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P30656 (PSB5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 151. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit beta type-5

EC=3.4.25.1
Alternative name(s):
Macropain subunit PRE2
Multicatalytic endopeptidase complex subunit PRE2
Proteasome component PRE2
Proteinase YSCE subunit PRE2
Gene names
Name:PRE2
Synonyms:DOA3, PRG1
Ordered Locus Names:YPR103W
ORF Names:P8283.10
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length287 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. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib.

This subunit is necessary for chymotryptic activity and degradation of ubiquitinated proteins.

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.

Miscellaneous

The side chain of Thr-76 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.

Present with 8530 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence caution

The sequence CAA82203.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BLM10P435833EBI-14001,EBI-22761

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 7575Removed in mature form
PRO_0000026611
Chain76 – 287212Proteasome subunit beta type-5
PRO_0000026612

Sites

Active site761Nucleophile Ref.8
Binding site1241Bortezomib; via amide nitrogen

Experimental info

Mutagenesis1261D → N in DOA3-1; decrease in activity. Ref.3
Sequence conflict282 – 2876FNNVIG → STTLLAK in AAA34906. Ref.1

Secondary structure

...................................... 287
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30656 [UniParc].

Last modified February 1, 1995. Version 3.
Checksum: D0EBAC611F7A4F37

FASTA28731,637
        10         20         30         40         50         60 
MQAIADSFSV PNRLVKELQY DNEQNLESDF VTGASQFQRL APSLTVPPIA SPQQFLRAHT 

        70         80         90        100        110        120 
DDSRNPDCKI KIAHGTTTLA FRFQGGIIVA VDSRATAGNW VASQTVKKVI EINPFLLGTM 

       130        140        150        160        170        180 
AGGAADCQFW ETWLGSQCRL HELREKERIS VAAASKILSN LVYQYKGAGL SMGTMICGYT 

       190        200        210        220        230        240 
RKEGPTIYYV DSDGTRLKGD IFCVGSGQTF AYGVLDSNYK WDLSVEDALY LGKRSILAAA 

