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26S proteasome non-ATPase regulatory subunit 8 homolog A (26S proteasome regulatory subunit RPN12a) (AtRPN12a) (26S proteasome regulatory subunit S14 homolog A)

 PSD8A_ARATH             Reviewed;         267 AA.
Q9SGW3; Q6XJF4;
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-APR-2021, entry version 128.
RecName: Full=26S proteasome non-ATPase regulatory subunit 8 homolog A;
AltName: Full=26S proteasome regulatory subunit RPN12a {ECO:0000303|PubMed:14623884};
Short=AtRPN12a {ECO:0000303|PubMed:14623884};
AltName: Full=26S proteasome regulatory subunit S14 homolog A;
Name=RPN12A {ECO:0000303|PubMed:14623884};
OrderedLocusNames=At1g64520 {ECO:0000312|Araport:AT1G64520};
ORFNames=F1N19.9 {ECO:0000312|EMBL:AAF19671.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY,
AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=14623884; DOI=10.1074/jbc.m311977200;
Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.;
"Purification of the Arabidopsis 26 S proteasome: biochemical and molecular
analyses revealed the presence of multiple isoforms.";
J. Biol. Chem. 279:6401-6413(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana reference
genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, IDENTIFICATION IN THE 26S PROTEASOME, INDUCTION, AND DISRUPTION
PHENOTYPE.
PubMed=11826296; DOI=10.1105/tpc.010381;
Smalle J., Kurepa J., Yang P., Babiychuk E., Kushnir S., Durski A.,
Vierstra R.D.;
"Cytokinin growth responses in Arabidopsis involve the 26S proteasome
subunit RPN12.";
Plant Cell 14:17-32(2002).
[6]
INTERACTION WITH PUB22 AND PUB23, AND UBIQUITINATION.
PubMed=18664614; DOI=10.1105/tpc.108.060699;
Cho S.K., Ryu M.Y., Song C., Kwak J.M., Kim W.T.;
"Arabidopsis PUB22 and PUB23 are homologous U-Box E3 ubiquitin ligases that
play combinatory roles in response to drought stress.";
Plant Cell 20:1899-1914(2008).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17971041; DOI=10.1111/j.1365-313x.2007.03322.x;
Kurepa J., Toh-E A., Smalle J.A.;
"26S proteasome regulatory particle mutants have increased oxidative stress
tolerance.";
Plant J. 53:102-114(2008).
[8]
INTERACTION WITH TIF3E1.
PubMed=19704582; DOI=10.4161/psb.3.6.5434;
Paz-Aviram T., Yahalom A., Chamovitz D.A.;
"Arabidopsis eIF3e interacts with subunits of the ribosome, Cop9
signalosome and proteasome.";
Plant Signal. Behav. 3:409-411(2008).
[9]
FUNCTION.
PubMed=19812900; DOI=10.1007/s10059-009-0132-x;
Ryu M.Y., Cho S.K., Kim W.T.;
"RNAi suppression of RPN12a decreases the expression of type-A ARRs,
negative regulators of cytokinin signaling pathway, in Arabidopsis.";
Mol. Cells 28:375-382(2009).
[10]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19321709; DOI=10.1104/pp.109.135970;
Kurepa J., Wang S., Li Y., Zaitlin D., Pierce A.J., Smalle J.A.;
"Loss of 26S proteasome function leads to increased cell size and decreased
cell number in Arabidopsis shoot organs.";
Plant Physiol. 150:178-189(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
COMPLEX, SUBUNIT, AND ACETYLATION AT MET-1.
PubMed=20516081; DOI=10.1074/jbc.m110.136622;
Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.;
"Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse
array of plant proteolytic complexes.";
J. Biol. Chem. 285:25554-25569(2010).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.m111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[13]
INTERACTION WITH UCH1 AND UCH2.
PubMed=22951400; DOI=10.4161/psb.21899;
Tian G., Lu Q., Kohalmi S.E., Rothstein S.J., Cui Y.;
"Evidence that the Arabidopsis Ubiquitin C-terminal Hydrolases 1 and 2
associate with the 26S proteasome and the TREX-2 complex.";
Plant Signal. Behav. 7:1415-1419(2012).
-!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
involved in the ATP-dependent degradation of ubiquitinated proteins.
May help to control the degradation of one or more factors that repress
cytokinin signaling. Plays an important role for balancing cell
expansion with cell proliferation rates during shoot development.
