Reviewed,
UniProtKB/Swiss-Prot Q9R1P4 (PSA1_MOUSE)
Last modified
November 3, 2009.
Version 77.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Proteasome subunit alpha type-1 EC=3.4.25.1 Alternative name(s): Proteasome component C2 Macropain subunit C2 Multicatalytic endopeptidase complex subunit C2 Proteasome nu chain | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 263 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | The proteasome is a multicatalytic proteinase complex which 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. The proteasome has an ATP-dependent proteolytic activity. |
| Catalytic activity | Cleavage of peptide bonds with very broad specificity. |
| Subunit structure | 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. |
| Subcellular location | |
| Post-translational modification | C-terminal extension is partially cleaved off by limited proteolysis leading to a conversion of the proteasome from its latent into its active form. |
| Sequence similarities | Belongs to the peptidase T1A family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus Proteasome |
| Molecular function | Hydrolase Protease Threonine protease |
| PTM | Acetylation Isopeptide bond Phosphoprotein Ubl conjugation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complexInferred from electronic annotation. Source: InterPro |
| Molecular function | protein binding Inferred from physical interaction. Source: IntAct threonine-type endopeptidase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| NOTCH3 | Q9UM47 | 1 | EBI-991653,EBI-1236377 | From a different organism. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 263 | 263 | Proteasome subunit alpha type-1 | PRO_0000124062 | |||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||
| Modified residue | 14 | 1 | Phosphoserine By similarity | ||||||
| Cross-link | 115 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
| Cross-link | 208 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete primary structure of mouse 20S proteasomes." Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N., Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J. Immunogenetics 49:835-842(1999) [PubMed: 10436176] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: B10.A. |
| [2] | "The mouse Psma1 gene coding for the alpha-type C2 proteasome subunit: structural and functional analysis, mapping, and colocalization with Pde3b on mouse chromosome 7." Hopitzan A., Himmelbauer H., Spevak W., Castanon M.J. Genomics 66:313-323(2000) [PubMed: 10873386] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Skeletal muscle. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N-3. Tissue: Mammary gland. |
| [4] | Lubec G., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 63-82 AND 97-107, MASS SPECTROMETRY. Tissue: Brain and Hippocampus. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF060088 mRNA. Translation: AAD50533.1. AJ272019 mRNA. Translation: CAB95966.1. AJ272272 Genomic DNA. Translation: CAB95969.1. BC005762 mRNA. Translation: AAH05762.1. | |
| IPI | IPI00283862. |
| RefSeq | NP_036095.1. |
| UniGene | Mm.121265 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1RYP based on UniProtKB P40302. |
| SMR | Q9R1P4. Positions 4-241. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9R1P4. 18 interactions. |
| STRING | Q9R1P4. |
Protein family/group databases | |
| MEROPS | T01.976. |
PTM databases | |
| PhosphoSite | Q9R1P4. |
2-D gel databases | |
| REPRODUCTION-2DPAGE | Q9R1P4. |
Proteomic databases | |
| PRIDE | Q9R1P4. |
Genome annotation databases | |
| Ensembl | ENSMUST00000033008; ENSMUSP00000033008; ENSMUSG00000030751; Mus musculus. [Genome view] |
| GeneID | 26440. |
| KEGG | mmu:26440. |
| NMPDR | fig|10090.3.peg.17468. |
| UCSC | uc009jhy.1. mouse. |
Organism-specific databases | |
| CTD | 26440. |
| MGI | MGI:1347005. Psma1. |
Phylogenomic databases | |
| HOGENOM | Q9R1P4. |
| HOVERGEN | Q9R1P4. |
| OMA | YAVEAMK. |
Enzyme and pathway databases | |
| BRENDA | 3.4.25.1. 244. |
Gene expression databases | |
| ArrayExpress | Q9R1P4. |
| Bgee | Q9R1P4. |
| Genevestigator | Q9R1P4. |
| GermOnline | ENSMUSG00000030751. Mus musculus. |
Family and domain databases | |
| InterPro | IPR000426. Proteasome_asu_CS. IPR001353. Proteasome_sua/b. [Graphical view] |
| Pfam | PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view] |
| PROSITE | PS00388. PROTEASOME_A. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 304517. |
| SOURCE | Search... |
Entry information
| Entry name | PSA1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9R1P4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


