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Protein

Proteasome subunit beta type

Gene

Prosbeta2

Organism
Drosophila melanogaster (Fruit fly)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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

  • cellular response to DNA damage stimulus Source: FlyBase
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine proteaseUniRule annotation

Enzyme and pathway databases

ReactomeiR-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-DME-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-DME-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-DME-174154. APC/C:Cdc20 mediated degradation of Securin.
R-DME-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-DME-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-202424. Downstream TCR signaling.
R-DME-2467813. Separation of Sister Chromatids.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-350562. Regulation of ornithine decarboxylase (ODC).
R-DME-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-DME-4608870. Asymmetric localization of PCP proteins.
R-DME-4641257. Degradation of AXIN.
R-DME-4641258. Degradation of DVL.
R-DME-5358346. Hedgehog ligand biogenesis.
R-DME-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
R-DME-5610780. Degradation of GLI1 by the proteasome.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
R-DME-5632684. Hedgehog 'on' state.
R-DME-5658442. Regulation of RAS by GAPs.
R-DME-5668541. TNFR2 non-canonical NF-kB pathway.
R-DME-5676590. NIK-->noncanonical NF-kB signaling.
R-DME-68949. Orc1 removal from chromatin.
R-DME-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-DME-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-DME-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.A02.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta typeUniRule annotation (EC:3.4.25.1UniRule annotation)
Gene namesi
Name:Prosbeta2Imported
Synonyms:beta2_dmImported, Pros-beta-2Imported
ORF Names:CG3329Imported
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Organism-specific databases

FlyBaseiFBgn0023174. Prosbeta2.

Subcellular locationi

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

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • proteasome complex Source: FlyBase
  • proteasome core complex Source: FlyBase
  • proteasome core complex, beta-subunit complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

NucleusSAAS annotation, ProteasomeUniRule annotation

PTM / Processingi

Proteomic databases

PaxDbiO17312.
PRIDEiO17312.

Expressioni

Gene expression databases

BgeeiFBgn0023174.
ExpressionAtlasiO17312. differential.

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

Protein-protein interaction databases

STRINGi7227.FBpp0075382.

Structurei

3D structure databases

ProteinModelPortaliO17312.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini231 – 26333Pr_beta_CInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0173. Eukaryota.
COG0638. LUCA.
OrthoDBiEOG091G0E5S.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF12465. Pr_beta_C. 1 hit.
PF00227. 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.

O17312-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLDNARELP RAGFNFDNCK RNATLLNRGF KPPTTTKTGT TIVGIIYKDG
60 70 80 90 100
VILGADTRAT EGPIVSDKNC AKIHYLAKNI YCCGAGTAAD TEMTTDLISS
110 120 130 140 150
QLELHRLQTD REVRVVAANT MLKQMLFRYQ GHISAALVLG GVDKTGPHIY
160 170 180 190 200
SIHPHGSSDK LPYATMGSGS LAAMTVFESR WKPDLSEEEG KKLVRDADPT
210 220 230 240 250
GVFNDLGSGS NIDLCVIRKG SVEYLRNYEL ANKKGKRQLD YRFKTGTSTV
260 270
LHTNIKDLLV TERVQAVPME IS
Length:272
Mass (Da):29,883
Last modified:January 1, 1998 - v1
Checksum:i22DBDB57DF6A4C0E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025792 Genomic DNA. Translation: AAB82571.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025792 Genomic DNA. Translation: AAB82571.1.

3D structure databases

ProteinModelPortaliO17312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0075382.

Protein family/group databases

MEROPSiT01.A02.

Proteomic databases

PaxDbiO17312.
PRIDEiO17312.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

FlyBaseiFBgn0023174. Prosbeta2.

Phylogenomic databases

eggNOGiKOG0173. Eukaryota.
COG0638. LUCA.
OrthoDBiEOG091G0E5S.

Enzyme and pathway databases

ReactomeiR-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-DME-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-DME-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-DME-174154. APC/C:Cdc20 mediated degradation of Securin.
R-DME-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-DME-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-202424. Downstream TCR signaling.
R-DME-2467813. Separation of Sister Chromatids.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-350562. Regulation of ornithine decarboxylase (ODC).
R-DME-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-DME-4608870. Asymmetric localization of PCP proteins.
R-DME-4641257. Degradation of AXIN.
R-DME-4641258. Degradation of DVL.
R-DME-5358346. Hedgehog ligand biogenesis.
R-DME-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
R-DME-5610780. Degradation of GLI1 by the proteasome.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
R-DME-5632684. Hedgehog 'on' state.
R-DME-5658442. Regulation of RAS by GAPs.
R-DME-5668541. TNFR2 non-canonical NF-kB pathway.
R-DME-5676590. NIK-->noncanonical NF-kB signaling.
R-DME-68949. Orc1 removal from chromatin.
R-DME-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-DME-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-DME-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Gene expression databases

BgeeiFBgn0023174.
ExpressionAtlasiO17312. differential.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF12465. Pr_beta_C. 1 hit.
PF00227. 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...

Entry informationi

Entry nameiO17312_DROME
AccessioniPrimary (citable) accession number: O17312
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 101 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.