SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P40301

- PSA2_DROME

UniProt

P40301 - PSA2_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Proteasome subunit alpha type-2

Gene
Prosalpha2, PROS-25, Pros25, CG5266
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 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.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. cell proliferation Source: FlyBase
  2. cellular process Source: FlyBase
  3. mitotic spindle elongation Source: FlyBase
  4. mitotic spindle organization Source: FlyBase
  5. 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 alpha type-2 (EC:3.4.25.1)
Alternative name(s):
PROS-Dm25
Proteasome 25 kDa subunit
Gene namesi
Name:Prosalpha2
Synonyms:PROS-25, Pros25
ORF Names:CG5266
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0086134. Prosalpha2.

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
  4. proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 234234Proteasome subunit alpha type-2PRO_0000124083Add
BLAST

Proteomic databases

PaxDbiP40301.
PRIDEiP40301.

Expressioni

Gene expression databases

BgeeiP40301.

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. Interacts with Rpn6.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Prosalpha3P180533EBI-98978,EBI-138951
Prosbeta4Q9VJJ03EBI-98978,EBI-90888

Protein-protein interaction databases

BioGridi66629. 43 interactions.
DIPiDIP-20541N.
IntActiP40301. 19 interactions.
MINTiMINT-795880.
STRINGi7227.FBpp0082062.

Structurei

3D structure databases

ProteinModelPortaliP40301.
SMRiP40301. Positions 2-233.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074870.
InParanoidiP40301.
KOiK02726.
OMAiWKATALG.
OrthoDBiEOG71VSTG.
PhylomeDBiP40301.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40301-1 [UniParc]FASTAAdd to Basket

« Hide

MATERYSFSL TTFSPSGKLV QLEYALAAVS GGAPSVGIIA SNGVVIATEN    50
KHKSPLYEQH SVHRVEMIYN HIGMVYSGMG PDYRLLVKQA RKIAQTYYLT 100
YKEPIPVSQL VQRVATLMQE YTQSGGVRPF GVSLLICGWD NDRPYLYQSD 150
PSGAYFAWKA TAMGKNAVNG KTFLEKRYSE DLELDDAVHT AILTLKEGFE 200
GKMTADNIEI GICDQNGFQR LDPASIKDYL ASIP 234
Length:234
Mass (Da):25,907
Last modified:February 1, 1995 - v1
Checksum:iBC6F98060BD9D7C2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X70304 Genomic DNA. Translation: CAA49783.1.
AE014297 Genomic DNA. Translation: AAF54814.1.
AY069280 mRNA. Translation: AAL39425.1.
PIRiS36116.
RefSeqiNP_524328.1. NM_079604.2.
UniGeneiDm.2198.

Genome annotation databases

EnsemblMetazoaiFBtr0082590; FBpp0082062; FBgn0086134.
GeneIDi41531.
KEGGidme:Dmel_CG5266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X70304 Genomic DNA. Translation: CAA49783.1 .
AE014297 Genomic DNA. Translation: AAF54814.1 .
AY069280 mRNA. Translation: AAL39425.1 .
PIRi S36116.
RefSeqi NP_524328.1. NM_079604.2.
UniGenei Dm.2198.

3D structure databases

ProteinModelPortali P40301.
SMRi P40301. Positions 2-233.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 66629. 43 interactions.
DIPi DIP-20541N.
IntActi P40301. 19 interactions.
MINTi MINT-795880.
STRINGi 7227.FBpp0082062.

Proteomic databases

PaxDbi P40301.
PRIDEi P40301.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0082590 ; FBpp0082062 ; FBgn0086134 .
GeneIDi 41531.
KEGGi dme:Dmel_CG5266.

Organism-specific databases

CTDi 41531.
FlyBasei FBgn0086134. Prosalpha2.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074870.
InParanoidi P40301.
KOi K02726.
OMAi WKATALG.
OrthoDBi EOG71VSTG.
PhylomeDBi P40301.

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 41531.
NextBioi 824277.
PROi P40301.

Gene expression databases

Bgeei P40301.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and genomic organization of the Drosophila proteasome PROS-Dm25 gene."
    Seelig A., Troxell M., Kloetzel P.-M.
    Biochim. Biophys. Acta 1174:215-217(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S.
  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(2000) [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: Ovary.
  5. "The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together."
    Pathare G.R., Nagy I., Bohn S., Unverdorben P., Hubert A., Korner R., Nickell S., Lasker K., Sali A., Tamura T., Nishioka T., Forster F., Baumeister W., Bracher A.
    Proc. Natl. Acad. Sci. U.S.A. 109:149-154(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPN6.

Entry informationi

Entry nameiPSA2_DROME
AccessioniPrimary (citable) accession number: P40301
Secondary accession number(s): Q9VG71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 3, 2014
This is version 128 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