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Protein

Proteasome subunit beta type-4

Gene

Psmb4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1 (By similarity).By similarity

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei45 – 451NucleophileBy similarity

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-4 (EC:3.4.25.1)
Alternative name(s):
Macropain beta chain
Multicatalytic endopeptidase complex beta chain
Proteasome beta chain
Proteasome chain 3
Short name:
RN3
Gene namesi
Name:Psmb4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi61877. Psmb4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 44441 PublicationPRO_0000026583Add
BLAST
Chaini45 – 263219Proteasome subunit beta type-4PRO_0000026584Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei101 – 1011PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP34067.
PRIDEiP34067.

2D gel databases

World-2DPAGE0004:P34067.

PTM databases

PhosphoSiteiP34067.

Expressioni

Inductioni

Up-regulated in cardiac hypertrophy and hypoxemia.1 Publication

Gene expression databases

GenevestigatoriP34067.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiP34067. 1 interaction.
STRINGi10116.ENSRNOP00000028484.

Structurei

3D structure databases

ProteinModelPortaliP34067.
SMRiP34067. Positions 45-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000181719.
HOVERGENiHBG018194.
InParanoidiP34067.
KOiK02736.
PhylomeDBiP34067.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P34067-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEAFWESRTG HWAGGPAPGQ FYRVPSTPSC LMDPMSAPAR PITRTQNPMV
60 70 80 90 100
TGTSVLGVKF DCGVVIAADM LGSYGSLARF RNISRIMRVN DSTMLGASGD
110 120 130 140 150
YADFQYLKQV LGQMVIDEEL FGDGHSYSPR AIHSWLTRAM YSRRSKMNPL
160 170 180 190 200
WNTKVIGGYA GGESFLGYVD MLGVAYEAPS LATGYGAYLA QPLLREVLEK
210 220 230 240 250
QPVLSQTEAR ELVERCMRVL YYRDARSYNR FQVATVTEKG VEIEGPLSAQ
260
TNWDIAHMIS GFE
Length:263
Mass (Da):29,197
Last modified:December 15, 1998 - v2
Checksum:iC8FCB91265F8FB90
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411P → S in AAA42054. (PubMed:8482379)Curated
Sequence conflicti50 – 501V → L in AAA42054. (PubMed:8482379)Curated
Sequence conflicti60 – 601F → S in AAB47113. (PubMed:8645151)Curated
Sequence conflicti80 – 801F → L in AAB47113. (PubMed:8645151)Curated
Sequence conflicti82 – 821N → I in AAA42054. (PubMed:8482379)Curated
Sequence conflicti86 – 861I → F in AAB47113. (PubMed:8645151)Curated
Sequence conflicti89 – 891V → L in AAB47113. (PubMed:8645151)Curated
Sequence conflicti121 – 1211F → L AA sequence 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S82190 mRNA. Translation: AAB47113.2.
L17127 mRNA. Translation: AAA42054.1.
PIRiS09084.
S32507.
RefSeqiNP_113817.1. NM_031629.1.
UniGeneiRn.6169.

Genome annotation databases

GeneIDi58854.
KEGGirno:58854.
UCSCiRGD:61877. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S82190 mRNA. Translation: AAB47113.2.
L17127 mRNA. Translation: AAA42054.1.
PIRiS09084.
S32507.
RefSeqiNP_113817.1. NM_031629.1.
UniGeneiRn.6169.

3D structure databases

ProteinModelPortaliP34067.
SMRiP34067. Positions 45-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP34067. 1 interaction.
STRINGi10116.ENSRNOP00000028484.

PTM databases

PhosphoSiteiP34067.

2D gel databases

World-2DPAGE0004:P34067.

Proteomic databases

PaxDbiP34067.
PRIDEiP34067.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi58854.
KEGGirno:58854.
UCSCiRGD:61877. rat.

Organism-specific databases

CTDi5692.
RGDi61877. Psmb4.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000181719.
HOVERGENiHBG018194.
InParanoidiP34067.
KOiK02736.
PhylomeDBiP34067.

Miscellaneous databases

NextBioi611445.
PROiP34067.

Gene expression databases

GenevestigatoriP34067.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Processing of N3, a mammalian proteasome beta-type subunit."
    Thomson S., Rivett A.J.
    Biochem. J. 315:733-738(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-140.
  2. "cDNA cloning of a new type of subunit of mammalian proteasomes."
    Thomson S., Balson D.F., Rivett A.J.
    FEBS Lett. 322:135-138(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-263.
  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 45-55.
  4. Lubec G., Diao W.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 60-79 AND 109-130, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  5. "Atrophy, hypertrophy, and hypoxemia induce transcriptional regulators of the ubiquitin proteasome system in the rat heart."
    Razeghi P., Baskin K.K., Sharma S., Young M.E., Stepkowski S., Essop M.F., Taegtmeyer H.
    Biochem. Biophys. Res. Commun. 342:361-364(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiPSB4_RAT
AccessioniPrimary (citable) accession number: P34067
Secondary accession number(s): P28071, P97719
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: December 15, 1998
Last modified: January 7, 2015
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.