PSME3_HUMAN
ID PSME3_HUMAN Reviewed; 254 AA.
AC P61289; A8K9A3; O35563; P97373; Q12920; Q13172; Q9BQD9;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Proteasome activator complex subunit 3;
DE AltName: Full=11S regulator complex subunit gamma;
DE Short=REG-gamma;
DE AltName: Full=Activator of multicatalytic protease subunit 3;
DE AltName: Full=Ki nuclear autoantigen;
DE AltName: Full=Proteasome activator 28 subunit gamma;
DE Short=PA28g;
DE Short=PA28gamma;
GN Name=PSME3;
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).
RX PubMed=1968796; DOI=10.1111/j.1365-2249.1990.tb05180.x;
RA Nikaido T., Shimada K., Shibata M., Hata M., Sakamoto M., Takasaki Y.,
RA Sato C., Takahashi T., Nishida Y.;
RT "Cloning and nucleotide sequence of cDNA for Ki antigen, a highly conserved
RT nuclear protein detected with sera from patients with systemic lupus
RT erythematosus.";
RL Clin. Exp. Immunol. 79:209-214(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=B-cell, and Fetal brain;
RX PubMed=7951316; DOI=10.1038/ng0894-472;
RA Albertsen H.M., Smith S.A., Mazoyer S., Fujimoto E., Stevens J.,
RA Williams B., Rodriguez P., Cropp C.S., Slijepcevic P., Carlson M.,
RA Robertson M., Bradley P., Lawrence E., Harrington T., Sheng Z.M.,
RA Hoopes R., Sternberg N., Brothman A., Callahan R., Ponder B.A.J., White R.;
RT "A physical map and candidate genes in the BRCA1 region on chromosome
RT 17q12-21.";
RL Nat. Genet. 7:472-479(1994).
RN [3]
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Ovary, and Placenta;
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 [9]
RP PROTEIN SEQUENCE OF 2-12 AND 111-121, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Ramsay A., Leung H.Y.;
RL Submitted (FEB-2009) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-135.
RC TISSUE=Ovary;
RX PubMed=7545954; DOI=10.1126/science.7545954;
RA Miki Y., Swensen J., Shattuck-Eidens D., Futreal P.A., Harshman K.,
RA Tavtigian S., Liu Q., Cochran C., Bennett L.M., Ding W., Bell R.,
RA Rosenthal J., Hussey C., Tran T., McClure M., Frye C., Hattier T.,
RA Phelps R., Haugen-Strano A., Katcher H., Yakumo K., Gholami Z., Shaffer D.,
RA Stone S., Bayer S., Wray C., Bogden R., Dayananth P., Ward J., Tonin P.,
RA Narod S., Bristow P.K., Norris F.H., Helvering L., Morrison P., Rosteck P.,
RA Lai M., Barrett J.C., Lewis C., Neuhausen S., Cannon-Albright L.,
RA Godlgar D., Wiseman R., Kamb A., Skolnick M.H.;
RT "A strong candidate for the breast and ovarian cancer susceptibility gene
RT BRCA1.";
RL Science 266:66-71(1994).
RN [11]
RP FUNCTION, SUBUNIT, INTERACTION WITH THE PROTEASOME, AND CALCIUM-BINDING.
RX PubMed=9325261; DOI=10.1074/jbc.272.41.25483;
RA Realini C., Jensen C.C., Zhang Z., Johnston S.C., Knowlton J.R., Hill C.P.,
RA Rechsteiner M.;
RT "Characterization of recombinant REGalpha, REGbeta, and REGgamma proteasome
RT activators.";
RL J. Biol. Chem. 272:25483-25492(1997).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11185562; DOI=10.1006/abbi.2000.2086;
RA Wilk S., Chen W.-E., Magnusson R.P.;
RT "Properties of the nuclear proteasome activator PA28gamma (REGgamma).";
RL Arch. Biochem. Biophys. 383:265-271(2000).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=10657252; DOI=10.1042/bj3460155;
RA Brooks P., Fuertes G., Murray R.Z., Bose S., Knecht E., Rechsteiner M.C.,
RA Hendil K.B., Tanaka K., Dyson J., Rivett J.;
RT "Subcellular localization of proteasomes and their regulatory complexes in
RT mammalian cells.";
RL Biochem. J. 346:155-161(2000).
