PSB5_HUMAN
ID PSB5_HUMAN Reviewed; 263 AA.
AC P28074; B2R4N9; B4DUM9; D3DS43; E9PAV2; Q16242; Q6PEW2; Q7Z3B5; Q86T01;
AC Q9TNN9;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 237.
DE RecName: Full=Proteasome subunit beta type-5;
DE EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
DE AltName: Full=Macropain epsilon chain;
DE AltName: Full=Multicatalytic endopeptidase complex epsilon chain;
DE AltName: Full=Proteasome chain 6;
DE AltName: Full=Proteasome epsilon chain;
DE AltName: Full=Proteasome subunit MB1;
DE AltName: Full=Proteasome subunit X;
DE Flags: Precursor;
GN Name=PSMB5; Synonyms=LMPX, MB1, X;
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 [GENOMIC DNA].
RX PubMed=8753855; DOI=10.1007/bf02602554;
RA Abdulla S., Beck S., Belich M., Jackson A., Nakamura T., Trowsdale J.;
RT "Divergent intron arrangement in the MB1/LMP7 proteasome gene pair.";
RL Immunogenetics 44:254-258(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skeletal muscle;
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] (ISOFORM 1).
RC TISSUE=Endometrial adenocarcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Embryonic stem cell, Hypothalamus, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-203 (ISOFORM 2).
RC TISSUE=Cervix carcinoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-263 (ISOFORM 1), AND INDUCTION.
RX PubMed=8066462; DOI=10.1126/science.8066462;
RA Akiyama K.-Y., Yokota K.-Y., Kagawa S., Shimbara N., Tamura T., Akioka H.,
RA Nothwang H.G., Noda C., Tanaka K., Ichihara A.;
RT "cDNA cloning and interferon gamma down-regulation of proteasomal subunits
RT X and Y.";
RL Science 265:1231-1234(1994).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-263 (ISOFORM 1).
RX PubMed=7820546; DOI=10.1016/s0960-9822(00)00174-3;
RA Belich M.P., Glynne R.J., Senger G., Sheer D., Trowsdale J.;
RT "Proteasome components with reciprocal expression to that of the MHC-
RT encoded LMP proteins.";
RL Curr. Biol. 4:769-776(1994).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-263 (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PROTEIN SEQUENCE OF 60-85.
RX PubMed=2306472; DOI=10.1016/0167-4838(90)90165-c;
RA Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N.,
RA Slaughter C.A.;
RT "Relationships among the subunits of the high molecular weight proteinase,
RT macropain (proteasome).";
RL Biochim. Biophys. Acta 1037:178-185(1990).
RN [12]
RP PROTEIN SEQUENCE OF 201-216 AND 226-239.
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 [13]
RP PROTEIN SEQUENCE OF 201-216, AND SUBUNIT.
RC TISSUE=Kidney;
RX PubMed=8163024; DOI=10.1016/0014-5793(94)80612-8;
RA Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M., Kristensen P.,
RA Hendil K.B., Tanaka K., Ichihara A.;
RT "Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by
RT interferon-gamma for acquirement of the functional diversity responsible
RT for antigen processing.";
RL FEBS Lett. 343:85-88(1994).
RN [14]
RP ERRATUM OF PUBMED:8163024.
RX PubMed=7864893; DOI=10.1006/bbrc.1995.1294;
RA Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
RL Biochem. Biophys. Res. Commun. 207:1059-1059(1995).
RN [15]
RP INDUCTION.
RX PubMed=8663318; DOI=10.1074/jbc.271.29.17275;
RA Gaczynska M., Goldberg A.L., Tanaka K., Hendil K.B., Rock K.L.;
RT "Proteasome subunits X and Y alter peptidase activities in opposite ways to
RT the interferon-gamma-induced subunits LMP2 and LMP7.";
RL J. Biol. Chem. 271:17275-17280(1996).
RN [16]
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 [17]
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 [18]
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 [19]
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 [20]
RP INTERACTION WITH ABCB1 AND TAP1.
