PSA3_HUMAN
ID PSA3_HUMAN Reviewed; 255 AA.
AC P25788; B2RCK6; Q86U83; Q8N1D8; Q9BS70;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 240.
DE RecName: Full=Proteasome subunit alpha type-3;
DE AltName: Full=Macropain subunit C8;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C8;
DE AltName: Full=Proteasome component C8;
GN Name=PSMA3; Synonyms=HC8, PSC8;
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=2025653; DOI=10.1016/0167-4781(91)90090-9;
RA Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K.,
RA Ichihara A.;
RT "Molecular cloning and sequence analysis of cDNAs for five major subunits
RT of human proteasomes (multi-catalytic proteinase complexes).";
RL Biochim. Biophys. Acta 1089:95-102(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Pancreas, and Urinary bladder;
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 [6]
RP PROTEIN SEQUENCE OF 116-130.
RX PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
RA Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
RT "Human proteasome subunits from 2-dimensional gels identified by partial
RT sequencing.";
RL Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
RN [7]
RP FUNCTION IN ANTIGEN PRESENTATION.
RX PubMed=8610016; DOI=10.1038/381166a0;
RA Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H.,
RA Rammensee H.G., Koszinowski U.H., Kloetzel P.M.;
RT "A role for the proteasome regulator PA28alpha in antigen presentation.";
RL Nature 381:166-168(1996).
RN [8]
RP INDUCTION BY BO-653 AND PROBUCOL.
RX PubMed=11521686; DOI=10.5551/jat1994.7.223;
RA Takabe W., Mataki C., Wada Y., Ishii M., Izumi A., Aburatani H.,
RA Hamakubo T., Niki E., Kodama T., Noguchi N.;
RT "Gene expression induced by BO-653, probucol and BHQ in human endothelial
RT cells.";
RL J. Atheroscler. Thromb. 7:223-230(2000).
RN [9]
RP FUNCTION, AND INTERACTION WITH CDKN1A.
RX PubMed=11350925; DOI=10.1093/emboj/20.10.2367;
RA Touitou R., Richardson J., Bose S., Nakanishi M., Rivett J., Allday M.J.;
RT "A degradation signal located in the C-terminus of p21WAF1/CIP1 is a
RT binding site for the C8 alpha-subunit of the 20S proteasome.";
RL EMBO J. 20:2367-2375(2001).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=12181345; DOI=10.1091/mbc.e02-03-0122;
RA Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D.,
RA Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.;
RT "Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes,
RT ubiquitin, and protein substrates of proteasome.";
RL Mol. Biol. Cell 13:2771-2782(2002).
RN [11]
RP ACETYLATION AT SER-2, AND PHOSPHORYLATION AT SER-250.
RX PubMed=12376572; DOI=10.1074/mcp.m200030-mcp200;
RA Claverol S., Burlet-Schiltz O., Girbal-Neuhauser E., Gairin J.E.,
RA Monsarrat B.;
RT "Mapping and structural dissection of human 20 s proteasome using proteomic
RT approaches.";
RL Mol. Cell. Proteomics 1:567-578(2002).
RN [12]
RP INDUCTION.
RX PubMed=12472671; DOI=10.1046/j.1365-3083.2002.01179.x;
RA Matsunaga T., Ishida T., Takekawa M., Nishimura S., Adachi M., Imai K.;
RT "Analysis of gene expression during maturation of immature dendritic cells
RT derived from peripheral blood monocytes.";
RL Scand. J. Immunol. 56:593-601(2002).
RN [13]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RX PubMed=14550573; DOI=10.1016/s0014-5793(03)01025-1;
RA Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA Mayer R.J., Krueger E.;
RT "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT proteasomal alpha and beta subunits.";
RL FEBS Lett. 553:200-204(2003).
RN [14]
RP INTERACTION WITH AURKB.
RX PubMed=14674694; DOI=10.1023/a:1027317014159;
RA Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C., Zhao S.,
RA Yu L.;
RT "Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes
RT degradation in a proteasome-dependent manner.";
RL Mol. Cell. Biochem. 254:157-162(2003).
RN [15]
RP FUNCTION.
RX PubMed=15244466; DOI=10.1021/bm049957a;
RA Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
RT "20S proteasome prevents aggregation of heat-denatured proteins without
RT PA700 regulatory subcomplex like a molecular chaperone.";
RL Biomacromolecules 5:1465-1469(2004).
