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P51665

- PSMD7_HUMAN

UniProt

P51665 - PSMD7_HUMAN

Protein

26S proteasome non-ATPase regulatory subunit 7

Gene

PSMD7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (10 May 2002)
      Previous versions | rss
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    Functioni

    Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    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

    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

    MEROPSiM67.973.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    26S proteasome non-ATPase regulatory subunit 7
    Alternative name(s):
    26S proteasome regulatory subunit RPN8
    26S proteasome regulatory subunit S12
    Mov34 protein homolog
    Proteasome subunit p40
    Gene namesi
    Name:PSMD7
    Synonyms:MOV34L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:9565. PSMD7.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProt
    6. proteasome complex Source: ProtInc
    7. proteasome regulatory particle Source: ProtInc

    Keywords - Cellular componenti

    Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33911.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 32432426S proteasome non-ATPase regulatory subunit 7PRO_0000213943Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki180 – 180Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei204 – 2041N6-acetyllysine1 Publication
    Modified residuei214 – 2141N6-acetyllysine1 Publication
    Modified residuei316 – 3161N6-acetyllysineBy similarity
    Modified residuei317 – 3171N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP51665.
    PaxDbiP51665.
    PeptideAtlasiP51665.
    PRIDEiP51665.

    PTM databases

    PhosphoSiteiP51665.

    Expressioni

    Gene expression databases

    ArrayExpressiP51665.
    BgeeiP51665.
    CleanExiHS_PSMD7.
    GenevestigatoriP51665.

    Organism-specific databases

    HPAiCAB019379.
    HPA049824.
    HPA056069.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with TRIM5.2 Publications

    Protein-protein interaction databases

    BioGridi111685. 70 interactions.
    DIPiDIP-27572N.
    IntActiP51665. 32 interactions.
    MINTiMINT-5002613.
    STRINGi9606.ENSP00000219313.

    Structurei

    Secondary structure

    1
    324
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115
    Helixi13 – 2816
    Beta strandi36 – 5621
    Beta strandi58 – 603
    Beta strandi67 – 704
    Helixi72 – 8312
    Beta strandi86 – 883
    Beta strandi90 – 967
    Helixi105 – 1128
    Turni113 – 1153
    Beta strandi120 – 1245
    Beta strandi134 – 14310
    Beta strandi152 – 16211
    Helixi166 – 17813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O95X-ray1.95A/B1-186[»]
    2O96X-ray3.00A/B1-177[»]
    ProteinModelPortaliP51665.
    SMRiP51665. Positions 1-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51665.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 118115MPNAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi286 – 32439Glu/Lys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M67A family.Curated
    Contains 1 MPN (JAB/Mov34) domain.Curated

    Phylogenomic databases

    eggNOGiCOG1310.
    HOGENOMiHOG000209236.
    HOVERGENiHBG035951.
    InParanoidiP51665.
    KOiK03038.
    OMAiDHNYVES.
    OrthoDBiEOG7B8S4G.
    PhylomeDBiP51665.

    Family and domain databases

    InterProiIPR000555. JAMM/MPN+_dom.
    IPR024969. Rpn11/EIF3F_C.
    [Graphical view]
    PfamiPF01398. JAB. 1 hit.
    PF13012. MitMem_reg. 1 hit.
    [Graphical view]
    SMARTiSM00232. JAB_MPN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P51665-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPELAVQKVV VHPLVLLSVV DHFNRIGKVG NQKRVVGVLL GSWQKKVLDV    50
    SNSFAVPFDE DDKDDSVWFL DHDYLENMYG MFKKVNARER IVGWYHTGPK 100
    LHKNDIAINE LMKRYCPNSV LVIIDVKPKD LGLPTEAYIS VEEVHDDGTP 150
    TSKTFEHVTS EIGAEEAEEV GVEHLLRDIK DTTVGTLSQR ITNQVHGLKG 200
    LNSKLLDIRS YLEKVATGKL PINHQIIYQL QDVFNLLPDV SLQEFVKAFY 250
    LKTNDQMVVV YLASLIRSVV ALHNLINNKI ANRDAEKKEG QEKEESKKDR 300
    KEDKEKDKDK EKSDVKKEEK KEKK 324
    Length:324
    Mass (Da):37,025
    Last modified:May 10, 2002 - v2
    Checksum:i3F7B343996B102B7
    GO

    Sequence cautioni

    The sequence AAH00338.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271G → V in BAA08780. (PubMed:7755639)Curated
    Sequence conflicti144 – 1452VH → DQ in BAA08780. (PubMed:7755639)Curated
    Sequence conflicti216 – 2161A → G in BAA08780. (PubMed:7755639)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50063 mRNA. Translation: BAA08780.1.
    CH471166 Genomic DNA. Translation: EAW59162.1.
    CH471166 Genomic DNA. Translation: EAW59163.1.
    BC000338 mRNA. Translation: AAH00338.1. Sequence problems.
    BC012606 mRNA. Translation: AAH12606.1.
    CCDSiCCDS10910.1.
    PIRiJC4154.
    S65491.
    RefSeqiNP_002802.2. NM_002811.4.
    UniGeneiHs.440604.

