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P28072

- PSB6_HUMAN

UniProt

P28072 - PSB6_HUMAN

Protein

Proteasome subunit beta type-6

Gene

PSMB6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 4 (10 May 2002)
      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. This unit is responsible of the peptidyl glutamyl-like activity. May catalyze basal processing of intracellular antigens.

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei35 – 351NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    5. apoptotic process Source: Reactome
    6. cellular nitrogen compound metabolic process Source: Reactome
    7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
    8. G1/S transition of mitotic cell cycle Source: Reactome
    9. gene expression Source: Reactome
    10. mitotic cell cycle Source: Reactome
    11. mRNA metabolic process Source: Reactome
    12. negative regulation of apoptotic process Source: Reactome
    13. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    14. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    15. protein polyubiquitination Source: Reactome
    16. regulation of apoptotic process Source: Reactome
    17. regulation of cellular amino acid metabolic process Source: Reactome
    18. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    19. RNA metabolic process Source: Reactome
    20. small molecule metabolic process Source: Reactome
    21. viral process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Protein family/group databases

    MEROPSiT01.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-6 (EC:3.4.25.1)
    Alternative name(s):
    Macropain delta chain
    Multicatalytic endopeptidase complex delta chain
    Proteasome delta chain
    Proteasome subunit Y
    Gene namesi
    Name:PSMB6
    Synonyms:LMPY, Y
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9543. PSMB6.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProt
    5. proteasome core complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33888.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Propeptidei2 – 3433Removed in mature form2 PublicationsPRO_0000026613Add
    BLAST
    Chaini35 – 239205Proteasome subunit beta type-6PRO_0000026614Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation, Zymogen

    Proteomic databases

    MaxQBiP28072.
    PaxDbiP28072.
    PeptideAtlasiP28072.
    PRIDEiP28072.

    2D gel databases

    OGPiP28072.
    SWISS-2DPAGEP28072.

    PTM databases

    PhosphoSiteiP28072.

    Expressioni

    Inductioni

    Down-regulated by IFNG/IFN-gamma (at protein level). Up-regulated in anaplastic thyroid cancer cell lines.2 Publications

    Gene expression databases

    ArrayExpressiP28072.
    BgeeiP28072.
    CleanExiHS_PSMB6.
    GenevestigatoriP28072.

    Organism-specific databases

    HPAiHPA023312.

    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. This subunit can be displaced by the equivalent immune-specific subunit PSMB9. Interacts with HIV-1 TAT protein.2 Publications

    Protein-protein interaction databases

    BioGridi111667. 56 interactions.
    IntActiP28072. 14 interactions.
    MINTiMINT-5004163.
    STRINGi9606.ENSP00000270586.

    Structurei

    3D structure databases

    ProteinModelPortaliP28072.
    SMRiP28072. Positions 35-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091079.
    HOVERGENiHBG000123.
    InParanoidiP28072.
    KOiK02738.
    OMAiTSIMAVQ.
    OrthoDBiEOG79GT80.
    PhylomeDBiP28072.
    TreeFamiTF106221.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    PRINTSiPR00141. PROTEASOME.
    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.

    P28072-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAATLLAARG AGPAPAWGPE AFTPDWESRE VSTGTTIMAV QFDGGVVLGA    50
    DSRTTTGSYI ANRVTDKLTP IHDRIFCCRS GSAADTQAVA DAVTYQLGFH 100
    SIELNEPPLV HTAASLFKEM CYRYREDLMA GIIIAGWDPQ EGGQVYSVPM 150
    GGMMVRQSFA IGGSGSSYIY GYVDATYREG MTKEECLQFT ANALALAMER 200
    DGSSGGVIRL AAIAESGVER QVLLGDQIPK FAVATLPPA 239
    Length:239
    Mass (Da):25,358
    Last modified:May 10, 2002 - v4
    Checksum:i7DF4081DC735930C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451V → G in BAA06098. (PubMed:8066462)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071P → A.
    Corresponds to variant rs2304974 [ dbSNP | Ensembl ].
    VAR_020030

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D29012 mRNA. Translation: BAA06098.1.
    BC000835 mRNA. Translation: AAH00835.1.
    X61971 mRNA. Translation: CAA43963.1.
    CCDSiCCDS11056.1.
    PIRiB54589.
    S17522.
    RefSeqiNP_002789.1. NM_002798.2.
    UniGeneiHs.77060.

