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Protein

Proteasome subunit beta type-5

Gene

PRE2

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. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib.
This subunit is necessary for chymotryptic activity and degradation of ubiquitinated proteins.

Miscellaneous

The side chain of Thr-76 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
Present with 8530 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 sitei76Nucleophile1 Publication1
Binding sitei124Bortezomib; via amide nitrogen1

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 core complex assembly Source: SGD
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciYEAST:G3O-34243-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

MEROPSiT01.012

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-5 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PRE2
Multicatalytic endopeptidase complex subunit PRE2
Proteasome component PRE2
Proteinase YSCE subunit PRE2
Gene namesi
Name:PRE2
Synonyms:DOA3, PRG1
Ordered Locus Names:YPR103W
ORF Names:P8283.10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR103W
SGDiS000006307 PRE2

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi126D → N in DOA3-1; decrease in activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4659

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000266111 – 75Removed in mature form1 PublicationAdd BLAST75
ChainiPRO_000002661276 – 287Proteasome subunit beta type-5Add BLAST212

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiP30656
PaxDbiP30656
PRIDEiP30656

PTM databases

iPTMnetiP30656

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

Show more details

Protein-protein interaction databases

BioGridi36269, 715 interactors
ComplexPortaliCPX-2262 26S Proteasome complex
DIPiDIP-2806N
IntActiP30656, 21 interactors
MINTiP30656
STRINGi4932.YPR103W

