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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: 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 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.

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, 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-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

MEROPSiT01.012.

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

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

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.
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

WithEntry#Exp.IntActNotes
BLM10P435833EBI-14001,EBI-22761

Protein-protein interaction databases

BioGridi36269. 125 interactors.
DIPiDIP-2806N.
IntActiP30656. 20 interactors.
MINTiMINT-489734.

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[»]
4ZZGX-ray3.00L/Z1-287[»]
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[»]
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.
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.

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.

Cross-referencesi

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.

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[»]
4ZZGX-ray3.00L/Z1-287[»]
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[»]
ProteinModelPortaliP30656.
SMRiP30656.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36269. 125 interactors.
DIPiDIP-2806N.
IntActiP30656. 20 interactors.
MINTiMINT-489734.

Chemistry databases

BindingDBiP30656.
ChEMBLiCHEMBL4659.

Protein family/group databases

MEROPSiT01.012.

PTM databases

iPTMnetiP30656.

Proteomic databases

MaxQBiP30656.
PRIDEiP30656.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR103W; YPR103W; YPR103W.
GeneIDi856218.
KEGGisce:YPR103W.

Organism-specific databases

EuPathDBiFungiDB:YPR103W.
SGDiS000006307. PRE2.

Phylogenomic databases

GeneTreeiENSGT00510000046395.
HOGENOMiHOG000091082.
InParanoidiP30656.
KOiK02737.
OMAiTMCAGVT.
OrthoDBiEOG092C4SID.

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-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

EvolutionaryTraceiP30656.
PROiP30656.

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 nameiPSB5_YEAST
AccessioniPrimary (citable) accession number: P30656
Secondary accession number(s): D6W4A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 177 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.