{ECO:0000269|PubMed:11826296, ECO:0000269|PubMed:17971041,
ECO:0000269|PubMed:19321709, ECO:0000269|PubMed:19812900}.
-!- SUBUNIT: Component of the 19S regulatory particle (RP/PA700) lid
subcomplex of the 26S proteasome. The 26S proteasome is composed of a
core protease (CP), known as the 20S proteasome, capped at one or both
ends by the 19S regulatory particle (RP/PA700). The RP/PA700 complex is
composed of at least 17 different subunits in two subcomplexes, the
base and the lid, which form the portions proximal and distal to the
20S proteolytic core, respectively. Interacts with PUB22 and PUB23.
Binds to the translation initiation factors TIF3E1 (PubMed:19704582).
Interacts with UCH1 and UCH2 (PubMed:22951400).
{ECO:0000269|PubMed:11826296, ECO:0000269|PubMed:14623884,
ECO:0000269|PubMed:18664614, ECO:0000269|PubMed:19704582,
ECO:0000269|PubMed:20516081, ECO:0000269|PubMed:22951400}.
-!- INTERACTION:
Q9SGW3; P46639: KNAT1; NbExp=3; IntAct=EBI-594133, EBI-530486;
Q9SGW3; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-594133, EBI-15192297;
-!- TISSUE SPECIFICITY: Ubiquitous with highest expression in flowers.
{ECO:0000269|PubMed:14623884}.
-!- INDUCTION: By cytokinins. {ECO:0000269|PubMed:11826296}.
-!- PTM: Ubiquitinated by PUB22 and PUB23. {ECO:0000269|PubMed:18664614}.
-!- DISRUPTION PHENOTYPE: Decreased rate of leaf formation, reduced root
elongation, delayed skotomorphogenesis and altered growth responses to
exogenous cytokinins. Increased sensitivity to heat shock and increased
tolerance to oxidative stress. Decreased 26S proteasome accumulation.
In flowers and cotyledons, epidermal cells were larger than those in
the wild type. {ECO:0000269|PubMed:11826296,
ECO:0000269|PubMed:17971041, ECO:0000269|PubMed:19321709}.
-!- SIMILARITY: Belongs to the proteasome subunit S14 family.
{ECO:0000305}.
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EMBL; AY230846; AAP86673.1; -; mRNA.
EMBL; AY230847; AAP86674.1; -; mRNA.
EMBL; AC009519; AAF19671.1; -; Genomic_DNA.
EMBL; CP002684; AEE34249.1; -; Genomic_DNA.
EMBL; AF410265; AAK95251.1; -; mRNA.
EMBL; AY039857; AAK63961.1; -; mRNA.
EMBL; AY143888; AAN28827.1; -; mRNA.
PIR; H96668; H96668.
RefSeq; NP_176633.1; NM_105127.4.
BioGRID; 27981; 10.
IntAct; Q9SGW3; 8.
STRING; 3702.AT1G64520.1; -.
iPTMnet; Q9SGW3; -.
SwissPalm; Q9SGW3; -.
PaxDb; Q9SGW3; -.
PRIDE; Q9SGW3; -.
ProteomicsDB; 226351; -.
DNASU; 842760; -.
EnsemblPlants; AT1G64520.1; AT1G64520.1; AT1G64520.
GeneID; 842760; -.
Gramene; AT1G64520.1; AT1G64520.1; AT1G64520.
KEGG; ath:AT1G64520; -.
Araport; AT1G64520; -.
TAIR; locus:2019504; AT1G64520.
eggNOG; KOG3151; Eukaryota.
HOGENOM; CLU_046003_0_0_1; -.
InParanoid; Q9SGW3; -.
OMA; LEIGAFW; -.
OrthoDB; 1183195at2759; -.
PhylomeDB; Q9SGW3; -.
PRO; PR:Q9SGW3; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9SGW3; baseline and differential.
Genevisible; Q9SGW3; AT.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; HDA:TAIR.
GO; GO:0000502; C:proteasome complex; IDA:TAIR.
GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
GO; GO:0048825; P:cotyledon development; IMP:TAIR.
GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0009908; P:flower development; IMP:TAIR.
GO; GO:0048366; P:leaf development; IMP:TAIR.
GO; GO:0048528; P:post-embryonic root development; IMP:TAIR.
GO; GO:0043248; P:proteasome assembly; IMP:TAIR.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:TAIR.
GO; GO:0030163; P:protein catabolic process; TAS:TAIR.
GO; GO:0031540; P:regulation of anthocyanin biosynthetic process; IMP:TAIR.
