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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)

 PSMD4_ARATH             Reviewed;         386 AA.
P55034; Q8L9G3;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
23-FEB-2022, entry version 162.
RecName: Full=26S proteasome non-ATPase regulatory subunit 4 homolog;
AltName: Full=26S proteasome regulatory subunit RPN10;
Short=AtRPN10;
AltName: Full=26S proteasome regulatory subunit S5A homolog;
AltName: Full=Multiubiquitin chain-binding protein 1;
Short=AtMCB1;
Name=RPN10; Synonyms=MBP1, MCB1; OrderedLocusNames=At4g38630;
ORFNames=F20M13.190, T9A14.7;
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], AND FUNCTION.
STRAIN=cv. Columbia; TISSUE=Seedling;
PubMed=8570648; DOI=10.1073/pnas.93.2.856;
van Nocker S., Deveraux Q., Rechsteiner M., Vierstra R.D.;
"Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component
of the 26S proteasome.";
Proc. Natl. Acad. Sci. U.S.A. 93:856-860(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION.
PubMed=8530351; DOI=10.1074/jbc.270.50.29660;
Deveraux Q., van Nocker S., Mahaffey D., Vierstra R.D., Rechsteiner M.;
"Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26 S
protease subunit S5a.";
J. Biol. Chem. 270:29660-29663(1995).
[7]
SUBUNIT, AND FUNCTION.
PubMed=9741626; DOI=10.1016/s0092-8674(00)81603-7;
Glickman M.H., Rubin D.M., Coux O., Wefes I., Pfeifer G., Cjeka Z.,
Baumeister W., Fried V.A., Finley D.;
"A subcomplex of the proteasome regulatory particle required for ubiquitin-
conjugate degradation and related to the COP9-signalosome and eIF3.";
Cell 94:615-623(1998).
[8]
POLYUBIQUITIN BINDING, AND FUNCTION.
PubMed=9442033; DOI=10.1074/jbc.273.4.1970;
Fu H., Sadis S., Rubin D.M., Glickman M., van Nocker S., Finley D.,
Vierstra R.D.;
"Multiubiquitin chain binding and protein degradation are mediated by
distinct domains within the 26 S proteasome subunit Mcb1.";
J. Biol. Chem. 273:1970-1981(1998).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12671091; DOI=10.1105/tpc.009217;
Smalle J., Kurepa J., Yang P., Emborg T.J., Babiychuk E., Kushnir S.,
Vierstra R.D.;
"The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis
growth and development supports a substrate-specific function in abscisic
acid signaling.";
Plant Cell 15:965-980(2003).
[10]
TISSUE SPECIFICITY.
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).
[11]
INTERACTION WITH PI4KG4, AND PHOSPHORYLATION BY PI4KG4.
PubMed=17880284; DOI=10.1042/bj20070959;
Galvao R.M., Kota U., Soderblom E.J., Goshe M.B., Boss W.F.;
"Characterization of a new family of protein kinases from Arabidopsis
containing phosphoinositide 3/4-kinase and ubiquitin-like domains.";
Biochem. J. 409:117-127(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by mass
spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[13]
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).
[14]
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).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[16]
FUNCTION, INTERACTION WITH RAD23B; RAD23C; RAD23D AND DSK2A, AND DISRUPTION
PHENOTYPE.
PubMed=20059542; DOI=10.1111/j.1742-4658.2009.07531.x;
Fatimababy A.S., Lin Y.L., Usharani R., Radjacommare R., Wang H.T.,
Tsai H.L., Lee Y., Fu H.;
"Cross-species divergence of the major recognition pathways of
ubiquitylated substrates for ubiquitin/26S proteasome-mediated
proteolysis.";
FEBS J. 277:796-816(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
COMPLEX, AND SUBUNIT.
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).
[18]
INTERACTION WITH RAD23B, AND POLYUBIQUITIN BINDING.
