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P18421 (PSB1_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-1

EC=3.4.25.1
Alternative name(s):
Macropain subunit C5
Multicatalytic endopeptidase complex subunit C5
Proteasome component C5
Proteasome gamma chain
Gene names
Name:Psmb1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length240 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. Interacts with SERPINB2 By similarity.

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Ubiquitous.

Induction

Up-regulated in prefrontal cortex (PFC) after nicotine exposure. Down-regulated by theophylline (THP) and 1,3-dinitrobenzene (DNB), two reprotoxic agents thought to induce infertility. Ref.3 Ref.4

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 2727
PRO_0000259625
Chain28 – 240213Proteasome subunit beta type-1
PRO_0000148032

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1491Phosphotyrosine By similarity
Modified residue2031N6-acetyllysine By similarity
Glycosylation571O-linked (GlcNAc) By similarity
Glycosylation2081O-linked (GlcNAc) By similarity

Sequences

Sequence LengthMass (Da)Tools
P18421 [UniParc].

Last modified May 1, 1992. Version 3.
Checksum: B79EB682CDB95A01

FASTA24026,479
        10         20         30         40         50         60 
MLSTAAYRDP DRELVMGPQG SAGPVQMRFS PYAFNGGTVL AIAGEDFSIV ASDTRLSEGF 

        70         80         90        100        110        120 
SIHTRDSPKC YKLTDKTVIG CSGFHGDCLT LTKIIEARLK MYKHSNNKAM TTGAIAAMLS 

       130        140        150        160        170        180 
TILYSRRFFP YYVYNIIEGL DEEGKGAVYS FDPVGSYQRD SFKAGGSASA MLQPLLDNQV 

       190        200        210        220        230        240 
GFKNMQNVEH VPLTLDRAMR LVKDVFISAA ERDVYTGDAL RICIVTKEGI REETVPLRKD 

« Hide

References

[1]"cDNA cloning and sequencing of component C5 of proteasomes from rat hepatoma cells."
Tamura T., Tanaka K., Kumatori A., Yamada F., Tsurumi C., Fujiwara T., Ichihara A., Tokunaga F., Aruga R., Iwanaga S.
FEBS Lett. 264:91-94(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The NH2-terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated."
Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T., Shimonishi Y.
FEBS Lett. 263:373-375(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-47.
Tissue: Liver.
[3]"Nicotine coregulates multiple pathways involved in protein modification/degradation in rat brain."
Kane J.K., Konu O., Ma J.Z., Li M.D.
Brain Res. Mol. Brain Res. 132:181-191(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY NICOTINE.
[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
X52783 mRNA. Translation: CAA36987.1.
PIRS09696.
RefSeqNP_446042.1. NM_053590.1.
UniGeneRn.6016.

3D structure databases

ProteinModelPortalP18421.
SMRP18421. Positions 28-240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP18421. 2 interactions.
STRING10116.ENSRNOP00000002037.

Protein family/group databases

MEROPST01.986.

PTM databases

PhosphoSiteP18421.

Proteomic databases

PaxDbP18421.
PRIDEP18421.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID94198.
KEGGrno:94198.
UCSCRGD:621092. rat.

Organism-specific databases

CTD5689.
RGD621092. Psmb1.

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091081.
HOVERGENHBG000961.
InParanoidP18421.
KOK02732.
PhylomeDBP18421.

Gene expression databases

GenevestigatorP18421.

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

NextBio617862.
PROP18421.

Entry information

Entry namePSB1_RAT
AccessionPrimary (citable) accession number: P18421
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 1, 1992
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