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O35523 (PSB9_MUSPL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-9

EC=3.4.25.1
Alternative name(s):
Low molecular mass protein 2
Macropain chain 7
Multicatalytic endopeptidase complex chain 7
Proteasome chain 7
Proteasome subunit beta-1i
Really interesting new gene 12 protein
Gene names
Name:Psmb9
Synonyms:Lmp2, Ring12
OrganismMus platythrix (Flat-haired mouse) (Pyromys platythrix)
Taxonomic identifier10101 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusPyromys

Protein attributes

Sequence length219 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. This subunit is involved in antigen processing to generate class I binding peptides.

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. Component of the immunoproteasome, where it displaces the equivalent houskeeping subunit PSMB6. Component of the spermatoproteasome, a form of the proteasome specifically found in testis.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Induction

Up-regulated by interferon gamma (at protein level).

Post-translational modification

Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity By similarity.

Miscellaneous

Encoded in the MHC class II region.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 2020Removed in mature form By similarity
PRO_0000026627
Chain21 – 219199Proteasome subunit beta type-9
PRO_0000026628

Sites

Active site211Nucleophile By similarity
Site20 – 212Cleavage; by autocatalysis By similarity

Amino acid modifications

Modified residue531N6-acetyllysine By similarity
Modified residue1091N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O35523 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 820E9AE4B73BB376

FASTA21923,442
        10         20         30         40         50         60 
MLRAGAPTAG SFRTKEVHTG TTIMAVEFDG GVVVGSDSRV SAGEAVVNRV FDKLSPLHQR 

        70         80         90        100        110        120 
IFCALSGSAA DAQAIADMAA YQLELHGLEL EEPPLVLAAA NVVKNISYKY REDLLAHLIV 

       130        140        150        160        170        180 
AGWDQREGGQ VYGTMGGMLI RQPFTIGGSG SSYIYGYVDA AYKPGMTSEE CRRFTTNAIT 

       190        200        210 
LAMNRDGSSG GVIYLVTITV AGVDHRVILG DELPKFYDE 

« Hide

References

[1]Mizuno K., Saitou N., Tsutiya K., Sagai T., Moriwaki K., Shiroishi T.
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D44459 mRNA. Translation: BAA22580.1.

3D structure databases

ProteinModelPortalO35523.
SMRO35523. Positions 21-216.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPST01.013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000123.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSB9_MUSPL
AccessionPrimary (citable) accession number: O35523
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 80 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