    Genome annotation databases

    EnsembliENST00000270586; ENSP00000270586; ENSG00000142507.
    GeneIDi5694.
    KEGGihsa:5694.
    UCSCiuc002fzb.4. human.

    Polymorphism databases

    DMDMi20532407.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D29012 mRNA. Translation: BAA06098.1 .
    BC000835 mRNA. Translation: AAH00835.1 .
    X61971 mRNA. Translation: CAA43963.1 .
    CCDSi CCDS11056.1.
    PIRi B54589.
    S17522.
    RefSeqi NP_002789.1. NM_002798.2.
    UniGenei Hs.77060.

    3D structure databases

    ProteinModelPortali P28072.
    SMRi P28072. Positions 35-236.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111667. 56 interactions.
    IntActi P28072. 14 interactions.
    MINTi MINT-5004163.
    STRINGi 9606.ENSP00000270586.

    Chemistry

    ChEMBLi CHEMBL1944496.

    Protein family/group databases

    MEROPSi T01.010.

    PTM databases

    PhosphoSitei P28072.

    Polymorphism databases

    DMDMi 20532407.

    2D gel databases

    OGPi P28072.
    SWISS-2DPAGE P28072.

    Proteomic databases

    MaxQBi P28072.
    PaxDbi P28072.
    PeptideAtlasi P28072.
    PRIDEi P28072.

    Protocols and materials databases

    DNASUi 5694.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000270586 ; ENSP00000270586 ; ENSG00000142507 .
    GeneIDi 5694.
    KEGGi hsa:5694.
    UCSCi uc002fzb.4. human.

    Organism-specific databases

    CTDi 5694.
    GeneCardsi GC17P004699.
    HGNCi HGNC:9543. PSMB6.
    HPAi HPA023312.
    MIMi 600307. gene.
    neXtProti NX_P28072.
    PharmGKBi PA33888.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091079.
    HOVERGENi HBG000123.
    InParanoidi P28072.
    KOi K02738.
    OMAi TSIMAVQ.
    OrthoDBi EOG79GT80.
    PhylomeDBi P28072.
    TreeFami TF106221.

    Enzyme and pathway databases

    Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Miscellaneous databases

    ChiTaRSi PSMB6. human.
    GeneWikii PSMB6.
    GenomeRNAii 5694.
    NextBioi 22118.
    PROi P28072.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28072.
    Bgeei P28072.
    CleanExi HS_PSMB6.
    Genevestigatori P28072.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PRINTSi PR00141. PROTEASOME.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and interferon gamma down-regulation of proteasomal subunits X and Y."
      Akiyama K.-Y., Yokota K.-Y., Kagawa S., Shimbara N., Tamura T., Akioka H., Nothwang H.G., Noda C., Tanaka K., Ichihara A.
      Science 265:1231-1234(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cervix.
    3. Bienvenut W.V., Zebisch A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-9; 54-63 AND 210-230, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    4. "The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous."
      DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R., Dawson P.A., Slaughter C.A.
      Biochim. Biophys. Acta 1079:29-38(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-239, PROTEIN SEQUENCE OF 35-75; 80-110 AND 210-233.
    5. "Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)."
      Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N., Slaughter C.A.
      Biochim. Biophys. Acta 1037:178-185(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 35-60.
    6. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 157-178, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    7. "Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by interferon-gamma for acquirement of the functional diversity responsible for antigen processing."
      Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M., Kristensen P., Hendil K.B., Tanaka K., Ichihara A.
      FEBS Lett. 343:85-88(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    8. "Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits."
      Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E.
      FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    9. "Comprehensive gene expression profiling of anaplastic thyroid cancers with cDNA microarray of 25 344 genes."
      Onda M., Emi M., Yoshida A., Miyamoto S., Akaishi J., Asaka S., Mizutani K., Shimizu K., Nagahama M., Ito K., Tanaka T., Tsunoda T.
      Endocr. Relat. Cancer 11:843-854(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
      Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
      Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPSB6_HUMAN
    AccessioniPrimary (citable) accession number: P28072
    Secondary accession number(s): Q96J55
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: May 10, 2002
    Last modified: October 1, 2014
    This is version 159 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3