P49721 · PSB2_HUMAN
- ProteinProteasome subunit beta type-2
- GenePSMB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids201 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Non-catalytic component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | membrane | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | proteasome complex | |
Cellular Component | proteasome core complex | |
Cellular Component | proteasome core complex, beta-subunit complex | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | response to organic cyclic compound | |
Biological Process | response to organonitrogen compound |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProteasome subunit beta type-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP49721
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 187 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000148043 | 1-201 | UniProt | Proteasome subunit beta type-2 | |||
Sequence: MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 76 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Induction
Up-regulated in ovarian cancer cell lines.
Gene expression databases
Organism-specific databases
Interaction
Subunit
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
(Microbial infection) Interacts with HIV-1 protein Tat.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P49721 | AXIN2 Q9Y2T1 | 3 | EBI-359335, EBI-4400025 | |
BINARY | P49721 | HTT P42858 | 7 | EBI-359335, EBI-466029 | |
BINARY | P49721 | INCA1 Q0VD86 | 3 | EBI-359335, EBI-6509505 | |
BINARY | P49721 | KCTD9 Q7L273 | 3 | EBI-359335, EBI-4397613 | |
BINARY | P49721 | KRT13 A1A4E9 | 3 | EBI-359335, EBI-10171552 | |
BINARY | P49721 | KRTAP19-1 Q8IUB9 | 3 | EBI-359335, EBI-12811111 | |
BINARY | P49721 | KRTAP19-5 Q3LI72 | 3 | EBI-359335, EBI-1048945 | |
BINARY | P49721 | KRTAP19-6 Q3LI70 | 3 | EBI-359335, EBI-12805508 | |
BINARY | P49721 | KRTAP19-7 Q3SYF9 | 3 | EBI-359335, EBI-10241353 | |
BINARY | P49721 | POMP Q9Y244 | 5 | EBI-359335, EBI-696895 | |
BINARY | P49721 | PSMA1 P25786 | 14 | EBI-359335, EBI-359352 | |
BINARY | P49721 | PSMB1 P20618 | 8 | EBI-359335, EBI-372273 | |
BINARY | P49721 | PSMB3 P49720 | 9 | EBI-359335, EBI-603340 | |
BINARY | P49721 | PSMB5 P28074 | 5 | EBI-359335, EBI-357828 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length201
- Mass (Da)22,836
- Last updated1996-10-01 v1
- Checksum04D085D7BAA76130
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A087WVV1 | A0A087WVV1_HUMAN | PSMB2 | 84 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D26599 EMBL· GenBank· DDBJ | BAA05646.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456862 EMBL· GenBank· DDBJ | CAG33143.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007137 EMBL· GenBank· DDBJ | AAP35801.1 EMBL· GenBank· DDBJ | mRNA | ||
AL354864 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL357035 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL157951 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471059 EMBL· GenBank· DDBJ | EAX07406.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX07407.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC101836 EMBL· GenBank· DDBJ | AAI01837.1 EMBL· GenBank· DDBJ | mRNA | ||
BC105126 EMBL· GenBank· DDBJ | AAI05127.1 EMBL· GenBank· DDBJ | mRNA | ||
BC107901 EMBL· GenBank· DDBJ | AAI07902.1 EMBL· GenBank· DDBJ | mRNA |