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-3

Gene

PRE9

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 core complex assembly 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-30841-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

MEROPSiT01.973.

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
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR135W.
SGDiS000003367. PRE9.

Subcellular locationi

GO - Cellular componenti

  • 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_00001241161 – 258Proteasome subunit alpha type-3Add BLAST258

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources1 Publication
Cross-linki231Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP23638.
PRIDEiP23638.

PTM databases

iPTMnetiP23638.

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. 336 interactors.
DIPiDIP-2823N.
IntActiP23638. 18 interactors.
MINTiMINT-484272.

Structurei

Secondary structure

1258
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Helixi20 – 29Combined sources10
Beta strandi35 – 40Combined sources6
Beta strandi43 – 49Combined sources7
Beta strandi55 – 57Combined sources3
Helixi59 – 61Combined sources3
Beta strandi64 – 79Combined sources16
Helixi81 – 102Combined sources22
Helixi108 – 124Combined sources17
Beta strandi125 – 127Combined sources3
Beta strandi133 – 141Combined sources9
Turni142 – 144Combined sources3
Beta strandi145 – 151Combined sources7
Beta strandi157 – 166Combined sources10
Helixi169 – 179Combined sources11
Helixi186 – 200Combined sources15
Beta strandi202 – 205Combined sources4
Helixi208 – 210Combined sources3
Beta strandi211 – 217Combined sources7
Beta strandi220 – 224Combined sources5
Beta strandi226 – 229Combined sources4
Helixi232 – 241Combined sources10
Turni242 – 244Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
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[»]
3JCOelectron microscopy4.80C/c1-258[»]
3JCPelectron microscopy4.60C/c1-258[»]
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[»]
3WXRX-ray3.15C/Q1-258[»]
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[»]
4QUXX-ray3.00B/P1-258[»]
4QUYX-ray2.80B/P1-258[»]
4QV0X-ray3.10B/P1-258[»]
4QV1X-ray2.50B/P1-258[»]
4QV3X-ray3.00B/P1-258[»]
4QV4X-ray2.70B/P1-258[»]
4QV5X-ray2.70B/P1-258[»]
4QV6X-ray2.80B/P1-258[»]
4QV7X-ray2.60B/P1-258[»]
4QV8X-ray2.90B/P1-258[»]
4QV9X-ray2.60B/P1-258[»]
4QVLX-ray2.80B/P1-258[»]
4QVMX-ray2.80B/P1-258[»]
4QVNX-ray2.90B/P1-258[»]
4QVPX-ray2.30B/P1-258[»]
4QVQX-ray2.60B/P1-258[»]
4QVVX-ray2.80B/P1-258[»]
4QVWX-ray3.00B/P1-258[»]
4QVYX-ray2.51B/P1-258[»]
4QW0X-ray2.90B/P1-258[»]
4QW1X-ray2.90B/P1-258[»]
4QW3X-ray2.90B/P1-258[»]
4QW4X-ray2.80B/P1-258[»]
4QW5X-ray3.00B/P1-258[»]
4QW6X-ray2.90B/P1-258[»]
4QW7X-ray2.70B/P1-258[»]
4QWFX-ray3.00B/P1-258[»]
4QWGX-ray2.60B/P1-258[»]
4QWIX-ray2.60B/P1-258[»]
4QWJX-ray2.90B/P1-258[»]
4QWKX-ray2.80B/P1-258[»]
