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Protein

26S protease regulatory subunit 4

Gene

Rpt2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi225 – 2328ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • cell proliferation Source: FlyBase
  • cellular response to DNA damage stimulus Source: FlyBase
  • ER-associated ubiquitin-dependent protein catabolic process Source: GO_Central
  • mitotic spindle assembly Source: FlyBase
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: GO_Central
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.4.25.1. 1994.
ReactomeiR-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-DME-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-DME-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-DME-174154. APC/C:Cdc20 mediated degradation of Securin.
R-DME-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-DME-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-202424. Downstream TCR signaling.
R-DME-2467813. Separation of Sister Chromatids.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-350562. Regulation of ornithine decarboxylase (ODC).
R-DME-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-DME-4608870. Asymmetric localization of PCP proteins.
R-DME-4641257. Degradation of AXIN.
R-DME-4641258. Degradation of DVL.
R-DME-5358346. Hedgehog ligand biogenesis.
R-DME-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
R-DME-5610780. Degradation of GLI1 by the proteasome.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
R-DME-5632684. Hedgehog 'on' state.
R-DME-5658442. Regulation of RAS by GAPs.
R-DME-5668541. TNFR2 non-canonical NF-kB pathway.
R-DME-5676590. NIK-->noncanonical NF-kB signaling.
R-DME-68949. Orc1 removal from chromatin.
R-DME-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-DME-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-DME-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S protease regulatory subunit 4
Short name:
P26s4
Gene namesi
Name:Rpt2
Synonyms:P26s4, Pros26.4
ORF Names:CG5289
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0015282. Rpt2.

Subcellular locationi

GO - Cellular componenti

  • cytosolic proteasome complex Source: GO_Central
  • nuclear proteasome complex Source: GO_Central
  • proteasome regulatory particle Source: FlyBase
  • proteasome regulatory particle, base subcomplex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 43943926S protease regulatory subunit 4PRO_0000084682Add
BLAST

Proteomic databases

PaxDbiP48601.
PRIDEiP48601.

Expressioni

Gene expression databases

BgeeiP48601.
GenevisibleiP48601. DM.

Interactioni

Subunit structurei

Interacts with PSMD5.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi67764. 51 interactions.
DIPiDIP-17276N.
IntActiP48601. 27 interactions.
MINTiMINT-817128.
STRINGi7227.FBpp0083906.

Structurei

3D structure databases

ProteinModelPortaliP48601.
SMRiP48601. Positions 77-438.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0726. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00550000074818.
InParanoidiP48601.
KOiK03062.
OMAiVLLHHKN.
OrthoDBiEOG7F24ST.
PhylomeDBiP48601.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48601-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQNQSAQGG AGEKKDDKDK KKKYEPPIPT RVGKKKRRAK GPDAAMKLPQ
60 70 80 90 100
VTPHTRCRLK LLKLERIKDY LMMEDEFIRN QERLKPQDEK NEEERSKVDD
110 120 130 140 150
LRGTPMSVGN LEEIIDDNHA IVSTSVGSEH YVSILSFVDK DQLEPGCSVL
160 170 180 190 200
LNHKVHAVVG VLSDDTDPMV TVMKLEKAPQ ETYADIGGLD TQIQEIKESV
210 220 230 240 250
ELPLTHPEYY EEMGIKPPKG VILYGPPGTG KTLLAKAVAN QTSATFLRVV
260 270 280 290 300
GSELIQKYLG DGPKLVRELF RVAEEHAPSI VFIDEIDAVG TKRYDSNSGG
310 320 330 340 350
EREIQRTMLE LLNQLDGFDS RGDVKVIMAT NRIETLDPAL IRPGRIDRKI
360 370 380 390 400
EFPLPDEKTK RRIFTIHTSR MTLAEDVNLS ELIMAKDDLS GADIKAICTE
410 420 430
AGLMALRERR MKVTNEDFKK SKESVLYRKK EGTPEGLYL
Length:439
Mass (Da):49,324
Last modified:May 9, 2003 - v2
Checksum:iA7E210A292FDC96C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571C → A in AAB34134 (PubMed:8808288).Curated
Sequence conflicti172 – 1721V → M in AAB34134 (PubMed:8808288).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39303 mRNA. Translation: AAB34134.1.
AE014297 Genomic DNA. Translation: AAF56205.1.
AY058759 mRNA. Translation: AAL13988.1.
RefSeqiNP_001287493.1. NM_001300564.1.
NP_524469.2. NM_079745.4.
UniGeneiDm.2368.

