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Proteasome activator complex subunit 3 (11S regulator complex subunit gamma) (REG-gamma) (Activator of multicatalytic protease subunit 3) (Ki nuclear autoantigen) (Proteasome activator 28 subunit gamma) (PA28g) (PA28gamma)

 PSME3_HUMAN             Reviewed;         254 AA.
P61289; A8K9A3; O35563; P97373; Q12920; Q13172; Q9BQD9;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 1.
22-NOV-2017, entry version 148.
RecName: Full=Proteasome activator complex subunit 3;
AltName: Full=11S regulator complex subunit gamma;
Short=REG-gamma;
AltName: Full=Activator of multicatalytic protease subunit 3;
AltName: Full=Ki nuclear autoantigen;
AltName: Full=Proteasome activator 28 subunit gamma;
Short=PA28g;
Short=PA28gamma;
Name=PSME3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1968796; DOI=10.1111/j.1365-2249.1990.tb05180.x;
Nikaido T., Shimada K., Shibata M., Hata M., Sakamoto M., Takasaki Y.,
Sato C., Takahashi T., Nishida Y.;
"Cloning and nucleotide sequence of cDNA for Ki antigen, a highly
conserved nuclear protein detected with sera from patients with
systemic lupus erythematosus.";
Clin. Exp. Immunol. 79:209-214(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=B-cell, and Fetal brain;
PubMed=7951316; DOI=10.1038/ng0894-472;
Albertsen H.M., Smith S.A., Mazoyer S., Fujimoto E., Stevens J.,
Williams B., Rodriguez P., Cropp C.S., Slijepcevic P., Carlson M.,
Robertson M., Bradley P., Lawrence E., Harrington T., Sheng Z.M.,
Hoopes R., Sternberg N., Brothman A., Callahan R., Ponder B.A.J.,
White R.;
"A physical map and candidate genes in the BRCA1 region on chromosome
17q12-21.";
Nat. Genet. 7:472-479(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, Ovary, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 2-12 AND 111-121, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Ramsay A., Leung H.Y.;
Submitted (FEB-2009) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-135.
TISSUE=Ovary;
PubMed=7545954; DOI=10.1126/science.7545954;
Miki Y., Swensen J., Shattuck-Eidens D., Futreal P.A., Harshman K.,
Tavtigian S., Liu Q., Cochran C., Bennett L.M., Ding W., Bell R.,
Rosenthal J., Hussey C., Tran T., McClure M., Frye C., Hattier T.,
Phelps R., Haugen-Strano A., Katcher H., Yakumo K., Gholami Z.,
Shaffer D., Stone S., Bayer S., Wray C., Bogden R., Dayananth P.,
Ward J., Tonin P., Narod S., Bristow P.K., Norris F.H., Helvering L.,
Morrison P., Rosteck P., Lai M., Barrett J.C., Lewis C., Neuhausen S.,
Cannon-Albright L., Godlgar D., Wiseman R., Kamb A., Skolnick M.H.;
"A strong candidate for the breast and ovarian cancer susceptibility
gene BRCA1.";
Science 266:66-71(1994).
[11]
FUNCTION, SUBUNIT, INTERACTION WITH THE PROTEASOME, AND
CALCIUM-BINDING.
PubMed=9325261; DOI=10.1074/jbc.272.41.25483;
Realini C., Jensen C.C., Zhang Z., Johnston S.C., Knowlton J.R.,
Hill C.P., Rechsteiner M.;
"Characterization of recombinant REGalpha, REGbeta, and REGgamma
proteasome activators.";
J. Biol. Chem. 272:25483-25492(1997).
[12]
FUNCTION, AND SUBUNIT.
PubMed=11185562; DOI=10.1006/abbi.2000.2086;
Wilk S., Chen W.-E., Magnusson R.P.;
"Properties of the nuclear proteasome activator PA28gamma
(REGgamma).";
Arch. Biochem. Biophys. 383:265-271(2000).
[13]
SUBCELLULAR LOCATION.
PubMed=10657252; DOI=10.1042/bj3460155;
Brooks P., Fuertes G., Murray R.Z., Bose S., Knecht E.,
Rechsteiner M.C., Hendil K.B., Tanaka K., Dyson J., Rivett J.;
"Subcellular localization of proteasomes and their regulatory
complexes in mammalian cells.";
Biochem. J. 346:155-161(2000).
[14]
FUNCTION, DOMAIN, INTERACTION WITH THE PROTEASOME, AND SUBUNIT.
PubMed=10835274; DOI=10.1006/jmbi.2000.3800;
Li J., Gao X., Joss L., Rechsteiner M.;
"The proteasome activator 11 S REG or PA28: chimeras implicate
carboxyl-terminal sequences in oligomerization and proteasome binding
but not in the activation of specific proteasome catalytic subunits.";
J. Mol. Biol. 299:641-654(2000).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
ACETYLATION AT LYS-195, AND SUBUNIT.
