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P42742

- PSB1_ARATH

UniProt

P42742 - PSB1_ARATH

Protein

Proteasome subunit beta type-1

Gene

PBF1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (08 Dec 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.

    GO - Molecular functioni

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

    GO - Biological processi

    1. defense response to fungus, incompatible interaction Source: TAIR
    2. proteolysis involved in cellular protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciARA:AT3G60820-MONOMER.
    ARA:GQT-2159-MONOMER.
    ARA:GQT-2160-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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-1 (EC:3.4.25.1)
    Alternative name(s):
    20S proteasome beta subunit F-1
    Proteasome component 5
    Proteasome subunit beta type-6
    TAS-F22/FAFP98
    TAS-G39.20
    Gene namesi
    Name:PBF1
    Synonyms:PRC5
    Ordered Locus Names:At3g60820
    ORF Names:T4C21_230
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G60820.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

    GO - Cellular componenti

    1. apoplast Source: TAIR
    2. chloroplast Source: TAIR
    3. cytosol Source: TAIR
    4. nucleus Source: UniProtKB-SubCell
    5. plasma membrane Source: TAIR
    6. proteasome complex Source: TAIR
    7. proteasome core complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 223223Proteasome subunit beta type-1PRO_0000148038Add
    BLAST

    Proteomic databases

    PaxDbiP42742.
    PRIDEiP42742.

    Expressioni

    Tissue specificityi

    Present in all tissues examined. Slightly lower levels in roots.1 Publication

    Developmental stagei

    Expressed at maximal levels after first day of cell growth.

    Inductioni

    During cell proliferation.1 Publication

    Gene expression databases

    ArrayExpressiP42742.
    GenevestigatoriP42742.

    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

    BioGridi10567. 8 interactions.
    IntActiP42742. 8 interactions.
    MINTiMINT-8065646.

    Structurei

    3D structure databases

    ProteinModelPortaliP42742.
    SMRiP42742. Positions 8-223.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091081.
    InParanoidiP42742.
    KOiK02732.
    PhylomeDBiP42742.

    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. Align

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

    Isoform 1 (identifier: P42742-1) [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.

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    MTKQHANWSP YDNNGGTCVA IAGSDYCVIA ADTRMSTGYS ILSRDYSKIH    50
    KLADRAVLSS SGFQADVKAL QKVLKSRHLI YQHQHNKQMS CPAMAQLLSN 100
    TLYFKRFFPY YAFNVLGGLD EEGKGCVFTY DAVGSYERVG YGAQGSGSTL 150
    IMPFLDNQLK SPSPLLLPKQ DSNTPLSEAE AVDLVKTVFA SATERDIYTG 200
    DKLEIMILKA DGIKTELMDL RKD 223
    Length:223
    Mass (Da):24,644
    Last modified:December 8, 2000 - v2
    Checksum:iE8050079F353D4C0
    GO

    Sequence cautioni

    The sequence CAA47753.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67338 mRNA. Translation: CAA47753.1. Different initiation.
    X79806 mRNA. Translation: CAA56201.1.
    AF043537 mRNA. Translation: AAC32073.1.
    AL162295 Genomic DNA. Translation: CAB82686.1.
    CP002686 Genomic DNA. Translation: AEE80112.1.
    CP002686 Genomic DNA. Translation: AEE80114.1.
    AY062790 mRNA. Translation: AAL32868.1.
    AY081571 mRNA. Translation: AAM10133.1.
    AY086619 mRNA. Translation: AAM63678.1.
    AK220787 mRNA. Translation: BAD94023.1.
    Z26405 mRNA. Translation: CAA81240.1.
    PIRiT47893.
    RefSeqiNP_001190146.1. NM_001203217.1. [P42742-1]
    NP_191641.1. NM_115946.3. [P42742-1]
    UniGeneiAt.20500.
    At.48789.

    Genome annotation databases

    EnsemblPlantsiAT3G60820.1; AT3G60820.1; AT3G60820. [P42742-1]
    AT3G60820.3; AT3G60820.3; AT3G60820. [P42742-1]
    GeneIDi825253.
    KEGGiath:AT3G60820.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67338 mRNA. Translation: CAA47753.1 . Different initiation.
    X79806 mRNA. Translation: CAA56201.1 .
    AF043537 mRNA. Translation: AAC32073.1 .
    AL162295 Genomic DNA. Translation: CAB82686.1 .
    CP002686 Genomic DNA. Translation: AEE80112.1 .
    CP002686 Genomic DNA. Translation: AEE80114.1 .
    AY062790 mRNA. Translation: AAL32868.1 .
    AY081571 mRNA. Translation: AAM10133.1 .
    AY086619 mRNA. Translation: AAM63678.1 .
    AK220787 mRNA. Translation: BAD94023.1 .
    Z26405 mRNA. Translation: CAA81240.1 .
    PIRi T47893.
    RefSeqi NP_001190146.1. NM_001203217.1. [P42742-1 ]
    NP_191641.1. NM_115946.3. [P42742-1 ]
    UniGenei At.20500.
    At.48789.

    3D structure databases

    ProteinModelPortali P42742.
    SMRi P42742. Positions 8-223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 10567. 8 interactions.
    IntActi P42742. 8 interactions.
    MINTi MINT-8065646.

    Proteomic databases

    PaxDbi P42742.
    PRIDEi P42742.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G60820.1 ; AT3G60820.1 ; AT3G60820 . [P42742-1 ]
    AT3G60820.3 ; AT3G60820.3 ; AT3G60820 . [P42742-1 ]
    GeneIDi 825253.
    KEGGi ath:AT3G60820.

    Organism-specific databases

    TAIRi AT3G60820.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091081.
    InParanoidi P42742.
    KOi K02732.
    PhylomeDBi P42742.

    Enzyme and pathway databases

    BioCyci ARA:AT3G60820-MONOMER.
    ARA:GQT-2159-MONOMER.
    ARA:GQT-2160-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 P42742.

    Gene expression databases

    ArrayExpressi P42742.
    Genevestigatori P42742.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    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 characterization of a beta-type proteasome subunit from Arabidopsis thaliana co-expressed at a high level with an alpha-type proteasome subunit early in the cell cycle."
      Genschik P., Jamet E., Phillips G., Parmentier Y., Gigot C., Fleck J.
      Plant J. 6:537-546(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
      Strain: cv. Columbia.
      Tissue: Leaf.
    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 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [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. "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 (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 168-223.
      Strain: cv. Columbia.
    8. "The Arabidopsis thaliana transcribed genome: the GDR cDNA program."
      Philipps G., Gigot C.
      Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 188-223.
    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.

    Entry informationi

    Entry nameiPSB1_ARATH
    AccessioniPrimary (citable) accession number: P42742
    Secondary accession number(s): P42741
    , Q570C3, Q6LAD2, Q9SBI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: December 8, 2000
    Last modified: October 1, 2014
    This is version 121 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