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Proteasome subunit alpha type-3 (EC 3.4.25.1) (Macropain subunit C8) (Multicatalytic endopeptidase complex subunit C8) (Proteasome component C8)

 PSA3_HUMAN              Reviewed;         255 AA.
P25788; B2RCK6; Q86U83; Q8N1D8; Q9BS70;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
03-JUL-2019, entry version 222.
RecName: Full=Proteasome subunit alpha type-3;
EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
AltName: Full=Macropain subunit C8;
AltName: Full=Multicatalytic endopeptidase complex subunit C8;
AltName: Full=Proteasome component C8;
Name=PSMA3; Synonyms=HC8, PSC8;
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=2025653; DOI=10.1016/0167-4781(91)90090-9;
Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H.,
Tanaka K., Ichihara A.;
"Molecular cloning and sequence analysis of cDNAs for five major
subunits of human proteasomes (multi-catalytic proteinase
complexes).";
Biochim. Biophys. Acta 1089:95-102(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Bone marrow, Pancreas, and Urinary bladder;
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).
[6]
PROTEIN SEQUENCE OF 116-130.
PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
"Human proteasome subunits from 2-dimensional gels identified by
partial sequencing.";
Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
[7]
FUNCTION IN ANTIGEN PRESENTATION.
PubMed=8610016; DOI=10.1038/381166a0;
Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H.,
Rammensee H.G., Koszinowski U.H., Kloetzel P.M.;
"A role for the proteasome regulator PA28alpha in antigen
presentation.";
Nature 381:166-168(1996).
[8]
INDUCTION BY BO-653 AND PROBUCOL.
PubMed=11521686; DOI=10.5551/jat1994.7.223;
Takabe W., Mataki C., Wada Y., Ishii M., Izumi A., Aburatani H.,
Hamakubo T., Niki E., Kodama T., Noguchi N.;
"Gene expression induced by BO-653, probucol and BHQ in human
endothelial cells.";
J. Atheroscler. Thromb. 7:223-230(2000).
[9]
FUNCTION, AND INTERACTION WITH CDKN1A.
PubMed=11350925; DOI=10.1093/emboj/20.10.2367;
Touitou R., Richardson J., Bose S., Nakanishi M., Rivett J.,
Allday M.J.;
"A degradation signal located in the C-terminus of p21WAF1/CIP1 is a
binding site for the C8 alpha-subunit of the 20S proteasome.";
EMBO J. 20:2367-2375(2001).
[10]
SUBCELLULAR LOCATION.
PubMed=12181345; DOI=10.1091/mbc.E02-03-0122;
Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D.,
Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.;
"Clastosome: a subtype of nuclear body enriched in 19S and 20S
proteasomes, ubiquitin, and protein substrates of proteasome.";
Mol. Biol. Cell 13:2771-2782(2002).
[11]
ACETYLATION AT SER-2, AND PHOSPHORYLATION AT SER-250.
PubMed=12376572; DOI=10.1074/mcp.M200030-MCP200;
Claverol S., Burlet-Schiltz O., Girbal-Neuhauser E., Gairin J.E.,
Monsarrat B.;
"Mapping and structural dissection of human 20 s proteasome using
proteomic approaches.";
Mol. Cell. Proteomics 1:567-578(2002).
[12]
INDUCTION.
PubMed=12472671; DOI=10.1046/j.1365-3083.2002.01179.x;
Matsunaga T., Ishida T., Takekawa M., Nishimura S., Adachi M.,
Imai K.;
"Analysis of gene expression during maturation of immature dendritic
cells derived from peripheral blood monocytes.";
Scand. J. Immunol. 56:593-601(2002).
[13]
INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
Mayer R.J., Krueger E.;
"Human immunodeficiency virus-1 Tat protein interacts with distinct
proteasomal alpha and beta subunits.";
FEBS Lett. 553:200-204(2003).
[14]
INTERACTION WITH AURKB.
PubMed=14674694; DOI=10.1023/A:1027317014159;
Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C.,
Zhao S., Yu L.;
"Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes
degradation in a proteasome-dependent manner.";
Mol. Cell. Biochem. 254:157-162(2003).
[15]
FUNCTION.
PubMed=15244466; DOI=10.1021/bm049957a;
Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
"20S proteasome prevents aggregation of heat-denatured proteins
without PA700 regulatory subcomplex like a molecular chaperone.";
Biomacromolecules 5:1465-1469(2004).
[16]
INTERACTION WITH DNAJB2.
PubMed=15936278; DOI=10.1016/j.cub.2005.04.058;
Westhoff B., Chapple J.P., van der Spuy J., Hoehfeld J.,
Cheetham M.E.;
"HSJ1 is a neuronal shuttling factor for the sorting of chaperone
clients to the proteasome.";
Curr. Biol. 15:1058-1064(2005).
[17]
INTERACTION WITH EBNA3 (MICROBIAL INFECTION).