RN [16]
RP INTERACTION WITH DNAJB2.
RX PubMed=15936278; DOI=10.1016/j.cub.2005.04.058;
RA Westhoff B., Chapple J.P., van der Spuy J., Hoehfeld J., Cheetham M.E.;
RT "HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients
RT to the proteasome.";
RL Curr. Biol. 15:1058-1064(2005).
RN [17]
RP INTERACTION WITH EBNA3 (MICROBIAL INFECTION).
RX PubMed=15831937; DOI=10.1099/vir.0.80763-0;
RA Touitou R., O'Nions J., Heaney J., Allday M.J.;
RT "Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of the 20S
RT proteasome and are degraded by 20S proteasomes in vitro, but are very
RT stable in latently infected B cells.";
RL J. Gen. Virol. 86:1269-1277(2005).
RN [18]
RP INTERACTION WITH MDM2 AND RB1.
RX PubMed=16337594; DOI=10.1016/j.molcel.2005.10.017;
RA Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R., Allday M.J.,
RA Xiao Z.X.;
RT "MDM2 promotes proteasome-dependent ubiquitin-independent degradation of
RT retinoblastoma protein.";
RL Mol. Cell 20:699-708(2005).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [21]
RP INDUCTION BY BO-653.
RX PubMed=16298756; DOI=10.1080/10715760500354430;
RA Takabe W., Matsukawa N., Kodama T., Tanaka K., Noguchi N.;
RT "Chemical structure-dependent gene expression of proteasome subunits via
RT regulation of the antioxidant response element.";
RL Free Radic. Res. 40:21-30(2006).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-250, AND
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [25]
RP FUNCTION, AND INTERACTION WITH TBXA2R.
RX PubMed=17499743; DOI=10.1016/j.prostaglandins.2006.12.001;
RA Sasaki M., Sukegawa J., Miyosawa K., Yanagisawa T., Ohkubo S., Nakahata N.;
RT "Low expression of cell-surface thromboxane A2 receptor beta-isoform
RT through the negative regulation of its membrane traffic by proteasomes.";
RL Prostaglandins Other Lipid Mediat. 83:237-249(2007).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [29]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [30]
RP INTERACTION WITH HCV F PROTEIN (MICROBIAL INFECTION).
RX PubMed=18971267; DOI=10.1128/jvi.00832-08;
RA Yuksek K., Chen W.-L., Chien D., Ou J.-H.;
RT "Ubiquitin-independent degradation of hepatitis C virus F protein.";
RL J. Virol. 83:612-621(2009).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP 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 [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-206 AND LYS-230, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [34]
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 [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP 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 [36]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [37]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-250, AND
RP IDENTIFICATION BY 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 [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [40]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27176742; DOI=10.1515/hsz-2016-0176;
RA Rut W., Drag M.;
RT "Human 20S proteasome activity towards fluorogenic peptides of various
RT chain lengths.";
RL Biol. Chem. 397:921-926(2016).
RN [41]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
RX PubMed=26133119; DOI=10.1038/ncomms8573;
RA da Fonseca P.C., Morris E.P.;
RT "Cryo-EM reveals the conformation of a substrate analogue in the human 20S
RT proteasome core.";
RL Nat. Commun. 6:7573-7573(2015).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (3.75 ANGSTROMS), AND SUBUNIT.
RX PubMed=26657688; DOI=10.1038/srep18167;
RA Ishii K., Noda M., Yagi H., Thammaporn R., Seetaha S., Satoh T., Kato K.,
RA Uchiyama S.;
RT "Disassembly of the self-assembled, double-ring structure of proteasome
RT alpha7 homo-tetradecamer by alpha6.";
RL Sci. Rep. 5:18167-18167(2015).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-246, AND SUBUNIT.
RX PubMed=25599644; DOI=10.1016/j.str.2014.11.017;
RA Harshbarger W., Miller C., Diedrich C., Sacchettini J.;
RT "Crystal structure of the human 20S proteasome in complex with
RT carfilzomib.";
RL Structure 23:418-424(2015).
RN [44]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
RX PubMed=27428775; DOI=10.1038/nsmb.3273;
RA Huang X., Luan B., Wu J., Shi Y.;
RT "An atomic structure of the human 26S proteasome.";
RL Nat. Struct. Mol. Biol. 23:778-785(2016).
