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 beta type-4

Gene

PRE1

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. This subunit has a chymotrypsin-like activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  • endopeptidase activator activity Source: SGD
  • threonine-type endopeptidase activity Source: UniProtKB-KW

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-30199-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

MEROPSiT01.984.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-4 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C11
Multicatalytic endopeptidase complex subunit C11
Proteasome component C11
Proteinase YSCE subunit 11
Gene namesi
Name:PRE1
Ordered Locus Names:YER012W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER012W.
SGDiS000000814. PRE1.

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001480551 – 198Proteasome subunit beta type-4Add BLAST198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei76PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP22141.
PRIDEiP22141.

PTM databases

iPTMnetiP22141.

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
PRE10P212423EBI-13988,EBI-13963
PRE6P403033EBI-13988,EBI-13980
RPT1P332992EBI-13988,EBI-13910

Protein-protein interaction databases

BioGridi36744. 142 interactors.
DIPiDIP-2808N.
IntActiP22141. 27 interactors.
MINTiMINT-592869.

Chemistry databases

BindingDBiP22141.

Structurei

Secondary structure

1198
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Beta strandi13 – 18Combined sources6
Beta strandi21 – 23Combined sources3
Beta strandi26 – 30Combined sources5
Beta strandi35 – 39Combined sources5
Beta strandi42 – 49Combined sources8
Helixi50 – 71Combined sources22
Helixi77 – 91Combined sources15
Beta strandi94 – 96Combined sources3
Beta strandi100 – 108Combined sources9
Turni109 – 112Combined sources4
Beta strandi113 – 119Combined sources7
Turni121 – 123Combined sources3
Beta strandi125 – 127Combined sources3
Beta strandi129 – 132Combined sources4
Helixi136 – 147Combined sources12
Helixi154 – 171Combined sources18
Beta strandi179 – 185Combined sources7
Beta strandi188 – 192Combined sources5
Turni194 – 197Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20K/Y1-198[»]
1G0UX-ray2.40J/X1-198[»]
1G65X-ray2.25J/X1-198[»]
1JD2X-ray3.00J/Q1-198[»]
1RYPX-ray1.90K/Y1-198[»]
1Z7QX-ray3.22K/Y1-198[»]
2F16X-ray2.80J/X1-198[»]
2FAKX-ray2.80J/X1-198[»]
2GPLX-ray2.81J/X1-198[»]
2ZCYX-ray2.90J/X1-198[»]
3BDMX-ray2.70J/X1-198[»]
3D29X-ray2.60J/X1-198[»]
3DY3X-ray2.81J/X1-198[»]
3DY4X-ray2.80J/X1-198[»]
3E47X-ray3.00J/X1-198[»]
3GPJX-ray2.70J/X1-198[»]
3GPTX-ray2.41J/X1-198[»]
3GPWX-ray2.50J/X1-198[»]
3HYEX-ray2.50J/X1-198[»]
3JCOelectron microscopy4.806/k1-198[»]
3JCPelectron microscopy4.606/k1-198[»]
3MG0X-ray2.68J/X1-198[»]
3MG4X-ray3.11J/X1-198[»]
3MG6X-ray2.60J/X1-198[»]
3MG7X-ray2.78J/X1-198[»]