PubMed=15831937; DOI=10.1099/vir.0.80763-0;
Touitou R., O'Nions J., Heaney J., Allday M.J.;
"Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of
the 20S proteasome and are degraded by 20S proteasomes in vitro, but
are very stable in latently infected B cells.";
J. Gen. Virol. 86:1269-1277(2005).
[18]
INTERACTION WITH MDM2 AND RB1.
PubMed=16337594; DOI=10.1016/j.molcel.2005.10.017;
Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R.,
Allday M.J., Xiao Z.X.;
"MDM2 promotes proteasome-dependent ubiquitin-independent degradation
of retinoblastoma protein.";
Mol. Cell 20:699-708(2005).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[21]
INDUCTION BY BO-653.
PubMed=16298756; DOI=10.1080/10715760500354430;
Takabe W., Matsukawa N., Kodama T., Tanaka K., Noguchi N.;
"Chemical structure-dependent gene expression of proteasome subunits
via regulation of the antioxidant response element.";
Free Radic. Res. 40:21-30(2006).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-250, AND
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[25]
FUNCTION, AND INTERACTION WITH TBXA2R.
PubMed=17499743; DOI=10.1016/j.prostaglandins.2006.12.001;
Sasaki M., Sukegawa J., Miyosawa K., Yanagisawa T., Ohkubo S.,
Nakahata N.;
"Low expression of cell-surface thromboxane A2 receptor beta-isoform
through the negative regulation of its membrane traffic by
proteasomes.";
Prostaglandins Other Lipid Mediat. 83:237-249(2007).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, 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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[30]
INTERACTION WITH HCV F PROTEIN (MICROBIAL INFECTION).
PubMed=18971267; DOI=10.1128/JVI.00832-08;
Yuksek K., Chen W.-L., Chien D., Ou J.-H.;
"Ubiquitin-independent degradation of hepatitis C virus F protein.";
J. Virol. 83:612-621(2009).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND 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).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-206 AND LYS-230, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[34]
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).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND 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).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[37]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-250, 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).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[40]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=27176742; DOI=10.1515/hsz-2016-0176;
Rut W., Drag M.;
"Human 20S proteasome activity towards fluorogenic peptides of various
chain lengths.";
Biol. Chem. 397:921-926(2016).
[41]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=26133119; DOI=10.1038/ncomms8573;
da Fonseca P.C., Morris E.P.;
"Cryo-EM reveals the conformation of a substrate analogue in the human
20S proteasome core.";
Nat. Commun. 6:7573-7573(2015).
[42]
X-RAY CRYSTALLOGRAPHY (3.75 ANGSTROMS), AND SUBUNIT.
PubMed=26657688; DOI=10.1038/srep18167;
Ishii K., Noda M., Yagi H., Thammaporn R., Seetaha S., Satoh T.,
Kato K., Uchiyama S.;
"Disassembly of the self-assembled, double-ring structure of
proteasome alpha7 homo-tetradecamer by alpha6.";
Sci. Rep. 5:18167-18167(2015).
[43]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-246, AND SUBUNIT.
PubMed=25599644; DOI=10.1016/j.str.2014.11.017;
Harshbarger W., Miller C., Diedrich C., Sacchettini J.;
"Crystal structure of the human 20S proteasome in complex with
carfilzomib.";
Structure 23:418-424(2015).
[44]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[45]
STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), AND SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
[46]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
PubMed=27493187; DOI=10.1126/science.aaf8993;
Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
Stark H., Bourenkov G., Chari A.;
"The inhibition mechanism of human 20S proteasomes enables next-
generation inhibitor design.";
Science 353:594-598(2016).
[47]
VARIANT ARG-233 DEL, AND CHARACTERIZATION OF VARIANT ARG-233 DEL.
PubMed=26524591; DOI=10.1172/JCI81260;
Brehm A., Liu Y., Sheikh A., Marrero B., Omoyinmi E., Zhou Q.,
Montealegre G., Biancotto A., Reinhardt A., Almeida de Jesus A.,
Pelletier M., Tsai W.L., Remmers E.F., Kardava L., Hill S., Kim H.,
Lachmann H.J., Megarbane A., Chae J.J., Brady J., Castillo R.D.,
Brown D., Casano A.V., Gao L., Chapelle D., Huang Y., Stone D.,
Chen Y., Sotzny F., Lee C.C., Kastner D.L., Torrelo A.,
Zlotogorski A., Moir S., Gadina M., McCoy P., Wesley R., Rother K.,
Hildebrand P.W., Brogan P., Krueger E., Aksentijevich I.,
Goldbach-Mansky R.;
"Additive loss-of-function proteasome subunit mutations in
CANDLE/PRAAS patients promote type I IFN production.";
