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P25043 (PSB2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit beta type-2

EC=3.4.25.1
Alternative name(s):
Macropain subunit PUP1
Multicatalytic endopeptidase complex subunit PUP1
Proteasome component PUP1
Proteinase YSCE subunit PUP1
Gene names
Name:PUP1
Ordered Locus Names:YOR157C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length261 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.

Miscellaneous

The side chain of Thr-30 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.

Present with 11400 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase T1B family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PUP3P254513EBI-14009,EBI-13993

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 2929Removed in mature form
PRO_0000026657
Chain30 – 261232Proteasome subunit beta type-2
PRO_0000026658

Sites

Active site301Nucleophile Ref.7

Secondary structure

...................................... 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25043 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 13A8F2B75584539A

FASTA26128,268
        10         20         30         40         50         60 
MAGLSFDNYQ RNNFLAENSH TQPKATSTGT TIVGVKFNNG VVIAADTRST QGPIVADKNC 

        70         80         90        100        110        120 
AKLHRISPKI WCAGAGTAAD TEAVTQLIGS NIELHSLYTS REPRVVSALQ MLKQHLFKYQ 

       130        140        150        160        170        180 
GHIGAYLIVA GVDPTGSHLF SIHAHGSTDV GYYLSLGSGS LAAMAVLESH WKQDLTKEEA 

       190        200        210        220        230        240 
IKLASDAIQA GIWNDLGSGS NVDVCVMEIG KDAEYLRNYL TPNVREEKQK SYKFPRGTTA 

       250        260 
VLKESIVNIC DIQEEQVDIT A 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of PUP1 encoding a putative proteasome subunit in Saccharomyces cerevisiae."
Haffter P., Fox T.D.
Nucleic Acids Res. 19:5075-5075(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae chromosome XV."
Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.
Yeast 13:73-83(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S288c / FY1678.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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].
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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 30-251 OF COMPLEX WITH THE 20S PROTEASOME, PROTEOLYTIC PROCESSING, ACTIVE SITE.
[8]"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 30-261 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
[9]"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.
[10]"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 30-251 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
[11]"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 30-251 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
[12]"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 30-251 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
[13]"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 30-251 IN COMPLEX WITH THE PROTEASOME.
[14]"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
X61189 Genomic DNA. Translation: CAA43492.1.
U55020 Genomic DNA. Translation: AAC49643.1.
Z75065 Genomic DNA. Translation: CAA99363.1.
BK006948 Genomic DNA. Translation: DAA10930.1.
PIRS26996.
RefSeqNP_014800.3. NM_001183576.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20I/W30-261[»]
1G0UX-ray2.40H/V30-251[»]
1G65X-ray2.25H/V30-251[»]
1JD2X-ray3.00H/O30-251[»]
1RYPX-ray1.90I/W30-251[»]
1VSYX-ray3.00I/W30-251[»]
1Z7QX-ray3.22I/W30-251[»]
2F16X-ray2.80H/V30-251[»]
2FAKX-ray2.80H/V30-251[»]
2GPLX-ray2.81H/V30-251[»]
2ZCYX-ray2.90H/V30-261[»]
3BDMX-ray2.70H/V30-261[»]
3D29X-ray2.60H/V30-251[»]
3DY3X-ray2.81H/V30-251[»]
3DY4X-ray2.80H/V30-251[»]
3E47X-ray3.00H/V30-251[»]
3GPJX-ray2.70H/V30-251[»]
3GPTX-ray2.41H/V30-251[»]
3GPWX-ray2.50H/V30-251[»]
3HYEX-ray2.50H/V30-251[»]
3L5QX-ray3.00M/Y30-251[»]
3MG0X-ray2.68H/V30-251[»]
3MG4X-ray3.11H/V30-251[»]
3MG6X-ray2.60H/V30-251[»]
3MG7X-ray2.78H/V30-251[»]
3MG8X-ray2.59H/V30-251[»]
3NZJX-ray2.40H/V1-261[»]
3NZWX-ray2.50H/V1-261[»]
3NZXX-ray2.70H/V1-261[»]
3OEUX-ray2.60H/V30-251[»]
3OEVX-ray2.85H/V30-251[»]
3OKJX-ray2.70H/V30-251[»]
3SDIX-ray2.65H/V30-251[»]
3SDKX-ray2.70H/V30-251[»]
3SHJX-ray2.80H/V30-251[»]
3TDDX-ray2.70H/V30-251[»]
3UN4X-ray3.40H/V30-261[»]
3UN8X-ray2.70H/V30-261[»]
4B4Telectron microscopy7.4021-261[»]
4C0Velectron microscopy9.8021-261[»]
4EU2X-ray2.51I/W30-251[»]
4FZCX-ray2.80H/V30-251[»]
4FZGX-ray3.00H/V30-251[»]
4G4SX-ray2.49I30-261[»]
4GK7X-ray2.80H/V30-251[»]
4HNPX-ray2.80H/V30-251[»]
4HRCX-ray2.80H/V30-251[»]
4HRDX-ray2.80H/V30-251[»]
4INRX-ray2.70H/V30-261[»]
4INTX-ray2.90H/V30-261[»]
4INUX-ray3.10H/V30-261[»]
4J70X-ray2.80H/V30-261[»]
4JSQX-ray2.80H/V30-261[»]
4JSUX-ray2.90H/V30-261[»]
4JT0X-ray3.10H/V30-261[»]
4LQIX-ray2.70H/V30-251[»]
4NNNX-ray2.50H/V30-261[»]
4NNWX-ray2.60H/V30-261[»]
4NO1X-ray2.50H/V30-261[»]
4NO6X-ray3.00H/V30-261[»]
4NO8X-ray2.70H/V30-261[»]
4NO9X-ray2.90H/V30-261[»]
ProteinModelPortalP25043.
SMRP25043. Positions 30-251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34553. 56 interactions.
DIPDIP-2818N.
IntActP25043. 9 interactions.
MINTMINT-498378.
STRING4932.YOR157C.

Protein family/group databases

MEROPST01.011.

Proteomic databases

PaxDbP25043.
PeptideAtlasP25043.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR157C; YOR157C; YOR157C.
GeneID854328.
KEGGsce:YOR157C.

Organism-specific databases

CYGDYOR157c.
SGDS000005683. PUP1.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00510000046533.
HOGENOMHOG000182856.
KOK02739.
OMAQIWCAGA.
OrthoDBEOG7TJ3V6.

Enzyme and pathway databases

BioCycYEAST:G3O-33674-MONOMER.

Gene expression databases

GenevestigatorP25043.

Family and domain databases

InterProIPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25043.
NextBio976378.
PROP25043.

Entry information

Entry namePSB2_YEAST
AccessionPrimary (citable) accession number: P25043
Secondary accession number(s): D6W2L4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
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 chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: 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