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Q3T108 (PSB4_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. 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-4

EC=3.4.25.1
Gene names
Name:PSMB4
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length264 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 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. Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the 20S proteasome By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 4545 By similarity
PRO_0000239854
Chain46 – 264219Proteasome subunit beta type-4
PRO_0000239855

Sites

Active site461Nucleophile By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1021Phosphotyrosine By similarity

Secondary structure

...................................... 264
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q3T108 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: B2C4029A25FCC76A

FASTA26429,031
        10         20         30         40         50         60 
MEALLESRSG LWAGGPAPGQ FYRIPPTPGS SVDPVSALYG SPITRTQNPM VTGTSVLGLK 

        70         80         90        100        110        120 
FEGGVVIAAD MLGSYGSLAR FRNISRIMRV NNSTMLGASG DYADFQYLKQ VLGQMVIDEE 

       130        140        150        160        170        180 
LLGDGHSYSP KAIHSWLTRA MYSRRSKMNP LWNTMVIGGY ADGESFLGYV DMLGVAYEAP 

       190        200        210        220        230        240 
SLATGYGAYL AQPLLREVLE KQPVLSQTEA RELVERCMRV LYYRDARSYN RFQIATVTEK 

       250        260 
GVEIEGPLSA ETNWDIAHMI SGFE 

« 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: Crossbred X Angus.
Tissue: Ileum.
[2]"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 46-264 OF COMPLEX WITH 20S PROTEASOME.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC102182 mRNA. Translation: AAI02183.1.
RefSeqNP_001029438.1. NM_001034266.2.
UniGeneBt.53288.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.752/N46-264[»]
ProteinModelPortalQ3T108.
SMRQ3T108. Positions 46-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000028364.

Protein family/group databases

MEROPST01.987.

Proteomic databases

PaxDbQ3T108.
PRIDEQ3T108.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000028364; ENSBTAP00000028364; ENSBTAG00000021288.
GeneID506203.
KEGGbta:506203.

Organism-specific databases

CTD5692.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00390000000698.
HOGENOMHOG000181719.
HOVERGENHBG018194.
InParanoidQ3T108.
KOK02736.
OMARIMRVND.
OrthoDBEOG74FF1D.
TreeFamTF106220.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ3T108.
NextBio20867498.

Entry information

Entry namePSB4_BOVIN
AccessionPrimary (citable) accession number: Q3T108
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: October 11, 2005
Last modified: June 11, 2014
This is version 73 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references