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Protein

Proteasome subunit beta type-7

Gene

PRE4

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. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.1 Publication

GO - Molecular functioni

GO - Biological processi

  • proteasomal ubiquitin-independent protein catabolic process Source: SGD
  • proteasome 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-30496-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

MEROPSiT01.987.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-7 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PRE4
Multicatalytic endopeptidase complex subunit PRE4
Proteasome component PRE4
Proteinase YSCE subunit PRE4
Gene namesi
Name:PRE4
Ordered Locus Names:YFR050C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFR050C.
SGDiS000001946. PRE4.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: SGD
  • nucleus Source: SGD
  • proteasome core complex, beta-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
PropeptideiPRO_00003314901 – 33Add BLAST33
ChainiPRO_000014807334 – 266Proteasome subunit beta type-7Add BLAST233

Proteomic databases

MaxQBiP30657.
PRIDEiP30657.

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 CIC1.3 Publications

Protein-protein interaction databases

BioGridi31208. 76 interactors.
DIPiDIP-2807N.
IntActiP30657. 20 interactors.
MINTiMINT-592513.

Structurei

Secondary structure

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 41Combined sources3
Beta strandi44 – 49Combined sources6
Beta strandi52 – 58Combined sources7
Beta strandi61 – 63Combined sources3
Beta strandi66 – 70Combined sources5
Beta strandi75 – 78Combined sources4
Turni79 – 81Combined sources3
Beta strandi82 – 89Combined sources8
Helixi90 – 108Combined sources19
Turni112 – 118Combined sources7
Helixi122 – 138Combined sources17
Beta strandi145 – 152Combined sources8
Beta strandi158 – 164Combined sources7
Beta strandi169 – 171Combined sources3
Beta strandi173 – 176Combined sources4
Helixi179 – 188Combined sources10
Turni189 – 191Combined sources3
Beta strandi192 – 194Combined sources3
Helixi195 – 200Combined sources6
Helixi203 – 220Combined sources18
Beta strandi226 – 234Combined sources9
Turni235 – 237Combined sources3
Beta strandi238 – 246Combined sources9
Helixi253 – 257Combined sources5
Beta strandi260 – 263Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20N/b34-265[»]
1G0UX-ray2.401/M1-266[»]
1G65X-ray2.251/M34-266[»]
1JD2X-ray3.00M/T34-266[»]
1RYPX-ray1.902/N34-266[»]
1Z7QX-ray3.22N/b34-266[»]
2F16X-ray2.801/M34-266[»]
2FAKX-ray2.801/M34-266[»]
2GPLX-ray2.811/M34-266[»]
2ZCYX-ray2.900/M1-266[»]
3BDMX-ray2.700/M1-266[»]
