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Protein

Proteasome subunit beta type-1

Gene

PRE3

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.
This subunit is necessary for the peptidylglutamyl-peptide hydrolyzing activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei20Nucleophile1 Publication1

GO - Molecular functioni

  • endopeptidase 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-31481-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

MEROPSiT01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-1 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PRE3
Multicatalytic endopeptidase complex subunit PRE3
Proteasome component PRE3
Proteinase YSCE subunit PRE3
Gene namesi
Name:PRE3
Ordered Locus Names:YJL001W
ORF Names:J1407
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL001W.
SGDiS000003538. PRE3.

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_00000266431 – 19Removed in mature formAdd BLAST19
ChainiPRO_000002664420 – 215Proteasome subunit beta type-1Add BLAST196

Amino acid modifications

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

Keywords - PTMi

Acetylation, Zymogen

Proteomic databases

MaxQBiP38624.
PRIDEiP38624.

2D gel databases

UCD-2DPAGEP38624.

PTM databases

iPTMnetiP38624.

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

BioGridi33756. 78 interactors.
DIPiDIP-1527N.
IntActiP38624. 21 interactors.
MINTiMINT-401012.

Structurei

Secondary structure

1215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 9Combined sources4
Beta strandi22 – 27Combined sources6
Beta strandi30 – 35Combined sources6
Beta strandi39 – 41Combined sources3
Beta strandi44 – 49Combined sources6
Beta strandi53 – 57Combined sources5
Beta strandi60 – 67Combined sources8
Helixi68 – 89Combined sources22
Helixi94 – 107Combined sources14
Turni108 – 111Combined sources4
Beta strandi114 – 122Combined sources9
Turni123 – 125Combined sources3
Beta strandi126 – 132Combined sources7
Turni134 – 136Combined sources3
Beta strandi139 – 147Combined sources9
Helixi148 – 153Combined sources6
Helixi154 – 160Combined sources7
Helixi167 – 184Combined sources18
Beta strandi185 – 187Combined sources3
Beta strandi192 – 198Combined sources7
Beta strandi201 – 207Combined sources7
Helixi209 – 212Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20H/V20-215[»]
1G0UX-ray2.402/N20-215[»]
1G65X-ray2.252/N20-215[»]
1JD2X-ray3.00N/U20-215[»]
1RYPX-ray1.90H/V11-215[»]
1Z7QX-ray3.22H/V20-215[»]
2F16X-ray2.802/N20-215[»]
2FAKX-ray2.802/N20-205[»]
2GPLX-ray2.812/N20-215[»]
2ZCYX-ray2.901/N20-215[»]
3BDMX-ray2.701/N20-215[»]
3D29X-ray2.602/N20-215[»]
3DY3X-ray2.812/N20-215[»]
3DY4X-ray2.802/N20-215[»]
3E47X-ray3.002/N20-215[»]