RN [14]
RP FUNCTION, DOMAIN, INTERACTION WITH THE PROTEASOME, AND SUBUNIT.
RX PubMed=10835274; DOI=10.1006/jmbi.2000.3800;
RA Li J., Gao X., Joss L., Rechsteiner M.;
RT "The proteasome activator 11 S REG or PA28: chimeras implicate carboxyl-
RT terminal sequences in oligomerization and proteasome binding but not in the
RT activation of specific proteasome catalytic subunits.";
RL J. Mol. Biol. 299:641-654(2000).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, 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 [17]
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 [18]
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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
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 [21]
RP ACETYLATION AT LYS-195, AND SUBUNIT.
RX PubMed=23612972; DOI=10.1074/jbc.m112.437129;
RA Liu J., Wang Y., Li L., Zhou L., Wei H., Zhou Q., Liu J., Wang W., Ji L.,
RA Shan P., Wang Y., Yang Y., Jung S.Y., Zhang P., Wang C., Long W., Zhang B.,
RA Li X.;
RT "Site-specific acetylation of the proteasome activator REGgamma directs its
RT heptameric structure and functions.";
RL J. Biol. Chem. 288:16567-16578(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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 [23]
RP FUNCTION, PHOSPHORYLATION AT SER-247, AND INTERACTION WITH CCAR2.
RX PubMed=25361978; DOI=10.1093/nar/gku1065;
RA Magni M., Ruscica V., Buscemi G., Kim J.E., Nachimuthu B.T., Fontanella E.,
RA Delia D., Zannini L.;
RT "Chk2 and REGgamma-dependent DBC1 regulation in DNA damage induced
RT apoptosis.";
RL Nucleic Acids Res. 42:13150-13160(2014).
RN [24]
RP ELECTRON MICROSCOPY, SUBUNIT, FUNCTION, AND MUTAGENESIS OF LYS-188.
RX PubMed=11432824; DOI=10.1093/emboj/20.13.3359;
RA Li J., Gao X., Ortega J., Nazif T., Joss L., Bogyo M., Steven A.C.,
RA Rechsteiner M.;
RT "Lysine 188 substitutions convert the pattern of proteasome activation by
RT REGgamma to that of REGs alpha and beta.";
RL EMBO J. 20:3359-3369(2001).
RN [25]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12629132; DOI=10.1210/jc.2002-021413;
RA Okamura T., Taniguchi S., Ohkura T., Yoshida A., Shimizu H., Sakai M.,
RA Maeta H., Fukui H., Ueta Y., Hisatome I., Shigemasa C.;
RT "Abnormally high expression of proteasome activator-gamma in thyroid
RT neoplasm.";
RL J. Clin. Endocrinol. Metab. 88:1374-1383(2003).
RN [26]
RP FUNCTION.
RX PubMed=15111123; DOI=10.1016/j.abb.2004.03.021;
RA Gao X., Li J., Pratt G., Wilk S., Rechsteiner M.;
RT "Purification procedures determine the proteasome activation properties of
RT REG gamma (PA28 gamma).";
RL Arch. Biochem. Biophys. 425:158-164(2004).
RN [27]
RP FUNCTION, AND INTERACTION WITH TP53 AND MDM2.
RX PubMed=18309296; DOI=10.1038/emboj.2008.25;
RA Zhang Z., Zhang R.;
RT "Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-
RT mediated degradation.";
RL EMBO J. 27:852-864(2008).
RN [28]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS UL27.
RX PubMed=21320693; DOI=10.1016/j.chom.2011.01.006;
RA Reitsma J.M., Savaryn J.P., Faust K., Sato H., Halligan B.D., Terhune S.S.;
RT "Antiviral inhibition targeting the HCMV kinase pUL97 requires pUL27-
RT dependent proteasomal degradation of Tip60 acetyltransferase and cell-cycle
RT arrest.";
RL Cell Host Microbe 9:103-114(2011).
