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P32379 (PSA5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. 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

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha type-5

EC=3.4.25.1
Alternative name(s):
Macropain subunit PUP2
Multicatalytic endopeptidase complex subunit PUP2
Proteasome component PUP2
Proteinase YSCE subunit PUP2
Gene names
Name:PUP2
Synonyms:DOA5
Ordered Locus Names:YGR253C
ORF Names:G9155
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length260 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.

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

Present with 17100 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260Proteasome subunit alpha type-5
PRO_0000124129

Amino acid modifications

Modified residue551Phosphothreonine Ref.8
Modified residue561Phosphoserine Ref.8
Modified residue2511Phosphoserine Ref.8 Ref.9 Ref.10

Experimental info

Mutagenesis491G → D in DOA5-1; slight decrease in activity. Ref.2
Sequence conflict1921T → S in CAA46111. Ref.1

Secondary structure

................................................ 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32379 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: E8EDEB212BF4EC6E

FASTA26028,617
        10         20         30         40         50         60 
MFLTRSEYDR GVSTFSPEGR LFQVEYSLEA IKLGSTAIGI ATKEGVVLGV EKRATSPLLE 

        70         80         90        100        110        120 
SDSIEKIVEI DRHIGCAMSG LTADARSMIE HARTAAVTHN LYYDEDINVE SLTQSVCDLA 

       130        140        150        160        170        180 
LRFGEGASGE ERLMSRPFGV ALLIAGHDAD DGYQLFHAEP SGTFYRYNAK AIGSGSEGAQ 

       190        200        210        220        230        240 
AELLNEWHSS LTLKEAELLV LKILKQVMEE KLDENNAQLS CITKQDGFKI YDNEKTAELI 

       250        260 
KELKEKEAAE SPEEADVEMS 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of an essential yeast gene encoding a proteasomal subunit."
Georgatsou E., Georgakopoulos T., Thireos G.
FEBS Lett. 299:39-43(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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], MUTAGENESIS OF GLY-49.
[3]"Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII reveals the presence of three new open reading frames and of a tRNAThr gene."
Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.
Yeast 13:369-372(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"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.
[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]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55; SER-56 AND SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[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-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
[12]"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).
[13]"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 1-250 OF COMPLEX WITH THE 20S PROTEASOME.
[14]"Crystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor."
Groll M., Koguchi Y., Huber R., Kohno J.
J. Mol. Biol. 311:543-548(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
[15]"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 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
[16]"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 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
[17]"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 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
[18]"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 1-250 IN COMPLEX WITH THE PROTEASOME.
[19]"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
X64918 Genomic DNA. Translation: CAA46111.1.
X99228 Genomic DNA. Translation: CAA67615.1.
Z73038 Genomic DNA. Translation: CAA97282.1.
AY558511 Genomic DNA. Translation: AAS56837.1.
BK006941 Genomic DNA. Translation: DAA08344.1.
PIRS64585.
RefSeqNP_011769.1. NM_001181382.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20E/S1-260[»]
1G0UX-ray2.40D/R1-250[»]
1G65X-ray2.25D/R9-250[»]
1JD2X-ray3.00D/Y9-250[»]
1RYPX-ray1.90E/S9-250[»]
1VSYX-ray3.00E/S1-250[»]
1Z7QX-ray3.22E/S1-260[»]
2F16X-ray2.80D/R9-250[»]
2FAKX-ray2.80D/R9-250[»]
2GPLX-ray2.81D/R9-250[»]
2Z5CX-ray2.90C/F1-260[»]
2ZCYX-ray2.90D/R1-260[»]
3BDMX-ray2.70D/R1-260[»]
3D29X-ray2.60D/R9-250[»]
3DY3X-ray2.81D/R9-250[»]
3DY4X-ray2.80D/R9-250[»]
3E47X-ray3.00D/R9-250[»]
3GPJX-ray2.70D/R9-250[»]
3GPTX-ray2.41D/R9-250[»]
3GPWX-ray2.50D/R9-250[»]
3HYEX-ray2.50D/R9-250[»]
3L5QX-ray3.00J/V1-250[»]
3MG0X-ray2.68D/R9-250[»]
3MG4X-ray3.11D/R9-250[»]
3MG6X-ray2.60D/R1-250[»]
3MG7X-ray2.78D/R1-250[»]
3MG8X-ray2.59D/R1-250[»]
3NZJX-ray2.40D/R1-260[»]
3NZWX-ray2.50D/R1-260[»]
3NZXX-ray2.70D/R1-260[»]
3OEUX-ray2.60D/R1-260[»]
3OEVX-ray2.85D/R1-260[»]
3OKJX-ray2.70D/R9-250[»]
3SDIX-ray2.65D/R1-260[»]
3SDKX-ray2.70D/R1-260[»]
3SHJX-ray2.80D/R9-250[»]
3TDDX-ray2.70D/R9-250[»]
3UN4X-ray3.40D/R1-260[»]
3UN8X-ray2.70D/R1-260[»]
4B4Telectron microscopy7.40E1-260[»]
4C0Velectron microscopy9.80E1-260[»]
4EU2X-ray2.51E/S9-250[»]
4FZCX-ray2.80D/R9-250[»]
4FZGX-ray3.00D/R9-250[»]
4G4SX-ray2.49E1-260[»]
4GK7X-ray2.80D/R9-250[»]
4HNPX-ray2.80D/R9-250[»]
4HRCX-ray2.80D/R9-250[»]
4HRDX-ray2.80D/R9-250[»]
4INRX-ray2.70D/R1-260[»]
4INTX-ray2.90D/R1-260[»]
4INUX-ray3.10D/R1-260[»]
4J70X-ray2.80D/R1-260[»]
4JSQX-ray2.80D/R1-260[»]
4JSUX-ray2.90D/R1-260[»]
4JT0X-ray3.10D/R1-260[»]
4LQIX-ray2.70D/R9-250[»]
4NNNX-ray2.50D/R1-260[»]
4NNWX-ray2.60D/R1-260[»]
4NO1X-ray2.50D/R1-260[»]
4NO6X-ray3.00D/R1-260[»]
4NO8X-ray2.70D/R1-260[»]
4NO9X-ray2.90D/R1-260[»]
ProteinModelPortalP32379.
SMRP32379. Positions 9-250.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33504. 58 interactions.
DIPDIP-1193N.
IntActP32379. 9 interactions.
MINTMINT-386734.
STRING4932.YGR253C.

Proteomic databases

PaxDbP32379.
PeptideAtlasP32379.
PRIDEP32379.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR253C; YGR253C; YGR253C.
GeneID853168.
KEGGsce:YGR253C.

Organism-specific databases

CYGDYGR253c.
SGDS000003485. PUP2.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074958.
HOGENOMHOG000091085.
KOK02729.
OMAFYRYNAK.
OrthoDBEOG7SBP0C.

Enzyme and pathway databases

BioCycYEAST:G3O-30926-MONOMER.

Gene expression databases

GenevestigatorP32379.

Family and domain databases

InterProIPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32379.
NextBio973285.
PROP32379.

Entry information

Entry namePSA5_YEAST
AccessionPrimary (citable) accession number: P32379
Secondary accession number(s): D6VV33
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: 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