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P23639

- PSA2_YEAST

UniProt

P23639 - PSA2_YEAST

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Protein

Proteasome subunit alpha type-2

Gene

PRE8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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-32677-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.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-2 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit Y7
Multicatalytic endopeptidase complex subunit Y7
Proteasome component Y7
Proteinase YSCE subunit 7
Gene namesi
Name:PRE8
Synonyms:PRS4
Ordered Locus Names:YML092C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYML092c.
SGDiS000004557. PRE8.

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 – 250250Proteasome subunit alpha type-2PRO_0000124090Add
BLAST

Proteomic databases

MaxQBiP23639.
PaxDbiP23639.
PeptideAtlasiP23639.

Expressioni

Gene expression databases

GenevestigatoriP23639.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
PRE9P236384EBI-13959,EBI-13967
SCL1P212436EBI-13959,EBI-13975

Protein-protein interaction databases

BioGridi35051. 55 interactions.
DIPiDIP-2822N.
IntActiP23639. 21 interactions.
MINTiMINT-475016.
STRINGi4932.YML092C.

Structurei

Secondary structure

1
250
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Turni14 – 163Combined sources
Helixi19 – 2911Combined sources
Beta strandi34 – 396Combined sources
Beta strandi42 – 487Combined sources
Beta strandi54 – 563Combined sources
Helixi58 – 603Combined sources
Beta strandi63 – 686Combined sources
Beta strandi71 – 777Combined sources
Helixi79 – 9517Combined sources
Helixi98 – 1014Combined sources
Helixi107 – 12014Combined sources
Turni121 – 1233Combined sources
Beta strandi132 – 1409Combined sources
Turni141 – 1433Combined sources
Beta strandi144 – 1507Combined sources
Beta strandi156 – 16510Combined sources
Helixi168 – 17811Combined sources
Helixi185 – 19915Combined sources
Turni206 – 2083Combined sources
Beta strandi209 – 2146Combined sources
Helixi219 – 2213Combined sources
Beta strandi223 – 2264Combined sources
Beta strandi234 – 2374Combined sources
Helixi240 – 2478Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20B/P1-250[»]
1G0UX-ray2.40A/O1-250[»]
1G65X-ray2.25A/O1-250[»]
1JD2X-ray3.00A/V1-250[»]
1RYPX-ray1.90B/P1-250[»]
1VSYX-ray3.00B/P20-250[»]
1Z7QX-ray3.22B/P1-250[»]
2F16X-ray2.80A/O1-250[»]
2FAKX-ray2.80A/O1-250[»]
2GPLX-ray2.81A/O1-250[»]
2ZCYX-ray2.90A/O1-250[»]
3BDMX-ray2.70A/O1-250[»]
3D29X-ray2.60A/O1-250[»]
3DY3X-ray2.81A/O1-250[»]
3DY4X-ray2.80A/O1-250[»]
3E47X-ray3.00A/O1-250[»]
3GPJX-ray2.70A/O1-250[»]
3GPTX-ray2.41A/O1-250[»]
3GPWX-ray2.50A/O1-250[»]
3HYEX-ray2.50A/O1-250[»]
3L5QX-ray3.00G/S20-250[»]
3MG0X-ray2.68A/O1-250[»]
3MG4X-ray3.11A/O1-250[»]
3MG6X-ray2.60A/O1-250[»]
3MG7X-ray2.78A/O1-250[»]
3MG8X-ray2.59A/O1-250[»]
3NZJX-ray2.40A/O1-250[»]
3NZWX-ray2.50A/O1-250[»]
3NZXX-ray2.70A/O1-250[»]
3OEUX-ray2.60A/O1-250[»]
3OEVX-ray2.85A/O1-250[»]
3OKJX-ray2.70A/O1-250[»]
3SDIX-ray2.65A/O1-250[»]
3SDKX-ray2.70A/O1-250[»]
3SHJX-ray2.80A/O1-250[»]
3TDDX-ray2.70A/O1-250[»]
3UN4X-ray3.40A/O1-250[»]
3UN8X-ray2.70A/O1-250[»]
4CR2electron microscopy7.70B1-250[»]
4CR3electron microscopy9.30B1-250[»]
4CR4electron microscopy8.80B1-250[»]
4EU2X-ray2.51B/P1-250[»]
4FZCX-ray2.80A/O1-250[»]
4FZGX-ray3.00A/O1-250[»]
4G4SX-ray2.49B1-250[»]
4GK7X-ray2.80A/O1-250[»]
4HNPX-ray2.80A/O1-250[»]
4HRCX-ray2.80A/O2-250[»]
4HRDX-ray2.80A/O1-250[»]
4INRX-ray2.70A/O1-250[»]
4INTX-ray2.90A/O1-250[»]
4INUX-ray3.10A/O1-250[»]
4J70X-ray2.80A/O1-250[»]
4JSQX-ray2.80A/O1-250[»]
4JSUX-ray2.90A/O1-250[»]
4JT0X-ray3.10A/O1-250[»]
4LQIX-ray2.70A/O1-250[»]
4LTCX-ray2.50A/O1-250[»]
4NNNX-ray2.50A/O1-250[»]
4NNWX-ray2.60A/O1-250[»]
4NO1X-ray2.50A/O1-250[»]
4NO6X-ray3.00A/O1-250[»]
4NO8X-ray2.70A/O1-250[»]
4NO9X-ray2.90A/O1-250[»]
4Q1SX-ray2.60A/O1-250[»]
4QBYX-ray3.00A/O1-250[»]
4QLQX-ray2.40A/O1-250[»]
4QLSX-ray2.80A/O1-250[»]
4QLTX-ray2.80A/O1-250[»]
4QLUX-ray2.80A/O1-250[»]
4QLVX-ray2.90A/O1-250[»]
4R02X-ray2.50A/O1-250[»]
ProteinModelPortaliP23639.
SMRiP23639. Positions 1-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23639.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074870.
HOGENOMiHOG000091085.
InParanoidiP23639.
KOiK02726.
OMAiWKATALG.
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.