PubMed=20086187; DOI=10.1105/tpc.109.072660;
Farmer L.M., Book A.J., Lee K.H., Lin Y.L., Fu H., Vierstra R.D.;
"The RAD23 family provides an essential connection between the 26S
proteasome and ubiquitylated proteins in Arabidopsis.";
Plant Cell 22:124-142(2010).
[19]
REVIEW.
PubMed=20399133; DOI=10.1016/j.tplants.2010.03.004;
Fu H., Lin Y.L., Fatimababy A.S.;
"Proteasomal recognition of ubiquitylated substrates.";
Trends Plant Sci. 15:375-386(2010).
[20]
FUNCTION, DISRUPTION PHENOTYPE, POLYUBIQUITIN BINDING, AND INTERACTION WITH
RAD23B; RAD23C; RAD23D AND DSK2B.
PubMed=21764993; DOI=10.1105/tpc.111.086702;
Lin Y.-L., Sung S.-C., Tsai H.-L., Yu T.-T., Radjacommare R., Usharani R.,
Fatimababy A.S., Lin H.-Y., Wang Y.-Y., Fu H.;
"The defective proteasome but not substrate recognition function is
responsible for the null phenotypes of the Arabidopsis proteasome subunit
RPN10.";
Plant Cell 23:2754-2773(2011).
[21]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22751321; DOI=10.4161/psb.20360;
Lin Y.L., Fu H.;
"In vivo relevance of substrate recognition function of major Arabidopsis
ubiquitin receptors.";
Plant Signal. Behav. 7:722-727(2012).
-!- FUNCTION: Plays a role in maintaining the structural integrity of the
19S regulatory particle (RP), subcomplex of the 26S proteasome. Plays a
major role in both the direct and indirect recognition of ubiquitinated
substrates of ubiquitin/26S proteasome-mediated proteolysis (UPP).
Binds and presumably selects ubiquitin-conjugates for destruction.
Prefers multiubiquitin chains rather than single ubiquitins, with a
binding affinity for 'Lys-48'-linked ubiquitin chains. Acts as a
potential docking subunit for both ubiquitin receptors RAD23s and
DSK2s. Plays a role in the growth and development via the proteasome-
dependent degradation of the ABA-signaling protein ABI5/DPBF1. Plays an
important role for balancing cell expansion with cell proliferation
rates during shoot development. {ECO:0000269|PubMed:12671091,
ECO:0000269|PubMed:17971041, ECO:0000269|PubMed:19321709,
ECO:0000269|PubMed:20059542, ECO:0000269|PubMed:21764993,
ECO:0000269|PubMed:22751321, ECO:0000269|PubMed:8530351,
ECO:0000269|PubMed:8570648, ECO:0000269|PubMed:9442033,
ECO:0000269|PubMed:9741626}.
-!- SUBUNIT: Component of the 19S regulatory particle (RP/PA700) base
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 PI4KG4. Interacts
with RAD23s and DSK2s via its UIM3 and UIM1 motif, respectively.
Interacts with 'Lys-48'-linked polyubiquitin chains via its UIM1 motif.
{ECO:0000269|PubMed:17880284, ECO:0000269|PubMed:20059542,
ECO:0000269|PubMed:20086187, ECO:0000269|PubMed:20516081,
ECO:0000269|PubMed:21764993, ECO:0000269|PubMed:9741626}.
-!- INTERACTION:
P55034; Q9SII8: DSK2B; NbExp=2; IntAct=EBI-2620423, EBI-4433040;
P55034; Q9SFT9: T1B9.26; NbExp=3; IntAct=EBI-2620423, EBI-4460083;
P55034; P0CG48: UBC; Xeno; NbExp=2; IntAct=EBI-2620423, EBI-3390054;
-!- TISSUE SPECIFICITY: Ubiquitous with highest expression in flowers.
{ECO:0000269|PubMed:14623884}.
-!- PTM: Phosphorylated by PI4KG4 in vitro. {ECO:0000269|PubMed:17880284}.
