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Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain epsilon chain) (Multicatalytic endopeptidase complex epsilon chain) (Proteasome chain 6) (Proteasome epsilon chain) (Proteasome subunit MB1) (Proteasome subunit X)

 PSB5_HUMAN              Reviewed;         263 AA.
P28074; B2R4N9; B4DUM9; D3DS43; E9PAV2; Q16242; Q6PEW2; Q7Z3B5;
Q86T01; Q9TNN9;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
29-APR-2008, sequence version 3.
18-JUL-2018, entry version 210.
RecName: Full=Proteasome subunit beta type-5;
EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
AltName: Full=Macropain epsilon chain;
AltName: Full=Multicatalytic endopeptidase complex epsilon chain;
AltName: Full=Proteasome chain 6;
AltName: Full=Proteasome epsilon chain;
AltName: Full=Proteasome subunit MB1;
AltName: Full=Proteasome subunit X;
Flags: Precursor;
Name=PSMB5; Synonyms=LMPX, MB1, X;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8753855; DOI=10.1007/BF02602554;
Abdulla S., Beck S., Belich M., Jackson A., Nakamura T., Trowsdale J.;
"Divergent intron arrangement in the MB1/LMP7 proteasome gene pair.";
Immunogenetics 44:254-258(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Endometrial adenocarcinoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Embryonic stem cell, Hypothalamus, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-203 (ISOFORM 2).
TISSUE=Cervix carcinoma;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-263 (ISOFORM 1), AND INDUCTION.
PubMed=8066462; DOI=10.1126/science.8066462;
Akiyama K.-Y., Yokota K.-Y., Kagawa S., Shimbara N., Tamura T.,
Akioka H., Nothwang H.G., Noda C., Tanaka K., Ichihara A.;
"cDNA cloning and interferon gamma down-regulation of proteasomal
subunits X and Y.";
Science 265:1231-1234(1994).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 49-263 (ISOFORM 1).
PubMed=7820546; DOI=10.1016/S0960-9822(00)00174-3;
Belich M.P., Glynne R.J., Senger G., Sheer D., Trowsdale J.;
"Proteasome components with reciprocal expression to that of the MHC-
encoded LMP proteins.";
Curr. Biol. 4:769-776(1994).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-263 (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 60-85.
PubMed=2306472; DOI=10.1016/0167-4838(90)90165-C;
Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N.,
Slaughter C.A.;
"Relationships among the subunits of the high molecular weight
proteinase, macropain (proteasome).";
Biochim. Biophys. Acta 1037:178-185(1990).
[12]
PROTEIN SEQUENCE OF 201-216 AND 226-239.
PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
"Human proteasome subunits from 2-dimensional gels identified by
partial sequencing.";
Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
[13]
PROTEIN SEQUENCE OF 201-216, AND SUBUNIT.
TISSUE=Kidney;
PubMed=8163024; DOI=10.1016/0014-5793(94)80612-8;
Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M.,
Kristensen P., Hendil K.B., Tanaka K., Ichihara A.;
"Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced
by interferon-gamma for acquirement of the functional diversity
responsible for antigen processing.";
FEBS Lett. 343:85-88(1994).
[14]
ERRATUM.
PubMed=7864893; DOI=10.1006/bbrc.1995.1294;
Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
Biochem. Biophys. Res. Commun. 207:1059-1059(1995).
[15]
INDUCTION.
PubMed=8663318; DOI=10.1074/jbc.271.29.17275;
Gaczynska M., Goldberg A.L., Tanaka K., Hendil K.B., Rock K.L.;
"Proteasome subunits X and Y alter peptidase activities in opposite
ways to the interferon-gamma-induced subunits LMP2 and LMP7.";
J. Biol. Chem. 271:17275-17280(1996).
[16]
FUNCTION IN ANTIGEN PRESENTATION.
PubMed=8610016; DOI=10.1038/381166a0;
Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H.,
Rammensee H.G., Koszinowski U.H., Kloetzel P.M.;
"A role for the proteasome regulator PA28alpha in antigen
presentation.";
Nature 381:166-168(1996).