3D29X-ray2.601/M34-266[»]
3DY3X-ray2.811/M34-266[»]
3DY4X-ray2.801/M34-266[»]
3E47X-ray3.001/M34-266[»]
3GPJX-ray2.701/M34-266[»]
3GPTX-ray2.411/M34-266[»]
3GPWX-ray2.501/M34-266[»]
3HYEX-ray2.501/M34-266[»]
3JCOelectron microscopy4.802/91-266[»]
3JCPelectron microscopy4.602/91-266[»]
3MG0X-ray2.681/M34-266[»]
3MG4X-ray3.111/M34-266[»]
3MG6X-ray2.601/M1-266[»]
3MG7X-ray2.781/M1-266[»]
3MG8X-ray2.591/M1-266[»]
3NZJX-ray2.401/M1-266[»]
3NZWX-ray2.501/M1-266[»]
3NZXX-ray2.701/M1-266[»]
3OEUX-ray2.601/M34-266[»]
3OEVX-ray2.851/M34-266[»]
3OKJX-ray2.701/M34-266[»]
3SDIX-ray2.651/M34-253[»]
3SDKX-ray2.701/M34-266[»]
3SHJX-ray2.801/M34-266[»]
3TDDX-ray2.701/M34-266[»]
3UN4X-ray3.40M/a34-266[»]
3UN8X-ray2.70M/a34-266[»]
3WXRX-ray3.152/N1-266[»]
4CR2electron microscopy7.7071-266[»]
4CR3electron microscopy9.3071-266[»]
4CR4electron microscopy8.8071-266[»]
4EU2X-ray2.512/N34-266[»]
4FZCX-ray2.80M/a34-266[»]
4FZGX-ray3.00M/a34-266[»]
4G4SX-ray2.49N34-266[»]
4GK7X-ray2.80M/a34-266[»]
4HNPX-ray2.80M/a34-266[»]
4HRCX-ray2.80M/a34-266[»]
4HRDX-ray2.80M/a34-266[»]
4INRX-ray2.70M/a34-266[»]
4INTX-ray2.90M/a34-266[»]
4INUX-ray3.10M/a34-266[»]
4J70X-ray2.80M/a34-266[»]
4JSQX-ray2.80M/a34-266[»]
4JSUX-ray2.90M/a34-266[»]
4JT0X-ray3.10M/a34-266[»]
4LQIX-ray2.70M/a34-266[»]
4LTCX-ray2.50M/a34-266[»]
4NNNX-ray2.50M/a21-266[»]
4NNWX-ray2.60M/a21-266[»]
4NO1X-ray2.50M/a21-266[»]
4NO6X-ray3.00M/a21-266[»]
4NO8X-ray2.70M/a21-266[»]
4NO9X-ray2.90M/a21-266[»]
4Q1SX-ray2.60M/a21-266[»]
4QBYX-ray3.00M/a21-266[»]
4QLQX-ray2.40M/a21-266[»]
4QLSX-ray2.80M/a21-266[»]
4QLTX-ray2.80M/a21-266[»]
4QLUX-ray2.80M/a21-266[»]
4QLVX-ray2.90M/a21-266[»]
4QUXX-ray3.00M/a21-266[»]
4QUYX-ray2.80M/a21-266[»]
4QV0X-ray3.10M/a21-266[»]
4QV1X-ray2.50M/a21-266[»]
4QV3X-ray3.00M/a21-266[»]
4QV4X-ray2.70M/a21-266[»]
4QV5X-ray2.70M/a21-266[»]
4QV6X-ray2.80M/a21-266[»]
4QV7X-ray2.60M/a21-266[»]
4QV8X-ray2.90M/a21-266[»]
4QV9X-ray2.60M/a21-266[»]
4QVLX-ray2.80M/a21-266[»]
4QVMX-ray2.80M/a21-266[»]
4QVNX-ray2.90M/a21-266[»]
4QVPX-ray2.30M/a21-266[»]
4QVQX-ray2.60M/a21-266[»]
4QVVX-ray2.80M/a21-266[»]
4QVWX-ray3.00M/a21-266[»]
4QVYX-ray2.51M/a21-266[»]
4QW0X-ray2.90M/a21-266[»]
4QW1X-ray2.90M/a21-266[»]
4QW3X-ray2.90M/a21-266[»]
4QW4X-ray2.80M/a21-266[»]
4QW5X-ray3.00M/a21-266[»]
4QW6X-ray2.90M/a21-266[»]
4QW7X-ray2.70M/a21-266[»]
4QWFX-ray3.00M/a21-266[»]
4QWGX-ray2.60M/a21-266[»]
4QWIX-ray2.60M/a21-266[»]
4QWJX-ray2.90M/a21-266[»]
4QWKX-ray2.80M/a21-266[»]
4QWLX-ray2.60M/a21-266[»]
4QWRX-ray2.90M/a21-266[»]
4QWSX-ray3.00M/a21-266[»]
4QWUX-ray3.00M/a21-266[»]
4QWXX-ray2.90M/a21-266[»]
4QXJX-ray2.80M/a21-266[»]
4QZ0X-ray3.00M/a21-266[»]
4QZ1X-ray3.00M/a21-266[»]
4QZ2X-ray2.70M/a21-266[»]
4QZ3X-ray2.80M/a21-266[»]
