Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8L4A7

- PSA2B_ARATH

UniProt

Q8L4A7 - PSA2B_ARATH

Protein

Proteasome subunit alpha type-2-B

Gene

PAB2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.PROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. defense response to bacterium Source: TAIR
    2. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciARA:AT1G79210-MONOMER.
    ARA:GQT-1829-MONOMER.
    ARA:GQT-1830-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 alpha type-2-B (EC:3.4.25.1)
    Alternative name(s):
    20S proteasome alpha subunit B-2
    Gene namesi
    Name:PAB2
    Ordered Locus Names:At1g79210
    ORF Names:YUP8H12R.19
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G79210.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: TAIR
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome complex Source: TAIR
    4. proteasome core complex, alpha-subunit complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 235235Proteasome subunit alpha type-2-BPRO_0000124086Add
    BLAST

    Proteomic databases

    PaxDbiQ8L4A7.
    PRIDEiQ8L4A7.

    Expressioni

    Gene expression databases

    GenevestigatoriQ8L4A7.

    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

    BioGridi29481. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8L4A7.
    SMRiQ8L4A7. Positions 6-232.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091085.
    InParanoidiQ8L4A7.
    KOiK02726.
    OMAiXGAYFAW.
    PhylomeDBiQ8L4A7.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view]
    SMARTiSM00948. Proteasome_A_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8L4A7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDSQYSFSL TTFSPSGKLV QIEHALTAVG SGQTSLGIKA SNGVVIATEK    50
    KLPSILVDEA SVQKIQHLTP NIGTVYSGMG PDFRVLVRKS RKQAEQYLRL 100
    YKEPIPVTQL VRETATVMQE FTQSGGVRPF GVSLLVAGYD DKGPQLYQVD 150
    PSGSYFSWKA SAMGKNVSNA KTFLEKRYTE DMELDDAIHT AILTLKEGFE 200
    GEISSKNIEI GKIGTDKVFR VLTPAEIDDY LAEVE 235
    Length:235
    Mass (Da):25,733
    Last modified:October 1, 2002 - v1
    Checksum:i9B2DA84B57FC8B95
    GO

    Sequence cautioni

    The sequence AAC17043.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC002986 Genomic DNA. Translation: AAC17043.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE36215.1.
    CP002684 Genomic DNA. Translation: AEE36216.1.
    CP002684 Genomic DNA. Translation: AEE36217.1.
    AY094433 mRNA. Translation: AAM19806.1.
    AY122893 mRNA. Translation: AAM67426.1.
    PIRiT01036.
    RefSeqiNP_001077845.1. NM_001084376.1.
    NP_001077846.1. NM_001084377.1.
    NP_178042.1. NM_106572.5.
    UniGeneiAt.10591.

    Genome annotation databases

    EnsemblPlantsiAT1G79210.1; AT1G79210.1; AT1G79210.
    AT1G79210.2; AT1G79210.2; AT1G79210.
    AT1G79210.3; AT1G79210.3; AT1G79210.
    GeneIDi844262.
    KEGGiath:AT1G79210.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC002986 Genomic DNA. Translation: AAC17043.1 . Sequence problems.
    CP002684 Genomic DNA. Translation: AEE36215.1 .
    CP002684 Genomic DNA. Translation: AEE36216.1 .
    CP002684 Genomic DNA. Translation: AEE36217.1 .
    AY094433 mRNA. Translation: AAM19806.1 .
    AY122893 mRNA. Translation: AAM67426.1 .
    PIRi T01036.
    RefSeqi NP_001077845.1. NM_001084376.1.
    NP_001077846.1. NM_001084377.1.
    NP_178042.1. NM_106572.5.
    UniGenei At.10591.

    3D structure databases

    ProteinModelPortali Q8L4A7.
    SMRi Q8L4A7. Positions 6-232.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 29481. 1 interaction.

    Proteomic databases

    PaxDbi Q8L4A7.
    PRIDEi Q8L4A7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G79210.1 ; AT1G79210.1 ; AT1G79210 .
    AT1G79210.2 ; AT1G79210.2 ; AT1G79210 .
    AT1G79210.3 ; AT1G79210.3 ; AT1G79210 .
    GeneIDi 844262.
    KEGGi ath:AT1G79210.

    Organism-specific databases

    TAIRi AT1G79210.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091085.
    InParanoidi Q8L4A7.
    KOi K02726.
    OMAi XGAYFAW.
    PhylomeDBi Q8L4A7.

    Enzyme and pathway databases

    BioCyci ARA:AT1G79210-MONOMER.
    ARA:GQT-1829-MONOMER.
    ARA:GQT-1830-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 Q8L4A7.

    Gene expression databases

    Genevestigatori Q8L4A7.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SMARTi SM00948. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    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. "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: GENE FAMILY, NOMENCLATURE.
    5. "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.
    6. "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.
    7. "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 nameiPSA2B_ARATH
    AccessioniPrimary (citable) accession number: Q8L4A7
    Secondary accession number(s): O64532
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 90 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