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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: -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.

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

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

Keywordsi

Molecular functionHydrolase, 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-187577 SCF(Skp2)-mediated degradation of p27/p21
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-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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP38624
PRIDEiP38624

2D gel databases

UCD-2DPAGEiP38624

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, 117 interactors
ComplexPortaliCPX-2262 26S Proteasome complex
DIPiDIP-1527N
IntActiP38624, 23 interactors
MINTiP38624
STRINGi4932.YJL001W

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/N20-215[»]
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[»]
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[»]
5L52X-ray2.70N/b20-215[»]
5L54X-ray2.80N/b20-215[»]
5L55X-ray2.90N/b20-215[»]
5L5AX-ray2.40N/b20-215[»]
5L5BX-ray2.80N/b20-215[»]
5L5DX-ray2.80N/b20-215[»]
5L5EX-ray2.90N/b20-215[»]
5L5FX-ray2.50N/b20-215[»]
5L5HX-ray2.60N/b20-215[»]
5L5IX-ray2.90N/b20-215[»]
5L5JX-ray2.90N/b20-215[»]
5L5OX-ray2.60N/b20-215[»]
5L5PX-ray2.80N/b20-215[»]
5L5QX-ray2.80N/b20-215[»]
5L5RX-ray2.90N/b20-215[»]
5L5SX-ray2.60N/b20-215[»]
5L5TX-ray2.90N/b20-215[»]
5L5UX-ray2.60N/b20-215[»]
5L5VX-ray2.70N/b20-215[»]
5L5WX-ray2.80N/b20-215[»]
5L5XX-ray2.90N/b20-215[»]
5L5YX-ray2.70N/b20-215[»]
5L5ZX-ray2.70N/b20-215[»]
5L60X-ray2.70N/b20-215[»]
5L61X-ray2.80N/b20-215[»]
5L62X-ray2.80N/b20-215[»]
5L63X-ray2.70N/b20-215[»]
5L64X-ray2.70N/b20-215[»]
5L65X-ray2.90N/b20-215[»]
5L66X-ray2.80N/b20-215[»]
5L67X-ray2.60N/b20-215[»]
5L68X-ray2.80N/b20-215[»]
5L69X-ray2.70N/b20-215[»]
5L6AX-ray2.80N/b20-215[»]
5L6BX-ray2.60N/b20-215[»]
5L6CX-ray2.60N/b20-215[»]
5LAIX-ray2.50N/b20-215[»]
5LAJX-ray2.90N/b20-215[»]
5LTTX-ray2.70N/b20-215[»]
5M2BX-ray2.70N/b20-215[»]
5MP9electron microscopy4.101/h1-215[»]
5MPAelectron microscopy4.501/h1-215[»]
5MPBelectron microscopy7.801/h1-215[»]
5MPCelectron microscopy7.701/h1-215[»]
5NIFX-ray3.00H/V1-215[»]
5WVIelectron microscopy6.301/b1-215[»]
5WVKelectron microscopy4.201/b1-215[»]
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
OMAiHDRIYCC
OrthoDBiEOG092C4SID

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR000243 Pept_T1A_subB
IPR037559 Proteasome_beta_Pre3
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF4 PTHR11599:SF4, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PRINTSiPR00141 PROTEASOME
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00854 PROTEASOME_BETA_1, 1 hit
PS51476 PROTEASOME_BETA_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPSB1_YEAST
AccessioniPrimary (citable) accession number: P38624
Secondary accession number(s): D6VWH4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1995
Last modified: June 20, 2018
This is version 186 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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