GenomeNet

Database: UniProt
Entry: P28070
LinkDB: P28070
Original site: P28070 
ID   PSB4_HUMAN              Reviewed;         264 AA.
AC   P28070; B2R9L3; P31148; Q5SZS5; Q6IBI4; Q969L6;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 4.
DT   02-JUN-2021, entry version 230.
DE   RecName: Full=Proteasome subunit beta type-4;
DE   AltName: Full=26 kDa prosomal protein;
DE            Short=HsBPROS26;
DE            Short=PROS-26;
DE   AltName: Full=Macropain beta chain;
DE   AltName: Full=Multicatalytic endopeptidase complex beta chain;
DE   AltName: Full=Proteasome beta chain;
DE   AltName: Full=Proteasome chain 3;
DE            Short=HsN3;
DE   Flags: Precursor;
GN   Name=PSMB4; Synonyms=PROS26;
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], AND VARIANT THR-234.
RX   PubMed=7918633; DOI=10.1016/0167-4781(94)90060-4;
RA   Nothwang H.G., Tamura T., Tanaka K., Ichihara A.;
RT   "Sequence analyses and inter-species comparisons of three novel human
RT   proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential
RT   proteolytic active-site residues.";
RL   Biochim. Biophys. Acta 1219:361-368(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-234.
RC   TISSUE=Brain;
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-234.
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-234.
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 31-264, AND VARIANT THR-234.
RX   PubMed=8013624; DOI=10.1016/0014-5793(94)00454-4;
RA   Gerards W.L., Hop F.W., Hendriks I.L., Bloemendal H.;
RT   "Cloning and expression of a human pro(tea)some beta-subunit cDNA: a
RT   homologue of the yeast PRE4-subunit essential for peptidylglutamyl-peptide
RT   hydrolase activity.";
RL   FEBS Lett. 346:151-155(1994).
RN   [8]
RP   PROTEIN SEQUENCE OF 46-73.
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   [9]
RP   PROTEIN SEQUENCE OF 46-57.
RC   TISSUE=Liver;
RA   Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA   Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA   Appel R.D., Hughes G.J.;
RL   Submitted (JUN-1992) to UniProtKB.
RN   [10]
RP   PROTEIN SEQUENCE OF 132-139; 220-224 AND 241-259.
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   [11]
RP   PROTEIN SEQUENCE OF 232-237 AND 241-253.
RC   TISSUE=Keratinocyte;
RX   PubMed=1286667; DOI=10.1002/elps.11501301199;
RA   Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA   Vandekerckhove J.;
RT   "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT   database of normal human epidermal keratinocytes.";
RL   Electrophoresis 13:960-969(1992).
RN   [12]
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   [13]
RP   INTERACTION WITH HTLV-1 PROTEIN TAX (MICROBIAL INFECTION).
RX   PubMed=8692272; DOI=10.1038/381328a0;
RA   Rousset R., Desbois C., Bantignies F., Jalinot P.;
RT   "Effects on NF-kappa B1/p105 processing of the interaction between the
RT   HTLV-1 transactivator Tax and the proteasome.";
RL   Nature 381:328-331(1996).
RN   [14]
RP   INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION).
RX   PubMed=9344905; DOI=10.1006/viro.1997.8752;
RA   Rossi F., Evstafieva A., Pedrali-Noy G., Gallina A., Milanesi G.;
RT   "HsN3 proteasomal subunit as a target for human immunodeficiency virus type
RT   1 Nef protein.";
RL   Virology 237:33-45(1997).
RN   [15]
RP   IDENTIFICATION IN A COMPLEX WITH SMAD1 AND OAZ1.
RX   PubMed=11571290; DOI=10.1074/jbc.m105500200;
RA   Gruendler C., Lin Y., Farley J., Wang T.;
RT   "Proteasomal degradation of Smad1 induced by bone morphogenetic proteins.";
RL   J. Biol. Chem. 276:46533-46543(2001).
