PSDE_HUMAN
ID PSDE_HUMAN Reviewed; 310 AA.
AC O00487; B3KNW2; O00176;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 14;
DE EC=3.4.19.-;
DE AltName: Full=26S proteasome regulatory subunit RPN11;
DE AltName: Full=26S proteasome-associated PAD1 homolog 1;
GN Name=PSMD14; Synonyms=POH1;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=9374539; DOI=10.1074/jbc.272.48.30470;
RA Spataro V., Toda T., Craig R., Seeger M., Dubiel W., Harris A.L.,
RA Norbury C.;
RT "Resistance to diverse drugs and ultraviolet light conferred by
RT overexpression of a novel human 26 S proteasome subunit.";
RL J. Biol. Chem. 272:30470-30475(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP PROTEIN SEQUENCE OF 199-208, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [9]
RP PROBABLE FUNCTION, AND IDENTIFICATION IN THE PROTEASOME.
RX PubMed=19214193; DOI=10.1038/emboj.2009.27;
RA Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M.,
RA Cohen R.E.;
RT "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated
RT Brcc36 and proteasomal Poh1.";
RL EMBO J. 28:621-631(2009).
RN [10]
RP INTERACTION WITH TXNL1.
RX PubMed=19349277; DOI=10.1074/jbc.m900016200;
RA Andersen K.M., Madsen L., Prag S., Johnsen A.H., Semple C.A., Hendil K.B.,
RA Hartmann-Petersen R.;
RT "Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S
RT proteasome.";
RL J. Biol. Chem. 284:15246-15254(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
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 [13]
RP FUNCTION, IDENTIFICATION IN THE PROTEASOME, AND MUTAGENESIS OF
RP 113-HIS--HIS-115.
RX PubMed=22909820; DOI=10.1038/emboj.2012.232;
RA Butler L.R., Densham R.M., Jia J., Garvin A.J., Stone H.R., Shah V.,
RA Weekes D., Festy F., Beesley J., Morris J.R.;
RT "The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand
RT DNA break response.";
RL EMBO J. 31:3918-3934(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, 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 [16]
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 [17]
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. The PSMD14 subunit is a metalloprotease that specifically
CC cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays
CC a role in response to double-strand breaks (DSBs): acts as a regulator
CC of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked
CC polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin
CC and restricting TP53BP1 accumulation. Also involved in homologous
CC recombination repair by promoting RAD51 loading.
CC {ECO:0000269|PubMed:1317798, ECO:0000269|PubMed:22909820,
CC ECO:0000269|PubMed:9374539}.
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 PSMD4, a base containing 6 ATPases and
CC few additional components (PubMed:27428775, PubMed:27342858). Within
CC the complex, PSMD4 interacts with subunit PSMD7 through their
CC respective MPN domain. Interacts with TXNL1 (PubMed:19349277).
CC {ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:19349277,
CC ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
CC -!- INTERACTION:
CC O00487; Q9C005: DPY30; NbExp=6; IntAct=EBI-722193, EBI-744973;
CC O00487; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-722193, EBI-10175124;
CC O00487; P42858: HTT; NbExp=7; IntAct=EBI-722193, EBI-466029;
CC O00487; P50222: MEOX2; NbExp=3; IntAct=EBI-722193, EBI-748397;
CC O00487; P51665: PSMD7; NbExp=14; IntAct=EBI-722193, EBI-357659;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart and
CC skeletal muscle. {ECO:0000269|PubMed:9374539}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. PSMD14 subfamily.
CC {ECO:0000305}.
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DR EMBL; U86782; AAC51866.1; -; mRNA.
DR EMBL; AK055128; BAG51474.1; -; mRNA.
DR EMBL; CH471058; EAX11370.1; -; Genomic_DNA.
DR EMBL; BC066336; AAH66336.1; -; mRNA.
DR CCDS; CCDS46437.1; -.
DR RefSeq; NP_005796.1; NM_005805.5.
DR PDB; 5GJQ; EM; 4.50 A; V=1-310.
DR PDB; 5GJR; EM; 3.50 A; 9/V=1-310.
DR PDB; 5L4K; EM; 4.50 A; V=1-310.
DR PDB; 5LN3; EM; 6.80 A; V=1-310.
DR PDB; 5M32; EM; 3.80 A; q=1-310.
DR PDB; 5T0C; EM; 3.80 A; Ac/Bc=1-310.
DR PDB; 5T0G; EM; 4.40 A; c=2-310.
DR PDB; 5T0H; EM; 6.80 A; c=2-310.
DR PDB; 5T0I; EM; 8.00 A; c=2-310.
DR PDB; 5T0J; EM; 8.00 A; c=2-310.
DR PDB; 5VFP; EM; 4.20 A; c=24-310.
DR PDB; 5VFQ; EM; 4.20 A; c=24-310.
DR PDB; 5VFR; EM; 4.90 A; c=24-310.
DR PDB; 5VFS; EM; 3.60 A; c=2-310.
DR PDB; 5VFT; EM; 7.00 A; c=24-310.
DR PDB; 5VFU; EM; 5.80 A; c=24-310.
DR PDB; 5VGZ; EM; 3.70 A; c=24-310.
DR PDB; 5VHF; EM; 5.70 A; c=24-310.
DR PDB; 5VHH; EM; 6.10 A; c=24-310.
DR PDB; 5VHI; EM; 6.80 A; c=24-310.
DR PDB; 5VHS; EM; 8.80 A; c=24-310.
