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PS11B_DANRE
ID   PS11B_DANRE             Reviewed;         422 AA.
AC   F1QGH9; Q7ZTZ8;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 11B;
DE   AltName: Full=26S proteasome regulatory subunit RPN6-B;
GN   Name=psmd11b;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the lid subcomplex of the 26S proteasome, a
CC       multiprotein complex involved in the ATP-dependent degradation of
CC       ubiquitinated proteins. In the complex, psmd11b is required for
CC       proteasome assembly (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the lid subcomplex of the 19S proteasome
CC       regulatory particle complex (also named PA700 complex). The 26S
CC       proteasome consists of a 20S proteasome core and two 19S regulatory
CC       subunits (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S9 family. {ECO:0000305}.
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DR   EMBL; CR391936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC051618; AAH51618.1; -; mRNA.
DR   EMBL; BC063978; AAH63978.1; -; mRNA.
DR   RefSeq; NP_955886.1; NM_199592.1.
DR   AlphaFoldDB; F1QGH9; -.
DR   SMR; F1QGH9; -.
DR   STRING; 7955.ENSDARP00000020942; -.
DR   PaxDb; F1QGH9; -.
DR   Ensembl; ENSDART00000016283; ENSDARP00000020942; ENSDARG00000005134.
DR   Ensembl; ENSDART00000164156; ENSDARP00000133045; ENSDARG00000005134.
DR   GeneID; 322265; -.
DR   KEGG; dre:322265; -.
DR   CTD; 322265; -.
DR   ZFIN; ZDB-GENE-030131-984; psmd11b.
DR   eggNOG; KOG1463; Eukaryota.
DR   GeneTree; ENSGT00530000063301; -.
DR   InParanoid; F1QGH9; -.
DR   OrthoDB; 1052430at2759; -.
DR   PhylomeDB; F1QGH9; -.
DR   TreeFam; TF106230; -.
DR   Reactome; R-DRE-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-DRE-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-DRE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-DRE-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-DRE-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-DRE-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-DRE-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-DRE-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-DRE-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DRE-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-DRE-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-DRE-382556; ABC-family proteins mediated transport.
DR   Reactome; R-DRE-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-DRE-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-DRE-4641257; Degradation of AXIN.
DR   Reactome; R-DRE-4641258; Degradation of DVL.
DR   Reactome; R-DRE-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-DRE-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-DRE-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-DRE-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-DRE-5632684; Hedgehog 'on' state.
DR   Reactome; R-DRE-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-DRE-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-DRE-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-DRE-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-DRE-5689603; UCH proteinases.
DR   Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   Reactome; R-DRE-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-DRE-68949; Orc1 removal from chromatin.
DR   Reactome; R-DRE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-DRE-69481; G2/M Checkpoints.
DR   Reactome; R-DRE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-DRE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-DRE-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-DRE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-DRE-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-DRE-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-DRE-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-DRE-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-DRE-8951664; Neddylation.
DR   Reactome; R-DRE-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-DRE-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:F1QGH9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 12.
DR   Bgee; ENSDARG00000005134; Expressed in muscle tissue and 26 other tissues.
DR   ExpressionAtlas; F1QGH9; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0043248; P:proteasome assembly; ISS:UniProtKB.
DR   GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR040780; Rpn6_C_helix.
DR   InterPro; IPR040773; Rpn6_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF18503; RPN6_C_helix; 1.
DR   Pfam; PF18055; RPN6_N; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..422
FT                   /note="26S proteasome non-ATPase regulatory subunit 11B"
FT                   /id="PRO_0000419980"
FT   DOMAIN          228..392
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   CONFLICT        217
FT                   /note="I -> T (in Ref. 2; AAH63978/AAH51618)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  47577 MW;  4B9E8A7BE4BE8F31 CRC64;
     MAAAAVVEFQ RAQSLISTDR NASIDIFHSI VRRDVQEDDE EAVRVKEQSI LELGSLLAKT
     GQAAELGGLL KFVRPFLISI SKAKAARLVR SLLDLFLDME AATGQEVELC LECIEWAKAE
     KRTFLRQALE ARLISLYFDT KRYQEALQLE SQLLQELKKM DDKALLVEVQ LLESKTYHAL
     SNLPKARAAL TSARTTANAI YCPPKLQAAL DMQSGIIHAA EEKDWKTAYS YFFEAFEGYD
     SIDSPRAVTA LKYMLLCKIM LSLPEEVQAL ISGKLGLRYA GRQTDALKCI AQASKNRSLA
     DFEKALTEYT KELRDDPIIN THLAKLYDNL LEQNLIRVIE PFSRVQITHI AGLIKLSKND
     VERKLSQMIL DKKFHGILDQ GEDVLIIFEE PPVDKTYEAA LETIQNMSKV VDSLYNKAKK
     LT
 
 
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