[17]
SUBCELLULAR LOCATION.
PubMed=12181345; DOI=10.1091/mbc.E02-03-0122;
Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D.,
Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.;
"Clastosome: a subtype of nuclear body enriched in 19S and 20S
proteasomes, ubiquitin, and protein substrates of proteasome.";
Mol. Biol. Cell 13:2771-2782(2002).
[18]
INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
Mayer R.J., Krueger E.;
"Human immunodeficiency virus-1 Tat protein interacts with distinct
proteasomal alpha and beta subunits.";
FEBS Lett. 553:200-204(2003).
[19]
FUNCTION.
PubMed=15244466; DOI=10.1021/bm049957a;
Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
"20S proteasome prevents aggregation of heat-denatured proteins
without PA700 regulatory subcomplex like a molecular chaperone.";
Biomacromolecules 5:1465-1469(2004).
[20]
INTERACTION WITH ABCB1 AND TAP1.
PubMed=15488952; DOI=10.1016/j.molimm.2004.07.005;
Begley G.S., Horvath A.R., Taylor J.C., Higgins C.F.;
"Cytoplasmic domains of the transporter associated with antigen
processing and P-glycoprotein interact with subunits of the
proteasome.";
Mol. Immunol. 42:137-141(2005).
[21]
INTERACTION WITH POMP.
PubMed=15944226; DOI=10.1073/pnas.0501711102;
Heink S., Ludwig D., Kloetzel P.-M., Krueger E.;
"IFN-gamma-induced immune adaptation of the proteasome system is an
accelerated and transient response.";
Proc. Natl. Acad. Sci. U.S.A. 102:9241-9246(2005).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[23]
INDUCTION.
PubMed=17004105; DOI=10.1007/s10549-006-9393-7;
Deng S., Zhou H., Xiong R., Lu Y., Yan D., Xing T., Dong L., Tang E.,
Yang H.;
"Over-expression of genes and proteins of ubiquitin specific
peptidases (USPs) and proteasome subunits (PSs) in breast cancer
tissue observed by the methods of RFDD-PCR and proteomics.";
Breast Cancer Res. Treat. 104:21-30(2007).
[24]
FUNCTION, AND MUTAGENESIS OF ALA-108.
PubMed=18565852; DOI=10.1182/blood-2007-08-104950;
Oerlemans R., Franke N.E., Assaraf Y.G., Cloos J., van Zantwijk I.,
Berkers C.R., Scheffer G.L., Debipersad K., Vojtekova K., Lemos C.,
van der Heijden J.W., Ylstra B., Peters G.J., Kaspers G.L.,
Dijkmans B.A., Scheper R.J., Jansen G.;
"Molecular basis of bortezomib resistance: proteasome subunit beta5
(PSMB5) gene mutation and overexpression of PSMB5 protein.";
Blood 112:2489-2499(2008).
[25]
FUNCTION, AND MUTAGENESIS OF ALA-108.
PubMed=18502982; DOI=10.1124/jpet.108.138131;
Lue S., Yang J., Song X., Gong S., Zhou H., Guo L., Song N., Bao X.,
Chen P., Wang J.;
"Point mutation of the proteasome beta5 subunit gene is an important
mechanism of bortezomib resistance in bortezomib-selected variants of
Jurkat T cell lymphoblastic lymphoma/leukemia line.";
J. Pharmacol. Exp. Ther. 326:423-431(2008).
[26]
MUTAGENESIS OF ALA-108 AND ALA-109.
PubMed=19426847; DOI=10.1016/j.exphem.2009.04.001;
Lue S., Yang J., Chen Z., Gong S., Zhou H., Xu X., Wang J.;
"Different mutants of PSMB5 confer varying bortezomib resistance in T
lymphoblastic lymphoma/leukemia cells derived from the Jurkat cell
line.";
Exp. Hematol. 37:831-837(2009).
[27]
INDUCTION BY SULFORAPHANE.
