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Q8LD27

- PSB6_ARATH

UniProt

Q8LD27 - PSB6_ARATH

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Protein

Proteasome subunit beta type-6

Gene

PBA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei13 – 131NucleophileBy similarity

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciARA:AT4G31300-MONOMER.
ARA:GQT-2435-MONOMER.
ARA:GQT-2436-MONOMER.
ReactomeiREACT_106068. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_107429. Orc1 removal from chromatin.
REACT_185297. Separation of Sister Chromatids.
REACT_187712. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_187719. ER-Phagosome pathway.
REACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_190947. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Protein family/group databases

MEROPSiT01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-6 (EC:3.4.25.1)
Alternative name(s):
20S proteasome beta subunit A-1
Proteasome component D
Proteasome subunit beta type-1
Gene namesi
Name:PBA1
Synonyms:PRCD
Ordered Locus Names:At4g31300
ORF Names:F8F16.120
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G31300.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
  3. proteasome core complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1212Removed in mature formPRO_0000042828Add
BLAST
Chaini13 – 233221Proteasome subunit beta type-6PRO_0000042829Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiQ8LD27.
PRIDEiQ8LD27.

Expressioni

Gene expression databases

ExpressionAtlasiQ8LD27. baseline and differential.
GenevestigatoriQ8LD27.

Interactioni

Subunit structurei

Component of the 20S core complex 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 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.3 Publications

Protein-protein interaction databases

BioGridi14543. 2 interactions.
IntActiQ8LD27. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8LD27.
SMRiQ8LD27. Positions 13-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091079.
InParanoidiQ8LD27.
KOiK02738.
PhylomeDBiQ8LD27.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q8LD27-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDLNLDAPHS MGTTIIGVTY NGGVVLGADS RTSTGMYVAN RASDKITQLT
60 70 80 90 100
DNVYVCRSGS AADSQVVSDY VRYFLHQHTI QHGQPATVKV SANLIRMLAY
110 120 130 140 150
NNKNMLQTGL IVGGWDKYEG GKIYGIPLGG TVVEQPFAIG GSGSSYLYGF
160 170 180 190 200
FDQAWKDNMT KEEAEQLVVK AVSLAIARDG ASGGVVRTVI INSEGVTRNF
210 220 230
YPGDKLQLWH EELEPQNSLL DILNAAGPEP MAM
Length:233
Mass (Da):25,151
Last modified:November 22, 2005 - v2
Checksum:iD9DBB0CBD42623AB
GO

Sequence cautioni

The sequence AAM64316.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731Y → H in AAM64316. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13694 mRNA. Translation: CAA74028.1.
AF043529 mRNA. Translation: AAC32065.1.
AL021633 Genomic DNA. Translation: CAA16533.1.
AL161578 Genomic DNA. Translation: CAB79848.1.
CP002687 Genomic DNA. Translation: AEE85887.1.
CP002687 Genomic DNA. Translation: AEE85889.1.
AY052354 mRNA. Translation: AAK96545.1.
AY058240 mRNA. Translation: AAL15414.1.
AY086241 mRNA. Translation: AAM64316.1. Different initiation.
PIRiT04497.
RefSeqiNP_001190879.1. NM_001203950.1. [Q8LD27-1]
NP_194858.1. NM_119279.4. [Q8LD27-1]
UniGeneiAt.24496.

Genome annotation databases

EnsemblPlantsiAT4G31300.1; AT4G31300.1; AT4G31300. [Q8LD27-1]
AT4G31300.3; AT4G31300.3; AT4G31300. [Q8LD27-1]
GeneIDi829257.
KEGGiath:AT4G31300.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13694 mRNA. Translation: CAA74028.1 .
AF043529 mRNA. Translation: AAC32065.1 .
AL021633 Genomic DNA. Translation: CAA16533.1 .
AL161578 Genomic DNA. Translation: CAB79848.1 .
CP002687 Genomic DNA. Translation: AEE85887.1 .
CP002687 Genomic DNA. Translation: AEE85889.1 .
AY052354 mRNA. Translation: AAK96545.1 .
AY058240 mRNA. Translation: AAL15414.1 .
AY086241 mRNA. Translation: AAM64316.1 . Different initiation.
PIRi T04497.
RefSeqi NP_001190879.1. NM_001203950.1. [Q8LD27-1 ]
NP_194858.1. NM_119279.4. [Q8LD27-1 ]
UniGenei At.24496.

3D structure databases

ProteinModelPortali Q8LD27.
SMRi Q8LD27. Positions 13-227.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 14543. 2 interactions.
IntActi Q8LD27. 2 interactions.

Protein family/group databases

MEROPSi T01.010.

Proteomic databases

PaxDbi Q8LD27.
PRIDEi Q8LD27.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G31300.1 ; AT4G31300.1 ; AT4G31300 . [Q8LD27-1 ]
AT4G31300.3 ; AT4G31300.3 ; AT4G31300 . [Q8LD27-1 ]
GeneIDi 829257.
KEGGi ath:AT4G31300.

Organism-specific databases

GeneFarmi 5118.
TAIRi AT4G31300.

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091079.
InParanoidi Q8LD27.
KOi K02738.
PhylomeDBi Q8LD27.

Enzyme and pathway databases

BioCyci ARA:AT4G31300-MONOMER.
ARA:GQT-2435-MONOMER.
ARA:GQT-2436-MONOMER.
Reactomei REACT_106068. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_107429. Orc1 removal from chromatin.
REACT_185297. Separation of Sister Chromatids.
REACT_187712. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_187719. ER-Phagosome pathway.
REACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_190947. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Miscellaneous databases

PROi Q8LD27.

Gene expression databases

ExpressionAtlasi Q8LD27. baseline and differential.
Genevestigatori Q8LD27.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The 20S proteasome gene family in Arabidopsis thaliana."
    Parmentier Y., Bouchez D., Fleck J., Genschik P.
    FEBS Lett. 416:281-285(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana."
    Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.
    Genetics 149:677-692(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  3. "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.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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.
  6. "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].
  7. "Structure and functional analyses of the 26S proteasome subunits from plants."
    Fu H., Girod P.-A., Doelling J.H., van Nocker S., Hochstrasser M., Finley D., Vierstra R.D.
    Mol. Biol. Rep. 26:137-146(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "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: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "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.

Entry informationi

Entry nameiPSB6_ARATH
AccessioniPrimary (citable) accession number: Q8LD27
Secondary accession number(s): O23716
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: October 29, 2014
This is version 94 of the entry and version 2 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. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3