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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

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-32978-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.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR314W.
SGDiS000004931. PRE5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm 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_00001240761 – 234Proteasome subunit alpha type-6Add BLAST234

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineCombined sources1
Cross-linki191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP40302.
PRIDEiP40302.

2D gel databases

UCD-2DPAGEP40302.

PTM databases

iPTMnetiP40302.

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. 85 interactors.
DIPiDIP-1528N.
IntActiP40302. 33 interactors.
MINTiMINT-400436.

Structurei

Secondary structure

1234
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Beta strandi15 – 17Combined sources3
Helixi20 – 30Combined sources11
Beta strandi35 – 39Combined sources5
Beta strandi41 – 49Combined sources9
Beta strandi52 – 54Combined sources3
Beta strandi63 – 67Combined sources5
Beta strandi70 – 76Combined sources7
Helixi78 – 99Combined sources22
Helixi105 – 121Combined sources17
Beta strandi122 – 124Combined sources3
Beta strandi130 – 138Combined sources9
Beta strandi141 – 147Combined sources7
Turni149 – 151Combined sources3
Beta strandi153 – 162Combined sources10
Turni163 – 165Combined sources3
Helixi166 – 179Combined sources14
Helixi186 – 197Combined sources12
Helixi198 – 200Combined sources3
Beta strandi202 – 204Combined sources3
Turni208 – 210Combined sources3
Beta strandi211 – 217Combined sources7
Beta strandi220 – 226Combined sources7
Helixi227 – 233Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3JCOelectron microscopy4.80F/f1-234[»]
3JCPelectron microscopy4.60F/f1-234[»]
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[»]
4QUXX-ray3.00E/S1-234[»]
4QUYX-ray2.80E/S1-234[»]
4QV0X-ray3.10E/S1-234[»]
4QV1X-ray2.50E/S1-234[»]
4QV3X-ray3.00E/S1-234[»]
4QV4X-ray2.70E/S1-234[»]
4QV5X-ray2.70E/S1-234[»]
4QV6X-ray2.80E/S1-234[»]
4QV7X-ray2.60E/S1-234[»]
4QV8X-ray2.90E/S1-234[»]
4QV9X-ray2.60E/S1-234[»]
4QVLX-ray2.80E/S1-234[»]
4QVMX-ray2.80E/S1-234[»]
4QVNX-ray2.90E/S1-234[»]
4QVPX-ray2.30E/S1-234[»]
4QVQX-ray2.60E/S1-234[»]
4QVVX-ray2.80E/S1-234[»]
4QVWX-ray3.00E/S1-234[»]
4QVYX-ray2.51E/S1-234[»]
4QW0X-ray2.90E/S1-234[»]
4QW1X-ray2.90E/S1-234[»]
4QW3X-ray2.90E/S1-234[»]
4QW4X-ray2.80E/S1-234[»]
4QW5X-ray3.00E/S1-234[»]
4QW6X-ray2.90E/S1-234[»]
4QW7X-ray2.70E/S1-234[»]
4QWFX-ray3.00E/S1-234[»]
4QWGX-ray2.60E/S1-234[»]
4QWIX-ray2.60E/S1-234[»]
4QWJX-ray2.90E/S1-234[»]
4QWKX-ray2.80E/S1-234[»]
4QWLX-ray2.60E/S1-234[»]
4QWRX-ray2.90E/S1-234[»]
4QWSX-ray3.00E/S1-234[»]
