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Database: UniProt
Entry: O00231
LinkDB: O00231
Original site: O00231 
ID   PSD11_HUMAN             Reviewed;         422 AA.
AC   O00231; A8K3I7; E1P663; O00495; Q53FT5;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-JUN-2021, entry version 196.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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 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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., 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 project:
RT   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., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   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 IDENTIFICATION BY MASS
RP   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   FUNCTION.
RX   PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
RA   Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N., Yoshimura T.,
RA   Tanaka K., Ichihara A.;
RT   "Demonstration that a human 26S proteolytic complex consists of a
RT   proteasome and multiple associated protein components and hydrolyzes ATP
RT   and ubiquitin-ligated proteins by closely linked mechanisms.";
RL   Eur. J. Biochem. 206:567-578(1992).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 26S
RT   proteasome complex.";
RL   Biochemistry 46:3553-3565(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
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   [14]
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., Buerckstuemmer T.,
RA   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   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [16]
RP   FUNCTION, IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX, TISSUE
RP   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 regulated
RT   by PSMD11.";
RL   Nature 489:304-308(2012).
RN   [17]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-23, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [20]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-274, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [21]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-274, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [22]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
RX   PubMed=27428775; DOI=10.1038/nsmb.3273;
RA   Huang X., Luan B., Wu J., Shi Y.;
RT   "An atomic structure of the human 26S proteasome.";
RL   Nat. Struct. Mol. Biol. 23:778-785(2016).
RN   [23]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), AND SUBUNIT.
RX   PubMed=27342858; DOI=10.1073/pnas.1608050113;
RA   Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
RA   Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
RT   "Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
CC   -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       This complex plays a key role in the maintenance of protein homeostasis
CC       by removing misfolded or damaged proteins, which could impair cellular
CC       functions, and by removing proteins whose functions are no longer
CC       required. Therefore, the proteasome participates in numerous cellular
CC       processes, including cell cycle progression, apoptosis, or DNA damage
CC       repair. In the complex, PSMD11 is required for proteasome assembly.
CC       Plays a key role in increased proteasome activity in embryonic stem
CC       cells (ESCs): its high expression in ESCs promotes enhanced assembly of
CC       the 26S proteasome, followed by higher proteasome activity.
CC       {ECO:0000269|PubMed:1317798, ECO:0000269|PubMed:22972301}.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC       The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC       regulatory subunits (RP). The regulatory particle is made of a lid
CC       composed of 9 subunits including PSMD11, a base containing 6 ATPases
CC       and few additional components. {ECO:0000269|PubMed:22972301,
CC       ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
CC   -!- INTERACTION:
CC       O00231; P61201: COPS2; NbExp=3; IntAct=EBI-357816, EBI-1050386;
CC       O00231; O43741: PRKAB2; NbExp=3; IntAct=EBI-357816, EBI-1053424;
CC       O00231; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-357816, EBI-912440;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
CC       {ECO:0000250}.
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   -!- TISSUE SPECIFICITY: Highly expressed in embryonic stem cells (ESCs).
CC       Expression decreases as ESCs differentiate.
CC       {ECO:0000269|PubMed:22972301}.
CC   -!- INDUCTION: By FOXO4; expression in embryonic stem cells (ESCs) is
CC       mediated by FOXO4. {ECO:0000269|PubMed:22972301}.
CC   -!- PTM: Phosphorylated by AMPK. {ECO:0000269|PubMed:19616115}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S9 family. {ECO:0000305}.
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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   CCDS; CCDS11272.1; -. [O00231-1]
DR   PIR; JC6524; JC6524.
DR   RefSeq; NP_001257411.1; NM_001270482.1. [O00231-1]
DR   RefSeq; NP_002806.2; NM_002815.3. [O00231-1]
DR   PDB; 5GJQ; EM; 4.50 A; Q=1-422.
DR   PDB; 5GJR; EM; 3.50 A; 4/Q=1-422.
DR   PDB; 5L4K; EM; 4.50 A; Q=1-422.
DR   PDB; 5LN3; EM; 6.80 A; Q=1-422.
DR   PDB; 5M32; EM; 3.80 A; l=1-422.
DR   PDB; 5T0C; EM; 3.80 A; AX/BX=1-422.
DR   PDB; 5T0G; EM; 4.40 A; X=1-422.
DR   PDB; 5T0H; EM; 6.80 A; X=1-422.
DR   PDB; 5T0I; EM; 8.00 A; X=1-422.
DR   PDB; 5T0J; EM; 8.00 A; X=1-422.
DR   PDB; 5VFP; EM; 4.20 A; X=43-422.
DR   PDB; 5VFQ; EM; 4.20 A; X=43-422.
DR   PDB; 5VFR; EM; 4.90 A; X=43-422.
DR   PDB; 5VFS; EM; 3.60 A; X=43-422.
DR   PDB; 5VFT; EM; 7.00 A; X=43-422.
DR   PDB; 5VFU; EM; 5.80 A; X=43-422.
DR   PDB; 5VGZ; EM; 3.70 A; X=38-422.
DR   PDB; 5VHF; EM; 5.70 A; X=38-422.
DR   PDB; 5VHH; EM; 6.10 A; X=38-422.
DR   PDB; 5VHI; EM; 6.80 A; X=38-422.
DR   PDB; 5VHS; EM; 8.80 A; X=38-422.
DR   PDB; 6MSB; EM; 3.00 A; X=1-422.
DR   PDB; 6MSD; EM; 3.20 A; X=1-422.
DR   PDB; 6MSE; EM; 3.30 A; X=1-422.
DR   PDB; 6MSG; EM; 3.50 A; X=1-422.
DR   PDB; 6MSH; EM; 3.60 A; X=1-422.
DR   PDB; 6MSJ; EM; 3.30 A; X=1-422.
DR   PDB; 6MSK; EM; 3.20 A; X=1-422.
DR   PDB; 6WJD; EM; 4.80 A; X=1-422.
DR   PDB; 6WJN; EM; 5.70 A; X=43-422.
DR   PDBsum; 5GJQ; -.
DR   PDBsum; 5GJR; -.
DR   PDBsum; 5L4K; -.
DR   PDBsum; 5LN3; -.
DR   PDBsum; 5M32; -.
DR   PDBsum; 5T0C; -.
DR   PDBsum; 5T0G; -.
DR   PDBsum; 5T0H; -.
DR   PDBsum; 5T0I; -.
DR   PDBsum; 5T0J; -.
DR   PDBsum; 5VFP; -.
DR   PDBsum; 5VFQ; -.
DR   PDBsum; 5VFR; -.
DR   PDBsum; 5VFS; -.
DR   PDBsum; 5VFT; -.
DR   PDBsum; 5VFU; -.
DR   PDBsum; 5VGZ; -.
DR   PDBsum; 5VHF; -.
DR   PDBsum; 5VHH; -.
DR   PDBsum; 5VHI; -.
DR   PDBsum; 5VHS; -.
DR   PDBsum; 6MSB; -.
DR   PDBsum; 6MSD; -.
DR   PDBsum; 6MSE; -.
DR   PDBsum; 6MSG; -.
DR   PDBsum; 6MSH; -.
DR   PDBsum; 6MSJ; -.
DR   PDBsum; 6MSK; -.
DR   PDBsum; 6WJD; -.
DR   PDBsum; 6WJN; -.
DR   SMR; O00231; -.
DR   BioGRID; 111689; 212.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; O00231; -.
DR   IntAct; O00231; 110.
DR   MINT; O00231; -.
DR   STRING; 9606.ENSP00000261712; -.
DR   ChEMBL; CHEMBL2364701; -.
DR   iPTMnet; O00231; -.
DR   MetOSite; O00231; -.
DR   PhosphoSitePlus; O00231; -.
DR   SwissPalm; O00231; -.
DR   BioMuta; PSMD11; -.
DR   OGP; O00231; -.
DR   EPD; O00231; -.
DR   jPOST; O00231; -.
DR   MassIVE; O00231; -.
DR   MaxQB; O00231; -.
DR   PaxDb; O00231; -.
DR   PeptideAtlas; O00231; -.