RN [45]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), AND SUBUNIT.
RX PubMed=27342858; DOI=10.1073/pnas.1608050113;
RA Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
RA Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
RT "Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
RX PubMed=27493187; DOI=10.1126/science.aaf8993;
RA Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
RA Stark H., Bourenkov G., Chari A.;
RT "The inhibition mechanism of human 20S proteasomes enables next-generation
RT inhibitor design.";
RL Science 353:594-598(2016).
RN [47]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH AKIRIN2,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=34711951; DOI=10.1038/s41586-021-04035-8;
RA de Almeida M., Hinterndorfer M., Brunner H., Grishkovskaya I., Singh K.,
RA Schleiffer A., Jude J., Deswal S., Kalis R., Vunjak M., Lendl T., Imre R.,
RA Roitinger E., Neumann T., Kandolf S., Schutzbier M., Mechtler K.,
RA Versteeg G.A., Haselbach D., Zuber J.;
RT "AKIRIN2 controls the nuclear import of proteasomes in vertebrates.";
RL Nature 599:491-496(2021).
RN [48]
RP VARIANT ARG-233 DEL, AND CHARACTERIZATION OF VARIANT ARG-233 DEL.
RX PubMed=26524591; DOI=10.1172/jci81260;
RA Brehm A., Liu Y., Sheikh A., Marrero B., Omoyinmi E., Zhou Q.,
RA Montealegre G., Biancotto A., Reinhardt A., Almeida de Jesus A.,
RA Pelletier M., Tsai W.L., Remmers E.F., Kardava L., Hill S., Kim H.,
RA Lachmann H.J., Megarbane A., Chae J.J., Brady J., Castillo R.D., Brown D.,
RA Casano A.V., Gao L., Chapelle D., Huang Y., Stone D., Chen Y., Sotzny F.,
RA Lee C.C., Kastner D.L., Torrelo A., Zlotogorski A., Moir S., Gadina M.,
RA McCoy P., Wesley R., Rother K., Hildebrand P.W., Brogan P., Krueger E.,
RA Aksentijevich I., Goldbach-Mansky R.;
RT "Additive loss-of-function proteasome subunit mutations in CANDLE/PRAAS
RT patients promote type I IFN production.";
RL J. Clin. Invest. 125:4196-4211(2015).
CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC proteolytic degradation of most intracellular proteins. This complex
CC plays numerous essential roles within the cell by associating with
CC different regulatory particles. Associated with two 19S regulatory
CC particles, forms the 26S proteasome and thus participates in the ATP-
CC dependent degradation of ubiquitinated proteins. The 26S proteasome
CC plays a key role in the maintenance of protein homeostasis by removing
CC misfolded or damaged proteins that could impair cellular functions, and
CC by removing proteins whose functions are no longer required. Associated
CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC independent protein degradation. This type of proteolysis is required
CC in several pathways including spermatogenesis (20S-PA200 complex) or
CC generation of a subset of MHC class I-presented antigenic peptides
CC (20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby
CC mediates its degradation. Negatively regulates the membrane trafficking
CC of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.
CC {ECO:0000269|PubMed:11350925, ECO:0000269|PubMed:14550573,
CC ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:17499743,
CC ECO:0000269|PubMed:27176742}.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits (PubMed:25599644, PubMed:26133119,
CC PubMed:26657688, PubMed:27342858, PubMed:27428775, PubMed:27493187,
CC PubMed:34711951). The 20S proteasome core is a barrel-shaped complex
CC made of 28 subunits that are arranged in four stacked rings
CC (PubMed:25599644, PubMed:26133119, PubMed:26657688, PubMed:27342858,
CC PubMed:27428775, PubMed:27493187, PubMed:34711951). The two outer rings
CC are each formed by seven alpha subunits, and the two inner rings are
CC formed by seven beta subunits (PubMed:25599644, PubMed:26133119,
CC PubMed:26657688, PubMed:27342858, PubMed:27428775, PubMed:27493187,
CC PubMed:34711951). The proteolytic activity is exerted by three beta-
CC subunits PSMB5, PSMB6 and PSMB7 (PubMed:25599644, PubMed:26133119,
CC PubMed:26657688, PubMed:27342858, PubMed:27428775, PubMed:27493187,
CC PubMed:34711951). Interacts with AURKB (PubMed:14674694). Interacts
CC with CDKN1A (PubMed:11350925). Interacts with MDM2 and RB1
CC (PubMed:16337594). Interacts with the C-terminus of TBXA2R isoform 2
CC (PubMed:17499743). Interacts with DNAJB2 (PubMed:15936278).
