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P23638

- PSA3_YEAST

UniProt

P23638 - PSA3_YEAST

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Protein

Proteasome subunit alpha type-3

Gene

PRE9

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 core complex assembly Source: SGD
  3. 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-30841-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

MEROPSiT01.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-3 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit Y13
Multicatalytic endopeptidase complex subunit Y13
Proteasome component Y13
Proteinase YSCE subunit 13
Gene namesi
Name:PRE9
Synonyms:PRS5
Ordered Locus Names:YGR135W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR135w.
SGDiS000003367. PRE9.

Subcellular locationi

GO - Cellular componenti

  1. nuclear outer membrane-endoplasmic reticulum membrane network Source: SGD
  2. nucleus Source: SGD
  3. proteasome core complex, alpha-subunit complex Source: SGD
  4. 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 – 258258Proteasome subunit alpha type-3PRO_0000124116Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki199 – 199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP23638.
PaxDbiP23638.
PeptideAtlasiP23638.

Expressioni

Gene expression databases

GenevestigatoriP23638.

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
PRE8P236394EBI-13967,EBI-13959

Protein-protein interaction databases

BioGridi33383. 328 interactions.
DIPiDIP-2823N.
IntActiP23638. 17 interactions.
MINTiMINT-484272.
STRINGi4932.YGR135W.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Turni15 – 173Combined sources
Helixi20 – 2910Combined sources
Beta strandi35 – 406Combined sources
Beta strandi43 – 497Combined sources
Beta strandi55 – 573Combined sources
Beta strandi59 – 613Combined sources
Beta strandi64 – 7916Combined sources
Helixi81 – 10222Combined sources
Helixi108 – 12417Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi133 – 1419Combined sources
Turni142 – 1443Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi157 – 16610Combined sources
Helixi169 – 17911Combined sources
Helixi186 – 20015Combined sources
Beta strandi202 – 2054Combined sources
Helixi208 – 2103Combined sources
Beta strandi211 – 2177Combined sources
Beta strandi220 – 2245Combined sources
Beta strandi226 – 2294Combined sources
Helixi232 – 24110Combined sources
Turni242 – 2443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20C/Q1-245[»]
1G0UX-ray2.40B/P1-245[»]
1G65X-ray2.25B/P2-245[»]
1JD2X-ray3.00B/W2-245[»]
1RYPX-ray1.90C/Q2-245[»]
1VSYX-ray3.00C/Q14-245[»]
1Z7QX-ray3.22C/Q1-258[»]
2F16X-ray2.80B/P2-245[»]
2FAKX-ray2.80B/P2-245[»]
2GPLX-ray2.81B/P2-245[»]
2ZCYX-ray2.90B/P1-258[»]
3BDMX-ray2.70B/P1-258[»]
3D29X-ray2.60B/P2-245[»]
3DY3X-ray2.81B/P2-245[»]
3DY4X-ray2.80B/P2-245[»]
3E47X-ray3.00B/P2-245[»]
3GPJX-ray2.70B/P2-245[»]
3GPTX-ray2.41B/P2-245[»]
3GPWX-ray2.50B/P2-245[»]
3HYEX-ray2.50B/P2-245[»]
3L5QX-ray3.00H/T14-245[»]
3MG0X-ray2.68B/P2-245[»]
3MG4X-ray3.11B/P2-245[»]
3MG6X-ray2.60B/P1-245[»]
3MG7X-ray2.78B/P1-245[»]
3MG8X-ray2.59B/P1-245[»]
3NZJX-ray2.40B/P1-258[»]
3NZWX-ray2.50B/P1-258[»]
3NZXX-ray2.70B/P1-258[»]
3OEUX-ray2.60B/P11-245[»]
3OEVX-ray2.85B/P11-245[»]
3OKJX-ray2.70B/P2-245[»]
3SDIX-ray2.65B/P11-245[»]
3SDKX-ray2.70B/P11-245[»]
3SHJX-ray2.80B/P2-245[»]
3TDDX-ray2.70B/P2-245[»]
3UN4X-ray3.40B/P1-258[»]
3UN8X-ray2.70B/P1-258[»]
4CR2electron microscopy7.70C1-258[»]
4CR3electron microscopy9.30C1-258[»]
4CR4electron microscopy8.80C1-258[»]
4EU2X-ray2.51C/Q2-245[»]
4FZCX-ray2.80B/P2-245[»]
4FZGX-ray3.00B/P2-245[»]
4G4SX-ray2.49C1-258[»]
4GK7X-ray2.80B/P2-245[»]
4HNPX-ray2.80B/P2-245[»]
4HRCX-ray2.80B/P2-245[»]
4HRDX-ray2.80B/P2-245[»]
4INRX-ray2.70B/P1-258[»]
4INTX-ray2.90B/P1-258[»]
4INUX-ray3.10B/P1-258[»]
4J70X-ray2.80B/P1-258[»]
4JSQX-ray2.80B/P1-258[»]
4JSUX-ray2.90B/P1-258[»]
4JT0X-ray3.10B/P1-258[»]
4LQIX-ray2.70B/P2-245[»]
4LTCX-ray2.50B/P1-258[»]
4NNNX-ray2.50B/P1-258[»]
4NNWX-ray2.60B/P1-258[»]
4NO1X-ray2.50B/P1-258[»]
4NO6X-ray3.00B/P1-258[»]
4NO8X-ray2.70B/P1-258[»]
4NO9X-ray2.90B/P1-258[»]
4Q1SX-ray2.60B/P1-258[»]
4QBYX-ray3.00B/P1-258[»]
4QLQX-ray2.40B/P1-258[»]
4QLSX-ray2.80B/P1-258[»]
4QLTX-ray2.80B/P1-258[»]
4QLUX-ray2.80B/P1-258[»]
4QLVX-ray2.90B/P1-258[»]
4R02X-ray2.50B/P1-258[»]
ProteinModelPortaliP23638.
SMRiP23638. Positions 2-245.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23638.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074827.
HOGENOMiHOG000091085.
InParanoidiP23638.
KOiK02728.
OMAiKQEYKDD.
OrthoDBiEOG7SBP0C.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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.

