Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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.
ReactomeiR-SCE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-SCE-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-SCE-382556. ABC-family proteins mediated transport.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-SCE-5668541. TNFR2 non-canonical NF-kB pathway.
R-SCE-5687128. MAPK6/MAPK4 signaling.
R-SCE-5689880. Ub-specific processing proteases.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SCE-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-SCE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-SCE-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001241651 – 254Proteasome subunit alpha type-4Add BLAST254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei60PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40303.
PRIDEiP40303.

PTM databases

iPTMnetiP40303.

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. 107 interactors.
DIPiDIP-4844N.
IntActiP40303. 42 interactors.
MINTiMINT-478854.

Structurei

Secondary structure

1254
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 10Combined sources4
Turni13 – 15Combined sources3
Helixi18 – 27Combined sources10
Beta strandi33 – 37Combined sources5
Beta strandi42 – 47Combined sources6
Turni57 – 59Combined sources3
Beta strandi63 – 68Combined sources6
Beta strandi71 – 77Combined sources7
Helixi79 – 100Combined sources22
Helixi106 – 119Combined sources14
Turni120 – 122Combined sources3
Beta strandi123 – 126Combined sources4
Beta strandi130 – 137Combined sources8
Beta strandi146 – 150Combined sources5
Turni152 – 154Combined sources3
Beta strandi156 – 165Combined sources10
Helixi168 – 176Combined sources9
Beta strandi181 – 183Combined sources3
Helixi188 – 203Combined sources16
Beta strandi204 – 207Combined sources4
Beta strandi210 – 216Combined sources7
Turni217 – 219Combined sources3
Beta strandi220 – 223Combined sources4
Helixi226 – 236Combined sources11
Helixi238 – 241Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3JCOelectron microscopy4.80D/d1-254[»]
3JCPelectron microscopy4.60D/d1-254[»]
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[»]
4X6ZX-ray2.70D/R1-254[»]
