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Q9PT26 (PSB9_ONCMY) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 68. 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
Gene names
Name:psmb9
Synonyms:lmp2
OrganismOncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Taxonomic identifier8022 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeOncorhynchus

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 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. Component of the immunoproteasome, where it displaces the equivalent houskeeping subunit PSMB6 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the peptidase T1B family.

Ontologies

Keywords
   Biological processImmunity
   Cellular componentCytoplasm
Nucleus
Proteasome
   Molecular functionHydrolase
Protease
Threonine protease
   PTMZymogen
Gene Ontology (GO)
   Biological_processimmune system process

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis involved in cellular protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteasome core complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionthreonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1818Removed in mature form By similarity
PRO_0000026635
Chain19 – 217199Proteasome subunit beta type-9
PRO_0000026636

Sites

Active site191Nucleophile By similarity
Site18 – 192Cleavage; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PT26 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 69E680F35464B671

FASTA21723,406
        10         20         30         40         50         60 
MLDESLEPGW LSEEVKTGTT IIAIEFDGGV VLGSDSRVSA GETVVNRVMN KLSLLHDKIY 

        70         80         90        100        110        120 
CALSGSAADA QTIAEMVNYQ LDVHSIEVGE DPQVRSAATL VKNISYKYKE DLSAHLIVAG 

       130        140        150        160        170        180 
WDKRGGGQVY VTLNGLLSRQ PFAVGGSGSS YVYGFVDAEY RKAMSKEDCQ QFVVNTLSLA 

       190        200        210 
MSRDGSSGGV AYLVTIDEKG AEEKCILGNE LPTFYDQ 

« Hide

References

[1]"Expression, linkage, and polymorphism of MHC-related genes in rainbow trout, Oncorhynchus mykiss."
Hansen J.D., Strassburger P., Thorgaard G.H., Young W.P., Du Pasquier L.
J. Immunol. 163:774-786(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Shasta.
Tissue: Thymocyte.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF115541 mRNA. Translation: AAD53038.1.
UniGeneOmy.11923.

3D structure databases

ProteinModelPortalQ9PT26.
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_ONCMY
AccessionPrimary (citable) accession number: Q9PT26
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 68 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