Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proteasome subunit beta type-5

Gene

Psmb5

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. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib (By similarity). Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway (By similarity).By similarity

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei60 – 601NucleophileBy similarity
Binding sitei108 – 1081Bortezomib; via amide nitrogenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Protein family/group databases

MEROPSiT01.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-5 (EC:3.4.25.1)
Alternative name(s):
Macropain epsilon chain
Multicatalytic endopeptidase complex epsilon chain
Proteasome chain 6
Proteasome epsilon chain
Proteasome subunit X
Gene namesi
Name:Psmb5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61879. Psmb5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 5959Removed in mature form1 PublicationPRO_0000026593Add
BLAST
Chaini60 – 263204Proteasome subunit beta type-5PRO_0000026594Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiP28075.
PRIDEiP28075.

PTM databases

PhosphoSiteiP28075.

Expressioni

Inductioni

Down-regulated by theophylline (THP) and up-regulated by 1,3-dinitrobenzene (DNB), two reprotoxic agents thought to induce infertility.1 Publication

Gene expression databases

GenevestigatoriP28075.

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. This subunit can be displaced by the equivalent immune-specific subunit PSMB8. Directly interacts with POMP (By similarity). Interacts with ABCB1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi248073. 1 interaction.
IntActiP28075. 1 interaction.
STRINGi10116.ENSRNOP00000018005.

Structurei

3D structure databases

ProteinModelPortaliP28075.
SMRiP28075. Positions 60-259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091082.
HOVERGENiHBG108297.
InParanoidiP28075.
KOiK02737.
PhylomeDBiP28075.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
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.

P28075-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALASVLQRP MPVNQHGFFG LGGRADLLDL GPGSPGDGLS LAAPSWGVPE
60 70 80 90 100
EPRIEMLHGT TTLAFKFQHG VIVAADSRAT AGPYIASQTV KKVIEINPYL
110 120 130 140 150
LGTMAGGAAD CSFWERLLAR QCRIYELRNK ERISVAAASK LLANMVYQYK
160 170 180 190 200
GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI SGTAFSVGSG SVYAFGVMDR
210 220 230 240 250
GYSYDLQVEE AYDLARRAIY QATYRDAYSG GAVNLYHVRE DGWIRVSSDN
260
VADLHDKYTS SIP
Length:263
Mass (Da):28,585
Last modified:April 29, 2008 - v3
Checksum:i317FC0C827FE65CA
GO

Sequence cautioni

The sequence BAA08204.1 differs from that shown.Sequencing error.Curated
The sequence BAA08204.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621T → I AA sequence (PubMed:2335214).Curated
Sequence conflicti69 – 691H → E AA sequence (PubMed:2335214).Curated
Sequence conflicti73 – 731V → L AA sequence (PubMed:2335214).Curated
Sequence conflicti83 – 831P → A in EDM14180 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45247 mRNA. Translation: BAA08204.1. Sequence problems.
CH474049 Genomic DNA. Translation: EDM14180.1.
PIRiS09087.
RefSeqiNP_001099197.2. NM_001105727.2.
UniGeneiRn.2.

Genome annotation databases

GeneIDi29425.
KEGGirno:29425.
UCSCiRGD:61879. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45247 mRNA. Translation: BAA08204.1. Sequence problems.
CH474049 Genomic DNA. Translation: EDM14180.1.
PIRiS09087.
RefSeqiNP_001099197.2. NM_001105727.2.
UniGeneiRn.2.

3D structure databases

ProteinModelPortaliP28075.
SMRiP28075. Positions 60-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248073. 1 interaction.
IntActiP28075. 1 interaction.
STRINGi10116.ENSRNOP00000018005.

Protein family/group databases

MEROPSiT01.012.

PTM databases

PhosphoSiteiP28075.

Proteomic databases

PaxDbiP28075.
PRIDEiP28075.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29425.
KEGGirno:29425.
UCSCiRGD:61879. rat.

Organism-specific databases

CTDi5693.
RGDi61879. Psmb5.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091082.
HOVERGENiHBG108297.
InParanoidiP28075.
KOiK02737.
PhylomeDBiP28075.

Miscellaneous databases

NextBioi609128.
PROiP28075.

Gene expression databases

GenevestigatoriP28075.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Yokota K.Y., Tanaka K.
    Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  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 60-77.
  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.

Entry informationi

Entry nameiPSB5_RAT
AccessioniPrimary (citable) accession number: P28075
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: April 29, 2008
Last modified: May 27, 2015
This is version 118 of the entry and version 3 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.