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P28075 (PSB5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 113. 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-5

EC=3.4.25.1
Alternative name(s):
Macropain epsilon chain
Multicatalytic endopeptidase complex epsilon chain
Proteasome chain 6
Proteasome epsilon chain
Proteasome subunit X
Gene names
Name:Psmb5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length263 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 unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib By similarity. Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway 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. This subunit can be displaced by the equivalent immune-specific subunit PSMB8. Directly interacts with POMP By similarity. Interacts with ABCB1 By similarity.

Subcellular location

Cytoplasm. Nucleus.

Induction

Down-regulated by theophylline (THP) and up-regulated by 1,3-dinitrobenzene (DNB), two reprotoxic agents thought to induce infertility. Ref.4

Sequence similarities

Belongs to the peptidase T1B family.

Sequence caution

The sequence BAA08204.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA08204.1 differs from that shown. Reason: Sequencing error.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5959Removed in mature form
PRO_0000026593
Chain60 – 263204Proteasome subunit beta type-5
PRO_0000026594

Sites

Active site601Nucleophile By similarity
Binding site1081Bortezomib; via amide nitrogen By similarity

Experimental info

Sequence conflict621T → I AA sequence Ref.3
Sequence conflict691H → E AA sequence Ref.3
Sequence conflict731V → L AA sequence Ref.3
Sequence conflict831P → A in EDM14180. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P28075 [UniParc].

Last modified April 29, 2008. Version 3.
Checksum: 317FC0C827FE65CA

FASTA26328,585
        10         20         30         40         50         60 
MALASVLQRP MPVNQHGFFG LGGRADLLDL GPGSPGDGLS LAAPSWGVPE EPRIEMLHGT 

        70         80         90        100        110        120 
TTLAFKFQHG VIVAADSRAT AGPYIASQTV KKVIEINPYL LGTMAGGAAD CSFWERLLAR 

       130        140        150        160        170        180 
QCRIYELRNK ERISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI 

       190        200        210        220        230        240 
SGTAFSVGSG SVYAFGVMDR GYSYDLQVEE AYDLARRAIY QATYRDAYSG GAVNLYHVRE 

       250        260 
DGWIRVSSDN VADLHDKYTS SIP 

« Hide

References

« Hide 'large scale' references
[1]Yokota K.Y., Tanaka K.
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[3]"N-terminal sequence similarities between components of the multicatalytic proteinase complex."
Lilley K.S., Davison M.D., Rivett A.J.
FEBS Lett. 262:327-329(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 60-77.
[4]"Differential expression of genes encoding constitutive and inducible 20S proteasomal core subunits in the testis and epididymis of theophylline- or 1,3-dinitrobenzene-exposed rats."
Tengowski M.W., Feng D., Sutovsky M., Sutovsky P.
Biol. Reprod. 76:149-163(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY THP AND DNB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D45247 mRNA. Translation: BAA08204.1. Sequence problems.
CH474049 Genomic DNA. Translation: EDM14180.1.
PIRS09087.
RefSeqNP_001099197.2. NM_001105727.2.
UniGeneRn.2.

3D structure databases

ProteinModelPortalP28075.
SMRP28075. Positions 60-259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248073. 1 interaction.
IntActP28075. 1 interaction.
STRING10116.ENSRNOP00000018005.

Protein family/group databases

MEROPST01.P01.

PTM databases

PhosphoSiteP28075.

Proteomic databases

PaxDbP28075.
PRIDEP28075.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29425.
KEGGrno:29425.
UCSCRGD:61879. rat.

Organism-specific databases

CTD5693.
RGD61879. Psmb5.

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091082.
HOVERGENHBG108297.
InParanoidP28075.
KOK02737.
PhylomeDBP28075.

Gene expression databases

GenevestigatorP28075.

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...

Other

NextBio609128.

Entry information

Entry namePSB5_RAT
AccessionPrimary (citable) accession number: P28075
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: April 29, 2008
Last modified: June 11, 2014
This is version 113 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