4QZ4X-ray3.00M/a21-266[»]
4QZ5X-ray2.80M/a21-266[»]
4QZ6X-ray2.90M/a21-266[»]
4QZ7X-ray2.80M/a21-266[»]
4QZWX-ray3.00M/a21-266[»]
4QZXX-ray2.60M/a21-266[»]
4QZZX-ray2.90M/a21-266[»]
4R00X-ray2.80M/a21-266[»]
4R02X-ray2.50M/a21-266[»]
4R17X-ray2.10M/a21-266[»]
4R18X-ray2.40M/a21-266[»]
4RURX-ray2.50M/a21-266[»]
4V7OX-ray3.00A4/AR/B2/BN34-266[»]
4X6ZX-ray2.702/N1-266[»]
4Y69X-ray2.90M/a21-266[»]
4Y6AX-ray2.60M/a21-266[»]
4Y6VX-ray2.80M/a21-266[»]
4Y6ZX-ray2.70M/a21-266[»]
4Y70X-ray2.40M/a21-266[»]
4Y74X-ray2.70M/a21-266[»]
4Y75X-ray2.80M/a21-266[»]
4Y77X-ray2.50M/a21-266[»]
4Y78X-ray2.80M/a21-266[»]
4Y7WX-ray2.50M/a21-266[»]
4Y7XX-ray2.60M/a21-266[»]
4Y7YX-ray2.40M/a21-266[»]
4Y80X-ray2.50M/a21-266[»]
4Y81X-ray2.80M/a21-266[»]
4Y82X-ray2.80M/a21-266[»]
4Y84X-ray2.70M/a21-266[»]
4Y8GX-ray2.60M/a21-266[»]
4Y8HX-ray2.50M/a21-266[»]
4Y8IX-ray2.60M/a21-266[»]
4Y8JX-ray2.70M/a21-266[»]
4Y8KX-ray2.60M/a21-266[»]
4Y8LX-ray2.40M/a21-266[»]
4Y8MX-ray2.80M/a21-259[»]
4Y8NX-ray2.60M/a21-259[»]
4Y8OX-ray2.70M/a21-259[»]
4Y8PX-ray2.80M/a21-259[»]
4Y8QX-ray2.60M/a21-259[»]
4Y8RX-ray2.70M/a21-266[»]
4Y8SX-ray2.70M/a21-266[»]
4Y8TX-ray2.70M/a21-266[»]
4Y8UX-ray2.90M/a21-266[»]
4Y9YX-ray2.80M/a21-266[»]
4Y9ZX-ray2.80M/a21-266[»]
4YA0X-ray2.80M/a21-266[»]
4YA1X-ray2.90M/a21-266[»]
4YA2X-ray2.70M/a21-266[»]
4YA3X-ray2.70M/a21-266[»]
4YA4X-ray2.90M/a21-266[»]
4YA5X-ray2.50M/a21-266[»]
4YA7X-ray2.70M/a21-266[»]
4YA9X-ray2.70M/a21-266[»]
4Z1LX-ray3.00M/a21-266[»]
4ZZGX-ray3.002/N1-266[»]
5A5Belectron microscopy9.5071-266[»]
5AHJX-ray2.80M/a34-266[»]
5BOUX-ray2.60M/a21-266[»]
5BXLX-ray2.80M/a21-266[»]
5BXNX-ray2.80M/a21-266[»]
5CGFX-ray2.80M/a21-266[»]
5CGGX-ray2.90M/a21-266[»]
5CGHX-ray2.50M/a21-266[»]
5CGIX-ray2.80M/a21-266[»]
5CZ4X-ray2.30M/a21-266[»]
5CZ5X-ray2.80M/a21-266[»]
5CZ6X-ray2.70M/a21-266[»]
5CZ7X-ray2.50M/a21-266[»]
5CZ8X-ray2.80M/a21-266[»]
5CZ9X-ray2.90M/a21-266[»]
5CZAX-ray2.50M/a21-266[»]
5D0SX-ray2.50M/a21-266[»]
5D0TX-ray2.60M/a21-266[»]
5D0VX-ray2.90M/a21-266[»]
5D0WX-ray2.80M/a21-266[»]
5D0XX-ray2.60M/a21-266[»]
5D0ZX-ray2.90M/a21-266[»]
5DKIX-ray2.80M/a21-266[»]
5DKJX-ray2.80M/a21-266[»]
5FG7X-ray2.70M/a21-266[»]
5FG9X-ray2.60M/a21-266[»]
5FGAX-ray2.70M/a21-266[»]
5FGDX-ray2.80M/a21-266[»]
5FGEX-ray2.60M/a21-266[»]
5FGFX-ray2.60M/a21-266[»]
5FGGX-ray2.70M/a21-266[»]
5FGHX-ray2.80M/a21-266[»]
5FGIX-ray2.90M/a21-266[»]
5FHSX-ray2.70M/a21-266[»]
5JHRX-ray2.90M/a21-266[»]
5JHSX-ray3.00M/a21-266[»]
ProteinModelPortaliP30657.
SMRiP30657.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30657.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000000698.
HOGENOMiHOG000181719.
InParanoidiP30657.
KOiK02736.
OMAiTQIANAG.
OrthoDBiEOG092C410Y.