4Y69X-ray2.90C/Q1-254[»]
4Y6AX-ray2.60C/Q1-254[»]
4Y6VX-ray2.80C/Q1-254[»]
4Y6ZX-ray2.70C/Q1-254[»]
4Y70X-ray2.40C/Q1-254[»]
4Y74X-ray2.70C/Q1-254[»]
4Y75X-ray2.80C/Q1-254[»]
4Y77X-ray2.50C/Q1-254[»]
4Y78X-ray2.80C/Q1-254[»]
4Y7WX-ray2.50C/Q1-254[»]
4Y7XX-ray2.60C/Q1-254[»]
4Y7YX-ray2.40C/Q1-254[»]
4Y80X-ray2.50C/Q1-254[»]
4Y81X-ray2.80C/Q1-254[»]
4Y82X-ray2.80C/Q1-254[»]
4Y84X-ray2.70C/Q1-254[»]
4Y8GX-ray2.60C/Q1-254[»]
4Y8HX-ray2.50C/Q1-254[»]
4Y8IX-ray2.60C/Q1-254[»]
4Y8JX-ray2.70C/Q1-254[»]
4Y8KX-ray2.60C/Q1-254[»]
4Y8LX-ray2.40C/Q1-254[»]
4Y8MX-ray2.80C/Q1-254[»]
4Y8NX-ray2.60C/Q1-254[»]
4Y8OX-ray2.70C/Q1-254[»]
4Y8PX-ray2.80C/Q1-254[»]
4Y8QX-ray2.60C/Q1-254[»]
4Y8RX-ray2.70C/Q1-254[»]
4Y8SX-ray2.70C/Q1-254[»]
4Y8TX-ray2.70C/Q1-254[»]
4Y8UX-ray2.90C/Q1-254[»]
4Y9YX-ray2.80C/Q1-254[»]
4Y9ZX-ray2.80C/Q1-254[»]
4YA0X-ray2.80C/Q1-254[»]
4YA1X-ray2.90C/Q1-254[»]
4YA2X-ray2.70C/Q1-254[»]
4YA3X-ray2.70C/Q1-254[»]
4YA4X-ray2.90C/Q1-254[»]
4YA5X-ray2.50C/Q1-254[»]
4YA7X-ray2.70C/Q1-254[»]
4YA9X-ray2.70C/Q1-254[»]
4Z1LX-ray3.00C/Q1-254[»]
4ZZGX-ray3.00D/R1-254[»]
5A5Belectron microscopy9.50D1-254[»]
5AHJX-ray2.80C/Q1-254[»]
5BOUX-ray2.60C/Q1-254[»]
5BXLX-ray2.80C/Q1-254[»]
5BXNX-ray2.80C/Q1-254[»]
5CGFX-ray2.80C/Q1-254[»]
5CGGX-ray2.90C/Q1-254[»]
5CGHX-ray2.50C/Q1-254[»]
5CGIX-ray2.80C/Q1-254[»]
5CZ4X-ray2.30C/Q1-254[»]
5CZ5X-ray2.80C/Q1-254[»]
5CZ6X-ray2.70C/Q1-254[»]
5CZ7X-ray2.50C/Q1-254[»]
5CZ8X-ray2.80C/Q1-254[»]
5CZ9X-ray2.90C/Q1-254[»]
5CZAX-ray2.50C/Q1-254[»]
5D0SX-ray2.50C/Q1-254[»]
5D0TX-ray2.60C/Q1-254[»]
5D0VX-ray2.90C/Q1-254[»]
5D0WX-ray2.80C/Q1-254[»]
5D0XX-ray2.60C/Q1-254[»]
5D0ZX-ray2.90C/Q1-254[»]
5DKIX-ray2.80C/Q1-254[»]
5DKJX-ray2.80C/Q1-254[»]
5FG7X-ray2.70C/Q1-254[»]
5FG9X-ray2.60C/Q1-254[»]
5FGAX-ray2.70C/Q1-254[»]
5FGDX-ray2.80C/Q1-254[»]
5FGEX-ray2.60C/Q1-254[»]
5FGFX-ray2.60C/Q1-254[»]
5FGGX-ray2.70C/Q1-254[»]
5FGHX-ray2.80C/Q1-254[»]
5FGIX-ray2.90C/Q1-254[»]
5FHSX-ray2.70C/Q1-254[»]
5JHRX-ray2.90C/Q1-254[»]
5JHSX-ray3.00C/Q1-254[»]
ProteinModelPortaliP40303.
SMRiP40303.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40303.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074753.
HOGENOMiHOG000091085.
InParanoidiP40303.
KOiK02731.
OMAiEVAIMAP.
OrthoDBiEOG092C47D8.