PubMed=18602823; DOI=10.1016/j.jnutbio.2008.02.002;
Ramirez M.C., Singletary K.;
"Regulation of estrogen receptor alpha expression in human breast
cancer cells by sulforaphane.";
J. Nutr. Biochem. 20:195-201(2009).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=27176742; DOI=10.1515/hsz-2016-0176;
Rut W., Drag M.;
"Human 20S proteasome activity towards fluorogenic peptides of various
chain lengths.";
Biol. Chem. 397:921-926(2016).
[31]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=26133119; DOI=10.1038/ncomms8573;
da Fonseca P.C., Morris E.P.;
"Cryo-EM reveals the conformation of a substrate analogue in the human
20S proteasome core.";
Nat. Commun. 6:7573-7573(2015).
[32]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 60-260, SUBUNIT, AND ACTIVE
SITE.
PubMed=25599644; DOI=10.1016/j.str.2014.11.017;
Harshbarger W., Miller C., Diedrich C., Sacchettini J.;
"Crystal structure of the human 20S proteasome in complex with
carfilzomib.";
Structure 23:418-424(2015).
[33]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[34]
STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), AND SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
[35]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
PubMed=27493187; DOI=10.1126/science.aaf8993;
Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
Stark H., Bourenkov G., Chari A.;
"The inhibition mechanism of human 20S proteasomes enables next-
generation inhibitor design.";
Science 353:594-598(2016).
-!- FUNCTION: Component of the 20S core proteasome complex involved in
the proteolytic degradation of most intracellular proteins. This
complex plays numerous essential roles within the cell by
associating with different regulatory particles. Associated with
two 19S regulatory particles, forms the 26S proteasome and thus
participates in the ATP-dependent degradation of ubiquitinated
proteins. The 26S proteasome plays a key role in the maintenance
of protein homeostasis by removing misfolded or damaged proteins
that could impair cellular functions, and by removing proteins
whose functions are no longer required. Associated with the PA200
or PA28, the 20S proteasome mediates ubiquitin-independent protein
degradation. This type of proteolysis is required in several
pathways including spermatogenesis (20S-PA200 complex) or
generation of a subset of MHC class I-presented antigenic peptides
(20S-PA28 complex). Within the 20S core complex, PSMB5 displays a
chymotrypsin-like activity. {ECO:0000269|PubMed:15244466,
ECO:0000269|PubMed:18502982, ECO:0000269|PubMed:18565852,
ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000269|PubMed:27176742}.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is a barrel-
shaped complex made of 28 subunits that are arranged in four
stacked rings. The two outer rings are each formed by seven alpha
subunits, and the two inner rings are formed by seven beta
subunits. The proteolytic activity is exerted by three beta-
subunits PSMB5, PSMB6 and PSMB7. Directly interacts with POMP
(PubMed:15944226). Interacts with ABCB1 and TAP1
(PubMed:15488952). {ECO:0000269|PubMed:15488952,
ECO:0000269|PubMed:15944226, ECO:0000269|PubMed:25599644,
ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858,
ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187,
ECO:0000269|PubMed:8163024}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 TAT protein.
{ECO:0000269|PubMed:14550573}.
-!- INTERACTION:
Q9Y244:POMP; NbExp=3; IntAct=EBI-357828, EBI-696895;
P20618:PSMB1; NbExp=3; IntAct=EBI-357828, EBI-372273;
Q99436:PSMB7; NbExp=7; IntAct=EBI-357828, EBI-603319;
Q9Y4K3:TRAF6; NbExp=2; IntAct=EBI-357828, EBI-359276;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}.
Nucleus {ECO:0000269|PubMed:12181345}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P28074-1; Sequence=Displayed;
Name=2;
IsoId=P28074-2; Sequence=VSP_041263;
Name=3;
IsoId=P28074-3; Sequence=VSP_045686;
Note=No experimental confirmation available.;
-!- INDUCTION: Down-regulated by IFNG/IFN-gamma (at protein level).