Chemistry databases

BindingDBiP30656

Structurei

Secondary structure

1287
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi78 – 83Combined sources6
Beta strandi86 – 91Combined sources6
Beta strandi95 – 97Combined sources3
Beta strandi100 – 104Combined sources5
Beta strandi109 – 113Combined sources5
Beta strandi116 – 119Combined sources4
Beta strandi121 – 123Combined sources3
Helixi124 – 145Combined sources22
Helixi151 – 164Combined sources14
Turni165 – 167Combined sources3
Beta strandi172 – 180Combined sources9
Turni181 – 183Combined sources3
Beta strandi184 – 191Combined sources8
Turni192 – 194Combined sources3
Beta strandi196 – 198Combined sources3
Beta strandi200 – 205Combined sources6
Helixi208 – 218Combined sources11
Helixi225 – 242Combined sources18
Beta strandi243 – 246Combined sources4
Beta strandi248 – 256Combined sources9
Beta strandi259 – 267Combined sources9
Helixi268 – 279Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20L/Z76-287[»]
1G0UX-ray2.40K/Y76-287[»]
1G65X-ray2.25K/Y76-287[»]
1JD2X-ray3.00K/R76-287[»]
1RYPX-ray1.90L/Z76-287[»]
1Z7QX-ray3.22L/Z76-287[»]
2F16X-ray2.80K/Y76-287[»]
2FAKX-ray2.80K/Y76-287[»]
2GPLX-ray2.81K/Y76-287[»]
2ZCYX-ray2.90K/Y76-287[»]
3BDMX-ray2.70K/Y76-287[»]
3D29X-ray2.60K/Y76-287[»]
3DY3X-ray2.81K/Y76-287[»]
3DY4X-ray2.80K/Y76-287[»]
3E47X-ray3.00K/Y76-287[»]
3GPJX-ray2.70K/Y76-287[»]
3GPTX-ray2.41K/Y76-287[»]
3GPWX-ray2.50K/Y76-287[»]
3HYEX-ray2.50K/Y76-287[»]
3JCOelectron microscopy4.807/l1-287[»]
3JCPelectron microscopy4.607/l1-287[»]
3MG0X-ray2.68K/Y76-287[»]
3MG4X-ray3.11K/Y76-287[»]
3MG6X-ray2.60K/Y76-287[»]
3MG7X-ray2.78K/Y76-287[»]
3MG8X-ray2.59K/Y76-287[»]
3NZJX-ray2.40K/Y1-287[»]
3NZWX-ray2.50K/Y1-287[»]
3NZXX-ray2.70K/Y1-287[»]
3OEUX-ray2.60K/Y76-287[»]
3OEVX-ray2.85K/Y76-287[»]
3OKJX-ray2.70K/Y76-287[»]
3SDIX-ray2.65K/Y76-287[»]
3SDKX-ray2.70K/Y76-287[»]
3SHJX-ray2.80K/Y76-287[»]
3TDDX-ray2.70K/Y76-287[»]
3UN4X-ray3.40K/Y76-287[»]
3UN8X-ray2.70K/Y76-287[»]
3WXRX-ray3.15L/Z1-287[»]
4CR2electron microscopy7.7051-287[»]
4CR3electron microscopy9.3051-287[»]
4CR4electron microscopy8.8051-287[»]
4EU2X-ray2.51L/Z76-287[»]
4FZCX-ray2.80K/Y76-287[»]
4FZGX-ray3.00K/Y76-287[»]
4G4SX-ray2.49L76-287[»]
4GK7X-ray2.80K/Y76-287[»]
4HNPX-ray2.80K/Y76-287[»]
4HRCX-ray2.80K/Y76-287[»]
4HRDX-ray2.80K/Y76-287[»]
4INRX-ray2.70K/Y76-287[»]
4INTX-ray2.90K/Y76-287[»]
4INUX-ray3.10K/Y76-287[»]
4J70X-ray2.80K/Y76-287[»]
4JSQX-ray2.80K/Y76-287[»]
4JSUX-ray2.90K/Y76-287[»]
4JT0X-ray3.10K/Y76-287[»]
4LQIX-ray2.70K/Y76-287[»]
4LTCX-ray2.50K/Y76-287[»]
4NNNX-ray2.50K/Y76-287[»]
4NNWX-ray2.60K/Y76-287[»]
4NO1X-ray2.50K/Y76-287[»]
4NO6X-ray3.00K/Y76-287[»]
4NO8X-ray2.70K/Y76-287[»]
4NO9X-ray2.90K/Y76-287[»]
4Q1SX-ray2.60K/Y76-287[»]
4QBYX-ray3.00K/Y76-287[»]
4QLQX-ray2.40K/Y76-287[»]
4QLSX-ray2.80K/Y76-287[»]
4QLTX-ray2.80K/Y76-287[»]
4QLUX-ray2.80K/Y76-287[»]
4QLVX-ray2.90K/Y76-287[»]
4QUXX-ray3.00K/Y76-287[»]
4QUYX-ray2.80K/Y76-287[»]
4QV0X-ray3.10K/Y76-287[»]
4QV1X-ray2.50K/Y76-287[»]
4QV3X-ray3.00K/Y76-287[»]
4QV4X-ray2.70K/Y76-287[»]
4QV5X-ray2.70K/Y76-287[»]
4QV6X-ray2.80K/Y76-287[»]
4QV7X-ray2.60K/Y76-287[»]
4QV8X-ray2.90K/Y76-287[»]
4QV9X-ray2.60K/Y76-287[»]
4QVLX-ray2.80K/Y76-287[»]
4QVMX-ray2.80K/Y76-287[»]
4QVNX-ray2.90K/Y76-287[»]
4QVPX-ray2.30K/Y76-287[»]
4QVQX-ray2.60K/Y76-287[»]
4QVVX-ray2.80K/Y76-287[»]
4QVWX-ray3.00K/Y76-287[»]
4QVYX-ray2.51K/Y76-287[»]
4QW0X-ray2.90K/Y76-287[»]
4QW1X-ray2.90K/Y76-287[»]
4QW3X-ray2.90K/Y76-287[»]
4QW4X-ray2.80K/Y76-287[»]
4QW5X-ray3.00K/Y76-287[»]
4QW6X-ray2.90K/Y76-287[»]
4QW7X-ray2.70K/Y76-287[»]
4QWFX-ray3.00K/Y76-287[»]
4QWGX-ray2.60K/Y76-287[»]
4QWIX-ray2.60K/Y76-287[»]
4QWJX-ray2.90K/Y76-287[»]
4QWKX-ray2.80K/Y76-287[»]
4QWLX-ray2.60K/Y76-287[»]
4QWRX-ray2.90K/Y76-287[»]
4QWSX-ray3.00K/Y76-287[»]
4QWUX-ray3.00K/Y76-287[»]
4QWXX-ray2.90K/Y76-287[»]
4QXJX-ray2.80K/Y76-287[»]
4QZ0X-ray3.00K/Y76-287[»]
4QZ1X-ray3.00K/Y76-287[»]
