P25787 · PSA2_HUMAN
- ProteinProteasome subunit alpha type-2
- GenePSMA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids234 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 | extracellular region | |
Cellular Component | ficolin-1-rich granule lumen | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | P-body | |
Cellular Component | proteasome complex | |
Cellular Component | proteasome core complex | |
Cellular Component | proteasome core complex, alpha-subunit complex | |
Cellular Component | secretory granule lumen | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | response to virus |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProteasome subunit alpha 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 accessionP25787
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_036278 | 110 | in a colorectal cancer sample; somatic mutation | |||
Sequence: L → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 127 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 initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000124077 | 2-234 | UniProt | Proteasome subunit alpha type-2 | |||
Sequence: AERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA | |||||||
Modified residue | 6 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 7 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 14 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 16 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 24 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 70 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 76 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 76 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 77 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 97 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 121 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 171 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 222 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated on tyrosine residues; which may be important for nuclear import.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Induction
Down-regulated by antioxidants BO-653 and probucol. Down-regulated in response to enterovirus 71 (EV71) infection (at protein level).
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.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P25787 | ORF9b Q6S8E0 | 2 | EBI-603262, EBI-25489144 | |
BINARY | P25787 | PSMA1 P25786 | 20 | EBI-603262, EBI-359352 | |
BINARY | P25787 | PSMA3 P25788 | 6 | EBI-603262, EBI-348380 | |
BINARY | P25787 | PSMA4 P25789 | 12 | EBI-603262, EBI-359310 | |
BINARY | P25787 | PSMA6 P60900 | 10 | EBI-603262, EBI-357793 | |
BINARY | P25787 | PSMA7 O14818 | 9 | EBI-603262, EBI-603272 | |
BINARY | P25787 | PSMD4 P55036 | 2 | EBI-603262, EBI-359318 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length234
- Mass (Da)25,899
- Last updated2007-01-23 v2
- Checksum63CB56A233583836
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BT36 | H3BT36_HUMAN | PSMA2 | 48 | ||
C9JCK5 | C9JCK5_HUMAN | PSMA2 | 164 | ||
A0A024RA52 | A0A024RA52_HUMAN | PSMA2 | 234 | ||
H7C3A7 | H7C3A7_HUMAN | PSMA2 | 18 | ||
A0A7I2YQP7 | A0A7I2YQP7_HUMAN | 156 | |||
A0A7I2V2H3 | A0A7I2V2H3_HUMAN | 182 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D00760 EMBL· GenBank· DDBJ | BAA00657.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290654 EMBL· GenBank· DDBJ | BAF83343.1 EMBL· GenBank· DDBJ | mRNA | ||
CR450317 EMBL· GenBank· DDBJ | CAG29313.1 EMBL· GenBank· DDBJ | mRNA | ||
CH236951 EMBL· GenBank· DDBJ | EAL24005.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471073 EMBL· GenBank· DDBJ | EAW94152.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002900 EMBL· GenBank· DDBJ | AAH02900.2 EMBL· GenBank· DDBJ | mRNA | ||
BC047697 EMBL· GenBank· DDBJ | AAH47697.1 EMBL· GenBank· DDBJ | mRNA |