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Protein

Proteasome subunit beta type-1

Gene

Prosbeta6

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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.

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. 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_293133. Degradation of GLI1 by the proteasome.
REACT_299289. degradation of DVL.
REACT_304845. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_307080. Hh ligand biogenesis disease.
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.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-1 (EC:3.4.25.1)
Alternative name(s):
Proteasome 26 kDa subunit
Gene namesi
Name:Prosbeta6
Synonyms:l(3)73Ai, PROS-26, Pros26
ORF Names:CG4097
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0002284. Prosbeta6.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. 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
Propeptidei1 – 2020By similarityPRO_0000259626Add
BLAST
Chaini21 – 235215Proteasome subunit beta type-1PRO_0000148036Add
BLAST

Proteomic databases

PaxDbiP40304.

Expressioni

Gene expression databases

BgeeiP40304.
ExpressionAtlasiP40304. 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. The catalytic chamber with the active sites is on the inside of the barrel (By similarity).By similarity

Protein-protein interaction databases

BioGridi65155. 44 interactions.
DIPiDIP-23672N.
IntActiP40304. 8 interactions.
MINTiMINT-754870.
STRINGi7227.FBpp0075119.

Structurei

3D structure databases

ProteinModelPortaliP40304.
SMRiP40304. Positions 22-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000075035.
InParanoidiP40304.
KOiK02732.
OMAiEHRFNPY.
OrthoDBiEOG7WHHBB.
PhylomeDBiP40304.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P40304-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRLGFEQFP DYQVPGMKHP DFSPYESNGG SIVAIAGDDF AVIAADTRLS
60 70 80 90 100
SGYNIHSRTQ SKLFKLSPQT VLGSAGCWAD TLSLTGSIKV RMQSYEHTHL
110 120 130 140 150
RTMTTEAVAQ MLSIAMYNRR FFPYYVSNIL AGIDNEGKGV VYSYDPIGHC
160 170 180 190 200
EKATYRAGGT AGTLLQPVLD NQIGHKNMNL EDADKIKLTK ERAVSVASDT
210 220 230
FISAAERDIY TGDSVLINII TKDGIEVRTL TLRQD
Length:235
Mass (Da):25,842
Last modified:January 10, 2001 - v2
Checksum:i592307AAEDD98B25
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921R → W in AAC46465 (PubMed:8415617).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00790 Unassigned DNA. Translation: AAC46465.1.
AE014296 Genomic DNA. Translation: AAF49435.1.
AY051697 mRNA. Translation: AAK93121.1.
RefSeqiNP_524115.1. NM_079391.3.
UniGeneiDm.2536.

Genome annotation databases

EnsemblMetazoaiFBtr0075360; FBpp0075119; FBgn0002284.
GeneIDi39855.
KEGGidme:Dmel_CG4097.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00790 Unassigned DNA. Translation: AAC46465.1.
AE014296 Genomic DNA. Translation: AAF49435.1.
AY051697 mRNA. Translation: AAK93121.1.
RefSeqiNP_524115.1. NM_079391.3.
UniGeneiDm.2536.

3D structure databases

ProteinModelPortaliP40304.
SMRiP40304. Positions 22-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65155. 44 interactions.
DIPiDIP-23672N.
IntActiP40304. 8 interactions.
MINTiMINT-754870.
STRINGi7227.FBpp0075119.

Proteomic databases

PaxDbiP40304.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075360; FBpp0075119; FBgn0002284.
GeneIDi39855.
KEGGidme:Dmel_CG4097.

Organism-specific databases

CTDi39855.
FlyBaseiFBgn0002284. Prosbeta6.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000075035.
InParanoidiP40304.
KOiK02732.
OMAiEHRFNPY.
OrthoDBiEOG7WHHBB.
PhylomeDBiP40304.

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_293133. Degradation of GLI1 by the proteasome.
REACT_299289. degradation of DVL.
REACT_304845. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_307080. Hh ligand biogenesis disease.
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.

Miscellaneous databases

GenomeRNAii39855.
NextBioi815727.
PROiP40304.

Gene expression databases

BgeeiP40304.
ExpressionAtlasiP40304. differential.

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. "Identification of an essential gene, l(3)73Ai, with a dominant temperature-sensitive lethal allele, encoding a Drosophila proteasome subunit."
    Saville K.J., Belote J.M.
    Proc. Natl. Acad. Sci. U.S.A. 90:8842-8846(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiPSB1_DROME
AccessioniPrimary (citable) accession number: P40304
Secondary accession number(s): Q9VV84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1995
Last sequence update: January 10, 2001
Last modified: March 31, 2015
This is version 123 of the entry and version 2 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.