RN   [16]
RP   IDENTIFICATION IN A COMPLEX WITH SMAD1 AND OAZ1, AND FUNCTION.
RX   PubMed=12097147; DOI=10.1186/1471-2121-3-15;
RA   Lin Y., Martin J., Gruendler C., Farley J., Meng X., Li B.-Y.,
RA   Lechleider R., Huff C., Kim R.H., Grasser W.A., Paralkar V., Wang T.;
RT   "A novel link between the proteasome pathway and the signal transduction
RT   pathway of the bone morphogenetic proteins (BMPs).";
RL   BMC Cell Biol. 3:15-15(2002).
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 PRPF19.
RX   PubMed=15660529; DOI=10.1042/bj20041517;
RA   Loescher M., Fortschegger K., Ritter G., Wostry M., Voglauer R.,
RA   Schmid J.A., Watters S., Rivett A.J., Ajuh P., Lamond A.I., Katinger H.,
RA   Grillari J.;
RT   "Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the
RT   20 S proteasome.";
RL   Biochem. J. 388:593-603(2005).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102, 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   [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=17367606; DOI=10.1016/j.humpath.2006.07.019;
RA   Kannangai R., Vivekanandan P., Martinez-Murillo F., Choti M., Torbenson M.;
RT   "Fibrolamellar carcinomas show overexpression of genes in the RAS, MAPK,
RT   PIK3, and xenobiotic degradation pathways.";
RL   Hum. Pathol. 38:639-644(2007).
RN   [24]
RP   IDENTIFICATION.
RX   PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA   Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA   Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core fucosylated
RT   glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [25]
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   [26]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [27]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [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   INVOLVEMENT IN PRAAS3, VARIANTS PRAAS3 212-ASP--VAL-214 DEL AND
RP   222-TYR--GLU-264 DEL, AND CHARACTERIZATION OF VARIANT PRAAS3
RP   212-ASP--VAL-214 DEL AND 222-TYR--GLU-264 DEL.
RX   PubMed=26524591; DOI=10.1172/jci81260;
RA   Brehm A., Liu Y., Sheikh A., Marrero B., Omoyinmi E., Zhou Q.,
RA   Montealegre G., Biancotto A., Reinhardt A., Almeida de Jesus A.,
RA   Pelletier M., Tsai W.L., Remmers E.F., Kardava L., Hill S., Kim H.,
RA   Lachmann H.J., Megarbane A., Chae J.J., Brady J., Castillo R.D., Brown D.,
RA   Casano A.V., Gao L., Chapelle D., Huang Y., Stone D., Chen Y., Sotzny F.,
RA   Lee C.C., Kastner D.L., Torrelo A., Zlotogorski A., Moir S., Gadina M.,
RA   McCoy P., Wesley R., Rother K., Hildebrand P.W., Brogan P., Krueger E.,
RA   Aksentijevich I., Goldbach-Mansky R.;
RT   "Additive loss-of-function proteasome subunit mutations in CANDLE/PRAAS
RT   patients promote type I IFN production.";
RL   J. Clin. Invest. 125:4196-4211(2015).
RN   [31]
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   [32]
RP   FUNCTION.
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   [33]
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   [34]
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   [35]
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   [36]
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   [37]
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).
CC   -!- FUNCTION: Non-catalytic component of the 20S core proteasome complex
CC       involved in the proteolytic degradation of most intracellular proteins.
CC       This complex plays numerous essential roles within the cell by
CC       associating with different regulatory particles. Associated with two
CC       19S regulatory particles, forms the 26S proteasome and thus
CC       participates in the ATP-dependent degradation of ubiquitinated
CC       proteins. The 26S proteasome plays a key role in the maintenance of
CC       protein homeostasis by removing misfolded or damaged proteins that
CC       could impair cellular functions, and by removing proteins whose
CC       functions are no longer required. Associated with the PA200 or PA28,
CC       the 20S proteasome mediates ubiquitin-independent protein degradation.