4QZ2X-ray2.70K/Y76-287[»]
4QZ3X-ray2.80K/Y76-287[»]
4QZ4X-ray3.00K/Y76-287[»]
4QZ5X-ray2.80K/Y76-287[»]
4QZ6X-ray2.90K/Y76-287[»]
4QZ7X-ray2.80K/Y76-287[»]
4QZWX-ray3.00K/Y76-287[»]
4QZXX-ray2.60K/Y76-287[»]
4QZZX-ray2.90K/Y76-287[»]
4R00X-ray2.80K/Y76-287[»]
4R02X-ray2.50K/Y76-287[»]
4R17X-ray2.10K/Y76-287[»]
4R18X-ray2.40K/Y76-287[»]
4RURX-ray2.50K/Y76-287[»]
4V7OX-ray3.00A2/AP/BL/BZ76-287[»]
4X6ZX-ray2.70L/Z1-287[»]
4Y69X-ray2.90K/Y76-287[»]
4Y6AX-ray2.60K/Y76-287[»]
4Y6VX-ray2.80K/Y76-287[»]
4Y6ZX-ray2.70K/Y76-287[»]
4Y70X-ray2.40K/Y76-287[»]
4Y74X-ray2.70K/Y76-287[»]
4Y75X-ray2.80K/Y76-287[»]
4Y77X-ray2.50K/Y76-287[»]
4Y78X-ray2.80K/Y76-287[»]
4Y7WX-ray2.50K/Y76-287[»]
4Y7XX-ray2.60K/Y76-287[»]
4Y7YX-ray2.40K/Y76-287[»]
4Y80X-ray2.50K/Y76-287[»]
4Y81X-ray2.80K/Y76-287[»]
4Y82X-ray2.80K/Y76-287[»]
4Y84X-ray2.70K/Y76-287[»]
4Y8GX-ray2.60K/Y76-287[»]
4Y8HX-ray2.50K/Y76-287[»]
4Y8IX-ray2.60K/Y76-287[»]
4Y8JX-ray2.70K/Y76-287[»]
4Y8KX-ray2.60K/Y76-287[»]
4Y8LX-ray2.40K/Y76-287[»]
4Y8MX-ray2.80K/Y76-287[»]
4Y8NX-ray2.60K/Y76-287[»]
4Y8OX-ray2.70K/Y76-287[»]
4Y8PX-ray2.80K/Y76-287[»]
4Y8QX-ray2.60K/Y76-287[»]
4Y8RX-ray2.70K/Y76-287[»]
4Y8SX-ray2.70K/Y76-287[»]
4Y8TX-ray2.70K/Y76-287[»]
4Y8UX-ray2.90K/Y76-287[»]
4Y9YX-ray2.80K/Y76-287[»]
4Y9ZX-ray2.80K/Y76-287[»]
4YA0X-ray2.80K/Y76-287[»]
4YA1X-ray2.90K/Y76-287[»]
4YA2X-ray2.70K/Y76-287[»]
4YA3X-ray2.70K/Y76-287[»]
4YA4X-ray2.90K/Y76-287[»]
4YA5X-ray2.50K/Y76-287[»]
4YA7X-ray2.70K/Y76-287[»]
4YA9X-ray2.70K/Y76-287[»]
4Z1LX-ray3.00K/Y76-287[»]
5A5Belectron microscopy9.5051-287[»]
5AHJX-ray2.80K/Y76-287[»]
5BOUX-ray2.60K/Y76-287[»]
5BXLX-ray2.80K/Y76-287[»]
5BXNX-ray2.80K/Y76-287[»]
5CGFX-ray2.80K/Y76-287[»]
5CGGX-ray2.90K/Y76-287[»]
5CGHX-ray2.50K/Y76-287[»]
5CGIX-ray2.80K/Y76-287[»]
5CZ4X-ray2.30K/Y76-287[»]
5CZ5X-ray2.80K/Y76-287[»]
5CZ6X-ray2.70K/Y76-287[»]
5CZ7X-ray2.50K/Y71-287[»]
5CZ8X-ray2.80K/Y67-287[»]
5CZ9X-ray2.90K/Y76-287[»]
5CZAX-ray2.50K/Y76-287[»]
5D0SX-ray2.50K/Y76-287[»]
5D0TX-ray2.60K/Y76-287[»]
5D0VX-ray2.90K/Y70-287[»]
5D0WX-ray2.80K/Y76-287[»]
5D0XX-ray2.60K/Y76-287[»]
5D0ZX-ray2.90K/Y76-287[»]
5DKIX-ray2.80K/Y76-287[»]
5DKJX-ray2.80K/Y76-287[»]
5FG7X-ray2.70K/Y76-287[»]
5FG9X-ray2.60K/Y76-287[»]
5FGAX-ray2.70K/Y76-287[»]
5FGDX-ray2.80K/Y72-287[»]
5FGEX-ray2.60K/Y70-287[»]
5FGFX-ray2.60K/Y74-287[»]
5FGGX-ray2.70K/Y76-287[»]
5FGHX-ray2.80K/Y76-287[»]
5FGIX-ray2.90K/Y76-287[»]
5FHSX-ray2.70K/Y76-287[»]
5JHRX-ray2.90K/Y76-287[»]
5JHSX-ray3.00K/Y76-287[»]
5L52X-ray2.70K/Y76-287[»]
5L54X-ray2.80K/Y76-287[»]
5L55X-ray2.90K/Y76-287[»]
5L5AX-ray2.40K/Y215-287[»]
5L5BX-ray2.80K/Y215-287[»]
5L5DX-ray2.80K/Y215-287[»]
5L5EX-ray2.90K/Y215-287[»]
5L5FX-ray2.50K/Y215-287[»]
5L5HX-ray2.60K/Y215-287[»]
5L5IX-ray2.90K/Y215-287[»]
5L5JX-ray2.90K/Y215-287[»]
5L5OX-ray2.60K/Y215-287[»]
5L5PX-ray2.80K/Y215-287[»]
5L5QX-ray2.80K/Y215-287[»]
5L5RX-ray2.90K/Y215-287[»]
5L5SX-ray2.60K/Y215-287[»]
5L5TX-ray2.90K/Y215-287[»]
5L5UX-ray2.60K/Y215-287[»]
5L5VX-ray2.70K/Y215-287[»]
5L5WX-ray2.80K/Y215-287[»]
5L5XX-ray2.90K/Y215-287[»]
5L5YX-ray2.70K/Y215-287[»]
5L5ZX-ray2.70K/Y215-287[»]
5L60X-ray2.70K/Y215-287[»]
5L61X-ray2.80K/Y211-287[»]
5L62X-ray2.80K/Y215-287[»]
5L63X-ray2.70K/Y215-287[»]
5L64X-ray2.70K/Y215-287[»]
5L65X-ray2.90K/Y215-287[»]
5L66X-ray2.80K/Y215-287[»]
5L67X-ray2.60K/Y215-287[»]
5L68X-ray2.80K/Y215-287[»]
5L69X-ray2.70K/Y215-287[»]
5L6AX-ray2.80K/Y215-287[»]
5L6BX-ray2.60K/Y215-287[»]
5L6CX-ray2.60K/Y215-287[»]
5LAIX-ray2.50K/Y76-287[»]
5LAJX-ray2.90K/Y76-287[»]
5LTTX-ray2.70K/Y215-287[»]
5M2BX-ray2.70K/Y215-287[»]
5MP9electron microscopy4.105/l1-287[»]
5MPAelectron microscopy4.505/l1-287[»]
5MPBelectron microscopy7.805/l1-287[»]
5MPCelectron microscopy7.705/l1-287[»]
5NIFX-ray3.00L/Z1-287[»]
5WVIelectron microscopy6.305/f1-287[»]
5WVKelectron microscopy4.205/f1-287[»]
ProteinModelPortaliP30656
SMRiP30656
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30656