Induced in breast cancer tissue. Up-regulated by sulforaphane in
breast cancer cells. {ECO:0000269|PubMed:17004105,
ECO:0000269|PubMed:18602823, ECO:0000269|PubMed:8066462,
ECO:0000269|PubMed:8663318}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
-!- SEQUENCE CAUTION:
Sequence=AAP35423.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA06097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAD97956.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X95586; CAA64838.1; -; Genomic_DNA.
EMBL; AK300714; BAG62391.1; -; mRNA.
EMBL; AK311895; BAG34836.1; -; mRNA.
EMBL; BX538001; CAD97956.1; ALT_INIT; mRNA.
EMBL; AL132780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471078; EAW66193.1; -; Genomic_DNA.
EMBL; CH471078; EAW66195.1; -; Genomic_DNA.
EMBL; BC004146; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC057840; AAH57840.1; -; mRNA.
EMBL; BC107720; AAI07721.1; -; mRNA.
EMBL; CD048996; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BX248299; CAD62626.1; -; mRNA.
EMBL; D29011; BAA06097.1; ALT_INIT; mRNA.
EMBL; S74378; AAB33092.1; -; mRNA.
EMBL; BT006777; AAP35423.1; ALT_INIT; mRNA.
CCDS; CCDS45083.1; -. [P28074-3]
CCDS; CCDS45084.1; -. [P28074-2]
CCDS; CCDS9584.1; -. [P28074-1]
PIR; A54589; A54589.
PIR; I52906; I52906.
PIR; PC2328; PC2328.
PIR; S08189; S08189.
RefSeq; NP_001124197.1; NM_001130725.1. [P28074-3]
RefSeq; NP_001138404.1; NM_001144932.2. [P28074-2]
RefSeq; NP_002788.1; NM_002797.4. [P28074-1]
UniGene; Hs.422990; -.
PDB; 4R3O; X-ray; 2.60 A; L/Z=60-260.
PDB; 4R67; X-ray; 2.89 A; 3/L/Z/n=60-260.
PDB; 5A0Q; EM; 3.50 A; L/Z=60-263.
PDB; 5GJQ; EM; 4.50 A; e/s=1-263.
PDB; 5GJR; EM; 3.50 A; e/s=1-263.
PDB; 5L4G; EM; 4.02 A; 5/Y=1-263.
PDB; 5L5W; X-ray; 2.80 A; K/Y=60-197.
PDB; 5L5X; X-ray; 2.90 A; K/Y=60-197.
PDB; 5L5Y; X-ray; 2.70 A; K/Y=60-197.
PDB; 5L5Z; X-ray; 2.70 A; K/Y=60-197.
PDB; 5L60; X-ray; 2.70 A; K/Y=60-197.
PDB; 5L61; X-ray; 2.80 A; K/Y=60-193.
PDB; 5L62; X-ray; 2.80 A; K/Y=60-197.
PDB; 5L63; X-ray; 2.70 A; K/Y=60-197.
PDB; 5L64; X-ray; 2.70 A; K/Y=60-197.
PDB; 5LE5; X-ray; 1.80 A; K/Y=60-263.
PDB; 5LEX; X-ray; 2.20 A; K/Y=60-263.
PDB; 5LEY; X-ray; 1.90 A; K/Y=60-263.
PDB; 5LEZ; X-ray; 2.19 A; K/Y=60-263.
PDB; 5LF0; X-ray; 2.41 A; K/Y=60-263.
PDB; 5LF1; X-ray; 2.00 A; K/Y=60-263.
PDB; 5LF3; X-ray; 2.10 A; K/Y=60-263.
PDB; 5LF4; X-ray; 1.99 A; K/Y=60-263.
PDB; 5LF6; X-ray; 2.07 A; K/Y=60-263.
PDB; 5LF7; X-ray; 2.00 A; K/Y=60-263.
PDB; 5LN3; EM; 6.80 A; 5=1-263.
PDB; 5M32; EM; 3.80 A; K/Y=60-263.