CC       This type of proteolysis is required in several pathways including
CC       spermatogenesis (20S-PA200 complex) or generation of a subset of MHC
CC       class I-presented antigenic peptides (20S-PA28 complex).
CC       SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300
CC       repressor SNIP1. {ECO:0000269|PubMed:12097147,
CC       ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742,
CC       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       Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is
CC       incorporated into the 20S proteasome. Interacts with PRPF19
CC       (PubMed:11571290, PubMed:12097147). {ECO:0000269|PubMed:11571290,
CC       ECO:0000269|PubMed:12097147, ECO:0000269|PubMed:15660529,
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:9344905}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Tax protein.
CC       {ECO:0000269|PubMed:8692272}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Nef and Tat
CC       proteins. {ECO:0000269|PubMed:14550573, ECO:0000269|PubMed:9344905}.
CC   -!- INTERACTION:
CC       P28070; P54253: ATXN1; NbExp=6; IntAct=EBI-603350, EBI-930964;
CC       P28070; P41182: BCL6; NbExp=3; IntAct=EBI-603350, EBI-765407;
CC       P28070; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-603350, EBI-8643161;
CC       P28070; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-603350, EBI-10961624;
CC       P28070; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-603350, EBI-743033;
CC       P28070; Q86UW9: DTX2; NbExp=3; IntAct=EBI-603350, EBI-740376;
CC       P28070; A1L4K1: FSD2; NbExp=3; IntAct=EBI-603350, EBI-5661036;
CC       P28070; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-603350, EBI-746969;
CC       P28070; P28676: GCA; NbExp=3; IntAct=EBI-603350, EBI-947242;
CC       P28070; Q9Y5R4: HEMK1; NbExp=3; IntAct=EBI-603350, EBI-10329202;
CC       P28070; O14964: HGS; NbExp=3; IntAct=EBI-603350, EBI-740220;
CC       P28070; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-603350, EBI-2556193;
CC       P28070; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-603350, EBI-1048945;
CC       P28070; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-603350, EBI-5662487;
CC       P28070; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-603350, EBI-10181968;
CC       P28070; Q99471: PFDN5; NbExp=3; IntAct=EBI-603350, EBI-357275;
CC       P28070; Q99697-2: PITX2; NbExp=3; IntAct=EBI-603350, EBI-12138495;
CC       P28070; Q16512: PKN1; NbExp=3; IntAct=EBI-603350, EBI-602382;
CC       P28070; O60260-5: PRKN; NbExp=3; IntAct=EBI-603350, EBI-21251460;
CC       P28070; O75360: PROP1; NbExp=3; IntAct=EBI-603350, EBI-9027467;
CC       P28070; P25788: PSMA3; NbExp=3; IntAct=EBI-603350, EBI-348380;
CC       P28070; P20618: PSMB1; NbExp=6; IntAct=EBI-603350, EBI-372273;
CC       P28070; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-603350, EBI-396669;
CC       P28070; Q15797: SMAD1; NbExp=4; IntAct=EBI-603350, EBI-1567153;
CC       P28070; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-603350, EBI-12288855;
CC       P28070; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-603350, EBI-742688;
CC       P28070; Q9H987-2: SYNPO2L; NbExp=3; IntAct=EBI-603350, EBI-12082116;
CC       P28070; Q13148: TARDBP; NbExp=3; IntAct=EBI-603350, EBI-372899;
CC       P28070; Q96M29: TEKT5; NbExp=3; IntAct=EBI-603350, EBI-10239812;
CC       P28070; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-603350, EBI-11952651;
CC       P28070; Q08117-2: TLE5; NbExp=5; IntAct=EBI-603350, EBI-11741437;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus
CC       {ECO:0000269|PubMed:12181345}.
CC   -!- INDUCTION: Up-regulated in fibrolamellar carcinomas.
CC       {ECO:0000269|PubMed:17367606}.