PubMed=23612972; DOI=10.1074/jbc.M112.437129;
Liu J., Wang Y., Li L., Zhou L., Wei H., Zhou Q., Liu J., Wang W.,
Ji L., Shan P., Wang Y., Yang Y., Jung S.Y., Zhang P., Wang C.,
Long W., Zhang B., Li X.;
"Site-specific acetylation of the proteasome activator REGgamma
directs its heptameric structure and functions.";
J. Biol. Chem. 288:16567-16578(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
FUNCTION, PHOSPHORYLATION AT SER-247, AND INTERACTION WITH CCAR2.
PubMed=25361978; DOI=10.1093/nar/gku1065;
Magni M., Ruscica V., Buscemi G., Kim J.E., Nachimuthu B.T.,
Fontanella E., Delia D., Zannini L.;
"Chk2 and REGgamma-dependent DBC1 regulation in DNA damage induced
apoptosis.";
Nucleic Acids Res. 42:13150-13160(2014).
[24]
ELECTRON MICROSCOPY, SUBUNIT, FUNCTION, AND MUTAGENESIS OF LYS-188.
PubMed=11432824; DOI=10.1093/emboj/20.13.3359;
Li J., Gao X., Ortega J., Nazif T., Joss L., Bogyo M., Steven A.C.,
Rechsteiner M.;
"Lysine 188 substitutions convert the pattern of proteasome activation
by REGgamma to that of REGs alpha and beta.";
EMBO J. 20:3359-3369(2001).
[25]
INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=12629132; DOI=10.1210/jc.2002-021413;
Okamura T., Taniguchi S., Ohkura T., Yoshida A., Shimizu H., Sakai M.,
Maeta H., Fukui H., Ueta Y., Hisatome I., Shigemasa C.;
"Abnormally high expression of proteasome activator-gamma in thyroid
neoplasm.";
J. Clin. Endocrinol. Metab. 88:1374-1383(2003).
[26]
FUNCTION.
PubMed=15111123; DOI=10.1016/j.abb.2004.03.021;
Gao X., Li J., Pratt G., Wilk S., Rechsteiner M.;
"Purification procedures determine the proteasome activation
properties of REG gamma (PA28 gamma).";
Arch. Biochem. Biophys. 425:158-164(2004).
[27]
FUNCTION, AND INTERACTION WITH TP53 AND MDM2.
PubMed=18309296; DOI=10.1038/emboj.2008.25;
Zhang Z., Zhang R.;
"Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-
mediated degradation.";
EMBO J. 27:852-864(2008).
[28]
INTERACTION WITH HUMAN CYTOMEGALOVIRUS UL27.
PubMed=21320693; DOI=10.1016/j.chom.2011.01.006;
Reitsma J.M., Savaryn J.P., Faust K., Sato H., Halligan B.D.,
Terhune S.S.;
"Antiviral inhibition targeting the HCMV kinase pUL97 requires pUL27-
dependent proteasomal degradation of Tip60 acetyltransferase and cell-
cycle arrest.";
Cell Host Microbe 9:103-114(2011).
-!- FUNCTION: Subunit of the 11S REG-gamma (also called PA28-gamma)
proteasome regulator, a doughnut-shaped homoheptamer which
associates with the proteasome. 11S REG-gamma activates the
trypsin-like catalytic subunit of the proteasome but inhibits the
chymotrypsin-like and postglutamyl-preferring (PGPH) subunits.
Facilitates the MDM2-p53/TP53 interaction which promotes
ubiquitination- and MDM2-dependent proteasomal degradation of
p53/TP53, limiting its accumulation and resulting in inhibited
apoptosis after DNA damage. May also be involved in cell cycle
regulation. Mediates CCAR2 and CHEK2-dependent SIRT1 inhibition
(PubMed:25361978). {ECO:0000269|PubMed:10835274,
ECO:0000269|PubMed:11185562, ECO:0000269|PubMed:11432824,
ECO:0000269|PubMed:15111123, ECO:0000269|PubMed:18309296,
ECO:0000269|PubMed:25361978, ECO:0000269|PubMed:9325261}.
