GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

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.
13-FEB-2019, entry version 214.
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 PROTEIN TAX (MICROBIAL INFECTION).
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 (MICROBIAL INFECTION).
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 (MICROBIAL INFECTION).
PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
Mayer R.J., Krueger E.;
"Human immunodeficiency virus-1 Tat protein interacts with distinct
proteasomal alpha and beta subunits.";
FEBS Lett. 553:200-204(2003).
[19]
FUNCTION.
PubMed=15244466; DOI=10.1021/bm049957a;
Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
"20S proteasome prevents aggregation of heat-denatured proteins
without PA700 regulatory subcomplex like a molecular chaperone.";
Biomacromolecules 5:1465-1469(2004).
[20]
INTERACTION WITH 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]
INVOLVEMENT IN PRAAS3, VARIANTS PRAAS3 212-ASP--VAL-214 DEL AND
222-TYR--GLU-264 DEL, AND CHARACTERIZATION OF VARIANT PRAAS3
212-ASP--VAL-214 DEL AND 222-TYR--GLU-264 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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
-!- 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:
Reaction=Cleavage of peptide bonds with very broad specificity.;
EC=3.4.25.1; Evidence={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. 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:15660529,
ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119,
ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
ECO:0000269|PubMed:27493187, ECO:0000269|PubMed:9344905}.
-!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Tax protein.
{ECO:0000269|PubMed:8692272}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Nef and Tat
proteins. {ECO:0000269|PubMed:14550573,
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}.
-!- DISEASE: Proteasome-associated autoinflammatory syndrome 3
(PRAAS3) [MIM:617591]: An autoinflammatory disorder characterized
by onset in early infancy and recurrent fever, nodular dermatitis,
myositis, panniculitis-induced lipodystrophy, lymphadenopathy, and
immune dysregulation. Variable accompanying features may include
joint contractures, hepatosplenomegaly, anemia, thrombocytopenia,
recurrent infections, autoantibodies, and hypergammaglobulinemia.
Some patients may have intracranial calcifications. PRAAS3
inheritance is autosomal recessive or digenic.
{ECO:0000269|PubMed:26524591}. Note=The disease is caused by
mutations affecting distinct genetic loci, including the gene
represented in this entry.
-!- 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 https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) 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.
PDB; 5VFO; EM; 3.50 A; T/t=46-260.
PDB; 5VFP; EM; 4.20 A; T/t=46-260.
PDB; 5VFQ; EM; 4.20 A; T/t=46-260.
PDB; 5VFR; EM; 4.90 A; T/t=46-260.
PDB; 5VFS; EM; 3.60 A; T/t=46-260.
PDB; 5VFT; EM; 7.00 A; T/t=46-260.
PDB; 5VFU; EM; 5.80 A; T/t=46-260.
PDB; 6AVO; EM; 3.80 A; W/a=46-264.
PDB; 6MSB; EM; 3.00 A; T/t=2-264.
PDB; 6MSD; EM; 3.20 A; T/t=2-264.
PDB; 6MSE; EM; 3.30 A; B=108-158.
PDB; 6MSG; EM; 3.50 A; T/t=2-264.
PDB; 6MSH; EM; 3.60 A; T/t=2-264.
PDB; 6MSJ; EM; 3.30 A; T/t=2-264.
PDB; 6MSK; EM; 3.20 A; T/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; -.
PDBsum; 5VFO; -.
PDBsum; 5VFP; -.
PDBsum; 5VFQ; -.
PDBsum; 5VFR; -.
PDBsum; 5VFS; -.
PDBsum; 5VFT; -.
PDBsum; 5VFU; -.
PDBsum; 6AVO; -.
PDBsum; 6MSB; -.
PDBsum; 6MSD; -.
PDBsum; 6MSE; -.
PDBsum; 6MSG; -.
PDBsum; 6MSH; -.
PDBsum; 6MSJ; -.
PDBsum; 6MSK; -.
ProteinModelPortal; P28070; -.
SMR; P28070; -.
BioGrid; 111665; 106.
CORUM; P28070; -.
DIP; DIP-33844N; -.
IntAct; P28070; 59.
MINT; P28070; -.
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; -.
jPOST; P28070; -.
MaxQB; P28070; -.
PaxDb; P28070; -.
PeptideAtlas; P28070; -.
PRIDE; P28070; -.
ProteomicsDB; 54446; -.
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.
MIM; 617591; phenotype.
neXtProt; NX_P28070; -.
OpenTargets; ENSG00000159377; -.
PharmGKB; PA33886; -.
eggNOG; KOG0185; Eukaryota.
eggNOG; ENOG410YAMA; LUCA.
GeneTree; ENSGT00390000000698; -.
HOGENOM; HOG000181719; -.
HOVERGEN; HBG018194; -.
InParanoid; P28070; -.
KO; K02736; -.
OMA; NWDIAHL; -.
OrthoDB; 1228942at2759; -.
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-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
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; Expressed in 228 organ(s), highest expression level in testis.
ExpressionAtlas; P28070; baseline and differential.
Genevisible; P28070; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; HDA: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:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd03760; proteasome_beta_type_4; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR016295; Proteasome_beta4.
InterPro; IPR016050; Proteasome_bsu_CS.
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; Disease mutation; 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 (in PRAAS3; decreased protein
maturation; changed proteasome assembly;
poor incorporation into 20S and 26S
proteasomes).
{ECO:0000269|PubMed:26524591}.
/FTId=VAR_075255.
VARIANT 222 264 Missing (in PRAAS3; digenic inheritance;
patient also carries a mutation in PSMB8;
no effect on protein abundance; changed
proteasome assembly; poor incorporation
into 20S and 26S proteasomes).
{ECO:0000269|PubMed:26524591}.
/FTId=VAR_081126.
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


