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PSD8B_ARATH
ID   PSD8B_ARATH             Reviewed;         233 AA.
AC   Q9FHY0;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Putative 26S proteasome non-ATPase regulatory subunit 8 homolog B;
DE   AltName: Full=26S proteasome regulatory subunit RPN12b {ECO:0000303|PubMed:14623884};
DE            Short=AtRPN12b {ECO:0000303|PubMed:14623884};
DE   AltName: Full=26S proteasome regulatory subunit S14 homolog B;
GN   Name=RPN12B {ECO:0000303|PubMed:14623884};
GN   OrderedLocusNames=At5g42040 {ECO:0000312|Araport:AT5G42040};
GN   ORFNames=MJC20.14 {ECO:0000312|EMBL:BAB08437.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT   features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT   clones.";
RL   DNA Res. 6:183-195(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 75-233.
RC   STRAIN=cv. Columbia;
RX   PubMed=14623884; DOI=10.1074/jbc.m311977200;
RA   Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.;
RT   "Purification of the Arabidopsis 26 S proteasome: biochemical and molecular
RT   analyses revealed the presence of multiple isoforms.";
RL   J. Biol. Chem. 279:6401-6413(2004).
RN   [4]
RP   CHARACTERIZATION OF THE 26S PROTEASOME COMPLEX, AND SUBUNIT.
RX   PubMed=20516081; DOI=10.1074/jbc.m110.136622;
RA   Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.;
RT   "Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse
RT   array of plant proteolytic complexes.";
RL   J. Biol. Chem. 285:25554-25569(2010).
RN   [5]
RP   INTERACTION WITH UCH1 AND UCH2.
RX   PubMed=22951400; DOI=10.4161/psb.21899;
RA   Tian G., Lu Q., Kohalmi S.E., Rothstein S.J., Cui Y.;
RT   "Evidence that the Arabidopsis Ubiquitin C-terminal Hydrolases 1 and 2
RT   associate with the 26S proteasome and the TREX-2 complex.";
RL   Plant Signal. Behav. 7:1415-1419(2012).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       {ECO:0000250|UniProtKB:Q9SGW3}.
CC   -!- SUBUNIT: Component of the 19S regulatory particle (RP/PA700) lid
CC       subcomplex of the 26S proteasome. The 26S proteasome is composed of a
CC       core protease (CP), known as the 20S proteasome, capped at one or both
CC       ends by the 19S regulatory particle (RP/PA700). The RP/PA700 complex is
CC       composed of at least 17 different subunits in two subcomplexes, the
CC       base and the lid, which form the portions proximal and distal to the
CC       20S proteolytic core, respectively (PubMed:20516081). Interacts with
CC       UCH1 and UCH2 (PubMed:22951400). {ECO:0000269|PubMed:20516081,
CC       ECO:0000269|PubMed:22951400}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S14 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was not identified as subunit of the 26S proteasome complex
CC       (PubMed:20516081). Could be the product of a pseudogene.
CC       {ECO:0000305|PubMed:20516081}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB08437.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB017067; BAB08437.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED94758.1; -; Genomic_DNA.
DR   EMBL; AY258413; AAP83301.1; -; mRNA.
DR   RefSeq; NP_199019.2; NM_123569.3.
DR   AlphaFoldDB; Q9FHY0; -.
DR   BioGRID; 19459; 96.
DR   STRING; 3702.AT5G42040.1; -.
DR   PaxDb; Q9FHY0; -.
DR   PRIDE; Q9FHY0; -.
DR   EnsemblPlants; AT5G42040.1; AT5G42040.1; AT5G42040.
DR   GeneID; 834209; -.
DR   Gramene; AT5G42040.1; AT5G42040.1; AT5G42040.
DR   KEGG; ath:AT5G42040; -.
DR   Araport; AT5G42040; -.
DR   TAIR; locus:2165750; AT5G42040.
DR   eggNOG; KOG3151; Eukaryota.
DR   HOGENOM; CLU_046003_0_0_1; -.
DR   InParanoid; Q9FHY0; -.
DR   OMA; SEKAYDH; -.
DR   OrthoDB; 1183195at2759; -.
DR   PhylomeDB; Q9FHY0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FHY0; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR006746; 26S_Psome_Rpn12.
DR   InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR12387; PTHR12387; 2.
DR   Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   5: Uncertain;
KW   Acetylation; Proteasome; Reference proteome.
FT   CHAIN           1..233
FT                   /note="Putative 26S proteasome non-ATPase regulatory
FT                   subunit 8 homolog B"
FT                   /id="PRO_0000397123"
FT   DOMAIN          38..217
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SGW3"
SQ   SEQUENCE   233 AA;  26732 MW;  F41FD0693E0D9A08 CRC64;
     MDPQLMEVSQ QFERFKAAFI IKDFDTCSSL LSQLKLFDHY LISLSLNALL LLTCALFFLC
     TRNRIPPSPQ ENLIMGLNLL RLLVQNRIAE FHTELGLLSS ATLENPCIKH AVELEQSFME
     GAYNRVLSAR QTAPDETYVY FMDLLAKTIR DEIAGCSEKA YDHLSISEGC KMLLFSSDQQ
     LLTYVNEEHP EWEVKDGLVV FQKTRETAPC KEIPSLQLIN QTLSYTRELE RIL
 
 
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