4QWUX-ray3.00E/S1-234[»]
4QWXX-ray2.90E/S1-234[»]
4QXJX-ray2.80E/S1-234[»]
4QZ0X-ray3.00E/S1-234[»]
4QZ1X-ray3.00E/S1-234[»]
4QZ2X-ray2.70E/S1-234[»]
4QZ3X-ray2.80E/S1-234[»]
4QZ4X-ray3.00E/S1-234[»]
4QZ5X-ray2.80E/S1-234[»]
4QZ6X-ray2.90E/S1-234[»]
4QZ7X-ray2.80E/S1-234[»]
4QZWX-ray3.00E/S1-234[»]
4QZXX-ray2.60E/S1-234[»]
4QZZX-ray2.90E/S1-234[»]
4R00X-ray2.80E/S1-234[»]
4R02X-ray2.50E/S1-234[»]
4R17X-ray2.10E/S1-234[»]
4R18X-ray2.40E/S1-234[»]
4RURX-ray2.50E/S1-234[»]
4V7OX-ray3.00AK/AW/BF/BT1-234[»]
4X6ZX-ray2.70F/T1-234[»]
4Y69X-ray2.90E/S1-234[»]
4Y6AX-ray2.60E/S1-234[»]
4Y6VX-ray2.80E/S1-234[»]
4Y6ZX-ray2.70E/S1-234[»]
4Y70X-ray2.40E/S1-234[»]
4Y74X-ray2.70E/S1-234[»]
4Y75X-ray2.80E/S1-234[»]
4Y77X-ray2.50E/S1-234[»]
4Y78X-ray2.80E/S1-234[»]
4Y7WX-ray2.50E/S1-234[»]
4Y7XX-ray2.60E/S1-234[»]
4Y7YX-ray2.40E/S1-234[»]
4Y80X-ray2.50E/S1-234[»]
4Y81X-ray2.80E/S1-234[»]
4Y82X-ray2.80E/S1-234[»]
4Y84X-ray2.70E/S1-234[»]
4Y8GX-ray2.60E/S1-234[»]
4Y8HX-ray2.50E/S1-234[»]
4Y8IX-ray2.60E/S1-234[»]
4Y8JX-ray2.70E/S1-234[»]
4Y8KX-ray2.60E/S1-234[»]
4Y8LX-ray2.40E/S1-234[»]
4Y8MX-ray2.80E/S1-234[»]
4Y8NX-ray2.60E/S1-234[»]
4Y8OX-ray2.70E/S1-234[»]
4Y8PX-ray2.80E/S1-234[»]
4Y8QX-ray2.60E/S1-234[»]
4Y8RX-ray2.70E/S1-234[»]
4Y8SX-ray2.70E/S1-234[»]
4Y8TX-ray2.70E/S1-234[»]
4Y8UX-ray2.90E/S1-234[»]
4Y9YX-ray2.80E/S1-234[»]
4Y9ZX-ray2.80E/S1-234[»]
4YA0X-ray2.80E/S1-234[»]
4YA1X-ray2.90E/S1-234[»]
4YA2X-ray2.70E/S1-234[»]
4YA3X-ray2.70E/S1-234[»]
4YA4X-ray2.90E/S1-234[»]
4YA5X-ray2.50E/S1-234[»]
4YA7X-ray2.70E/S1-234[»]
4YA9X-ray2.70E/S1-234[»]
4Z1LX-ray3.00E/S1-234[»]
4ZZGX-ray3.00F/T1-234[»]
5A5Belectron microscopy9.50F1-234[»]
5AHJX-ray2.80E/S1-234[»]
5BOUX-ray2.60E/S1-234[»]
5BXLX-ray2.80E/S1-234[»]
5BXNX-ray2.80E/S1-234[»]
5CGFX-ray2.80E/S1-234[»]
5CGGX-ray2.90E/S1-234[»]
5CGHX-ray2.50E/S1-234[»]
5CGIX-ray2.80E/S1-234[»]
5CZ4X-ray2.30E/S1-234[»]
5CZ5X-ray2.80E/S1-234[»]
5CZ6X-ray2.70E/S1-234[»]
5CZ7X-ray2.50E/S1-234[»]
5CZ8X-ray2.80E/S1-234[»]
5CZ9X-ray2.90E/S1-234[»]
5CZAX-ray2.50E/S1-234[»]
5D0SX-ray2.50E/S1-234[»]
5D0TX-ray2.60E/S1-234[»]
5D0VX-ray2.90E/S1-234[»]
5D0WX-ray2.80E/S1-234[»]
5D0XX-ray2.60E/S1-234[»]
5D0ZX-ray2.90E/S1-234[»]
5DKIX-ray2.80E/S1-234[»]
5DKJX-ray2.80E/S1-234[»]
5FG7X-ray2.70E/S1-234[»]
5FG9X-ray2.60E/S1-234[»]
5FGAX-ray2.70E/S1-234[»]
5FGDX-ray2.80E/S1-234[»]
5FGEX-ray2.60E/S1-234[»]
5FGFX-ray2.60E/S1-234[»]
5FGGX-ray2.70E/S1-234[»]
5FGHX-ray2.80E/S1-234[»]
5FGIX-ray2.90E/S1-234[»]
5FHSX-ray2.70E/S1-234[»]
5JHRX-ray2.90E/S1-234[»]
5JHSX-ray3.00E/S1-234[»]
ProteinModelPortaliP40302.
SMRiP40302.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40302.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074855.
HOGENOMiHOG000091080.
InParanoidiP40302.
KOiK02725.
OMAiEIDSHMG.
OrthoDBiEOG092C47D8.

