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Q9XYN7

- PSB3_DROME

UniProt

Q9XYN7 - PSB3_DROME

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Protein

Proteasome subunit beta type-3

Gene
Prosbeta3, CG11980
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 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.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_180649. Activation of NF-kappaB in B cells.
REACT_180655. ER-Phagosome pathway.
REACT_180671. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_181662. Separation of Sister Chromatids.
REACT_184330. Asymmetric localization of PCP proteins.
REACT_211248. CDK-mediated phosphorylation and removal of Cdc6.
REACT_215026. degradation of AXIN.
REACT_218589. Orc1 removal from chromatin.
REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

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: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0026380. Prosbeta3.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. 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.

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.

Protein-protein interaction databases

BioGridi66247. 57 interactions.
DIPiDIP-18901N.
IntActiQ9XYN7. 16 interactions.
MINTiMINT-306832.
STRINGi7227.FBpp0081488.

Structurei

3D structure databases

ProteinModelPortaliQ9XYN7.
SMRiQ9XYN7. Positions 2-205.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074820.
InParanoidiQ9XYN7.
KOiK02735.
OMAiMDLIGCP.
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

MSILAYNGGC VVAMRGKDCV AIATDHRFGI QAQTISTDFK KVFHIGPRMF    50
LGLTGLQTDI LTVRDRLMFR KNLYETRENR EMCPKPFSAM MSSFLYEHRF 100
GPYFIEPVVA GLDPKTMEPF ICNMDLIGCP NAPDDFVVAG TCAEQLYGMC 150
ETLWKPDLEP DQLFEVIAQS IVNAFDRDAM SGWGATVYII EKDKITERTL 200
KTRMD 205
Length:205
Mass (Da):23,234
Last modified:November 1, 1999 - v1
Checksum:i3AE365887AF3A247
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_649858.1. NM_141601.2.
UniGenei Dm.6972.

3D structure databases

ProteinModelPortali Q9XYN7.
SMRi Q9XYN7. Positions 2-205.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 66247. 57 interactions.
DIPi DIP-18901N.
IntActi Q9XYN7. 16 interactions.
MINTi MINT-306832.
STRINGi 7227.FBpp0081488.

Proteomic databases

PaxDbi Q9XYN7.
PRIDEi Q9XYN7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0082010 ; FBpp0081488 ; FBgn0026380 .
GeneIDi 41079.
KEGGi dme:Dmel_CG11981.

Organism-specific databases

CTDi 41079.
FlyBasei FBgn0026380. Prosbeta3.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074820.
InParanoidi Q9XYN7.
KOi K02735.
OMAi MDLIGCP.
OrthoDBi EOG783MWB.
PhylomeDBi Q9XYN7.

Enzyme and pathway databases

Reactomei REACT_180649. Activation of NF-kappaB in B cells.
REACT_180655. ER-Phagosome pathway.
REACT_180671. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_181662. Separation of Sister Chromatids.
REACT_184330. Asymmetric localization of PCP proteins.
REACT_211248. CDK-mediated phosphorylation and removal of Cdc6.
REACT_215026. degradation of AXIN.
REACT_218589. Orc1 removal from chromatin.
REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

Miscellaneous databases

GenomeRNAii 41079.
NextBioi 822046.
PROi Q9XYN7.

Gene expression databases

Bgeei Q9XYN7.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 112 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