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Protein

26S proteasome non-ATPase regulatory subunit 4 homolog

Gene

RPN10

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in maintaining the structural integrity of the 19S regulatory particule (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.10 Publications

GO - Molecular functioni

  • peptide receptor activity Source: TAIR
  • polyubiquitin binding Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: TAIR
  • leaf development Source: TAIR
  • leaf senescence Source: TAIR
  • pollen development Source: TAIR
  • post-embryonic root development Source: TAIR
  • proteasome assembly Source: TAIR
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: TAIR
  • protein catabolic process Source: TAIR
  • regulation of seed germination Source: TAIR
  • response to abscisic acid Source: TAIR
  • response to auxin Source: TAIR
  • response to cytokinin Source: TAIR
  • response to heat Source: TAIR
  • response to misfolded protein Source: TAIR
  • response to salt stress Source: TAIR
  • response to sucrose Source: TAIR
  • root hair elongation Source: TAIR
  • stamen formation Source: TAIR
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-ATH-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-ATH-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-ATH-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-ATH-5632684. Hedgehog 'on' state.
R-ATH-68949. Orc1 removal from chromatin.
R-ATH-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-ATH-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 4 homolog
Alternative name(s):
26S proteasome regulatory subunit RPN10
Short name:
AtRPN10
26S proteasome regulatory subunit S5A homolog
Multiubiquitin chain-binding protein 1
Short name:
AtMCB1
Gene namesi
Name:RPN10
Synonyms:MBP1, MCB1
Ordered Locus Names:At4g38630
ORF Names:F20M13.190, T9A14.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G38630.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • membrane Source: TAIR
  • nucleus Source: TAIR
  • proteasome complex Source: TAIR
  • proteasome regulatory particle, base subcomplex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Disruption phenotypei

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.6 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 38638626S proteasome non-ATPase regulatory subunit 4 homologPRO_0000173832Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei263 – 2631PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by PI4KG4 in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP55034.
PRIDEiP55034.

PTM databases

iPTMnetiP55034.

Expressioni

Tissue specificityi

Ubiquitous with highest expression in flowers.1 Publication

Gene expression databases

GenevisibleiP55034. AT.

Interactioni

Subunit structurei

Component of the 19S regulatory particule (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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DSK2BQ9SII82EBI-2620423,EBI-4433040
RAD23AQ84L323EBI-2620423,EBI-6394924
RAD23BP547273EBI-2620423,EBI-954531From a different organism.
UBCP0CG482EBI-2620423,EBI-3390054From a different organism.

GO - Molecular functioni

  • polyubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi15299. 11 interactions.
IntActiP55034. 9 interactions.
MINTiMINT-7308061.
STRINGi3702.AT4G38630.1.