CC {ECO:0000269|PubMed:11350925, ECO:0000269|PubMed:14674694,
CC ECO:0000269|PubMed:15936278, ECO:0000269|PubMed:16337594,
CC ECO:0000269|PubMed:17499743, ECO:0000269|PubMed:25599644,
CC ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:26657688,
CC ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC ECO:0000269|PubMed:27493187, ECO:0000269|PubMed:34711951}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat protein.
CC {ECO:0000269|PubMed:14550573}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus (HCV) F
CC protein. {ECO:0000269|PubMed:18971267}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus EBNA3
CC proteins. {ECO:0000269|PubMed:15831937}.
CC -!- INTERACTION:
CC P25788; P27449: ATP6V0C; NbExp=3; IntAct=EBI-348380, EBI-721179;
CC P25788; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-348380, EBI-8648738;
CC P25788; O95561: C1orf105; NbExp=3; IntAct=EBI-348380, EBI-10191951;
CC P25788; Q96CW7: C4orf42; NbExp=3; IntAct=EBI-348380, EBI-752053;
CC P25788; Q9NRJ3: CCL28; NbExp=3; IntAct=EBI-348380, EBI-7783254;
CC P25788; Q9BUF7: CRB3; NbExp=3; IntAct=EBI-348380, EBI-9844372;
CC P25788; P09228: CST2; NbExp=3; IntAct=EBI-348380, EBI-8832659;
CC P25788; Q7Z3D6: DGLUCY; NbExp=3; IntAct=EBI-348380, EBI-2807872;
CC P25788; Q14565: DMC1; NbExp=7; IntAct=EBI-348380, EBI-930865;
CC P25788; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-348380, EBI-9679045;
CC P25788; Q8N0U1: FAM171A2; NbExp=3; IntAct=EBI-348380, EBI-10264767;
CC P25788; Q96MZ4: FAM218A; NbExp=3; IntAct=EBI-348380, EBI-10291578;
CC P25788; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-348380, EBI-1384254;
CC P25788; Q96D16: FBXL18; NbExp=3; IntAct=EBI-348380, EBI-744419;
CC P25788; Q9Y3I1: FBXO7; NbExp=6; IntAct=EBI-348380, EBI-1161222;
CC P25788; P23769: GATA2; NbExp=4; IntAct=EBI-348380, EBI-2806671;
CC P25788; P23771: GATA3; NbExp=3; IntAct=EBI-348380, EBI-6664760;
CC P25788; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-348380, EBI-739467;
CC P25788; Q8N779: hCG_1998195; NbExp=3; IntAct=EBI-348380, EBI-10267476;
CC P25788; A0A024R5S0: hCG_2003792; NbExp=3; IntAct=EBI-348380, EBI-10188461;
CC P25788; Q6IPM2: IQCE; NbExp=4; IntAct=EBI-348380, EBI-3893098;
CC P25788; Q6UWL6: KIRREL2; NbExp=3; IntAct=EBI-348380, EBI-10254473;
CC P25788; Q8N7Y1: KIRREL3-AS3; NbExp=3; IntAct=EBI-348380, EBI-10267656;
CC P25788; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-348380, EBI-1048945;
CC P25788; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-348380, EBI-3957672;
CC P25788; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-348380, EBI-10261141;
CC P25788; Q14847: LASP1; NbExp=3; IntAct=EBI-348380, EBI-742828;
CC P25788; O95202: LETM1; NbExp=3; IntAct=EBI-348380, EBI-1052895;
CC P25788; Q8NAJ2: LINC02913; NbExp=3; IntAct=EBI-348380, EBI-10173129;
CC P25788; Q00987: MDM2; NbExp=2; IntAct=EBI-348380, EBI-389668;
CC P25788; Q96PC5: MIA2; NbExp=3; IntAct=EBI-348380, EBI-1050253;
CC P25788; Q9H6H2: MUM1; NbExp=3; IntAct=EBI-348380, EBI-10307610;
CC P25788; P48146: NPBWR2; NbExp=3; IntAct=EBI-348380, EBI-10210114;
CC P25788; P16860: NPPB; NbExp=3; IntAct=EBI-348380, EBI-747044;
CC P25788; Q8N2R0: OSR2; NbExp=3; IntAct=EBI-348380, EBI-5660512;
CC P25788; Q86TB9: PATL1; NbExp=3; IntAct=EBI-348380, EBI-2562092;
CC P25788; Q58A44: PCOTH; NbExp=3; IntAct=EBI-348380, EBI-10243387;