RX PubMed=15488952; DOI=10.1016/j.molimm.2004.07.005;
RA Begley G.S., Horvath A.R., Taylor J.C., Higgins C.F.;
RT "Cytoplasmic domains of the transporter associated with antigen processing
RT and P-glycoprotein interact with subunits of the proteasome.";
RL Mol. Immunol. 42:137-141(2005).
RN [21]
RP INTERACTION WITH POMP.
RX PubMed=15944226; DOI=10.1073/pnas.0501711102;
RA Heink S., Ludwig D., Kloetzel P.-M., Krueger E.;
RT "IFN-gamma-induced immune adaptation of the proteasome system is an
RT accelerated and transient response.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9241-9246(2005).
RN [22]
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 [23]
RP INDUCTION.
RX PubMed=17004105; DOI=10.1007/s10549-006-9393-7;
RA Deng S., Zhou H., Xiong R., Lu Y., Yan D., Xing T., Dong L., Tang E.,
RA Yang H.;
RT "Over-expression of genes and proteins of ubiquitin specific peptidases
RT (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by
RT the methods of RFDD-PCR and proteomics.";
RL Breast Cancer Res. Treat. 104:21-30(2007).
RN [24]
RP FUNCTION, AND MUTAGENESIS OF ALA-108.
RX PubMed=18565852; DOI=10.1182/blood-2007-08-104950;
RA Oerlemans R., Franke N.E., Assaraf Y.G., Cloos J., van Zantwijk I.,
RA Berkers C.R., Scheffer G.L., Debipersad K., Vojtekova K., Lemos C.,
RA van der Heijden J.W., Ylstra B., Peters G.J., Kaspers G.L., Dijkmans B.A.,
RA Scheper R.J., Jansen G.;
RT "Molecular basis of bortezomib resistance: proteasome subunit beta5 (PSMB5)
RT gene mutation and overexpression of PSMB5 protein.";
RL Blood 112:2489-2499(2008).
RN [25]
RP FUNCTION, AND MUTAGENESIS OF ALA-108.
RX PubMed=18502982; DOI=10.1124/jpet.108.138131;
RA Lue S., Yang J., Song X., Gong S., Zhou H., Guo L., Song N., Bao X.,
RA Chen P., Wang J.;
RT "Point mutation of the proteasome beta5 subunit gene is an important
RT mechanism of bortezomib resistance in bortezomib-selected variants of
RT Jurkat T cell lymphoblastic lymphoma/leukemia line.";
RL J. Pharmacol. Exp. Ther. 326:423-431(2008).
RN [26]
RP MUTAGENESIS OF ALA-108 AND ALA-109.
RX PubMed=19426847; DOI=10.1016/j.exphem.2009.04.001;
RA Lue S., Yang J., Chen Z., Gong S., Zhou H., Xu X., Wang J.;
RT "Different mutants of PSMB5 confer varying bortezomib resistance in T
RT lymphoblastic lymphoma/leukemia cells derived from the Jurkat cell line.";
RL Exp. Hematol. 37:831-837(2009).
RN [27]
RP INDUCTION BY SULFORAPHANE.
RX PubMed=18602823; DOI=10.1016/j.jnutbio.2008.02.002;
RA Ramirez M.C., Singletary K.;
RT "Regulation of estrogen receptor alpha expression in human breast cancer
RT cells by sulforaphane.";
RL J. Nutr. Biochem. 20:195-201(2009).
RN [28]
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 [29]
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 [30]
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 [31]
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 [32]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 60-260, SUBUNIT, AND ACTIVE SITE.
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 [33]
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 [34]
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 [35]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
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 [36]
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).
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). Within the 20S core complex, PSMB5 displays a
CC chymotrypsin-like activity. {ECO:0000269|PubMed:15244466,
CC ECO:0000269|PubMed:18502982, ECO:0000269|PubMed:18565852,
CC ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={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:27342858, PubMed:27428775, PubMed:27493187, PubMed:8163024,
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:27342858, PubMed:27428775,
CC PubMed:27493187, PubMed:8163024, 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:27342858, PubMed:27428775, PubMed:27493187, PubMed:8163024,
CC PubMed:34711951). The proteolytic activity is exerted by three beta-
CC subunits PSMB5, PSMB6 and PSMB7 (PubMed:25599644, PubMed:26133119,
CC PubMed:27342858, PubMed:27428775, PubMed:27493187, PubMed:8163024,
CC PubMed:34711951). Directly interacts with POMP (PubMed:15944226).