J. Clin. Invest. 125:4196-4211(2015).
-!- FUNCTION: Component of the 20S core proteasome complex involved in
the proteolytic degradation of most intracellular proteins. This
complex plays numerous essential roles within the cell by
associating with different regulatory particles. Associated with
two 19S regulatory particles, forms the 26S proteasome and thus
participates in the ATP-dependent degradation of ubiquitinated
proteins. The 26S proteasome plays a key role in the maintenance
of protein homeostasis by removing misfolded or damaged proteins
that could impair cellular functions, and by removing proteins
whose functions are no longer required. Associated with the PA200
or PA28, the 20S proteasome mediates ubiquitin-independent protein
degradation. This type of proteolysis is required in several
pathways including spermatogenesis (20S-PA200 complex) or
generation of a subset of MHC class I-presented antigenic peptides
(20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby
mediates its degradation. Negatively regulates the membrane
trafficking of the cell-surface thromboxane A2 receptor (TBXA2R)
isoform 2. {ECO:0000269|PubMed:11350925,
ECO:0000269|PubMed:14550573, ECO:0000269|PubMed:15244466,
ECO:0000269|PubMed:17499743, ECO:0000269|PubMed:27176742}.
-!- CATALYTIC ACTIVITY:
Reaction=Cleavage of peptide bonds with very broad specificity.;
EC=3.4.25.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00808,
ECO:0000269|PubMed:27176742};
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is a barrel-
shaped complex made of 28 subunits that are arranged in four
stacked rings. The two outer rings are each formed by seven alpha
subunits, and the two inner rings are formed by seven beta
subunits. The proteolytic activity is exerted by three beta-
subunits PSMB5, PSMB6 and PSMB7. Interacts with AURKB. Interacts
with CDKN1A (PubMed:11350925). Interacts with MDM2 and RB1
(PubMed:16337594). Interacts with the C-terminus of TBXA2R isoform
2 (PubMed:17499743). Interacts with DNAJB2 (PubMed:15936278).
{ECO:0000269|PubMed:11350925, ECO:0000269|PubMed:14674694,
ECO:0000269|PubMed:15936278, ECO:0000269|PubMed:16337594,
ECO:0000269|PubMed:17499743, ECO:0000269|PubMed:25599644,
ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:26657688,
ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
ECO:0000269|PubMed:27493187}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat protein.
{ECO:0000269|PubMed:14550573}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus
(HCV) F protein. {ECO:0000269|PubMed:18971267}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
EBNA3 proteins. {ECO:0000269|PubMed:15831937}.
-!- INTERACTION:
B2R550:-; NbExp=3; IntAct=EBI-348380, EBI-10175488;
Q5JPT6:-; NbExp=3; IntAct=EBI-348380, EBI-10244213;
Q5W150:-; NbExp=3; IntAct=EBI-348380, EBI-10248148;
Q7KZQ1:-; NbExp=3; IntAct=EBI-348380, EBI-10255941;
Q9H8E5:-; NbExp=3; IntAct=EBI-348380, EBI-10309031;
Q9HAA0:-; NbExp=3; IntAct=EBI-348380, EBI-10309885;
Q9NWL9:-; NbExp=3; IntAct=EBI-348380, EBI-10315054;
P27449:ATP6V0C; NbExp=3; IntAct=EBI-348380, EBI-721179;
Q8WVV5:BTN2A2; NbExp=3; IntAct=EBI-348380, EBI-8648738;
O95561:C1orf105; NbExp=3; IntAct=EBI-348380, EBI-10191951;
Q96CW7:C4orf42; NbExp=3; IntAct=EBI-348380, EBI-752053;
A2RU00:C9orf106; NbExp=3; IntAct=EBI-348380, EBI-10173129;
Q9NRJ3:CCL28; NbExp=3; IntAct=EBI-348380, EBI-7783254;
Q9BUF7:CRB3; NbExp=3; IntAct=EBI-348380, EBI-9844372;