3GPJX-ray2.702/N20-215[»]
3GPTX-ray2.412/N20-215[»]
3GPWX-ray2.502/N20-215[»]
3HYEX-ray2.502/N20-215[»]
3JCOelectron microscopy4.803/h1-215[»]
3JCPelectron microscopy4.603/h1-215[»]
3MG0X-ray2.682/N20-215[»]
3MG4X-ray3.112/N20-215[»]
3MG6X-ray2.602/N20-215[»]
3MG7X-ray2.782/N20-215[»]
3MG8X-ray2.592/N20-215[»]
3NZJX-ray2.402/N1-215[»]
3NZWX-ray2.502/N1-215[»]
3NZXX-ray2.702/N1-215[»]
3OEUX-ray2.602/N20-215[»]
3OEVX-ray2.852/N20-215[»]
3OKJX-ray2.702/N20-215[»]
3SDIX-ray2.652/N20-215[»]
3SDKX-ray2.702/N20-215[»]
3SHJX-ray2.802/N20-215[»]
3TDDX-ray2.702/N20-215[»]
3UN4X-ray3.40N/b20-215[»]
3UN8X-ray2.70N/b20-215[»]
3WXRX-ray3.15H/V1-215[»]
4CR2electron microscopy7.7011-215[»]
4CR3electron microscopy9.3011-215[»]
4CR4electron microscopy8.8011-215[»]
4EU2X-ray2.51H/V20-215[»]
4FZCX-ray2.80N/b20-215[»]
4FZGX-ray3.00N/b20-215[»]
4G4SX-ray2.49H20-215[»]
4GK7X-ray2.80N/b20-215[»]
4HNPX-ray2.80N/b20-215[»]
4HRCX-ray2.80N/b20-215[»]
4HRDX-ray2.80N/b20-215[»]
4INRX-ray2.70N/b20-215[»]
4INTX-ray2.90N/b20-215[»]
4INUX-ray3.10N/b20-215[»]
4J70X-ray2.80N/b20-215[»]
4JSQX-ray2.80N/b20-215[»]
4JSUX-ray2.90N/b20-215[»]
4JT0X-ray3.10N/b20-215[»]
4LQIX-ray2.70N/b20-215[»]
4LTCX-ray2.50N/b20-215[»]
4NNNX-ray2.50N/b20-215[»]
4NNWX-ray2.60N/b20-215[»]
4NO1X-ray2.50N/b20-215[»]
4NO6X-ray3.00N/b20-215[»]
4NO8X-ray2.70N/b20-215[»]
4NO9X-ray2.90N/b20-215[»]
4Q1SX-ray2.60N/b20-215[»]
4QBYX-ray3.00N/b20-215[»]
4QLQX-ray2.40N/b20-215[»]
4QLSX-ray2.80N/b20-215[»]
4QLTX-ray2.80N/b20-215[»]
4QLUX-ray2.80N/b20-215[»]
4QLVX-ray2.90N/b20-215[»]
4QUXX-ray3.00N/b20-215[»]
4QUYX-ray2.80N/b20-215[»]
4QV0X-ray3.10N/b20-215[»]
4QV1X-ray2.50N/b20-215[»]
4QV3X-ray3.00N/b20-215[»]
4QV4X-ray2.70N/b20-215[»]
4QV5X-ray2.70N/b20-215[»]
4QV6X-ray2.80N/b20-215[»]
4QV7X-ray2.60N/b20-215[»]
4QV8X-ray2.90N/b20-215[»]
4QV9X-ray2.60N/b20-215[»]
4QVLX-ray2.80N/b20-215[»]
4QVMX-ray2.80N/b20-215[»]
4QVNX-ray2.90N/b20-215[»]
4QVPX-ray2.30N/b20-215[»]
4QVQX-ray2.60N/b20-215[»]
4QVVX-ray2.80N/b20-215[»]
4QVWX-ray3.00N/b20-215[»]
4QVYX-ray2.51N/b20-215[»]
4QW0X-ray2.90N/b20-215[»]
4QW1X-ray2.90N/b20-215[»]
4QW3X-ray2.90N/b20-215[»]
4QW4X-ray2.80N/b20-215[»]
4QW5X-ray3.00N/b20-215[»]
4QW6X-ray2.90N/b20-215[»]
4QW7X-ray2.70N/b20-215[»]
4QWFX-ray3.00N/b20-215[»]
4QWGX-ray2.60N/b20-215[»]
4QWIX-ray2.60N/b20-215[»]
4QWJX-ray2.90N/b20-215[»]
4QWKX-ray2.80N/b20-215[»]
4QWLX-ray2.60N/b20-215[»]
4QWRX-ray2.90N/b20-215[»]
4QWSX-ray3.00N/b20-215[»]
4QWUX-ray3.00N/b20-215[»]
4QWXX-ray2.90N/b20-215[»]
4QXJX-ray2.80N/b20-215[»]
4QZ0X-ray3.00N/b20-215[»]
4QZ1X-ray3.00N/b20-215[»]
4QZ2X-ray2.70N/b20-215[»]
4QZ3X-ray2.80N/b20-215[»]
4QZ4X-ray3.00N/b20-215[»]
4QZ5X-ray2.80N/b20-215[»]
4QZ6X-ray2.90N/b20-215[»]
