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

Gene

Prosbeta5

Organism
Drosophila melanogaster (Fruit fly)
Status
Unreviewed-Annotation score: Annotation score: 5 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.UniRule annotation

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.UniRule annotation

GO - Molecular functioni

GO - Biological processi

  • cell proliferation Source: FlyBase
  • centrosome organization Source: FlyBase
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • neurogenesis 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.A06.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta typeUniRule annotation (EC:3.4.25.1UniRule annotation)
Gene namesi
Name:Prosbeta5Imported
Synonyms:Pros-beta-5Imported
ORF Names:CG12323Imported, Dmel_CG12323Imported
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0029134. Prosbeta5.

Subcellular locationi

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

GO - Cellular componenti

  • cytosol Source: FlyBase
  • nucleoplasm Source: FlyBase
  • 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 annotationImported

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.FBpp0087319.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0175. Eukaryota.
ENOG410XQRP. LUCA.
GeneTreeiENSGT00510000046395.
KOiK02737.
OMAiTMCAGVT.
OrthoDBiEOG7FNC86.

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.

Q7K148-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALAEICKIS NAPYMRPNAW SSADVEEEQK GLMCNLANPY TLAAPPFENP
60 70 80 90 100
LHNLNQIQAN GDKTGVKINF DHGTTTLGFK FKGGVLLAVD SRATGGSYIG
110 120 130 140 150
SQSMKKIVEI NQFMLGTLAG GAADCVYWDR VLSKECRLHE LRNKERISVA
160 170 180 190 200
AASKIMANIA HEYKGMGLSM GMMLAGYDKR GPGLYYVDSE GSRTPGNLFS
210 220 230 240 250
VGSGSLYAYG VLDSGYHWDL EDKEAQELGR RAIYHATFRD AYSGGIIRVY
260 270 280
HIKEDGWVNI SNTDCMELHY MYQEQLKQQA AK
Length:282
Mass (Da):31,161
Last modified:October 3, 2006 - v1
Checksum:i3D27742832793AEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58748.1.
AY069381 mRNA. Translation: AAL39526.1.
AE013599 Genomic DNA. Translation: AAM68751.1.
RefSeqiNP_652014.1. NM_143757.4.
NP_724974.1. NM_165801.2.
UniGeneiDm.1454.

Genome annotation databases

EnsemblMetazoaiFBtr0088224; FBpp0087319; FBgn0029134.
FBtr0088225; FBpp0087320; FBgn0029134.
GeneIDi45269.
KEGGidme:Dmel_CG12323.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58748.1.
AY069381 mRNA. Translation: AAL39526.1.
AE013599 Genomic DNA. Translation: AAM68751.1.
RefSeqiNP_652014.1. NM_143757.4.
NP_724974.1. NM_165801.2.
UniGeneiDm.1454.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0087319.

Protein family/group databases

MEROPSiT01.A06.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088224; FBpp0087319; FBgn0029134.
FBtr0088225; FBpp0087320; FBgn0029134.
GeneIDi45269.
KEGGidme:Dmel_CG12323.

Organism-specific databases

CTDi45269.
FlyBaseiFBgn0029134. Prosbeta5.

Phylogenomic databases

eggNOGiKOG0175. Eukaryota.
ENOG410XQRP. LUCA.
GeneTreeiENSGT00510000046395.
KOiK02737.
OMAiTMCAGVT.
OrthoDBiEOG7FNC86.

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.

Miscellaneous databases

GenomeRNAii45269.

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. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BerkeleyImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BerkeleyImported.
  5. "The transposable elements of the Drosophila melanogaster euchromatin: a genomics perspective."
    Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., Celniker S.E.
    Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  6. "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."
    Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., Karpen G.H.
    Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  7. "Combined evidence annotation of transposable elements in genome sequences."
    Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., Ashburner M., Anxolabehere D.
    PLoS Comput. Biol. 1:166-175(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  8. Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., Svirskas R., Rubin G.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  9. "Drosophila melanogaster release 4 sequence."
    Berkeley Drosophila Genome Project
    Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C., Rubin G.
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  10. "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."
    Smith C.D., Shu S., Mungall C.J., Karpen G.H.
    Science 316:1586-1591(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  12. FlyBase
    Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiQ7K148_DROME
AccessioniPrimary (citable) accession number: Q7K148
Entry historyi
Integrated into UniProtKB/TrEMBL: October 3, 2006
Last sequence update: October 3, 2006
Last modified: July 6, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.