4QWLX-ray2.60B/P1-258[»]
4QWRX-ray2.90B/P1-258[»]
4QWSX-ray3.00B/P1-258[»]
4QWUX-ray3.00B/P1-258[»]
4QWXX-ray2.90B/P1-258[»]
4QXJX-ray2.80B/P1-258[»]
4QZ0X-ray3.00B/P1-258[»]
4QZ1X-ray3.00B/P1-258[»]
4QZ2X-ray2.70B/P1-258[»]
4QZ3X-ray2.80B/P1-258[»]
4QZ4X-ray3.00B/P1-258[»]
4QZ5X-ray2.80B/P1-258[»]
4QZ6X-ray2.90B/P1-258[»]
4QZ7X-ray2.80B/P1-258[»]
4QZWX-ray3.00B/P1-258[»]
4QZXX-ray2.60B/P1-258[»]
4QZZX-ray2.90B/P1-258[»]
4R00X-ray2.80B/P1-258[»]
4R02X-ray2.50B/P1-258[»]
4R17X-ray2.10B/P1-258[»]
4R18X-ray2.40B/P1-258[»]
4RURX-ray2.50B/P1-258[»]
4V7OX-ray3.00AH/AT/BC/BQ14-245[»]
4X6ZX-ray2.70C/Q1-258[»]
4Y69X-ray2.90B/P1-258[»]
4Y6AX-ray2.60B/P1-258[»]
4Y6VX-ray2.80B/P1-258[»]
4Y6ZX-ray2.70B/P1-258[»]
4Y70X-ray2.40B/P1-258[»]
4Y74X-ray2.70B/P1-258[»]
4Y75X-ray2.80B/P1-258[»]
4Y77X-ray2.50B/P1-258[»]
4Y78X-ray2.80B/P1-258[»]
4Y7WX-ray2.50B/P1-258[»]
4Y7XX-ray2.60B/P1-258[»]
4Y7YX-ray2.40B/P1-258[»]
4Y80X-ray2.50B/P1-258[»]
4Y81X-ray2.80B/P1-258[»]
4Y82X-ray2.80B/P1-258[»]
4Y84X-ray2.70B/P1-258[»]
4Y8GX-ray2.60B/P1-258[»]
4Y8HX-ray2.50B/P1-258[»]
4Y8IX-ray2.60B/P1-258[»]
4Y8JX-ray2.70B/P1-258[»]
4Y8KX-ray2.60B/P1-258[»]
4Y8LX-ray2.40B/P1-258[»]
4Y8MX-ray2.80B/P1-258[»]
4Y8NX-ray2.60B/P1-258[»]
4Y8OX-ray2.70B/P1-258[»]
4Y8PX-ray2.80B/P1-258[»]
4Y8QX-ray2.60B/P1-258[»]
4Y8RX-ray2.70B/P1-258[»]
4Y8SX-ray2.70B/P1-258[»]
4Y8TX-ray2.70B/P1-258[»]
4Y8UX-ray2.90B/P1-258[»]
4Y9YX-ray2.80B/P1-258[»]
4Y9ZX-ray2.80B/P1-258[»]
4YA0X-ray2.80B/P1-258[»]
4YA1X-ray2.90B/P1-258[»]
4YA2X-ray2.70B/P1-258[»]
4YA3X-ray2.70B/P1-258[»]
4YA4X-ray2.90B/P1-258[»]
4YA5X-ray2.50B/P1-258[»]
4YA7X-ray2.70B/P1-258[»]
4YA9X-ray2.70B/P1-258[»]
4Z1LX-ray3.00B/P1-258[»]
4ZZGX-ray3.00C/Q1-258[»]
5A5Belectron microscopy9.50C1-258[»]
5AHJX-ray2.80B/P1-258[»]
5BOUX-ray2.60B/P1-258[»]
5BXLX-ray2.80B/P1-258[»]
5BXNX-ray2.80B/P1-258[»]
5CGFX-ray2.80B/P1-258[»]
5CGGX-ray2.90B/P1-258[»]
5CGHX-ray2.50B/P1-258[»]
5CGIX-ray2.80B/P1-258[»]
5CZ4X-ray2.30B/P1-258[»]
5CZ5X-ray2.80B/P1-258[»]
5CZ6X-ray2.70B/P1-258[»]
5CZ7X-ray2.50B/P1-258[»]
5CZ8X-ray2.80B/P1-258[»]
5CZ9X-ray2.90B/P1-258[»]
5CZAX-ray2.50B/P1-258[»]
5D0SX-ray2.50B/P1-258[»]
5D0TX-ray2.60B/P1-258[»]
5D0VX-ray2.90B/P1-258[»]
5D0WX-ray2.80B/P1-258[»]
5D0XX-ray2.60B/P1-258[»]
5D0ZX-ray2.90B/P1-258[»]
5DKIX-ray2.80B/P1-258[»]
5DKJX-ray2.80B/P1-258[»]
5FG7X-ray2.70B/P1-258[»]
5FG9X-ray2.60B/P1-258[»]
5FGAX-ray2.70B/P1-258[»]
5FGDX-ray2.80B/P1-258[»]
5FGEX-ray2.60B/P1-258[»]
5FGFX-ray2.60B/P1-258[»]
5FGGX-ray2.70B/P1-258[»]
5FGHX-ray2.80B/P1-258[»]
5FGIX-ray2.90B/P1-258[»]
5FHSX-ray2.70B/P1-258[»]
5JHRX-ray2.90B/P1-258[»]
5JHSX-ray3.00B/P1-258[»]
ProteinModelPortaliP23638.
SMRiP23638.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23638.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074827.
HOGENOMiHOG000091085.
InParanoidiP23638.
KOiK02728.
OMAiCNEKQRY.
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.