RN [29]
RP INTERACTION WITH COIL AND PSME3IP1.
RX PubMed=29934401; DOI=10.1073/pnas.1722299115;
RA Jonik-Nowak B., Menneteau T., Fesquet D., Baldin V., Bonne-Andrea C.,
RA Mechali F., Fabre B., Boisguerin P., de Rossi S., Henriquet C.,
RA Pugniere M., Ducoux-Petit M., Burlet-Schiltz O., Lamond A.I., Fort P.,
RA Boulon S., Bousquet M.P., Coux O.;
RT "PIP30/FAM192A is a novel regulator of the nuclear proteasome activator
RT PA28gamma.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E6477-E6486(2018).
CC -!- FUNCTION: Subunit of the 11S REG-gamma (also called PA28-gamma)
CC proteasome regulator, a doughnut-shaped homoheptamer which associates
CC with the proteasome. 11S REG-gamma activates the trypsin-like catalytic
CC subunit of the proteasome but inhibits the chymotrypsin-like and
CC postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53
CC interaction which promotes ubiquitination- and MDM2-dependent
CC proteasomal degradation of p53/TP53, limiting its accumulation and
CC resulting in inhibited apoptosis after DNA damage. May also be involved
CC in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1
CC inhibition (PubMed:25361978). {ECO:0000269|PubMed:10835274,
CC ECO:0000269|PubMed:11185562, ECO:0000269|PubMed:11432824,
CC ECO:0000269|PubMed:15111123, ECO:0000269|PubMed:18309296,
CC ECO:0000269|PubMed:25361978, ECO:0000269|PubMed:9325261}.
CC -!- SUBUNIT: Homoheptamer; the stability of the heptamer is essential for
CC the specific activation of the trypsine-like subunit and inhibition of
CC the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits of
CC the proteasome. Interacts with p53/TP53 and MDM2. Interacts with MAP3K3
CC (By similarity). Associates with the proteasome. Interacts with CCAR2.
CC Interacts with PSME3IP1 (via C-terminus); the interaction is direct and
CC promotes the association of PSME3 with the 20S proteasome
CC (PubMed:29934401). Interacts with COIL; the interaction is inhibited by
CC PSME3IP1 (PubMed:29934401). {ECO:0000250|UniProtKB:P61290,
CC ECO:0000269|PubMed:10835274, ECO:0000269|PubMed:11185562,
CC ECO:0000269|PubMed:11432824, ECO:0000269|PubMed:18309296,
CC ECO:0000269|PubMed:23612972, ECO:0000269|PubMed:25361978,
CC ECO:0000269|PubMed:29934401, ECO:0000269|PubMed:9325261}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC UL27. {ECO:0000269|PubMed:21320693}.
