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Proteasome subunit beta type-4 (EC 3.4.25.1) (26 kDa prosomal protein) (HsBPROS26) (PROS-26) (Macropain beta chain) (Multicatalytic endopeptidase complex beta chain) (Proteasome beta chain) (Proteasome chain 3) (HsN3)

 PSB4_HUMAN              Reviewed;         264 AA.
P28070; B2R9L3; P31148; Q5SZS5; Q6IBI4; Q969L6;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 4.
22-NOV-2017, entry version 200.
RecName: Full=Proteasome subunit beta type-4;
EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
AltName: Full=26 kDa prosomal protein;
Short=HsBPROS26;
Short=PROS-26;
AltName: Full=Macropain beta chain;
AltName: Full=Multicatalytic endopeptidase complex beta chain;
AltName: Full=Proteasome beta chain;
AltName: Full=Proteasome chain 3;
Short=HsN3;
Flags: Precursor;
Name=PSMB4; Synonyms=PROS26;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-234.
PubMed=7918633; DOI=10.1016/0167-4781(94)90060-4;
Nothwang H.G., Tamura T., Tanaka K., Ichihara A.;
"Sequence analyses and inter-species comparisons of three novel human
proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential
proteolytic active-site residues.";
Biochim. Biophys. Acta 1219:361-368(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-234.
TISSUE=Brain;
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].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-234.
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-234.
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.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 31-264, AND VARIANT THR-234.
PubMed=8013624; DOI=10.1016/0014-5793(94)00454-4;
Gerards W.L., Hop F.W., Hendriks I.L., Bloemendal H.;
"Cloning and expression of a human pro(tea)some beta-subunit cDNA: a
homologue of the yeast PRE4-subunit essential for peptidylglutamyl-
peptide hydrolase activity.";
FEBS Lett. 346:151-155(1994).
[8]
PROTEIN SEQUENCE OF 46-73.
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).
[9]
PROTEIN SEQUENCE OF 46-57.
TISSUE=Liver;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
Submitted (JUN-1992) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 132-139; 220-224 AND 241-259.
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).
[11]
PROTEIN SEQUENCE OF 232-237 AND 241-253.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[12]
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).
[13]
INTERACTION WITH HTLV-1 TAX.
PubMed=8692272; DOI=10.1038/381328a0;
Rousset R., Desbois C., Bantignies F., Jalinot P.;
"Effects on NF-kappa B1/p105 processing of the interaction between the
HTLV-1 transactivator Tax and the proteasome.";
Nature 381:328-331(1996).
[14]
INTERACTION WITH HIV-1 NEF.
PubMed=9344905; DOI=10.1006/viro.1997.8752;
Rossi F., Evstafieva A., Pedrali-Noy G., Gallina A., Milanesi G.;
"HsN3 proteasomal subunit as a target for human immunodeficiency virus
type 1 Nef protein.";
Virology 237:33-45(1997).
[15]
IDENTIFICATION IN A COMPLEX WITH SMAD1 AND OAZ1.
PubMed=11571290; DOI=10.1074/jbc.M105500200;
Gruendler C., Lin Y., Farley J., Wang T.;
"Proteasomal degradation of Smad1 induced by bone morphogenetic
proteins.";
J. Biol. Chem. 276:46533-46543(2001).
[16]
IDENTIFICATION IN A COMPLEX WITH SMAD1 AND OAZ1, AND FUNCTION.
PubMed=12097147; DOI=10.1186/1471-2121-3-15;
Lin Y., Martin J., Gruendler C., Farley J., Meng X., Li B.-Y.,
Lechleider R., Huff C., Kim R.H., Grasser W.A., Paralkar V., Wang T.;
"A novel link between the proteasome pathway and the signal
transduction pathway of the bone morphogenetic proteins (BMPs).";
BMC Cell Biol. 3:15-15(2002).
[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.
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 PRPF19.
PubMed=15660529; DOI=10.1042/BJ20041517;
Loescher M., Fortschegger K., Ritter G., Wostry M., Voglauer R.,
Schmid J.A., Watters S., Rivett A.J., Ajuh P., Lamond A.I.,
Katinger H., Grillari J.;
"Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of
the 20 S proteasome.";
Biochem. J. 388:593-603(2005).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(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=17367606; DOI=10.1016/j.humpath.2006.07.019;
Kannangai R., Vivekanandan P., Martinez-Murillo F., Choti M.,
Torbenson M.;
"Fibrolamellar carcinomas show overexpression of genes in the RAS,
MAPK, PIK3, and xenobiotic degradation pathways.";
Hum. Pathol. 38:639-644(2007).
[24]
IDENTIFICATION.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[25]
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).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[31]
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).
[32]
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).
[33]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), AND SUBUNIT.
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).
[34]
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).
[35]
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).
[36]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
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).
[37]
VARIANT 212-ASP--VAL-214 DEL, AND CHARACTERIZATION OF VARIANT
212-ASP--VAL-214 DEL.