CC Interacts with ABCB1 and TAP1 (PubMed:15488952).
CC {ECO:0000269|PubMed:15488952, ECO:0000269|PubMed:15944226,
CC ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119,
CC ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC ECO:0000269|PubMed:27493187, ECO:0000269|PubMed:34711951,
CC ECO:0000269|PubMed:8163024}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 TAT protein.
CC {ECO:0000269|PubMed:14550573}.
CC -!- INTERACTION:
CC P28074; O95429: BAG4; NbExp=5; IntAct=EBI-357828, EBI-2949658;
CC P28074; Q8NCX0-3: CCDC150; NbExp=3; IntAct=EBI-357828, EBI-12235840;
CC P28074; Q92989: CLP1; NbExp=3; IntAct=EBI-357828, EBI-2559831;
CC P28074; Q68J44: DUSP29; NbExp=3; IntAct=EBI-357828, EBI-1054321;
CC P28074; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-357828, EBI-81279;
CC P28074; O15116: LSM1; NbExp=4; IntAct=EBI-357828, EBI-347619;
CC P28074; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-357828, EBI-741158;
CC P28074; Q9Y244: POMP; NbExp=3; IntAct=EBI-357828, EBI-696895;
CC P28074; P20618: PSMB1; NbExp=4; IntAct=EBI-357828, EBI-372273;
CC P28074; P49720: PSMB3; NbExp=3; IntAct=EBI-357828, EBI-603340;
CC P28074; Q99436: PSMB7; NbExp=8; IntAct=EBI-357828, EBI-603319;
CC P28074; Q9BT92: TCHP; NbExp=3; IntAct=EBI-357828, EBI-740781;
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=3;
CC Name=1;
CC IsoId=P28074-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28074-2; Sequence=VSP_041263;
CC Name=3;
CC IsoId=P28074-3; Sequence=VSP_045686;
CC -!- INDUCTION: Down-regulated by IFNG/IFN-gamma (at protein level). Induced
CC in breast cancer tissue. Up-regulated by sulforaphane in breast cancer
CC cells. {ECO:0000269|PubMed:17004105, ECO:0000269|PubMed:18602823,
CC ECO:0000269|PubMed:8066462, ECO:0000269|PubMed:8663318}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP35423.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA06097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD97956.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X95586; CAA64838.1; -; Genomic_DNA.
DR EMBL; AK300714; BAG62391.1; -; mRNA.
DR EMBL; AK311895; BAG34836.1; -; mRNA.
DR EMBL; BX538001; CAD97956.1; ALT_INIT; mRNA.
DR EMBL; AL132780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66193.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66195.1; -; Genomic_DNA.
DR EMBL; BC004146; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC057840; AAH57840.1; -; mRNA.
DR EMBL; BC107720; AAI07721.1; -; mRNA.
DR EMBL; CD048996; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX248299; CAD62626.1; -; mRNA.
DR EMBL; D29011; BAA06097.1; ALT_INIT; mRNA.
DR EMBL; S74378; AAB33092.1; -; mRNA.
DR EMBL; BT006777; AAP35423.1; ALT_INIT; mRNA.
DR CCDS; CCDS45083.1; -. [P28074-3]
DR CCDS; CCDS45084.1; -. [P28074-2]
DR CCDS; CCDS9584.1; -. [P28074-1]
DR PIR; A54589; A54589.
DR PIR; I52906; I52906.
DR PIR; PC2328; PC2328.
DR PIR; S08189; S08189.
DR RefSeq; NP_001124197.1; NM_001130725.1. [P28074-3]
DR RefSeq; NP_001138404.1; NM_001144932.2. [P28074-2]
DR RefSeq; NP_002788.1; NM_002797.4. [P28074-1]
DR PDB; 4R3O; X-ray; 2.60 A; L/Z=60-260.
DR PDB; 4R67; X-ray; 2.89 A; 3/L/Z/n=60-260.
