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O00231

- PSD11_HUMAN

UniProt

O00231 - PSD11_HUMAN

Protein

26S proteasome non-ATPase regulatory subunit 11

Gene

PSMD11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    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. proteasome assembly Source: UniProtKB
    16. protein polyubiquitination Source: Reactome
    17. regulation of apoptotic process Source: Reactome
    18. regulation of cellular amino acid metabolic process Source: Reactome
    19. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    20. RNA metabolic process Source: Reactome
    21. small molecule metabolic process Source: Reactome
    22. stem cell differentiation Source: UniProtKB
    23. ubiquitin-dependent protein catabolic process Source: UniProtKB
    24. 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    26S proteasome non-ATPase regulatory subunit 11
    Alternative name(s):
    26S proteasome regulatory subunit RPN6
    26S proteasome regulatory subunit S9
    26S proteasome regulatory subunit p44.5
    Gene namesi
    Name:PSMD11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9556. PSMD11.

    Subcellular locationi

    Nucleus By similarity. Cytoplasmcytosol By similarity

    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 accessory complex Source: UniProtKB
    7. proteasome complex Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141S → A: Does not affect phosphorylation by AMPK; when associated with A-79 and A-272. 1 Publication
    Mutagenesisi79 – 791S → A: Does not affect phosphorylation by AMPK; when associated with A-14 and A-272. 1 Publication
    Mutagenesisi272 – 2721S → A: Does not affect phosphorylation by AMPK; when associated with A14- and A-79. 1 Publication

    Organism-specific databases

    PharmGKBiPA33902.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 42242126S proteasome non-ATPase regulatory subunit 11PRO_0000173857Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei14 – 141Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by AMPK.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00231.
    PaxDbiO00231.
    PRIDEiO00231.

    2D gel databases

    OGPiO00231.

    PTM databases

    PhosphoSiteiO00231.

    Expressioni

    Tissue specificityi

    Highly expressed in embryonic stem cells (ESCs). Expression decreases as ESCs differentiate.1 Publication

    Inductioni

    By FOXO4; expression in embryonic stem cells (ESCs) is mediated by FOXO4.1 Publication

    Gene expression databases

    ArrayExpressiO00231.
    BgeeiO00231.
    CleanExiHS_PSMD11.
    GenevestigatoriO00231.

    Organism-specific databases

    HPAiHPA042275.

    Interactioni

    Subunit structurei

    Component of the lid subcomplex of the 19S proteasome regulatory particle complex (also named PA700 complex). The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRMT6Q96LA82EBI-357816,EBI-912440

    Protein-protein interaction databases

    BioGridi111689. 103 interactions.
    IntActiO00231. 48 interactions.
    MINTiMINT-1154929.
    STRINGi9606.ENSP00000261712.

    Structurei

    3D structure databases

    ProteinModelPortaliO00231.
    SMRiO00231. Positions 38-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini222 – 389168PCIAdd
    BLAST

    Sequence similaritiesi

    Belongs to the proteasome subunit S9 family.Curated
    Contains 1 PCI domain.Curated

    Phylogenomic databases

    eggNOGiCOG5159.
    HOVERGENiHBG053738.
    InParanoidiO00231.
    KOiK03036.
    OMAiNLDMQSG.
    OrthoDBiEOG7F24T1.
    PhylomeDBiO00231.
    TreeFamiTF106230.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.25.40.10. 1 hit.
    InterProiIPR013143. PAM.
    IPR000717. PCI_dom.
    IPR011990. TPR-like_helical.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF01399. PCI. 1 hit.
    [Graphical view]
    SMARTiSM00753. PAM. 1 hit.
    SM00088. PINT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00231-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI    50
    LELGSLLAKT GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME 100
    AATGQEVELC LECIEWAKSE KRTFLRQALE ARLVSLYFDT KRYQEALHLG 150
    SQLLRELKKM DDKALLVEVQ LLESKTYHAL SNLPKARAAL TSARTTANAI 200
    YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD SIDSPKAITS 250
    LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA 300
    DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI 350
    SSLIKLSKAD VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA 400
    LETIQNMSKV VDSLYNKAKK LT 422
    Length:422
    Mass (Da):47,464
    Last modified:January 23, 2007 - v3
    Checksum:iCE113054CBEBDB05
    GO
    Isoform 2 (identifier: O00231-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         375-375: H → HA

    Note: No experimental confirmation available.

