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Protein

Proteasome subunit beta type

Gene

psmb8a

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Unreviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine proteaseUniRule annotation

Enzyme and pathway databases

ReactomeiR-DRE-1169091. Activation of NF-kappaB in B cells.
R-DRE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-DRE-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-DRE-174154. APC/C:Cdc20 mediated degradation of Securin.
R-DRE-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-DRE-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DRE-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-DRE-195253. Degradation of beta-catenin by the destruction complex.
R-DRE-202424. Downstream TCR signaling.
R-DRE-2467813. Separation of Sister Chromatids.
R-DRE-2871837. FCERI mediated NF-kB activation.
R-DRE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-DRE-350562. Regulation of ornithine decarboxylase (ODC).
R-DRE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-DRE-4608870. Asymmetric localization of PCP proteins.
R-DRE-4641257. Degradation of AXIN.
R-DRE-4641258. Degradation of DVL.
R-DRE-5358346. Hedgehog ligand biogenesis.
R-DRE-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DRE-5607764. CLEC7A (Dectin-1) signaling.
R-DRE-5610780. Degradation of GLI1 by the proteasome.
R-DRE-5632684. Hedgehog 'on' state.
R-DRE-5658442. Regulation of RAS by GAPs.
R-DRE-5668541. TNFR2 non-canonical NF-kB pathway.
R-DRE-5676590. NIK-->noncanonical NF-kB signaling.
R-DRE-5687128. MAPK6/MAPK4 signaling.
R-DRE-68827. CDT1 association with the CDC6:ORC:origin complex.
R-DRE-68949. Orc1 removal from chromatin.
R-DRE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-DRE-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-DRE-69481. G2/M Checkpoints.
R-DRE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-DRE-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-DRE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta typeUniRule annotation (EC:3.4.25.1UniRule annotation)
Gene namesi
Name:psmb8aImported
Synonyms:LMP7Imported, psmb8Imported
ORF Names:CH211-51F10.3-001Imported, psmb8-001Imported
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 19

Organism-specific databases

ZFINiZDB-GENE-990415-141. psmb8a.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation
  • Nucleus SAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

NucleusSAAS annotation, ProteasomeUniRule annotationImported

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.UniRule annotation

Protein-protein interaction databases

STRINGi7955.ENSDARP00000095608.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0175. Eukaryota.
ENOG410XQRP. LUCA.
GeneTreeiENSGT00510000046395.
HOGENOMiHOG000091082.
HOVERGENiHBG108297.
KOiK02740.
OMAiVHATHRD.
OrthoDBiEOG7FNC86.
TreeFamiTF106223.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O57330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLDVSGYK YNSASQFGFK QTLLDRSNHY SFGTKCQEFA VPVGVDPSKF
60 70 80 90 100
LKSCSCEDGV CIDLNHGTTT LAFKFRHGVI VAVDSRASAG KYIASKEANK
110 120 130 140 150
VIEINPYLLG TMSGSAADCQ YWERLLAKEC RLYKLRNKQR ISVSAASKLL
160 170 180 190 200
SNMMLGYRGM GLSMGSMICG WDKQGPGLYY VDDNGTRLSG RMFSTGCGNS
210 220 230 240 250
YAYGVVDSGY REDMTVEEAY ELGRRGIAHA THRDAYSGGV VNLYHMQEDG
260 270
WIKVCKEDVS ELIHRYKKGM F
Length:271
Mass (Da):30,086
Last modified:June 1, 1998 - v1
Checksum:i3233966FCEE07DB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FP074889 Genomic DNA. No translation available.
AF032390 mRNA. Translation: AAB87679.1.
BC162883 mRNA. Translation: AAI62883.1.
BC162902 mRNA. Translation: AAI62902.1.
AL672164 Genomic DNA. Translation: CAD87792.1.
BX510994 Genomic DNA. Translation: CAK04955.1.
RefSeqiNP_571467.3. NM_131392.3.
UniGeneiDr.7957.

Genome annotation databases

EnsembliENSDART00000104838; ENSDARP00000095608; ENSDARG00000001303.
GeneIDi30666.
KEGGidre:30666.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FP074889 Genomic DNA. No translation available.
AF032390 mRNA. Translation: AAB87679.1.
BC162883 mRNA. Translation: AAI62883.1.
BC162902 mRNA. Translation: AAI62902.1.
AL672164 Genomic DNA. Translation: CAD87792.1.
BX510994 Genomic DNA. Translation: CAK04955.1.
RefSeqiNP_571467.3. NM_131392.3.
UniGeneiDr.7957.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000095608.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000104838; ENSDARP00000095608; ENSDARG00000001303.
GeneIDi30666.
KEGGidre:30666.

Organism-specific databases

CTDi30666.
ZFINiZDB-GENE-990415-141. psmb8a.

Phylogenomic databases

eggNOGiKOG0175. Eukaryota.
ENOG410XQRP. LUCA.
GeneTreeiENSGT00510000046395.
HOGENOMiHOG000091082.
HOVERGENiHBG108297.
KOiK02740.
OMAiVHATHRD.
OrthoDBiEOG7FNC86.
TreeFamiTF106223.

Enzyme and pathway databases

ReactomeiR-DRE-1169091. Activation of NF-kappaB in B cells.
R-DRE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-DRE-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-DRE-174154. APC/C:Cdc20 mediated degradation of Securin.
R-DRE-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-DRE-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DRE-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-DRE-195253. Degradation of beta-catenin by the destruction complex.
R-DRE-202424. Downstream TCR signaling.
R-DRE-2467813. Separation of Sister Chromatids.
R-DRE-2871837. FCERI mediated NF-kB activation.
R-DRE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-DRE-350562. Regulation of ornithine decarboxylase (ODC).
R-DRE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-DRE-4608870. Asymmetric localization of PCP proteins.
R-DRE-4641257. Degradation of AXIN.
R-DRE-4641258. Degradation of DVL.
R-DRE-5358346. Hedgehog ligand biogenesis.
R-DRE-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DRE-5607764. CLEC7A (Dectin-1) signaling.
R-DRE-5610780. Degradation of GLI1 by the proteasome.
R-DRE-5632684. Hedgehog 'on' state.
R-DRE-5658442. Regulation of RAS by GAPs.
R-DRE-5668541. TNFR2 non-canonical NF-kB pathway.
R-DRE-5676590. NIK-->noncanonical NF-kB signaling.
R-DRE-5687128. MAPK6/MAPK4 signaling.
R-DRE-68827. CDT1 association with the CDC6:ORC:origin complex.
R-DRE-68949. Orc1 removal from chromatin.
R-DRE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-DRE-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-DRE-69481. G2/M Checkpoints.
R-DRE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-DRE-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-DRE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
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. "Linkage of LMP, TAP, and RING3 with Mhc class I rather than class II genes in the zebrafish."
    Takami K., Zaleska-Rutczynska Z., Figueroa F., Klein J.
    J. Immunol. 159:6052-6060(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Howden P.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. Pandian R.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  5. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: TuebingenImported.
  6. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TuebingenImported.

Entry informationi

Entry nameiO57330_DANRE
AccessioniPrimary (citable) accession number: O57330
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 1998
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.