Full text data of PSMD11
PSMD11
[Confidence: high (present in two of the MS resources)]
26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory subunit RPN6; 26S proteasome regulatory subunit S9; 26S proteasome regulatory subunit p44.5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory subunit RPN6; 26S proteasome regulatory subunit S9; 26S proteasome regulatory subunit p44.5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00105598
IPI00105598 Proteasome 26S non-ATPase subunit 11 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00105598 Proteasome 26S non-ATPase subunit 11 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
O00231
ID PSD11_HUMAN Reviewed; 422 AA.
AC O00231; A8K3I7; E1P663; O00495; Q53FT5;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 11;
DE AltName: Full=26S proteasome regulatory subunit RPN6;
DE AltName: Full=26S proteasome regulatory subunit S9;
DE AltName: Full=26S proteasome regulatory subunit p44.5;
GN Name=PSMD11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=9119060; DOI=10.1016/S0014-5793(97)00126-9;
RA Hoffman L., Rechsteiner M.;
RT "Molecular cloning and expression of subunit 9 of the 26S
RT proteasome.";
RL FEBS Lett. 404:179-184(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9426256; DOI=10.1016/S0378-1119(97)00524-6;
RA Saito A., Watanabe T.K., Shimada Y., Fujiwara T., Slaughter C.A.,
RA DeMartino G.N., Tanahashi N., Tanaka K.;
RT "cDNA cloning and functional analysis of p44.5 and p55, two regulatory
RT subunits of the 26S proteasome.";
RL Gene 203:241-250(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V., Potts A., Brablan J., Quadroni M.;
RL Submitted (JUL-2004) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-14; SER-79 AND SER-272.
RX PubMed=19616115; DOI=10.1016/j.biocel.2009.07.002;
RA Moreno D., Viana R., Sanz P.;
RT "Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the
RT proteasome, as a novel interaction partner of AMP-activated protein
RT kinase.";
RL Int. J. Biochem. Cell Biol. 41:2431-2439(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION, IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX,
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=22972301; DOI=10.1038/nature11468;
RA Vilchez D., Boyer L., Morantte I., Lutz M., Merkwirth C., Joyce D.,
RA Spencer B., Page L., Masliah E., Berggren W.T., Gage F.H., Dillin A.;
RT "Increased proteasome activity in human embryonic stem cells is
RT regulated by PSMD11.";
RL Nature 489:304-308(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the lid subcomplex of the 26S proteasome, a
CC multiprotein complex involved in the ATP-dependent degradation of
CC ubiquitinated proteins. In the complex, PSMD11 is required for
CC proteasome assembly. Plays a key role in increased proteasome
CC activity in embryonic stem cells (ESCs): its high expression in
CC ESCs promotes enhanced assembly of the 26S proteasome, followed by
CC higher proteasome activity.
CC -!- SUBUNIT: Component of the lid subcomplex of the 19S proteasome
CC regulatory particle complex (also named PA700 complex). The 26S
CC proteasome consists of a 20S proteasome core and two 19S
CC regulatory subunits.
CC -!- INTERACTION:
CC Q96LA8:PRMT6; NbExp=2; IntAct=EBI-357816, EBI-912440;
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm, cytosol
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00231-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00231-2; Sequence=VSP_044400;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in embryonic stem cells
CC (ESCs). Expression decreases as ESCs differentiate.
CC -!- INDUCTION: By FOXO4; expression in embryonic stem cells (ESCs) is
CC mediated by FOXO4.
CC -!- PTM: Phosphorylated by AMPK.
CC -!- SIMILARITY: Belongs to the proteasome subunit S9 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
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DR EMBL; AF001212; AAB58732.1; -; mRNA.
DR EMBL; AB003102; BAA19748.1; -; mRNA.
DR EMBL; AK290602; BAF83291.1; -; mRNA.
DR EMBL; AK223196; BAD96916.1; -; mRNA.
DR EMBL; CH471147; EAW80229.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80230.1; -; Genomic_DNA.
DR EMBL; BC000437; AAH00437.1; -; mRNA.
DR EMBL; BC004430; AAH04430.1; -; mRNA.
DR PIR; JC6524; JC6524.
DR RefSeq; NP_001257411.1; NM_001270482.1.
DR RefSeq; NP_002806.2; NM_002815.3.
DR UniGene; Hs.443379; -.
DR ProteinModelPortal; O00231; -.
DR SMR; O00231; 38-390.
DR IntAct; O00231; 48.
DR MINT; MINT-1154929; -.