PDB; 5T0C; EM; 3.80 A; AR/BR=2-263.
PDB; 5T0G; EM; 4.40 A; R=2-263.
PDB; 5T0H; EM; 6.80 A; R=2-263.
PDB; 5T0I; EM; 8.00 A; R=2-263.
PDB; 5T0J; EM; 8.00 A; R=2-263.
PDBsum; 4R3O; -.
PDBsum; 4R67; -.
PDBsum; 5A0Q; -.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4G; -.
PDBsum; 5L5W; -.
PDBsum; 5L5X; -.
PDBsum; 5L5Y; -.
PDBsum; 5L5Z; -.
PDBsum; 5L60; -.
PDBsum; 5L61; -.
PDBsum; 5L62; -.
PDBsum; 5L63; -.
PDBsum; 5L64; -.
PDBsum; 5LE5; -.
PDBsum; 5LEX; -.
PDBsum; 5LEY; -.
PDBsum; 5LEZ; -.
PDBsum; 5LF0; -.
PDBsum; 5LF1; -.
PDBsum; 5LF3; -.
PDBsum; 5LF4; -.
PDBsum; 5LF6; -.
PDBsum; 5LF7; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
ProteinModelPortal; P28074; -.
SMR; P28074; -.
BioGrid; 111666; 106.
CORUM; P28074; -.
DIP; DIP-27540N; -.
IntAct; P28074; 48.
MINT; P28074; -.
STRING; 9606.ENSP00000355325; -.
BindingDB; P28074; -.
ChEMBL; CHEMBL4662; -.
DrugBank; DB00188; Bortezomib.
DrugBank; DB08889; Carfilzomib.
GuidetoPHARMACOLOGY; 2406; -.
MEROPS; T01.012; -.
iPTMnet; P28074; -.
PhosphoSitePlus; P28074; -.
SwissPalm; P28074; -.
BioMuta; PSMB5; -.
DMDM; 187608890; -.
REPRODUCTION-2DPAGE; IPI00479306; -.
EPD; P28074; -.
MaxQB; P28074; -.
PaxDb; P28074; -.
PeptideAtlas; P28074; -.
PRIDE; P28074; -.
ProteomicsDB; 54448; -.
ProteomicsDB; 54449; -. [P28074-2]
TopDownProteomics; P28074-1; -. [P28074-1]
DNASU; 5693; -.
Ensembl; ENST00000361611; ENSP00000355325; ENSG00000100804. [P28074-1]
Ensembl; ENST00000425762; ENSP00000395206; ENSG00000100804. [P28074-3]
Ensembl; ENST00000493471; ENSP00000452424; ENSG00000100804. [P28074-2]
GeneID; 5693; -.
KEGG; hsa:5693; -.
UCSC; uc001wii.3; human. [P28074-1]
CTD; 5693; -.
DisGeNET; 5693; -.
EuPathDB; HostDB:ENSG00000100804.18; -.
GeneCards; PSMB5; -.
HGNC; HGNC:9542; PSMB5.
HPA; HPA049518; -.
HPA; HPA061796; -.
MIM; 600306; gene.
neXtProt; NX_P28074; -.
OpenTargets; ENSG00000100804; -.
PharmGKB; PA33887; -.
eggNOG; KOG0175; Eukaryota.
eggNOG; ENOG410XQRP; LUCA.
GeneTree; ENSGT00510000046395; -.
HOVERGEN; HBG108297; -.
InParanoid; P28074; -.
KO; K02737; -.
OMA; TMCAGVT; -.
OrthoDB; EOG091G0BPS; -.
PhylomeDB; P28074; -.
TreeFam; TF106223; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; P28074; -.
ChiTaRS; PSMB5; human.
GeneWiki; PSMB5; -.
GenomeRNAi; 5693; -.
PRO; PR:P28074; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100804; -.
CleanEx; HS_PSMB5; -.
ExpressionAtlas; P28074; baseline and differential.
Genevisible; P28074; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006508; P:proteolysis; IDA:MGI.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000243; Pept_T1A_subB.
