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Q9VNA5

- PSB4_DROME

UniProt

Q9VNA5 - PSB4_DROME

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Protein

Proteasome subunit beta type-4

Gene

Prosbeta7

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 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. cell proliferation Source: FlyBase
  2. cellular process Source: FlyBase
  3. cellular response to DNA damage stimulus Source: FlyBase
  4. centrosome organization Source: FlyBase
  5. mitotic spindle elongation Source: FlyBase
  6. mitotic spindle organization Source: FlyBase
  7. neurogenesis Source: FlyBase
  8. proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase
  9. spindle assembly involved in mitosis 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.

Protein family/group databases

MEROPSiT01.987.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-4 (EC:3.4.25.1)
Alternative name(s):
Proteasome subunit beta type-7
Gene namesi
Name:Prosbeta7
Synonyms:Prosb4, Prosbeta4
ORF Names:CG12000
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0250746. Prosbeta7.

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: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 268268Proteasome subunit beta type-4PRO_0000148071Add
BLAST

Proteomic databases

PaxDbiQ9VNA5.
PRIDEiQ9VNA5.

Expressioni

Gene expression databases

BgeeiQ9VNA5.

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

BioGridi65850. 41 interactions.
DIPiDIP-19164N.
IntActiQ9VNA5. 8 interactions.
MINTiMINT-924269.

Structurei

3D structure databases

ProteinModelPortaliQ9VNA5.
SMRiQ9VNA5. Positions 37-265.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00390000000698.
InParanoidiQ9VNA5.
KOiK02736.
OMAiRIMRVND.
OrthoDBiEOG74FF1D.
PhylomeDBiQ9VNA5.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VNA5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLNNYNSLAQ PMWQNGPAPG EFYNFTGGQT PVQQLPRELT TMGPYGTKHS
60 70 80 90 100
TASSTTGTSV LGIRYDSGVM LAADTLVSYG SMARYQNIER VFKVNKNILL
110 120 130 140 150
GGSGDFADIQ SIKRNIDQKM IEDQCCDDNI EMKPKSLASW MTRVLYNRRS
160 170 180 190 200
RMNPLYIDVV VGGVDNEGTP YLANVDLRGR SYEDYVVATG FARHLAVPLV
210 220 230 240 250
REKKPKDRDF TAVEASELIR TCMEVLYYRD TRNISQYTVG VCSVNGCGVE
260
GPFQVNENWT FAETIKGY
Length:268
Mass (Da):29,986
Last modified:May 1, 2000 - v1
Checksum:i215433952659EAD0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF52041.1.
AE014297 Genomic DNA. Translation: AAN13277.1.
AY118936 mRNA. Translation: AAM50796.1.
RefSeqiNP_649529.1. NM_141272.1.
NP_730922.1. NM_169049.2.
UniGeneiDm.11642.

Genome annotation databases

EnsemblMetazoaiFBtr0078805; FBpp0078448; FBgn0250746.
FBtr0078806; FBpp0078449; FBgn0250746.
GeneIDi40639.
KEGGidme:Dmel_CG12000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF52041.1 .
AE014297 Genomic DNA. Translation: AAN13277.1 .
AY118936 mRNA. Translation: AAM50796.1 .
RefSeqi NP_649529.1. NM_141272.1.
NP_730922.1. NM_169049.2.
UniGenei Dm.11642.

3D structure databases

ProteinModelPortali Q9VNA5.
SMRi Q9VNA5. Positions 37-265.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 65850. 41 interactions.
DIPi DIP-19164N.
IntActi Q9VNA5. 8 interactions.
MINTi MINT-924269.

Protein family/group databases

MEROPSi T01.987.

Proteomic databases

PaxDbi Q9VNA5.
PRIDEi Q9VNA5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0078805 ; FBpp0078448 ; FBgn0250746 .
FBtr0078806 ; FBpp0078449 ; FBgn0250746 .
GeneIDi 40639.
KEGGi dme:Dmel_CG12000.

Organism-specific databases

CTDi 40639.
FlyBasei FBgn0250746. Prosbeta7.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00390000000698.
InParanoidi Q9VNA5.
KOi K02736.
OMAi RIMRVND.
OrthoDBi EOG74FF1D.
PhylomeDBi Q9VNA5.

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 40639.
NextBioi 819792.
PROi Q9VNA5.

Gene expression databases

Bgeei Q9VNA5.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PIRSFi PIRSF001213. Psome_endopept_beta. 1 hit.
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: Embryo.
  4. "Genes required for mitotic spindle assembly in Drosophila S2 cells."
    Goshima G., Wollman R., Goodwin S.S., Zhang N., Scholey J.M., Vale R.D., Stuurman N.
    Science 316:417-421(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiPSB4_DROME
AccessioniPrimary (citable) accession number: Q9VNA5
Secondary accession number(s): A4V2F4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 113 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