P09228:CST2; NbExp=3; IntAct=EBI-348380, EBI-8832659;
Q7Z3D6:DGLUCY; NbExp=3; IntAct=EBI-348380, EBI-2807872;
Q14565:DMC1; NbExp=6; IntAct=EBI-348380, EBI-930865;
Q9NQL9:DMRT3; NbExp=3; IntAct=EBI-348380, EBI-9679045;
Q8N0U1:FAM171A2; NbExp=3; IntAct=EBI-348380, EBI-10264767;
Q96MZ4:FAM218A; NbExp=3; IntAct=EBI-348380, EBI-10291578;
Q96D16:FBXL18; NbExp=3; IntAct=EBI-348380, EBI-744419;
Q9Y3I1:FBXO7; NbExp=6; IntAct=EBI-348380, EBI-1161222;
P23769:GATA2; NbExp=3; IntAct=EBI-348380, EBI-2806671;
P23771:GATA3; NbExp=3; IntAct=EBI-348380, EBI-6664760;
Q9H8Y8:GORASP2; NbExp=3; IntAct=EBI-348380, EBI-739467;
Q8N779:hCG_1998195; NbExp=3; IntAct=EBI-348380, EBI-10267476;
A0A024R5S0:hCG_2003792; NbExp=3; IntAct=EBI-348380, EBI-10188461;
Q6IPM2:IQCE; NbExp=4; IntAct=EBI-348380, EBI-3893098;
Q6UWL6:KIRREL2; NbExp=3; IntAct=EBI-348380, EBI-10254473;
Q8N7Y1:KIRREL3-AS3; NbExp=3; IntAct=EBI-348380, EBI-10267656;
Q3LI72:KRTAP19-5; NbExp=3; IntAct=EBI-348380, EBI-1048945;
Q6PEX3:KRTAP26-1; NbExp=3; IntAct=EBI-348380, EBI-3957672;
Q8IUC2:KRTAP8-1; NbExp=3; IntAct=EBI-348380, EBI-10261141;
Q14847:LASP1; NbExp=3; IntAct=EBI-348380, EBI-742828;
O95202:LETM1; NbExp=3; IntAct=EBI-348380, EBI-1052895;
Q00987:MDM2; NbExp=2; IntAct=EBI-348380, EBI-389668;
Q96PC5:MIA2; NbExp=3; IntAct=EBI-348380, EBI-1050253;
Q9H6H2:MUM1; NbExp=3; IntAct=EBI-348380, EBI-10307610;
P48146:NPBWR2; NbExp=3; IntAct=EBI-348380, EBI-10210114;
P16860:NPPB; NbExp=3; IntAct=EBI-348380, EBI-747044;
Q8N2R0:OSR2; NbExp=3; IntAct=EBI-348380, EBI-5660512;
Q86TB9:PATL1; NbExp=3; IntAct=EBI-348380, EBI-2562092;
Q58A44:PCOTH; NbExp=3; IntAct=EBI-348380, EBI-10243387;
P29590:PML; NbExp=2; IntAct=EBI-348380, EBI-295890;
Q14CW7:PRR10; NbExp=3; IntAct=EBI-348380, EBI-10234793;
Q9NZ81:PRR13; NbExp=3; IntAct=EBI-348380, EBI-740924;
P79522:PRR3; NbExp=3; IntAct=EBI-348380, EBI-2803328;
P25786:PSMA1; NbExp=13; IntAct=EBI-348380, EBI-359352;
P25789:PSMA4; NbExp=4; IntAct=EBI-348380, EBI-359310;
P60900:PSMA6; NbExp=9; IntAct=EBI-348380, EBI-357793;
O14818:PSMA7; NbExp=6; IntAct=EBI-348380, EBI-603272;
P28070:PSMB4; NbExp=3; IntAct=EBI-348380, EBI-603350;
Q9H3S7:PTPN23; NbExp=3; IntAct=EBI-348380, EBI-724478;
Q6NUJ5:PWWP2B; NbExp=3; IntAct=EBI-348380, EBI-10251192;
Q8TBN0:RAB3IL1; NbExp=3; IntAct=EBI-348380, EBI-743796;
Q9Y4B4:RAD54L2; NbExp=3; IntAct=EBI-348380, EBI-948156;
Q9BTL3:RAMAC; NbExp=3; IntAct=EBI-348380, EBI-744023;
O43251:RBFOX2; NbExp=3; IntAct=EBI-348380, EBI-746056;
Q9BTD8:RBM42; NbExp=3; IntAct=EBI-348380, EBI-746862;
Q14D33:RTP5; NbExp=3; IntAct=EBI-348380, EBI-10217913;
Q66K80:RUSC1-AS1; NbExp=3; IntAct=EBI-348380, EBI-10248967;
Q15637:SF1; NbExp=3; IntAct=EBI-348380, EBI-744603;
Q8ND83:SLAIN1; NbExp=3; IntAct=EBI-348380, EBI-10269374;
Q7L9D0:SLC22A23; NbExp=3; IntAct=EBI-348380, EBI-10256583;
P14678-2:SNRPB; NbExp=3; IntAct=EBI-348380, EBI-372475;
Q5TAL4:SNRPC; NbExp=3; IntAct=EBI-348380, EBI-10246938;
Q6RVD6:SPATA8; NbExp=3; IntAct=EBI-348380, EBI-8635958;
Q12846:STX4; NbExp=3; IntAct=EBI-348380, EBI-744942;
O43752:STX6; NbExp=3; IntAct=EBI-348380, EBI-2695795;
Q96HZ7:URB1-AS1; NbExp=3; IntAct=EBI-348380, EBI-10288943;
A5D8V6:VPS37C; NbExp=3; IntAct=EBI-348380, EBI-2559305;
Q8N895:ZNF366; NbExp=3; IntAct=EBI-348380, EBI-2813661;
Q66K41:ZNF385C; NbExp=4; IntAct=EBI-348380, EBI-8651919;
A0A0S2Z5X4:ZNF688; NbExp=3; IntAct=EBI-348380, EBI-16429014;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}.
