P30656 · PSB5_YEAST
- ProteinProteasome subunit beta type-5
- GenePRE2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids287 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 a nucleophile, and the N-terminal amino group acts as a proton acceptor.
Present with 8530 molecules/cell in log phase SD medium.
Catalytic activity
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Cellular Component | peroxisome | |
Cellular Component | proteasome complex | |
Cellular Component | proteasome core complex, beta-subunit complex | |
Molecular Function | endopeptidase activity | |
Molecular Function | threonine-type endopeptidase activity | |
Biological Process | proteasomal ubiquitin-independent protein catabolic process | |
Biological Process | proteasome core complex assembly | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProteasome subunit beta type-5
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP30656
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 126 | In DOA3-1; decrease in activity. | ||||
Sequence: D → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for propeptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000026611 | 1-75 | Removed in mature form | |||
Sequence: MQAIADSFSVPNRLVKELQYDNEQNLESDFVTGASQFQRLAPSLTVPPIASPQQFLRAHTDDSRNPDCKIKIAHG | ||||||
Chain | PRO_0000026612 | 76-287 | Proteasome subunit beta type-5 | |||
Sequence: TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
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.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P30656 | BLM10 P43583 | 4 | EBI-14001, EBI-22761 | |
BINARY | P30656 | PRE1 P22141 | 5 | EBI-14001, EBI-13988 | |
BINARY | P30656 | PRE10 P21242 | 4 | EBI-14001, EBI-13963 | |
BINARY | P30656 | PRE3 P38624 | 3 | EBI-14001, EBI-14005 | |
BINARY | P30656 | PRE4 P30657 | 3 | EBI-14001, EBI-13997 | |
BINARY | P30656 | PRE5 P40302 | 3 | EBI-14001, EBI-13955 | |
BINARY | P30656 | PRE6 P40303 | 4 | EBI-14001, EBI-13980 | |
BINARY | P30656 | PRE7 P23724 | 2 | EBI-14001, EBI-13984 | |
BINARY | P30656 | PRE8 P23639 | 2 | EBI-14001, EBI-13959 | |
BINARY | P30656 | PRE9 P23638 | 3 | EBI-14001, EBI-13967 | |
BINARY | P30656 | PUP3 P25451 | 3 | EBI-14001, EBI-13993 | |
BINARY | P30656 | SCL1 P21243 | 9 | EBI-14001, EBI-13975 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length287
- Mass (Da)31,637
- Last updated1995-02-01 v3
- ChecksumD0EBAC611F7A4F37
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 282-287 | in Ref. 1; AAA34906 | ||||
Sequence: FNNVIG → STTLLAK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M96667 EMBL· GenBank· DDBJ | AAA34906.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X68662 EMBL· GenBank· DDBJ | CAA48628.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U32445 EMBL· GenBank· DDBJ | AAB68073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z28348 EMBL· GenBank· DDBJ | CAA82203.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
BK006949 EMBL· GenBank· DDBJ | DAA11517.1 EMBL· GenBank· DDBJ | Genomic DNA |