DR PDB; 6MSB; EM; 3.00 A; c=2-310.
DR PDB; 6MSD; EM; 3.20 A; c=2-310.
DR PDB; 6MSE; EM; 3.30 A; c=2-310.
DR PDB; 6MSG; EM; 3.50 A; c=2-310.
DR PDB; 6MSH; EM; 3.60 A; c=2-310.
DR PDB; 6MSJ; EM; 3.30 A; c=2-310.
DR PDB; 6MSK; EM; 3.20 A; c=2-310.
DR PDB; 6WJD; EM; 4.80 A; c=2-310.
DR PDB; 6WJN; EM; 5.70 A; c=24-310.
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 AlphaFoldDB; O00487; -.
DR SMR; O00487; -.
DR BioGRID; 115508; 445.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; O00487; -.
DR IntAct; O00487; 100.
DR MINT; O00487; -.
DR STRING; 9606.ENSP00000386541; -.
DR BindingDB; O00487; -.
DR ChEMBL; CHEMBL2007629; -.
DR MEROPS; M67.A10; -.
DR GlyGen; O00487; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; O00487; -.
DR MetOSite; O00487; -.
DR PhosphoSitePlus; O00487; -.
DR SwissPalm; O00487; -.
DR BioMuta; PSMD14; -.
DR OGP; O00487; -.
DR REPRODUCTION-2DPAGE; IPI00024821; -.
DR EPD; O00487; -.
DR jPOST; O00487; -.
DR MassIVE; O00487; -.
DR MaxQB; O00487; -.
DR PaxDb; O00487; -.
DR PeptideAtlas; O00487; -.
DR PRIDE; O00487; -.
DR ProteomicsDB; 47932; -.
DR TopDownProteomics; O00487; -.
DR Antibodypedia; 1047; 259 antibodies from 34 providers.
DR DNASU; 10213; -.
DR Ensembl; ENST00000409682.8; ENSP00000386541.3; ENSG00000115233.12.
DR GeneID; 10213; -.
DR KEGG; hsa:10213; -.
DR MANE-Select; ENST00000409682.8; ENSP00000386541.3; NM_005805.6; NP_005796.1.
DR UCSC; uc002ubu.4; human.
DR CTD; 10213; -.
DR DisGeNET; 10213; -.
DR GeneCards; PSMD14; -.
DR HGNC; HGNC:16889; PSMD14.
DR HPA; ENSG00000115233; Low tissue specificity.
DR MIM; 607173; gene.
DR neXtProt; NX_O00487; -.
DR OpenTargets; ENSG00000115233; -.
DR PharmGKB; PA134957776; -.
DR VEuPathDB; HostDB:ENSG00000115233; -.
DR eggNOG; KOG1555; Eukaryota.
DR GeneTree; ENSGT00730000111116; -.
DR HOGENOM; CLU_052991_0_1_1; -.
DR InParanoid; O00487; -.
DR OMA; VFQTRMM; -.
DR OrthoDB; 1031881at2759; -.
DR PhylomeDB; O00487; -.
DR TreeFam; TF105748; -.
DR PathwayCommons; O00487; -.
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-5689901; Metalloprotease DUBs.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative 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-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O00487; -.
DR SIGNOR; O00487; -.
DR BioGRID-ORCS; 10213; 789 hits in 1085 CRISPR screens.
DR ChiTaRS; PSMD14; human.
DR GeneWiki; PSMD14; -.
DR GenomeRNAi; 10213; -.
DR Pharos; O00487; Tchem.
DR PRO; PR:O00487; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O00487; protein.
DR Bgee; ENSG00000115233; Expressed in middle temporal gyrus and 211 other tissues.
DR ExpressionAtlas; O00487; baseline and differential.
DR Genevisible; O00487; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031597; C:cytosolic proteasome complex; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IMP:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0061133; F:endopeptidase activator activity; IMP:UniProtKB.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IMP:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IMP:UniProtKB.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:UniProtKB.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR035299; PSMD14.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR PANTHER; PTHR10410:SF22; PTHR10410:SF22; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair; Hydrolase;
KW Metal-binding; Metalloprotease; Phosphoprotein; Protease; Proteasome;
KW Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..310
FT /note="26S proteasome non-ATPase regulatory subunit 14"
FT /id="PRO_0000213952"
FT DOMAIN 31..166
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 113..126
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17693683,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17323924"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 113..115
FT /note="HSH->ASA: Abolishes ubiquitin thioesterase activity,
FT leading to prevent maintenance of JMJD2A/KDM4A on
FT chromatin."
FT /evidence="ECO:0000269|PubMed:22909820"
SQ SEQUENCE 310 AA; 34577 MW; 18ACE876C7682039 CRC64;
MDRLLRLGGG MPGLGQGPPT DAPAVDTAEQ VYISSLALLK MLKHGRAGVP MEVMGLMLGE
FVDDYTVRVI DVFAMPQSGT GVSVEAVDPV FQAKMLDMLK QTGRPEMVVG WYHSHPGFGC
WLSGVDINTQ QSFEALSERA VAVVVDPIQS VKGKVVIDAF RLINANMMVL GHEPRQTTSN
LGHLNKPSIQ ALIHGLNRHY YSITINYRKN ELEQKMLLNL HKKSWMEGLT LQDYSEHCKH
NESVVKEMLE LAKNYNKAVE EEDKMTPEQL AIKNVGKQDP KRHLEEHVDV LMTSNIVQCL
AAMLDTVVFK
