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Q5E9K0 (PSB2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. 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 beta type-2

EC=3.4.25.1
Gene names
Name:PSMB2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
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. This subunit has a chymotrypsin-like activity 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.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Proteasome subunit beta type-2
PRO_0000239852

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Secondary structure

.................................. 201
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5E9K0 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 8D195EBA1DBB02DE

FASTA20122,896
        10         20         30         40         50         60 
MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA GDTVQFAEYI 

        70         80         90        100        110        120 
QKNVQLYKMR NGYELSPTAA ANFTRRNLAD YLRSRTPYHV NLLLAGYDEH EGPALYYMDY 

       130        140        150        160        170        180 
LAALAKAPFA AHGYGAFLTL SILDRYYTPT ISREKAVELL RKCLEELQKR FILNLPTFSV 

       190        200 
RIIDRNGIHD LDNISFPKQG S 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]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.
[3]"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 20S PROTEASOME.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT020855 mRNA. Translation: AAX08872.1.
BT020920 mRNA. Translation: AAX08937.1.
BC102367 mRNA. Translation: AAI02368.1.
RefSeqNP_001015615.1. NM_001015615.1.
UniGeneBt.40863.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75K/Y1-201[»]
ProteinModelPortalQ5E9K0.
SMRQ5E9K0. Positions 1-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ5E9K0. 1 interaction.
STRING9913.ENSBTAP00000003072.

Protein family/group databases

MEROPST01.984.

Proteomic databases

PaxDbQ5E9K0.
PRIDEQ5E9K0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000003072; ENSBTAP00000003072; ENSBTAG00000002377.
GeneID516919.
KEGGbta:516919.

Organism-specific databases

CTD5690.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00640000091536.
HOGENOMHOG000188743.
HOVERGENHBG000815.
InParanoidQ5E9K0.
KOK02734.
OMAHFVRGEL.
OrthoDBEOG7N63NQ.
TreeFamTF106219.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5E9K0.
NextBio20872333.

Entry information

Entry namePSB2_BOVIN
AccessionPrimary (citable) accession number: Q5E9K0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 15, 2005
Last modified: June 11, 2014
This is version 75 of the entry and version 1 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