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Q3T0Y5

- PSA2_BOVIN

UniProt

Q3T0Y5 - PSA2_BOVIN

Protein

Proteasome subunit alpha type-2

Gene

PSMA2

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation By similarity.By similarity

    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. response to virus Source: Ensembl
    2. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    ReactomeiREACT_203965. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_205339. APC/C:Cdc20 mediated degradation of Securin.
    REACT_205897. Activation of NF-kappaB in B cells.
    REACT_206368. CDT1 association with the CDC6:ORC:origin complex.
    REACT_207857. Asymmetric localization of PCP proteins.
    REACT_208116. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_208851. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_208889. degradation of AXIN.
    REACT_211738. ER-Phagosome pathway.
    REACT_212887. Separation of Sister Chromatids.
    REACT_213030. Orc1 removal from chromatin.
    REACT_215163. degradation of DVL.
    REACT_217860. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_218058. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_222557. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_222622. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_223494. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_224434. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_225648. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_226120. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.

    Protein family/group databases

    MEROPSiT01.972.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-2 (EC:3.4.25.1)
    Gene namesi
    Name:PSMA2
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 4

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. CytoplasmP-body By similarity
    Note: Colocalizes with TRIM5 in the cytoplasmic bodies.By similarity

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: UniProtKB
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome core complex Source: UniProtKB
    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
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 234233Proteasome subunit alpha type-2PRO_0000239865Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei70 – 701N6-acetyllysineBy similarity
    Modified residuei76 – 761PhosphotyrosineBy similarity
    Modified residuei171 – 1711N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues; which may be important for nuclear import.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ3T0Y5.
    PRIDEiQ3T0Y5.

    Interactioni

    Subunit structurei

    The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. 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.

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000001309.

    Structurei

    Secondary structure

    1
    234
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 103
    Helixi20 – 3011
    Beta strandi35 – 395
    Beta strandi44 – 496
    Beta strandi55 – 573
    Beta strandi64 – 7815
    Helixi80 – 10122
    Helixi107 – 12014
    Turni121 – 1233
    Beta strandi131 – 1399
    Beta strandi141 – 1499
    Beta strandi155 – 16410
    Helixi167 – 17711
    Helixi184 – 19613
    Beta strandi205 – 21410
    Beta strandi217 – 2204
    Helixi223 – 2308

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IRUX-ray2.75B/P2-234[»]
    ProteinModelPortaliQ3T0Y5.
    SMRiQ3T0Y5. Positions 2-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ3T0Y5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074870.
    HOGENOMiHOG000091085.
    HOVERGENiHBG003005.
    InParanoidiQ3T0Y5.
    KOiK02726.
    OMAiWKATALG.
    OrthoDBiEOG71VSTG.
    TreeFamiTF106207.

    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.

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

    Q3T0Y5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK    50
    KQKSILYDER SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV 100
    YQEPIPTAQL VQRVASVMQE YTQSGGVRPF GVSLLICGWN EGRPYLFQSD 150
    PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE DLELEDAIHT AILTLKESFE 200
    GQMTEDNIEV GICNEAGFRR LTPTEVKDYL AAIA 234
    Length:234
    Mass (Da):25,899
    Last modified:January 23, 2007 - v3
    Checksum:i63CB56A233583836
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102206 mRNA. Translation: AAI02207.1.
    RefSeqiNP_001029834.1. NM_001034662.2.
    UniGeneiBt.49020.

    Genome annotation databases

    EnsembliENSBTAT00000001309; ENSBTAP00000001309; ENSBTAG00000000990.
    GeneIDi539141.
    KEGGibta:539141.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102206 mRNA. Translation: AAI02207.1 .
    RefSeqi NP_001029834.1. NM_001034662.2.
    UniGenei Bt.49020.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IRU X-ray 2.75 B/P 2-234 [» ]
    ProteinModelPortali Q3T0Y5.
    SMRi Q3T0Y5. Positions 2-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000001309.

    Protein family/group databases

    MEROPSi T01.972.

    Proteomic databases

    PaxDbi Q3T0Y5.
    PRIDEi Q3T0Y5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000001309 ; ENSBTAP00000001309 ; ENSBTAG00000000990 .
    GeneIDi 539141.
    KEGGi bta:539141.

    Organism-specific databases

    CTDi 5683.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074870.
    HOGENOMi HOG000091085.
    HOVERGENi HBG003005.
    InParanoidi Q3T0Y5.
    KOi K02726.
    OMAi WKATALG.
    OrthoDBi EOG71VSTG.
    TreeFami TF106207.

    Enzyme and pathway databases

    Reactomei REACT_203965. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_205339. APC/C:Cdc20 mediated degradation of Securin.
    REACT_205897. Activation of NF-kappaB in B cells.
    REACT_206368. CDT1 association with the CDC6:ORC:origin complex.
    REACT_207857. Asymmetric localization of PCP proteins.
    REACT_208116. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_208851. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_208889. degradation of AXIN.
    REACT_211738. ER-Phagosome pathway.
    REACT_212887. Separation of Sister Chromatids.
    REACT_213030. Orc1 removal from chromatin.
    REACT_215163. degradation of DVL.
    REACT_217860. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_218058. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_222557. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_222622. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_223494. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_224434. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_225648. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_226120. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.

    Miscellaneous databases

    EvolutionaryTracei Q3T0Y5.
    NextBioi 20877807.

    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. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Ileum.
    2. "The structure of the mammalian 20S proteasome at 2.75 A resolution."
      Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., Tsukihara T.
      Structure 10:609-618(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.

    Entry informationi

    Entry nameiPSA2_BOVIN
    AccessioniPrimary (citable) accession number: Q3T0Y5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 79 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3