Structurei

3D structure databases

ProteinModelPortaliP55034.
SMRiP55034. Positions 1-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 190186VWFAPROSITE-ProRule annotationAdd
BLAST
Domaini221 – 24020UIM 1PROSITE-ProRule annotationAdd
BLAST
Domaini282 – 30120UIM 2PROSITE-ProRule annotationAdd
BLAST
Domaini305 – 32420UIM 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the proteasome subunit S5A family.Curated
Contains 3 UIM (ubiquitin-interacting motif) domains.PROSITE-ProRule annotation
Contains 1 VWFA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2884. Eukaryota.
COG5148. LUCA.
HOGENOMiHOG000165630.
InParanoidiP55034.
KOiK03029.
OMAiATSPILM.
PhylomeDBiP55034.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR027040. Proteasome_su_Rpn10.
IPR003903. UIM_dom.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10223. PTHR10223. 1 hit.
PfamiPF02809. UIM. 2 hits.
PF13519. VWA_2. 1 hit.
[Graphical view]
SMARTiSM00726. UIM. 3 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
PROSITEiPS50330. UIM. 3 hits.
PS50234. VWFA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P55034-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLEATMICI DNSEWMRNGD YSPSRLQAQT EAVNLLCGAK TQSNPENTVG
60 70 80 90 100
ILTMAGKGVR VLTTPTSDLG KILACMHGLD VGGEINLTAA IQIAQLALKH
110 120 130 140 150
RQNKNQRQRI IVFAGSPIKY EKKALEIVGK RLKKNSVSLD IVNFGEDDDE
160 170 180 190 200
EKPQKLEALL TAVNNNDGSH IVHVPSGANA LSDVLLSTPV FTGDEGASGY
210 220 230 240 250
VSAAAAAAAA GGDFDFGVDP NIDPELALAL RVSMEEERAR QEAAAKKAAD
260 270 280 290 300
EAGQKDKDGD TASASQETVA RTTDKNAEPM DEDSALLDQA IAMSVGDVNM
310 320 330 340 350
SEAADEDQDL ALALQMSMSG EESSEATGAG NNLLGNQAFI SSVLSSLPGV
360 370 380
DPNDPAVKEL LASLPDESKR TEEEESSSKK GEDEKK
Length:386
Mass (Da):40,757
Last modified:October 1, 1996 - v1
Checksum:i2F5C89D9FACB4550
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531G → C in AAM65985 (Ref. 5) Curated
Sequence conflicti371 – 3711T → H in AAM65985 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33269 mRNA. Translation: AAA85583.1.
AL035540 Genomic DNA. Translation: CAB37519.1.
AL035656 Genomic DNA. No translation available.
AL161593 Genomic DNA. Translation: CAB80527.1.
CP002687 Genomic DNA. Translation: AEE86956.1.
AF360319 mRNA. Translation: AAK26029.1.
AY113889 mRNA. Translation: AAM44937.1.
AY088449 mRNA. Translation: AAM65985.1.
PIRiT05691.
RefSeqiNP_195575.1. NM_120024.2.
UniGeneiAt.1553.

Genome annotation databases

EnsemblPlantsiAT4G38630.1; AT4G38630.1; AT4G38630.
GeneIDi830019.
GrameneiAT4G38630.1; AT4G38630.1; AT4G38630.
KEGGiath:AT4G38630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33269 mRNA. Translation: AAA85583.1.
AL035540 Genomic DNA. Translation: CAB37519.1.
AL035656 Genomic DNA. No translation available.
AL161593 Genomic DNA. Translation: CAB80527.1.
CP002687 Genomic DNA. Translation: AEE86956.1.
AF360319 mRNA. Translation: AAK26029.1.
AY113889 mRNA. Translation: AAM44937.1.
AY088449 mRNA. Translation: AAM65985.1.
PIRiT05691.
RefSeqiNP_195575.1. NM_120024.2.
UniGeneiAt.1553.

3D structure databases

ProteinModelPortaliP55034.
SMRiP55034. Positions 1-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15299. 11 interactions.
IntActiP55034. 9 interactions.
MINTiMINT-7308061.
STRINGi3702.AT4G38630.1.

PTM databases

iPTMnetiP55034.

Proteomic databases

PaxDbiP55034.
PRIDEiP55034.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G38630.1; AT4G38630.1; AT4G38630.
GeneIDi830019.
GrameneiAT4G38630.1; AT4G38630.1; AT4G38630.
KEGGiath:AT4G38630.

Organism-specific databases

TAIRiAT4G38630.

Phylogenomic databases

eggNOGiKOG2884. Eukaryota.
COG5148. LUCA.
HOGENOMiHOG000165630.
InParanoidiP55034.
KOiK03029.
OMAiATSPILM.
PhylomeDBiP55034.

Enzyme and pathway databases

ReactomeiR-ATH-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-ATH-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-ATH-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-ATH-5632684. Hedgehog 'on' state.
R-ATH-68949. Orc1 removal from chromatin.
R-ATH-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-ATH-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiP55034.

