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Q9XI05

- PSB3A_ARATH

UniProt

Q9XI05 - PSB3A_ARATH

Protein

Proteasome subunit beta type-3-A

Gene

PBC1

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 109 (01 Oct 2014)
      Sequence version 2 (09 Feb 2010)
      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. proteolysis involved in cellular protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciARA:AT1G21720-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-3-A (EC:3.4.25.1)
    Alternative name(s):
    20S proteasome beta subunit C-1
    Proteasome component T
    Gene namesi
    Name:PBC1
    Synonyms:PRCT
    Ordered Locus Names:At1g21720
    ORF Names:F8K7.15
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G21720.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: TAIR
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome complex Source: TAIR
    4. proteasome core complex Source: InterPro
    5. vacuolar membrane Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 204203Proteasome subunit beta type-3-APRO_0000148065Add
    BLAST

    Proteomic databases

    PaxDbiQ9XI05.
    PRIDEiQ9XI05.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9XI05.

    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

    BioGridi24015. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9XI05.
    SMRiQ9XI05. Positions 2-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000090523.
    InParanoidiQ9XI05.
    KOiK02735.
    OMAiMDLIGCP.
    PhylomeDBiQ9XI05.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9XI05-1) [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

    MSIFEYNGSA VVAMVGKNCF AIASDRRLGV QLQTIATDFQ RISKIHDRVF    50
    IGLSGLATDV QTLYQRLVFR HKLYQLREER DMKPETFASL VSAILYEKRF 100
    GPYLCQPVIA GLGDDDKPFI CTMDSIGAKE LAKDFVVSGT ASESLYGACE 150
    AMYKPDMEAE ELFETISQAL LSSVDRDCLS GWGGHVYIVT PTEIKERILK 200
    GRMD 204
    Length:204
    Mass (Da):22,798
    Last modified:February 9, 2010 - v2
    Checksum:iB52E22CDB3EDA467
    GO
    Isoform 2 (identifier: Q9XI05-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-2: S → Q

    Note: May be due to intron retention. No experimental confirmation available.

    Show »
    Length:204
    Mass (Da):22,839
    Checksum:iE1CD9513D8D2F3B9
    GO

    Sequence cautioni

    The sequence AAC32068.1 differs from that shown. Reason: Frameshift at position 41.
    The sequence CAA73616.1 differs from that shown. Reason: Frameshift at position 41.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81G → V in AAM62756. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 21S → Q in isoform 2. 1 PublicationVSP_016143

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13173 mRNA. Translation: CAA73616.1. Frameshift.
    AF043532 mRNA. Translation: AAC32068.1. Frameshift.
    AC007727 Genomic DNA. Translation: AAD41426.1.
    CP002684 Genomic DNA. Translation: AEE30146.1.
    AY065070 mRNA. Translation: AAL38246.1.
    AY114628 mRNA. Translation: AAM47947.1.
    AF344327 mRNA. Translation: AAK06878.1.
    AK226397 mRNA. Translation: BAE98543.1.
    AY085532 mRNA. Translation: AAM62756.1.
    PIRiF86350.
    RefSeqiNP_564149.1. NM_102021.2. [Q9XI05-1]
    UniGeneiAt.11467.

    Genome annotation databases

    EnsemblPlantsiAT1G21720.1; AT1G21720.1; AT1G21720. [Q9XI05-1]
    GeneIDi838776.
    KEGGiath:AT1G21720.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13173 mRNA. Translation: CAA73616.1 . Frameshift.
    AF043532 mRNA. Translation: AAC32068.1 . Frameshift.
    AC007727 Genomic DNA. Translation: AAD41426.1 .
    CP002684 Genomic DNA. Translation: AEE30146.1 .
    AY065070 mRNA. Translation: AAL38246.1 .
    AY114628 mRNA. Translation: AAM47947.1 .
    AF344327 mRNA. Translation: AAK06878.1 .
    AK226397 mRNA. Translation: BAE98543.1 .
    AY085532 mRNA. Translation: AAM62756.1 .
    PIRi F86350.
    RefSeqi NP_564149.1. NM_102021.2. [Q9XI05-1 ]
    UniGenei At.11467.

    3D structure databases

    ProteinModelPortali Q9XI05.
    SMRi Q9XI05. Positions 2-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 24015. 1 interaction.

    Proteomic databases

    PaxDbi Q9XI05.
    PRIDEi Q9XI05.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G21720.1 ; AT1G21720.1 ; AT1G21720 . [Q9XI05-1 ]
    GeneIDi 838776.
    KEGGi ath:AT1G21720.

    Organism-specific databases

    TAIRi AT1G21720.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000090523.
    InParanoidi Q9XI05.
    KOi K02735.
    OMAi MDLIGCP.
    PhylomeDBi Q9XI05.

    Enzyme and pathway databases

    BioCyci ARA:AT1G21720-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 Q9XI05.

    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. "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] (ISOFORM 1).
      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] (ISOFORM 1), GENE FAMILY, NOMENCLATURE.
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(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] (ISOFORMS 1 AND 2).
      Strain: cv. Columbia.
    6. "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] (ISOFORM 1).
      Strain: cv. Columbia.
    7. "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] (ISOFORM 1).
    8. "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.
    9. "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.
    10. "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, CLEAVAGE OF INITIATOR METHIONINE.

    Entry informationi

    Entry nameiPSB3A_ARATH
    AccessioniPrimary (citable) accession number: Q9XI05
    Secondary accession number(s): O23707
    , Q0WWF5, Q8LEA7, Q8VZC4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 109 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