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P25451 (PSB3_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-3

EC=3.4.25.1
Alternative name(s):
Macropain subunit PUP3
Multicatalytic endopeptidase complex subunit PUP3
Proteasome component PUP3
Gene names
Name:PUP3
Ordered Locus Names:YER094C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
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 subunit may participate in the trypsin-like activity of the enzyme complex.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PUP1P250433EBI-13993,EBI-14009

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205Proteasome subunit beta type-3
PRO_0000148070

Amino acid modifications

Modified residue311Phosphoserine Ref.4

Secondary structure

........................................ 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25451 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 5AA92D746454BCB7

FASTA20522,605
        10         20         30         40         50         60 
MSDPSSINGG IVVAMTGKDC VAIACDLRLG SQSLGVSNKF EKIFHYGHVF LGITGLATDV 

        70         80         90        100        110        120 
TTLNEMFRYK TNLYKLKEER AIEPETFTQL VSSSLYERRF GPYFVGPVVA GINSKSGKPF 

       130        140        150        160        170        180 
IAGFDLIGCI DEAKDFIVSG TASDQLFGMC ESLYEPNLEP EDLFETISQA LLNAADRDAL 

       190        200 
SGWGAVVYII KKDEVVKRYL KMRQD 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and transcriptional regulation of the yeast recombinational repair gene RAD51."
Basile G.M., Aker M., Mortimer R.K.
Mol. Cell. Biol. 12:3235-3246(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"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 COMPLEX WITH THE 20S PROTEASOME.
[7]"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 COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
[8]"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.
[9]"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 COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
[10]"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 COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
[11]"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 COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
[12]"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 2-205 IN COMPLEX WITH THE PROTEASOME.
[13]"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
M88470 Genomic DNA. Translation: AAA34946.1.
U18839 Genomic DNA. Translation: AAB64649.1.
BK006939 Genomic DNA. Translation: DAA07756.1.
PIRS29251.
RefSeqNP_011020.3. NM_001178985.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20J/X1-205[»]
1G0UX-ray2.40I/W1-205[»]
1G65X-ray2.25I/W2-205[»]
1JD2X-ray3.00I/P2-205[»]
1RYPX-ray1.90J/X2-205[»]
1VSYX-ray3.00J/X2-205[»]
1Z7QX-ray3.22J/X1-205[»]
2F16X-ray2.80I/W2-205[»]
2FAKX-ray2.80I/W2-205[»]
2GPLX-ray2.81I/W2-205[»]
2ZCYX-ray2.90I/W1-205[»]
3BDMX-ray2.70I/W1-205[»]
3D29X-ray2.60I/W2-205[»]
3DY3X-ray2.81I/W2-205[»]
3DY4X-ray2.80I/W2-205[»]
3E47X-ray3.00I/W2-205[»]
3GPJX-ray2.70I/W2-205[»]
3GPTX-ray2.41I/W2-205[»]
3GPWX-ray2.50I/W2-205[»]
3HYEX-ray2.50I/W2-205[»]
3L5QX-ray3.00N/Z2-205[»]
3MG0X-ray2.68I/W2-205[»]
3MG4X-ray3.11I/W2-205[»]
3MG6X-ray2.60I/W1-205[»]
3MG7X-ray2.78I/W1-205[»]
3MG8X-ray2.59I/W1-205[»]
3NZJX-ray2.40I/W1-205[»]
3NZWX-ray2.50I/W1-205[»]
3NZXX-ray2.70I/W1-205[»]
3OEUX-ray2.60I/W2-205[»]
3OEVX-ray2.85I/W2-205[»]
3OKJX-ray2.70I/W2-205[»]
3SDIX-ray2.65I/W2-205[»]
3SDKX-ray2.70I/W2-205[»]
3SHJX-ray2.80I/W2-205[»]
3TDDX-ray2.70I/W2-205[»]
3UN4X-ray3.40I/W1-205[»]
3UN8X-ray2.70I/W1-205[»]
4B4Telectron microscopy7.4031-205[»]
4C0Velectron microscopy9.8031-205[»]
4EU2X-ray2.51J/X2-205[»]
4FZCX-ray2.80I/W2-205[»]
4FZGX-ray3.00I/W2-205[»]
4G4SX-ray2.49J1-205[»]
4GK7X-ray2.80I/W2-205[»]
4HNPX-ray2.80I/W2-205[»]
4HRCX-ray2.80I/W2-205[»]
4HRDX-ray2.80I/W2-205[»]
4INRX-ray2.70I/W1-205[»]
4INTX-ray2.90I/W1-205[»]
4INUX-ray3.10I/W1-205[»]
4J70X-ray2.80I/W1-205[»]
4JSQX-ray2.80I/W1-205[»]
4JSUX-ray2.90I/W1-205[»]
4JT0X-ray3.10I/W1-205[»]
4LQIX-ray2.70I/W2-205[»]
4NNNX-ray2.50I/W1-205[»]
4NNWX-ray2.60I/W1-205[»]
4NO1X-ray2.50I/W1-205[»]
4NO6X-ray3.00I/W1-205[»]
4NO8X-ray2.70I/W1-205[»]
4NO9X-ray2.90I/W1-205[»]
ProteinModelPortalP25451.
SMRP25451. Positions 2-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36840. 33 interactions.
DIPDIP-2039N.
IntActP25451. 12 interactions.
MINTMINT-498393.
STRING4932.YER094C.

Proteomic databases

PaxDbP25451.
PeptideAtlasP25451.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER094C; YER094C; YER094C.
GeneID856830.
KEGGsce:YER094C.

Organism-specific databases

CYGDYER094c.
SGDS000000896. PUP3.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074820.
HOGENOMHOG000090523.
KOK02735.
OMAMVSNLLY.
OrthoDBEOG7SJDGM.

Enzyme and pathway databases

BioCycYEAST:G3O-30261-MONOMER.

Gene expression databases

GenevestigatorP25451.

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_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25451.
NextBio983127.
PROP25451.

Entry information

Entry namePSB3_YEAST
AccessionPrimary (citable) accession number: P25451
Secondary accession number(s): D3DM02
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 V

Yeast (Saccharomyces cerevisiae) chromosome V: 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