P23638-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSRRYDSRT TIFSPEGRLY QVEYALESIS HAGTAIGIMA SDGIVLAAER
60 70 80 90 100
KVTSTLLEQD TSTEKLYKLN DKIAVAVAGL TADAEILINT ARIHAQNYLK
110 120 130 140 150
TYNEDIPVEI LVRRLSDIKQ GYTQHGGLRP FGVSFIYAGY DDRYGYQLYT
160 170 180 190 200
SNPSGNYTGW KAISVGANTS AAQTLLQMDY KDDMKVDDAI ELALKTLSKT
210 220 230 240 250
TDSSALTYDR LEFATIRKGA NDGEVYQKIF KPQEIKDILV KTGITKKDED

EEADEDMK
Length:258
Mass (Da):28,714
Last modified:November 1, 1991 - v1
Checksum:iB43BB05233A01A9E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63851 Genomic DNA. Translation: AAA34907.1.
X56730 Genomic DNA. Translation: CAA40054.1.
Z72920 Genomic DNA. Translation: CAA97148.1.
BK006941 Genomic DNA. Translation: DAA08228.1.
PIRiS12940. SNBYY3.
RefSeqiNP_011651.3. NM_001181264.3.

Genome annotation databases

EnsemblFungiiYGR135W; YGR135W; YGR135W.
GeneIDi853036.
KEGGisce:YGR135W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63851 Genomic DNA. Translation: AAA34907.1 .
X56730 Genomic DNA. Translation: CAA40054.1 .
Z72920 Genomic DNA. Translation: CAA97148.1 .
BK006941 Genomic DNA. Translation: DAA08228.1 .
PIRi S12940. SNBYY3.
RefSeqi NP_011651.3. NM_001181264.3.