DR PDB; 5A0Q; EM; 3.50 A; L/Z=60-263.
DR PDB; 5GJQ; EM; 4.50 A; e/s=1-263.
DR PDB; 5GJR; EM; 3.50 A; e/s=1-263.
DR PDB; 5L4G; EM; 4.02 A; 5/Y=1-263.
DR PDB; 5L5W; X-ray; 2.80 A; K/Y=60-197.
DR PDB; 5L5X; X-ray; 2.90 A; K/Y=60-197.
DR PDB; 5L5Y; X-ray; 2.70 A; K/Y=60-197.
DR PDB; 5L5Z; X-ray; 2.70 A; K/Y=60-197.
DR PDB; 5L60; X-ray; 2.70 A; K/Y=60-197.
DR PDB; 5L61; X-ray; 2.80 A; K/Y=60-193.
DR PDB; 5L62; X-ray; 2.80 A; K/Y=60-197.
DR PDB; 5L63; X-ray; 2.70 A; K/Y=60-197.
DR PDB; 5L64; X-ray; 2.70 A; K/Y=60-197.
DR PDB; 5LE5; X-ray; 1.80 A; K/Y=60-263.
DR PDB; 5LEX; X-ray; 2.20 A; K/Y=60-263.
DR PDB; 5LEY; X-ray; 1.90 A; K/Y=60-263.
DR PDB; 5LEZ; X-ray; 2.19 A; K/Y=60-263.
DR PDB; 5LF0; X-ray; 2.41 A; K/Y=60-263.
DR PDB; 5LF1; X-ray; 2.00 A; K/Y=60-263.
DR PDB; 5LF3; X-ray; 2.10 A; K/Y=60-263.
DR PDB; 5LF4; X-ray; 1.99 A; K/Y=60-263.
DR PDB; 5LF6; X-ray; 2.07 A; K/Y=60-263.
DR PDB; 5LF7; X-ray; 2.00 A; K/Y=60-263.
DR PDB; 5LN3; EM; 6.80 A; 5=1-263.
DR PDB; 5M32; EM; 3.80 A; K/Y=60-263.
DR PDB; 5T0C; EM; 3.80 A; AR/BR=2-263.
DR PDB; 5T0G; EM; 4.40 A; R=2-263.
DR PDB; 5T0H; EM; 6.80 A; R=2-263.
DR PDB; 5T0I; EM; 8.00 A; R=2-263.
DR PDB; 5T0J; EM; 8.00 A; R=2-263.
DR PDB; 5VFO; EM; 3.50 A; R/r=60-260.
DR PDB; 5VFP; EM; 4.20 A; R/r=60-260.
DR PDB; 5VFQ; EM; 4.20 A; R/r=60-260.
DR PDB; 5VFR; EM; 4.90 A; R/r=60-260.
DR PDB; 5VFS; EM; 3.60 A; R/r=60-260.
DR PDB; 5VFT; EM; 7.00 A; R/r=60-260.
DR PDB; 5VFU; EM; 5.80 A; R/r=60-260.
DR PDB; 6KWY; EM; 2.72 A; K/Y=1-263.
DR PDB; 6MSB; EM; 3.00 A; R/r=2-263.
DR PDB; 6MSD; EM; 3.20 A; R/r=2-263.
DR PDB; 6MSE; EM; 3.30 A; f=146-201.
DR PDB; 6MSG; EM; 3.50 A; R/r=2-263.
DR PDB; 6MSH; EM; 3.60 A; R/r=2-263.
DR PDB; 6MSJ; EM; 3.30 A; R/r=2-263.
DR PDB; 6MSK; EM; 3.20 A; R/r=2-263.
DR PDB; 6R70; EM; 3.50 A; K/Y=60-260.
DR PDB; 6REY; EM; 3.00 A; L/Z=60-263.
DR PDB; 6RGQ; EM; 2.60 A; L/Z=60-263.
DR PDB; 6WJD; EM; 4.80 A; R/r=2-263.
DR PDB; 6WJN; EM; 5.70 A; R/r=60-260.
