PSMD3_HUMAN
ID PSMD3_HUMAN Reviewed; 534 AA.
AC O43242; B3KMW9; B4DT72; Q96EI2; Q9BQA4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 3;
DE AltName: Full=26S proteasome regulatory subunit RPN3;
DE AltName: Full=26S proteasome regulatory subunit S3;
DE AltName: Full=Proteasome subunit p58;
GN Name=PSMD3;
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).
RC TISSUE=Hepatoblastoma;
RX PubMed=9017604; DOI=10.1091/mbc.8.1.171;
RA Kominami K., Okura N., Kawamura M., Demartino G.N., Slaughter C.A.,
RA Shimbara N., Chung C.H., Fujimuro M., Yokosawa H., Shimizu Y.,
RA Tanahashi N., Tanaka K., Toh-e A.;
RT "Yeast counterparts of subunits S5a and p58 (S3) of the human 26S
RT proteasome are encoded by two multicopy suppressors of nin1-1.";
RL Mol. Biol. Cell 8:171-187(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pericardium;
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 GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, Lung, Pancreas, and Skin;
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 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 [8]
RP INTERACTION WITH UBQLN1.
RX PubMed=15147878; DOI=10.1016/j.febslet.2004.04.031;
RA Ko H.S., Uehara T., Tsuruma K., Nomura Y.;
RT "Ubiquilin interacts with ubiquitylated proteins and proteasome through its
RT ubiquitin-associated and ubiquitin-like domains.";
RL FEBS Lett. 566:110-114(2004).
RN [9]
RP IDENTIFICATION BY 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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418 AND SER-430, 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 [13]
RP IDENTIFICATION BY 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-38, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [15]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-38, 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 [17]
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 [18]
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. {ECO:0000269|PubMed:1317798}.
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 PSMD3, a base containing 6 ATPases and
CC few additional components (PubMed:27428775, PubMed:27342858). Interacts
CC with UBQLN1 (via ubiquitin-like domain) (PubMed:15147878). Interacts
CC with ERCC6 (PubMed:26030138). {ECO:0000269|PubMed:15147878,
CC ECO:0000269|PubMed:26030138, ECO:0000269|PubMed:27342858,
CC ECO:0000269|PubMed:27428775}.
CC -!- INTERACTION:
CC O43242; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-357622, EBI-744115;
CC O43242; P42858: HTT; NbExp=3; IntAct=EBI-357622, EBI-466029;
CC O43242; P25963: NFKBIA; NbExp=3; IntAct=EBI-357622, EBI-307386;
CC O43242; P16885: PLCG2; NbExp=2; IntAct=EBI-357622, EBI-617403;
CC O43242; O43395: PRPF3; NbExp=3; IntAct=EBI-357622, EBI-744322;
CC O43242; P60900: PSMA6; NbExp=3; IntAct=EBI-357622, EBI-357793;
CC O43242; P60896: SEM1; NbExp=3; IntAct=EBI-357622, EBI-79819;
CC O43242; O43298: ZBTB43; NbExp=7; IntAct=EBI-357622, EBI-740718;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43242-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43242-2; Sequence=VSP_056362, VSP_056363;
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family. {ECO:0000305}.
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DR EMBL; D67025; BAA23651.1; -; mRNA.
DR EMBL; BT007217; AAP35881.1; -; mRNA.
DR EMBL; AK022896; BAG51131.1; -; mRNA.
DR EMBL; AK300081; BAG61884.1; -; mRNA.
DR EMBL; AC090844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60625.1; -; Genomic_DNA.
DR EMBL; BC000074; AAH00074.1; -; mRNA.
DR EMBL; BC004859; AAH04859.1; -; mRNA.
DR EMBL; BC012302; AAH12302.1; -; mRNA.
DR EMBL; BC020518; AAH20518.1; -; mRNA.
DR EMBL; BC025686; AAH25686.1; -; mRNA.
DR CCDS; CCDS11356.1; -. [O43242-1]
DR RefSeq; NP_002800.2; NM_002809.3. [O43242-1]
DR PDB; 5GJQ; EM; 4.50 A; S=1-534.
DR PDB; 5GJR; EM; 3.50 A; 6/S=1-525.
DR PDB; 5L4K; EM; 4.50 A; S=1-534.
DR PDB; 5LN3; EM; 6.80 A; S=1-534.
DR PDB; 5M32; EM; 3.80 A; j=1-534.
DR PDB; 5T0C; EM; 3.80 A; AV/BV=2-534.
DR PDB; 5T0G; EM; 4.40 A; V=2-534.
DR PDB; 5T0H; EM; 6.80 A; V=2-534.
DR PDB; 5T0I; EM; 8.00 A; V=2-534.
DR PDB; 5T0J; EM; 8.00 A; V=2-534.
DR PDB; 5VFP; EM; 4.20 A; V=18-497.
DR PDB; 5VFQ; EM; 4.20 A; V=18-497.
DR PDB; 5VFR; EM; 4.90 A; V=18-497.
DR PDB; 5VFS; EM; 3.60 A; V=18-497.
DR PDB; 5VFT; EM; 7.00 A; V=18-497.
DR PDB; 5VFU; EM; 5.80 A; V=18-497.
DR PDB; 5VGZ; EM; 3.70 A; V=18-505.
DR PDB; 5VHF; EM; 5.70 A; V=323-505.
DR PDB; 5VHH; EM; 6.10 A; V=18-505.
DR PDB; 5VHI; EM; 6.80 A; V=18-505.
DR PDB; 5VHS; EM; 8.80 A; V=18-505.
DR PDB; 6MSB; EM; 3.00 A; V=1-534.
DR PDB; 6MSD; EM; 3.20 A; V=1-534.