CC   -!- DISEASE: Proteasome-associated autoinflammatory syndrome 3 (PRAAS3)
CC       [MIM:617591]: An autoinflammatory disorder characterized by onset in
CC       early infancy and recurrent fever, nodular dermatitis, myositis,
CC       panniculitis-induced lipodystrophy, lymphadenopathy, and immune
CC       dysregulation. Variable accompanying features may include joint
CC       contractures, hepatosplenomegaly, anemia, thrombocytopenia, recurrent
CC       infections, autoantibodies, and hypergammaglobulinemia. Some patients
CC       may have intracranial calcifications. PRAAS3 inheritance is autosomal
CC       recessive or digenic. {ECO:0000269|PubMed:26524591}. Note=The disease
CC       is caused by variants affecting distinct genetic loci, including the
CC       gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
CC   -!- CAUTION: A report observed N-glycosylation at Asn-83 (PubMed:19139490).
CC       However, as the protein does not localize in an extracellular
CC       compartment of the cell, additional evidence is required to confirm
CC       this result. {ECO:0000305|PubMed:19139490}.
CC   ---------------------------------------------------------------------------
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DR   EMBL; D26600; BAA05647.1; -; mRNA.
DR   EMBL; AK313825; BAG36560.1; -; mRNA.
DR   EMBL; CR456820; CAG33101.1; -; mRNA.
DR   EMBL; BT006917; AAP35563.1; -; mRNA.
DR   EMBL; AL589764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53442.1; -; Genomic_DNA.
DR   EMBL; S71381; AAB31085.1; -; mRNA.
DR   CCDS; CCDS996.1; -.
DR   PIR; S08186; S08186.
DR   PIR; S45719; S45719.
DR   PIR; S50147; S50147.
DR   RefSeq; NP_002787.2; NM_002796.2.
DR   PDB; 4R3O; X-ray; 2.60 A; 2/N=46-262.
DR   PDB; 4R67; X-ray; 2.89 A; 2/N/b/p=46-262.
DR   PDB; 5A0Q; EM; 3.50 A; N/b=46-264.
DR   PDB; 5GJQ; EM; 4.50 A; g/u=1-264.
DR   PDB; 5GJR; EM; 3.50 A; g/u=1-264.
DR   PDB; 5L4G; EM; 4.02 A; 4/X=1-264.
DR   PDB; 5LE5; X-ray; 1.80 A; M/a=46-264.
DR   PDB; 5LEX; X-ray; 2.20 A; M/a=46-264.
DR   PDB; 5LEY; X-ray; 1.90 A; M/a=46-264.
DR   PDB; 5LEZ; X-ray; 2.19 A; M/a=46-264.
DR   PDB; 5LF0; X-ray; 2.41 A; M/a=46-264.
DR   PDB; 5LF1; X-ray; 2.00 A; M/a=46-264.
DR   PDB; 5LF3; X-ray; 2.10 A; M/a=46-264.
DR   PDB; 5LF4; X-ray; 1.99 A; M/a=46-264.
DR   PDB; 5LF6; X-ray; 2.07 A; M/a=46-264.
DR   PDB; 5LF7; X-ray; 2.00 A; M/a=46-264.
DR   PDB; 5LN3; EM; 6.80 A; 7=1-264.
DR   PDB; 5M32; EM; 3.80 A; M/a=1-264.
DR   PDB; 5T0C; EM; 3.80 A; AT/BT=2-264.
DR   PDB; 5T0G; EM; 4.40 A; T=2-264.
DR   PDB; 5T0H; EM; 6.80 A; T=2-264.
DR   PDB; 5T0I; EM; 8.00 A; T=2-264.
DR   PDB; 5T0J; EM; 8.00 A; T=2-264.
DR   PDB; 5VFO; EM; 3.50 A; T/t=46-260.
DR   PDB; 5VFP; EM; 4.20 A; T/t=46-260.
DR   PDB; 5VFQ; EM; 4.20 A; T/t=46-260.
DR   PDB; 5VFR; EM; 4.90 A; T/t=46-260.
DR   PDB; 5VFS; EM; 3.60 A; T/t=46-260.