       250        260        270        280 
HRDAYSGGSV NLYHVTEDGW IYHGNHDVGE LFWKVKEEEG SFNNVIG 

« Hide

References

« Hide 'large scale' references
[1]"A homolog of the proteasome-related RING10 gene is essential for yeast cell growth."
Friedman H., Goebel M., Snyder M.
Gene 122:203-206(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins."
Heinemeyer W., Gruhler A., Moehrle V., Mahe Y., Wolf D.H.
J. Biol. Chem. 268:5115-5120(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 5288C.
[3]"Biogenesis, structure and function of the yeast 20S proteasome."
Chen P., Hochstrasser M.
EMBO J. 14:2620-2630(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 76-90, MUTAGENESIS OF ASP-126.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Suppression of yeast RNA polymerase III mutations by FHL1, a gene coding for a fork head protein involved in rRNA processing."
Hermann-Ledenmat S., Werner M., Sentenac A., Thuriaux P.
Mol. Cell. Biol. 14:2905-2913(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 176-287.
Strain: ATCC 28383 / FL100 / VTT C-80102.
[7]"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].
[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 76-287 OF COMPLEX WITH THE 20S PROTEASOME, PROTEOLYTIC PROCESSING, ACTIVE SITE.
[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 76-287 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
[10]"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 76-287 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 76-287 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 76-287 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 76-287 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 76-287 IN COMPLEX WITH THE PROTEASOME.
[15]"Near-atomic resolution structural model of the yeast 26S proteasome."
Beck F., Unverdorben P., Bohn S., Schweitzer A., Pfeifer G., Sakata E., Nickell S., Plitzko J.M., Villa E., Baumeister W., Forster F.
Proc. Natl. Acad. Sci. U.S.A. 109:14870-14875(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96667 Genomic DNA. Translation: AAA34906.1.
X68662 Genomic DNA. Translation: CAA48628.1.
U32445 Genomic DNA. Translation: AAB68073.1.
Z28348 Genomic DNA. Translation: CAA82203.1. Different initiation.
BK006949 Genomic DNA. Translation: DAA11517.1.
PIRA45411.
RefSeqNP_015428.1. NM_001184200.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20L/Z76-287[»]
1G0UX-ray2.40K/Y76-287[»]
1G65X-ray2.25K/Y76-287[»]
1JD2X-ray3.00K/R76-287[»]
1RYPX-ray1.90L/Z76-287[»]
1VSYX-ray3.00L/Z76-287[»]
1Z7QX-ray3.22L/Z76-287[»]
2F16X-ray2.80K/Y76-287[»]
2FAKX-ray2.80K/Y76-287[»]
2GPLX-ray2.81K/Y76-287[»]
2ZCYX-ray2.90K/Y76-287[»]
3BDMX-ray2.70K/Y76-287[»]
3D29X-ray2.60K/Y76-287[»]
3DY3X-ray2.81K/Y76-287[»]
3DY4X-ray2.80K/Y76-287[»]
3E47X-ray3.00K/Y76-287[»]
3GPJX-ray2.70K/Y76-287[»]
3GPTX-ray2.41K/Y76-287[»]
3GPWX-ray2.50K/Y76-287[»]
3HYEX-ray2.50K/Y76-287[»]
3L5QX-ray3.002/P76-287[»]
3MG0X-ray2.68K/Y76-287[»]
3MG4X-ray3.11K/Y76-287[»]
3MG6X-ray2.60K/Y76-287[»]
3MG7X-ray2.78K/Y76-287[»]
3MG8X-ray2.59K/Y76-287[»]
3NZJX-ray2.40K/Y1-287[»]
3NZWX-ray2.50K/Y1-287[»]
3NZXX-ray2.70K/Y1-287[»]
3OEUX-ray2.60K/Y76-287[»]
3OEVX-ray2.85K/Y76-287[»]
3OKJX-ray2.70K/Y76-287[»]
3SDIX-ray2.65K/Y76-287[»]
3SDKX-ray2.70K/Y76-287[»]
3SHJX-ray2.80K/Y76-287[»]
3TDDX-ray2.70K/Y76-287[»]
3UN4X-ray3.40K/Y76-287[»]
3UN8X-ray2.70K/Y76-287[»]
4CR2electron microscopy7.7051-287[»]
4CR3electron microscopy9.3051-287[»]
4CR4electron microscopy8.8051-287[»]
4EU2X-ray2.51L/Z76-287[»]
4FZCX-ray2.80K/Y76-287[»]
4FZGX-ray3.00K/Y76-287[»]
4G4SX-ray2.49L76-287[»]
4GK7X-ray2.80K/Y76-287[»]
4HNPX-ray2.80K/Y76-287[»]
4HRCX-ray2.80K/Y76-287[»]
4HRDX-ray2.80K/Y76-287[»]
4INRX-ray2.70K/Y76-287[»]
4INTX-ray2.90K/Y76-287[»]
4INUX-ray3.10K/Y76-287[»]
4J70X-ray2.80K/Y76-287[»]
4JSQX-ray2.80K/Y76-287[»]
4JSUX-ray2.90K/Y76-287[»]
4JT0X-ray3.10K/Y76-287[»]
4LQIX-ray2.70K/Y76-287[»]
4NNNX-ray2.50K/Y76-287[»]
4NNWX-ray2.60K/Y76-287[»]
4NO1X-ray2.50K/Y76-287[»]
4NO6X-ray3.00K/Y76-287[»]
4NO8X-ray2.70K/Y76-287[»]
4NO9X-ray2.90K/Y76-287[»]
ProteinModelPortalP30656.
SMRP30656. Positions 49-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36269. 119 interactions.
DIPDIP-2806N.
IntActP30656. 20 interactions.
MINTMINT-489734.
STRING4932.YPR103W.

Chemistry

BindingDBP30656.
ChEMBLCHEMBL4659.

Protein family/group databases

MEROPST01.012.

Proteomic databases

MaxQBP30656.
PaxDbP30656.
PeptideAtlasP30656.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR103W; YPR103W; YPR103W.
GeneID856218.
KEGGsce:YPR103W.

Organism-specific databases

CYGDYPR103w.
SGDS000006307. PRE2.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00510000046395.
HOGENOMHOG000091082.
KOK02737.
OMATMCAGVT.
OrthoDBEOG70W3R5.

Enzyme and pathway databases

BioCycYEAST:G3O-34243-MONOMER.

Gene expression databases

GenevestigatorP30656.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30656.
NextBio981441.
PROP30656.

Entry information

Entry namePSB5_YEAST
AccessionPrimary (citable) accession number: P30656
Secondary accession number(s): D6W4A1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references