CC -!- INTERACTION:
CC P61289; A0A0S2Z645: ABCF3; NbExp=3; IntAct=EBI-355546, EBI-16432404;
CC P61289; P54259: ATN1; NbExp=3; IntAct=EBI-355546, EBI-945980;
CC P61289; Q86V38: ATN1; NbExp=3; IntAct=EBI-355546, EBI-11954292;
CC P61289; Q9BXC9: BBS2; NbExp=7; IntAct=EBI-355546, EBI-748297;
CC P61289; P30305: CDC25B; NbExp=3; IntAct=EBI-355546, EBI-1051746;
CC P61289; Q86X02: CDR2L; NbExp=3; IntAct=EBI-355546, EBI-11063830;
CC P61289; P38432: COIL; NbExp=6; IntAct=EBI-355546, EBI-945751;
CC P61289; P02489: CRYAA; NbExp=3; IntAct=EBI-355546, EBI-6875961;
CC P61289; Q14689-6: DIP2A; NbExp=3; IntAct=EBI-355546, EBI-10233719;
CC P61289; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-355546, EBI-9679045;
CC P61289; Q92997: DVL3; NbExp=3; IntAct=EBI-355546, EBI-739789;
CC P61289; Q96JC9: EAF1; NbExp=9; IntAct=EBI-355546, EBI-769261;
CC P61289; Q96CJ1: EAF2; NbExp=3; IntAct=EBI-355546, EBI-1245604;
CC P61289; Q6PCT2-2: FBXL19; NbExp=3; IntAct=EBI-355546, EBI-11959077;
CC P61289; Q9Y3I1: FBXO7; NbExp=3; IntAct=EBI-355546, EBI-1161222;
CC P61289; Q9NU39: FOXD4L1; NbExp=3; IntAct=EBI-355546, EBI-11320806;
CC P61289; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-355546, EBI-11959863;
CC P61289; P31942-2: HNRNPH3; NbExp=3; IntAct=EBI-355546, EBI-16399628;
CC P61289; Q15735: INPP5J; NbExp=3; IntAct=EBI-355546, EBI-10236940;
CC P61289; Q8WVZ9: KBTBD7; NbExp=3; IntAct=EBI-355546, EBI-473695;
CC P61289; Q92876: KLK6; NbExp=3; IntAct=EBI-355546, EBI-2432309;
CC P61289; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-355546, EBI-739832;
CC P61289; Q00987: MDM2; NbExp=8; IntAct=EBI-355546, EBI-389668;
CC P61289; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-355546, EBI-16439278;
CC P61289; Q9Y6Q9: NCOA3; NbExp=5; IntAct=EBI-355546, EBI-81196;
CC P61289; Q96HA8: NTAQ1; NbExp=5; IntAct=EBI-355546, EBI-741158;
CC P61289; Q99471: PFDN5; NbExp=6; IntAct=EBI-355546, EBI-357275;
CC P61289; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-355546, EBI-79165;
CC P61289; O43741: PRKAB2; NbExp=9; IntAct=EBI-355546, EBI-1053424;
CC P61289; Q9NZ81: PRR13; NbExp=6; IntAct=EBI-355546, EBI-740924;
CC P61289; P61289: PSME3; NbExp=8; IntAct=EBI-355546, EBI-355546;
CC P61289; Q9UNE2: RPH3AL; NbExp=3; IntAct=EBI-355546, EBI-2855824;
CC P61289; P42677: RPS27; NbExp=3; IntAct=EBI-355546, EBI-356336;
CC P61289; Q9HCE7: SMURF1; NbExp=5; IntAct=EBI-355546, EBI-976466;
CC P61289; Q9UQ90: SPG7; NbExp=3; IntAct=EBI-355546, EBI-717201;
CC P61289; Q32MN6: TBP; NbExp=3; IntAct=EBI-355546, EBI-10239991;
CC P61289; Q9P2Z0: THAP10; NbExp=3; IntAct=EBI-355546, EBI-745404;
CC P61289; Q8WVP5: TNFAIP8L1; NbExp=6; IntAct=EBI-355546, EBI-752102;
CC P61289; P04637: TP53; NbExp=7; IntAct=EBI-355546, EBI-366083;
CC P61289; Q99757: TXN2; NbExp=3; IntAct=EBI-355546, EBI-2932492;
CC P61289; Q64LD2-2: WDR25; NbExp=3; IntAct=EBI-355546, EBI-12032042;
CC P61289; Q8TBK6: ZCCHC10; NbExp=7; IntAct=EBI-355546, EBI-597063;
CC P61289; P0DTC9: N; Xeno; NbExp=3; IntAct=EBI-355546, EBI-25475856;
CC P61289; P12504: vif; Xeno; NbExp=2; IntAct=EBI-355546, EBI-779991;
CC P61289; O93077; Xeno; NbExp=11; IntAct=EBI-355546, EBI-9636511;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10657252,
CC ECO:0000269|PubMed:12629132}. Cytoplasm {ECO:0000250}. Note=Localizes
CC to the cytoplasm during mitosis following nuclear envelope breakdown at
CC this distinct stage of the cell cycle which allows its interaction with
CC MAP3K3 kinase. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P61289-1, Q12920-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P61289-2, Q12920-2;
CC Sequence=VSP_004516;
CC Name=3;
CC IsoId=P61289-3; Sequence=VSP_055047;
CC -!- INDUCTION: Up-regulated in thyroid carcinoma cells.
