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Protein

Proteasome subunit alpha type-6

Gene

PRE5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteasomal ubiquitin-independent protein catabolic process Source: SGD
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciYEAST:G3O-32978-MONOMER.
ReactomeiREACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189025. ER-Phagosome pathway.
REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_230653. SCF-beta-TrCP mediated degradation of Emi1.
REACT_245870. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_245912. CDK-mediated phosphorylation and removal of Cdc6.
REACT_268441. Ubiquitin-dependent degradation of Cyclin D1.
REACT_83036. Orc1 removal from chromatin.

Protein family/group databases

MEROPSiT01.976.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PRE5
Ordered Locus Names:YMR314W
ORF Names:YM9924.06
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYMR314w.
SGDiS000004931. PRE5.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nuclear outer membrane-endoplasmic reticulum membrane network Source: SGD
  3. nucleus Source: SGD
  4. proteasome core complex, alpha-subunit complex Source: SGD
  5. proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 234234Proteasome subunit alpha type-6PRO_0000124076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40302.
PaxDbiP40302.
PeptideAtlasiP40302.
PRIDEiP40302.

2D gel databases

UCD-2DPAGEP40302.

Expressioni

Gene expression databases

GenevestigatoriP40302.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi35494. 88 interactions.
DIPiDIP-1528N.
IntActiP40302. 33 interactions.
MINTiMINT-400436.
STRINGi4932.YMR314W.

Structurei

Secondary structure

1
234
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Beta strandi15 – 173Combined sources
Helixi20 – 3011Combined sources
Beta strandi35 – 395Combined sources
Beta strandi41 – 499Combined sources
Beta strandi52 – 543Combined sources
Beta strandi63 – 675Combined sources
Beta strandi70 – 767Combined sources
Helixi78 – 9922Combined sources
Helixi105 – 12117Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi130 – 1389Combined sources
Beta strandi141 – 1477Combined sources
Turni149 – 1513Combined sources
Beta strandi153 – 16210Combined sources
Turni163 – 1653Combined sources
Helixi166 – 17914Combined sources
Helixi186 – 19712Combined sources
Helixi198 – 2003Combined sources
Beta strandi202 – 2043Combined sources
Turni208 – 2103Combined sources
Beta strandi211 – 2177Combined sources
Beta strandi220 – 2267Combined sources
Helixi227 – 2337Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
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[»]
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[»]
3WXRX-ray3.15F/T1-234[»]
4CR2electron microscopy7.70F1-234[»]
4CR3electron microscopy9.30F1-234[»]
4CR4electron microscopy8.80F1-234[»]
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[»]
4LTCX-ray2.50E/S1-234[»]
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[»]
4Q1SX-ray2.60E/S1-234[»]
4QBYX-ray3.00E/S1-234[»]
4QLQX-ray2.40E/S1-234[»]
4QLSX-ray2.80E/S1-234[»]
4QLTX-ray2.80E/S1-234[»]
4QLUX-ray2.80E/S1-234[»]
4QLVX-ray2.90E/S1-234[»]
4R02X-ray2.50E/S1-234[»]
4R17X-ray2.10E/S1-234[»]
4R18X-ray2.40E/S1-234[»]
4RURX-ray2.50E/S1-234[»]
4V7OX-ray3.00F/K/T/W1-234[»]
ProteinModelPortaliP40302.
SMRiP40302. Positions 2-234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40302.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074855.
HOGENOMiHOG000091080.
InParanoidiP40302.
KOiK02725.
OMAiFMKQQCL.
OrthoDBiEOG7SBP0C.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40302-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFRNNYDGDT VTFSPTGRLF QVEYALEAIK QGSVTVGLRS NTHAVLVALK
60 70 80 90 100
RNADELSSYQ KKIIKCDEHM GLSLAGLAPD ARVLSNYLRQ QCNYSSLVFN
110 120 130 140 150
RKLAVERAGH LLCDKAQKNT QSYGGRPYGV GLLIIGYDKS GAHLLEFQPS
160 170 180 190 200
GNVTELYGTA IGARSQGAKT YLERTLDTFI KIDGNPDELI KAGVEAISQS
210 220 230
LRDESLTVDN LSIAIVGKDT PFTIYDGEAV AKYI
Length:234
Mass (Da):25,604
Last modified:February 1, 1995 - v1
Checksum:iC43CBCC1C6B9E39E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34347 Genomic DNA. Translation: AAA53544.1.
Z54141 Genomic DNA. Translation: CAA90832.1.
AY557978 Genomic DNA. Translation: AAS56304.1.
BK006946 Genomic DNA. Translation: DAA10215.1.
PIRiA55904.
RefSeqiNP_014045.1. NM_001182825.1.

