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Q7DLR9

- PSB4_ARATH

UniProt

Q7DLR9 - PSB4_ARATH

Protein

Proteasome subunit beta type-4

Gene

PBG1

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 81 (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 sitei24 – 241NucleophileBy 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
    2. response to cadmium ion Source: TAIR
    3. response to salt stress Source: TAIR

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciARA:AT1G56450-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

    MEROPSiT01.987.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-4 (EC:3.4.25.1)
    Alternative name(s):
    20S proteasome beta subunit G-1
    Proteasome component H
    Proteasome subunit beta type-7
    Gene namesi
    Name:PBG1
    Synonyms:PRCH
    Ordered Locus Names:At1g56450
    ORF Names:F13N6.3
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G56450.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 2323By similarityPRO_0000042824Add
    BLAST
    Chaini24 – 246223Proteasome subunit beta type-4PRO_0000042825Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    PaxDbiQ7DLR9.
    PRIDEiQ7DLR9.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    GenevestigatoriQ7DLR9.

    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

    BioGridi27323. 1 interaction.
    IntActiQ7DLR9. 1 interaction.
    STRINGi3702.AT1G56450.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7DLR9.
    SMRiQ7DLR9. Positions 24-233.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000181719.
    InParanoidiQ7DLR9.
    KOiK02736.
    OMAiRIMRVND.
    PhylomeDBiQ7DLR9.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR016295. Proteasome_endopept_cplx_B.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
    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.

    Q7DLR9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTFSVPIDN GDSMKIAEEE SQRTLYPYVT GTSIVAIKYK DGVLMASDMG    50
    GSYGSTLRYK NIERVKAIGK HSLLGASGEI SDFQEILRYL DELTLNDNMW 100
    DDGNSLGPKE IHNYLTRVMY NRRNKFNPLW NTLVLGGVKN GKSYLGMVSM 150
    IGVSFEDDHV ATGFGNHLAR PILRDEWHAD LSFEDGVKLL EKCMRVLLYR 200
    DRSAINKLQI AKITEEGVTV SQPYSLKTYW EFSSFHNPTA GAAGSW 246
    Length:246
    Mass (Da):27,651
    Last modified:November 22, 2005 - v2
    Checksum:i295B7CB39C6C66D6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341I → V in AAC32074. (PubMed:9611183)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043538 mRNA. Translation: AAC32074.1.
    AC058785 Genomic DNA. Translation: AAG51500.1.
    CP002684 Genomic DNA. Translation: AEE33397.1.
    AF378880 mRNA. Translation: AAK55683.1.
    AY045596 mRNA. Translation: AAK73954.1.
    AY052739 mRNA. Translation: AAK96453.1.
    AK221762 mRNA. Translation: BAD93840.1.
    Y13696 mRNA. Translation: CAA74030.1.
    PIRiD96606.
    T51986.
    RefSeqiNP_176040.1. NM_104523.3.
    UniGeneiAt.399.

    Genome annotation databases

    EnsemblPlantsiAT1G56450.1; AT1G56450.1; AT1G56450.
    GeneIDi842098.
    KEGGiath:AT1G56450.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043538 mRNA. Translation: AAC32074.1 .
    AC058785 Genomic DNA. Translation: AAG51500.1 .
    CP002684 Genomic DNA. Translation: AEE33397.1 .
    AF378880 mRNA. Translation: AAK55683.1 .
    AY045596 mRNA. Translation: AAK73954.1 .
    AY052739 mRNA. Translation: AAK96453.1 .
    AK221762 mRNA. Translation: BAD93840.1 .
    Y13696 mRNA. Translation: CAA74030.1 .
    PIRi D96606.
    T51986.
    RefSeqi NP_176040.1. NM_104523.3.
    UniGenei At.399.

    3D structure databases

    ProteinModelPortali Q7DLR9.
    SMRi Q7DLR9. Positions 24-233.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 27323. 1 interaction.
    IntActi Q7DLR9. 1 interaction.
    STRINGi 3702.AT1G56450.1-P.

    Protein family/group databases

    MEROPSi T01.987.

    Proteomic databases

    PaxDbi Q7DLR9.
    PRIDEi Q7DLR9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G56450.1 ; AT1G56450.1 ; AT1G56450 .
    GeneIDi 842098.
    KEGGi ath:AT1G56450.

    Organism-specific databases

    GeneFarmi 5117.
    TAIRi AT1G56450.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000181719.
    InParanoidi Q7DLR9.
    KOi K02736.
    OMAi RIMRVND.
    PhylomeDBi Q7DLR9.

    Enzyme and pathway databases

    BioCyci ARA:AT1G56450-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 Q7DLR9.

    Gene expression databases

    Genevestigatori Q7DLR9.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR016295. Proteasome_endopept_cplx_B.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001213. Psome_endopept_beta. 1 hit.
    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], TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
      Strain: cv. Columbia.
    2. "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.
    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. "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].
      Strain: cv. Columbia.
    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 126-246.
      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. "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.
    9. "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 nameiPSB4_ARATH
    AccessioniPrimary (citable) accession number: Q7DLR9
    Secondary accession number(s): O23718, Q9C7X3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 81 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