-!- DISRUPTION PHENOTYPE: Displays reduced seed germination, growth rate,
stamen number, genetic transmission through the male gamete, hormone-
induced cell division and increased oxidative stress tolerance. Is also
more sensitive to abscisic acid (ABA), salt, sucrose stress, heat shock
and DNA-damaging agents and shows a decreased sensitivity to cytokinin
and auxin. In flowers, epidermal cells in petals were larger than those
in the wild type. {ECO:0000269|PubMed:12671091,
ECO:0000269|PubMed:17971041, ECO:0000269|PubMed:19321709,
ECO:0000269|PubMed:20059542, ECO:0000269|PubMed:21764993,
ECO:0000269|PubMed:22751321}.
-!- SIMILARITY: Belongs to the proteasome subunit S5A family.
{ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; U33269; AAA85583.1; -; mRNA.
EMBL; AL035540; CAB37519.1; -; Genomic_DNA.
EMBL; AL035656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL161593; CAB80527.1; -; Genomic_DNA.
EMBL; CP002687; AEE86956.1; -; Genomic_DNA.
EMBL; AF360319; AAK26029.1; -; mRNA.
EMBL; AY113889; AAM44937.1; -; mRNA.
EMBL; AY088449; AAM65985.1; -; mRNA.
PIR; T05691; T05691.
RefSeq; NP_195575.1; NM_120024.3.
SMR; P55034; -.
BioGRID; 15299; 47.
IntAct; P55034; 11.
MINT; P55034; -.
STRING; 3702.AT4G38630.1; -.
iPTMnet; P55034; -.
PaxDb; P55034; -.
PRIDE; P55034; -.
ProteomicsDB; 224827; -.
EnsemblPlants; AT4G38630.1; AT4G38630.1; AT4G38630.
GeneID; 830019; -.
Gramene; AT4G38630.1; AT4G38630.1; AT4G38630.
KEGG; ath:AT4G38630; -.
Araport; AT4G38630; -.
TAIR; locus:2121269; AT4G38630.
eggNOG; KOG2884; Eukaryota.
HOGENOM; CLU_033293_0_0_1; -.
InParanoid; P55034; -.
OMA; PMEDENA; -.
OrthoDB; 1244685at2759; -.
PhylomeDB; P55034; -.
PRO; PR:P55034; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; P55034; baseline and differential.
Genevisible; P55034; AT.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; HDA:TAIR.
GO; GO:0000502; C:proteasome complex; IDA:TAIR.
GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
GO; GO:0001653; F:peptide receptor activity; IDA:TAIR.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
GO; GO:0048366; P:leaf development; IMP:TAIR.
GO; GO:0010150; P:leaf senescence; IMP:TAIR.
GO; GO:0009555; P:pollen 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:0010029; P:regulation of seed germination; IMP:TAIR.
GO; GO:0009737; P:response to abscisic acid; 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:0009651; P:response to salt stress; IMP:TAIR.
GO; GO:0009744; P:response to sucrose; IMP:TAIR.
GO; GO:0048767; P:root hair elongation; IMP:TAIR.
GO; GO:0048455; P:stamen formation; IMP:TAIR.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR003903; UIM_dom.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF02809; UIM; 2.
Pfam; PF13519; VWA_2; 1.
SMART; SM00726; UIM; 3.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
PROSITE; PS50330; UIM; 3.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
Phosphoprotein; Proteasome; Reference proteome; Repeat.