DR STRING; 9606.ENSP00000261712; -.
DR PhosphoSite; O00231; -.
DR OGP; O00231; -.
DR PaxDb; O00231; -.
DR PRIDE; O00231; -.
DR Ensembl; ENST00000261712; ENSP00000261712; ENSG00000108671.
DR Ensembl; ENST00000457654; ENSP00000393185; ENSG00000108671.
DR GeneID; 5717; -.
DR KEGG; hsa:5717; -.
DR UCSC; uc002hhm.4; human.
DR CTD; 5717; -.
DR GeneCards; GC17P030771; -.
DR HGNC; HGNC:9556; PSMD11.
DR HPA; HPA042275; -.
DR MIM; 604449; gene.
DR neXtProt; NX_O00231; -.
DR PharmGKB; PA33902; -.
DR eggNOG; COG5159; -.
DR HOVERGEN; HBG053738; -.
DR InParanoid; O00231; -.
DR KO; K03036; -.
DR OMA; DKDFNTA; -.
DR OrthoDB; EOG7F24T1; -.
DR PhylomeDB; O00231; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; PSMD11; -.
DR GenomeRNAi; 5717; -.
DR NextBio; 22212; -.
DR PRO; PR:O00231; -.
DR ArrayExpress; O00231; -.
DR Bgee; O00231; -.
DR CleanEx; HS_PSMD11; -.
DR Genevestigator; O00231; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0022624; C:proteasome accessory complex; IDA:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0043248; P:proteasome assembly; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR013143; PAM.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 422 26S proteasome non-ATPase regulatory
FT subunit 11.
FT /FTId=PRO_0000173857.
FT DOMAIN 222 389 PCI.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 14 14 Phosphoserine.
FT VAR_SEQ 375 375 H -> HA (in isoform 2).
FT /FTId=VSP_044400.
FT MUTAGEN 14 14 S->A: Does not affect phosphorylation by
FT AMPK; when associated with A-79 and A-
FT 272.
FT MUTAGEN 79 79 S->A: Does not affect phosphorylation by
FT AMPK; when associated with A-14 and A-
FT 272.
FT MUTAGEN 272 272 S->A: Does not affect phosphorylation by
FT AMPK; when associated with A14- and A-79.
FT CONFLICT 113 113 C -> S (in Ref. 1; AAB58732).
SQ SEQUENCE 422 AA; 47464 MW; CE113054CBEBDB05 CRC64;
MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI LELGSLLAKT
GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME AATGQEVELC LECIEWAKSE
KRTFLRQALE ARLVSLYFDT KRYQEALHLG SQLLRELKKM DDKALLVEVQ LLESKTYHAL
SNLPKARAAL TSARTTANAI YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD
SIDSPKAITS LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA
DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI SSLIKLSKAD
VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA LETIQNMSKV VDSLYNKAKK
LT
//
ID PSD11_HUMAN Reviewed; 422 AA.
AC O00231; A8K3I7; E1P663; O00495; Q53FT5;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 11;
DE AltName: Full=26S proteasome regulatory subunit RPN6;
DE AltName: Full=26S proteasome regulatory subunit S9;
DE AltName: Full=26S proteasome regulatory subunit p44.5;
GN Name=PSMD11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=9119060; DOI=10.1016/S0014-5793(97)00126-9;
RA Hoffman L., Rechsteiner M.;
RT "Molecular cloning and expression of subunit 9 of the 26S
RT proteasome.";
RL FEBS Lett. 404:179-184(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9426256; DOI=10.1016/S0378-1119(97)00524-6;
RA Saito A., Watanabe T.K., Shimada Y., Fujiwara T., Slaughter C.A.,
RA DeMartino G.N., Tanahashi N., Tanaka K.;
RT "cDNA cloning and functional analysis of p44.5 and p55, two regulatory
RT subunits of the 26S proteasome.";
RL Gene 203:241-250(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V., Potts A., Brablan J., Quadroni M.;
RL Submitted (JUL-2004) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-14; SER-79 AND SER-272.