Family and domain databases

CDDicd03760. proteasome_beta_type_4. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30657-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNHDPFSWGR PADSTYGAYN TQIANAGASP MVNTQQPIVT GTSVISMKYD
60 70 80 90 100
NGVIIAADNL GSYGSLLRFN GVERLIPVGD NTVVGISGDI SDMQHIERLL
110 120 130 140 150
KDLVTENAYD NPLADAEEAL EPSYIFEYLA TVMYQRRSKM NPLWNAIIVA
160 170 180 190 200
GVQSNGDQFL RYVNLLGVTY SSPTLATGFG AHMANPLLRK VVDRESDIPK
210 220 230 240 250
TTVQVAEEAI VNAMRVLYYR DARSSRNFSL AIIDKNTGLT FKKNLQVENM
260
KWDFAKDIKG YGTQKI
Length:266
Mass (Da):29,443
Last modified:April 1, 1993 - v1
Checksum:iE585BB3B5D0C8E2C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti188L → V in AAT92966 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68663 Genomic DNA. Translation: CAA48629.1.
D50617 Genomic DNA. Translation: BAA09289.1.
AY692947 Genomic DNA. Translation: AAT92966.1.
BK006940 Genomic DNA. Translation: DAA12493.1.
PIRiA46610.
RefSeqiNP_116708.1. NM_001180015.1.

