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P40302 (PSA6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. 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-6

EC=3.4.25.1
Alternative name(s):
Macropain subunit PRE5
Multicatalytic endopeptidase complex subunit PRE5
Proteasome component PRE5
Proteinase YSCE subunit PRE5
Gene names
Name:PRE5
Ordered Locus Names:YMR314W
ORF Names:YM9924.06
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length234 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 7210 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 – 234234Proteasome subunit alpha type-6
PRO_0000124076

Amino acid modifications

Modified residue141Phosphoserine Ref.6 Ref.8

Secondary structure

........................................... 234
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40302 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: C43CBCC1C6B9E39E

FASTA23425,604
        10         20         30         40         50         60 
MFRNNYDGDT VTFSPTGRLF QVEYALEAIK QGSVTVGLRS NTHAVLVALK RNADELSSYQ 

        70         80         90        100        110        120 
KKIIKCDEHM GLSLAGLAPD ARVLSNYLRQ QCNYSSLVFN RKLAVERAGH LLCDKAQKNT 

       130        140        150        160        170        180 
QSYGGRPYGV GLLIIGYDKS GAHLLEFQPS GNVTELYGTA IGARSQGAKT YLERTLDTFI 

       190        200        210        220        230 
KIDGNPDELI KAGVEAISQS LRDESLTVDN LSIAIVGKDT PFTIYDGEAV AKYI 

« Hide

References

« Hide 'large scale' references
[1]"PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core."
Heinemeyer W., Troendle N., Albrecht G., Wolf D.H.
Biochemistry 33:12229-12237(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 141-149 AND 220-228.
Strain: ATCC 204508 / S288c.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(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]"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.
[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]"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 SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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].
[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 COMPLEX WITH THE 20S PROTEASOME.
[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 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 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 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 COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
[16]"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) IN COMPLEX WITH THE PROTEASOME.
[17]"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
L34347 Genomic DNA. Translation: AAA53544.1.
Z54141 Genomic DNA. Translation: CAA90832.1.
AY557978 Genomic DNA. Translation: AAS56304.1.
BK006946 Genomic DNA. Translation: DAA10215.1.
PIRA55904.
RefSeqNP_014045.1. NM_001182825.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20F/T1-234[»]
1G0UX-ray2.40E/S1-234[»]
1G65X-ray2.25E/S2-234[»]
1JD2X-ray3.00E/Z2-234[»]
1RYPX-ray1.90F/T2-234[»]
1VSYX-ray3.00F/T1-234[»]
1Z7QX-ray3.22F/T1-234[»]
2F16X-ray2.80E/S2-234[»]
2FAKX-ray2.80E/S2-234[»]
2GPLX-ray2.81E/S2-234[»]
2ZCYX-ray2.90E/S1-234[»]
3BDMX-ray2.70E/S1-234[»]
3D29X-ray2.60E/S2-234[»]
3DY3X-ray2.81E/S2-234[»]
3DY4X-ray2.80E/S2-234[»]
3E47X-ray3.00E/S2-234[»]
3GPJX-ray2.70E/S2-234[»]
3GPTX-ray2.41E/S2-234[»]
3GPWX-ray2.50E/S2-234[»]
3HYEX-ray2.50E/S2-234[»]
3L5QX-ray3.00K/W1-234[»]
3MG0X-ray2.68E/S2-234[»]
3MG4X-ray3.11E/S2-234[»]
3MG6X-ray2.60E/S1-234[»]
3MG7X-ray2.78E/S1-234[»]
3MG8X-ray2.59E/S1-234[»]
3NZJX-ray2.40E/S1-234[»]
3NZWX-ray2.50E/S1-234[»]
3NZXX-ray2.70E/S1-234[»]
3OEUX-ray2.60E/S2-234[»]
3OEVX-ray2.85E/S2-234[»]
3OKJX-ray2.70E/S2-234[»]
3SDIX-ray2.65E/S2-234[»]
3SDKX-ray2.70E/S2-234[»]
3SHJX-ray2.80E/S2-234[»]
3TDDX-ray2.70E/S2-234[»]
3UN4X-ray3.40E/S1-234[»]
3UN8X-ray2.70E/S1-234[»]
4B4Telectron microscopy7.40F1-234[»]
4C0Velectron microscopy9.80F1-234[»]
4EU2X-ray2.51F/T2-234[»]
4FZCX-ray2.80E/S2-234[»]
4FZGX-ray3.00E/S2-234[»]
4G4SX-ray2.49F1-234[»]
4GK7X-ray2.80E/S2-234[»]
4HNPX-ray2.80E/S2-234[»]
4HRCX-ray2.80E/S2-234[»]
4HRDX-ray2.80E/S2-234[»]
4INRX-ray2.70E/S1-234[»]
4INTX-ray2.90E/S1-234[»]
4INUX-ray3.10E/S1-234[»]
4J70X-ray2.80E/S1-234[»]
4JSQX-ray2.80E/S1-234[»]
4JSUX-ray2.90E/S1-234[»]
4JT0X-ray3.10E/S1-234[»]
4LQIX-ray2.70E/S2-234[»]
4NNNX-ray2.50E/S1-234[»]
4NNWX-ray2.60E/S1-234[»]
4NO1X-ray2.50E/S1-234[»]
4NO6X-ray3.00E/S1-234[»]
4NO8X-ray2.70E/S1-234[»]
4NO9X-ray2.90E/S1-234[»]
ProteinModelPortalP40302.
SMRP40302. Positions 2-234.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35494. 85 interactions.
DIPDIP-1528N.
IntActP40302. 33 interactions.
MINTMINT-400436.
STRING4932.YMR314W.

Protein family/group databases

MEROPST01.976.

2D gel databases

UCD-2DPAGEP40302.

Proteomic databases

PaxDbP40302.
PeptideAtlasP40302.
PRIDEP40302.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR314W; YMR314W; YMR314W.
GeneID855362.
KEGGsce:YMR314W.

Organism-specific databases

CYGDYMR314w.
SGDS000004931. PRE5.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074855.
HOGENOMHOG000091080.
KOK02725.
OMAFMKQQCL.
OrthoDBEOG7SBP0C.

Enzyme and pathway databases

BioCycYEAST:G3O-32978-MONOMER.

Gene expression databases

GenevestigatorP40302.

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

EvolutionaryTraceP40302.
NextBio979136.
PROP40302.

Entry information

Entry namePSA6_YEAST
AccessionPrimary (citable) accession number: P40302
Secondary accession number(s): D6W0E1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 150 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 XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: 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