3MG8X-ray2.59J/X1-198[»]
3NZJX-ray2.40J/X1-198[»]
3NZWX-ray2.50J/X1-198[»]
3NZXX-ray2.70J/X1-198[»]
3OEUX-ray2.60J/X1-198[»]
3OEVX-ray2.85J/X1-198[»]
3OKJX-ray2.70J/X1-198[»]
3SDIX-ray2.65J/X1-198[»]
3SDKX-ray2.70J/X1-198[»]
3SHJX-ray2.80J/X1-198[»]
3TDDX-ray2.70J/X1-198[»]
3UN4X-ray3.40J/X1-198[»]
3UN8X-ray2.70J/X1-198[»]
3WXRX-ray3.15K/Y1-198[»]
4CR2electron microscopy7.7041-198[»]
4CR3electron microscopy9.3041-198[»]
4CR4electron microscopy8.8041-198[»]
4EU2X-ray2.51K/Y1-198[»]
4FZCX-ray2.80J/X1-198[»]
4FZGX-ray3.00J/X1-198[»]
4G4SX-ray2.49K1-198[»]
4GK7X-ray2.80J/X1-198[»]
4HNPX-ray2.80J/X1-198[»]
4HRCX-ray2.80J/X1-198[»]
4HRDX-ray2.80J/X1-198[»]
4INRX-ray2.70J/X1-198[»]
4INTX-ray2.90J/X1-198[»]
4INUX-ray3.10J/X1-198[»]
4J70X-ray2.80J/X1-198[»]
4JSQX-ray2.80J/X1-198[»]
4JSUX-ray2.90J/X1-198[»]
4JT0X-ray3.10J/X1-198[»]
4LQIX-ray2.70J/X1-198[»]
4LTCX-ray2.50J/X1-198[»]
4NNNX-ray2.50J/X1-198[»]
4NNWX-ray2.60J/X1-198[»]
4NO1X-ray2.50J/X1-198[»]
4NO6X-ray3.00J/X1-198[»]
4NO8X-ray2.70J/X1-198[»]
4NO9X-ray2.90J/X1-198[»]
4Q1SX-ray2.60J/X1-198[»]
4QBYX-ray3.00J/X1-198[»]
4QLQX-ray2.40J/X1-198[»]
4QLSX-ray2.80J/X1-198[»]
4QLTX-ray2.80J/X1-198[»]
4QLUX-ray2.80J/X1-198[»]
4QLVX-ray2.90J/X1-198[»]
4QUXX-ray3.00J/X1-198[»]
4QUYX-ray2.80J/X1-198[»]
4QV0X-ray3.10J/X1-198[»]
4QV1X-ray2.50J/X1-198[»]
4QV3X-ray3.00J/X1-198[»]
4QV4X-ray2.70J/X1-198[»]
4QV5X-ray2.70J/X1-198[»]
4QV6X-ray2.80J/X1-198[»]
4QV7X-ray2.60J/X1-198[»]
4QV8X-ray2.90J/X1-198[»]
4QV9X-ray2.60J/X1-198[»]
4QVLX-ray2.80J/X1-198[»]
4QVMX-ray2.80J/X1-198[»]
4QVNX-ray2.90J/X1-198[»]
4QVPX-ray2.30J/X1-198[»]
4QVQX-ray2.60J/X1-198[»]
4QVVX-ray2.80J/X1-198[»]
4QVWX-ray3.00J/X1-198[»]
4QVYX-ray2.51J/X1-198[»]
4QW0X-ray2.90J/X1-198[»]
4QW1X-ray2.90J/X1-198[»]
4QW3X-ray2.90J/X1-198[»]
4QW4X-ray2.80J/X1-198[»]
4QW5X-ray3.00J/X1-198[»]
4QW6X-ray2.90J/X1-198[»]
4QW7X-ray2.70J/X1-198[»]
4QWFX-ray3.00J/X1-198[»]
4QWGX-ray2.60J/X1-198[»]
4QWIX-ray2.60J/X1-198[»]
4QWJX-ray2.90J/X1-198[»]
4QWKX-ray2.80J/X1-198[»]
4QWLX-ray2.60J/X1-198[»]
4QWRX-ray2.90J/X1-198[»]
4QWSX-ray3.00J/X1-198[»]
4QWUX-ray3.00J/X1-198[»]
4QWXX-ray2.90J/X1-198[»]
4QXJX-ray2.80J/X1-198[»]
4QZ0X-ray3.00J/X1-198[»]
4QZ1X-ray3.00J/X1-198[»]
4QZ2X-ray2.70J/X1-198[»]
4QZ3X-ray2.80J/X1-198[»]
4QZ4X-ray3.00J/X1-198[»]
4QZ5X-ray2.80J/X1-198[»]
4QZ6X-ray2.90J/X1-198[»]
4QZ7X-ray2.80J/X1-198[»]
4QZWX-ray3.00J/X1-198[»]
4QZXX-ray2.60J/X1-198[»]
4QZZX-ray2.90J/X1-198[»]
4R00X-ray2.80J/X1-198[»]
4R02X-ray2.50J/X1-198[»]
4R17X-ray2.10J/X1-198[»]
4R18X-ray2.40J/X1-198[»]
4RURX-ray2.50J/X1-198[»]
4V7OX-ray3.00A1/AO/BK/BY1-198[»]
4X6ZX-ray2.70K/Y1-198[»]
4Y69X-ray2.90J/X1-198[»]
4Y6AX-ray2.60J/X1-198[»]
4Y6VX-ray2.80J/X1-198[»]
4Y6ZX-ray2.70J/X1-198[»]
4Y70X-ray2.40J/X1-198[»]
4Y74X-ray2.70J/X1-198[»]
4Y75X-ray2.80J/X1-198[»]
4Y77X-ray2.50J/X1-198[»]
4Y78X-ray2.80J/X1-198[»]
4Y7WX-ray2.50J/X1-198[»]
4Y7XX-ray2.60J/X1-198[»]