DR PDB; 6MSE; EM; 3.30 A; D=314-523.
DR PDB; 6MSG; EM; 3.50 A; V=2-534.
DR PDB; 6MSH; EM; 3.60 A; V=2-534.
DR PDB; 6MSJ; EM; 3.30 A; V=2-534.
DR PDB; 6MSK; EM; 3.20 A; V=2-534.
DR PDB; 6WJD; EM; 4.80 A; V=1-534.
DR PDB; 6WJN; EM; 5.70 A; V=18-497.
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; O43242; -.
DR SMR; O43242; -.
DR BioGRID; 111682; 249.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; O43242; -.
DR DIP; DIP-27571N; -.
DR IntAct; O43242; 85.
DR MINT; O43242; -.
DR STRING; 9606.ENSP00000264639; -.
DR ChEMBL; CHEMBL2364701; -.
DR GlyGen; O43242; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43242; -.
DR MetOSite; O43242; -.
DR PhosphoSitePlus; O43242; -.
DR SwissPalm; O43242; -.
DR BioMuta; PSMD3; -.
DR CPTAC; CPTAC-152; -.
DR CPTAC; CPTAC-153; -.
DR EPD; O43242; -.
DR jPOST; O43242; -.
DR MassIVE; O43242; -.
DR MaxQB; O43242; -.
DR PaxDb; O43242; -.
DR PeptideAtlas; O43242; -.
DR PRIDE; O43242; -.
DR ProteomicsDB; 48822; -. [O43242-1]
DR ProteomicsDB; 5082; -.
DR Antibodypedia; 28451; 307 antibodies from 29 providers.
DR DNASU; 5709; -.
DR Ensembl; ENST00000264639.9; ENSP00000264639.4; ENSG00000108344.15. [O43242-1]
DR GeneID; 5709; -.
DR KEGG; hsa:5709; -.
DR MANE-Select; ENST00000264639.9; ENSP00000264639.4; NM_002809.4; NP_002800.2.
DR UCSC; uc002htn.3; human. [O43242-1]
DR CTD; 5709; -.
DR DisGeNET; 5709; -.
DR GeneCards; PSMD3; -.
DR HGNC; HGNC:9560; PSMD3.
DR HPA; ENSG00000108344; Tissue enhanced (skeletal).
DR MIM; 617676; gene.
DR neXtProt; NX_O43242; -.
DR OpenTargets; ENSG00000108344; -.
DR PharmGKB; PA38123; -.
DR VEuPathDB; HostDB:ENSG00000108344; -.
DR eggNOG; KOG2581; Eukaryota.
DR GeneTree; ENSGT00940000153653; -.
DR HOGENOM; CLU_019858_1_2_1; -.
DR InParanoid; O43242; -.
DR OMA; ENFGPQF; -.
DR OrthoDB; 836599at2759; -.
DR PhylomeDB; O43242; -.
DR TreeFam; TF106110; -.
DR PathwayCommons; O43242; -.
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-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; O43242; -.
DR SIGNOR; O43242; -.
DR BioGRID-ORCS; 5709; 791 hits in 1078 CRISPR screens.
DR ChiTaRS; PSMD3; human.
DR GeneWiki; PSMD3; -.
DR GenomeRNAi; 5709; -.
DR Pharos; O43242; Tbio.
DR PRO; PR:O43242; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O43242; protein.
DR Bgee; ENSG00000108344; Expressed in gastrocnemius and 202 other tissues.
DR ExpressionAtlas; O43242; baseline and differential.
DR Genevisible; O43242; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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; ISS: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:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR013586; 26S_Psome_reg_C.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035267; PSMD3.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10758:SF2; PTHR10758:SF2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF08375; Rpn3_C; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Phosphoprotein;
KW Proteasome; Reference proteome; Ubl conjugation.
FT CHAIN 1..534
FT /note="26S proteasome non-ATPase regulatory subunit 3"
FT /id="PRO_0000173816"
FT DOMAIN 286..465
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056362"
FT VAR_SEQ 493..534
FT /note="AMRFPPKSYNKDLESAEERREREQQDLEFAKEMAEDDDDSFP -> GW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056363"
FT CONFLICT 60
FT /note="A -> V (in Ref. 1; BAA23651)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..158
FT /note="TP -> NT (in Ref. 6; AAH12302)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="E -> V (in Ref. 6; AAH12302)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 60978 MW; 3B3FB5593542C078 CRC64;
MKQEGSARRR GADKAKPPPG GGEQEPPPPP APQDVEMKEE AATGGGSTGE ADGKTAAAAA
EHSQRELDTV TLEDIKEHVK QLEKAVSGKE PRFVLRALRM LPSTSRRLNH YVLYKAVQGF
FTSNNATRDF LLPFLEEPMD TEADLQFRPR TGKAASTPLL PEVEAYLQLL VVIFMMNSKR
YKEAQKISDD LMQKISTQNR RALDLVAAKC YYYHARVYEF LDKLDVVRSF LHARLRTATL
RHDADGQATL LNLLLRNYLH YSLYDQAEKL VSKSVFPEQA NNNEWARYLY YTGRIKAIQL
EYSEARRTMT NALRKAPQHT AVGFKQTVHK LLIVVELLLG EIPDRLQFRQ PSLKRSLMPY
FLLTQAVRTG NLAKFNQVLD QFGEKFQADG TYTLIIRLRH NVIKTGVRMI SLSYSRISLA
DIAQKLQLDS PEDAEFIVAK AIRDGVIEAS INHEKGYVQS KEMIDIYSTR EPQLAFHQRI
SFCLDIHNMS VKAMRFPPKS YNKDLESAEE RREREQQDLE FAKEMAEDDD DSFP