GO; GO:0009733; P:response to auxin; IMP:TAIR.
GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
GO; GO:0009408; P:response to heat; IMP:TAIR.
GO; GO:0051788; P:response to misfolded protein; IMP:TAIR.
GO; GO:0009647; P:skotomorphogenesis; IMP:TAIR.
InterPro; IPR006746; 26S_Psome_Rpn12.
InterPro; IPR033464; CSN8_PSD8_EIF3K.
InterPro; IPR000717; PCI_dom.
PANTHER; PTHR12387; PTHR12387; 1.
Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
PROSITE; PS50250; PCI; 1.
1: Evidence at protein level;
Acetylation; Cytokinin signaling pathway; Proteasome; Reference proteome;
Ubl conjugation.
CHAIN 1..267
/note="26S proteasome non-ATPase regulatory subunit 8
homolog A"
/id="PRO_0000397122"
DOMAIN 79..251
/note="PCI"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000269|PubMed:20516081,
ECO:0007744|PubMed:22223895"
CONFLICT 182
/note="T -> P (in Ref. 1; AAP86674)"
/evidence="ECO:0000305"
SEQUENCE 267 AA; 30706 MW; D3EC626161AAA4E8 CRC64;
MDPQLTEVSQ QFERFKAAFA RKDYNTCSDL LSQLKVLLTK FTSLPPLFEN SPNAAKELTI
ARDIYEHAVV LSVKTEDQDA FERDFFQLKP YYVDARNRIP QSPQENLILG LNLLRLLVQN
RIAEFHTELE LLSSATLEDP CIKHAVELEQ SFMEGAYNRV LSARQTAPDA TYVYFMDLLA
KTIRDEIAGC SEKAYDYVSI SDARQMLLFS SDQELLTYVT DEHPEWEVKE GFVVFQKAKE
TAPCKEIPSL QLINQTLSYA RELERIV


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WP1240: Proteasome Degradation
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WP158: Proteasome Degradation
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Related Genes :
[RPN12A At1g64520 F1N19.9] 26S proteasome non-ATPase regulatory subunit 8 homolog A (26S proteasome regulatory subunit RPN12a) (AtRPN12a) (26S proteasome regulatory subunit S14 homolog A)
[RPT2A HLR At4g29040 F19B15.70 F25O24.6] 26S proteasome regulatory subunit 4 homolog A (26S proteasome AAA-ATPase subunit RPT2a) (26S proteasome subunit 4 homolog A) (Protein HALTED ROOT) (Regulatory particle triple-A ATPase subunit 2a)
[PSMD8] 26S proteasome non-ATPase regulatory subunit 8 (26S proteasome regulatory subunit RPN12) (26S proteasome regulatory subunit S14) (p31)
[RPT5B TBP1 At1g09100 F7G19.2] 26S proteasome regulatory subunit 6A homolog B (26S proteasome AAA-ATPase subunit RPT5b) (Proteasome 26S subunit 6A homolog B) (Regulatory particle triple-A ATPase subunit 5b) (Tat-binding protein 1 homolog B) (TBP-1 homolog B)
[RPT5A ATS6A.2 TBP1 At3g05530 F22F7.1] 26S proteasome regulatory subunit 6A homolog A (26S proteasome AAA-ATPase subunit RPT5a) (Proteasome 26S subunit 6A homolog A) (Regulatory particle triple-A ATPase subunit 5a) (Tat-binding protein 1 homolog A) (TBP-1 homolog A)
[RPT2B At2g20140 T2G17.6] 26S proteasome regulatory subunit 4 homolog B (26S proteasome AAA-ATPase subunit RPT2b) (26S proteasome subunit 4 homolog B) (Regulatory particle triple-A ATPase subunit 2b)
[RPN1A At2g20580 F23N11.10] 26S proteasome non-ATPase regulatory subunit 2 homolog A (26S proteasome regulatory subunit RPN1a) (AtRPN1a) (26S proteasome regulatory subunit S2 homolog A)
[RPN10 MBP1 MCB1 At4g38630 F20M13.190 T9A14.7] 26S proteasome non-ATPase regulatory subunit 4 homolog (26S proteasome regulatory subunit RPN10) (AtRPN10) (26S proteasome regulatory subunit S5A homolog) (Multiubiquitin chain-binding protein 1) (AtMCB1)
[RPN8A AE3 MOV34 At5g05780 MJJ3.19] 26S proteasome non-ATPase regulatory subunit 7 homolog A (26S proteasome regulatory subunit RPN8a) (AtRPN8a) (Protein ASYMMETRIC LEAVES ENHANCER 3) (Protein MOV34) (AtMOV34)
[PSMD7 MOV34L] 26S proteasome non-ATPase regulatory subunit 7 (26S proteasome regulatory subunit RPN8) (26S proteasome regulatory subunit S12) (Mov34 protein homolog) (Proteasome subunit p40)