4Y7YX-ray2.40J/X1-198[»]
4Y80X-ray2.50J/X1-198[»]
4Y81X-ray2.80J/X1-198[»]
4Y82X-ray2.80J/X1-198[»]
4Y84X-ray2.70J/X1-198[»]
4Y8GX-ray2.60J/X1-198[»]
4Y8HX-ray2.50J/X1-198[»]
4Y8IX-ray2.60J/X1-198[»]
4Y8JX-ray2.70J/X1-198[»]
4Y8KX-ray2.60J/X1-198[»]
4Y8LX-ray2.40J/X1-198[»]
4Y8MX-ray2.80J/X1-198[»]
4Y8NX-ray2.60J/X1-198[»]
4Y8OX-ray2.70J/X1-198[»]
4Y8PX-ray2.80J/X1-198[»]
4Y8QX-ray2.60J/X1-198[»]
4Y8RX-ray2.70J/X1-198[»]
4Y8SX-ray2.70J/X1-198[»]
4Y8TX-ray2.70J/X1-198[»]
4Y8UX-ray2.90J/X1-198[»]
4Y9YX-ray2.80J/X1-198[»]
4Y9ZX-ray2.80J/X1-198[»]
4YA0X-ray2.80J/X1-198[»]
4YA1X-ray2.90J/X1-198[»]
4YA2X-ray2.70J/X1-198[»]
4YA3X-ray2.70J/X1-198[»]
4YA4X-ray2.90J/X1-198[»]
4YA5X-ray2.50J/X1-198[»]
4YA7X-ray2.70J/X1-198[»]
4YA9X-ray2.70J/X1-198[»]
4Z1LX-ray3.00J/X1-198[»]
4ZZGX-ray3.00K/Y1-198[»]
5A5Belectron microscopy9.5041-198[»]
5AHJX-ray2.80J/X1-198[»]
5BOUX-ray2.60J/X1-198[»]
5BXLX-ray2.80J/X1-198[»]
5BXNX-ray2.80J/X1-198[»]
5CGFX-ray2.80J/X1-198[»]
5CGGX-ray2.90J/X1-198[»]
5CGHX-ray2.50J/X1-198[»]
5CGIX-ray2.80J/X1-198[»]
5CZ4X-ray2.30J/X1-198[»]
5CZ5X-ray2.80J/X1-198[»]
5CZ6X-ray2.70J/X1-198[»]
5CZ7X-ray2.50J/X1-198[»]
5CZ8X-ray2.80J/X1-198[»]
5CZ9X-ray2.90J/X1-198[»]
5CZAX-ray2.50J/X1-198[»]
5D0SX-ray2.50J/X1-198[»]
5D0TX-ray2.60J/X1-198[»]
5D0VX-ray2.90J/X1-198[»]
5D0WX-ray2.80J/X1-198[»]
5D0XX-ray2.60J/X1-198[»]
5D0ZX-ray2.90J/X1-198[»]
5DKIX-ray2.80J/X1-198[»]
5DKJX-ray2.80J/X1-198[»]
5FG7X-ray2.70J/X1-198[»]
5FG9X-ray2.60J/X1-198[»]
5FGAX-ray2.70J/X1-198[»]
5FGDX-ray2.80J/X1-198[»]
5FGEX-ray2.60J/X1-198[»]
5FGFX-ray2.60J/X1-198[»]
5FGGX-ray2.70J/X1-198[»]
5FGHX-ray2.80J/X1-198[»]
5FGIX-ray2.90J/X1-198[»]
5FHSX-ray2.70J/X1-198[»]
5JHRX-ray2.90J/X1-198[»]
5JHSX-ray3.00J/X1-198[»]
ProteinModelPortaliP22141.
SMRiP22141.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22141.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00640000091536.
HOGENOMiHOG000188743.
InParanoidiP22141.
KOiK02734.
OMAiHFVRGEL.
OrthoDBiEOG092C3ZSC.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P22141-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIILGIRVQ DSVILASSKA VTRGISVLKD SDDKTRQLSP HTLMSFAGEA
60 70 80 90 100
GDTVQFAEYI QANIQLYSIR EDYELSPQAV SSFVRQELAK SIRSRRPYQV
110 120 130 140 150
NVLIGGYDKK KNKPELYQID YLGTKVELPY GAHGYSGFYT FSLLDHHYRP
160 170 180 190
DMTTEEGLDL LKLCVQELEK RMPMDFKGVI VKIVDKDGIR QVDDFQAQ
Length:198
Mass (Da):22,517
Last modified:February 1, 1995 - v2
Checksum:iED43D319A5895B40
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti183I → T (PubMed:2001673).Curated1
Sequence conflicti188G → R (PubMed:2001673).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56812 Genomic DNA. Translation: CAA40149.1.
U18778 Genomic DNA. Translation: AAB64545.1.
AY557807 Genomic DNA. Translation: AAS56133.1.
BK006939 Genomic DNA. Translation: DAA07663.1.
PIRiS50470.
RefSeqiNP_010928.1. NM_001178903.1.