Nucleus {ECO:0000269|PubMed:12181345}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P25788-1; Sequence=Displayed;
Name=2;
IsoId=P25788-2; Sequence=VSP_005280;
-!- INDUCTION: Down-regulated by antioxidants BO-653 and probucol. Up-
regulated by bacterial lipopolysaccharides (LPS) and TNF.
{ECO:0000269|PubMed:11521686, ECO:0000269|PubMed:12472671,
ECO:0000269|PubMed:16298756}.
-!- SIMILARITY: Belongs to the peptidase T1A family.
{ECO:0000255|PROSITE-ProRule:PRU00808}.
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EMBL; D00762; BAA00659.1; -; mRNA.
EMBL; BT006711; AAP35357.1; -; mRNA.
EMBL; BT019715; AAV38520.1; -; mRNA.
EMBL; AK315158; BAG37603.1; -; mRNA.
EMBL; CH471061; EAW80719.1; -; Genomic_DNA.
EMBL; BC005265; AAH05265.1; -; mRNA.
EMBL; BC029402; AAH29402.1; -; mRNA.
EMBL; BC038990; AAH38990.1; -; mRNA.
CCDS; CCDS45113.1; -. [P25788-2]
CCDS; CCDS9731.1; -. [P25788-1]
PIR; S15971; SNHUC8.
RefSeq; NP_002779.1; NM_002788.3. [P25788-1]
RefSeq; NP_687033.1; NM_152132.2. [P25788-2]
PDB; 4R3O; X-ray; 2.60 A; G/U=2-246.
PDB; 4R67; X-ray; 2.89 A; G/U/i/w=2-246.
PDB; 5A0Q; EM; 3.50 A; G/U=1-255.
PDB; 5DSV; X-ray; 3.75 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-255.
PDB; 5GJQ; EM; 4.50 A; X/n=1-255.
PDB; 5GJR; EM; 3.50 A; X/n=1-255.
PDB; 5L4G; EM; 4.02 A; G/T=1-255.
PDB; 5LE5; X-ray; 1.80 A; F/T=1-255.
PDB; 5LEX; X-ray; 2.20 A; F/T=1-255.
PDB; 5LEY; X-ray; 1.90 A; F/T=1-255.
PDB; 5LEZ; X-ray; 2.19 A; F/T=1-255.
PDB; 5LF0; X-ray; 2.41 A; F/T=1-255.
PDB; 5LF1; X-ray; 2.00 A; F/T=1-255.
PDB; 5LF3; X-ray; 2.10 A; F/T=1-255.
PDB; 5LF4; X-ray; 1.99 A; F/T=1-255.
PDB; 5LF6; X-ray; 2.07 A; F/T=1-255.
PDB; 5LF7; X-ray; 2.00 A; F/T=1-255.
PDB; 5LN3; EM; 6.80 A; G=1-255.
PDB; 5M32; EM; 3.80 A; F/T=1-255.
PDB; 5T0C; EM; 3.80 A; AM/BM=2-255.
PDB; 5T0G; EM; 4.40 A; M=2-255.
PDB; 5T0H; EM; 6.80 A; M=2-255.
PDB; 5T0I; EM; 8.00 A; M=2-255.
PDB; 5T0J; EM; 8.00 A; M=2-255.
PDB; 5VFO; EM; 3.50 A; M/m=2-246.
PDB; 5VFP; EM; 4.20 A; M/m=2-246.
PDB; 5VFQ; EM; 4.20 A; M/m=2-246.
PDB; 5VFR; EM; 4.90 A; M/m=2-246.
PDB; 5VFS; EM; 3.60 A; M/m=2-246.
PDB; 5VFT; EM; 7.00 A; M/m=2-246.
PDB; 5VFU; EM; 5.80 A; M/m=2-246.
PDB; 6AVO; EM; 3.80 A; J/Q=1-255.
PDB; 6MSB; EM; 3.00 A; M/m=2-255.
PDB; 6MSD; EM; 3.20 A; M/m=2-255.
PDB; 6MSE; EM; 3.30 A; a=166-213.
PDB; 6MSG; EM; 3.50 A; M/m=2-255.
PDB; 6MSH; EM; 3.60 A; M/m=2-255.
PDB; 6MSJ; EM; 3.30 A; M/m=2-255.
PDB; 6MSK; EM; 3.20 A; M/m=2-255.
PDBsum; 4R3O; -.
PDBsum; 4R67; -.
PDBsum; 5A0Q; -.
PDBsum; 5DSV; -.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4G; -.
PDBsum; 5LE5; -.
PDBsum; 5LEX; -.
PDBsum; 5LEY; -.
PDBsum; 5LEZ; -.
PDBsum; 5LF0; -.
PDBsum; 5LF1; -.
PDBsum; 5LF3; -.
PDBsum; 5LF4; -.
PDBsum; 5LF6; -.
PDBsum; 5LF7; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 5VFO; -.
PDBsum; 5VFP; -.
PDBsum; 5VFQ; -.
PDBsum; 5VFR; -.
PDBsum; 5VFS; -.
PDBsum; 5VFT; -.