CC P25788; P29590: PML; NbExp=2; IntAct=EBI-348380, EBI-295890;
CC P25788; Q14CW7: PRR10; NbExp=3; IntAct=EBI-348380, EBI-10234793;
CC P25788; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-348380, EBI-740924;
CC P25788; P79522: PRR3; NbExp=3; IntAct=EBI-348380, EBI-2803328;
CC P25788; P25786: PSMA1; NbExp=14; IntAct=EBI-348380, EBI-359352;
CC P25788; P25789: PSMA4; NbExp=4; IntAct=EBI-348380, EBI-359310;
CC P25788; P60900: PSMA6; NbExp=10; IntAct=EBI-348380, EBI-357793;
CC P25788; O14818: PSMA7; NbExp=6; IntAct=EBI-348380, EBI-603272;
CC P25788; P28070: PSMB4; NbExp=3; IntAct=EBI-348380, EBI-603350;
CC P25788; Q9H3S7: PTPN23; NbExp=3; IntAct=EBI-348380, EBI-724478;
CC P25788; Q6NUJ5: PWWP2B; NbExp=3; IntAct=EBI-348380, EBI-10251192;
CC P25788; Q8TBN0: RAB3IL1; NbExp=3; IntAct=EBI-348380, EBI-743796;
CC P25788; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-348380, EBI-948156;
CC P25788; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-348380, EBI-744023;
CC P25788; O43251: RBFOX2; NbExp=3; IntAct=EBI-348380, EBI-746056;
CC P25788; Q9BTD8: RBM42; NbExp=3; IntAct=EBI-348380, EBI-746862;
CC P25788; Q14D33: RTP5; NbExp=3; IntAct=EBI-348380, EBI-10217913;
CC P25788; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-348380, EBI-10248967;
CC P25788; Q15637: SF1; NbExp=3; IntAct=EBI-348380, EBI-744603;
CC P25788; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-348380, EBI-10269374;
CC P25788; Q7L9D0: SLC22A23; NbExp=3; IntAct=EBI-348380, EBI-10256583;
CC P25788; P14678-2: SNRPB; NbExp=3; IntAct=EBI-348380, EBI-372475;
CC P25788; Q5TAL4: SNRPC; NbExp=3; IntAct=EBI-348380, EBI-10246938;
CC P25788; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-348380, EBI-8635958;
CC P25788; Q12846: STX4; NbExp=3; IntAct=EBI-348380, EBI-744942;
CC P25788; O43752: STX6; NbExp=3; IntAct=EBI-348380, EBI-2695795;
CC P25788; Q96HZ7: URB1-AS1; NbExp=3; IntAct=EBI-348380, EBI-10288943;
CC P25788; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-348380, EBI-2559305;
CC P25788; Q8N895: ZNF366; NbExp=5; IntAct=EBI-348380, EBI-2813661;
CC P25788; Q66K41: ZNF385C; NbExp=4; IntAct=EBI-348380, EBI-8651919;
CC P25788; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-348380, EBI-16429014;
CC P25788; B2R550; NbExp=3; IntAct=EBI-348380, EBI-10175488;
CC P25788; Q5JPT6; NbExp=3; IntAct=EBI-348380, EBI-10244213;
CC P25788; Q5W150; NbExp=3; IntAct=EBI-348380, EBI-10248148;
CC P25788; Q7KZQ1; NbExp=3; IntAct=EBI-348380, EBI-10255941;
CC P25788; Q9H8E5; NbExp=3; IntAct=EBI-348380, EBI-10309031;
CC P25788; Q9HAA0; NbExp=3; IntAct=EBI-348380, EBI-10309885;
CC P25788; Q9NWL9; NbExp=3; IntAct=EBI-348380, EBI-10315054;
CC P25788-2; P49821: NDUFV1; NbExp=3; IntAct=EBI-348394, EBI-748312;
CC P25788-2; O76024: WFS1; NbExp=3; IntAct=EBI-348394, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345,
CC ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345,
CC ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into
CC the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000269|PubMed:34711951}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P25788-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P25788-2; Sequence=VSP_005280;
CC -!- INDUCTION: Down-regulated by antioxidants BO-653 and probucol. Up-
CC regulated by bacterial lipopolysaccharides (LPS) and TNF.