Genome annotation databases

EnsemblFungiiYMR314W; YMR314W; YMR314W.
GeneIDi855362.
KEGGisce:YMR314W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34347 Genomic DNA. Translation: AAA53544.1.
Z54141 Genomic DNA. Translation: CAA90832.1.
AY557978 Genomic DNA. Translation: AAS56304.1.
BK006946 Genomic DNA. Translation: DAA10215.1.
PIRiA55904.
RefSeqiNP_014045.1. NM_001182825.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
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[»]
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[»]
3WXRX-ray3.15F/T1-234[»]
4CR2electron microscopy7.70F1-234[»]
4CR3electron microscopy9.30F1-234[»]
4CR4electron microscopy8.80F1-234[»]
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[»]
4LTCX-ray2.50E/S1-234[»]
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[»]
4Q1SX-ray2.60E/S1-234[»]
4QBYX-ray3.00E/S1-234[»]
4QLQX-ray2.40E/S1-234[»]
4QLSX-ray2.80E/S1-234[»]
4QLTX-ray2.80E/S1-234[»]
4QLUX-ray2.80E/S1-234[»]
4QLVX-ray2.90E/S1-234[»]
4R02X-ray2.50E/S1-234[»]
4R17X-ray2.10E/S1-234[»]
4R18X-ray2.40E/S1-234[»]
4RURX-ray2.50E/S1-234[»]
4V7OX-ray3.00F/K/T/W1-234[»]
ProteinModelPortaliP40302.
SMRiP40302. Positions 2-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35494. 88 interactions.
DIPiDIP-1528N.
IntActiP40302. 33 interactions.
MINTiMINT-400436.
STRINGi4932.YMR314W.

Protein family/group databases

MEROPSiT01.976.

2D gel databases

UCD-2DPAGEP40302.

Proteomic databases

MaxQBiP40302.
PaxDbiP40302.
PeptideAtlasiP40302.
PRIDEiP40302.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR314W; YMR314W; YMR314W.
GeneIDi855362.
KEGGisce:YMR314W.

Organism-specific databases

CYGDiYMR314w.
SGDiS000004931. PRE5.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074855.
HOGENOMiHOG000091080.
InParanoidiP40302.
KOiK02725.
OMAiFMKQQCL.
OrthoDBiEOG7SBP0C.

Enzyme and pathway databases

BioCyciYEAST:G3O-32978-MONOMER.
ReactomeiREACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189025. ER-Phagosome pathway.
REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_230653. SCF-beta-TrCP mediated degradation of Emi1.
REACT_245870. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_245912. CDK-mediated phosphorylation and removal of Cdc6.
REACT_268441. Ubiquitin-dependent degradation of Cyclin D1.
REACT_83036. Orc1 removal from chromatin.

Miscellaneous databases

EvolutionaryTraceiP40302.
NextBioi979136.
PROiP40302.

Gene expression databases

GenevestigatoriP40302.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. 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. 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. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSA6_YEAST
AccessioniPrimary (citable) accession number: P40302
Secondary accession number(s): D6W0E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 4, 2015
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7210 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.