PDBsum; 5VFU; -.
PDBsum; 6AVO; -.
PDBsum; 6MSB; -.
PDBsum; 6MSD; -.
PDBsum; 6MSE; -.
PDBsum; 6MSG; -.
PDBsum; 6MSH; -.
PDBsum; 6MSJ; -.
PDBsum; 6MSK; -.
SMR; P25788; -.
BioGrid; 111657; 307.
CORUM; P25788; -.
DIP; DIP-29366N; -.
IntAct; P25788; 127.
MINT; P25788; -.
STRING; 9606.ENSP00000216455; -.
BindingDB; P25788; -.
ChEMBL; CHEMBL2364701; -.
ChEMBL; CHEMBL3831201; -.
MEROPS; T01.977; -.
MoonDB; P25788; Predicted.
iPTMnet; P25788; -.
PhosphoSitePlus; P25788; -.
SwissPalm; P25788; -.
BioMuta; PSMA3; -.
DMDM; 130859; -.
OGP; P25788; -.
REPRODUCTION-2DPAGE; IPI00171199; -.
EPD; P25788; -.
jPOST; P25788; -.
MaxQB; P25788; -.
PaxDb; P25788; -.
PeptideAtlas; P25788; -.
PRIDE; P25788; -.
ProteomicsDB; 54290; -.
ProteomicsDB; 54291; -. [P25788-2]
DNASU; 5684; -.
Ensembl; ENST00000216455; ENSP00000216455; ENSG00000100567. [P25788-1]
Ensembl; ENST00000412908; ENSP00000390491; ENSG00000100567. [P25788-2]
GeneID; 5684; -.
KEGG; hsa:5684; -.
UCSC; uc001xdj.3; human. [P25788-1]
CTD; 5684; -.
DisGeNET; 5684; -.
GeneCards; PSMA3; -.
H-InvDB; HIX0155215; -.
HGNC; HGNC:9532; PSMA3.
HPA; HPA000905; -.
MIM; 176843; gene.
MIM; 176845; gene.
neXtProt; NX_P25788; -.
OpenTargets; ENSG00000100567; -.
PharmGKB; PA33877; -.
eggNOG; KOG0184; Eukaryota.
eggNOG; ENOG410XP01; LUCA.
GeneTree; ENSGT00550000074912; -.
HOGENOM; HOG000091086; -.
InParanoid; P25788; -.
KO; K02727; -.
OMA; SMYMHAY; -.
OrthoDB; 1222564at2759; -.
PhylomeDB; P25788; -.
TreeFam; TF106208; -.
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-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-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
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-9020702; Interleukin-1 signaling.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; P25788; -.
GeneWiki; PSMA3; -.
GenomeRNAi; 5684; -.
PRO; PR:P25788; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100567; Expressed in 232 organ(s), highest expression level in adenohypophysis.
ExpressionAtlas; P25788; baseline and differential.
Genevisible; P25788; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0005839; C:proteasome core complex; IDA:BHF-UCL.
GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
GO; GO:0045202; C:synapse; IBA:GO_Central.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ARUK-UCL.
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:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0070498; P:interleukin-1-mediated 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:0010972; P:negative regulation of G2/M transition of 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:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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:0052548; P:regulation of endopeptidase activity; IMP:UniProtKB.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
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:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR023332; Proteasome_alpha-type.
InterPro; IPR037555; Proteasome_alpha_3.
InterPro; IPR000426; Proteasome_asu_N.
InterPro; IPR001353; Proteasome_sua/b.
PANTHER; PTHR11599:SF10; PTHR11599:SF10; 1.
Pfam; PF00227; Proteasome; 1.
Pfam; PF10584; Proteasome_A_N; 1.
SMART; SM00948; Proteasome_A_N; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Host-virus interaction;
Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Protease;
Proteasome; Reference proteome; Threonine protease.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12376572}.
CHAIN 2 255 Proteasome subunit alpha type-3.
/FTId=PRO_0000124091.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12376572}.
MOD_RES 57 57 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 206 206 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 230 230 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000244|PubMed:17323924,
ECO:0000244|PubMed:23186163}.
MOD_RES 250 250 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17323924,
ECO:0000244|PubMed:17487921,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:12376572}.
VAR_SEQ 136 142 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_005280.
VARIANT 233 233 Missing (found in a patient with Nakajo
syndrome who also carries a mutation in
PSMB8; unknown pathological significance;
patients' cells show reduction of
proteasome content and endopeptidase
activity of the proteasome).
{ECO:0000269|PubMed:26524591}.
/FTId=VAR_075259.
CONFLICT 91 91 I -> M (in Ref. 5; AAH29402).
{ECO:0000305}.
STRAND 11 14 {ECO:0000244|PDB:5A0Q}.
STRAND 17 19 {ECO:0000244|PDB:5VFO}.
HELIX 22 32 {ECO:0000244|PDB:5LE5}.
STRAND 37 42 {ECO:0000244|PDB:5LE5}.