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
PDB 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[»]
3JCOelectron microscopy4.80F/f1-234[»]
3JCPelectron microscopy4.60F/f1-234[»]
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[»]
4QUXX-ray3.00E/S1-234[»]
4QUYX-ray2.80E/S1-234[»]
4QV0X-ray3.10E/S1-234[»]
4QV1X-ray2.50E/S1-234[»]
4QV3X-ray3.00E/S1-234[»]
4QV4X-ray2.70E/S1-234[»]
4QV5X-ray2.70E/S1-234[»]
4QV6X-ray2.80E/S1-234[»]
4QV7X-ray2.60E/S1-234[»]
4QV8X-ray2.90E/S1-234[»]
4QV9X-ray2.60E/S1-234[»]
4QVLX-ray2.80E/S1-234[»]
4QVMX-ray2.80E/S1-234[»]
4QVNX-ray2.90E/S1-234[»]
4QVPX-ray2.30E/S1-234[»]
4QVQX-ray2.60E/S1-234[»]
4QVVX-ray2.80E/S1-234[»]
4QVWX-ray3.00E/S1-234[»]
4QVYX-ray2.51E/S1-234[»]
4QW0X-ray2.90E/S1-234[»]
4QW1X-ray2.90E/S1-234[»]
4QW3X-ray2.90E/S1-234[»]
4QW4X-ray2.80E/S1-234[»]
4QW5X-ray3.00E/S1-234[»]
4QW6X-ray2.90E/S1-234[»]
4QW7X-ray2.70E/S1-234[»]
4QWFX-ray3.00E/S1-234[»]
4QWGX-ray2.60E/S1-234[»]
4QWIX-ray2.60E/S1-234[»]
4QWJX-ray2.90E/S1-234[»]
4QWKX-ray2.80E/S1-234[»]
4QWLX-ray2.60E/S1-234[»]
4QWRX-ray2.90E/S1-234[»]
4QWSX-ray3.00E/S1-234[»]
4QWUX-ray3.00E/S1-234[»]
4QWXX-ray2.90E/S1-234[»]
4QXJX-ray2.80E/S1-234[»]
4QZ0X-ray3.00E/S1-234[»]
4QZ1X-ray3.00E/S1-234[»]
4QZ2X-ray2.70E/S1-234[»]
4QZ3X-ray2.80E/S1-234[»]
4QZ4X-ray3.00E/S1-234[»]
4QZ5X-ray2.80E/S1-234[»]
4QZ6X-ray2.90E/S1-234[»]
4QZ7X-ray2.80E/S1-234[»]
4QZWX-ray3.00E/S1-234[»]
4QZXX-ray2.60E/S1-234[»]
4QZZX-ray2.90E/S1-234[»]
4R00X-ray2.80E/S1-234[»]
4R02X-ray2.50E/S1-234[»]
4R17X-ray2.10E/S1-234[»]
4R18X-ray2.40E/S1-234[»]
4RURX-ray2.50E/S1-234[»]
4V7OX-ray3.00AK/AW/BF/BT1-234[»]
4X6ZX-ray2.70F/T1-234[»]
4Y69X-ray2.90E/S1-234[»]
4Y6AX-ray2.60E/S1-234[»]
4Y6VX-ray2.80E/S1-234[»]
4Y6ZX-ray2.70E/S1-234[»]
4Y70X-ray2.40E/S1-234[»]
4Y74X-ray2.70E/S1-234[»]
4Y75X-ray2.80E/S1-234[»]
4Y77X-ray2.50E/S1-234[»]
4Y78X-ray2.80E/S1-234[»]
4Y7WX-ray2.50E/S1-234[»]
4Y7XX-ray2.60E/S1-234[»]
4Y7YX-ray2.40E/S1-234[»]
4Y80X-ray2.50E/S1-234[»]
4Y81X-ray2.80E/S1-234[»]
4Y82X-ray2.80E/S1-234[»]
4Y84X-ray2.70E/S1-234[»]
4Y8GX-ray2.60E/S1-234[»]
4Y8HX-ray2.50E/S1-234[»]
4Y8IX-ray2.60E/S1-234[»]
4Y8JX-ray2.70E/S1-234[»]
4Y8KX-ray2.60E/S1-234[»]
4Y8LX-ray2.40E/S1-234[»]
4Y8MX-ray2.80E/S1-234[»]
4Y8NX-ray2.60E/S1-234[»]
4Y8OX-ray2.70E/S1-234[»]
4Y8PX-ray2.80E/S1-234[»]
4Y8QX-ray2.60E/S1-234[»]