[RPT3 BIM409 At5g58290 MCK7.16] 26S proteasome regulatory subunit 6B homolog (26S protease subunit 6B homolog) (26S proteasome AAA-ATPase subunit RPT3) (Protein BMAA insensitive morphology 409) (Regulatory particle triple-A ATPase subunit 3)
[RPN3A EMB2719 HAP15 At1g20200 T20H2.3] 26S proteasome non-ATPase regulatory subunit 3 homolog A (26S proteasome regulatory subunit RPN3a) (AtRPN3a) (26S proteasome regulatory subunit S3 homolog A) (Protein EMBRYO DEFECTIVE 2719) (Protein HAPLESS 15)
[PSMC5 SUG1] 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (Thyroid hormone receptor-interacting protein 1) (TRIP1) (p45/SUG)
[RPT4A At5g43010 MBD2.21] 26S proteasome regulatory subunit 10B homolog A (26S proteasome AAA-ATPase subunit RPT4a) (26S proteasome subunit 10B homolog A) (Regulatory particle triple-A ATPase subunit 4a)
[RPN5B At5g64760 MVP7.9] 26S proteasome non-ATPase regulatory subunit 12 homolog B (26S proteasome regulatory subunit RPN5b) (AtRPN5b) (26S proteasome regulatory subunit p55 homolog B)
[PSMD1] 26S proteasome non-ATPase regulatory subunit 1 (26S proteasome regulatory subunit RPN2) (26S proteasome regulatory subunit S1) (26S proteasome subunit p112)
[Psmc5 Sug1] 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (p45/SUG) (mSUG1)
[PSMD14 POH1] 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (26S proteasome-associated PAD1 homolog 1)
[PSMD6 KIAA0107 PFAAP4] 26S proteasome non-ATPase regulatory subunit 6 (26S proteasome regulatory subunit RPN7) (26S proteasome regulatory subunit S10) (Breast cancer-associated protein SGA-113M) (Phosphonoformate immuno-associated protein 4) (Proteasome regulatory particle subunit p44S10) (p42A)
[RPT4B At1g45000 F27F5.8] 26S proteasome regulatory subunit S10B homolog B (26S proteasome AAA-ATPase subunit RPT4b) (26S proteasome subunit S10B homolog B) (Regulatory particle triple-A ATPase subunit 4b)
[PSMD4 MCB1] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Antisecretory factor 1) (AF) (ASF) (Multiubiquitin chain-binding protein)
[Rpn10 PROS-54 Pros54 CG7619] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (54 kDa subunit of mu particle) (Multiubiquitin chain-binding protein) (p54)
[PSMC3 TBP1] 26S proteasome regulatory subunit 6A (26S proteasome AAA-ATPase subunit RPT5) (Proteasome 26S subunit ATPase 3) (Proteasome subunit P50) (Tat-binding protein 1) (TBP-1)
[PSMD2 TRAP2] 26S proteasome non-ATPase regulatory subunit 2 (26S proteasome regulatory subunit RPN1) (26S proteasome regulatory subunit S2) (26S proteasome subunit p97) (Protein 55.11) (Tumor necrosis factor type 1 receptor-associated protein 2)
[Psmd4 Mcb1] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Multiubiquitin chain-binding protein)
[Psmc5 Sug1] 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (Thyroid hormone receptor-interacting protein 1) (TRIP1) (p45/SUG)
[PSMD11] 26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory subunit RPN6) (26S proteasome regulatory subunit S9) (26S proteasome regulatory subunit p44.5)
[PSMD13] 26S proteasome non-ATPase regulatory subunit 13 (26S proteasome regulatory subunit RPN9) (26S proteasome regulatory subunit S11) (26S proteasome regulatory subunit p40.5)
[RPT6 CIM3 CRL3 SUG1 TBPY TBY1 YGL048C] 26S proteasome regulatory subunit 8 homolog (Protein CIM3) (Protein SUG1) (Tat-binding protein TBY1)
[PSMD3] 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3) (26S proteasome regulatory subunit S3) (Proteasome subunit p58)

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