PubMed=26524591; DOI=10.1172/JCI81260;
Brehm A., Liu Y., Sheikh A., Marrero B., Omoyinmi E., Zhou Q.,
Montealegre G., Biancotto A., Reinhardt A., Almeida de Jesus A.,
Pelletier M., Tsai W.L., Remmers E.F., Kardava L., Hill S., Kim H.,
Lachmann H.J., Megarbane A., Chae J.J., Brady J., Castillo R.D.,
Brown D., Casano A.V., Gao L., Chapelle D., Huang Y., Stone D.,
Chen Y., Sotzny F., Lee C.C., Kastner D.L., Torrelo A.,
Zlotogorski A., Moir S., Gadina M., McCoy P., Wesley R., Rother K.,
Hildebrand P.W., Brogan P., Krueger E., Aksentijevich I.,
Goldbach-Mansky R.;
"Additive loss-of-function proteasome subunit mutations in
CANDLE/PRAAS patients promote type I IFN production.";
J. Clin. Invest. 125:4196-4211(2015).
-!- 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). SMAD1/OAZ1/PSMB4 complex mediates the
degradation of the CREBBP/EP300 repressor SNIP1.
{ECO:0000269|PubMed:12097147, ECO:0000269|PubMed:15244466,
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. Interacts with HIV-1 TAT and HIV-
1 NEF proteins (PubMed:14550573). Interaction with HTLV-1 TAX
protein favors NFKB1 activation (PubMed:8692272). Forms a ternary
complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the
20S proteasome. Interacts with PRPF19 (PubMed:11571290,
PubMed:12097147). {ECO:0000269|PubMed:11571290,
ECO:0000269|PubMed:12097147, ECO:0000269|PubMed:14550573,
ECO:0000269|PubMed:15660529, ECO:0000269|PubMed:25599644,
ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858,
ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187,
ECO:0000269|PubMed:8692272, ECO:0000269|PubMed:9344905}.
-!- INTERACTION:
A1L4K1:FSD2; NbExp=3; IntAct=EBI-603350, EBI-5661036;
P25788:PSMA3; NbExp=3; IntAct=EBI-603350, EBI-348380;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}.
Nucleus {ECO:0000269|PubMed:12181345}.
-!- INDUCTION: Up-regulated in fibrolamellar carcinomas.
{ECO:0000269|PubMed:17367606}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
-!- CAUTION: A report observed N-glycosylation at Asn-83
(PubMed:19139490). However, as the protein does not localize in an
extracellular compartment of the cell, additional evidences are
required to confirm this result. {ECO:0000305|PubMed:19139490}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D26600; BAA05647.1; -; mRNA.
EMBL; AK313825; BAG36560.1; -; mRNA.
EMBL; CR456820; CAG33101.1; -; mRNA.
EMBL; BT006917; AAP35563.1; -; mRNA.
EMBL; AL589764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53442.1; -; Genomic_DNA.
EMBL; S71381; AAB31085.1; -; mRNA.
CCDS; CCDS996.1; -.
PIR; S08186; S08186.
PIR; S45719; S45719.
PIR; S50147; S50147.
RefSeq; NP_002787.2; NM_002796.2.
UniGene; Hs.89545; -.
PDB; 4R3O; X-ray; 2.60 A; 2/N=46-262.
PDB; 4R67; X-ray; 2.89 A; 2/N/b/p=46-262.
PDB; 5A0Q; EM; 3.50 A; N/b=46-264.
PDB; 5GJQ; EM; 4.50 A; g/u=1-264.
PDB; 5GJR; EM; 3.50 A; g/u=1-264.
PDB; 5L4G; EM; 4.02 A; 4/X=1-264.
PDB; 5LE5; X-ray; 1.80 A; M/a=46-264.
PDB; 5LEX; X-ray; 2.20 A; M/a=46-264.
PDB; 5LEY; X-ray; 1.90 A; M/a=46-264.
PDB; 5LEZ; X-ray; 2.19 A; M/a=46-264.
PDB; 5LF0; X-ray; 2.41 A; M/a=46-264.
PDB; 5LF1; X-ray; 2.00 A; M/a=46-264.
PDB; 5LF3; X-ray; 2.10 A; M/a=46-264.
PDB; 5LF4; X-ray; 1.99 A; M/a=46-264.
PDB; 5LF6; X-ray; 2.07 A; M/a=46-264.
PDB; 5LF7; X-ray; 2.00 A; M/a=46-264.
PDB; 5LN3; EM; 6.80 A; 7=1-264.
PDB; 5M32; EM; 3.80 A; M/a=1-264.
PDB; 5T0C; EM; 3.80 A; AT/BT=2-264.
PDB; 5T0G; EM; 4.40 A; T=2-264.
PDB; 5T0H; EM; 6.80 A; T=2-264.
PDB; 5T0I; EM; 8.00 A; T=2-264.
PDB; 5T0J; EM; 8.00 A; T=2-264.
PDBsum; 4R3O; -.
PDBsum; 4R67; -.
PDBsum; 5A0Q; -.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4G; -.
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; P28070; -.
SMR; P28070; -.
BioGrid; 111665; 97.
CORUM; P28070; -.
DIP; DIP-33844N; -.
IntAct; P28070; 46.