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
PDB 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[»]
3JCOelectron microscopy4.80D/d1-254[»]
3JCPelectron microscopy4.60D/d1-254[»]
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[»]
4X6ZX-ray2.70D/R1-254[»]
4Y69X-ray2.90C/Q1-254[»]
4Y6AX-ray2.60C/Q1-254[»]
4Y6VX-ray2.80C/Q1-254[»]
4Y6ZX-ray2.70C/Q1-254[»]
4Y70X-ray2.40C/Q1-254[»]
4Y74X-ray2.70C/Q1-254[»]
4Y75X-ray2.80C/Q1-254[»]
4Y77X-ray2.50C/Q1-254[»]
4Y78X-ray2.80C/Q1-254[»]
4Y7WX-ray2.50C/Q1-254[»]
4Y7XX-ray2.60C/Q1-254[»]
4Y7YX-ray2.40C/Q1-254[»]
4Y80X-ray2.50C/Q1-254[»]
4Y81X-ray2.80C/Q1-254[»]
4Y82X-ray2.80C/Q1-254[»]
4Y84X-ray2.70C/Q1-254[»]
4Y8GX-ray2.60C/Q1-254[»]
4Y8HX-ray2.50C/Q1-254[»]
4Y8IX-ray2.60C/Q1-254[»]
4Y8JX-ray2.70C/Q1-254[»]
4Y8KX-ray2.60C/Q1-254[»]
4Y8LX-ray2.40C/Q1-254[»]
4Y8MX-ray2.80C/Q1-254[»]
4Y8NX-ray2.60C/Q1-254[»]
4Y8OX-ray2.70C/Q1-254[»]
4Y8PX-ray2.80C/Q1-254[»]
4Y8QX-ray2.60C/Q1-254[»]
4Y8RX-ray2.70C/Q1-254[»]
4Y8SX-ray2.70C/Q1-254[»]
4Y8TX-ray2.70C/Q1-254[»]
4Y8UX-ray2.90C/Q1-254[»]
4Y9YX-ray2.80C/Q1-254[»]
4Y9ZX-ray2.80C/Q1-254[»]
4YA0X-ray2.80C/Q1-254[»]
4YA1X-ray2.90C/Q1-254[»]
4YA2X-ray2.70C/Q1-254[»]
4YA3X-ray2.70C/Q1-254[»]
4YA4X-ray2.90C/Q1-254[»]
4YA5X-ray2.50C/Q1-254[»]
4YA7X-ray2.70C/Q1-254[»]
4YA9X-ray2.70C/Q1-254[»]
4Z1LX-ray3.00C/Q1-254[»]
4ZZGX-ray3.00D/R1-254[»]
5A5Belectron microscopy9.50D1-254[»]
5AHJX-ray2.80C/Q1-254[»]
5BOUX-ray2.60C/Q1-254[»]
5BXLX-ray2.80C/Q1-254[»]
5BXNX-ray2.80C/Q1-254[»]
5CGFX-ray2.80C/Q1-254[»]
5CGGX-ray2.90C/Q1-254[»]
5CGHX-ray2.50C/Q1-254[»]
5CGIX-ray2.80C/Q1-254[»]
5CZ4X-ray2.30C/Q1-254[»]
5CZ5X-ray2.80C/Q1-254[»]
5CZ6X-ray2.70C/Q1-254[»]
5CZ7X-ray2.50C/Q1-254[»]
5CZ8X-ray2.80C/Q1-254[»]
5CZ9X-ray2.90C/Q1-254[»]
5CZAX-ray2.50C/Q1-254[»]
5D0SX-ray2.50C/Q1-254[»]
5D0TX-ray2.60C/Q1-254[»]
5D0VX-ray2.90C/Q1-254[»]
5D0WX-ray2.80C/Q1-254[»]
5D0XX-ray2.60C/Q1-254[»]
5D0ZX-ray2.90C/Q1-254[»]
5DKIX-ray2.80C/Q1-254[»]
5DKJX-ray2.80C/Q1-254[»]
5FG7X-ray2.70C/Q1-254[»]
5FG9X-ray2.60C/Q1-254[»]
5FGAX-ray2.70C/Q1-254[»]
5FGDX-ray2.80C/Q1-254[»]
5FGEX-ray2.60C/Q1-254[»]
5FGFX-ray2.60C/Q1-254[»]
5FGGX-ray2.70C/Q1-254[»]
5FGHX-ray2.80C/Q1-254[»]
5FGIX-ray2.90C/Q1-254[»]
5FHSX-ray2.70C/Q1-254[»]
5JHRX-ray2.90C/Q1-254[»]
5JHSX-ray3.00C/Q1-254[»]
ProteinModelPortaliP40303.
SMRiP40303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34364. 107 interactors.
DIPiDIP-4844N.
IntActiP40303. 42 interactors.
MINTiMINT-478854.

PTM databases

iPTMnetiP40303.

Proteomic databases

MaxQBiP40303.
PRIDEiP40303.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YOL038W.
SGDiS000005398. PRE6.

Phylogenomic databases

GeneTreeiENSGT00550000074753.
HOGENOMiHOG000091085.
InParanoidiP40303.
KOiK02731.
OMAiEVAIMAP.
OrthoDBiEOG092C47D8.

Enzyme and pathway databases

BioCyciYEAST:G3O-33452-MONOMER.
ReactomeiR-SCE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-SCE-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-SCE-382556. ABC-family proteins mediated transport.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-SCE-5668541. TNFR2 non-canonical NF-kB pathway.
R-SCE-5687128. MAPK6/MAPK4 signaling.
R-SCE-5689880. Ub-specific processing proteases.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SCE-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-SCE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-SCE-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiP40303.
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...

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: November 30, 2016
This is version 177 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

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 one 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.