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.
PIRiS12940. SNBYY3.
RefSeqiNP_011651.3. NM_001181264.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
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[»]
3JCOelectron microscopy4.80C/c1-258[»]
3JCPelectron microscopy4.60C/c1-258[»]
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[»]
3WXRX-ray3.15C/Q1-258[»]
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[»]
4QUXX-ray3.00B/P1-258[»]
4QUYX-ray2.80B/P1-258[»]
4QV0X-ray3.10B/P1-258[»]
4QV1X-ray2.50B/P1-258[»]
4QV3X-ray3.00B/P1-258[»]
4QV4X-ray2.70B/P1-258[»]
4QV5X-ray2.70B/P1-258[»]
4QV6X-ray2.80B/P1-258[»]
4QV7X-ray2.60B/P1-258[»]
4QV8X-ray2.90B/P1-258[»]
4QV9X-ray2.60B/P1-258[»]
4QVLX-ray2.80B/P1-258[»]
4QVMX-ray2.80B/P1-258[»]
4QVNX-ray2.90B/P1-258[»]
4QVPX-ray2.30B/P1-258[»]
4QVQX-ray2.60B/P1-258[»]
4QVVX-ray2.80B/P1-258[»]
4QVWX-ray3.00B/P1-258[»]
4QVYX-ray2.51B/P1-258[»]
4QW0X-ray2.90B/P1-258[»]
4QW1X-ray2.90B/P1-258[»]
4QW3X-ray2.90B/P1-258[»]
4QW4X-ray2.80B/P1-258[»]
4QW5X-ray3.00B/P1-258[»]
4QW6X-ray2.90B/P1-258[»]
4QW7X-ray2.70B/P1-258[»]
4QWFX-ray3.00B/P1-258[»]
4QWGX-ray2.60B/P1-258[»]
4QWIX-ray2.60B/P1-258[»]
4QWJX-ray2.90B/P1-258[»]
4QWKX-ray2.80B/P1-258[»]
4QWLX-ray2.60B/P1-258[»]
4QWRX-ray2.90B/P1-258[»]
4QWSX-ray3.00B/P1-258[»]
4QWUX-ray3.00B/P1-258[»]
4QWXX-ray2.90B/P1-258[»]
4QXJX-ray2.80B/P1-258[»]
4QZ0X-ray3.00B/P1-258[»]
4QZ1X-ray3.00B/P1-258[»]
4QZ2X-ray2.70B/P1-258[»]
4QZ3X-ray2.80B/P1-258[»]
4QZ4X-ray3.00B/P1-258[»]
4QZ5X-ray2.80B/P1-258[»]
4QZ6X-ray2.90B/P1-258[»]
4QZ7X-ray2.80B/P1-258[»]
4QZWX-ray3.00B/P1-258[»]
4QZXX-ray2.60B/P1-258[»]
4QZZX-ray2.90B/P1-258[»]
4R00X-ray2.80B/P1-258[»]
4R02X-ray2.50B/P1-258[»]
4R17X-ray2.10B/P1-258[»]
4R18X-ray2.40B/P1-258[»]
4RURX-ray2.50B/P1-258[»]
4V7OX-ray3.00AH/AT/BC/BQ14-245[»]
4X6ZX-ray2.70C/Q1-258[»]
4Y69X-ray2.90B/P1-258[»]
4Y6AX-ray2.60B/P1-258[»]
4Y6VX-ray2.80B/P1-258[»]
4Y6ZX-ray2.70B/P1-258[»]
4Y70X-ray2.40B/P1-258[»]
4Y74X-ray2.70B/P1-258[»]
4Y75X-ray2.80B/P1-258[»]
4Y77X-ray2.50B/P1-258[»]
4Y78X-ray2.80B/P1-258[»]
4Y7WX-ray2.50B/P1-258[»]
4Y7XX-ray2.60B/P1-258[»]
4Y7YX-ray2.40B/P1-258[»]
4Y80X-ray2.50B/P1-258[»]
4Y81X-ray2.80B/P1-258[»]
4Y82X-ray2.80B/P1-258[»]
4Y84X-ray2.70B/P1-258[»]
4Y8GX-ray2.60B/P1-258[»]
4Y8HX-ray2.50B/P1-258[»]
4Y8IX-ray2.60B/P1-258[»]
4Y8JX-ray2.70B/P1-258[»]
4Y8KX-ray2.60B/P1-258[»]
4Y8LX-ray2.40B/P1-258[»]