DR   PDB; 5VFT; EM; 7.00 A; T/t=46-260.
DR   PDB; 5VFU; EM; 5.80 A; T/t=46-260.
DR   PDB; 6AVO; EM; 3.80 A; W/a=46-264.
DR   PDB; 6E5B; X-ray; 2.77 A; M/a=1-264.
DR   PDB; 6KWY; EM; 2.72 A; M/a=1-264.
DR   PDB; 6MSB; EM; 3.00 A; T/t=2-264.
DR   PDB; 6MSD; EM; 3.20 A; T/t=2-264.
DR   PDB; 6MSE; EM; 3.30 A; B=108-158.
DR   PDB; 6MSG; EM; 3.50 A; T/t=2-264.
DR   PDB; 6MSH; EM; 3.60 A; T/t=2-264.
DR   PDB; 6MSJ; EM; 3.30 A; T/t=2-264.
DR   PDB; 6MSK; EM; 3.20 A; T/t=2-264.
DR   PDB; 6R70; EM; 3.50 A; M/a=46-261.
DR   PDB; 6REY; EM; 3.00 A; N/b=46-264.
DR   PDB; 6RGQ; EM; 2.60 A; N/b=46-264.
DR   PDB; 6WJD; EM; 4.80 A; T/t=2-264.
DR   PDB; 6WJN; EM; 5.70 A; T/t=46-260.
DR   PDB; 6XMJ; EM; 3.00 A; N=46-262.
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; P28070; -.
DR   BioGRID; 111665; 156.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P28070; -.
DR   DIP; DIP-33844N; -.
DR   IntAct; P28070; 90.
DR   MINT; P28070; -.
DR   STRING; 9606.ENSP00000290541; -.
DR   BindingDB; P28070; -.
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; T01.987; -.
DR   iPTMnet; P28070; -.
DR   MetOSite; P28070; -.
DR   PhosphoSitePlus; P28070; -.
DR   BioMuta; PSMB4; -.
DR   DMDM; 116242733; -.
DR   DOSAC-COBS-2DPAGE; P28070; -.
DR   OGP; P28070; -.
DR   REPRODUCTION-2DPAGE; IPI00555956; -.
DR   SWISS-2DPAGE; P28070; -.
DR   EPD; P28070; -.
DR   jPOST; P28070; -.
DR   MassIVE; P28070; -.
DR   MaxQB; P28070; -.
DR   PaxDb; P28070; -.
DR   PeptideAtlas; P28070; -.
DR   PRIDE; P28070; -.
DR   ProteomicsDB; 54446; -.
DR   TopDownProteomics; P28070; -.
DR   Antibodypedia; 1673; 439 antibodies.
DR   DNASU; 5692; -.
DR   Ensembl; ENST00000290541; ENSP00000290541; ENSG00000159377.
DR   GeneID; 5692; -.
DR   KEGG; hsa:5692; -.
DR   UCSC; uc001eyc.2; human.
DR   CTD; 5692; -.
DR   DisGeNET; 5692; -.
DR   GeneCards; PSMB4; -.
DR   HGNC; HGNC:9541; PSMB4.
DR   HPA; ENSG00000159377; Low tissue specificity.
DR   MalaCards; PSMB4; -.
DR   MIM; 602177; gene.
DR   MIM; 617591; phenotype.
DR   neXtProt; NX_P28070; -.
DR   OpenTargets; ENSG00000159377; -.
DR   PharmGKB; PA33886; -.
DR   VEuPathDB; HostDB:ENSG00000159377.10; -.
DR   eggNOG; KOG0185; Eukaryota.
DR   GeneTree; ENSGT00390000000698; -.
DR   HOGENOM; CLU_072435_2_0_1; -.
DR   InParanoid; P28070; -.
DR   OMA; QSWAFAD; -.
DR   OrthoDB; 1228942at2759; -.
DR   PhylomeDB; P28070; -.
DR   TreeFam; TF106220; -.
DR   PathwayCommons; P28070; -.
