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Q3T0Y5 (PSA2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-2

EC=3.4.25.1
Gene names
Name:PSMA2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length234 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. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation By similarity.

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 By similarity. Nucleus By similarity. CytoplasmP-body By similarity. Note: Colocalizes with TRIM5 in the cytoplasmic bodies By similarity.

Post-translational modification

Phosphorylated on tyrosine residues; which may be important for nuclear import By similarity.

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 234233Proteasome subunit alpha type-2
PRO_0000239865

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue701N6-acetyllysine By similarity
Modified residue761Phosphotyrosine By similarity
Modified residue1711N6-acetyllysine By similarity

Secondary structure

.................................. 234
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q3T0Y5 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 63CB56A233583836

FASTA23425,899
        10         20         30         40         50         60 
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER 

        70         80         90        100        110        120 
SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE 

       130        140        150        160        170        180 
YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE 

       190        200        210        220        230 
DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVKDYL AAIA 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[2]"The structure of the mammalian 20S proteasome at 2.75 A resolution."
Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., Tsukihara T.
Structure 10:609-618(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC102206 mRNA. Translation: AAI02207.1.
RefSeqNP_001029834.1. NM_001034662.2.
UniGeneBt.49020.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75B/P2-234[»]
ProteinModelPortalQ3T0Y5.
SMRQ3T0Y5. Positions 2-234.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000001309.

Protein family/group databases

MEROPST01.972.

Proteomic databases

PaxDbQ3T0Y5.
PRIDEQ3T0Y5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000001309; ENSBTAP00000001309; ENSBTAG00000000990.
GeneID539141.
KEGGbta:539141.

Organism-specific databases

CTD5683.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074870.
HOGENOMHOG000091085.
HOVERGENHBG003005.
InParanoidQ3T0Y5.
KOK02726.
OMAWKATALG.
OrthoDBEOG71VSTG.
TreeFamTF106207.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000426. 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]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ3T0Y5.
NextBio20877807.

Entry information

Entry namePSA2_BOVIN
AccessionPrimary (citable) accession number: Q3T0Y5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 77 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