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Protein

Proteasome subunit alpha type-4

Gene

PRE6

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

GO - Biological processi

  • proteasomal ubiquitin-independent protein catabolic process Source: SGD
  • 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-33452-MONOMER.
ReactomeiREACT_291351. Orc1 removal from chromatin.
REACT_305425. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_343770. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_344477. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_346191. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_347103. ER-Phagosome pathway.
REACT_354180. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-4 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PRE6
Multicatalytic endopeptidase complex subunit PRE6
Proteasome component PRE6
Proteinase YSCE subunit PRE6
Gene namesi
Name:PRE6
Ordered Locus Names:YOL038W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOL038w.
EuPathDBiFungiDB:YOL038W.
SGDiS000005398. PRE6.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
  • nuclear outer membrane-endoplasmic reticulum membrane network Source: SGD
  • nucleus Source: SGD
  • proteasome core complex, alpha-subunit complex Source: SGD
  • 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 – 254254Proteasome subunit alpha type-4PRO_0000124165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40303.
PaxDbiP40303.
PeptideAtlasiP40303.
PRIDEiP40303.

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. Interacts with CIC1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CIC1P387795EBI-13980,EBI-24538
cut8P389372EBI-13980,EBI-1152591From a different organism.
PRE1P221413EBI-13980,EBI-13988

Protein-protein interaction databases

BioGridi34364. 106 interactions.
DIPiDIP-4844N.
IntActiP40303. 42 interactions.
MINTiMINT-478854.

Structurei

Secondary structure

1
254
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Turni13 – 153Combined sources
Helixi18 – 2710Combined sources
Beta strandi33 – 375Combined sources
Beta strandi42 – 476Combined sources
Turni57 – 593Combined sources
Beta strandi63 – 686Combined sources
Beta strandi71 – 777Combined sources
Helixi79 – 10022Combined sources
Helixi106 – 11914Combined sources
Turni120 – 1223Combined sources
Beta strandi123 – 1264Combined sources
Beta strandi130 – 1378Combined sources
Beta strandi146 – 1505Combined sources
Turni152 – 1543Combined sources
Beta strandi156 – 16510Combined sources
Helixi168 – 1769Combined sources
Beta strandi181 – 1833Combined sources
Helixi188 – 20316Combined sources
Beta strandi204 – 2074Combined sources
Beta strandi210 – 2167Combined sources
Turni217 – 2193Combined sources
Beta strandi220 – 2234Combined sources
Helixi226 – 23611Combined sources
Helixi238 – 2414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20D/R1-254[»]
1G0UX-ray2.40C/Q1-243[»]
1G65X-ray2.25C/Q3-243[»]
1JD2X-ray3.00C/X3-243[»]
1RYPX-ray1.90D/R3-243[»]
1Z7QX-ray3.22D/R1-254[»]
2F16X-ray2.80C/Q3-243[»]
2FAKX-ray2.80C/Q3-243[»]
2GPLX-ray2.81C/Q3-243[»]
2ZCYX-ray2.90C/Q1-254[»]
3BDMX-ray2.70C/Q1-254[»]
3D29X-ray2.60C/Q3-236[»]
3DY3X-ray2.81C/Q3-243[»]
3DY4X-ray2.80C/Q3-243[»]
3E47X-ray3.00C/Q3-243[»]
3GPJX-ray2.70C/Q3-243[»]
3GPTX-ray2.41C/Q3-243[»]
3GPWX-ray2.50C/Q3-243[»]
3HYEX-ray2.50C/Q3-243[»]
3MG0X-ray2.68C/Q3-243[»]
3MG4X-ray3.11C/Q3-243[»]
3MG6X-ray2.60C/Q1-243[»]
3MG7X-ray2.78C/Q1-243[»]
3MG8X-ray2.59C/Q1-243[»]
3NZJX-ray2.40C/Q1-254[»]
3NZWX-ray2.50C/Q1-254[»]
3NZXX-ray2.70C/Q1-254[»]
3OEUX-ray2.60C/Q3-243[»]
3OEVX-ray2.85C/Q3-243[»]
3OKJX-ray2.70C/Q3-243[»]
3SDIX-ray2.65C/Q3-243[»]
3SDKX-ray2.70C/Q3-243[»]
3SHJX-ray2.80C/Q3-243[»]
3TDDX-ray2.70C/Q3-243[»]
3UN4X-ray3.40C/Q1-254[»]
3UN8X-ray2.70C/Q1-254[»]
3WXRX-ray3.15D/R1-254[»]
4CR2electron microscopy7.70D1-254[»]
4CR3electron microscopy9.30D1-254[»]
4CR4electron microscopy8.80D1-254[»]
4EU2X-ray2.51D/R3-243[»]
4FZCX-ray2.80C/Q3-243[»]
4FZGX-ray3.00C/Q3-243[»]
4G4SX-ray2.49D1-254[»]
4GK7X-ray2.80C/Q3-243[»]
4HNPX-ray2.80C/Q3-243[»]
4HRCX-ray2.80C/Q3-243[»]
4HRDX-ray2.80C/Q3-243[»]
4INRX-ray2.70C/Q1-254[»]
4INTX-ray2.90C/Q1-254[»]
4INUX-ray3.10C/Q1-254[»]
4J70X-ray2.80C/Q1-254[»]
4JSQX-ray2.80C/Q1-254[»]
4JSUX-ray2.90C/Q1-254[»]
4JT0X-ray3.10C/Q1-254[»]
4LQIX-ray2.70C/Q3-243[»]
4LTCX-ray2.50C/Q1-254[»]
4NNNX-ray2.50C/Q1-254[»]
4NNWX-ray2.60C/Q1-254[»]
4NO1X-ray2.50C/Q1-254[»]
4NO6X-ray3.00C/Q1-254[»]
4NO8X-ray2.70C/Q1-254[»]
4NO9X-ray2.90C/Q1-254[»]
4Q1SX-ray2.60C/Q1-254[»]
4QBYX-ray3.00C/Q1-254[»]
4QLQX-ray2.40C/Q1-254[»]
4QLSX-ray2.80C/Q1-254[»]
4QLTX-ray2.80C/Q1-254[»]
4QLUX-ray2.80C/Q1-254[»]
4QLVX-ray2.90C/Q1-254[»]
4QUXX-ray3.00C/Q1-254[»]
4QUYX-ray2.80C/Q1-254[»]
4QV0X-ray3.10C/Q1-254[»]
4QV1X-ray2.50C/Q1-254[»]
4QV3X-ray3.00C/Q1-254[»]
4QV4X-ray2.70C/Q1-254[»]
4QV5X-ray2.70C/Q1-254[»]
4QV6X-ray2.80C/Q1-254[»]
4QV7X-ray2.60C/Q1-254[»]
4QV8X-ray2.90C/Q1-254[»]
4QV9X-ray2.60C/Q1-254[»]
4QVLX-ray2.80C/Q1-254[»]
4QVMX-ray2.80C/Q1-254[»]
4QVNX-ray2.90C/Q1-254[»]
4QVPX-ray2.30C/Q1-254[»]
4QVQX-ray2.60C/Q1-254[»]
4QVVX-ray2.80C/Q1-254[»]
4QVWX-ray3.00C/Q1-254[»]
4QVYX-ray2.51C/Q1-254[»]
4QW0X-ray2.90C/Q1-254[»]
4QW1X-ray2.90C/Q1-254[»]
4QW3X-ray2.90C/Q1-254[»]
4QW4X-ray2.80C/Q1-254[»]
4QW5X-ray3.00C/Q1-254[»]
4QW6X-ray2.90C/Q1-254[»]
4QW7X-ray2.70C/Q1-254[»]
4QWFX-ray3.00C/Q1-254[»]
4QWGX-ray2.60C/Q1-254[»]
4QWIX-ray2.60C/Q1-254[»]
4QWJX-ray2.90C/Q1-254[»]
4QWKX-ray2.80C/Q1-254[»]
4QWLX-ray2.60C/Q1-254[»]
4QWRX-ray2.90C/Q1-254[»]
4QWSX-ray3.00C/Q1-254[»]
4QWUX-ray3.00C/Q1-254[»]
4QWXX-ray2.90C/Q1-254[»]
4QXJX-ray2.80C/Q1-254[»]
4QZ0X-ray3.00C/Q1-254[»]
4QZ1X-ray3.00C/Q1-254[»]
4QZ2X-ray2.70C/Q1-254[»]
4QZ3X-ray2.80C/Q1-254[»]
4QZ4X-ray3.00C/Q1-254[»]
4QZ5X-ray2.80C/Q1-254[»]
4QZ6X-ray2.90C/Q1-254[»]
4QZ7X-ray2.80C/Q1-254[»]
4QZWX-ray3.00C/Q1-254[»]
4QZXX-ray2.60C/Q1-254[»]
4QZZX-ray2.90C/Q1-254[»]
4R00X-ray2.80C/Q1-254[»]
4R02X-ray2.50C/Q1-254[»]
4R17X-ray2.10C/Q1-254[»]
4R18X-ray2.40C/Q1-254[»]
4RURX-ray2.50C/Q1-254[»]
4V7OX-ray3.00AI/AU/BD/BR17-243[»]
4Z1LX-ray3.00C/Q1-254[»]
5AHJX-ray2.80C/Q1-254[»]
ProteinModelPortaliP40303.
SMRiP40303. Positions 3-243.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40303.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074753.
HOGENOMiHOG000091085.
InParanoidiP40303.
KOiK02731.
OMAiERNYKED.
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.

P40303-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGYDRALSI FSPDGHIFQV EYALEAVKRG TCAVGVKGKN CVVLGCERRS
60 70 80 90 100
TLKLQDTRIT PSKVSKIDSH VVLSFSGLNA DSRILIEKAR VEAQSHRLTL
110 120 130 140 150
EDPVTVEYLT RYVAGVQQRY TQSGGVRPFG VSTLIAGFDP RDDEPKLYQT
160 170 180 190 200
EPSGIYSSWS AQTIGRNSKT VREFLEKNYD RKEPPATVEE CVKLTVRSLL
210 220 230 240 250
EVVQTGAKNI EITVVKPDSD IVALSSEEIN QYVTQIEQEK QEQQEQDKKK

KSNH
Length:254
Mass (Da):28,439
Last modified:February 1, 1995 - v1
Checksum:i73AEE63B836E618A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34348 Genomic DNA. Translation: AAA34903.1.
Z74780 Genomic DNA. Translation: CAA99040.1.
BK006948 Genomic DNA. Translation: DAA10745.1.
PIRiB55904.
RefSeqiNP_014604.1. NM_001183292.1.

Genome annotation databases

EnsemblFungiiYOL038W; YOL038W; YOL038W.
GeneIDi854119.
KEGGisce:YOL038W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34348 Genomic DNA. Translation: AAA34903.1.
Z74780 Genomic DNA. Translation: CAA99040.1.
BK006948 Genomic DNA. Translation: DAA10745.1.
PIRiB55904.
RefSeqiNP_014604.1. NM_001183292.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20D/R1-254[»]
1G0UX-ray2.40C/Q1-243[»]
1G65X-ray2.25C/Q3-243[»]
1JD2X-ray3.00C/X3-243[»]
1RYPX-ray1.90D/R3-243[»]
1Z7QX-ray3.22D/R1-254[»]
2F16X-ray2.80C/Q3-243[»]
2FAKX-ray2.80C/Q3-243[»]
2GPLX-ray2.81C/Q3-243[»]
2ZCYX-ray2.90C/Q1-254[»]
3BDMX-ray2.70C/Q1-254[»]
3D29X-ray2.60C/Q3-236[»]
3DY3X-ray2.81C/Q3-243[»]
3DY4X-ray2.80C/Q3-243[»]
3E47X-ray3.00C/Q3-243[»]
3GPJX-ray2.70C/Q3-243[»]
3GPTX-ray2.41C/Q3-243[»]
3GPWX-ray2.50C/Q3-243[»]
3HYEX-ray2.50C/Q3-243[»]
3MG0X-ray2.68C/Q3-243[»]
3MG4X-ray3.11C/Q3-243[»]
3MG6X-ray2.60C/Q1-243[»]
3MG7X-ray2.78C/Q1-243[»]
3MG8X-ray2.59C/Q1-243[»]
3NZJX-ray2.40C/Q1-254[»]
3NZWX-ray2.50C/Q1-254[»]
3NZXX-ray2.70C/Q1-254[»]
3OEUX-ray2.60C/Q3-243[»]
3OEVX-ray2.85C/Q3-243[»]
3OKJX-ray2.70C/Q3-243[»]
3SDIX-ray2.65C/Q3-243[»]
3SDKX-ray2.70C/Q3-243[»]
3SHJX-ray2.80C/Q3-243[»]
3TDDX-ray2.70C/Q3-243[»]
3UN4X-ray3.40C/Q1-254[»]
3UN8X-ray2.70C/Q1-254[»]
3WXRX-ray3.15D/R1-254[»]
4CR2electron microscopy7.70D1-254[»]
4CR3electron microscopy9.30D1-254[»]
4CR4electron microscopy8.80D1-254[»]
4EU2X-ray2.51D/R3-243[»]
4FZCX-ray2.80C/Q3-243[»]
4FZGX-ray3.00C/Q3-243[»]
4G4SX-ray2.49D1-254[»]