STRAND 45 53 {ECO:0000244|PDB:5LE5}.
TURN 61 64 {ECO:0000244|PDB:5LE5}.
STRAND 67 71 {ECO:0000244|PDB:5LE5}.
STRAND 74 80 {ECO:0000244|PDB:5LE5}.
HELIX 82 103 {ECO:0000244|PDB:5LE5}.
HELIX 109 122 {ECO:0000244|PDB:5LE5}.
STRAND 124 129 {ECO:0000244|PDB:4R3O}.
STRAND 133 142 {ECO:0000244|PDB:5LE5}.
TURN 143 145 {ECO:0000244|PDB:5LE5}.
STRAND 146 152 {ECO:0000244|PDB:5LE5}.
STRAND 158 167 {ECO:0000244|PDB:5LE5}.
HELIX 170 177 {ECO:0000244|PDB:5LE5}.
HELIX 182 184 {ECO:0000244|PDB:5LE5}.
HELIX 187 201 {ECO:0000244|PDB:5LE5}.
TURN 204 206 {ECO:0000244|PDB:5LE5}.
STRAND 210 218 {ECO:0000244|PDB:5LE5}.
HELIX 219 221 {ECO:0000244|PDB:5LE5}.
STRAND 225 227 {ECO:0000244|PDB:4R67}.
HELIX 230 244 {ECO:0000244|PDB:5LE5}.
SEQUENCE 255 AA; 28433 MW; A1854ED3C0650FB1 CRC64;
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE
EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV
HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL
QMKEMTCRDI VKEVAKIIYI VHDEVKDKAF ELELSWVGEL TNGRHEIVPK DIREEAEKYA
KESLKEEDES DDDNM


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EIAAB32707 Lmpc3,Macropain subunit C3,Mouse,Multicatalytic endopeptidase complex subunit C3,Mus musculus,Proteasome component C3,Proteasome subunit alpha type-2,Psma2
EIAAB32708 HC3,Homo sapiens,Human,Macropain subunit C3,Multicatalytic endopeptidase complex subunit C3,Proteasome component C3,Proteasome subunit alpha type-2,PSC3,PSMA2
EIAAB32712 HC8,Homo sapiens,Human,Macropain subunit C8,Multicatalytic endopeptidase complex subunit C8,Proteasome component C8,Proteasome subunit alpha type-3,PSC8,PSMA3
EIAAB32737 Macropain subunit C5,Mouse,Multicatalytic endopeptidase complex subunit C5,Mus musculus,Proteasome component C5,Proteasome gamma chain,Proteasome subunit beta type-1,Psmb1
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Pathways :
WP2272: Pathogenic Escherichia coli infection
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP1566: Citrate cycle (TCA cycle)
WP1663: Homologous recombination
WP1680: Oxidative phosphorylation
WP1693: Purine metabolism
WP1626: Benzoate degradation via CoA ligation
WP470: Proteasome Degradation
WP1672: Mismatch repair
WP1711: Trinitrotoluene degradation
WP2292: Chemokine signaling pathway
WP1644: DNA replication
WP1671: Methane metabolism
WP1694: Pyrimidine metabolism
WP1718: Vitamin B6 metabolism
WP1634: Butanoate metabolism
WP519: Proteasome Degradation
WP267: Proteasome Degradation
WP158: Proteasome Degradation
WP1224: EBV LMP1 signaling
WP281: Proteasome Degradation
WP183: Proteasome Degradation
WP1571: EBV LMP1 signaling
WP1209: EBV LMP1 signaling

Related Genes :
[PSMA3 HC8 PSC8] Proteasome subunit alpha type-3 (EC 3.4.25.1) (Macropain subunit C8) (Multicatalytic endopeptidase complex subunit C8) (Proteasome component C8)
[Psma3] Proteasome subunit alpha type-3 (EC 3.4.25.1) (Macropain subunit C8) (Multicatalytic endopeptidase complex subunit C8) (Proteasome component C8) (Proteasome subunit K)
[Psma3] Proteasome subunit alpha type-3 (EC 3.4.25.1) (Macropain subunit C8) (Multicatalytic endopeptidase complex subunit C8) (Proteasome component C8) (Proteasome subunit K)
[Psma1] Proteasome subunit alpha type-1 (EC 3.4.25.1) (Macropain subunit C2) (Multicatalytic endopeptidase complex subunit C2) (Proteasome component C2) (Proteasome nu chain)
[Psma2] Proteasome subunit alpha type-2 (EC 3.4.25.1) (Macropain subunit C3) (Multicatalytic endopeptidase complex subunit C3) (Proteasome component C3)
[SCL1 PRC2 PRS2 YGL011C] Proteasome subunit alpha type-1 (EC 3.4.25.1) (Macropain subunit C7-alpha) (Multicatalytic endopeptidase complex C7) (Proteasome component C7-alpha) (Proteasome component Y8) (Proteinase YSCE subunit 7) (SCL1 suppressor protein)