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00510000046395
HOGENOMiHOG000091082
InParanoidiP30656
KOiK02737
OMAiTMCAGVT
OrthoDBiEOG092C4SID

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR000243 Pept_T1A_subB
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
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.

P30656-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAIADSFSV PNRLVKELQY DNEQNLESDF VTGASQFQRL APSLTVPPIA
60 70 80 90 100
SPQQFLRAHT DDSRNPDCKI KIAHGTTTLA FRFQGGIIVA VDSRATAGNW
110 120 130 140 150
VASQTVKKVI EINPFLLGTM AGGAADCQFW ETWLGSQCRL HELREKERIS
160 170 180 190 200
VAAASKILSN LVYQYKGAGL SMGTMICGYT RKEGPTIYYV DSDGTRLKGD
210 220 230 240 250
IFCVGSGQTF AYGVLDSNYK WDLSVEDALY LGKRSILAAA HRDAYSGGSV
260 270 280
NLYHVTEDGW IYHGNHDVGE LFWKVKEEEG SFNNVIG
Length:287
Mass (Da):31,637
Last modified:February 1, 1995 - v3
Checksum:iD0EBAC611F7A4F37
GO

Sequence cautioni

The sequence CAA82203 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti282 – 287FNNVIG → STTLLAK in AAA34906 (PubMed:1452031).Curated6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96667 Genomic DNA Translation: AAA34906.1
X68662 Genomic DNA Translation: CAA48628.1
U32445 Genomic DNA Translation: AAB68073.1
Z28348 Genomic DNA Translation: CAA82203.1 Different initiation.
BK006949 Genomic DNA Translation: DAA11517.1
PIRiA45411
RefSeqiNP_015428.1, NM_001184200.1

Genome annotation databases

EnsemblFungiiYPR103W; YPR103W; YPR103W
GeneIDi856218
KEGGisce:YPR103W

Similar proteinsi

Entry informationi

Entry nameiPSB5_YEAST
AccessioniPrimary (citable) accession number: P30656
Secondary accession number(s): D6W4A1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1995
Last modified: June 20, 2018
This is version 190 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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