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)

Q2YDE4

- PSA6_BOVIN

UniProt

Q2YDE4 - PSA6_BOVIN

Protein

Proteasome subunit alpha type-6

Gene

PSMA6

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      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 By similarity.By similarity

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

    GO - Molecular functioni

    1. RNA binding Source: Ensembl
    2. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. positive regulation of NF-kappaB transcription factor activity 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

    MEROPSiT01.971.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-6 (EC:3.4.25.1)
    Gene namesi
    Name:PSMA6
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    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. mitochondrion Source: Ensembl
    3. nuclear matrix Source: Ensembl
    4. polysome Source: Ensembl
    5. proteasome core complex Source: UniProtKB
    6. 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 – 246246Proteasome subunit alpha type-6PRO_0000274034Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi5 – 51O-linked (GlcNAc)By similarity
    Cross-linki59 – 59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei102 – 1021N6-acetyllysineBy similarity
    Modified residuei104 – 1041N6-acetyllysineBy similarity
    Modified residuei159 – 1591PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ2YDE4.
    PRIDEiQ2YDE4.

    Interactioni

    Subunit structurei

    Interacts with ALKBH4 By similarity. 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.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000012773.

    Structurei

    Secondary structure

    1
    246
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni8 – 125
    Helixi23 – 3311
    Beta strandi38 – 436
    Beta strandi45 – 539
    Beta strandi59 – 613
    Helixi63 – 653
    Beta strandi68 – 758
    Beta strandi77 – 826
    Helixi84 – 10522
    Helixi111 – 12717
    Beta strandi128 – 1314
    Beta strandi135 – 14410
    Turni145 – 1473
    Beta strandi148 – 1547
    Beta strandi160 – 16910
    Helixi172 – 18211
    Helixi191 – 20515
    Beta strandi214 – 2218
    Beta strandi224 – 2296
    Helixi232 – 24312

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IRUX-ray2.75A/O1-246[»]
    ProteinModelPortaliQ2YDE4.
    SMRiQ2YDE4. Positions 2-245.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ2YDE4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091084.
    HOVERGENiHBG107363.
    InParanoidiQ2YDE4.
    KOiK02730.

    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.

    Q2YDE4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI    50
    VTQKKVPDKL LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN 100
    WKYKYGYEIP VDMLCKRIAD ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ 150
    VYKCDPAGYY CGFKATAAGV KQTESTSFLE KKVKKKFDWT FEQTVETAIT 200
    CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV ALAERD 246
    Length:246
    Mass (Da):27,399
    Last modified:December 20, 2005 - v1
    Checksum:i94D1FD3C0A7CC72A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC110260 mRNA. Translation: AAI10261.1.
    RefSeqiNP_001039427.1. NM_001045962.1.
    UniGeneiBt.15837.

    Genome annotation databases

    GeneIDi507213.
    KEGGibta:507213.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC110260 mRNA. Translation: AAI10261.1 .
    RefSeqi NP_001039427.1. NM_001045962.1.
    UniGenei Bt.15837.

    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 A/O 1-246 [» ]
    ProteinModelPortali Q2YDE4.
    SMRi Q2YDE4. Positions 2-245.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000012773.

    Protein family/group databases

    MEROPSi T01.971.

    Proteomic databases

    PaxDbi Q2YDE4.
    PRIDEi Q2YDE4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 507213.
    KEGGi bta:507213.

    Organism-specific databases

    CTDi 5687.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091084.
    HOVERGENi HBG107363.
    InParanoidi Q2YDE4.
    KOi K02730.

    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 Q2YDE4.
    NextBioi 20867961.

    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 (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Liver.
    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 nameiPSA6_BOVIN
    AccessioniPrimary (citable) accession number: Q2YDE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 86 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