4QZ7X-ray2.80N/b20-215[»]
4QZWX-ray3.00N/b20-215[»]
4QZXX-ray2.60N/b20-215[»]
4QZZX-ray2.90N/b20-215[»]
4R00X-ray2.80N/b20-215[»]
4R02X-ray2.50N/b20-215[»]
4R17X-ray2.10N/b20-215[»]
4R18X-ray2.40N/b20-215[»]
4RURX-ray2.50N/b20-215[»]
4V7OX-ray3.00AB/AD/BH/BV21-215[»]
4X6ZX-ray2.70H/V1-215[»]
4Y69X-ray2.90N/b20-215[»]
4Y6AX-ray2.60N/b20-215[»]
4Y6VX-ray2.80N/b20-215[»]
4Y6ZX-ray2.70N/b20-215[»]
4Y70X-ray2.40N/b20-215[»]
4Y74X-ray2.70N/b20-215[»]
4Y75X-ray2.80N/b20-215[»]
4Y77X-ray2.50N/b20-215[»]
4Y78X-ray2.80N/b20-215[»]
4Y7WX-ray2.50N/b20-215[»]
4Y7XX-ray2.60N/b20-215[»]
4Y7YX-ray2.40N/b20-215[»]
4Y80X-ray2.50N/b20-215[»]
4Y81X-ray2.80N/b20-215[»]
4Y82X-ray2.80N/b20-215[»]
4Y84X-ray2.70N/b20-215[»]
4Y8GX-ray2.60N/b20-215[»]
4Y8HX-ray2.50N/b20-215[»]
4Y8IX-ray2.60N/b20-215[»]
4Y8JX-ray2.70N/b20-215[»]
4Y8KX-ray2.60N/b20-215[»]
4Y8LX-ray2.40N/b20-215[»]
4Y8MX-ray2.80N/b20-215[»]
4Y8NX-ray2.60N/b20-215[»]
4Y8OX-ray2.70N/b20-215[»]
4Y8PX-ray2.80N/b20-215[»]
4Y8QX-ray2.60N/b20-215[»]
4Y8RX-ray2.70N/b20-215[»]
4Y8SX-ray2.70N/b20-215[»]
4Y8TX-ray2.70N/b20-215[»]
4Y8UX-ray2.90N/b20-215[»]
4Y9YX-ray2.80N/b20-215[»]
4Y9ZX-ray2.80N/b20-215[»]
4YA0X-ray2.80N/b20-215[»]
4YA1X-ray2.90N/b20-215[»]
4YA2X-ray2.70N/b20-215[»]
4YA3X-ray2.70N/b20-215[»]
4YA4X-ray2.90N/b20-215[»]
4YA5X-ray2.50N/b20-215[»]
4YA7X-ray2.70N/b20-215[»]
4YA9X-ray2.70N/b20-215[»]
4Z1LX-ray3.00N/b20-215[»]
4ZZGX-ray3.00H/V1-215[»]
5A5Belectron microscopy9.5011-215[»]
5AHJX-ray2.80N/b20-215[»]
5BOUX-ray2.60N/b20-215[»]
5BXLX-ray2.80N/b20-215[»]
5BXNX-ray2.80N/b20-215[»]
5CGFX-ray2.80N/b20-215[»]
5CGGX-ray2.90N/b20-215[»]
5CGHX-ray2.50N/b20-215[»]
5CGIX-ray2.80N/b20-215[»]
5CZ4X-ray2.30N/b20-215[»]
5CZ5X-ray2.80N/b10-215[»]
5CZ6X-ray2.70N/b20-215[»]
5CZ7X-ray2.50N/b20-215[»]
5CZ8X-ray2.80N/b20-215[»]
5CZ9X-ray2.90N/b20-215[»]
5CZAX-ray2.50N/b20-215[»]
5D0SX-ray2.50N/b20-215[»]
5D0TX-ray2.60N/b20-215[»]
5D0VX-ray2.90N/b20-215[»]
5D0WX-ray2.80N/b20-215[»]
5D0XX-ray2.60N/b20-215[»]
5D0ZX-ray2.90N/b20-215[»]
5DKIX-ray2.80N/b20-215[»]
5DKJX-ray2.80N/b20-215[»]
5FG7X-ray2.70N/b20-215[»]
5FG9X-ray2.60N/b20-215[»]
5FGAX-ray2.70N/b20-215[»]
5FGDX-ray2.80N/b20-215[»]
5FGEX-ray2.60N/b20-215[»]
5FGFX-ray2.60N/b20-215[»]
5FGGX-ray2.70N/b20-215[»]
5FGHX-ray2.80N/b20-215[»]
5FGIX-ray2.90N/b3-215[»]
5FHSX-ray2.70N/b20-215[»]
5JHRX-ray2.90N/b20-215[»]
5JHSX-ray3.00N/b20-215[»]
ProteinModelPortaliP38624.
SMRiP38624.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38624.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
InParanoidiP38624.
KOiK02738.
OMAiTSIMAVQ.
OrthoDBiEOG092C4SID.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
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.

P38624-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGIQVDINR LKKGEVSLGT SIMAVTFKDG VILGADSRTT TGAYIANRVT
60 70 80 90 100
DKLTRVHDKI WCCRSGSAAD TQAIADIVQY HLELYTSQYG TPSTETAASV
110 120 130 140 150
FKELCYENKD NLTAGIIVAG YDDKNKGEVY TIPLGGSVHK LPYAIAGSGS
160 170 180 190 200
TFIYGYCDKN FRENMSKEET VDFIKHSLSQ AIKWDGSSGG VIRMVVLTAA
210
GVERLIFYPD EYEQL
Length:215
Mass (Da):23,548
Last modified:November 1, 1995 - v2
Checksum:iBD1FCE649678D86B
GO

Sequence cautioni

The sequence CAA55591 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA60921 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78991 Genomic DNA. Translation: CAA55591.1. Different initiation.
Z49276 Genomic DNA. Translation: CAA89290.1.
Z49277 Genomic DNA. Translation: CAA89292.1.
X87611 Genomic DNA. Translation: CAA60921.1. Different initiation.
X86020 mRNA. Translation: CAA60015.1.
S78566 mRNA. Translation: AAB34629.1.
BK006943 Genomic DNA. Translation: DAA08790.1.
PIRiS61337.
RefSeqiNP_012533.1. NM_001181435.1.

Genome annotation databases

EnsemblFungiiYJL001W; YJL001W; YJL001W.
GeneIDi853456.
KEGGisce:YJL001W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78991 Genomic DNA. Translation: CAA55591.1. Different initiation.
Z49276 Genomic DNA. Translation: CAA89290.1.
Z49277 Genomic DNA. Translation: CAA89292.1.
X87611 Genomic DNA. Translation: CAA60921.1. Different initiation.
X86020 mRNA. Translation: CAA60015.1.
S78566 mRNA. Translation: AAB34629.1.
BK006943 Genomic DNA. Translation: DAA08790.1.
PIRiS61337.
RefSeqiNP_012533.1. NM_001181435.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20H/V20-215[»]
1G0UX-ray2.402/N20-215[»]
1G65X-ray2.252/N20-215[»]
1JD2X-ray3.00N/U20-215[»]
1RYPX-ray1.90H/V11-215[»]
1Z7QX-ray3.22H/V20-215[»]
2F16X-ray2.802/N20-215[»]
2FAKX-ray2.802/N20-205[»]
2GPLX-ray2.812/N20-215[»]
2ZCYX-ray2.901/N20-215[»]
3BDMX-ray2.701/N20-215[»]
3D29X-ray2.602/N20-215[»]
3DY3X-ray2.812/N20-215[»]
3DY4X-ray2.802/N20-215[»]
3E47X-ray3.002/N20-215[»]
3GPJX-ray2.702/N20-215[»]
3GPTX-ray2.412/N20-215[»]
3GPWX-ray2.502/N20-215[»]
3HYEX-ray2.502/N20-215[»]
3JCOelectron microscopy4.803/h1-215[»]
3JCPelectron microscopy4.603/h1-215[»]
3MG0X-ray2.682/N20-215[»]
3MG4X-ray3.112/N20-215[»]
3MG6X-ray2.602/N20-215[»]
3MG7X-ray2.782/N20-215[»]
3MG8X-ray2.592/N20-215[»]
3NZJX-ray2.402/N1-215[»]
3NZWX-ray2.502/N1-215[»]
3NZXX-ray2.702/N1-215[»]
3OEUX-ray2.602/N20-215[»]
3OEVX-ray2.852/N20-215[»]
3OKJX-ray2.702/N20-215[»]
3SDIX-ray2.652/N20-215[»]
3SDKX-ray2.702/N20-215[»]
3SHJX-ray2.802/N20-215[»]
3TDDX-ray2.702/N20-215[»]
3UN4X-ray3.40N/b20-215[»]
3UN8X-ray2.70N/b20-215[»]
3WXRX-ray3.15H/V1-215[»]
4CR2electron microscopy7.7011-215[»]
4CR3electron microscopy9.3011-215[»]
4CR4electron microscopy8.8011-215[»]
4EU2X-ray2.51H/V20-215[»]
4FZCX-ray2.80N/b20-215[»]
4FZGX-ray3.00N/b20-215[»]
4G4SX-ray2.49H20-215[»]
4GK7X-ray2.80N/b20-215[»]
4HNPX-ray2.80N/b20-215[»]
4HRCX-ray2.80N/b20-215[»]
4HRDX-ray2.80N/b20-215[»]
4INRX-ray2.70N/b20-215[»]
4INTX-ray2.90N/b20-215[»]
4INUX-ray3.10N/b20-215[»]
4J70X-ray2.80N/b20-215[»]
4JSQX-ray2.80N/b20-215[»]
4JSUX-ray2.90N/b20-215[»]
4JT0X-ray3.10N/b20-215[»]
4LQIX-ray2.70N/b20-215[»]
4LTCX-ray2.50N/b20-215[»]
4NNNX-ray2.50N/b20-215[»]
4NNWX-ray2.60N/b20-215[»]
4NO1X-ray2.50N/b20-215[»]
4NO6X-ray3.00N/b20-215[»]
4NO8X-ray2.70N/b20-215[»]
4NO9X-ray2.90N/b20-215[»]
4Q1SX-ray2.60N/b20-215[»]
4QBYX-ray3.00N/b20-215[»]
4QLQX-ray2.40N/b20-215[»]
4QLSX-ray2.80N/b20-215[»]
4QLTX-ray2.80N/b20-215[»]
4QLUX-ray2.80N/b20-215[»]
4QLVX-ray2.90N/b20-215[»]
4QUXX-ray3.00N/b20-215[»]
4QUYX-ray2.80N/b20-215[»]
4QV0X-ray3.10N/b20-215[»]
4QV1X-ray2.50N/b20-215[»]
4QV3X-ray3.00N/b20-215[»]
4QV4X-ray2.70N/b20-215[»]
4QV5X-ray2.70N/b20-215[»]
4QV6X-ray2.80N/b20-215[»]
4QV7X-ray2.60N/b20-215[»]
4QV8X-ray2.90N/b20-215[»]
4QV9X-ray2.60N/b20-215[»]
4QVLX-ray2.80N/b20-215[»]
4QVMX-ray2.80N/b20-215[»]
4QVNX-ray2.90N/b20-215[»]
4QVPX-ray2.30N/b20-215[»]
4QVQX-ray2.60N/b20-215[»]
4QVVX-ray2.80N/b20-215[»]
4QVWX-ray3.00N/b20-215[»]
4QVYX-ray2.51N/b20-215[»]
4QW0X-ray2.90N/b20-215[»]
4QW1X-ray2.90N/b20-215[»]
4QW3X-ray2.90N/b20-215[»]
4QW4X-ray2.80N/b20-215[»]
4QW5X-ray3.00N/b20-215[»]
4QW6X-ray2.90N/b20-215[»]
4QW7X-ray2.70N/b20-215[»]
4QWFX-ray3.00N/b20-215[»]
4QWGX-ray2.60N/b20-215[»]
4QWIX-ray2.60N/b20-215[»]
4QWJX-ray2.90N/b20-215[»]
4QWKX-ray2.80N/b20-215[»]
4QWLX-ray2.60N/b20-215[»]
4QWRX-ray2.90N/b20-215[»]
4QWSX-ray3.00N/b20-215[»]
4QWUX-ray3.00N/b20-215[»]
4QWXX-ray2.90N/b20-215[»]
4QXJX-ray2.80N/b20-215[»]
4QZ0X-ray3.00N/b20-215[»]
4QZ1X-ray3.00N/b20-215[»]
4QZ2X-ray2.70N/b20-215[»]
4QZ3X-ray2.80N/b20-215[»]
4QZ4X-ray3.00N/b20-215[»]
4QZ5X-ray2.80N/b20-215[»]
4QZ6X-ray2.90N/b20-215[»]
4QZ7X-ray2.80N/b20-215[»]
4QZWX-ray3.00N/b20-215[»]
4QZXX-ray2.60N/b20-215[»]
4QZZX-ray2.90N/b20-215[»]
4R00X-ray2.80N/b20-215[»]
4R02X-ray2.50N/b20-215[»]
4R17X-ray2.10N/b20-215[»]
4R18X-ray2.40N/b20-215[»]
4RURX-ray2.50N/b20-215[»]
4V7OX-ray3.00AB/AD/BH/BV21-215[»]
4X6ZX-ray2.70H/V1-215[»]
4Y69X-ray2.90N/b20-215[»]
4Y6AX-ray2.60N/b20-215[»]
4Y6VX-ray2.80N/b20-215[»]
4Y6ZX-ray2.70N/b20-215[»]
4Y70X-ray2.40N/b20-215[»]
4Y74X-ray2.70N/b20-215[»]
4Y75X-ray2.80N/b20-215[»]
4Y77X-ray2.50N/b20-215[»]
4Y78X-ray2.80N/b20-215[»]
4Y7WX-ray2.50N/b20-215[»]
4Y7XX-ray2.60N/b20-215[»]
4Y7YX-ray2.40N/b20-215[»]
4Y80X-ray2.50N/b20-215[»]
4Y81X-ray2.80N/b20-215[»]
4Y82X-ray2.80N/b20-215[»]
4Y84X-ray2.70N/b20-215[»]
4Y8GX-ray2.60N/b20-215[»]
4Y8HX-ray2.50N/b20-215[»]
4Y8IX-ray2.60N/b20-215[»]
4Y8JX-ray2.70N/b20-215[»]
4Y8KX-ray2.60N/b20-215[»]
4Y8LX-ray2.40N/b20-215[»]
4Y8MX-ray2.80N/b20-215[»]
4Y8NX-ray2.60N/b20-215[»]
4Y8OX-ray2.70N/b20-215[»]
4Y8PX-ray2.80N/b20-215[»]
4Y8QX-ray2.60N/b20-215[»]
4Y8RX-ray2.70N/b20-215[»]
4Y8SX-ray2.70N/b20-215[»]
4Y8TX-ray2.70N/b20-215[»]
4Y8UX-ray2.90N/b20-215[»]
4Y9YX-ray2.80N/b20-215[»]
4Y9ZX-ray2.80N/b20-215[»]
4YA0X-ray2.80N/b20-215[»]
4YA1X-ray2.90N/b20-215[»]
4YA2X-ray2.70N/b20-215[»]
4YA3X-ray2.70N/b20-215[»]