RX PubMed=19616115; DOI=10.1016/j.biocel.2009.07.002;
RA Moreno D., Viana R., Sanz P.;
RT "Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the
RT proteasome, as a novel interaction partner of AMP-activated protein
RT kinase.";
RL Int. J. Biochem. Cell Biol. 41:2431-2439(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION, IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX,
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=22972301; DOI=10.1038/nature11468;
RA Vilchez D., Boyer L., Morantte I., Lutz M., Merkwirth C., Joyce D.,
RA Spencer B., Page L., Masliah E., Berggren W.T., Gage F.H., Dillin A.;
RT "Increased proteasome activity in human embryonic stem cells is
RT regulated by PSMD11.";
RL Nature 489:304-308(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the lid subcomplex of the 26S proteasome, a
CC multiprotein complex involved in the ATP-dependent degradation of
CC ubiquitinated proteins. In the complex, PSMD11 is required for
CC proteasome assembly. Plays a key role in increased proteasome
CC activity in embryonic stem cells (ESCs): its high expression in
CC ESCs promotes enhanced assembly of the 26S proteasome, followed by
CC higher proteasome activity.
CC -!- SUBUNIT: Component of the lid subcomplex of the 19S proteasome
CC regulatory particle complex (also named PA700 complex). The 26S
CC proteasome consists of a 20S proteasome core and two 19S
CC regulatory subunits.
CC -!- INTERACTION:
CC Q96LA8:PRMT6; NbExp=2; IntAct=EBI-357816, EBI-912440;
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm, cytosol
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00231-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00231-2; Sequence=VSP_044400;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in embryonic stem cells
CC (ESCs). Expression decreases as ESCs differentiate.
CC -!- INDUCTION: By FOXO4; expression in embryonic stem cells (ESCs) is
CC mediated by FOXO4.
CC -!- PTM: Phosphorylated by AMPK.
CC -!- SIMILARITY: Belongs to the proteasome subunit S9 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
CC -----------------------------------------------------------------------
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DR EMBL; AF001212; AAB58732.1; -; mRNA.
DR EMBL; AB003102; BAA19748.1; -; mRNA.
DR EMBL; AK290602; BAF83291.1; -; mRNA.
DR EMBL; AK223196; BAD96916.1; -; mRNA.
DR EMBL; CH471147; EAW80229.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80230.1; -; Genomic_DNA.
DR EMBL; BC000437; AAH00437.1; -; mRNA.
DR EMBL; BC004430; AAH04430.1; -; mRNA.
DR PIR; JC6524; JC6524.
DR RefSeq; NP_001257411.1; NM_001270482.1.
DR RefSeq; NP_002806.2; NM_002815.3.
DR UniGene; Hs.443379; -.
DR ProteinModelPortal; O00231; -.
DR SMR; O00231; 38-390.
DR IntAct; O00231; 48.
DR MINT; MINT-1154929; -.
DR STRING; 9606.ENSP00000261712; -.
DR PhosphoSite; O00231; -.
DR OGP; O00231; -.
DR PaxDb; O00231; -.
DR PRIDE; O00231; -.
DR Ensembl; ENST00000261712; ENSP00000261712; ENSG00000108671.
DR Ensembl; ENST00000457654; ENSP00000393185; ENSG00000108671.
DR GeneID; 5717; -.
DR KEGG; hsa:5717; -.
DR UCSC; uc002hhm.4; human.
DR CTD; 5717; -.
DR GeneCards; GC17P030771; -.
DR HGNC; HGNC:9556; PSMD11.
DR HPA; HPA042275; -.
DR MIM; 604449; gene.
DR neXtProt; NX_O00231; -.
DR PharmGKB; PA33902; -.
DR eggNOG; COG5159; -.
DR HOVERGEN; HBG053738; -.
DR InParanoid; O00231; -.
DR KO; K03036; -.
DR OMA; DKDFNTA; -.
DR OrthoDB; EOG7F24T1; -.
DR PhylomeDB; O00231; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; PSMD11; -.
DR GenomeRNAi; 5717; -.
DR NextBio; 22212; -.
DR PRO; PR:O00231; -.
DR ArrayExpress; O00231; -.
DR Bgee; O00231; -.
DR CleanEx; HS_PSMD11; -.
DR Genevestigator; O00231; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0022624; C:proteasome accessory complex; IDA:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0043248; P:proteasome assembly; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR013143; PAM.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 422 26S proteasome non-ATPase regulatory
FT subunit 11.
FT /FTId=PRO_0000173857.
FT DOMAIN 222 389 PCI.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 14 14 Phosphoserine.
FT VAR_SEQ 375 375 H -> HA (in isoform 2).
FT /FTId=VSP_044400.
FT MUTAGEN 14 14 S->A: Does not affect phosphorylation by
FT AMPK; when associated with A-79 and A-
FT 272.
FT MUTAGEN 79 79 S->A: Does not affect phosphorylation by
FT AMPK; when associated with A-14 and A-
FT 272.