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 C/Q 1-245 [» ]
1G0U X-ray 2.40 B/P 1-245 [» ]
1G65 X-ray 2.25 B/P 2-245 [» ]
1JD2 X-ray 3.00 B/W 2-245 [» ]
1RYP X-ray 1.90 C/Q 2-245 [» ]
1VSY X-ray 3.00 C/Q 14-245 [» ]
1Z7Q X-ray 3.22 C/Q 1-258 [» ]
2F16 X-ray 2.80 B/P 2-245 [» ]
2FAK X-ray 2.80 B/P 2-245 [» ]
2GPL X-ray 2.81 B/P 2-245 [» ]
2ZCY X-ray 2.90 B/P 1-258 [» ]
3BDM X-ray 2.70 B/P 1-258 [» ]
3D29 X-ray 2.60 B/P 2-245 [» ]
3DY3 X-ray 2.81 B/P 2-245 [» ]
3DY4 X-ray 2.80 B/P 2-245 [» ]
3E47 X-ray 3.00 B/P 2-245 [» ]
3GPJ X-ray 2.70 B/P 2-245 [» ]
3GPT X-ray 2.41 B/P 2-245 [» ]
3GPW X-ray 2.50 B/P 2-245 [» ]
3HYE X-ray 2.50 B/P 2-245 [» ]
3L5Q X-ray 3.00 H/T 14-245 [» ]
3MG0 X-ray 2.68 B/P 2-245 [» ]
3MG4 X-ray 3.11 B/P 2-245 [» ]
3MG6 X-ray 2.60 B/P 1-245 [» ]
3MG7 X-ray 2.78 B/P 1-245 [» ]
3MG8 X-ray 2.59 B/P 1-245 [» ]
3NZJ X-ray 2.40 B/P 1-258 [» ]
3NZW X-ray 2.50 B/P 1-258 [» ]
3NZX X-ray 2.70 B/P 1-258 [» ]
3OEU X-ray 2.60 B/P 11-245 [» ]
3OEV X-ray 2.85 B/P 11-245 [» ]
3OKJ X-ray 2.70 B/P 2-245 [» ]
3SDI X-ray 2.65 B/P 11-245 [» ]
3SDK X-ray 2.70 B/P 11-245 [» ]
3SHJ X-ray 2.80 B/P 2-245 [» ]
3TDD X-ray 2.70 B/P 2-245 [» ]
3UN4 X-ray 3.40 B/P 1-258 [» ]
3UN8 X-ray 2.70 B/P 1-258 [» ]
4CR2 electron microscopy 7.70 C 1-258 [» ]
4CR3 electron microscopy 9.30 C 1-258 [» ]
4CR4 electron microscopy 8.80 C 1-258 [» ]
4EU2 X-ray 2.51 C/Q 2-245 [» ]
4FZC X-ray 2.80 B/P 2-245 [» ]
4FZG X-ray 3.00 B/P 2-245 [» ]
4G4S X-ray 2.49 C 1-258 [» ]
4GK7 X-ray 2.80 B/P 2-245 [» ]
4HNP X-ray 2.80 B/P 2-245 [» ]
4HRC X-ray 2.80 B/P 2-245 [» ]
4HRD X-ray 2.80 B/P 2-245 [» ]
4INR X-ray 2.70 B/P 1-258 [» ]
4INT X-ray 2.90 B/P 1-258 [» ]
4INU X-ray 3.10 B/P 1-258 [» ]
4J70 X-ray 2.80 B/P 1-258 [» ]
4JSQ X-ray 2.80 B/P 1-258 [» ]
4JSU X-ray 2.90 B/P 1-258 [» ]
4JT0 X-ray 3.10 B/P 1-258 [» ]
4LQI X-ray 2.70 B/P 2-245 [» ]
4LTC X-ray 2.50 B/P 1-258 [» ]
4NNN X-ray 2.50 B/P 1-258 [» ]
4NNW X-ray 2.60 B/P 1-258 [» ]
4NO1 X-ray 2.50 B/P 1-258 [» ]
4NO6 X-ray 3.00 B/P 1-258 [» ]
4NO8 X-ray 2.70 B/P 1-258 [» ]
4NO9 X-ray 2.90 B/P 1-258 [» ]
4Q1S X-ray 2.60 B/P 1-258 [» ]
4QBY X-ray 3.00 B/P 1-258 [» ]
4QLQ X-ray 2.40 B/P 1-258 [» ]
4QLS X-ray 2.80 B/P 1-258 [» ]
4QLT X-ray 2.80 B/P 1-258 [» ]
4QLU X-ray 2.80 B/P 1-258 [» ]
4QLV X-ray 2.90 B/P 1-258 [» ]
4R02 X-ray 2.50 B/P 1-258 [» ]
ProteinModelPortali P23638.
SMRi P23638. Positions 2-245.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33383. 328 interactions.
DIPi DIP-2823N.
IntActi P23638. 17 interactions.
MINTi MINT-484272.
STRINGi 4932.YGR135W.

Protein family/group databases

MEROPSi T01.973.

Proteomic databases

MaxQBi P23638.
PaxDbi P23638.
PeptideAtlasi P23638.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR135W ; YGR135W ; YGR135W .
GeneIDi 853036.
KEGGi sce:YGR135W.

Organism-specific databases

CYGDi YGR135w.
SGDi S000003367. PRE9.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074827.
HOGENOMi HOG000091085.
InParanoidi P23638.
KOi K02728.
OMAi KQEYKDD.
OrthoDBi EOG7SBP0C.

Enzyme and pathway databases

BioCyci YEAST:G3O-30841-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 P23638.
NextBioi 972935.
PROi P23638.

Gene expression databases

Genevestigatori P23638.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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], PROTEIN SEQUENCE OF 73-92; 120-139 AND 200-236.
    Strain: ATCC 26786 / X2180-1A.
  2. "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.
    , 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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
    Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-199.
  6. "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].
  7. "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 2-245 OF COMPLEX WITH THE 20S PROTEASOME.
  8. "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 1-245 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-245 OF COMPLEX WITH THE 20S PROTEASOME.
  10. "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 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
  11. "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 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
  12. "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 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
  13. "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 14-245 IN COMPLEX WITH THE PROTEASOME.
  14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSA3_YEAST
AccessioniPrimary (citable) accession number: P23638
Secondary accession number(s): D6VUR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 26, 2014
This is version 155 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 17100 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3