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Q7DLS1

- PSB7B_ARATH

UniProt

Q7DLS1 - PSB7B_ARATH

Protein

Proteasome subunit beta type-7-B

Gene

PBB2

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 83 (01 Oct 2014)
      Sequence version 2 (22 Nov 2005)
      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 sitei38 – 381NucleophileBy 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:AT5G40580-MONOMER.
    ARA:GQT-2095-MONOMER.
    ARA:GQT-2725-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

    MEROPSiT01.011.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-7-B (EC:3.4.25.1)
    Alternative name(s):
    20S proteasome beta subunit B-2
    Proteasome component FC
    Proteasome subunit beta type-2
    Gene namesi
    Name:PBB2
    Synonyms:PRCFC
    Ordered Locus Names:At5g40580
    ORF Names:MNF13.10
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G40580.

    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 – 3737Removed in mature formPRO_0000042832Add
    BLAST
    Chaini38 – 274237Proteasome subunit beta type-7-BPRO_0000042833Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    PaxDbiQ7DLS1.
    PRIDEiQ7DLS1.

    Expressioni

    Gene expression databases

    GenevestigatoriQ7DLS1.

    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

    BioGridi19307. 2 interactions.
    IntActiQ7DLS1. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7DLS1.
    SMRiQ7DLS1. Positions 40-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000182856.
    InParanoidiQ7DLS1.
    KOiK02739.
    OMAiQIWCAGA.
    PhylomeDBiQ7DLS1.

    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: Q7DLS1-1) [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

    MSQSSVDIPP KGGFSFDLCK RNDMLTQKGL KAPSFLKTGT TIVGLIFKDG    50
    VILGADTRAT EGPIVADKNC EKIHYMAPNI YCCGAGTAAD TEAVTDMVSS 100
    QLRLHRYQTG RDSRVVTALT LLKKHLFSYQ GHVSAALVLG GVDITGPHLH 150
    TIYPHGSTDT LPFATMGSGS LAAMSVFEAK YKEGLTRDEG IKLVAEAICS 200
    GIFNDLGSGS NVDICVITKG HKEYLRNYME PNPRTYVSSK GYSFTKKTEV 250
    LLTKITPLLE RVEIVEVAGE AMEE 274
    Length:274
    Mass (Da):29,617
    Last modified:November 22, 2005 - v2
    Checksum:i4AD31807A97D4C51
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti173 – 1731A → V in AAM13010. (PubMed:14593172)Curated
    Sequence conflicti173 – 1731A → V in AAM47910. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043531 mRNA. Translation: AAC32067.1.
    AB009052 Genomic DNA. Translation: BAB08528.1.
    CP002688 Genomic DNA. Translation: AED94567.1.
    CP002688 Genomic DNA. Translation: AED94568.1.
    AY093011 mRNA. Translation: AAM13010.1.
    AY114591 mRNA. Translation: AAM47910.1.
    AY087750 mRNA. Translation: AAM65286.1.
    Y13177 mRNA. Translation: CAA73620.1.
    PIRiT51979.
    RefSeqiNP_198874.1. NM_123422.3. [Q7DLS1-1]
    NP_851108.1. NM_180777.2. [Q7DLS1-1]
    UniGeneiAt.47287.
    At.66685.

    Genome annotation databases

    EnsemblPlantsiAT5G40580.1; AT5G40580.1; AT5G40580. [Q7DLS1-1]
    AT5G40580.2; AT5G40580.2; AT5G40580. [Q7DLS1-1]
    GeneIDi834056.
    KEGGiath:AT5G40580.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043531 mRNA. Translation: AAC32067.1 .
    AB009052 Genomic DNA. Translation: BAB08528.1 .
    CP002688 Genomic DNA. Translation: AED94567.1 .
    CP002688 Genomic DNA. Translation: AED94568.1 .
    AY093011 mRNA. Translation: AAM13010.1 .
    AY114591 mRNA. Translation: AAM47910.1 .
    AY087750 mRNA. Translation: AAM65286.1 .
    Y13177 mRNA. Translation: CAA73620.1 .
    PIRi T51979.
    RefSeqi NP_198874.1. NM_123422.3. [Q7DLS1-1 ]
    NP_851108.1. NM_180777.2. [Q7DLS1-1 ]
    UniGenei At.47287.
    At.66685.

    3D structure databases

    ProteinModelPortali Q7DLS1.
    SMRi Q7DLS1. Positions 40-258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 19307. 2 interactions.
    IntActi Q7DLS1. 1 interaction.

    Protein family/group databases

    MEROPSi T01.011.

    Proteomic databases

    PaxDbi Q7DLS1.
    PRIDEi Q7DLS1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G40580.1 ; AT5G40580.1 ; AT5G40580 . [Q7DLS1-1 ]
    AT5G40580.2 ; AT5G40580.2 ; AT5G40580 . [Q7DLS1-1 ]
    GeneIDi 834056.
    KEGGi ath:AT5G40580.

    Organism-specific databases

    GeneFarmi 5120.
    TAIRi AT5G40580.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000182856.
    InParanoidi Q7DLS1.
    KOi K02739.
    OMAi QIWCAGA.
    PhylomeDBi Q7DLS1.

    Enzyme and pathway databases

    BioCyci ARA:AT5G40580-MONOMER.
    ARA:GQT-2095-MONOMER.
    ARA:GQT-2725-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 Q7DLS1.

    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. "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.
    2. "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
      Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
      DNA Res. 5:41-54(1998) [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. "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] OF 57-274.
      Strain: cv. Columbia.
    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. "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 nameiPSB7B_ARATH
    AccessioniPrimary (citable) accession number: Q7DLS1
    Secondary accession number(s): O23709, Q8LAK8, Q8RWL9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 83 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