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Q9LIP2

- PSB5B_ARATH

UniProt

Q9LIP2 - PSB5B_ARATH

Protein

Proteasome subunit beta type-5-B

Gene

PBE2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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 sitei58 – 581NucleophileBy 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

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciARA:AT3G26340-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.A10.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-5-B (EC:3.4.25.1)
    Alternative name(s):
    20S proteasome beta subunit E-2
    Proteasome epsilon-2 chain
    Gene namesi
    Name:PBE2
    Ordered Locus Names:At3g26340
    ORF Names:F20C19.6
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G26340.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome complex Source: TAIR
    4. proteasome core complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 5757Removed in mature formBy similarityPRO_0000042826Add
    BLAST
    Chaini58 – 273216Proteasome subunit beta type-5-BPRO_0000042827Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    PaxDbiQ9LIP2.
    PRIDEiQ9LIP2.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9LIP2.

    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.2 Publications

    Protein-protein interaction databases

    BioGridi7569. 3 interactions.
    IntActiQ9LIP2. 2 interactions.
    STRINGi3702.AT3G26340.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LIP2.
    SMRiQ9LIP2. Positions 58-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091082.
    InParanoidiQ9LIP2.
    KOiK02737.
    OMAiTMCAGVT.
    PhylomeDBiQ9LIP2.

    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.

    Q9LIP2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLDTSGLET TMPVIGFGSN SEMLDGFSSA PSFDLPRTTD FDGFQKKAVE    50
    MVKPAKGTTT LAFIFKEGVM VAADSRASMG GYISSQSVKK IIEINPYMLG 100
    TMAGGAADCQ FWHRNLGIKC RLHELANKRR ISVSGASKLL ANMLYSYRGM 150
    GLSVGTMIAG WDETGPGLYY VDNEGGRLKG DRFSVGSGSP YAYGVLDSGY 200
    KFDMSVEEAS ELARRSIYHA TFRDGASGGV ASVYHVGPQG WTKLSGDDVG 250
    ELHYHYYPVA PITAEHVMEE AAE 273
    Length:273
    Mass (Da):29,485
    Last modified:October 1, 2000 - v1
    Checksum:iFAE197B491BDE6A7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP001298 Genomic DNA. Translation: BAB02194.1.
    CP002686 Genomic DNA. Translation: AEE77147.1.
    AY125569 mRNA. Translation: AAM78079.1.
    AF439846 mRNA. Translation: AAL27514.1.
    AY085678 mRNA. Translation: AAM62897.1.
    RefSeqiNP_189265.1. NM_113541.3.
    UniGeneiAt.6729.

    Genome annotation databases

    EnsemblPlantsiAT3G26340.1; AT3G26340.1; AT3G26340.
    GeneIDi822238.
    KEGGiath:AT3G26340.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP001298 Genomic DNA. Translation: BAB02194.1 .
    CP002686 Genomic DNA. Translation: AEE77147.1 .
    AY125569 mRNA. Translation: AAM78079.1 .
    AF439846 mRNA. Translation: AAL27514.1 .
    AY085678 mRNA. Translation: AAM62897.1 .
    RefSeqi NP_189265.1. NM_113541.3.
    UniGenei At.6729.

    3D structure databases

    ProteinModelPortali Q9LIP2.
    SMRi Q9LIP2. Positions 58-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 7569. 3 interactions.
    IntActi Q9LIP2. 2 interactions.
    STRINGi 3702.AT3G26340.1-P.

    Protein family/group databases

    MEROPSi T01.A10.

    Proteomic databases

    PaxDbi Q9LIP2.
    PRIDEi Q9LIP2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G26340.1 ; AT3G26340.1 ; AT3G26340 .
    GeneIDi 822238.
    KEGGi ath:AT3G26340.

    Organism-specific databases

    TAIRi AT3G26340.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091082.
    InParanoidi Q9LIP2.
    KOi K02737.
    OMAi TMCAGVT.
    PhylomeDBi Q9LIP2.

    Enzyme and pathway databases

    BioCyci ARA:AT3G26340-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.

    Gene expression databases

    Genevestigatori Q9LIP2.

    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

    1. "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
      Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
      DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "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.
    4. "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].
    5. "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.
    6. "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 nameiPSB5B_ARATH
    AccessioniPrimary (citable) accession number: Q9LIP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 96 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