DR   PRIDE; O00231; -.
DR   ProteomicsDB; 47796; -. [O00231-1]
DR   Antibodypedia; 15394; 312 antibodies.
DR   DNASU; 5717; -.
DR   Ensembl; ENST00000261712; ENSP00000261712; ENSG00000108671. [O00231-1]
DR   Ensembl; ENST00000457654; ENSP00000393185; ENSG00000108671. [O00231-1]
DR   Ensembl; ENST00000649012; ENSP00000497128; ENSG00000108671. [O00231-1]
DR   GeneID; 5717; -.
DR   KEGG; hsa:5717; -.
DR   UCSC; uc002hhm.5; human. [O00231-1]
DR   CTD; 5717; -.
DR   DisGeNET; 5717; -.
DR   GeneCards; PSMD11; -.
DR   HGNC; HGNC:9556; PSMD11.
DR   HPA; ENSG00000108671; Low tissue specificity.
DR   MIM; 604449; gene.
DR   neXtProt; NX_O00231; -.
DR   OpenTargets; ENSG00000108671; -.
DR   PharmGKB; PA33902; -.
DR   VEuPathDB; HostDB:ENSG00000108671.9; -.
DR   eggNOG; KOG1463; Eukaryota.
DR   GeneTree; ENSGT00530000063301; -.
DR   HOGENOM; CLU_029573_2_1_1; -.
DR   InParanoid; O00231; -.
DR   OMA; DKVFYGV; -.
DR   OrthoDB; 1052430at2759; -.
DR   PhylomeDB; O00231; -.
DR   TreeFam; TF106230; -.
DR   PathwayCommons; O00231; -.
DR   Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR   Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR   Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR   Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-HSA-202424; Downstream TCR signaling.
DR   Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR   Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-HSA-4641257; Degradation of AXIN.
DR   Reactome; R-HSA-4641258; Degradation of DVL.
DR   Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR   Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR   Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR   Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR   Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-HSA-5689603; UCH proteinases.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
DR   Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR   Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-HSA-69481; G2/M Checkpoints.
DR   Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR   Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR   Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; O00231; -.
DR   BioGRID-ORCS; 5717; 732 hits in 966 CRISPR screens.
DR   ChiTaRS; PSMD11; human.
DR   GeneWiki; PSMD11; -.
DR   GenomeRNAi; 5717; -.
DR   Pharos; O00231; Tbio.
DR   PRO; PR:O00231; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; O00231; protein.
DR   Bgee; ENSG00000108671; Expressed in testis and 244 other tissues.
DR   ExpressionAtlas; O00231; baseline and differential.
DR   Genevisible; O00231; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0022624; C:proteasome accessory complex; IDA:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent 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:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
DR   GO; GO:0043248; P:proteasome assembly; IMP:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
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:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR035295; PSMD11.
DR   InterPro; IPR040780; Rpn6_C_helix.
DR   InterPro; IPR040773; Rpn6_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10678:SF6; PTHR10678:SF6; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF18503; RPN6_C_helix; 1.
DR   Pfam; PF18055; RPN6_N; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Proteasome; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8,
FT                   ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..422
FT                   /note="26S proteasome non-ATPase regulatory subunit 11"
FT                   /id="PRO_0000173857"
FT   DOMAIN          224..392
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17323924,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        274
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         375
FT                   /note="H -> HA (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_044400"
FT   MUTAGEN         14
FT                   /note="S->A: Does not affect phosphorylation by AMPK; when
FT                   associated with A-79 and A-272."
FT                   /evidence="ECO:0000269|PubMed:19616115"
FT   MUTAGEN         79
FT                   /note="S->A: Does not affect phosphorylation by AMPK; when
FT                   associated with A-14 and A-272."
FT                   /evidence="ECO:0000269|PubMed:19616115"
FT   MUTAGEN         272
FT                   /note="S->A: Does not affect phosphorylation by AMPK; when
FT                   associated with A14- and A-79."
FT                   /evidence="ECO:0000269|PubMed:19616115"
FT   CONFLICT        113
FT                   /note="C -> S (in Ref. 1; AAB58732)"
FT                   /evidence="ECO:0000305"
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
//
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