CHAIN 1..386
/note="26S proteasome non-ATPase regulatory subunit 4
homolog"
/id="PRO_0000173832"
DOMAIN 5..190
/note="VWFA"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
DOMAIN 221..240
/note="UIM 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
DOMAIN 282..301
/note="UIM 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
DOMAIN 305..324
/note="UIM 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
REGION 241..281
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 344..386
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 241..262
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 363..386
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 263
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18433157"
CONFLICT 253
/note="G -> C (in Ref. 5; AAM65985)"
/evidence="ECO:0000305"
CONFLICT 371
/note="T -> H (in Ref. 5; AAM65985)"
/evidence="ECO:0000305"
SEQUENCE 386 AA; 40757 MW; 2F5C89D9FACB4550 CRC64;
MVLEATMICI DNSEWMRNGD YSPSRLQAQT EAVNLLCGAK TQSNPENTVG ILTMAGKGVR
VLTTPTSDLG KILACMHGLD VGGEINLTAA IQIAQLALKH RQNKNQRQRI IVFAGSPIKY
EKKALEIVGK RLKKNSVSLD IVNFGEDDDE EKPQKLEALL TAVNNNDGSH IVHVPSGANA
LSDVLLSTPV FTGDEGASGY VSAAAAAAAA GGDFDFGVDP NIDPELALAL RVSMEEERAR
QEAAAKKAAD EAGQKDKDGD TASASQETVA RTTDKNAEPM DEDSALLDQA IAMSVGDVNM
SEAADEDQDL ALALQMSMSG EESSEATGAG NNLLGNQAFI SSVLSSLPGV DPNDPAVKEL
LASLPDESKR TEEEESSSKK GEDEKK


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EIAAB32846 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Homo sapiens,Human,Protein 55.11,PSMD2,TRAP2,Tumor
EIAAB32847 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Bos taurus,Bovine,PSMD2,TRAP2,Tumor necrosis facto
EIAAB32669 26S protease regulatory subunit 8,26S proteasome AAA-ATPase subunit RPT6,p45_SUG,Pig,Proteasome 26S subunit ATPase 5,Proteasome subunit p45,PSMC5,Sus scrofa,Tat-binding protein homolog 10,TBP10
EIAAB32850 26S proteasome non-ATPase regulatory subunit 3,26S proteasome regulatory subunit RPN3,26S proteasome regulatory subunit S3,Mouse,Mus musculus,P91a,Proteasome subunit p58,Psmd3,Transplantation antigen
EIAAB32789 26S proteasome non-ATPase regulatory subunit 11,26S proteasome regulatory subunit p44.5,26S proteasome regulatory subunit RPN6,26S proteasome regulatory subunit S9,Homo sapiens,Human,PSMD11
EIAAB32798 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Homo sapiens,Human,PSMD13
EIAAB32858 26S proteasome non-ATPase regulatory subunit 6,26S proteasome regulatory subunit RPN7,26S proteasome regulatory subunit S10,Breast cancer-associated protein SGA-113M,Homo sapiens,Human,KIAA0107,p42A,P
EIAAB32842 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,26S proteasome subunit p112,Homo sapiens,Human,PSMD1
EIAAB32809 26S proteasome non-ATPase regulatory subunit 14,26S proteasome regulatory subunit RPN11,26S proteasome-associated PAD1 homolog 1,Homo sapiens,Human,POH1,PSMD14
EIAAB32848 26S proteasome non-ATPase regulatory subunit 3,26S proteasome regulatory subunit RPN3,26S proteasome regulatory subunit S3,Homo sapiens,Human,Proteasome subunit p58,PSMD3
EIAAB32841 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,26S proteasome subunit p112,Psmd1,Rat,Rattus norvegicus
EIAAB32791 26S proteasome non-ATPase regulatory subunit 11,26S proteasome regulatory subunit p44.5,26S proteasome regulatory subunit RPN6,26S proteasome regulatory subunit S9,Mouse,Mus musculus,Psmd11
EIAAB32799 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Bos taurus,Bovine,PSMD13
EIAAB32796 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Psmd13,Rat,Rattus norvegicus
EIAAB32797 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Mouse,Mus musculus,Psmd13
EIAAB32807 26S proteasome non-ATPase regulatory subunit 7,26S proteasome regulatory subunit RPN8,26S proteasome regulatory subunit S12,Mouse,Mov34,Mov-34,Mov34 protein,Mus musculus,Proteasome subunit p40,Psmd7