[PRE9 PRS5 YGR135W] Proteasome subunit alpha type-3 (EC 3.4.25.1) (Macropain subunit Y13) (Multicatalytic endopeptidase complex subunit Y13) (Proteasome component Y13) (Proteinase YSCE subunit 13)
[PRE8 PRS4 YML092C] Proteasome subunit alpha type-2 (EC 3.4.25.1) (Macropain subunit Y7) (Multicatalytic endopeptidase complex subunit Y7) (Proteasome component Y7) (Proteinase YSCE subunit 7)
[Psma1] Proteasome subunit alpha type-1 (EC 3.4.25.1) (Macropain subunit C2) (Multicatalytic endopeptidase complex subunit C2) (Proteasome component C2) (Proteasome nu chain)
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[PRE6 YOL038W] Proteasome subunit alpha type-4 (EC 3.4.25.1) (Macropain subunit PRE6) (Multicatalytic endopeptidase complex subunit PRE6) (Proteasome component PRE6) (Proteinase YSCE subunit PRE6)
[PUP2 DOA5 YGR253C G9155] Proteasome subunit alpha type-5 (EC 3.4.25.1) (Macropain subunit PUP2) (Multicatalytic endopeptidase complex subunit PUP2) (Proteasome component PUP2) (Proteinase YSCE subunit PUP2)
[PRE5 YMR314W YM9924.06] Proteasome subunit alpha type-6 (EC 3.4.25.1) (Macropain subunit PRE5) (Multicatalytic endopeptidase complex subunit PRE5) (Proteasome component PRE5) (Proteinase YSCE subunit PRE5)
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[PSMA4 HC9 PSC9] Proteasome subunit alpha type-4 (EC 3.4.25.1) (Macropain subunit C9) (Multicatalytic endopeptidase complex subunit C9) (Proteasome component C9) (Proteasome subunit L)
[PSMA2 HC3 PSC3] Proteasome subunit alpha type-2 (EC 3.4.25.1) (Macropain subunit C3) (Multicatalytic endopeptidase complex subunit C3) (Proteasome component C3)
[PRE3 YJL001W J1407] Proteasome subunit beta type-1 (EC 3.4.25.1) (Macropain subunit PRE3) (Multicatalytic endopeptidase complex subunit PRE3) (Proteasome component PRE3) (Proteinase YSCE subunit PRE3)
[PRE1 YER012W] Proteasome subunit beta type-4 (EC 3.4.25.1) (Macropain subunit C11) (Multicatalytic endopeptidase complex subunit C11) (Proteasome component C11) (Proteinase YSCE subunit 11)
[PRE4 YFR050C] Proteasome subunit beta type-7 (EC 3.4.25.1) (Macropain subunit PRE4) (Multicatalytic endopeptidase complex subunit PRE4) (Proteasome component PRE4) (Proteinase YSCE subunit PRE4)
[PUP3 YER094C] Proteasome subunit beta type-3 (EC 3.4.25.1) (Macropain subunit PUP3) (Multicatalytic endopeptidase complex subunit PUP3) (Proteasome component PUP3)
[PRE2 DOA3 PRG1 YPR103W P8283.10] Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain subunit PRE2) (Multicatalytic endopeptidase complex subunit PRE2) (Proteasome component PRE2) (Proteinase YSCE subunit PRE2)
[PUP1 YOR157C] Proteasome subunit beta type-2 (EC 3.4.25.1) (Macropain subunit PUP1) (Multicatalytic endopeptidase complex subunit PUP1) (Proteasome component PUP1) (Proteinase YSCE subunit PUP1)
[Psma2 Lmpc3] Proteasome subunit alpha type-2 (EC 3.4.25.1) (Macropain subunit C3) (Multicatalytic endopeptidase complex subunit C3) (Proteasome component C3)
[PSMB10 LMP10 MECL1] Proteasome subunit beta type-10 (EC 3.4.25.1) (Low molecular mass protein 10) (Macropain subunit MECl-1) (Multicatalytic endopeptidase complex subunit MECl-1) (Proteasome MECl-1) (Proteasome subunit beta-2i)
[PSMB1 PSC5] Proteasome subunit beta type-1 (EC 3.4.25.1) (Macropain subunit C5) (Multicatalytic endopeptidase complex subunit C5) (Proteasome component C5) (Proteasome gamma chain)
[PSMB9 LMP2 PSMB6i RING12] Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
[Psma4] Proteasome subunit alpha type-4 (EC 3.4.25.1) (Macropain subunit C9) (Multicatalytic endopeptidase complex subunit C9) (Proteasome component C9) (Proteasome subunit L)
[Psmb10 Lmp10 Mecl1] Proteasome subunit beta type-10 (EC 3.4.25.1) (Low molecular mass protein 10) (Macropain subunit MECl-1) (Multicatalytic endopeptidase complex subunit MECl-1) (Proteasome MECl-1) (Proteasome subunit beta-2i)

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