DR PDB; 6XMJ; EM; 3.00 A; L=60-260.
DR PDB; 7LXV; EM; 3.40 A; K/Y=60-263.
DR PDB; 7NHT; EM; 2.80 A; K=1-263.
DR PDB; 7PG9; EM; 3.70 A; L/Z=60-263.
DR PDB; 7V5G; EM; 4.47 A; E/L=60-263.
DR PDB; 7V5M; EM; 3.88 A; L/Z=60-263.
DR PDBsum; 4R3O; -.
DR PDBsum; 4R67; -.
DR PDBsum; 5A0Q; -.
DR PDBsum; 5GJQ; -.
DR PDBsum; 5GJR; -.
DR PDBsum; 5L4G; -.
DR PDBsum; 5L5W; -.
DR PDBsum; 5L5X; -.
DR PDBsum; 5L5Y; -.
DR PDBsum; 5L5Z; -.
DR PDBsum; 5L60; -.
DR PDBsum; 5L61; -.
DR PDBsum; 5L62; -.
DR PDBsum; 5L63; -.
DR PDBsum; 5L64; -.
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; 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; 7LXV; -.
DR PDBsum; 7NHT; -.
DR PDBsum; 7PG9; -.
DR PDBsum; 7V5G; -.
DR PDBsum; 7V5M; -.
DR AlphaFoldDB; P28074; -.
DR SMR; P28074; -.
DR BioGRID; 111666; 193.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P28074; -.
DR DIP; DIP-27540N; -.
DR IntAct; P28074; 73.
DR MINT; P28074; -.
DR STRING; 9606.ENSP00000355325; -.
DR BindingDB; P28074; -.
DR ChEMBL; CHEMBL4662; -.
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; DB00188; Bortezomib.
DR DrugBank; DB08889; Carfilzomib.
DR DrugCentral; P28074; -.
DR GuidetoPHARMACOLOGY; 2406; -.
DR MEROPS; T01.012; -.
DR GlyGen; P28074; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P28074; -.
DR PhosphoSitePlus; P28074; -.
DR SwissPalm; P28074; -.
DR BioMuta; PSMB5; -.
DR DMDM; 187608890; -.
DR REPRODUCTION-2DPAGE; IPI00479306; -.
DR EPD; P28074; -.
DR jPOST; P28074; -.
DR MassIVE; P28074; -.
DR MaxQB; P28074; -.
DR PaxDb; P28074; -.
DR PeptideAtlas; P28074; -.
DR PRIDE; P28074; -.
DR ProteomicsDB; 19085; -.
DR ProteomicsDB; 54448; -. [P28074-1]
DR ProteomicsDB; 54449; -. [P28074-2]
DR TopDownProteomics; P28074-1; -. [P28074-1]
DR Antibodypedia; 22368; 246 antibodies from 34 providers.
DR DNASU; 5693; -.
DR Ensembl; ENST00000361611.11; ENSP00000355325.6; ENSG00000100804.19. [P28074-1]
DR Ensembl; ENST00000425762.2; ENSP00000395206.2; ENSG00000100804.19. [P28074-3]
DR Ensembl; ENST00000493471.2; ENSP00000452424.1; ENSG00000100804.19. [P28074-2]
DR GeneID; 5693; -.
DR KEGG; hsa:5693; -.
DR MANE-Select; ENST00000361611.11; ENSP00000355325.6; NM_002797.5; NP_002788.1.
DR UCSC; uc001wii.3; human. [P28074-1]
DR CTD; 5693; -.
DR DisGeNET; 5693; -.
DR GeneCards; PSMB5; -.
DR HGNC; HGNC:9542; PSMB5.
DR HPA; ENSG00000100804; Low tissue specificity.
DR MIM; 600306; gene.
DR neXtProt; NX_P28074; -.
DR OpenTargets; ENSG00000100804; -.
DR PharmGKB; PA33887; -.
DR VEuPathDB; HostDB:ENSG00000100804; -.
DR eggNOG; KOG0175; Eukaryota.
DR GeneTree; ENSGT00940000157841; -.
DR HOGENOM; CLU_035750_7_0_1; -.