18-003-42215 26S proteasome non-ATPase regulatory subunit 14 - 26S proteasome regulatory subunit rpn11; 26S proteasome-associated PAD1 homolog 1 Polyclonal 0.05 mg Aff Pur
18-003-42216 26S proteasome non-ATPase regulatory subunit 14 - 26S proteasome regulatory subunit rpn11; 26S proteasome-associated PAD1 homolog 1 Polyclonal 0.1 mg Protein A
EIAAB32844 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Mouse,Mus musculus,Psmd2
EIAAB32656 26S protease regulatory subunit 6A,26S proteasome AAA-ATPase subunit RPT5,Proteasome 26S subunit ATPase 3,Psmc3,Rat,Rattus norvegicus,Spermatogenic cell_sperm-associated Tat-binding protein homolog SA
Pathways :
WP2292: Chemokine signaling pathway
WP731: Sterol regulatory element binding protein related
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1691: Proteasome
WP158: Proteasome Degradation
WP1694: Pyrimidine metabolism
WP1626: Benzoate degradation via CoA ligation
WP1644: DNA replication
WP470: Proteasome Degradation
WP2272: Pathogenic Escherichia coli infection
WP1493: Carbon assimilation C4 pathway
WP1909: Signal regulatory protein (SIRP) family interactions
WP1566: Citrate cycle (TCA cycle)
WP1693: Purine metabolism
WP1614: 1- and 2-Methylnaphthalene degradation
WP1196: Proteasome Degradation
WP519: Proteasome Degradation
WP1655: Geraniol degradation
WP841: Proteasome Degradation
WP1711: Trinitrotoluene degradation
WP281: Proteasome Degradation
WP1079: Proteasome Degradation
WP1671: Methane metabolism
WP960: Proteasome Degradation

Related Genes :
[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)
[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)
[Psmd4 Mcb1] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Multiubiquitin chain-binding protein)
[RPN10 MCB1 SUN1 YHR200W] 26S proteasome regulatory subunit RPN10
[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)
[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)
[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)
[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)
[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)
[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)
[PSMD14 POH1] 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (26S proteasome-associated PAD1 homolog 1)
[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) (Thyroid hormone receptor-interacting protein 1) (TRIP1) (p45/SUG)
[Psmc5 Sug1] 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (p45/SUG) (mSUG1)
[PSMD3] 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3) (26S proteasome regulatory subunit S3) (Proteasome subunit p58)
[RPT5 YTA1 YOR117W O3258 YOR3258W] 26S proteasome regulatory subunit 6A (Tat-binding protein homolog 1) (TBP-1)
[RPT3 YNT1 YTA2 YDR394W D9509.14] 26S proteasome regulatory subunit 6B homolog (Protein YNT1) (Tat-binding homolog 2)
[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)
[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)
[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)
[PSMC4 MIP224 TBP7] 26S proteasome regulatory subunit 6B (26S proteasome AAA-ATPase subunit RPT3) (MB67-interacting protein) (MIP224) (Proteasome 26S subunit ATPase 4) (Tat-binding protein 7) (TBP-7)
[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)
[RPT2 YHS4 YTA5 YDL007W D2920] 26S proteasome regulatory subunit 4 homolog (Tat-binding homolog 5)
[RPT1 CIM5 YTA3 YKL145W] 26S proteasome regulatory subunit 7 homolog (Protein CIM5) (Tat-binding homolog 3)
[PSMC1] 26S proteasome regulatory subunit 4 (P26s4) (26S proteasome AAA-ATPase subunit RPT2) (Proteasome 26S subunit ATPase 1)
[RPT6 CIM3 CRL3 SUG1 TBPY TBY1 YGL048C] 26S proteasome regulatory subunit 8 homolog (Protein CIM3) (Protein SUG1) (Tat-binding protein TBY1)
[Psmc1] 26S proteasome regulatory subunit 4 (P26s4) (26S proteasome AAA-ATPase subunit RPT2) (Proteasome 26S subunit ATPase 1)
[PSMD11] 26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory subunit RPN6) (26S proteasome regulatory subunit S9) (26S proteasome regulatory subunit p44.5)

Bibliography :