InterPro; IPR037558; Proteasome_beta_5.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF51; PTHR11599:SF51; 1.
Pfam; PF00227; Proteasome; 1.
PRINTS; PR00141; PROTEASOME.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Host-virus interaction; Hydrolase; Nucleus;
Polymorphism; Protease; Proteasome; Reference proteome;
Threonine protease; Zymogen.
PROPEP 1 59 Removed in mature form.
{ECO:0000269|PubMed:2306472}.
/FTId=PRO_0000026589.
CHAIN 60 263 Proteasome subunit beta type-5.
/FTId=PRO_0000026590.
ACT_SITE 60 60 Nucleophile.
{ECO:0000269|PubMed:25599644,
ECO:0000269|PubMed:27493187}.
BINDING 108 108 Bortezomib; via amide nitrogen.
{ECO:0000250}.
VAR_SEQ 1 103 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045686.
VAR_SEQ 169 263 GLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVE
QAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDN
VADLHEKYSGSTP -> VSEVLCLKPKSFGMYLFCGCAERI
GNMARPLLRGQ (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.7}.
/FTId=VSP_041263.
VARIANT 24 24 R -> C (in dbSNP:rs11543947).
/FTId=VAR_051549.
MUTAGEN 108 108 A->T: Displays resistance to the
bortezomib, a proteasome inhibitor of the
chymotrypsin-like activity. Displays high
resistance to the bortezomib, a
proteasome inhibitor of the chymotrypsin-
like activity; when associated with V-
109. {ECO:0000269|PubMed:18502982,
ECO:0000269|PubMed:18565852,
ECO:0000269|PubMed:19426847}.
MUTAGEN 108 108 A->V: Displays high resistance to the
bortezomib, a proteasome inhibitor of the
chymotrypsin-like activity.
{ECO:0000269|PubMed:18502982,
ECO:0000269|PubMed:18565852,
ECO:0000269|PubMed:19426847}.
MUTAGEN 109 109 A->V: Displays high resistance to the
bortezomib, a proteasome inhibitor of the
chymotrypsin-like activity; when
associated with T-108.
{ECO:0000269|PubMed:19426847}.
CONFLICT 3 6 LASV -> IRGR (in Ref. 8; BAA06097).
{ECO:0000305}.
CONFLICT 3 5 LAS -> HEG (in Ref. 6; BC004146).
{ECO:0000305}.
CONFLICT 85 85 I -> F (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 109 109 A -> G (in Ref. 9; AAB33092).
{ECO:0000305}.
CONFLICT 158 158 T -> S (in Ref. 9; AAB33092).
{ECO:0000305}.
STRAND 62 67 {ECO:0000244|PDB:5LE5}.
STRAND 70 75 {ECO:0000244|PDB:5LE5}.
STRAND 79 81 {ECO:0000244|PDB:5LE5}.
STRAND 84 88 {ECO:0000244|PDB:5LE5}.
STRAND 93 97 {ECO:0000244|PDB:5LE5}.
STRAND 100 103 {ECO:0000244|PDB:5LE5}.
HELIX 108 129 {ECO:0000244|PDB:5LE5}.
HELIX 135 147 {ECO:0000244|PDB:5LE5}.
TURN 148 151 {ECO:0000244|PDB:5LE5}.
STRAND 156 164 {ECO:0000244|PDB:5LE5}.
STRAND 167 174 {ECO:0000244|PDB:5LE5}.
STRAND 179 181 {ECO:0000244|PDB:5LE5}.
STRAND 183 188 {ECO:0000244|PDB:5LE5}.
HELIX 191 201 {ECO:0000244|PDB:5LE5}.
HELIX 208 225 {ECO:0000244|PDB:5LE5}.
STRAND 231 239 {ECO:0000244|PDB:5LE5}.
STRAND 242 250 {ECO:0000244|PDB:5LE5}.
HELIX 251 258 {ECO:0000244|PDB:5LE5}.
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


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