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Reviewed, UniProtKB/Swiss-Prot O70435 (PSA3_MOUSE)

Last modified November 3, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Proteasome subunit alpha type-3
    EC=3.4.25.1
Alternative name(s):
    Proteasome component C8
    Macropain subunit C8
    Multicatalytic endopeptidase complex subunit C8
    Proteasome subunit K
Gene names
Name: Psma3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cytoplasm. Nucleus.

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 255254Proteasome subunit alpha type-3
PRO_0000124092

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue571N6-acetyllysine By similarity
Modified residue1101N6-acetyllysine By similarity
Modified residue1611Phosphotyrosine By similarity
Modified residue2061N6-acetyllysine By similarity
Modified residue2301N6-acetyllysine By similarity
Modified residue2381N6-acetyllysine By similarity
Modified residue2431Phosphoserine Ref.5
Modified residue2501Phosphoserine Ref.5 Ref.4 Ref.6 Ref.7 Ref.8

Sequences

Sequence LengthMass (Da)Tools
O70435-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CFB4405E143CEB23

FASTA25528,405
        10         20         30         40         50         60 
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE 

        70         80         90        100        110        120 
EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV 

       130        140        150        160        170        180 
HAYTLYSAVR PFGCSFMLGS YSANDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL 

       190        200        210        220        230        240 
QMKEMTCRDV VKEVAKIIYI VHDEVKDKAF ELELSWVGEL TKGRHEIVPK DIREEAEKYA 

       250 
KESLKEEDES DDDNM 

« Hide

References

« Hide 'large scale' references
[1]Gao Y., Simons M.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: BALB/c.
[3]Lubec G., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 73-86.
Tissue: Brain.
[4]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY.
Tissue: Liver.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-250, MASS SPECTROMETRY.
Tissue: Liver.
[6]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed: 18630941] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY.
Tissue: Liver.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY.
Tissue: Macrophage.
[8]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF055983 mRNA. Translation: AAC12943.1.
AF060089 mRNA. Translation: AAD50534.1.
IPIIPI00331644.
UniGeneMm.296338

3D structure databases

HSSPHSSP built from PDB template 1RYP based on UniProtKB P21242.
ModBaseSearch...

Protein-protein interaction databases

STRINGO70435.

Protein family/group databases

MEROPST01.977.

PTM databases

PhosphoSiteO70435.

Proteomic databases

PRIDEO70435.

Genome annotation databases

EnsemblENSMUST00000071704; ENSMUSP00000071624; ENSMUSG00000060073; Mus musculus. [Genome view]

Organism-specific databases

MGIMGI:104883. Psma3.

Phylogenomic databases

HOGENOMO70435.
HOVERGENO70435.
OMALSWVGEI.

Enzyme and pathway databases

BRENDA3.4.25.1. 244.

Gene expression databases

ArrayExpressO70435.
BgeeO70435.
GenevestigatorO70435.
GermOnlineENSMUSG00000060073. Mus musculus.

Family and domain databases

InterProIPR000426. Proteasome_asu_CS.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
PROSITEPS00388. PROTEASOME_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry namePSA3_MOUSE
AccessionPrimary (citable) accession number: O70435
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents