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Protein

Proteasome subunit beta type-3

Gene

Prosbeta3

Organism
Drosophila melanogaster (Fruit fly)
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.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_273531. CDK-mediated phosphorylation and removal of Cdc6.
REACT_274251. degradation of AXIN.
REACT_274764. ER-Phagosome pathway.
REACT_274899. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_283069. Degradation of GLI2 by the proteasome.
REACT_284680. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_285954. APC/C:Cdc20 mediated degradation of Securin.
REACT_287787. Activation of NF-kappaB in B cells.
REACT_289889. GLI3 is processed to GLI3R by the proteasome.
REACT_299289. degradation of DVL.
REACT_308142. Hedgehog ligand biogenesis.
REACT_320700. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_323570. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329319. SCF(Skp2)-mediated degradation of p27/p21.
REACT_330960. Hedgehog 'on' state.
REACT_333353. Asymmetric localization of PCP proteins.
REACT_335389. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_335593. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_335971. SCF-beta-TrCP mediated degradation of Emi1.
REACT_336807. Regulation of ornithine decarboxylase (ODC).
REACT_337097. Ubiquitin-dependent degradation of Cyclin D1.
REACT_343999. Orc1 removal from chromatin.
REACT_346613. Separation of Sister Chromatids.
REACT_347454. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_354443. Degradation of beta-catenin by the destruction complex.
REACT_359614. Degradation of GLI1 by the proteasome.
REACT_361037. CLEC7A (Dectin-1) signaling.
REACT_362328. Dectin-1 mediated noncanonical NF-kB signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-3 (EC:3.4.25.1)
Alternative name(s):
20S proteasome subunit beta-3
Gene namesi
Name:Prosbeta3
ORF Names:CG11980
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0026380. Prosbeta3.

Subcellular locationi

  • Cytoplasm PROSITE-ProRule annotation
  • Nucleus By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 205205Proteasome subunit beta type-3PRO_0000148062Add
BLAST

Proteomic databases

PaxDbiQ9XYN7.
PRIDEiQ9XYN7.

Expressioni

Gene expression databases

BgeeiQ9XYN7.
ExpressionAtlasiQ9XYN7. differential.
GenevisibleiQ9XYN7. DM.

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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Prosbeta5Q7K1483EBI-119764,EBI-116800

Protein-protein interaction databases

BioGridi66247. 58 interactions.
DIPiDIP-18901N.
IntActiQ9XYN7. 16 interactions.
MINTiMINT-306832.
STRINGi7227.FBpp0081488.

Structurei

3D structure databases

ProteinModelPortaliQ9XYN7.
SMRiQ9XYN7. Positions 2-205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074820.
InParanoidiQ9XYN7.
KOiK02735.
OMAiGCLNFAK.
OrthoDBiEOG783MWB.
PhylomeDBiQ9XYN7.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9XYN7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSILAYNGGC VVAMRGKDCV AIATDHRFGI QAQTISTDFK KVFHIGPRMF
60 70 80 90 100
LGLTGLQTDI LTVRDRLMFR KNLYETRENR EMCPKPFSAM MSSFLYEHRF
110 120 130 140 150
GPYFIEPVVA GLDPKTMEPF ICNMDLIGCP NAPDDFVVAG TCAEQLYGMC
160 170 180 190 200
ETLWKPDLEP DQLFEVIAQS IVNAFDRDAM SGWGATVYII EKDKITERTL

KTRMD
Length:205
Mass (Da):23,234
Last modified:November 1, 1999 - v1
Checksum:i3AE365887AF3A247
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF116898 Genomic DNA. Translation: AAD22968.1.
AM294562 Genomic DNA. Translation: CAL26545.1.
AM294563 Genomic DNA. Translation: CAL26546.1.
AM294564 Genomic DNA. Translation: CAL26547.1.
AM294565 Genomic DNA. Translation: CAL26548.1.
AM294566 Genomic DNA. Translation: CAL26549.1.
AM294567 Genomic DNA. Translation: CAL26550.1.
AM294568 Genomic DNA. Translation: CAL26551.1.
AM294569 Genomic DNA. Translation: CAL26552.1.
AE014297 Genomic DNA. Translation: AAF54320.1.
AY095029 mRNA. Translation: AAM11357.1.
RefSeqiNP_649858.1. NM_141601.2.
UniGeneiDm.6972.

Genome annotation databases

EnsemblMetazoaiFBtr0082010; FBpp0081488; FBgn0026380.
GeneIDi41079.
KEGGidme:Dmel_CG11981.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF116898 Genomic DNA. Translation: AAD22968.1.
AM294562 Genomic DNA. Translation: CAL26545.1.
AM294563 Genomic DNA. Translation: CAL26546.1.
AM294564 Genomic DNA. Translation: CAL26547.1.
AM294565 Genomic DNA. Translation: CAL26548.1.
AM294566 Genomic DNA. Translation: CAL26549.1.
AM294567 Genomic DNA. Translation: CAL26550.1.
AM294568 Genomic DNA. Translation: CAL26551.1.
AM294569 Genomic DNA. Translation: CAL26552.1.
AE014297 Genomic DNA. Translation: AAF54320.1.
AY095029 mRNA. Translation: AAM11357.1.
RefSeqiNP_649858.1. NM_141601.2.
UniGeneiDm.6972.

3D structure databases

ProteinModelPortaliQ9XYN7.
SMRiQ9XYN7. Positions 2-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66247. 58 interactions.
DIPiDIP-18901N.
IntActiQ9XYN7. 16 interactions.
MINTiMINT-306832.
STRINGi7227.FBpp0081488.

Proteomic databases

PaxDbiQ9XYN7.
PRIDEiQ9XYN7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082010; FBpp0081488; FBgn0026380.
GeneIDi41079.
KEGGidme:Dmel_CG11981.

Organism-specific databases

CTDi41079.
FlyBaseiFBgn0026380. Prosbeta3.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074820.
InParanoidiQ9XYN7.
KOiK02735.
OMAiGCLNFAK.
OrthoDBiEOG783MWB.
PhylomeDBiQ9XYN7.

Enzyme and pathway databases

ReactomeiREACT_273531. CDK-mediated phosphorylation and removal of Cdc6.
REACT_274251. degradation of AXIN.
REACT_274764. ER-Phagosome pathway.
REACT_274899. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_283069. Degradation of GLI2 by the proteasome.
REACT_284680. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_285954. APC/C:Cdc20 mediated degradation of Securin.
REACT_287787. Activation of NF-kappaB in B cells.
REACT_289889. GLI3 is processed to GLI3R by the proteasome.
REACT_299289. degradation of DVL.
REACT_308142. Hedgehog ligand biogenesis.
REACT_320700. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_323570. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329319. SCF(Skp2)-mediated degradation of p27/p21.
REACT_330960. Hedgehog 'on' state.
REACT_333353. Asymmetric localization of PCP proteins.
REACT_335389. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_335593. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_335971. SCF-beta-TrCP mediated degradation of Emi1.
REACT_336807. Regulation of ornithine decarboxylase (ODC).
REACT_337097. Ubiquitin-dependent degradation of Cyclin D1.
REACT_343999. Orc1 removal from chromatin.
REACT_346613. Separation of Sister Chromatids.
REACT_347454. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_354443. Degradation of beta-catenin by the destruction complex.
REACT_359614. Degradation of GLI1 by the proteasome.
REACT_361037. CLEC7A (Dectin-1) signaling.
REACT_362328. Dectin-1 mediated noncanonical NF-kB signaling.

Miscellaneous databases

GenomeRNAii41079.
NextBioi822046.
PROiQ9XYN7.

Gene expression databases

BgeeiQ9XYN7.
ExpressionAtlasiQ9XYN7. differential.
GenevisibleiQ9XYN7. DM.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
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 dominant temperature-sensitive lethal DTS7 of Drosophila melanogaster encodes an altered 20S proteasome beta-type subunit."
    Smyth K.A., Belote J.M.
    Genetics 151:211-220(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: Samarkand.
  2. "Widespread adaptive evolution of Drosophila genes with sex-biased expression."
    Proeschel M., Zhang Z., Parsch J.
    Genetics 174:893-900(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL82, ZBMEL84 and ZBMEL95.
  3. "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.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 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.A., 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.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., 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.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., 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., Woodage T., 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.C., 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: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiPSB3_DROME
AccessioniPrimary (citable) accession number: Q9XYN7
Secondary accession number(s): A0APH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.