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-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; P28070; -.
DR   BioGRID-ORCS; 5692; 796 hits in 1000 CRISPR screens.
DR   ChiTaRS; PSMB4; human.
DR   GeneWiki; PSMB4; -.
DR   GenomeRNAi; 5692; -.
DR   Pharos; P28070; Tbio.
DR   PRO; PR:P28070; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P28070; protein.
DR   Bgee; ENSG00000159377; Expressed in testis and 241 other tissues.
DR   ExpressionAtlas; P28070; baseline and differential.
DR   Genevisible; P28070; HS.
DR   GO; GO:0036064; C:ciliary basal body; IDA:GO_Central.
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:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR   GO; GO:0005839; C:proteasome core complex; ISS: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:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
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:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
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; IBA:GO_Central.
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: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:0016032; P:viral process; IEA:UniProtKB-KW.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   CDD; cd03760; proteasome_beta_type_4; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR016295; Proteasome_beta4.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF5; PTHR11599:SF5; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PIRSF; PIRSF001213; Psome_endopept_beta; 1.
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; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Disease variant; Host-virus interaction; Nucleus; Phosphoprotein;
KW   Proteasome; Reference proteome.
FT   PROPEP          1..45
FT                   /evidence="ECO:0000269|PubMed:2306472, ECO:0000269|Ref.9"
FT                   /id="PRO_0000026579"
FT   CHAIN           46..264
FT                   /note="Proteasome subunit beta type-4"
FT                   /id="PRO_0000026580"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         102
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455"
FT   VARIANT         95
FT                   /note="M -> I (in dbSNP:rs1804241)"
FT                   /id="VAR_012072"
FT   VARIANT         212..214
FT                   /note="Missing (in PRAAS3; decreased protein maturation;
FT                   changed proteasome assembly; poor incorporation into 20S
FT                   and 26S proteasomes)"
FT                   /evidence="ECO:0000269|PubMed:26524591"
FT                   /id="VAR_075255"
FT   VARIANT         222..264
FT                   /note="Missing (in PRAAS3; digenic inheritance; patient
FT                   also carries a mutation in PSMB8; no effect on protein
FT                   abundance; changed proteasome assembly; poor incorporation
FT                   into 20S and 26S proteasomes)"
FT                   /evidence="ECO:0000269|PubMed:26524591"
FT                   /id="VAR_081126"
FT   VARIANT         234
FT                   /note="I -> T (in dbSNP:rs4603)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:7918633, ECO:0000269|PubMed:8013624,
FT                   ECO:0000269|Ref.4, ECO:0000269|Ref.6"
FT                   /id="VAR_013115"
FT   CONFLICT        264
FT                   /note="E -> D (in Ref. 3; CAG33101)"
FT                   /evidence="ECO:0000305"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          56..61
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          64..70
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          87..91
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          94..101
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           102..122
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           130..146
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          153..161
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          164..170
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          172..174
FT                   /evidence="ECO:0007829|PDB:4R3O"
FT   STRAND          176..178
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          180..183
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           187..190
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           192..201
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:6REY"
FT   HELIX           207..224
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          232..238
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          241..248
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           255..258
FT                   /evidence="ECO:0007829|PDB:5LE5"
SQ   SEQUENCE   264 AA;  29204 MW;  B8701C565069F563 CRC64;
     MEAFLGSRSG LWAGGPAPGQ FYRIPSTPDS FMDPASALYR GPITRTQNPM VTGTSVLGVK
     FEGGVVIAAD MLGSYGSLAR FRNISRIMRV NNSTMLGASG DYADFQYLKQ VLGQMVIDEE
     LLGDGHSYSP RAIHSWLTRA MYSRRSKMNP LWNTMVIGGY ADGESFLGYV DMLGVAYEAP
     SLATGYGAYL AQPLLREVLE KQPVLSQTEA RDLVERCMRV LYYRDARSYN RFQIATVTEK
     GVEIEGPLST ETNWDIAHMI SGFE
//
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