MINT; MINT-1192686; -.
STRING; 9606.ENSP00000290541; -.
BindingDB; P28070; -.
ChEMBL; CHEMBL3831201; -.
MEROPS; T01.987; -.
iPTMnet; P28070; -.
PhosphoSitePlus; P28070; -.
BioMuta; PSMB4; -.
DMDM; 116242733; -.
DOSAC-COBS-2DPAGE; P28070; -.
OGP; P28070; -.
REPRODUCTION-2DPAGE; IPI00555956; -.
SWISS-2DPAGE; P28070; -.
EPD; P28070; -.
MaxQB; P28070; -.
PaxDb; P28070; -.
PeptideAtlas; P28070; -.
PRIDE; P28070; -.
TopDownProteomics; P28070; -.
DNASU; 5692; -.
Ensembl; ENST00000290541; ENSP00000290541; ENSG00000159377.
GeneID; 5692; -.
KEGG; hsa:5692; -.
UCSC; uc001eyc.2; human.
CTD; 5692; -.
DisGeNET; 5692; -.
EuPathDB; HostDB:ENSG00000159377.10; -.
GeneCards; PSMB4; -.
HGNC; HGNC:9541; PSMB4.
HPA; HPA006700; -.
MIM; 602177; gene.
neXtProt; NX_P28070; -.
OpenTargets; ENSG00000159377; -.
PharmGKB; PA33886; -.
eggNOG; KOG0185; Eukaryota.
eggNOG; ENOG410YAMA; LUCA.
GeneTree; ENSGT00390000000698; -.
HOGENOM; HOG000181719; -.
HOVERGEN; HBG018194; -.
InParanoid; P28070; -.
KO; K02736; -.
OMA; KECMKVL; -.
OrthoDB; EOG091G0JV7; -.
PhylomeDB; P28070; -.
TreeFam; TF106220; -.
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-446652; Interleukin-1 family signaling.
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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSMB4; human.
GeneWiki; PSMB4; -.
GenomeRNAi; 5692; -.
PRO; PR:P28070; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000159377; -.
CleanEx; HS_PSMB4; -.
ExpressionAtlas; P28070; baseline and differential.
Genevisible; P28070; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
CDD; cd03760; proteasome_beta_type_4; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR016295; Proteasome_endopept_cplx_B.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF5; PTHR11599:SF5; 1.
Pfam; PF00227; Proteasome; 1.
PIRSF; PIRSF001213; Psome_endopept_beta; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Host-virus interaction; Hydrolase; Nucleus;
Phosphoprotein; Polymorphism; Protease; Proteasome;
Reference proteome; Threonine protease; Zymogen.
PROPEP 1 45 {ECO:0000269|PubMed:2306472,
ECO:0000269|Ref.9}.
/FTId=PRO_0000026579.
CHAIN 46 264 Proteasome subunit beta type-4.
/FTId=PRO_0000026580.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 102 102 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
VARIANT 95 95 M -> I (in dbSNP:rs1804241).
/FTId=VAR_012072.
VARIANT 212 214 Missing (found in a patient with Nakajo
syndrome; unknown pathological
significance; patients' cells show
proteasome assembly defects).
{ECO:0000269|PubMed:26524591}.
/FTId=VAR_075255.
VARIANT 234 234 I -> T (in dbSNP:rs4603).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:7918633,
ECO:0000269|PubMed:8013624,
ECO:0000269|Ref.4, ECO:0000269|Ref.6}.
/FTId=VAR_013115.
CONFLICT 264 264 E -> D (in Ref. 3; CAG33101).
{ECO:0000305}.
STRAND 51 53 {ECO:0000244|PDB:5LE5}.
STRAND 56 61 {ECO:0000244|PDB:5LE5}.
STRAND 64 70 {ECO:0000244|PDB:5LE5}.
STRAND 73 75 {ECO:0000244|PDB:5LE5}.
STRAND 78 81 {ECO:0000244|PDB:5LE5}.
STRAND 87 91 {ECO:0000244|PDB:5LE5}.
STRAND 94 101 {ECO:0000244|PDB:5LE5}.
HELIX 102 122 {ECO:0000244|PDB:5LE5}.
HELIX 130 146 {ECO:0000244|PDB:5LE5}.
STRAND 153 161 {ECO:0000244|PDB:5LE5}.
STRAND 164 170 {ECO:0000244|PDB:5LE5}.
STRAND 172 174 {ECO:0000244|PDB:4R3O}.
STRAND 176 178 {ECO:0000244|PDB:5LE5}.
STRAND 180 183 {ECO:0000244|PDB:5LE5}.
HELIX 187 190 {ECO:0000244|PDB:5LE5}.
HELIX 192 201 {ECO:0000244|PDB:5LE5}.
STRAND 202 204 {ECO:0000244|PDB:5A0Q}.
HELIX 207 224 {ECO:0000244|PDB:5LE5}.
STRAND 232 238 {ECO:0000244|PDB:5LE5}.
STRAND 241 248 {ECO:0000244|PDB:5LE5}.
HELIX 255 258 {ECO:0000244|PDB:5LE5}.
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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