FT MUTAGEN 272 272 S->A: Does not affect phosphorylation by
FT AMPK; when associated with A14- and A-79.
FT CONFLICT 113 113 C -> S (in Ref. 1; AAB58732).
SQ SEQUENCE 422 AA; 47464 MW; CE113054CBEBDB05 CRC64;
MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI LELGSLLAKT
GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME AATGQEVELC LECIEWAKSE
KRTFLRQALE ARLVSLYFDT KRYQEALHLG SQLLRELKKM DDKALLVEVQ LLESKTYHAL
SNLPKARAAL TSARTTANAI YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD
SIDSPKAITS LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA
DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI SSLIKLSKAD
VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA LETIQNMSKV VDSLYNKAKK
LT
//
MIM
604449
*RECORD*
*FIELD* NO
604449
*FIELD* TI
*604449 PROTEASOME 26S SUBUNIT, NON-ATPase, 11; PSMD11
;;PROTEASE 26S, SUBUNIT 9; S9;;
read morep44.5
*FIELD* TX
DESCRIPTION
The PSMD11 gene encodes a non-ATPase subunit of the PA700 regulatory
subcomplex of the 26S proteasome. The 26S proteasome is responsible for
the ATP-dependent degradation of a variety of cellular proteins.
Selective breakdown of these proteins is mediated by the ubiquitin
pathway. The 26S proteasome is a 2,000-kD protein complex composed of
the 20S proteasome, which is the catalytic subcomplex, and PA700, which
is the regulatory subcomplex. The approximately 700-kD PA700 complex
consists of approximately 20 heterogeneous proteins ranging from 25 to
112 kD. These subunits can be divided into 2 classes, those that are
members of the AAA (ATPases associated with various cellular activities)
family and those that are not (summary by Hoffman and Rechsteiner, 1997,
Saito et al., 1997).
CLONING
Hoffman and Rechsteiner (1997) sequenced peptides from subunit 9 of the
human 26S proteasome. Using the amino acid sequences, they cloned HeLa
cell cDNAs encoding subunit 9, also called PSMD11. The predicted
422-amino acid protein has 9 dileucine repeats, possible coiled-coil
domains, and potential myristylation and phosphorylation sites. PSMD11
is not a member of the ATPase family. Whereas the calculated molecular
mass of PSMD11 is 47,469 Da, it migrates as an approximately 46-kD
protein on SDS-polyacrylamide gels.
Saito et al. (1997) sequenced peptides from the p44.5 subunit of the
bovine PA700 complex. They identified human ESTs encoding homologous
proteins and used these ESTs to isolate hepatoblastoma HepG2 cell cDNAs
encoding human p44.5. The authors stated that the p44.5 subunit is
equivalent to subunit 9 (Hoffman and Rechsteiner, 1997), or PSMD11.
Saito et al. (1997) identified a putative S. cerevisiae homolog, which
they named NAS4, that shares 45.4% amino acid sequence identity with
PSMD11. Disruption of the NAS4 gene resulted in lethality.
GENE FUNCTION
Vilchez et al. (2012) demonstrated that human embryonic stem cells
exhibit high proteasome activity that is correlated with increased
levels of the 19S proteasome subunit PSMD11 and a corresponding
increased assembly of the 26S/30S proteasome. Ectopic expression of
PSMD11 is sufficient to increase proteasome assembly and activity. FOXO4
(300033), an insulin/insulin-like growth factor-I (IGF1;
147440)-responsive transcription factor associated with long lifespan in
invertebrates, regulates proteasome activity by modulating the
expression of PSMD11 in human embryonic stem cells. Proteasome
inhibition in human embryonic stem cells affects the expression of
pluripotency markers and the levels of specific markers of the distinct
germ layers. Vilchez et al. (2012) concluded that their results
suggested a new regulation of proteostasis in human embryonic stem cells
that links longevity and stress resistance in invertebrates to human
embryonic stem cell function and identity.
*FIELD* RF
1. Hoffman, L.; Rechsteiner, M.: Molecular cloning and expression
of subunit 9 of the 26S proteasome. FEBS Lett. 404: 179-184, 1997.
2. Saito, A.; Watanabe, T. K.; Shimada, Y.; Fujiwara, T.; Slaughter,
C. A.; DeMartino, G. N.; Tanahashi, N.; Tanaka, K.: cDNA cloning
and functional analysis of p44.5 and p55, two regulatory subunits
of the 26S proteasome. Gene 203: 241-250, 1997.
