NO9 X-ray 2.90 L/Z 20-241 [» ]
4QBY X-ray 3.00 L/Z 20-241 [» ]
ProteinModelPortali P23724.
SMRi P23724. Positions 20-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32656. 41 interactions.
DIPi DIP-2821N.
IntActi P23724. 16 interactions.
MINTi MINT-592611.
STRINGi 4932.YBL041W.

Chemistry

BindingDBi P23724.
ChEMBLi CHEMBL4904.

Protein family/group databases

MEROPSi T01.A12.

2D gel databases

UCD-2DPAGE P23724.

Proteomic databases

MaxQBi P23724.
PaxDbi P23724.
PeptideAtlasi P23724.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBL041W ; YBL041W ; YBL041W .
GeneIDi 852239.
KEGGi sce:YBL041W.

Organism-specific databases

CYGDi YBL041w.
SGDi S000000137. PRE7.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000075035.
HOGENOMi HOG000091081.
KOi K02732.
OMAi QCRAGGA.
OrthoDBi EOG7VMPGM.

Enzyme and pathway databases

BioCyci YEAST:G3O-28942-MONOMER.
Reactomei REACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189025. ER-Phagosome pathway.
REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_83036. Orc1 removal from chromatin.

Miscellaneous databases

EvolutionaryTracei P23724.
NextBioi 970787.
PROi P23724.

Gene expression databases

Genevestigatori P23724.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway."
    Semenza J.C., Hardwick K.G., Dean N., Pelham H.R.B.
    Cell 61:1349-1357(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A yeast homologue of a proteasome subunit."
    Semenza J.C., Pelham H.R.
    DNA Seq. 1:219-219(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "PRS3 encoding an essential subunit of yeast proteasomes homologous to mammalian proteasome subunit C5."
    Lee D.H., Tanaka K., Tamura T., Chung C.H., Ichihara A.
    Biochem. Biophys. Res. Commun. 182:452-460(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The sequence of a 22.4 kb DNA fragment from the left arm of yeast chromosome II reveals homologues to bacterial proline synthetase and murine alpha-adaptin, as well as a new permease and a DNA-binding protein."
    de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J., Goffeau A.
    Yeast 10:1489-1496(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  8. "Structure of 20S proteasome from yeast at 2.4-A resolution."
    Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D., Huber R.
    Nature 386:463-471(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 20-241 OF COMPLEX WITH THE 20S PROTEASOME, PROTEOLYTIC PROCESSING.
  9. "Structural basis for the activation of 20S proteasomes by 11S regulators."
    Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P.
    Nature 408:115-120(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 20-241 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
  11. "TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome."
    Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.
    Chem. Biol. 13:607-614(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 20-241 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
  12. "Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding."
    Groll M., Huber R., Potts B.C.M.
    J. Am. Chem. Soc. 128:5136-5141(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-241 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
  13. "Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome."
    Groll M., Berkers C.R., Ploegh H.L., Ovaa H.
    Structure 14:451-456(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-241 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
  14. "Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening."
    Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.
    Mol. Cell 37:728-735(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 20-241 IN COMPLEX WITH THE PROTEASOME.
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSB6_YEAST
AccessioniPrimary (citable) accession number: P23724
Secondary accession number(s): D6VPV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: September 3, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

Similar proteinsi