CC {ECO:0000269|PubMed:11521686, ECO:0000269|PubMed:12472671,
CC ECO:0000269|PubMed:16298756}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; D00762; BAA00659.1; -; mRNA.
DR EMBL; BT006711; AAP35357.1; -; mRNA.
DR EMBL; BT019715; AAV38520.1; -; mRNA.
DR EMBL; AK315158; BAG37603.1; -; mRNA.
DR EMBL; CH471061; EAW80719.1; -; Genomic_DNA.
DR EMBL; BC005265; AAH05265.1; -; mRNA.
DR EMBL; BC029402; AAH29402.1; -; mRNA.
DR EMBL; BC038990; AAH38990.1; -; mRNA.
DR CCDS; CCDS45113.1; -. [P25788-2]
DR CCDS; CCDS9731.1; -. [P25788-1]
DR PIR; S15971; SNHUC8.
DR RefSeq; NP_002779.1; NM_002788.3. [P25788-1]
DR RefSeq; NP_687033.1; NM_152132.2. [P25788-2]
DR PDB; 4R3O; X-ray; 2.60 A; G/U=2-246.
DR PDB; 4R67; X-ray; 2.89 A; G/U/i/w=2-246.
DR PDB; 5A0Q; EM; 3.50 A; G/U=1-255.
DR PDB; 5DSV; X-ray; 3.75 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-255.
DR PDB; 5GJQ; EM; 4.50 A; X/n=1-255.
DR PDB; 5GJR; EM; 3.50 A; X/n=1-255.
DR PDB; 5L4G; EM; 4.02 A; G/T=1-255.
DR PDB; 5LE5; X-ray; 1.80 A; F/T=1-255.
DR PDB; 5LEX; X-ray; 2.20 A; F/T=1-255.
DR PDB; 5LEY; X-ray; 1.90 A; F/T=1-255.
DR PDB; 5LEZ; X-ray; 2.19 A; F/T=1-255.
DR PDB; 5LF0; X-ray; 2.41 A; F/T=1-255.
DR PDB; 5LF1; X-ray; 2.00 A; F/T=1-255.
DR PDB; 5LF3; X-ray; 2.10 A; F/T=1-255.
DR PDB; 5LF4; X-ray; 1.99 A; F/T=1-255.
DR PDB; 5LF6; X-ray; 2.07 A; F/T=1-255.
DR PDB; 5LF7; X-ray; 2.00 A; F/T=1-255.
DR PDB; 5LN3; EM; 6.80 A; G=1-255.
DR PDB; 5M32; EM; 3.80 A; F/T=1-255.
DR PDB; 5T0C; EM; 3.80 A; AM/BM=2-255.
DR PDB; 5T0G; EM; 4.40 A; M=2-255.
DR PDB; 5T0H; EM; 6.80 A; M=2-255.
DR PDB; 5T0I; EM; 8.00 A; M=2-255.
DR PDB; 5T0J; EM; 8.00 A; M=2-255.
DR PDB; 5VFO; EM; 3.50 A; M/m=2-246.
DR PDB; 5VFP; EM; 4.20 A; M/m=2-246.
DR PDB; 5VFQ; EM; 4.20 A; M/m=2-246.
DR PDB; 5VFR; EM; 4.90 A; M/m=2-246.
DR PDB; 5VFS; EM; 3.60 A; M/m=2-246.
DR PDB; 5VFT; EM; 7.00 A; M/m=2-246.
DR PDB; 5VFU; EM; 5.80 A; M/m=2-246.
DR PDB; 6AVO; EM; 3.80 A; J/Q=1-255.
DR PDB; 6E5B; X-ray; 2.77 A; F/T=1-255.
DR PDB; 6KWY; EM; 2.72 A; F/T=1-255.
DR PDB; 6MSB; EM; 3.00 A; M/m=2-255.
DR PDB; 6MSD; EM; 3.20 A; M/m=2-255.
DR PDB; 6MSE; EM; 3.30 A; a=166-213.
DR PDB; 6MSG; EM; 3.50 A; M/m=2-255.
DR PDB; 6MSH; EM; 3.60 A; M/m=2-255.
DR PDB; 6MSJ; EM; 3.30 A; M/m=2-255.
DR PDB; 6MSK; EM; 3.20 A; M/m=2-255.
DR PDB; 6R70; EM; 3.50 A; F/T=6-245.
DR PDB; 6REY; EM; 3.00 A; G/U=1-255.
DR PDB; 6RGQ; EM; 2.60 A; G/U=1-255.
DR PDB; 6WJD; EM; 4.80 A; M/m=2-255.
DR PDB; 6WJN; EM; 5.70 A; M/m=2-246.
DR PDB; 6XMJ; EM; 3.00 A; G=2-246.
DR PDB; 7AWE; X-ray; 2.29 A; G/U=5-246.
DR PDB; 7B12; X-ray; 2.43 A; G/U=3-246.
DR PDB; 7E55; EM; 5.90 A; A=1-255.
DR PDB; 7LXV; EM; 3.40 A; F/T=1-255.
DR PDB; 7NHT; EM; 2.80 A; F=1-255.
DR PDB; 7PG9; EM; 3.70 A; G/U=1-255.
DR PDB; 7V5G; EM; 4.47 A; U/b=1-255.
DR PDB; 7V5M; EM; 3.88 A; G/U=1-255.
DR PDBsum; 4R3O; -.
DR PDBsum; 4R67; -.
DR PDBsum; 5A0Q; -.
DR PDBsum; 5DSV; -.
DR PDBsum; 5GJQ; -.
DR PDBsum; 5GJR; -.
DR PDBsum; 5L4G; -.
DR PDBsum; 5LE5; -.
DR PDBsum; 5LEX; -.
DR PDBsum; 5LEY; -.
DR PDBsum; 5LEZ; -.
DR PDBsum; 5LF0; -.
DR PDBsum; 5LF1; -.
DR PDBsum; 5LF3; -.
DR PDBsum; 5LF4; -.
DR PDBsum; 5LF6; -.
DR PDBsum; 5LF7; -.
DR PDBsum; 5LN3; -.
DR PDBsum; 5M32; -.
DR PDBsum; 5T0C; -.
DR PDBsum; 5T0G; -.
DR PDBsum; 5T0H; -.
DR PDBsum; 5T0I; -.
DR PDBsum; 5T0J; -.
DR PDBsum; 5VFO; -.
DR PDBsum; 5VFP; -.
DR PDBsum; 5VFQ; -.
DR PDBsum; 5VFR; -.
DR PDBsum; 5VFS; -.
DR PDBsum; 5VFT; -.
DR PDBsum; 5VFU; -.
DR PDBsum; 6AVO; -.
DR PDBsum; 6E5B; -.
DR PDBsum; 6KWY; -.
DR PDBsum; 6MSB; -.
DR PDBsum; 6MSD; -.
DR PDBsum; 6MSE; -.
DR PDBsum; 6MSG; -.
DR PDBsum; 6MSH; -.
DR PDBsum; 6MSJ; -.
DR PDBsum; 6MSK; -.
DR PDBsum; 6R70; -.
DR PDBsum; 6REY; -.
DR PDBsum; 6RGQ; -.
DR PDBsum; 6WJD; -.
DR PDBsum; 6WJN; -.
DR PDBsum; 6XMJ; -.
DR PDBsum; 7AWE; -.
DR PDBsum; 7B12; -.
DR PDBsum; 7E55; -.
DR PDBsum; 7LXV; -.
DR PDBsum; 7NHT; -.
DR PDBsum; 7PG9; -.
DR PDBsum; 7V5G; -.
DR PDBsum; 7V5M; -.
DR AlphaFoldDB; P25788; -.
DR SMR; P25788; -.
DR BioGRID; 111657; 381.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P25788; -.
DR DIP; DIP-29366N; -.
DR IntAct; P25788; 143.