Genome annotation databases

EnsemblFungiiBAA09289; BAA09289; BAA09289.
YFR050C; YFR050C; YFR050C.
GeneIDi850611.
KEGGisce:YFR050C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68663 Genomic DNA. Translation: CAA48629.1.
D50617 Genomic DNA. Translation: BAA09289.1.
AY692947 Genomic DNA. Translation: AAT92966.1.
BK006940 Genomic DNA. Translation: DAA12493.1.
PIRiA46610.
RefSeqiNP_116708.1. NM_001180015.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20N/b34-265[»]
1G0UX-ray2.401/M1-266[»]
1G65X-ray2.251/M34-266[»]
1JD2X-ray3.00M/T34-266[»]
1RYPX-ray1.902/N34-266[»]
1Z7QX-ray3.22N/b34-266[»]
2F16X-ray2.801/M34-266[»]
2FAKX-ray2.801/M34-266[»]
2GPLX-ray2.811/M34-266[»]
2ZCYX-ray2.900/M1-266[»]
3BDMX-ray2.700/M1-266[»]
3D29X-ray2.601/M34-266[»]
3DY3X-ray2.811/M34-266[»]
3DY4X-ray2.801/M34-266[»]
3E47X-ray3.001/M34-266[»]
3GPJX-ray2.701/M34-266[»]
3GPTX-ray2.411/M34-266[»]
3GPWX-ray2.501/M34-266[»]
3HYEX-ray2.501/M34-266[»]
3JCOelectron microscopy4.802/91-266[»]
3JCPelectron microscopy4.602/91-266[»]
3MG0X-ray2.681/M34-266[»]
3MG4X-ray3.111/M34-266[»]
3MG6X-ray2.601/M1-266[»]
3MG7X-ray2.781/M1-266[»]
3MG8X-ray2.591/M1-266[»]
3NZJX-ray2.401/M1-266[»]
3NZWX-ray2.501/M1-266[»]
3NZXX-ray2.701/M1-266[»]
3OEUX-ray2.601/M34-266[»]
3OEVX-ray2.851/M34-266[»]
3OKJX-ray2.701/M34-266[»]
3SDIX-ray2.651/M34-253[»]
3SDKX-ray2.701/M34-266[»]
3SHJX-ray2.801/M34-266[»]
3TDDX-ray2.701/M34-266[»]
3UN4X-ray3.40M/a34-266[»]
3UN8X-ray2.70M/a34-266[»]
3WXRX-ray3.152/N1-266[»]
4CR2electron microscopy7.7071-266[»]
4CR3electron microscopy9.3071-266[»]
4CR4electron microscopy8.8071-266[»]
4EU2X-ray2.512/N34-266[»]
4FZCX-ray2.80M/a34-266[»]
4FZGX-ray3.00M/a34-266[»]
4G4SX-ray2.49N34-266[»]
4GK7X-ray2.80M/a34-266[»]
4HNPX-ray2.80M/a34-266[»]
4HRCX-ray2.80M/a34-266[»]
4HRDX-ray2.80M/a34-266[»]
4INRX-ray2.70M/a34-266[»]
4INTX-ray2.90M/a34-266[»]
4INUX-ray3.10M/a34-266[»]
4J70X-ray2.80M/a34-266[»]
4JSQX-ray2.80M/a34-266[»]
4JSUX-ray2.90M/a34-266[»]
4JT0X-ray3.10M/a34-266[»]
4LQIX-ray2.70M/a34-266[»]
4LTCX-ray2.50M/a34-266[»]
4NNNX-ray2.50M/a21-266[»]
4NNWX-ray2.60M/a21-266[»]
4NO1X-ray2.50M/a21-266[»]
4NO6X-ray3.00M/a21-266[»]
4NO8X-ray2.70M/a21-266[»]
4NO9X-ray2.90M/a21-266[»]
4Q1SX-ray2.60M/a21-266[»]
4QBYX-ray3.00M/a21-266[»]
4QLQX-ray2.40M/a21-266[»]
4QLSX-ray2.80M/a21-266[»]
4QLTX-ray2.80M/a21-266[»]
4QLUX-ray2.80M/a21-266[»]
4QLVX-ray2.90M/a21-266[»]
4QUXX-ray3.00M/a21-266[»]
4QUYX-ray2.80M/a21-266[»]
4QV0X-ray3.10M/a21-266[»]