4YA4X-ray2.90N/b20-215[»]
4YA5X-ray2.50N/b20-215[»]
4YA7X-ray2.70N/b20-215[»]
4YA9X-ray2.70N/b20-215[»]
4Z1LX-ray3.00N/b20-215[»]
4ZZGX-ray3.00H/V1-215[»]
5A5Belectron microscopy9.5011-215[»]
5AHJX-ray2.80N/b20-215[»]
5BOUX-ray2.60N/b20-215[»]
5BXLX-ray2.80N/b20-215[»]
5BXNX-ray2.80N/b20-215[»]
5CGFX-ray2.80N/b20-215[»]
5CGGX-ray2.90N/b20-215[»]
5CGHX-ray2.50N/b20-215[»]
5CGIX-ray2.80N/b20-215[»]
5CZ4X-ray2.30N/b20-215[»]
5CZ5X-ray2.80N/b10-215[»]
5CZ6X-ray2.70N/b20-215[»]
5CZ7X-ray2.50N/b20-215[»]
5CZ8X-ray2.80N/b20-215[»]
5CZ9X-ray2.90N/b20-215[»]
5CZAX-ray2.50N/b20-215[»]
5D0SX-ray2.50N/b20-215[»]
5D0TX-ray2.60N/b20-215[»]
5D0VX-ray2.90N/b20-215[»]
5D0WX-ray2.80N/b20-215[»]
5D0XX-ray2.60N/b20-215[»]
5D0ZX-ray2.90N/b20-215[»]
5DKIX-ray2.80N/b20-215[»]
5DKJX-ray2.80N/b20-215[»]
5FG7X-ray2.70N/b20-215[»]
5FG9X-ray2.60N/b20-215[»]
5FGAX-ray2.70N/b20-215[»]
5FGDX-ray2.80N/b20-215[»]
5FGEX-ray2.60N/b20-215[»]
5FGFX-ray2.60N/b20-215[»]
5FGGX-ray2.70N/b20-215[»]
5FGHX-ray2.80N/b20-215[»]
5FGIX-ray2.90N/b3-215[»]
5FHSX-ray2.70N/b20-215[»]
5JHRX-ray2.90N/b20-215[»]
5JHSX-ray3.00N/b20-215[»]
ProteinModelPortaliP38624.
SMRiP38624.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33756. 78 interactors.
DIPiDIP-1527N.
IntActiP38624. 21 interactors.
MINTiMINT-401012.

Protein family/group databases

MEROPSiT01.010.

PTM databases

iPTMnetiP38624.

2D gel databases

UCD-2DPAGEP38624.

Proteomic databases

MaxQBiP38624.
PRIDEiP38624.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL001W; YJL001W; YJL001W.
GeneIDi853456.
KEGGisce:YJL001W.

Organism-specific databases

EuPathDBiFungiDB:YJL001W.
SGDiS000003538. PRE3.

Phylogenomic databases

GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
InParanoidiP38624.
KOiK02738.
OMAiTSIMAVQ.
OrthoDBiEOG092C4SID.

Enzyme and pathway databases

BioCyciYEAST:G3O-31481-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

EvolutionaryTraceiP38624.
PROiP38624.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPSB1_YEAST
AccessioniPrimary (citable) accession number: P38624
Secondary accession number(s): D6VWH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 171 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The side chain of Thr-20 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
Present with 7250 molecules/cell in log phase SD medium.1 Publication

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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.