-!- SUBUNIT: Homoheptamer; the stability of the heptamer is essential
for the specific activation of the trypsine-like subunit and
inhibition of the chymotrypsin-like and postglutamyl-preferring
(PGPH) subunits of the proteasome. Interacts with p53/TP53 and
MDM2. Interacts with MAP3K3 (By similarity). Associates with the
proteasome. Interacts with human cytomegalovirus UL27. Interacts
with CCAR2. {ECO:0000250|UniProtKB:P61290,
ECO:0000269|PubMed:10835274, ECO:0000269|PubMed:11185562,
ECO:0000269|PubMed:11432824, ECO:0000269|PubMed:18309296,
ECO:0000269|PubMed:21320693, ECO:0000269|PubMed:23612972,
ECO:0000269|PubMed:25361978, ECO:0000269|PubMed:9325261}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-355546, EBI-355546;
O93077:- (xeno); NbExp=11; IntAct=EBI-355546, EBI-9636511;
P54259:ATN1; NbExp=3; IntAct=EBI-355546, EBI-945980;
Q9BXC9:BBS2; NbExp=8; IntAct=EBI-355546, EBI-748297;
P38432:COIL; NbExp=5; IntAct=EBI-355546, EBI-945751;
Q14689-6:DIP2A; NbExp=3; IntAct=EBI-355546, EBI-10233719;
Q96JC9:EAF1; NbExp=10; IntAct=EBI-355546, EBI-769261;
Q96CJ1:EAF2; NbExp=3; IntAct=EBI-355546, EBI-1245604;
Q9Y3I1:FBXO7; NbExp=3; IntAct=EBI-355546, EBI-1161222;
Q00987:MDM2; NbExp=8; IntAct=EBI-355546, EBI-389668;
Q9Y6Q9:NCOA3; NbExp=5; IntAct=EBI-355546, EBI-81196;
Q99471:PFDN5; NbExp=5; IntAct=EBI-355546, EBI-357275;
O43741:PRKAB2; NbExp=7; IntAct=EBI-355546, EBI-1053424;
Q9NZ81:PRR13; NbExp=5; IntAct=EBI-355546, EBI-740924;
Q9HCE7:SMURF1; NbExp=5; IntAct=EBI-355546, EBI-976466;
Q9UQ90:SPG7; NbExp=3; IntAct=EBI-355546, EBI-717201;
Q8WVP5:TNFAIP8L1; NbExp=5; IntAct=EBI-355546, EBI-752102;
P04637:TP53; NbExp=7; IntAct=EBI-355546, EBI-366083;
Q99757:TXN2; NbExp=3; IntAct=EBI-355546, EBI-2932492;
P12504:vif (xeno); NbExp=2; IntAct=EBI-355546, EBI-779991;
Q64LD2-2:WDR25; NbExp=4; IntAct=EBI-355546, EBI-12032042;
Q96HA8:WDYHV1; NbExp=4; IntAct=EBI-355546, EBI-741158;
Q8TBK6:ZCCHC10; NbExp=6; IntAct=EBI-355546, EBI-597063;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10657252,
ECO:0000269|PubMed:12629132}. Cytoplasm {ECO:0000250}.
Note=Localizes to the cytoplasm during mitosis following nuclear
envelope breakdown at this distinct stage of the cell cycle which
allows its interaction with MAP3K3 kinase. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P61289-1, Q12920-1;
Sequence=Displayed;
Name=2;
IsoId=P61289-2, Q12920-2;
Sequence=VSP_004516;
Name=3;
IsoId=P61289-3; Sequence=VSP_055047;
Note=No experimental confirmation. Gene prediction based on EST
data.;
-!- INDUCTION: Up-regulated in thyroid carcinoma cells.
{ECO:0000269|PubMed:12629132}.
-!- DOMAIN: The C-terminal sequences affect heptamer stability and
proteasome affinity. {ECO:0000269|PubMed:10835274}.
-!- PTM: Phosphorylated by MAP3K3 (By similarity). Phosphorylation at
Ser-247 promotes its association with CCAR2.
{ECO:0000250|UniProtKB:P61290, ECO:0000269|PubMed:25361978}.
-!- PTM: Acetylation at the major site Lys-195 is important for
oligomerization and ability to degrade its target substrates.
Deacetylated by SIRT1. {ECO:0000269|PubMed:23612972,
ECO:0000269|Ref.9}.
-!- SIMILARITY: Belongs to the PA28 family. {ECO:0000305}.
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EMBL; U11292; AAB60335.1; -; mRNA.
EMBL; BT019386; AAV38193.1; -; mRNA.
EMBL; AK292618; BAF85307.1; -; mRNA.
EMBL; AK074999; BAG52046.1; -; mRNA.
EMBL; AC016889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471152; EAW60893.1; -; Genomic_DNA.
EMBL; BC001423; AAH01423.1; -; mRNA.
EMBL; BC002684; AAH02684.1; -; mRNA.
EMBL; BC008020; AAH08020.1; -; mRNA.
EMBL; U25756; AAA93227.1; -; Genomic_DNA.