DR MINT; P25788; -.
DR STRING; 9606.ENSP00000216455; -.
DR BindingDB; P25788; -.
DR ChEMBL; CHEMBL2364701; -.
DR ChEMBL; CHEMBL3831201; -.
DR DrugBank; DB08515; (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR MEROPS; T01.977; -.
DR MoonDB; P25788; Predicted.
DR GlyGen; P25788; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P25788; -.
DR MetOSite; P25788; -.
DR PhosphoSitePlus; P25788; -.
DR SwissPalm; P25788; -.
DR BioMuta; PSMA3; -.
DR DMDM; 130859; -.
DR OGP; P25788; -.
DR REPRODUCTION-2DPAGE; IPI00171199; -.
DR EPD; P25788; -.
DR jPOST; P25788; -.
DR MassIVE; P25788; -.
DR MaxQB; P25788; -.
DR PaxDb; P25788; -.
DR PeptideAtlas; P25788; -.
DR PRIDE; P25788; -.
DR ProteomicsDB; 54290; -. [P25788-1]
DR ProteomicsDB; 54291; -. [P25788-2]
DR Antibodypedia; 80; 313 antibodies from 35 providers.
DR DNASU; 5684; -.
DR Ensembl; ENST00000216455.9; ENSP00000216455.4; ENSG00000100567.13. [P25788-1]
DR Ensembl; ENST00000412908.6; ENSP00000390491.2; ENSG00000100567.13. [P25788-2]
DR GeneID; 5684; -.
DR KEGG; hsa:5684; -.
DR MANE-Select; ENST00000216455.9; ENSP00000216455.4; NM_002788.4; NP_002779.1.
DR UCSC; uc001xdj.3; human. [P25788-1]
DR CTD; 5684; -.
DR DisGeNET; 5684; -.
DR GeneCards; PSMA3; -.
DR HGNC; HGNC:9532; PSMA3.
DR HPA; ENSG00000100567; Low tissue specificity.
DR MIM; 176843; gene.
DR MIM; 176845; gene.
DR neXtProt; NX_P25788; -.
DR OpenTargets; ENSG00000100567; -.
DR PharmGKB; PA33877; -.
DR VEuPathDB; HostDB:ENSG00000100567; -.
DR eggNOG; KOG0184; Eukaryota.
DR GeneTree; ENSGT00550000074912; -.
DR HOGENOM; CLU_035750_0_0_1; -.
DR InParanoid; P25788; -.
DR OMA; SMYMHAY; -.
DR PhylomeDB; P25788; -.
DR TreeFam; TF106208; -.
DR PathwayCommons; P25788; -.
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; P25788; -.
DR SIGNOR; P25788; -.
DR BioGRID-ORCS; 5684; 807 hits in 1102 CRISPR screens.
DR ChiTaRS; PSMA3; human.
DR GeneWiki; PSMA3; -.
DR GenomeRNAi; 5684; -.
DR Pharos; P25788; Tbio.
DR PRO; PR:P25788; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P25788; protein.
DR Bgee; ENSG00000100567; Expressed in adrenal tissue and 206 other tissues.
DR ExpressionAtlas; P25788; baseline and differential.
DR Genevisible; P25788; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ARUK-UCL.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR GO; GO:0052548; P:regulation of endopeptidase activity; IMP:UniProtKB.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR037555; Proteasome_alpha_3.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF10; PTHR11599:SF10; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; 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|PubMed:12376572,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..255
FT /note="Proteasome subunit alpha type-3"
FT /id="PRO_0000124091"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:12376572,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17323924,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12376572,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17323924, ECO:0007744|PubMed:17487921,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 136..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_005280"
FT VARIANT 233
FT /note="Missing (found in a patient with Nakajo syndrome who
FT also carries a mutation in PSMB8; unknown pathological
FT significance; patients' cells show reduction of proteasome
FT content and endopeptidase activity of the proteasome;
FT dbSNP:rs1555353410)"
FT /evidence="ECO:0000269|PubMed:26524591"
FT /id="VAR_075259"
FT CONFLICT 91
FT /note="I -> M (in Ref. 5; AAH29402)"
FT /evidence="ECO:0000305"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:5A0Q"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5VFO"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 82..103
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6RGQ"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:5LE5"
SQ 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
