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O70435 (PSA3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha type-3

EC=3.4.25.1
Alternative name(s):
Macropain subunit C8
Multicatalytic endopeptidase complex subunit C8
Proteasome component C8
Proteasome subunit K
Gene names
Name:Psma3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.10

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. Interacts with AURKB. Ref.4 Ref.10

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Detected in liver (at protein level). Ref.10

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Amino acid modifications

Modified residue21N-acetylserine Ref.4
Modified residue571N6-acetyllysine Ref.9
Modified residue2061N6-acetyllysine By similarity
Modified residue2301N6-acetyllysine By similarity
Modified residue2431Phosphoserine By similarity
Modified residue2501Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8

Secondary structure

........................................ 255
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O70435 [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] [Europe PMC] [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]"Mapping the murine cardiac 26S proteasome complexes."
Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J., Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.
Circ. Res. 99:362-371(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX, ACETYLATION AT SER-2.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[10]"Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity."
Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M., Groll M.
Cell 148:727-738(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF055983 mRNA. Translation: AAC12943.1.
AF060089 mRNA. Translation: AAD50534.1.
RefSeqNP_035314.3. NM_011184.4.
UniGeneMm.296338.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90F/T/h/v1-255[»]
3UNEX-ray3.20F/T/h/v1-255[»]
3UNFX-ray2.90F/T1-255[»]
3UNHX-ray3.20F/T1-255[»]
ProteinModelPortalO70435.
SMRO70435. Positions 2-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202417. 1 interaction.
IntActO70435. 9 interactions.

Protein family/group databases

MEROPST01.977.

PTM databases

PhosphoSiteO70435.

Proteomic databases

PaxDbO70435.
PRIDEO70435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000160027; ENSMUSP00000125548; ENSMUSG00000060073.
GeneID19167.
KEGGmmu:19167.
UCSCuc007ntz.2. mouse.

Organism-specific databases

CTD5684.
MGIMGI:104883. Psma3.

Phylogenomic databases

eggNOGCOG0638.
HOVERGENHBG105566.
InParanoidO70435.
KOK02727.
OMAVPDGRHF.
OrthoDBEOG73JKW6.
PhylomeDBO70435.
TreeFamTF106208.

Enzyme and pathway databases

ReactomeREACT_102124. Immune System.

Gene expression databases

BgeeO70435.
GenevestigatorO70435.

Family and domain databases

InterProIPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio295834.
PROO70435.
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: April 16, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot