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Q9VQE5

- PSB2_DROME

UniProt

Q9VQE5 - PSB2_DROME

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Protein

Probable proteasome subunit beta type-2

Gene

Prosbeta4R2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 2 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 (By similarity).By similarity

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. proteolysis involved in cellular protein catabolic process Source: InterPro
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_230692. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_232776. Regulation of ornithine decarboxylase (ODC).
REACT_233284. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_234235. Hh ligand biogenesis disease.
REACT_234707. SCF(Skp2)-mediated degradation of p27/p21.
REACT_238120. degradation of DVL.
REACT_239151. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_242866. Degradation of beta-catenin by the destruction complex.
REACT_247767. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_250603. SCF-beta-TrCP mediated degradation of Emi1.
REACT_258701. Hedgehog ligand biogenesis.
REACT_260216. Ubiquitin-dependent degradation of Cyclin D1.
REACT_269395. GLI3 is processed to GLI3R by the proteasome.
REACT_271013. Degradation of GLI1 by the proteasome.
REACT_271479. Degradation of GLI2 by the proteasome.
REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

Protein family/group databases

MEROPSiT01.984.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable proteasome subunit beta type-2 (EC:3.4.25.1)
Gene namesi
Name:Prosbeta4R2
ORF Names:CG17302
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0031443. Prosbeta4R2.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
  3. proteasome core complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210Probable proteasome subunit beta type-2PRO_0000148047Add
BLAST

Proteomic databases

PaxDbiQ9VQE5.
PRIDEiQ9VQE5.

Expressioni

Gene expression databases

BgeeiQ9VQE5.

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

BioGridi59678. 13 interactions.
IntActiQ9VQE5. 1 interaction.
MINTiMINT-1573384.

Structurei

3D structure databases

ProteinModelPortaliQ9VQE5.
SMRiQ9VQE5. Positions 3-196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00640000091536.
InParanoidiQ9VQE5.
KOiK02734.
OMAiNTRYQVA.
OrthoDBiEOG7N63NQ.
PhylomeDBiQ9VQE5.

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.

Q9VQE5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAMETILGIK GPDFVMLASD TMQAKSLVFM KDDQSKIHRL SDFNMMATVG
60 70 80 90 100
DGGDTIQFTD FISKNLHLYK ISHGYHLSAK SAAHFTRKTL ADYIRTNTRY
110 120 130 140 150
QVAMLLAGYD AVEGPDLHYI DSYGAAQSIN HAGHGWGSMF CGSILQRYWN
160 170 180 190 200
SKLSQEDAYS LMKKCVLEIQ RRLIINQRNF EVYVVDSKGM RKMEAINPGS
210
LNKESISLSW
Length:210
Mass (Da):23,721
Last modified:July 25, 2003 - v3
Checksum:i1B568F3FFCC3C3EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF51229.3.
AY119488 mRNA. Translation: AAM50142.1.
RefSeqiNP_001259950.1. NM_001273021.1.
NP_722823.2. NM_164491.3.
UniGeneiDm.2603.

Genome annotation databases

EnsemblMetazoaiFBtr0077699; FBpp0077383; FBgn0031443.
FBtr0332513; FBpp0304788; FBgn0031443.
GeneIDi33451.
KEGGidme:Dmel_CG17302.
UCSCiCG17302-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF51229.3 .
AY119488 mRNA. Translation: AAM50142.1 .
RefSeqi NP_001259950.1. NM_001273021.1.
NP_722823.2. NM_164491.3.
UniGenei Dm.2603.

3D structure databases

ProteinModelPortali Q9VQE5.
SMRi Q9VQE5. Positions 3-196.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 59678. 13 interactions.
IntActi Q9VQE5. 1 interaction.
MINTi MINT-1573384.

Protein family/group databases

MEROPSi T01.984.

Proteomic databases

PaxDbi Q9VQE5.
PRIDEi Q9VQE5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0077699 ; FBpp0077383 ; FBgn0031443 .
FBtr0332513 ; FBpp0304788 ; FBgn0031443 .
GeneIDi 33451.
KEGGi dme:Dmel_CG17302.
UCSCi CG17302-RA. d. melanogaster.

Organism-specific databases

CTDi 33451.
FlyBasei FBgn0031443. Prosbeta4R2.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00640000091536.
InParanoidi Q9VQE5.
KOi K02734.
OMAi NTRYQVA.
OrthoDBi EOG7N63NQ.
PhylomeDBi Q9VQE5.

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_230692. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_232776. Regulation of ornithine decarboxylase (ODC).
REACT_233284. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_234235. Hh ligand biogenesis disease.
REACT_234707. SCF(Skp2)-mediated degradation of p27/p21.
REACT_238120. degradation of DVL.
REACT_239151. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_242866. Degradation of beta-catenin by the destruction complex.
REACT_247767. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_250603. SCF-beta-TrCP mediated degradation of Emi1.
REACT_258701. Hedgehog ligand biogenesis.
REACT_260216. Ubiquitin-dependent degradation of Cyclin D1.
REACT_269395. GLI3 is processed to GLI3R by the proteasome.
REACT_271013. Degradation of GLI1 by the proteasome.
REACT_271479. Degradation of GLI2 by the proteasome.
REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

Miscellaneous databases

GenomeRNAii 33451.
NextBioi 783640.

Gene expression databases

Bgeei Q9VQE5.

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 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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  4. "Expression of proteasome subunit isoforms during spermatogenesis in Drosophila melanogaster."
    Ma J., Katz E., Belote J.M.
    Insect Mol. Biol. 11:627-639(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiPSB2_DROME
AccessioniPrimary (citable) accession number: Q9VQE5
Secondary accession number(s): Q8MRP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 25, 2003
Last modified: November 26, 2014
This is version 107 of the entry and version 3 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