Genome annotation databases

EnsemblFungiiYER012W; YER012W; YER012W.
GeneIDi856731.
KEGGisce:YER012W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56812 Genomic DNA. Translation: CAA40149.1.
U18778 Genomic DNA. Translation: AAB64545.1.
AY557807 Genomic DNA. Translation: AAS56133.1.
BK006939 Genomic DNA. Translation: DAA07663.1.
PIRiS50470.
RefSeqiNP_010928.1. NM_001178903.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20K/Y1-198[»]
1G0UX-ray2.40J/X1-198[»]
1G65X-ray2.25J/X1-198[»]
1JD2X-ray3.00J/Q1-198[»]
1RYPX-ray1.90K/Y1-198[»]
1Z7QX-ray3.22K/Y1-198[»]
2F16X-ray2.80J/X1-198[»]
2FAKX-ray2.80J/X1-198[»]
2GPLX-ray2.81J/X1-198[»]
2ZCYX-ray2.90J/X1-198[»]
3BDMX-ray2.70J/X1-198[»]
3D29X-ray2.60J/X1-198[»]
3DY3X-ray2.81J/X1-198[»]
3DY4X-ray2.80J/X1-198[»]
3E47X-ray3.00J/X1-198[»]
3GPJX-ray2.70J/X1-198[»]
3GPTX-ray2.41J/X1-198[»]
3GPWX-ray2.50J/X1-198[»]
3HYEX-ray2.50J/X1-198[»]
3JCOelectron microscopy4.806/k1-198[»]
3JCPelectron microscopy4.606/k1-198[»]
3MG0X-ray2.68J/X1-198[»]
3MG4X-ray3.11J/X1-198[»]
3MG6X-ray2.60J/X1-198[»]
3MG7X-ray2.78J/X1-198[»]
3MG8X-ray2.59J/X1-198[»]
3NZJX-ray2.40J/X1-198[»]
3NZWX-ray2.50J/X1-198[»]
3NZXX-ray2.70J/X1-198[»]
3OEUX-ray2.60J/X1-198[»]
3OEVX-ray2.85J/X1-198[»]
3OKJX-ray2.70J/X1-198[»]
3SDIX-ray2.65J/X1-198[»]
3SDKX-ray2.70J/X1-198[»]
3SHJX-ray2.80J/X1-198[»]
3TDDX-ray2.70J/X1-198[»]
3UN4X-ray3.40J/X1-198[»]
3UN8X-ray2.70J/X1-198[»]
3WXRX-ray3.15K/Y1-198[»]
4CR2electron microscopy7.7041-198[»]
4CR3electron microscopy9.3041-198[»]
4CR4electron microscopy8.8041-198[»]
4EU2X-ray2.51K/Y1-198[»]
4FZCX-ray2.80J/X1-198[»]
4FZGX-ray3.00J/X1-198[»]
4G4SX-ray2.49K1-198[»]
4GK7X-ray2.80J/X1-198[»]
4HNPX-ray2.80J/X1-198[»]
4HRCX-ray2.80J/X1-198[»]
4HRDX-ray2.80J/X1-198[»]
4INRX-ray2.70J/X1-198[»]
4INTX-ray2.90J/X1-198[»]
4INUX-ray3.10J/X1-198[»]
4J70X-ray2.80J/X1-198[»]
4JSQX-ray2.80J/X1-198[»]
4JSUX-ray2.90J/X1-198[»]
4JT0X-ray3.10J/X1-198[»]
4LQIX-ray2.70J/X1-198[»]
4LTCX-ray2.50J/X1-198[»]
4NNNX-ray2.50J/X1-198[»]
4NNWX-ray2.60J/X1-198[»]
4NO1X-ray2.50J/X1-198[»]
4NO6X-ray3.00J/X1-198[»]
4NO8X-ray2.70J/X1-198[»]
4NO9X-ray2.90J/X1-198[»]
4Q1SX-ray2.60J/X1-198[»]
4QBYX-ray3.00J/X1-198[»]
4QLQX-ray2.40J/X1-198[»]
4QLSX-ray2.80J/X1-198[»]
4QLTX-ray2.80J/X1-198[»]
4QLUX-ray2.80J/X1-198[»]
4QLVX-ray2.90J/X1-198[»]
4QUXX-ray3.00J/X1-198[»]
4QUYX-ray2.80J/X1-198[»]
