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P23724 (PSB6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit beta type-6
EC=3.4.25.1
Alternative name(s):
Multicatalytic endopeptidase complex subunit C5
Proteasome component C5
Gene names
Name:PRE7
Synonyms:PRS3, PTS1
Ordered Locus Names:YBL041W
ORF Names:YBL0407
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

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.

Subcellular location

Cytoplasm. Nucleus.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1919
PRO_0000331489
Chain20 – 241222Proteasome subunit beta type-6
PRO_0000148042

Amino acid modifications

Modified residue531Phosphoserine Ref.9
Modified residue2091Phosphoserine Ref.8
Modified residue2111Phosphothreonine Ref.8

Secondary structure

1 ...................................... 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23724 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 770A4DF1DF0A0F0E

FASTA24126,871
        10         20         30         40         50         60 
MATIASEYSS EASNTPIEHQ FNPYGDNGGT ILGIAGEDFA VLAGDTRNIT DYSINSRYEP 

        70         80         90        100        110        120 
KVFDCGDNIV MSANGFAADG DALVKRFKNS VKWYHFDHND KKLSINSAAR NIQHLLYGKR 

       130        140        150        160        170        180 
FFPYYVHTII AGLDEDGKGA VYSFDPVGSY EREQCRAGGA AASLIMPFLD NQVNFKNQYE 

       190        200        210        220        230        240 
PGTNGKVKKP LKYLSVEEVI KLVRDSFTSA TERHIQVGDG LEILIVTKDG VRKEFYELKR 


D

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[8]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND THR-211, MASS SPECTROMETRY.
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, MASS SPECTROMETRY.
[10]"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.
[11]"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.
[12]"A gated channel into the proteasome core particle."
Groll M., Bajorek M., Koehler A., Moroder L., Rubin D.M., Huber R., Glickman M.H., Finley D.
Nat. Struct. Biol. 7:1062-1067(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
[13]"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.
[14]"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.
[15]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
PIRS42436.
RefSeqNP_009512.1. NM_001178281.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20M/a20-241[»]
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[»]
4B4Telectron microscopy7.4061-241[»]
4FZCX-ray2.80L/Z20-241[»]
4FZGX-ray3.00L/Z20-241[»]
4G4SX-ray2.49M20-241[»]
4GK7X-ray2.80L/Z20-241[»]
4INRX-ray2.70L/Z20-241[»]
4INTX-ray2.90L/Z20-241[»]
4INUX-ray3.10L/Z20-241[»]
ProteinModelPortalP23724.
SMRP23724. Positions 20-241.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2821N.
IntActP23724. 16 interactions.
MINTMINT-592611.
STRING4932.YBL041W.

Protein family/group databases

MEROPST01.986.

2D gel databases

UCD-2DPAGEP23724.

Proteomic databases

PaxDbP23724.
PeptideAtlasP23724.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL041W; YBL041W; YBL041W.
GeneID852239.
KEGGsce:YBL041W.

Organism-specific databases

CYGDYBL041w.
SGDS000000137. PRE7.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000075035.
HOGENOMHOG000091081.
KOK02732.
OMAYDPIGHC.
OrthoDBEOG4PG98X.

Gene expression databases

GenevestigatorP23724.
GermOnlineYBL041W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PROSITEPS00854. PROTEASOME_B_1. 1 hit.
PS51476. PROTEASOME_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP23724.
ChEMBLCHEMBL4904.
EvolutionaryTraceP23724.
NextBio970787.

Entry information

Entry namePSB6_YEAST
AccessionPrimary (citable) accession number: P23724
Secondary accession number(s): D6VPV7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 3, 2013
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome II

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

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents