PSB4_HUMAN
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 03-AUG-2022, entry version 234.
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).
RN [38]
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: 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 (PubMed:25599644, PubMed:26133119,
CC PubMed:27342858, PubMed:27428775, PubMed:27493187, PubMed:9344905,
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:9344905, 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:9344905,
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:9344905,
CC PubMed:34711951). Forms a ternary complex with SMAD1 and OAZ1 before
CC PSMB4 is incorporated into the 20S proteasome (PubMed:11571290,
CC PubMed:12097147). Interacts with PRPF19 (PubMed:15660529).
CC {ECO:0000269|PubMed:11571290, ECO:0000269|PubMed:12097147,
CC ECO:0000269|PubMed:15660529, ECO:0000269|PubMed:25599644,
CC ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858,
CC ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187,
CC ECO:0000269|PubMed:34711951, 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,
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 -!- 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 PDB; 7AWE; X-ray; 2.29 A; N/b=46-259.
DR PDB; 7B12; X-ray; 2.43 A; 2/N=46-259.
DR PDB; 7LXV; EM; 3.40 A; M/a=46-264.
DR PDB; 7NHT; EM; 2.80 A; M=1-264.
DR PDB; 7PG9; EM; 3.70 A; N/b=46-264.
DR PDB; 7V5G; EM; 4.47 A; G/N=46-264.
DR PDB; 7V5M; EM; 3.88 A; N/b=46-264.
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 PDBsum; 7AWE; -.
DR PDBsum; 7B12; -.
DR PDBsum; 7LXV; -.
DR PDBsum; 7NHT; -.
DR PDBsum; 7PG9; -.
DR PDBsum; 7V5G; -.
DR PDBsum; 7V5M; -.
DR AlphaFoldDB; P28070; -.
DR SMR; P28070; -.
DR BioGRID; 111665; 174.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P28070; -.
DR DIP; DIP-33844N; -.
DR IntAct; P28070; 101.
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 GlyGen; P28070; 1 site, 1 O-linked glycan (1 site).
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; 459 antibodies from 35 providers.
DR DNASU; 5692; -.
DR Ensembl; ENST00000290541.7; ENSP00000290541.6; ENSG00000159377.11.
DR GeneID; 5692; -.
DR KEGG; hsa:5692; -.
DR MANE-Select; ENST00000290541.7; ENSP00000290541.6; NM_002796.3; NP_002787.2.
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; -.
DR eggNOG; KOG0185; Eukaryota.
DR GeneTree; ENSGT00390000000698; -.
DR HOGENOM; CLU_072435_2_0_1; -.
DR InParanoid; P28070; -.
DR OMA; KGYGTQT; -.
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-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; P28070; -.
DR SIGNOR; P28070; -.
DR BioGRID-ORCS; 5692; 806 hits in 1089 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 endometrium epithelium and 205 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; IDA:UniProtKB.
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; 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:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
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 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