4QV1X-ray2.50M/a21-266[»]
4QV3X-ray3.00M/a21-266[»]
4QV4X-ray2.70M/a21-266[»]
4QV5X-ray2.70M/a21-266[»]
4QV6X-ray2.80M/a21-266[»]
4QV7X-ray2.60M/a21-266[»]
4QV8X-ray2.90M/a21-266[»]
4QV9X-ray2.60M/a21-266[»]
4QVLX-ray2.80M/a21-266[»]
4QVMX-ray2.80M/a21-266[»]
4QVNX-ray2.90M/a21-266[»]
4QVPX-ray2.30M/a21-266[»]
4QVQX-ray2.60M/a21-266[»]
4QVVX-ray2.80M/a21-266[»]
4QVWX-ray3.00M/a21-266[»]
4QVYX-ray2.51M/a21-266[»]
4QW0X-ray2.90M/a21-266[»]
4QW1X-ray2.90M/a21-266[»]
4QW3X-ray2.90M/a21-266[»]
4QW4X-ray2.80M/a21-266[»]
4QW5X-ray3.00M/a21-266[»]
4QW6X-ray2.90M/a21-266[»]
4QW7X-ray2.70M/a21-266[»]
4QWFX-ray3.00M/a21-266[»]
4QWGX-ray2.60M/a21-266[»]
4QWIX-ray2.60M/a21-266[»]
4QWJX-ray2.90M/a21-266[»]
4QWKX-ray2.80M/a21-266[»]
4QWLX-ray2.60M/a21-266[»]
4QWRX-ray2.90M/a21-266[»]
4QWSX-ray3.00M/a21-266[»]
4QWUX-ray3.00M/a21-266[»]
4QWXX-ray2.90M/a21-266[»]
4QXJX-ray2.80M/a21-266[»]
4QZ0X-ray3.00M/a21-266[»]
4QZ1X-ray3.00M/a21-266[»]
4QZ2X-ray2.70M/a21-266[»]
4QZ3X-ray2.80M/a21-266[»]
4QZ4X-ray3.00M/a21-266[»]
4QZ5X-ray2.80M/a21-266[»]
4QZ6X-ray2.90M/a21-266[»]
4QZ7X-ray2.80M/a21-266[»]
4QZWX-ray3.00M/a21-266[»]
4QZXX-ray2.60M/a21-266[»]
4QZZX-ray2.90M/a21-266[»]
4R00X-ray2.80M/a21-266[»]
4R02X-ray2.50M/a21-266[»]
4R17X-ray2.10M/a21-266[»]
4R18X-ray2.40M/a21-266[»]
4RURX-ray2.50M/a21-266[»]
4V7OX-ray3.00A4/AR/B2/BN34-266[»]
4X6ZX-ray2.702/N1-266[»]
4Y69X-ray2.90M/a21-266[»]
4Y6AX-ray2.60M/a21-266[»]
4Y6VX-ray2.80M/a21-266[»]
4Y6ZX-ray2.70M/a21-266[»]
4Y70X-ray2.40M/a21-266[»]
4Y74X-ray2.70M/a21-266[»]
4Y75X-ray2.80M/a21-266[»]
4Y77X-ray2.50M/a21-266[»]
4Y78X-ray2.80M/a21-266[»]
4Y7WX-ray2.50M/a21-266[»]
4Y7XX-ray2.60M/a21-266[»]
4Y7YX-ray2.40M/a21-266[»]
4Y80X-ray2.50M/a21-266[»]
4Y81X-ray2.80M/a21-266[»]
4Y82X-ray2.80M/a21-266[»]
4Y84X-ray2.70M/a21-266[»]
4Y8GX-ray2.60M/a21-266[»]
4Y8HX-ray2.50M/a21-266[»]
4Y8IX-ray2.60M/a21-266[»]
4Y8JX-ray2.70M/a21-266[»]
4Y8KX-ray2.60M/a21-266[»]
4Y8LX-ray2.40M/a21-266[»]
4Y8MX-ray2.80M/a21-259[»]
4Y8NX-ray2.60M/a21-259[»]
4Y8OX-ray2.70M/a21-259[»]
4Y8PX-ray2.80M/a21-259[»]
4Y8QX-ray2.60M/a21-259[»]
4Y8RX-ray2.70M/a21-266[»]
4Y8SX-ray2.70M/a21-266[»]
4Y8TX-ray2.70M/a21-266[»]
4Y8UX-ray2.90M/a21-266[»]
4Y9YX-ray2.80M/a21-266[»]
4Y9ZX-ray2.80M/a21-266[»]
4YA0X-ray2.80M/a21-266[»]
4YA1X-ray2.90M/a21-266[»]
4YA2X-ray2.70M/a21-266[»]
4YA3X-ray2.70M/a21-266[»]
4YA4X-ray2.90M/a21-266[»]
4YA5X-ray2.50M/a21-266[»]
4YA7X-ray2.70M/a21-266[»]
4YA9X-ray2.70M/a21-266[»]