CC {ECO:0000269|PubMed:12629132}.
CC -!- DOMAIN: The C-terminal sequences affect heptamer stability and
CC proteasome affinity. {ECO:0000269|PubMed:10835274}.
CC -!- PTM: Phosphorylated by MAP3K3 (By similarity). Phosphorylation at Ser-
CC 247 promotes its association with CCAR2. {ECO:0000250|UniProtKB:P61290,
CC ECO:0000269|PubMed:25361978}.
CC -!- PTM: Acetylation at the major site Lys-195 is important for
CC oligomerization and ability to degrade its target substrates.
CC Deacetylated by SIRT1. {ECO:0000269|PubMed:23612972,
CC ECO:0000269|Ref.9}.
CC -!- SIMILARITY: Belongs to the PA28 family. {ECO:0000305}.
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DR EMBL; U11292; AAB60335.1; -; mRNA.
DR EMBL; BT019386; AAV38193.1; -; mRNA.
DR EMBL; AK292618; BAF85307.1; -; mRNA.
DR EMBL; AK074999; BAG52046.1; -; mRNA.
DR EMBL; AC016889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60893.1; -; Genomic_DNA.
DR EMBL; BC001423; AAH01423.1; -; mRNA.
DR EMBL; BC002684; AAH02684.1; -; mRNA.
DR EMBL; BC008020; AAH08020.1; -; mRNA.
DR EMBL; U25756; AAA93227.1; -; Genomic_DNA.
DR CCDS; CCDS11442.1; -. [P61289-2]
DR CCDS; CCDS45689.1; -.
DR CCDS; CCDS59290.1; -. [P61289-3]
DR PIR; I38702; A60537.
DR RefSeq; NP_005780.2; NM_005789.3. [P61289-1]
DR RefSeq; NP_789839.1; NM_176863.2. [P61289-2]
DR AlphaFoldDB; P61289; -.
DR SMR; P61289; -.
DR BioGRID; 115492; 356.
DR CORUM; P61289; -.
DR IntAct; P61289; 164.
DR MINT; P61289; -.
DR STRING; 9606.ENSP00000293362; -.
DR ChEMBL; CHEMBL4296023; -.
DR GlyGen; P61289; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61289; -.
DR PhosphoSitePlus; P61289; -.
DR SwissPalm; P61289; -.
DR BioMuta; PSME3; -.
DR DMDM; 47117724; -.
DR EPD; P61289; -.
DR jPOST; P61289; -.
DR MassIVE; P61289; -.
DR MaxQB; P61289; -.
DR PaxDb; P61289; -.
DR PeptideAtlas; P61289; -.
DR PRIDE; P61289; -.
DR ProteomicsDB; 57290; -.
DR ProteomicsDB; 57291; -. [P61289-2]
DR Antibodypedia; 1736; 336 antibodies from 34 providers.
DR DNASU; 10197; -.
DR Ensembl; ENST00000293362.7; ENSP00000293362.1; ENSG00000131467.12. [P61289-2]
DR Ensembl; ENST00000441946.6; ENSP00000409487.2; ENSG00000131467.12. [P61289-3]
DR Ensembl; ENST00000590720.6; ENSP00000466794.1; ENSG00000131467.12. [P61289-1]
DR GeneID; 10197; -.
DR KEGG; hsa:10197; -.
DR MANE-Select; ENST00000590720.6; ENSP00000466794.1; NM_005789.4; NP_005780.2.
DR UCSC; uc002ibq.5; human.
DR CTD; 10197; -.
DR DisGeNET; 10197; -.
DR GeneCards; PSME3; -.
DR HGNC; HGNC:9570; PSME3.