DR InParanoid; P28074; -.
DR OMA; NLGMAMQ; -.
DR OrthoDB; 929961at2759; -.
DR PhylomeDB; P28074; -.
DR TreeFam; TF106223; -.
DR PathwayCommons; P28074; -.
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; P28074; -.
DR SIGNOR; P28074; -.
DR BioGRID-ORCS; 5693; 767 hits in 1102 CRISPR screens.
DR ChiTaRS; PSMB5; human.
DR GeneWiki; PSMB5; -.
DR GenomeRNAi; 5693; -.
DR Pharos; P28074; Tclin.
DR PRO; PR:P28074; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P28074; protein.
DR Bgee; ENSG00000100804; Expressed in gastrocnemius and 211 other tissues.
DR ExpressionAtlas; P28074; baseline and differential.
DR Genevisible; P28074; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
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; IDA:HPA.
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:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
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:0006508; P:proteolysis; IDA:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR037558; Proteasome_beta_5.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF51; PTHR11599:SF51; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Hydrolase; Nucleus; Protease; Proteasome;
KW Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..59
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:2306472"
FT /id="PRO_0000026589"
FT CHAIN 60..263
FT /note="Proteasome subunit beta type-5"
FT /id="PRO_0000026590"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:25599644,
FT ECO:0000269|PubMed:27493187"
FT BINDING 108
FT /ligand="bortezomib"
FT /ligand_id="ChEBI:CHEBI:52717"
FT /evidence="ECO:0000269|PubMed:18502982,
FT ECO:0000269|PubMed:18565852, ECO:0000269|PubMed:19426847"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045686"
FT VAR_SEQ 169..263
FT /note="GLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIY
FT QATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP -> VSEVLCLKPKSF
FT GMYLFCGCAERIGNMARPLLRGQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.7"
FT /id="VSP_041263"
FT VARIANT 24
FT /note="R -> C (in dbSNP:rs11543947)"
FT /id="VAR_051549"
FT MUTAGEN 108
FT /note="A->T: Displays resistance to the bortezomib, a
FT proteasome inhibitor of the chymotrypsin-like activity.
FT Displays high resistance to the bortezomib, a proteasome
FT inhibitor of the chymotrypsin-like activity; when
FT associated with V-109."
FT /evidence="ECO:0000269|PubMed:18502982,
FT ECO:0000269|PubMed:18565852, ECO:0000269|PubMed:19426847"
FT MUTAGEN 108
FT /note="A->V: Displays high resistance to the bortezomib, a
FT proteasome inhibitor of the chymotrypsin-like activity."
FT /evidence="ECO:0000269|PubMed:18502982,
FT ECO:0000269|PubMed:18565852, ECO:0000269|PubMed:19426847"
FT MUTAGEN 109
FT /note="A->V: Displays high resistance to the bortezomib, a
FT proteasome inhibitor of the chymotrypsin-like activity;
FT when associated with T-108."
FT /evidence="ECO:0000269|PubMed:19426847"
FT CONFLICT 3..6
FT /note="LASV -> IRGR (in Ref. 8; BAA06097)"
FT /evidence="ECO:0000305"
FT CONFLICT 3..5
FT /note="LAS -> HEG (in Ref. 6; BC004146)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="I -> F (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="A -> G (in Ref. 9; AAB33092)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="T -> S (in Ref. 9; AAB33092)"
FT /evidence="ECO:0000305"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:7NHT"
FT HELIX 108..129
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 208..225
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6KWY"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:5LE5"
SQ SEQUENCE 263 AA; 28480 MW; AED4A73DF41AA6EF CRC64;
MALASVLERP LPVNQRGFFG LGGRADLLDL GPGSLSDGLS LAAPGWGVPE EPGIEMLHGT
TTLAFKFRHG VIVAADSRAT AGAYIASQTV KKVIEINPYL LGTMAGGAAD CSFWERLLAR
QCRIYELRNK ERISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI
SGATFSVGSG SVYAYGVMDR GYSYDLEVEQ AYDLARRAIY QATYRDAYSG GAVNLYHVRE
DGWIRVSSDN VADLHEKYSG STP