4Y8MX-ray2.80B/P1-258[»]
4Y8NX-ray2.60B/P1-258[»]
4Y8OX-ray2.70B/P1-258[»]
4Y8PX-ray2.80B/P1-258[»]
4Y8QX-ray2.60B/P1-258[»]
4Y8RX-ray2.70B/P1-258[»]
4Y8SX-ray2.70B/P1-258[»]
4Y8TX-ray2.70B/P1-258[»]
4Y8UX-ray2.90B/P1-258[»]
4Y9YX-ray2.80B/P1-258[»]
4Y9ZX-ray2.80B/P1-258[»]
4YA0X-ray2.80B/P1-258[»]
4YA1X-ray2.90B/P1-258[»]
4YA2X-ray2.70B/P1-258[»]
4YA3X-ray2.70B/P1-258[»]
4YA4X-ray2.90B/P1-258[»]
4YA5X-ray2.50B/P1-258[»]
4YA7X-ray2.70B/P1-258[»]
4YA9X-ray2.70B/P1-258[»]
4Z1LX-ray3.00B/P1-258[»]
4ZZGX-ray3.00C/Q1-258[»]
5A5Belectron microscopy9.50C1-258[»]
5AHJX-ray2.80B/P1-258[»]
5BOUX-ray2.60B/P1-258[»]
5BXLX-ray2.80B/P1-258[»]
5BXNX-ray2.80B/P1-258[»]
5CGFX-ray2.80B/P1-258[»]
5CGGX-ray2.90B/P1-258[»]
5CGHX-ray2.50B/P1-258[»]
5CGIX-ray2.80B/P1-258[»]
5CZ4X-ray2.30B/P1-258[»]
5CZ5X-ray2.80B/P1-258[»]
5CZ6X-ray2.70B/P1-258[»]
5CZ7X-ray2.50B/P1-258[»]
5CZ8X-ray2.80B/P1-258[»]
5CZ9X-ray2.90B/P1-258[»]
5CZAX-ray2.50B/P1-258[»]
5D0SX-ray2.50B/P1-258[»]
5D0TX-ray2.60B/P1-258[»]
5D0VX-ray2.90B/P1-258[»]
5D0WX-ray2.80B/P1-258[»]
5D0XX-ray2.60B/P1-258[»]
5D0ZX-ray2.90B/P1-258[»]
5DKIX-ray2.80B/P1-258[»]
5DKJX-ray2.80B/P1-258[»]
5FG7X-ray2.70B/P1-258[»]
5FG9X-ray2.60B/P1-258[»]
5FGAX-ray2.70B/P1-258[»]
5FGDX-ray2.80B/P1-258[»]
5FGEX-ray2.60B/P1-258[»]
5FGFX-ray2.60B/P1-258[»]
5FGGX-ray2.70B/P1-258[»]
5FGHX-ray2.80B/P1-258[»]
5FGIX-ray2.90B/P1-258[»]
5FHSX-ray2.70B/P1-258[»]
5JHRX-ray2.90B/P1-258[»]
5JHSX-ray3.00B/P1-258[»]
ProteinModelPortaliP23638.
SMRiP23638.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33383. 336 interactors.
DIPiDIP-2823N.
IntActiP23638. 18 interactors.
MINTiMINT-484272.

Protein family/group databases

MEROPSiT01.973.

PTM databases

iPTMnetiP23638.

Proteomic databases

MaxQBiP23638.
PRIDEiP23638.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YGR135W.
SGDiS000003367. PRE9.

Phylogenomic databases

GeneTreeiENSGT00550000074827.
HOGENOMiHOG000091085.
InParanoidiP23638.
KOiK02728.
OMAiCNEKQRY.
OrthoDBiEOG092C47D8.

Enzyme and pathway databases

BioCyciYEAST:G3O-30841-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

EvolutionaryTraceiP23638.
PROiP23638.

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 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 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 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

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.