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Q9R1P3 (PSB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. 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 beta type-2

EC=3.4.25.1
Alternative name(s):
Macropain subunit C7-I
Multicatalytic endopeptidase complex subunit C7-I
Proteasome component C7-I
Gene names
Name:Psmb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.5

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. Ref.4 Ref.5

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Detected in liver (at protein level). Ref.5

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_0000148044

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9R1P3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E9B3121974777958

FASTA20122,906
        10         20         30         40         50         60 
MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA GDTVQFAEYI 

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

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

       190        200 
RVIDKDGIHN LENIAFPKRD S 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: B10.BR.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[3]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 71-85; 127-145 AND 171-198, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[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.
[5]"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
AF060090 mRNA. Translation: AAD50535.1.
BC008265 mRNA. Translation: AAH08265.1.
CCDSCCDS18657.1.
RefSeqNP_036100.3. NM_011970.4.
UniGeneMm.22233.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90J/X/l/z1-201[»]
3UNEX-ray3.20J/X/l/z1-201[»]
3UNFX-ray2.90J/X1-201[»]
3UNHX-ray3.20J/X1-201[»]
ProteinModelPortalQ9R1P3.
SMRQ9R1P3. Positions 1-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204996. 2 interactions.
IntActQ9R1P3. 7 interactions.
MINTMINT-1856775.

Protein family/group databases

MEROPST01.984.

PTM databases

PhosphoSiteQ9R1P3.

2D gel databases

REPRODUCTION-2DPAGEQ9R1P3.

Proteomic databases

MaxQBQ9R1P3.
PaxDbQ9R1P3.
PRIDEQ9R1P3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030642; ENSMUSP00000030642; ENSMUSG00000028837.
GeneID26445.
KEGGmmu:26445.
UCSCuc008utr.2. mouse.

Organism-specific databases

CTD5690.
MGIMGI:1347045. Psmb2.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00640000091536.
HOGENOMHOG000188743.
HOVERGENHBG000815.
InParanoidQ9R1P3.
KOK02734.
OMAHFVRGEL.
OrthoDBEOG7N63NQ.
PhylomeDBQ9R1P3.
TreeFamTF106219.

Gene expression databases

BgeeQ9R1P3.
GenevestigatorQ9R1P3.

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

ChiTaRSPSMB2. mouse.
NextBio304537.
PROQ9R1P3.
SOURCESearch...

Entry information

Entry namePSB2_MOUSE
AccessionPrimary (citable) accession number: Q9R1P3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 123 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

MGD cross-references

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