P23639-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTDRYSFSLT TFSPSGKLGQ IDYALTAVKQ GVTSLGIKAT NGVVIATEKK
60 70 80 90 100
SSSPLAMSET LSKVSLLTPD IGAVYSGMGP DYRVLVDKSR KVAHTSYKRI
110 120 130 140 150
YGEYPPTKLL VSEVAKIMQE ATQSGGVRPF GVSLLIAGHD EFNGFSLYQV
160 170 180 190 200
DPSGSYFPWK ATAIGKGSVA AKTFLEKRWN DELELEDAIH IALLTLKESV
210 220 230 240 250
EGEFNGDTIE LAIIGDENPD LLGYTGIPTD KGPRFRKLTS QEINDRLEAL
Length:250
Mass (Da):27,162
Last modified:November 1, 1991 - v1
Checksum:i12D7DFB1AA10E9FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56731 Genomic DNA. Translation: CAA40055.1.
Z46660 Genomic DNA. Translation: CAA86646.1.
AY557762 Genomic DNA. Translation: AAS56088.1.
BK006946 Genomic DNA. Translation: DAA09807.1.
PIRiS12938. SNBYY7.
RefSeqiNP_013618.1. NM_001182451.1.

Genome annotation databases

EnsemblFungiiYML092C; YML092C; YML092C.
GeneIDi854882.
KEGGisce:YML092C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56731 Genomic DNA. Translation: CAA40055.1 .
Z46660 Genomic DNA. Translation: CAA86646.1 .
AY557762 Genomic DNA. Translation: AAS56088.1 .
BK006946 Genomic DNA. Translation: DAA09807.1 .
PIRi S12938. SNBYY7.
RefSeqi NP_013618.1. NM_001182451.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FNT X-ray 3.20 B/P 1-250 [» ]
1G0U X-ray 2.40 A/O 1-250 [» ]
1G65 X-ray 2.25 A/O 1-250 [» ]
1JD2 X-ray 3.00 A/V 1-250 [» ]
1RYP X-ray 1.90 B/P 1-250 [» ]
1VSY X-ray 3.00 B/P 20-250 [» ]
1Z7Q X-ray 3.22 B/P 1-250 [» ]
2F16 X-ray 2.80 A/O 1-250 [» ]
2FAK X-ray 2.80 A/O 1-250 [» ]
2GPL X-ray 2.81 A/O 1-250 [» ]
2ZCY X-ray 2.90 A/O 1-250 [» ]
3BDM X-ray 2.70 A/O 1-250 [» ]
3D29 X-ray 2.60 A/O 1-250 [» ]
3DY3 X-ray 2.81 A/O 1-250 [» ]
3DY4 X-ray 2.80 A/O 1-250 [» ]
3E47 X-ray 3.00 A/O 1-250 [» ]
3GPJ X-ray 2.70 A/O 1-250 [» ]
3GPT X-ray 2.41 A/O 1-250 [» ]
3GPW X-ray 2.50 A/O 1-250 [» ]
3HYE X-ray 2.50 A/O 1-250 [» ]
3L5Q X-ray 3.00 G/S 20-250 [» ]
3MG0 X-ray 2.68 A/O 1-250 [» ]
3MG4 X-ray 3.11 A/O 1-250 [» ]
3MG6 X-ray 2.60 A/O 1-250 [» ]
3MG7 X-ray 2.78 A/O 1-250 [» ]
3MG8 X-ray 2.59 A/O 1-250 [» ]
3NZJ X-ray 2.40 A/O 1-250 [» ]
3NZW X-ray 2.50 A/O 1-250 [» ]
3NZX X-ray 2.70 A/O 1-250 [» ]
3OEU X-ray 2.60 A/O 1-250 [» ]
3OEV X-ray 2.85 A/O 1-250 [» ]
3OKJ X-ray 2.70 A/O 1-250 [» ]
3SDI X-ray 2.65 A/O 1-250 [» ]
3SDK X-ray 2.70 A/O 1-250 [» ]
3SHJ X-ray 2.80 A/O 1-250 [» ]
3TDD X-ray 2.70 A/O 1-250 [» ]
3UN4 X-ray 3.40 A/O 1-250 [» ]
3UN8 X-ray 2.70 A/O 1-250 [» ]
4CR2 electron microscopy 7.70 B 1-250 [» ]
4CR3 electron microscopy 9.30 B 1-250 [» ]
4CR4 electron microscopy 8.80 B 1-250 [» ]
4EU2 X-ray 2.51 B/P 1-250 [» ]
4FZC X-ray 2.80 A/O 1-250 [» ]
4FZG X-ray 3.00 A/O 1-250 [» ]
4G4S X-ray 2.49 B 1-250 [» ]
4GK7 X-ray 2.80 A/O 1-250 [» ]
4HNP X-ray 2.80 A/O 1-250 [» ]
4HRC X-ray 2.80 A/O 2-250 [» ]
4HRD X-ray 2.80 A/O 1-250 [» ]
4INR X-ray 2.70 A/O 1-250 [» ]
4INT X-ray 2.90 A/O 1-250 [» ]
4INU X-ray 3.10 A/O 1-250 [» ]
4J70 X-ray 2.80 A/O 1-250 [» ]
4JSQ X-ray 2.80 A/O 1-250 [» ]
4JSU X-ray 2.90 A/O 1-250 [» ]
4JT0 X-ray 3.10 A/O 1-250 [» ]
4LQI X-ray 2.70 A/O 1-250 [» ]
4LTC X-ray 2.50 A/O 1-250 [» ]
4NNN X-ray 2.50 A/O 1-250 [» ]
4NNW X-ray 2.60 A/O 1-250 [» ]
4NO1 X-ray 2.50 A/O 1-250 [» ]
4NO6 X-ray 3.00 A/O 1-250 [» ]
4NO8 X-ray 2.70 A/O 1-250 [» ]
4NO9 X-ray 2.90 A/O 1-250 [» ]
4Q1S X-ray 2.60 A/O 1-250 [» ]
4QBY X-ray 3.00 A/O 1-250 [» ]
4QLQ X-ray 2.40 A/O 1-250 [» ]
4QLS X-ray 2.80 A/O 1-250 [» ]
4QLT X-ray 2.80 A/O 1-250 [» ]
4QLU X-ray 2.80 A/O 1-250 [» ]
4QLV X-ray 2.90 A/O 1-250 [» ]
4R02 X-ray 2.50 A/O 1-250 [» ]
ProteinModelPortali P23639.
SMRi P23639. Positions 1-250.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35051. 55 interactions.
DIPi DIP-2822N.
IntActi P23639. 21 interactions.
MINTi MINT-475016.
STRINGi 4932.YML092C.

Proteomic databases

MaxQBi P23639.
PaxDbi P23639.
PeptideAtlasi P23639.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YML092C ; YML092C ; YML092C .
GeneIDi 854882.
KEGGi sce:YML092C.

Organism-specific databases

CYGDi YML092c.
SGDi S000004557. PRE8.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074870.
HOGENOMi HOG000091085.
InParanoidi P23639.
KOi K02726.
OMAi WKATALG.
OrthoDBi EOG7SBP0C.

Enzyme and pathway databases

BioCyci YEAST:G3O-32677-MONOMER.
Reactomei REACT_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

EvolutionaryTracei P23639.
NextBioi 977831.
PROi P23639.

Gene expression databases

Genevestigatori P23639.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional analysis of three subunits of yeast proteasome."
    Emori Y., Tsukahara T., Kawasaki H., Ishiura S., Sugita H., Suzuki K.
    Mol. Cell. Biol. 11:344-353(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 26786 / X2180-1A.
  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. "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].
  7. "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].
  8. "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.
  9. "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.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
  11. "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.
  12. "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.
  13. "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.
  14. "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 20-250 IN COMPLEX WITH THE PROTEASOME.
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSA2_YEAST
AccessioniPrimary (citable) accession number: P23639
Secondary accession number(s): D6W0J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 26, 2014
This is version 160 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 7060 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