4GK7X-ray2.80C/Q3-243[»]
4HNPX-ray2.80C/Q3-243[»]
4HRCX-ray2.80C/Q3-243[»]
4HRDX-ray2.80C/Q3-243[»]
4INRX-ray2.70C/Q1-254[»]
4INTX-ray2.90C/Q1-254[»]
4INUX-ray3.10C/Q1-254[»]
4J70X-ray2.80C/Q1-254[»]
4JSQX-ray2.80C/Q1-254[»]
4JSUX-ray2.90C/Q1-254[»]
4JT0X-ray3.10C/Q1-254[»]
4LQIX-ray2.70C/Q3-243[»]
4LTCX-ray2.50C/Q1-254[»]
4NNNX-ray2.50C/Q1-254[»]
4NNWX-ray2.60C/Q1-254[»]
4NO1X-ray2.50C/Q1-254[»]
4NO6X-ray3.00C/Q1-254[»]
4NO8X-ray2.70C/Q1-254[»]
4NO9X-ray2.90C/Q1-254[»]
4Q1SX-ray2.60C/Q1-254[»]
4QBYX-ray3.00C/Q1-254[»]
4QLQX-ray2.40C/Q1-254[»]
4QLSX-ray2.80C/Q1-254[»]
4QLTX-ray2.80C/Q1-254[»]
4QLUX-ray2.80C/Q1-254[»]
4QLVX-ray2.90C/Q1-254[»]
4QUXX-ray3.00C/Q1-254[»]
4QUYX-ray2.80C/Q1-254[»]
4QV0X-ray3.10C/Q1-254[»]
4QV1X-ray2.50C/Q1-254[»]
4QV3X-ray3.00C/Q1-254[»]
4QV4X-ray2.70C/Q1-254[»]
4QV5X-ray2.70C/Q1-254[»]
4QV6X-ray2.80C/Q1-254[»]
4QV7X-ray2.60C/Q1-254[»]
4QV8X-ray2.90C/Q1-254[»]
4QV9X-ray2.60C/Q1-254[»]
4QVLX-ray2.80C/Q1-254[»]
4QVMX-ray2.80C/Q1-254[»]
4QVNX-ray2.90C/Q1-254[»]
4QVPX-ray2.30C/Q1-254[»]
4QVQX-ray2.60C/Q1-254[»]
4QVVX-ray2.80C/Q1-254[»]
4QVWX-ray3.00C/Q1-254[»]
4QVYX-ray2.51C/Q1-254[»]
4QW0X-ray2.90C/Q1-254[»]
4QW1X-ray2.90C/Q1-254[»]
4QW3X-ray2.90C/Q1-254[»]
4QW4X-ray2.80C/Q1-254[»]
4QW5X-ray3.00C/Q1-254[»]
4QW6X-ray2.90C/Q1-254[»]
4QW7X-ray2.70C/Q1-254[»]
4QWFX-ray3.00C/Q1-254[»]
4QWGX-ray2.60C/Q1-254[»]
4QWIX-ray2.60C/Q1-254[»]
4QWJX-ray2.90C/Q1-254[»]
4QWKX-ray2.80C/Q1-254[»]
4QWLX-ray2.60C/Q1-254[»]
4QWRX-ray2.90C/Q1-254[»]
4QWSX-ray3.00C/Q1-254[»]
4QWUX-ray3.00C/Q1-254[»]
4QWXX-ray2.90C/Q1-254[»]
4QXJX-ray2.80C/Q1-254[»]
4QZ0X-ray3.00C/Q1-254[»]
4QZ1X-ray3.00C/Q1-254[»]
4QZ2X-ray2.70C/Q1-254[»]
4QZ3X-ray2.80C/Q1-254[»]
4QZ4X-ray3.00C/Q1-254[»]
4QZ5X-ray2.80C/Q1-254[»]
4QZ6X-ray2.90C/Q1-254[»]
4QZ7X-ray2.80C/Q1-254[»]
4QZWX-ray3.00C/Q1-254[»]
4QZXX-ray2.60C/Q1-254[»]
4QZZX-ray2.90C/Q1-254[»]
4R00X-ray2.80C/Q1-254[»]
4R02X-ray2.50C/Q1-254[»]
4R17X-ray2.10C/Q1-254[»]
4R18X-ray2.40C/Q1-254[»]
4RURX-ray2.50C/Q1-254[»]
4V7OX-ray3.00AI/AU/BD/BR17-243[»]
4Z1LX-ray3.00C/Q1-254[»]
5AHJX-ray2.80C/Q1-254[»]
ProteinModelPortaliP40303.
SMRiP40303. Positions 3-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34364. 106 interactions.
DIPiDIP-4844N.
IntActiP40303. 42 interactions.
MINTiMINT-478854.