    Show »
    Length:423
    Mass (Da):47,535
    Checksum:iBDE786518637385D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti113 – 1131C → S in AAB58732. (PubMed:9119060)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei375 – 3751H → HA in isoform 2. 1 PublicationVSP_044400

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001212 mRNA. Translation: AAB58732.1.
    AB003102 mRNA. Translation: BAA19748.1.
    AK290602 mRNA. Translation: BAF83291.1.
    AK223196 mRNA. Translation: BAD96916.1.
    CH471147 Genomic DNA. Translation: EAW80229.1.
    CH471147 Genomic DNA. Translation: EAW80230.1.
    BC000437 mRNA. Translation: AAH00437.1.
    BC004430 mRNA. Translation: AAH04430.1.
    CCDSiCCDS11272.1. [O00231-1]
    PIRiJC6524.
    RefSeqiNP_001257411.1. NM_001270482.1. [O00231-1]
    NP_002806.2. NM_002815.3. [O00231-1]
    UniGeneiHs.443379.

    Genome annotation databases

    EnsembliENST00000261712; ENSP00000261712; ENSG00000108671. [O00231-1]
    ENST00000457654; ENSP00000393185; ENSG00000108671. [O00231-1]
    GeneIDi5717.
    KEGGihsa:5717.
    UCSCiuc002hhm.4. human. [O00231-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001212 mRNA. Translation: AAB58732.1 .
    AB003102 mRNA. Translation: BAA19748.1 .
    AK290602 mRNA. Translation: BAF83291.1 .
    AK223196 mRNA. Translation: BAD96916.1 .
    CH471147 Genomic DNA. Translation: EAW80229.1 .
    CH471147 Genomic DNA. Translation: EAW80230.1 .
    BC000437 mRNA. Translation: AAH00437.1 .
    BC004430 mRNA. Translation: AAH04430.1 .
    CCDSi CCDS11272.1. [O00231-1 ]
    PIRi JC6524.
    RefSeqi NP_001257411.1. NM_001270482.1. [O00231-1 ]
    NP_002806.2. NM_002815.3. [O00231-1 ]
    UniGenei Hs.443379.

    3D structure databases

    ProteinModelPortali O00231.
    SMRi O00231. Positions 38-390.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111689. 103 interactions.
    IntActi O00231. 48 interactions.
    MINTi MINT-1154929.
    STRINGi 9606.ENSP00000261712.

    PTM databases

    PhosphoSitei O00231.

    2D gel databases

    OGPi O00231.

    Proteomic databases

    MaxQBi O00231.
    PaxDbi O00231.
    PRIDEi O00231.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261712 ; ENSP00000261712 ; ENSG00000108671 . [O00231-1 ]
    ENST00000457654 ; ENSP00000393185 ; ENSG00000108671 . [O00231-1 ]
    GeneIDi 5717.
    KEGGi hsa:5717.
    UCSCi uc002hhm.4. human. [O00231-1 ]

    Organism-specific databases

    CTDi 5717.
    GeneCardsi GC17P030771.
    HGNCi HGNC:9556. PSMD11.
    HPAi HPA042275.
    MIMi 604449. gene.
    neXtProti NX_O00231.
    PharmGKBi PA33902.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5159.
    HOVERGENi HBG053738.
    InParanoidi O00231.
    KOi K03036.
    OMAi NLDMQSG.
    OrthoDBi EOG7F24T1.
    PhylomeDBi O00231.
    TreeFami TF106230.

    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

    GeneWikii PSMD11.
    GenomeRNAii 5717.
    NextBioi 22212.
    PROi O00231.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00231.
    Bgeei O00231.
    CleanExi HS_PSMD11.
    Genevestigatori O00231.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.25.40.10. 1 hit.
    InterProi IPR013143. PAM.
    IPR000717. PCI_dom.
    IPR011990. TPR-like_helical.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF01399. PCI. 1 hit.
    [Graphical view ]
    SMARTi SM00753. PAM. 1 hit.
    SM00088. PINT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of subunit 9 of the 26S proteasome."
      Hoffman L., Rechsteiner M.
      FEBS Lett. 404:179-184(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits of the 26S proteasome."
      Saito A., Watanabe T.K., Shimada Y., Fujiwara T., Slaughter C.A., DeMartino G.N., Tanahashi N., Tanaka K.
      Gene 203:241-250(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Heart.
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Pancreas.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Lung.
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11.
      Tissue: Platelet.
    8. Bienvenut W.V., Potts A., Brablan J., Quadroni M.
      Submitted (JUL-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase."
      Moreno D., Viana R., Sanz P.
      Int. J. Biochem. Cell Biol. 41:2431-2439(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-14; SER-79 AND SER-272.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Increased proteasome activity in human embryonic stem cells is regulated by PSMD11."
      Vilchez D., Boyer L., Morantte I., Lutz M., Merkwirth C., Joyce D., Spencer B., Page L., Masliah E., Berggren W.T., Gage F.H., Dillin A.
      Nature 489:304-308(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX, TISSUE SPECIFICITY, INDUCTION.
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPSD11_HUMAN
    AccessioniPrimary (citable) accession number: O00231
    Secondary accession number(s): A8K3I7
    , E1P663, O00495, Q53FT5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 3 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3