4Y8RX-ray2.70E/S1-234[»]
4Y8SX-ray2.70E/S1-234[»]
4Y8TX-ray2.70E/S1-234[»]
4Y8UX-ray2.90E/S1-234[»]
4Y9YX-ray2.80E/S1-234[»]
4Y9ZX-ray2.80E/S1-234[»]
4YA0X-ray2.80E/S1-234[»]
4YA1X-ray2.90E/S1-234[»]
4YA2X-ray2.70E/S1-234[»]
4YA3X-ray2.70E/S1-234[»]
4YA4X-ray2.90E/S1-234[»]
4YA5X-ray2.50E/S1-234[»]
4YA7X-ray2.70E/S1-234[»]
4YA9X-ray2.70E/S1-234[»]
4Z1LX-ray3.00E/S1-234[»]
4ZZGX-ray3.00F/T1-234[»]
5A5Belectron microscopy9.50F1-234[»]
5AHJX-ray2.80E/S1-234[»]
5BOUX-ray2.60E/S1-234[»]
5BXLX-ray2.80E/S1-234[»]
5BXNX-ray2.80E/S1-234[»]
5CGFX-ray2.80E/S1-234[»]
5CGGX-ray2.90E/S1-234[»]
5CGHX-ray2.50E/S1-234[»]
5CGIX-ray2.80E/S1-234[»]
5CZ4X-ray2.30E/S1-234[»]
5CZ5X-ray2.80E/S1-234[»]
5CZ6X-ray2.70E/S1-234[»]
5CZ7X-ray2.50E/S1-234[»]
5CZ8X-ray2.80E/S1-234[»]
5CZ9X-ray2.90E/S1-234[»]
5CZAX-ray2.50E/S1-234[»]
5D0SX-ray2.50E/S1-234[»]
5D0TX-ray2.60E/S1-234[»]
5D0VX-ray2.90E/S1-234[»]
5D0WX-ray2.80E/S1-234[»]
5D0XX-ray2.60E/S1-234[»]
5D0ZX-ray2.90E/S1-234[»]
5DKIX-ray2.80E/S1-234[»]
5DKJX-ray2.80E/S1-234[»]
5FG7X-ray2.70E/S1-234[»]
5FG9X-ray2.60E/S1-234[»]
5FGAX-ray2.70E/S1-234[»]
5FGDX-ray2.80E/S1-234[»]
5FGEX-ray2.60E/S1-234[»]
5FGFX-ray2.60E/S1-234[»]
5FGGX-ray2.70E/S1-234[»]
5FGHX-ray2.80E/S1-234[»]
5FGIX-ray2.90E/S1-234[»]
5FHSX-ray2.70E/S1-234[»]
5JHRX-ray2.90E/S1-234[»]
5JHSX-ray3.00E/S1-234[»]
ProteinModelPortaliP40302.
SMRiP40302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35494. 85 interactors.
DIPiDIP-1528N.
IntActiP40302. 33 interactors.
MINTiMINT-400436.

Protein family/group databases

MEROPSiT01.976.

PTM databases

iPTMnetiP40302.

2D gel databases

UCD-2DPAGEP40302.

Proteomic databases

MaxQBiP40302.
PRIDEiP40302.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YMR314W.
SGDiS000004931. PRE5.

Phylogenomic databases

GeneTreeiENSGT00550000074855.
HOGENOMiHOG000091080.
InParanoidiP40302.
KOiK02725.
OMAiEIDSHMG.
OrthoDBiEOG092C47D8.

Enzyme and pathway databases

BioCyciYEAST:G3O-32978-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

EvolutionaryTraceiP40302.
PROiP40302.

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...

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: November 30, 2016
This is version 178 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

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.