DR HPA; ENSG00000131467; Low tissue specificity.
DR MIM; 605129; gene.
DR neXtProt; NX_P61289; -.
DR OpenTargets; ENSG00000131467; -.
DR PharmGKB; PA33916; -.
DR VEuPathDB; HostDB:ENSG00000131467; -.
DR eggNOG; KOG4470; Eukaryota.
DR GeneTree; ENSGT00950000183098; -.
DR InParanoid; P61289; -.
DR OMA; PCNKPLC; -.
DR OrthoDB; 1251022at2759; -.
DR PhylomeDB; P61289; -.
DR TreeFam; TF106236; -.
DR PathwayCommons; P61289; -.
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-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; P61289; -.
DR BioGRID-ORCS; 10197; 86 hits in 1096 CRISPR screens.
DR ChiTaRS; PSME3; human.
DR GeneWiki; PSME3; -.
DR GenomeRNAi; 10197; -.
DR Pharos; P61289; Tbio.
DR PRO; PR:P61289; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P61289; protein.
DR Bgee; ENSG00000131467; Expressed in islet of Langerhans and 202 other tissues.
DR ExpressionAtlas; P61289; baseline and differential.
DR Genevisible; P61289; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR GO; GO:0000502; C:proteasome complex; TAS:ProtInc.
DR GO; GO:0061133; F:endopeptidase activator activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0010950; P:positive regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:UniProtKB.
DR Gene3D; 1.20.120.180; -; 1.
DR Gene3D; 1.20.5.120; -; 1.
DR InterPro; IPR003186; PA28_C.
DR InterPro; IPR036997; PA28_C_sf.
DR InterPro; IPR036996; PA28_N_sf.
DR InterPro; IPR009077; Proteasome_activ_PA28.
DR InterPro; IPR003185; Proteasome_activ_PA28_N.
DR InterPro; IPR036252; Proteasome_activ_sf.
DR PANTHER; PTHR10660; PTHR10660; 1.
DR Pfam; PF02251; PA28_alpha; 1.
DR Pfam; PF02252; PA28_beta; 1.
DR SUPFAM; SSF47216; SSF47216; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Cell cycle; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:22814378"
FT CHAIN 2..254
FT /note="Proteasome activator complex subunit 3"
FT /id="PRO_0000161789"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:22814378"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 195
FT /note="N6-acetyllysine; by P300/CBP"
FT /evidence="ECO:0000269|PubMed:23612972"
FT MOD_RES 247
FT /note="Phosphoserine; by CHEK2"
FT /evidence="ECO:0000269|PubMed:25361978"
FT VAR_SEQ 1..13
FT /note="MASLLKVDQEVKL -> MEKWILKKIKYLQSGGLSASYYSY (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055047"
FT VAR_SEQ 135
FT /note="T -> TPSGKGPHICFDLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7951316"
FT /id="VSP_004516"
FT MUTAGEN 188
FT /note="K->E,D,A,C,N,Q,H,F,S,I,P: Assembles into less stable
FT hexamers/heptamers and therefore impairs specificity of
FT activation of trypsin-like subunits of the proteasome."
FT /evidence="ECO:0000269|PubMed:11432824"
FT CONFLICT 25
FT /note="E -> K (in Ref. 2; AAB60335)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="E -> K (in Ref. 10; AAA93227)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 29506 MW; 116FAB47D60A26C0 CRC64;
MASLLKVDQE VKLKVDSFRE RITSEAEDLV ANFFPKKLLE LDSFLKEPIL NIHDLTQIHS
DMNLPVPDPI LLTNSHDGLD GPTYKKRRLD ECEEAFQGTK VFVMPNGMLK SNQQLVDIIE
KVKPEIRLLI EKCNTVKMWV QLLIPRIEDG NNFGVSIQEE TVAELRTVES EAASYLDQIS
RYYITRAKLV SKIAKYPHVE DYRRTVTEID EKEYISLRLI ISELRNQYVT LHDMILKNIE
KIKRPRSSNA ETLY
