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P33672 (PSB3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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 By similarity
Chain2 – 205204Proteasome subunit beta type-3
PRO_0000148056

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue771N6-acetyllysine By similarity

Experimental info

Sequence conflict891S → C AA sequence Ref.2

Secondary structure

.................................. 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33672 [UniParc].

Last modified June 13, 2006. Version 3.
Checksum: 62551E484D5042FD

FASTA20522,993
        10         20         30         40         50         60 
MSIMSYNGGA 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 TCTEQMYGMC ESLWEPNMDP EHLFETISQA MLNAVDRDAV 

       190        200 
SGMGVIVHII EKDKITTRTL KARMD 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Testis.
[2]"Identification and localization of a cysteinyl residue critical for the trypsin-like catalytic activity of the proteasome."
Dick L.R., Moomaw C.R., Pramanik B.C., DeMartino G.N., Slaughter C.A.
Biochemistry 31:7347-7355(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 14-79; 89-114; 121-141; 160-170 AND 183-205.
[3]"The structure of the mammalian 20S proteasome at 2.75 A resolution."
Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., Tsukihara T.
Structure 10:609-618(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH 20S PROTEASOME.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC102554 mRNA. Translation: AAI02555.1.
PIRA42762.
B42762.
C42762.
D42762.
G42762.
RefSeqNP_001029768.1. NM_001034596.2.
UniGeneBt.44351.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75J/X1-205[»]
ProteinModelPortalP33672.
SMRP33672. Positions 2-205.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPST01.983.

Proteomic databases

PaxDbP33672.
PRIDEP33672.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000004984; ENSBTAP00000004984; ENSBTAG00000003830.
GeneID533874.
KEGGbta:533874.

Organism-specific databases

CTD5691.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074820.
HOGENOMHOG000090523.
HOVERGENHBG004446.
InParanoidP33672.
KOK02735.
OMAMDLIGCP.
OrthoDBEOG783MWB.
TreeFamTF106216.

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

EvolutionaryTraceP33672.
NextBio20876178.

Entry information

Entry namePSB3_BOVIN
AccessionPrimary (citable) accession number: P33672
Secondary accession number(s): Q3T059
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 13, 2006
Last modified: June 11, 2014
This is version 119 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references