4QV0X-ray3.10J/X1-198[»]
4QV1X-ray2.50J/X1-198[»]
4QV3X-ray3.00J/X1-198[»]
4QV4X-ray2.70J/X1-198[»]
4QV5X-ray2.70J/X1-198[»]
4QV6X-ray2.80J/X1-198[»]
4QV7X-ray2.60J/X1-198[»]
4QV8X-ray2.90J/X1-198[»]
4QV9X-ray2.60J/X1-198[»]
4QVLX-ray2.80J/X1-198[»]
4QVMX-ray2.80J/X1-198[»]
4QVNX-ray2.90J/X1-198[»]
4QVPX-ray2.30J/X1-198[»]
4QVQX-ray2.60J/X1-198[»]
4QVVX-ray2.80J/X1-198[»]
4QVWX-ray3.00J/X1-198[»]
4QVYX-ray2.51J/X1-198[»]
4QW0X-ray2.90J/X1-198[»]
4QW1X-ray2.90J/X1-198[»]
4QW3X-ray2.90J/X1-198[»]
4QW4X-ray2.80J/X1-198[»]
4QW5X-ray3.00J/X1-198[»]
4QW6X-ray2.90J/X1-198[»]
4QW7X-ray2.70J/X1-198[»]
4QWFX-ray3.00J/X1-198[»]
4QWGX-ray2.60J/X1-198[»]
4QWIX-ray2.60J/X1-198[»]
4QWJX-ray2.90J/X1-198[»]
4QWKX-ray2.80J/X1-198[»]
4QWLX-ray2.60J/X1-198[»]
4QWRX-ray2.90J/X1-198[»]
4QWSX-ray3.00J/X1-198[»]
4QWUX-ray3.00J/X1-198[»]
4QWXX-ray2.90J/X1-198[»]
4QXJX-ray2.80J/X1-198[»]
4QZ0X-ray3.00J/X1-198[»]
4QZ1X-ray3.00J/X1-198[»]
4QZ2X-ray2.70J/X1-198[»]
4QZ3X-ray2.80J/X1-198[»]
4QZ4X-ray3.00J/X1-198[»]
4QZ5X-ray2.80J/X1-198[»]
4QZ6X-ray2.90J/X1-198[»]
4QZ7X-ray2.80J/X1-198[»]
4QZWX-ray3.00J/X1-198[»]
4QZXX-ray2.60J/X1-198[»]
4QZZX-ray2.90J/X1-198[»]
4R00X-ray2.80J/X1-198[»]
4R02X-ray2.50J/X1-198[»]
4R17X-ray2.10J/X1-198[»]
4R18X-ray2.40J/X1-198[»]
4RURX-ray2.50J/X1-198[»]
4V7OX-ray3.00A1/AO/BK/BY1-198[»]
4X6ZX-ray2.70K/Y1-198[»]
4Y69X-ray2.90J/X1-198[»]
4Y6AX-ray2.60J/X1-198[»]
4Y6VX-ray2.80J/X1-198[»]
4Y6ZX-ray2.70J/X1-198[»]
4Y70X-ray2.40J/X1-198[»]
4Y74X-ray2.70J/X1-198[»]
4Y75X-ray2.80J/X1-198[»]
4Y77X-ray2.50J/X1-198[»]
4Y78X-ray2.80J/X1-198[»]
4Y7WX-ray2.50J/X1-198[»]
4Y7XX-ray2.60J/X1-198[»]
4Y7YX-ray2.40J/X1-198[»]
4Y80X-ray2.50J/X1-198[»]
4Y81X-ray2.80J/X1-198[»]
4Y82X-ray2.80J/X1-198[»]
4Y84X-ray2.70J/X1-198[»]
4Y8GX-ray2.60J/X1-198[»]
4Y8HX-ray2.50J/X1-198[»]
4Y8IX-ray2.60J/X1-198[»]
4Y8JX-ray2.70J/X1-198[»]
4Y8KX-ray2.60J/X1-198[»]
4Y8LX-ray2.40J/X1-198[»]
4Y8MX-ray2.80J/X1-198[»]
4Y8NX-ray2.60J/X1-198[»]
4Y8OX-ray2.70J/X1-198[»]
4Y8PX-ray2.80J/X1-198[»]
4Y8QX-ray2.60J/X1-198[»]
4Y8RX-ray2.70J/X1-198[»]
4Y8SX-ray2.70J/X1-198[»]
4Y8TX-ray2.70J/X1-198[»]
4Y8UX-ray2.90J/X1-198[»]
4Y9YX-ray2.80J/X1-198[»]
4Y9ZX-ray2.80J/X1-198[»]
4YA0X-ray2.80J/X1-198[»]
4YA1X-ray2.90J/X1-198[»]
4YA2X-ray2.70J/X1-198[»]
4YA3X-ray2.70J/X1-198[»]
4YA4X-ray2.90J/X1-198[»]
4YA5X-ray2.50J/X1-198[»]
4YA7X-ray2.70J/X1-198[»]
