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Q5E987

- PSA5_BOVIN

UniProt

Q5E987 - PSA5_BOVIN

Protein

Proteasome subunit alpha type-5

Gene

PSMA5

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (15 Mar 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 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. 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

    MEROPSiT01.975.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-5 (EC:3.4.25.1)
    Gene namesi
    Name:PSMA5
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 3

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    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
    Chaini1 – 241241Proteasome subunit alpha type-5PRO_0000274033Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei16 – 161PhosphoserineBy similarity
    Modified residuei55 – 551PhosphothreonineBy similarity
    Modified residuei56 – 561PhosphoserineBy similarity
    Glycosylationi198 – 1981O-linked (GlcNAc)By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ5E987.
    PRIDEiQ5E987.

    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. PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly.

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000027507.

    Structurei

    Secondary structure

    1
    241
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 3110
    Beta strandi37 – 426
    Beta strandi45 – 517
    Beta strandi66 – 716
    Beta strandi74 – 807
    Helixi82 – 10322
    Helixi109 – 1179
    Turni118 – 1214
    Beta strandi133 – 1353
    Beta strandi139 – 1479
    Beta strandi150 – 1567
    Beta strandi162 – 17110
    Helixi174 – 18411
    Helixi191 – 20515
    Beta strandi214 – 2207
    Beta strandi222 – 2243
    Helixi231 – 2388

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IRUX-ray2.75E/S1-241[»]
    ProteinModelPortaliQ5E987.
    SMRiQ5E987. Positions 9-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5E987.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074958.
    HOGENOMiHOG000091085.
    HOVERGENiHBG003005.
    InParanoidiQ5E987.
    KOiK02729.
    OMAiCAMSGLT.
    OrthoDBiEOG769ZKB.
    TreeFamiTF106211.

    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.

    Q5E987-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV    50
    EKRITSPLME PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW 100
    FTYNETMTVE SVTQAVSNLA LQFGEEDADP GAMSRPFGVA LLFGGVDEKG 150
    PQLFHMDPSG TFVQCDARAI GSASEGAQSS LQEVYHKSMT LKEAIKSSLI 200
    ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD I 241
    Length:241
    Mass (Da):26,411
    Last modified:March 15, 2005 - v1
    Checksum:i5610CDA00469120A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT021033 mRNA. Translation: AAX09050.1.
    BC102343 mRNA. Translation: AAI02344.1.
    RefSeqiNP_001015566.1. NM_001015566.1.
    UniGeneiBt.47769.

    Genome annotation databases

    EnsembliENSBTAT00000027507; ENSBTAP00000027507; ENSBTAG00000020641.
    GeneIDi510155.
    KEGGibta:510155.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT021033 mRNA. Translation: AAX09050.1 .
    BC102343 mRNA. Translation: AAI02344.1 .
    RefSeqi NP_001015566.1. NM_001015566.1.
    UniGenei Bt.47769.

    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 E/S 1-241 [» ]
    ProteinModelPortali Q5E987.
    SMRi Q5E987. Positions 9-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000027507.

    Protein family/group databases

    MEROPSi T01.975.

    Proteomic databases

    PaxDbi Q5E987.
    PRIDEi Q5E987.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000027507 ; ENSBTAP00000027507 ; ENSBTAG00000020641 .
    GeneIDi 510155.
    KEGGi bta:510155.

    Organism-specific databases

    CTDi 5686.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074958.
    HOGENOMi HOG000091085.
    HOVERGENi HBG003005.
    InParanoidi Q5E987.
    KOi K02729.
    OMAi CAMSGLT.
    OrthoDBi EOG769ZKB.
    TreeFami TF106211.

    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 Q5E987.
    NextBioi 20869301.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. 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.
    3. "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 nameiPSA5_BOVIN
    AccessioniPrimary (citable) accession number: Q5E987
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 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