P61289 · PSME3_HUMAN
- ProteinProteasome activator complex subunit 3
- GenePSME3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids254 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1 inhibition (PubMed:25361978).
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 | membrane | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | proteasome activator complex | |
Cellular Component | proteasome complex | |
Molecular Function | endopeptidase activator activity | |
Molecular Function | identical protein binding | |
Molecular Function | MDM2/MDM4 family protein binding | |
Molecular Function | p53 binding | |
Biological Process | apoptotic process | |
Biological Process | negative regulation of extrinsic apoptotic signaling pathway | |
Biological Process | regulation of G1/S transition of mitotic cell cycle | |
Biological Process | regulation of proteasomal protein catabolic process |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProteasome activator complex subunit 3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP61289
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 188 | Assembles into less stable hexamers/heptamers and therefore impairs specificity of activation of trypsin-like subunits of the proteasome. | ||||
Sequence: K → E, D, A, C, N, Q, H, F, S, I, or P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 188 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_0000161789 | 2-254 | UniProt | Proteasome activator complex subunit 3 | |||
Sequence: ASLLKVDQEVKLKVDSFRERITSEAEDLVANFFPKKLLELDSFLKEPILNIHDLTQIHSDMNLPVPDPILLTNSHDGLDGPTYKKRRLDECEEAFQGTKVFVMPNGMLKSNQQLVDIIEKVKPEIRLLIEKCNTVKMWVQLLIPRIEDGNNFGVSIQEETVAELRTVESEAASYLDQISRYYITRAKLVSKIAKYPHVEDYRRTVTEIDEKEYISLRLIISELRNQYVTLHDMILKNIEKIKRPRSSNAETLY | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 17 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 24 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 24 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 43 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 195 | UniProt | N6-acetyllysine; by P300/CBP | ||||
Sequence: K | |||||||
Modified residue | 247 | UniProt | Phosphoserine; by CHEK2 | ||||
Sequence: S |
Post-translational modification
Phosphorylated by MAP3K3 (By similarity).
Phosphorylation at Ser-247 promotes its association with CCAR2
Phosphorylation at Ser-247 promotes its association with CCAR2
Acetylation at the major site Lys-195 is important for oligomerization and ability to degrade its target substrates. Deacetylated by SIRT1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Up-regulated in thyroid carcinoma cells.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homoheptamer; the stability of the heptamer is essential for the specific activation of the trypsine-like subunit and inhibition of the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits of the proteasome. Interacts with p53/TP53 and MDM2. Interacts with MAP3K3 (By similarity).
Associates with the proteasome. Interacts with CCAR2. Interacts with PSME3IP1 (via C-terminus); the interaction is direct and promotes the association of PSME3 with the 20S proteasome (PubMed:29934401).
Interacts with COIL; the interaction is inhibited by PSME3IP1 (PubMed:29934401).
Associates with the proteasome. Interacts with CCAR2. Interacts with PSME3IP1 (via C-terminus); the interaction is direct and promotes the association of PSME3 with the 20S proteasome (PubMed:29934401).
Interacts with COIL; the interaction is inhibited by PSME3IP1 (PubMed:29934401).
(Microbial infection) Interacts with human cytomegalovirus UL27.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P61289-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length254
- Mass (Da)29,506
- Last updated2004-05-10 v1
- Checksum116FAB47D60A26C0
P61289-2
- Name2
- Differences from canonical
- 135-135: T → TPSGKGPHICFDLQ
P61289-3
- Name3
- Differences from canonical
- 1-13: MASLLKVDQEVKL → MEKWILKKIKYLQSGGLSASYYSY
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_055047 | 1-13 | in isoform 3 | |||
Sequence: MASLLKVDQEVKL → MEKWILKKIKYLQSGGLSASYYSY | ||||||
Sequence conflict | 25 | in Ref. 2; AAB60335 | ||||
Sequence: E → K | ||||||
Sequence conflict | 94 | in Ref. 10; AAA93227 | ||||
Sequence: E → K | ||||||
Alternative sequence | VSP_004516 | 135 | in isoform 2 | |||
Sequence: T → TPSGKGPHICFDLQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U11292 EMBL· GenBank· DDBJ | AAB60335.1 EMBL· GenBank· DDBJ | mRNA | ||
BT019386 EMBL· GenBank· DDBJ | AAV38193.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292618 EMBL· GenBank· DDBJ | BAF85307.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074999 EMBL· GenBank· DDBJ | BAG52046.1 EMBL· GenBank· DDBJ | mRNA | ||
AC016889 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471152 EMBL· GenBank· DDBJ | EAW60893.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001423 EMBL· GenBank· DDBJ | AAH01423.1 EMBL· GenBank· DDBJ | mRNA | ||
BC002684 EMBL· GenBank· DDBJ | AAH02684.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008020 EMBL· GenBank· DDBJ | AAH08020.1 EMBL· GenBank· DDBJ | mRNA | ||
U25756 EMBL· GenBank· DDBJ | AAA93227.1 EMBL· GenBank· DDBJ | Genomic DNA |