Genome annotation databases

EnsemblMetazoaiFBtr0084520; FBpp0083906; FBgn0015282.
FBtr0346154; FBpp0311982; FBgn0015282.
GeneIDi42828.
KEGGidme:Dmel_CG5289.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39303 mRNA. Translation: AAB34134.1.
AE014297 Genomic DNA. Translation: AAF56205.1.
AY058759 mRNA. Translation: AAL13988.1.
RefSeqiNP_001287493.1. NM_001300564.1.
NP_524469.2. NM_079745.4.
UniGeneiDm.2368.

3D structure databases

ProteinModelPortaliP48601.
SMRiP48601. Positions 77-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67764. 51 interactions.
DIPiDIP-17276N.
IntActiP48601. 27 interactions.
MINTiMINT-817128.
STRINGi7227.FBpp0083906.

Proteomic databases

PaxDbiP48601.
PRIDEiP48601.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084520; FBpp0083906; FBgn0015282.
FBtr0346154; FBpp0311982; FBgn0015282.
GeneIDi42828.
KEGGidme:Dmel_CG5289.

Organism-specific databases

CTDi42828.
FlyBaseiFBgn0015282. Rpt2.

Phylogenomic databases

eggNOGiKOG0726. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00550000074818.
InParanoidiP48601.
KOiK03062.
OMAiVLLHHKN.
OrthoDBiEOG7F24ST.
PhylomeDBiP48601.

Enzyme and pathway databases

BRENDAi3.4.25.1. 1994.
ReactomeiR-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-DME-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-DME-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-DME-174154. APC/C:Cdc20 mediated degradation of Securin.
R-DME-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-DME-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-202424. Downstream TCR signaling.
R-DME-2467813. Separation of Sister Chromatids.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-350562. Regulation of ornithine decarboxylase (ODC).
R-DME-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-DME-4608870. Asymmetric localization of PCP proteins.
R-DME-4641257. Degradation of AXIN.
R-DME-4641258. Degradation of DVL.
R-DME-5358346. Hedgehog ligand biogenesis.
R-DME-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
R-DME-5610780. Degradation of GLI1 by the proteasome.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
R-DME-5632684. Hedgehog 'on' state.
R-DME-5658442. Regulation of RAS by GAPs.
R-DME-5668541. TNFR2 non-canonical NF-kB pathway.
R-DME-5676590. NIK-->noncanonical NF-kB signaling.
R-DME-68949. Orc1 removal from chromatin.
R-DME-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-DME-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-DME-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPros26.4. fly.
GenomeRNAii42828.
PROiP48601.

Gene expression databases

BgeeiP48601.
GenevisibleiP48601. DM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic organization and mapping of the mouse P26s4 ATPase gene: a member of the remarkably conserved AAA gene family."
    Hoyle J., Fisher E.M.C.
    Genomics 31:115-118(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Embryo.
  5. "Proteasome regulation by ADP-ribosylation."
    Cho-Park P.F., Steller H.
    Cell 153:614-627(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSMD5.

Entry informationi

Entry nameiPRS4_DROME
AccessioniPrimary (citable) accession number: P48601
Secondary accession number(s): Q9VCG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 9, 2003
Last modified: July 6, 2016
This is version 139 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.