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Protein

Proteasome subunit beta type

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript 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.UniRule annotation

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine proteaseUniRule annotation

Protein family/group databases

MEROPSiT01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta typeUniRule annotation (EC:3.4.25.1UniRule annotation)
OrganismiXenopus laevis (African clawed frog)Imported
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation
  • Nucleus SAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

NucleusSAAS annotation, ProteasomeUniRule annotationImported

PTM / Processingi

Proteomic databases

PRIDEiO13000.

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.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliO13000.
SMRiO13000. Positions 31-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

HOVERGENiHBG000123.

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.

O13000-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLQAAAAG PQSSAPPGDT DWMGREVSTG TTIMAVEFDG GVVIGADSRT
60 70 80 90 100
TTGAYIANRV TDKLTPVHDR IFCCRSGSAA DTQAIADAVT YQLGFHSIEL
110 120 130 140 150
DGPPLVHTAA NLFKEMCYRY REDLMAGIIV AGWDKRKGGQ VYTVPMGGML
160 170 180 190 200
VHQQFSIGGS GSSYIYGFVD STYRPGMTKE ECLKFTANAL ALAMERDGSS
210 220 230
GGVIRLAAIT EEGVERQVIL GNQLPRFPSS
Length:230
Mass (Da):24,553
Last modified:July 1, 1997 - v1
Checksum:i2A1C9B3494473D87
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87689 mRNA. Translation: BAA19760.1.
UniGeneiXl.3152.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87689 mRNA. Translation: BAA19760.1.
UniGeneiXl.3152.

3D structure databases

ProteinModelPortaliO13000.
SMRiO13000. Positions 31-227.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiT01.010.

Proteomic databases

PRIDEiO13000.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000123.

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

  1. "Evolution of proteasome subunits delta and LMP2: complementary DNA cloning and linkage analysis with MHC in lower vertebrates."
    Nonaka M., Namikawa C., Sasaki M., Salter-Cid L., Flajnik M.F.
    J. Immunol. 159:734-740(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: LiverImported.

Entry informationi

Entry nameiO13000_XENLA
AccessioniPrimary (citable) accession number: O13000
Entry historyi
Integrated into UniProtKB/TrEMBL: July 1, 1997
Last sequence update: July 1, 1997
Last modified: May 11, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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 one 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.