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Protein

Proteasome subunit beta type-2-B

Gene

PBD2

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.

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:GQT-552-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_240263. Ubiquitin-dependent degradation of Cyclin D1.
REACT_241531. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_244054. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_252436. CDK-mediated phosphorylation and removal of Cdc6.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-2-B (EC:3.4.25.1)
Alternative name(s):
20S proteasome beta subunit D-2
Proteasome component GA
Proteasome subunit beta type-4
Gene namesi
Name:PBD2
Synonyms:PRCGA
Ordered Locus Names:At4g14800
ORF Names:dl3440w, FCAALL.135
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G14800.

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
Chaini1 – 199199Proteasome subunit beta type-2-BPRO_0000148050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO24633.
PRIDEiO24633.

Expressioni

Tissue specificityi

Ubiquitous low levels, higher expression in siliques and flowers.1 Publication

Gene expression databases

ExpressionAtlasiO24633. baseline and differential.
GenevestigatoriO24633.

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

BioGridi12432. 1 interaction.
IntActiO24633. 1 interaction.
STRINGi3702.AT4G14800.1-P.

Structurei

3D structure databases

ProteinModelPortaliO24633.
SMRiO24633. Positions 1-186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000188743.
InParanoidiO24633.
KOiK02734.
PhylomeDBiO24633.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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: O24633-1) [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
MECVFGLVGN GFAIVAADTS AVHSILLHKN KEDKIMTLDS HKLVAASGEP
60 70 80 90 100
GDRVQFTEYV QKNVSLYQFR NGIPLSTAAA ANFTRGELAT ALRKNPYSVN
110 120 130 140 150
ILMAGYDKEA GASLYYIDYI ATLHKVDKGA FGYGSYFSLS TMDRHYRSDM
160 170 180 190
SVEEAIELVD KCILEIRSRL VIAPPNFVIK IVDKDGAREY GWRISTADA
Length:199
Mass (Da):21,984
Last modified:January 1, 1998 - v1
Checksum:i26C43A69FABC3D3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13175 mRNA. Translation: CAA73618.1.
AF043535 mRNA. Translation: AAC32071.1.
Z97337 Genomic DNA. Translation: CAB10259.1.
AL161540 Genomic DNA. Translation: CAB78522.1.
CP002687 Genomic DNA. Translation: AEE83500.1.
BT024588 mRNA. Translation: ABD42986.1.
AK227835 mRNA. Translation: BAE99813.1.
AY086350 mRNA. Translation: AAM64418.1.
PIRiA71411.
RefSeqiNP_193216.1. NM_117565.3. [O24633-1]
UniGeneiAt.395.

Genome annotation databases

EnsemblPlantsiAT4G14800.1; AT4G14800.1; AT4G14800. [O24633-1]
GeneIDi827135.
KEGGiath:AT4G14800.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13175 mRNA. Translation: CAA73618.1.
AF043535 mRNA. Translation: AAC32071.1.
Z97337 Genomic DNA. Translation: CAB10259.1.
AL161540 Genomic DNA. Translation: CAB78522.1.
CP002687 Genomic DNA. Translation: AEE83500.1.
BT024588 mRNA. Translation: ABD42986.1.
AK227835 mRNA. Translation: BAE99813.1.
AY086350 mRNA. Translation: AAM64418.1.
PIRiA71411.
RefSeqiNP_193216.1. NM_117565.3. [O24633-1]
UniGeneiAt.395.

3D structure databases

ProteinModelPortaliO24633.
SMRiO24633. Positions 1-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12432. 1 interaction.
IntActiO24633. 1 interaction.
STRINGi3702.AT4G14800.1-P.

Proteomic databases

PaxDbiO24633.
PRIDEiO24633.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G14800.1; AT4G14800.1; AT4G14800. [O24633-1]
GeneIDi827135.
KEGGiath:AT4G14800.

Organism-specific databases

TAIRiAT4G14800.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000188743.
InParanoidiO24633.
KOiK02734.
PhylomeDBiO24633.

Enzyme and pathway databases

BioCyciARA:GQT-552-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_240263. Ubiquitin-dependent degradation of Cyclin D1.
REACT_241531. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_244054. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_252436. CDK-mediated phosphorylation and removal of Cdc6.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Gene expression databases

ExpressionAtlasiO24633. baseline and differential.
GenevestigatoriO24633.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
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(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], TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  3. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
    , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. "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.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Arabidopsis ORF clones."
    Shinn P., Chen H., Kim C.J., Ecker J.R.
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  8. "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].
  9. "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.
  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: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "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, ACETYLATION AT MET-1.

Entry informationi

Entry nameiPSB2B_ARATH
AccessioniPrimary (citable) accession number: O24633
Secondary accession number(s): Q2HIJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 119 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. 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.