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P40112 (PSB3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 109. 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-3

EC=3.4.25.1
Alternative name(s):
Proteasome chain 13
Proteasome component C10-II
Proteasome theta chain
Gene names
Name:Psmb3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length205 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.

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. Nucleus.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 205204Proteasome subunit beta type-3
PRO_0000148059

Amino acid modifications

Modified residue21N-acetylserine Ref.4
Modified residue771N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P40112 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 2197685F3089F7FD

FASTA20522,965
        10         20         30         40         50         60 
MSVMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY IGLAGLATDV 

        70         80         90        100        110        120 
QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF GPYYTEPVIA GLDPKTFKPF 

       130        140        150        160        170        180 
ICSLDLIGCP MVTDDFVVSG TCSEQMYGMC ESLWEPNMDP EHLFETISQA MLNAVDRDAV 

       190        200 
SGMGVIVHII EKDKITTRTL KARMD 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning of rat proteasome subunit RC10-II, assumed to be responsible for trypsin-like catalytic activity."
Nishimura C., Tamura T., Akioka H., Tokunaga F., Tanaka K., Ichihara A.
FEBS Lett. 336:462-466(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 119-143.
Tissue: Embryonic brain and Liver.
[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].
Tissue: Brain.
[3]Lubec G., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 28-41; 49-66 AND 100-115, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[4]Lubec G., Chen W.-Q.
Submitted (FEB-2007) to UniProtKB
Cited for: ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D21800 mRNA. Translation: BAA04824.1.
BC084723 mRNA. Translation: AAH84723.1.
PIRS40468.
RefSeqNP_058981.1. NM_017285.1.
UniGeneRn.94551.

3D structure databases

ProteinModelPortalP40112.
SMRP40112. Positions 2-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP40112. 1 interaction.
MINTMINT-4569088.
STRING10116.ENSRNOP00000017377.

Protein family/group databases

MEROPST01.983.

PTM databases

PhosphoSiteP40112.

2D gel databases

World-2DPAGE0004:P40112.

Proteomic databases

PaxDbP40112.
PRIDEP40112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29676.
KEGGrno:29676.
UCSCRGD:61875. rat.

Organism-specific databases

CTD5691.
RGD61875. Psmb3.

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000090523.
HOVERGENHBG004446.
InParanoidP40112.
KOK02735.
PhylomeDBP40112.

Gene expression databases

GenevestigatorP40112.

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

NextBio610015.
PROP40112.

Entry information

Entry namePSB3_RAT
AccessionPrimary (citable) accession number: P40112
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 109 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