Gene expression databases

GenevisibleiP55034. AT.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR027040. Proteasome_su_Rpn10.
IPR003903. UIM_dom.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10223. PTHR10223. 1 hit.
PfamiPF02809. UIM. 2 hits.
PF13519. VWA_2. 1 hit.
[Graphical view]
SMARTiSM00726. UIM. 3 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
PROSITEiPS50330. UIM. 3 hits.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome."
    van Nocker S., Deveraux Q., Rechsteiner M., Vierstra R.D.
    Proc. Natl. Acad. Sci. U.S.A. 93:856-860(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: cv. Columbia.
    Tissue: Seedling.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    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.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26 S protease subunit S5a."
    Deveraux Q., van Nocker S., Mahaffey D., Vierstra R.D., Rechsteiner M.
    J. Biol. Chem. 270:29660-29663(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3."
    Glickman M.H., Rubin D.M., Coux O., Wefes I., Pfeifer G., Cjeka Z., Baumeister W., Fried V.A., Finley D.
    Cell 94:615-623(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, FUNCTION.
  8. "Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1."
    Fu H., Sadis S., Rubin D.M., Glickman M., van Nocker S., Finley D., Vierstra R.D.
    J. Biol. Chem. 273:1970-1981(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYUBIQUITIN BINDING, FUNCTION.
  9. "The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis growth and development supports a substrate-specific function in abscisic acid signaling."
    Smalle J., Kurepa J., Yang P., Emborg T.J., Babiychuk E., Kushnir S., Vierstra R.D.
    Plant Cell 15:965-980(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms."
    Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.
    J. Biol. Chem. 279:6401-6413(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Characterization of a new family of protein kinases from Arabidopsis containing phosphoinositide 3/4-kinase and ubiquitin-like domains."
    Galvao R.M., Kota U., Soderblom E.J., Goshe M.B., Boss W.F.
    Biochem. J. 409:117-127(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PI4KG4, PHOSPHORYLATION BY PI4KG4.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Root.
  13. "26S proteasome regulatory particle mutants have increased oxidative stress tolerance."
    Kurepa J., Toh-E A., Smalle J.A.
    Plant J. 53:102-114(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  14. "Loss of 26S proteasome function leads to increased cell size and decreased cell number in Arabidopsis shoot organs."
    Kurepa J., Wang S., Li Y., Zaitlin D., Pierce A.J., Smalle J.A.
    Plant Physiol. 150:178-189(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  15. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis."
    Fatimababy A.S., Lin Y.L., Usharani R., Radjacommare R., Wang H.T., Tsai H.L., Lee Y., Fu H.
    FEBS J. 277:796-816(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAD23B; RAD23C; RAD23D AND DSK2A, DISRUPTION PHENOTYPE.
  17. "Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes."
    Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.
    J. Biol. Chem. 285:25554-25569(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME COMPLEX, SUBUNIT.
  18. "The RAD23 family provides an essential connection between the 26S proteasome and ubiquitylated proteins in Arabidopsis."
    Farmer L.M., Book A.J., Lee K.H., Lin Y.L., Fu H., Vierstra R.D.
    Plant Cell 22:124-142(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD23B, POLYUBIQUITIN BINDING.
  19. "Proteasomal recognition of ubiquitylated substrates."
    Fu H., Lin Y.L., Fatimababy A.S.
    Trends Plant Sci. 15:375-386(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  20. "The defective proteasome but not substrate recognition function is responsible for the null phenotypes of the Arabidopsis proteasome subunit RPN10."
    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.
    Plant Cell 23:2754-2773(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, POLYUBIQUITIN BINDING, INTERACTION WITH RAD23B; RAD23C; RAD23D AND DSK2B.
  21. "In vivo relevance of substrate recognition function of major Arabidopsis ubiquitin receptors."
    Lin Y.L., Fu H.
    Plant Signal. Behav. 7:722-727(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPSMD4_ARATH
AccessioniPrimary (citable) accession number: P55034
Secondary accession number(s): Q8L9G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.