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Protein

Proteasome subunit beta type-6

Gene

PBA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: 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_275043. Orc1 removal from chromatin.
REACT_283762. Hedgehog 'on' state.
REACT_295391. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_301780. APC/C:Cdc20 mediated degradation of Securin.
REACT_302317. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_305944. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_309046. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_318090. Separation of Sister Chromatids.
REACT_319658. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_327677. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_336812. ER-Phagosome pathway.
REACT_340730. Autodegradation of the E3 ubiquitin ligase COP1.

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 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G31300.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  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 13-206.
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. AlignAdd to basket

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 21, 2005 - v2
Checksum:iD9DBB0CBD42623AB
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731Y → H in AAM64316 (Ref. 6) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ8LD27.
SMRiQ8LD27. Positions 13-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14543. 2 interactions.
IntActiQ8LD27. 2 interactions.

Protein family/group databases

MEROPSiT01.010.

Proteomic databases

PaxDbiQ8LD27.
PRIDEiQ8LD27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GeneFarmi5118.
TAIRiAT4G31300.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091079.
InParanoidiQ8LD27.
KOiK02738.
PhylomeDBiQ8LD27.

Enzyme and pathway databases

BioCyciARA:AT4G31300-MONOMER.
ARA:GQT-2435-MONOMER.
ARA:GQT-2436-MONOMER.
ReactomeiREACT_275043. Orc1 removal from chromatin.
REACT_283762. Hedgehog 'on' state.
REACT_295391. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_301780. APC/C:Cdc20 mediated degradation of Securin.
REACT_302317. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_305944. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_309046. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_318090. Separation of Sister Chromatids.
REACT_319658. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_327677. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_336812. ER-Phagosome pathway.
REACT_340730. Autodegradation of the E3 ubiquitin ligase COP1.

Miscellaneous databases

PROiQ8LD27.

Gene expression databases

ExpressionAtlasiQ8LD27. baseline and differential.
GenevestigatoriQ8LD27.

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]
ProtoNetiSearch...

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(1996) [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(1997) [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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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(2002) [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 (FEB-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(1998) [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(2003) [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(2009) [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 21, 2005
Last sequence update: November 21, 2005
Last modified: March 31, 2015
This is version 98 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

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 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.