4Z1LX-ray3.00M/a21-266[»]
4ZZGX-ray3.002/N1-266[»]
5A5Belectron microscopy9.5071-266[»]
5AHJX-ray2.80M/a34-266[»]
5BOUX-ray2.60M/a21-266[»]
5BXLX-ray2.80M/a21-266[»]
5BXNX-ray2.80M/a21-266[»]
5CGFX-ray2.80M/a21-266[»]
5CGGX-ray2.90M/a21-266[»]
5CGHX-ray2.50M/a21-266[»]
5CGIX-ray2.80M/a21-266[»]
5CZ4X-ray2.30M/a21-266[»]
5CZ5X-ray2.80M/a21-266[»]
5CZ6X-ray2.70M/a21-266[»]
5CZ7X-ray2.50M/a21-266[»]
5CZ8X-ray2.80M/a21-266[»]
5CZ9X-ray2.90M/a21-266[»]
5CZAX-ray2.50M/a21-266[»]
5D0SX-ray2.50M/a21-266[»]
5D0TX-ray2.60M/a21-266[»]
5D0VX-ray2.90M/a21-266[»]
5D0WX-ray2.80M/a21-266[»]
5D0XX-ray2.60M/a21-266[»]
5D0ZX-ray2.90M/a21-266[»]
5DKIX-ray2.80M/a21-266[»]
5DKJX-ray2.80M/a21-266[»]
5FG7X-ray2.70M/a21-266[»]
5FG9X-ray2.60M/a21-266[»]
5FGAX-ray2.70M/a21-266[»]
5FGDX-ray2.80M/a21-266[»]
5FGEX-ray2.60M/a21-266[»]
5FGFX-ray2.60M/a21-266[»]
5FGGX-ray2.70M/a21-266[»]
5FGHX-ray2.80M/a21-266[»]
5FGIX-ray2.90M/a21-266[»]
5FHSX-ray2.70M/a21-266[»]
5JHRX-ray2.90M/a21-266[»]
5JHSX-ray3.00M/a21-266[»]
ProteinModelPortaliP30657.
SMRiP30657.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31208. 76 interactors.
DIPiDIP-2807N.
IntActiP30657. 20 interactors.
MINTiMINT-592513.

Protein family/group databases

MEROPSiT01.987.

Proteomic databases

MaxQBiP30657.
PRIDEiP30657.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09289; BAA09289; BAA09289.
YFR050C; YFR050C; YFR050C.
GeneIDi850611.
KEGGisce:YFR050C.

Organism-specific databases

EuPathDBiFungiDB:YFR050C.
SGDiS000001946. PRE4.

Phylogenomic databases

GeneTreeiENSGT00390000000698.
HOGENOMiHOG000181719.
InParanoidiP30657.
KOiK02736.
OMAiTQIANAG.
OrthoDBiEOG092C410Y.

Enzyme and pathway databases

BioCyciYEAST:G3O-30496-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

EvolutionaryTraceiP30657.
PROiP30657.

Family and domain databases

CDDicd03760. proteasome_beta_type_4. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPSB7_YEAST
AccessioniPrimary (citable) accession number: P30657
Secondary accession number(s): D6VTT3, E9P8Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
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 16900 molecules/cell in log phase SD medium.1 Publication

Caution

It is uncertain whether Met-1 or Met-31 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, 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 VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: 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.