GenomeNet

Database: UniProt
Entry: P25787
LinkDB: P25787
Original site: P25787 
ID   PSA2_HUMAN              Reviewed;         234 AA.
AC   P25787; Q6ICS6; Q9BU45;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-JUN-2021, entry version 222.
DE   RecName: Full=Proteasome subunit alpha type-2;
DE   AltName: Full=Macropain subunit C3;
DE   AltName: Full=Multicatalytic endopeptidase complex subunit C3;
DE   AltName: Full=Proteasome component C3;
GN   Name=PSMA2; Synonyms=HC3, PSC3;
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].
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].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 5-39; 71-84; 93-113 AND 178-196, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [8]
RP   PROTEIN SEQUENCE OF 5-14.
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   [9]
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   [10]
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   [11]
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   [12]
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, AND IDENTIFICATION BY
RP   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   [14]
RP   INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA   Leong W.F., Chow V.T.;
RT   "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT   differential cellular gene expression in response to enterovirus 71
RT   infection.";
RL   Cell. Microbiol. 8:565-580(2006).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17323924; DOI=10.1021/bi061994u;
RA   Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT   "Mass spectrometric characterization of the affinity-purified human 26S
RT   proteasome complex.";
RL   Biochemistry 46:3553-3565(2007).
RN   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=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   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-171, 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   [19]
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   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-14; SER-16 AND TYR-76,
RP   AND 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   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [23]
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   [24]
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   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), 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   [26]
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   [27]
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   [28]
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   [29]
RP   VARIANT [LARGE SCALE ANALYSIS] VAL-110.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
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). {ECO:0000269|PubMed:15244466,
CC       ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC       complex made of 28 subunits that are arranged in four stacked rings.
CC       The two outer rings are each formed by seven alpha subunits, and the
CC       two inner rings are formed by seven beta subunits. The proteolytic
CC       activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
CC       {ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119,
CC       ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC       ECO:0000269|PubMed:27493187}.
CC   -!- INTERACTION:
CC       P25787; P25786: PSMA1; NbExp=12; IntAct=EBI-603262, EBI-359352;
CC       P25787; P25789: PSMA4; NbExp=7; IntAct=EBI-603262, EBI-359310;
CC       P25787; P60900: PSMA6; NbExp=5; IntAct=EBI-603262, EBI-357793;
CC       P25787; O14818: PSMA7; NbExp=5; IntAct=EBI-603262, EBI-603272;
CC       P25787; Q6S8E0: ORF9b; Xeno; NbExp=2; IntAct=EBI-603262, EBI-25489144;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus
CC       {ECO:0000269|PubMed:12181345}. Note=Colocalizes with TRIM5 in
CC       cytoplasmic bodies. {ECO:0000250|UniProtKB:P49722}.
CC   -!- INDUCTION: Down-regulated by antioxidants BO-653 and probucol. Down-
CC       regulated in response to enterovirus 71 (EV71) infection (at protein
CC       level). {ECO:0000269|PubMed:11521686, ECO:0000269|PubMed:16548883}.
CC   -!- PTM: Phosphorylated on tyrosine residues; which may be important for
CC       nuclear import. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; D00760; BAA00657.1; -; mRNA.
DR   EMBL; AK290654; BAF83343.1; -; mRNA.
DR   EMBL; CR450317; CAG29313.1; -; mRNA.
DR   EMBL; CH236951; EAL24005.1; -; Genomic_DNA.
DR   EMBL; CH471073; EAW94152.1; -; Genomic_DNA.
DR   EMBL; BC002900; AAH02900.2; -; mRNA.
DR   EMBL; BC047697; AAH47697.1; -; mRNA.
DR   CCDS; CCDS5467.1; -.
DR   PIR; S15970; SNHUC3.
DR   RefSeq; NP_002778.1; NM_002787.4.
DR   PDB; 4R3O; X-ray; 2.60 A; B/P=2-234.
DR   PDB; 4R67; X-ray; 2.89 A; B/P/d/r=2-234.
DR   PDB; 5A0Q; EM; 3.50 A; B/P=1-234.
DR   PDB; 5GJQ; EM; 4.50 A; C/i=1-234.
DR   PDB; 5GJR; EM; 3.50 A; C/i=1-234.
DR   PDB; 5L4G; EM; 4.02 A; B/O=1-234.
DR   PDB; 5LE5; X-ray; 1.80 A; A/O=1-234.
DR   PDB; 5LEX; X-ray; 2.20 A; A/O=1-234.
DR   PDB; 5LEY; X-ray; 1.90 A; A/O=1-234.
DR   PDB; 5LEZ; X-ray; 2.19 A; A/O=1-234.
DR   PDB; 5LF0; X-ray; 2.41 A; A/O=1-234.
DR   PDB; 5LF1; X-ray; 2.00 A; A/O=1-234.
DR   PDB; 5LF3; X-ray; 2.10 A; A/O=1-234.
DR   PDB; 5LF4; X-ray; 1.99 A; A/O=1-234.
DR   PDB; 5LF6; X-ray; 2.07 A; A/O=1-234.
DR   PDB; 5LF7; X-ray; 2.00 A; A/O=1-234.
DR   PDB; 5LN3; EM; 6.80 A; B=1-234.
DR   PDB; 5M32; EM; 3.80 A; A/O=1-234.
DR   PDB; 5T0C; EM; 3.80 A; AH/BH=2-234.
DR   PDB; 5T0G; EM; 4.40 A; H=2-234.
DR   PDB; 5T0H; EM; 6.80 A; H=2-234.
DR   PDB; 5T0I; EM; 8.00 A; H=2-234.
DR   PDB; 5T0J; EM; 8.00 A; H=2-234.
DR   PDB; 5VFO; EM; 3.50 A; H/h=3-234.
DR   PDB; 5VFP; EM; 4.20 A; H/h=3-234.
DR   PDB; 5VFQ; EM; 4.20 A; H/h=3-234.
DR   PDB; 5VFR; EM; 4.90 A; H/h=3-234.
DR   PDB; 5VFS; EM; 3.60 A; H/h=3-234.
DR   PDB; 5VFT; EM; 7.00 A; H/h=3-234.
DR   PDB; 5VFU; EM; 5.80 A; H/h=3-234.
DR   PDB; 6AVO; EM; 3.80 A; P/b=1-234.
DR   PDB; 6E5B; X-ray; 2.77 A; A/O=1-234.
DR   PDB; 6KWY; EM; 2.72 A; A/O=1-234.
DR   PDB; 6MSB; EM; 3.00 A; H/h=2-234.
DR   PDB; 6MSD; EM; 3.20 A; H/h=2-234.
DR   PDB; 6MSE; EM; 3.30 A; V=21-102.
DR   PDB; 6MSG; EM; 3.50 A; H/h=2-234.
DR   PDB; 6MSH; EM; 3.60 A; H/h=2-234.
DR   PDB; 6MSJ; EM; 3.30 A; H/h=2-234.
DR   PDB; 6MSK; EM; 3.20 A; H/h=2-234.
DR   PDB; 6R70; EM; 3.50 A; A/O=4-233.
DR   PDB; 6REY; EM; 3.00 A; B/P=1-234.
DR   PDB; 6RGQ; EM; 2.60 A; B/P=1-234.
DR   PDB; 6WJD; EM; 4.80 A; H/h=2-234.
DR   PDB; 6WJN; EM; 5.70 A; H/h=3-234.
DR   PDB; 6XMJ; EM; 3.00 A; B=2-234.
DR   PDBsum; 4R3O; -.
DR   PDBsum; 4R67; -.
DR   PDBsum; 5A0Q; -.
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   SMR; P25787; -.
DR   BioGRID; 111656; 170.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P25787; -.
DR   DIP; DIP-29364N; -.
DR   IntAct; P25787; 50.
DR   MINT; P25787; -.
DR   STRING; 9606.ENSP00000223321; -.
DR   BindingDB; P25787; -.
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   MEROPS; T01.972; -.
DR   iPTMnet; P25787; -.
DR   MetOSite; P25787; -.
DR   PhosphoSitePlus; P25787; -.
DR   SwissPalm; P25787; -.
DR   BioMuta; PSMA2; -.
DR   DMDM; 130850; -.
DR   OGP; P25787; -.
DR   REPRODUCTION-2DPAGE; IPI00219622; -.
DR   EPD; P25787; -.
DR   jPOST; P25787; -.
DR   MassIVE; P25787; -.
DR   MaxQB; P25787; -.
DR   PaxDb; P25787; -.
DR   PeptideAtlas; P25787; -.
DR   PRIDE; P25787; -.
DR   ProteomicsDB; 54289; -.
DR   TopDownProteomics; P25787; -.
DR   Antibodypedia; 2176; 384 antibodies.
DR   DNASU; 5683; -.
DR   Ensembl; ENST00000223321; ENSP00000223321; ENSG00000106588.
DR   GeneID; 5683; -.
DR   KEGG; hsa:5683; -.
DR   UCSC; uc003thy.5; human.
DR   CTD; 5683; -.
DR   DisGeNET; 5683; -.
DR   GeneCards; PSMA2; -.
DR   HGNC; HGNC:9531; PSMA2.
DR   HPA; ENSG00000106588; Low tissue specificity.
DR   MIM; 176842; gene.
DR   neXtProt; NX_P25787; -.
DR   OpenTargets; ENSG00000106588; -.
DR   OpenTargets; ENSG00000256646; -.
DR   PharmGKB; PA33876; -.
DR   VEuPathDB; HostDB:ENSG00000106588.10; -.
DR   eggNOG; KOG0181; Eukaryota.
DR   GeneTree; ENSGT00550000074870; -.
DR   HOGENOM; CLU_035750_4_1_1; -.
DR   InParanoid; P25787; -.
DR   OMA; CVYSGMG; -.
DR   OrthoDB; 1222564at2759; -.
DR   PhylomeDB; P25787; -.
DR   TreeFam; TF106207; -.
DR   PathwayCommons; P25787; -.
DR   Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR   Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR   Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR   Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-HSA-202424; Downstream TCR signaling.
DR   Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR   Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-HSA-4641257; Degradation of AXIN.
DR   Reactome; R-HSA-4641258; Degradation of DVL.
DR   Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR   Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR   Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR   Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR   Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-HSA-5689603; UCH proteinases.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin 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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; P25787; -.
DR   BioGRID-ORCS; 5683; 783 hits in 977 CRISPR screens.
DR   ChiTaRS; PSMA2; human.
DR   GeneWiki; PSMA2; -.
DR   GenomeRNAi; 5683; -.
DR   Pharos; P25787; Tbio.
DR   PRO; PR:P25787; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P25787; protein.
DR   Bgee; ENSG00000106588; Expressed in kidney and 237 other tissues.
DR   ExpressionAtlas; P25787; baseline and differential.
DR   Genevisible; P25787; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR   GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:FlyBase.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR034644; Proteasome_subunit_alpha2.
DR   PANTHER; PTHR11599:SF16; PTHR11599:SF16; 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; Cytoplasm; Direct protein sequencing; Nucleus;
KW   Phosphoprotein; Proteasome; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..234
FT                   /note="Proteasome subunit alpha type-2"
FT                   /id="PRO_0000124077"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         6
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P49722"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         24
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455"
FT   MOD_RES         70
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         76
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         121
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P17220"
FT   MOD_RES         171
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VARIANT         110
FT                   /note="L -> V (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036278"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:5LF3"
FT   STRAND          15..17
FT                   /evidence="ECO:0007829|PDB:5VFO"
FT   HELIX           20..30
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:4R67"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:5LEY"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          72..78
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           80..101
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           107..120
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          124..127
FT                   /evidence="ECO:0007829|PDB:6R70"
FT   STRAND          131..140
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   TURN            151..153
FT                   /evidence="ECO:0007829|PDB:6E5B"
FT   STRAND          155..164
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           167..177
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           184..196
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          207..214
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          217..220
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           223..231
FT                   /evidence="ECO:0007829|PDB:5LE5"
SQ   SEQUENCE   234 AA;  25899 MW;  63CB56A233583836 CRC64;
     MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER
     SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE
     YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE
     DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVKDYL AAIA
//
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