3. 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.: Increased proteasome activity in human embryonic
stem cells is regulated by PSMD11. Nature 489: 304-308, 2012.
*FIELD* CN
Ada Hamosh - updated: 10/9/2012
*FIELD* CD
Patti M. Sherman: 1/20/2000
*FIELD* ED
alopez: 10/24/2012
terry: 10/9/2012
mgross: 1/21/2000
psherman: 1/20/2000
*RECORD*
*FIELD* NO
604449
*FIELD* TI
*604449 PROTEASOME 26S SUBUNIT, NON-ATPase, 11; PSMD11
;;PROTEASE 26S, SUBUNIT 9; S9;;
read morep44.5
*FIELD* TX
DESCRIPTION
The PSMD11 gene encodes a non-ATPase subunit of the PA700 regulatory
subcomplex of the 26S proteasome. The 26S proteasome is responsible for
the ATP-dependent degradation of a variety of cellular proteins.
Selective breakdown of these proteins is mediated by the ubiquitin
pathway. The 26S proteasome is a 2,000-kD protein complex composed of
the 20S proteasome, which is the catalytic subcomplex, and PA700, which
is the regulatory subcomplex. The approximately 700-kD PA700 complex
consists of approximately 20 heterogeneous proteins ranging from 25 to
112 kD. These subunits can be divided into 2 classes, those that are
members of the AAA (ATPases associated with various cellular activities)
family and those that are not (summary by Hoffman and Rechsteiner, 1997,
Saito et al., 1997).
CLONING
Hoffman and Rechsteiner (1997) sequenced peptides from subunit 9 of the
human 26S proteasome. Using the amino acid sequences, they cloned HeLa
cell cDNAs encoding subunit 9, also called PSMD11. The predicted
422-amino acid protein has 9 dileucine repeats, possible coiled-coil
domains, and potential myristylation and phosphorylation sites. PSMD11
is not a member of the ATPase family. Whereas the calculated molecular
mass of PSMD11 is 47,469 Da, it migrates as an approximately 46-kD
protein on SDS-polyacrylamide gels.
Saito et al. (1997) sequenced peptides from the p44.5 subunit of the
bovine PA700 complex. They identified human ESTs encoding homologous
proteins and used these ESTs to isolate hepatoblastoma HepG2 cell cDNAs
encoding human p44.5. The authors stated that the p44.5 subunit is
equivalent to subunit 9 (Hoffman and Rechsteiner, 1997), or PSMD11.
Saito et al. (1997) identified a putative S. cerevisiae homolog, which
they named NAS4, that shares 45.4% amino acid sequence identity with
PSMD11. Disruption of the NAS4 gene resulted in lethality.
GENE FUNCTION
Vilchez et al. (2012) demonstrated that human embryonic stem cells
exhibit high proteasome activity that is correlated with increased
levels of the 19S proteasome subunit PSMD11 and a corresponding
increased assembly of the 26S/30S proteasome. Ectopic expression of
PSMD11 is sufficient to increase proteasome assembly and activity. FOXO4
(300033), an insulin/insulin-like growth factor-I (IGF1;
147440)-responsive transcription factor associated with long lifespan in
invertebrates, regulates proteasome activity by modulating the
expression of PSMD11 in human embryonic stem cells. Proteasome
inhibition in human embryonic stem cells affects the expression of
pluripotency markers and the levels of specific markers of the distinct
germ layers. Vilchez et al. (2012) concluded that their results
suggested a new regulation of proteostasis in human embryonic stem cells
that links longevity and stress resistance in invertebrates to human
embryonic stem cell function and identity.
*FIELD* RF
1. Hoffman, L.; Rechsteiner, M.: Molecular cloning and expression
of subunit 9 of the 26S proteasome. FEBS Lett. 404: 179-184, 1997.
2. Saito, A.; Watanabe, T. K.; Shimada, Y.; Fujiwara, T.; Slaughter,
C. A.; DeMartino, G. N.; Tanahashi, N.; Tanaka, K.: cDNA cloning
and functional analysis of p44.5 and p55, two regulatory subunits
of the 26S proteasome. Gene 203: 241-250, 1997.
3. 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.: Increased proteasome activity in human embryonic
stem cells is regulated by PSMD11. Nature 489: 304-308, 2012.
*FIELD* CN
Ada Hamosh - updated: 10/9/2012
*FIELD* CD
Patti M. Sherman: 1/20/2000
*FIELD* ED
alopez: 10/24/2012
terry: 10/9/2012
mgross: 1/21/2000
psherman: 1/20/2000