Proteomic databases

MaxQBiP40303.
PaxDbiP40303.
PeptideAtlasiP40303.
PRIDEiP40303.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL038W; YOL038W; YOL038W.
GeneIDi854119.
KEGGisce:YOL038W.

Organism-specific databases

CYGDiYOL038w.
EuPathDBiFungiDB:YOL038W.
SGDiS000005398. PRE6.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074753.
HOGENOMiHOG000091085.
InParanoidiP40303.
KOiK02731.
OMAiERNYKED.
OrthoDBiEOG7SBP0C.

Enzyme and pathway databases

BioCyciYEAST:G3O-33452-MONOMER.
ReactomeiREACT_291351. Orc1 removal from chromatin.
REACT_305425. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_343770. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_344477. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_346191. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_347103. ER-Phagosome pathway.
REACT_354180. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

Miscellaneous databases

EvolutionaryTraceiP40303.
NextBioi975822.
PROiP40303.

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]
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].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(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. Troendle N.
    Thesis (1991), University of Stuttgart, Germany
    Cited for: PROTEIN SEQUENCE OF 112-133.
  5. "Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4."
    Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.
    EMBO J. 20:4423-4431(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIC1.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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 3-343 OF COMPLEX WITH THE 20S PROTEASOME.
  10. "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.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-243 OF COMPLEX WITH THE 20S PROTEASOME.
  12. "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 3-243 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 3-243 OF COMPLEX WITH THE 20S PROTEASOME.
  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 3-243 OF COMPLEX WITH THE 20S PROTEASOME.
  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 3-243 OF COMPLEX WITH THE 20S PROTEASOME.
  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) OF 17-243 IN COMPLEX WITH THE PROTEASOME.
  17. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSA4_YEAST
AccessioniPrimary (citable) accession number: P40303
Secondary accession number(s): D6W229
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 163 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 16800 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.