4YA9X-ray2.70J/X1-198[»]
4Z1LX-ray3.00J/X1-198[»]
4ZZGX-ray3.00K/Y1-198[»]
5A5Belectron microscopy9.5041-198[»]
5AHJX-ray2.80J/X1-198[»]
5BOUX-ray2.60J/X1-198[»]
5BXLX-ray2.80J/X1-198[»]
5BXNX-ray2.80J/X1-198[»]
5CGFX-ray2.80J/X1-198[»]
5CGGX-ray2.90J/X1-198[»]
5CGHX-ray2.50J/X1-198[»]
5CGIX-ray2.80J/X1-198[»]
5CZ4X-ray2.30J/X1-198[»]
5CZ5X-ray2.80J/X1-198[»]
5CZ6X-ray2.70J/X1-198[»]
5CZ7X-ray2.50J/X1-198[»]
5CZ8X-ray2.80J/X1-198[»]
5CZ9X-ray2.90J/X1-198[»]
5CZAX-ray2.50J/X1-198[»]
5D0SX-ray2.50J/X1-198[»]
5D0TX-ray2.60J/X1-198[»]
5D0VX-ray2.90J/X1-198[»]
5D0WX-ray2.80J/X1-198[»]
5D0XX-ray2.60J/X1-198[»]
5D0ZX-ray2.90J/X1-198[»]
5DKIX-ray2.80J/X1-198[»]
5DKJX-ray2.80J/X1-198[»]
5FG7X-ray2.70J/X1-198[»]
5FG9X-ray2.60J/X1-198[»]
5FGAX-ray2.70J/X1-198[»]
5FGDX-ray2.80J/X1-198[»]
5FGEX-ray2.60J/X1-198[»]
5FGFX-ray2.60J/X1-198[»]
5FGGX-ray2.70J/X1-198[»]
5FGHX-ray2.80J/X1-198[»]
5FGIX-ray2.90J/X1-198[»]
5FHSX-ray2.70J/X1-198[»]
5JHRX-ray2.90J/X1-198[»]
5JHSX-ray3.00J/X1-198[»]
ProteinModelPortaliP22141.
SMRiP22141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36744. 142 interactors.
DIPiDIP-2808N.
IntActiP22141. 27 interactors.
MINTiMINT-592869.

Chemistry databases

BindingDBiP22141.
ChEMBLiCHEMBL4206.

Protein family/group databases

MEROPSiT01.984.

PTM databases

iPTMnetiP22141.

Proteomic databases

MaxQBiP22141.
PRIDEiP22141.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER012W; YER012W; YER012W.
GeneIDi856731.
KEGGisce:YER012W.

Organism-specific databases

EuPathDBiFungiDB:YER012W.
SGDiS000000814. PRE1.

Phylogenomic databases

GeneTreeiENSGT00640000091536.
HOGENOMiHOG000188743.
InParanoidiP22141.
KOiK02734.
OMAiHFVRGEL.
OrthoDBiEOG092C3ZSC.

Enzyme and pathway databases

BioCyciYEAST:G3O-30199-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

EvolutionaryTraceiP22141.
PROiP22141.

Family and domain databases

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

Entry informationi

Entry nameiPSB4_YEAST
AccessioniPrimary (citable) accession number: P22141
Secondary accession number(s): D3DLQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 181 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 21800 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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: 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.