CCDS; CCDS11442.1; -. [P61289-2]
CCDS; CCDS45689.1; -.
CCDS; CCDS59290.1; -. [P61289-3]
PIR; I38702; A60537.
RefSeq; NP_005780.2; NM_005789.3. [P61289-1]
RefSeq; NP_789839.1; NM_176863.2. [P61289-2]
UniGene; Hs.152978; -.
ProteinModelPortal; P61289; -.
SMR; P61289; -.
BioGrid; 115492; 177.
CORUM; P61289; -.
IntAct; P61289; 85.
MINT; MINT-5002653; -.
STRING; 9606.ENSP00000293362; -.
iPTMnet; P61289; -.
PhosphoSitePlus; P61289; -.
SwissPalm; P61289; -.
BioMuta; PSME3; -.
DMDM; 47117724; -.
EPD; P61289; -.
PaxDb; P61289; -.
PeptideAtlas; P61289; -.
PRIDE; P61289; -.
DNASU; 10197; -.
Ensembl; ENST00000293362; ENSP00000293362; ENSG00000131467. [P61289-2]
Ensembl; ENST00000441946; ENSP00000409487; ENSG00000131467. [P61289-3]
Ensembl; ENST00000590720; ENSP00000466794; ENSG00000131467. [P61289-1]
GeneID; 10197; -.
KEGG; hsa:10197; -.
UCSC; uc002ibq.5; human.
CTD; 10197; -.
DisGeNET; 10197; -.
EuPathDB; HostDB:ENSG00000131467.10; -.
GeneCards; PSME3; -.
HGNC; HGNC:9570; PSME3.
HPA; CAB008388; -.
HPA; HPA012510; -.
MIM; 605129; gene.
neXtProt; NX_P61289; -.
OpenTargets; ENSG00000131467; -.
PharmGKB; PA33916; -.
eggNOG; KOG4470; Eukaryota.
eggNOG; ENOG410XQVX; LUCA.
GeneTree; ENSGT00510000046374; -.
HOVERGEN; HBG053745; -.
InParanoid; P61289; -.
KO; K06698; -.
OMA; PCNKPLC; -.
OrthoDB; EOG091G0GX7; -.
PhylomeDB; P61289; -.
TreeFam; TF106236; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSME3; human.
GeneWiki; PSME3; -.
GenomeRNAi; 10197; -.
PMAP-CutDB; P61289; -.
PRO; PR:P61289; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000131467; -.
CleanEx; HS_PSME3; -.
ExpressionAtlas; P61289; baseline and differential.
Genevisible; P61289; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
GO; GO:0000502; C:proteasome complex; TAS:ProtInc.
GO; GO:0061133; F:endopeptidase activator activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IDA:UniProtKB.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:UniProtKB.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
Gene3D; 1.20.120.180; -; 1.
Gene3D; 1.20.5.120; -; 1.
InterPro; IPR003186; PA28_C.
InterPro; IPR036997; PA28_C_sf.
InterPro; IPR036996; PA28_N_sf.
InterPro; IPR009077; Proteasome_activ_PA28.
InterPro; IPR003185; Proteasome_activ_PA28_N.
InterPro; IPR036252; Proteasome_activ_sf.
PANTHER; PTHR10660; PTHR10660; 1.
Pfam; PF02251; PA28_alpha; 1.
Pfam; PF02252; PA28_beta; 1.
SUPFAM; SSF47216; SSF47216; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; Cell cycle;
Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus;
Phosphoprotein; Proteasome; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.9}.
CHAIN 2 254 Proteasome activator complex subunit 3.
/FTId=PRO_0000161789.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.9}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 195 195 N6-acetyllysine; by P300/CBP.
{ECO:0000269|PubMed:23612972}.
MOD_RES 247 247 Phosphoserine; by CHEK2.
{ECO:0000269|PubMed:25361978}.
VAR_SEQ 1 13 MASLLKVDQEVKL -> MEKWILKKIKYLQSGGLSASYYSY
(in isoform 3). {ECO:0000305}.
/FTId=VSP_055047.
VAR_SEQ 135 135 T -> TPSGKGPHICFDLQ (in isoform 2).
{ECO:0000303|PubMed:7951316}.
/FTId=VSP_004516.
MUTAGEN 188 188 K->E,D,A,C,N,Q,H,F,S,I,P: Assembles into
less stable hexamers/heptamers and
therefore impairs specificity of
activation of trypsin-like subunits of
the proteasome.
{ECO:0000269|PubMed:11432824}.
CONFLICT 25 25 E -> K (in Ref. 2; AAB60335).
{ECO:0000305}.
CONFLICT 94 94 E -> K (in Ref. 10; AAA93227).
{ECO:0000305}.
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


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