    Genome annotation databases

    EnsembliENST00000219313; ENSP00000219313; ENSG00000103035.
    GeneIDi5713.
    KEGGihsa:5713.
    UCSCiuc002fcq.3. human.

    Polymorphism databases

    DMDMi20532412.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50063 mRNA. Translation: BAA08780.1 .
    CH471166 Genomic DNA. Translation: EAW59162.1 .
    CH471166 Genomic DNA. Translation: EAW59163.1 .
    BC000338 mRNA. Translation: AAH00338.1 . Sequence problems.
    BC012606 mRNA. Translation: AAH12606.1 .
    CCDSi CCDS10910.1.
    PIRi JC4154.
    S65491.
    RefSeqi NP_002802.2. NM_002811.4.
    UniGenei Hs.440604.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2O95 X-ray 1.95 A/B 1-186 [» ]
    2O96 X-ray 3.00 A/B 1-177 [» ]
    ProteinModelPortali P51665.
    SMRi P51665. Positions 1-288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111685. 70 interactions.
    DIPi DIP-27572N.
    IntActi P51665. 32 interactions.
    MINTi MINT-5002613.
    STRINGi 9606.ENSP00000219313.

    Protein family/group databases

    MEROPSi M67.973.

    PTM databases

    PhosphoSitei P51665.

    Polymorphism databases

    DMDMi 20532412.

    Proteomic databases

    MaxQBi P51665.
    PaxDbi P51665.
    PeptideAtlasi P51665.
    PRIDEi P51665.

    Protocols and materials databases

    DNASUi 5713.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219313 ; ENSP00000219313 ; ENSG00000103035 .
    GeneIDi 5713.
    KEGGi hsa:5713.
    UCSCi uc002fcq.3. human.

    Organism-specific databases

    CTDi 5713.
    GeneCardsi GC16P074330.
    HGNCi HGNC:9565. PSMD7.
    HPAi CAB019379.
    HPA049824.
    HPA056069.
    MIMi 157970. gene.
    neXtProti NX_P51665.
    PharmGKBi PA33911.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1310.
    HOGENOMi HOG000209236.
    HOVERGENi HBG035951.
    InParanoidi P51665.
    KOi K03038.
    OMAi DHNYVES.
    OrthoDBi EOG7B8S4G.
    PhylomeDBi P51665.

    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 PSMD7. human.
    EvolutionaryTracei P51665.
    GeneWikii PSMD7.
    GenomeRNAii 5713.
    NextBioi 22194.
    PROi P51665.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51665.
    Bgeei P51665.
    CleanExi HS_PSMD7.
    Genevestigatori P51665.

    Family and domain databases

    InterProi IPR000555. JAMM/MPN+_dom.
    IPR024969. Rpn11/EIF3F_C.
    [Graphical view ]
    Pfami PF01398. JAB. 1 hit.
    PF13012. MitMem_reg. 1 hit.
    [Graphical view ]
    SMARTi SM00232. JAB_MPN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of p40, a regulatory subunit of the human 26S proteasome, and a homolog of the Mov-34 gene product."
      Tsurumi C., DeMartino G.N., Slaughter C., Shimbara N., Tanaka K.
      Biochem. Biophys. Res. Commun. 210:600-608(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Lung and Skin.
    4. "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.
    5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions."
      Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., Luban J., Campbell E.M.
      Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM5.
    8. "The crystal structure of the human Mov34 MPN domain reveals a metal-free dimer."
      Sanches M., Alves B.S.C., Zanchin N.I.T., Guimaraes B.G.
      J. Mol. Biol. 370:846-855(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-186, SUBUNIT, LACK OF METAL-BINDING.

    Entry informationi

    Entry nameiPSMD7_HUMAN
    AccessioniPrimary (citable) accession number: P51665
    Secondary accession number(s): D3DWS9, Q6PKI2, Q96E97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 10, 2002
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 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

    Miscellaneous

    Does not bind a metal ion.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3