Related products :

Catalog number Product name Quantity
EIAAB32754 26 kDa prosomal protein,Homo sapiens,HsBPROS26,HsN3,Human,Macropain beta chain,Multicatalytic endopeptidase complex beta chain,PROS26,PROS-26,Proteasome beta chain,Proteasome chain 3,Proteasome subuni
15-288-22554F Proteasome subunit beta type 4 - EC 3.4.25.1; Proteasome beta chain; Macropain beta chain; Multicatalytic endopeptidase complex beta chain; Proteasome chain 3; HSN3; HsBPROS26 Polyclonal 0.1 mg
15-288-22554F Proteasome subunit beta type 4 - EC 3.4.25.1; Proteasome beta chain; Macropain beta chain; Multicatalytic endopeptidase complex beta chain; Proteasome chain 3; HSN3; HsBPROS26 Polyclonal 0.05 mg
10-288-22554F Proteasome subunit beta type 4 - EC 3.4.25.1; Proteasome beta chain; Macropain beta chain; Multicatalytic endopeptidase complex beta chain; Proteasome chain 3; HSN3; HsBPROS26 0.05 mg
10-288-22554F Proteasome subunit beta type 4 - EC 3.4.25.1; Proteasome beta chain; Macropain beta chain; Multicatalytic endopeptidase complex beta chain; Proteasome chain 3; HSN3; HsBPROS26 0.1 mg
EIAAB32753 Lmp3,Low molecular mass protein 3,Macropain beta chain,Mouse,Multicatalytic endopeptidase complex beta chain,Mus musculus,Proteasome beta chain,Proteasome chain 3,Proteasome subunit beta type-4,Psmb4
EIAAB32757 Macropain beta chain,Multicatalytic endopeptidase complex beta chain,Proteasome beta chain,Proteasome chain 3,Proteasome subunit beta type-4,Psmb4,Rat,Rattus norvegicus,RN3
EIAAB32755 Macropain beta chain,Multicatalytic endopeptidase complex beta chain,Pig,Proteasome beta chain,Proteasome chain 3,Proteasome subunit beta type-4,PSMB4,Sus scrofa
E1177h ELISA Homo sapiens,Human,LMP2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta-1i,P 96T
U1177r CLIA Lmp2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta-1i,Psmb9,Rat,Rattus norv 96T
U1177h CLIA Homo sapiens,Human,LMP2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta-1i,PS 96T
E1177h ELISA kit Homo sapiens,Human,LMP2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta 96T
E1177r ELISA Lmp2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta-1i,Psmb9,Rat,Rattus nor 96T
E1177r ELISA kit Lmp2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta-1i,Psmb9,Rat,Rattu 96T
E1177m ELISA kit Lmp2,LMP-2d,Low molecular mass protein 2,Macropain chain 7,Mouse,Multicatalytic endopeptidase complex chain 7,Mus musculus,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subun 96T
E1177m ELISA Lmp2,LMP-2d,Low molecular mass protein 2,Macropain chain 7,Mouse,Multicatalytic endopeptidase complex chain 7,Mus musculus,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit be 96T
U1177m CLIA Lmp2,LMP-2d,Low molecular mass protein 2,Macropain chain 7,Mouse,Multicatalytic endopeptidase complex chain 7,Mus musculus,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit bet 96T
EIAAB32766 Macropain delta chain,Multicatalytic endopeptidase complex delta chain,Proteasome chain 5,Proteasome delta chain,Proteasome subunit beta type-6,Proteasome subunit Y,Psmb6,Psmb6l,Rat,Rattus norvegicus
EIAAB32761 Homo sapiens,Human,LMPX,Macropain epsilon chain,MB1,Multicatalytic endopeptidase complex epsilon chain,Proteasome chain 6,Proteasome epsilon chain,Proteasome subunit beta type-5,Proteasome subunit MB1
EIAAB32762 Macropain epsilon chain,Multicatalytic endopeptidase complex epsilon chain,Proteasome chain 6,Proteasome epsilon chain,Proteasome subunit beta type-5,Proteasome subunit X,Psmb5,Rat,Rattus norvegicus
EIAAB32758 Macropain epsilon chain,Mouse,Multicatalytic endopeptidase complex epsilon chain,Mus musculus,Proteasome chain 6,Proteasome epsilon chain,Proteasome subunit beta type-5,Proteasome subunit X,Psmb5
EIAAB32726 27 kDa prosomal protein,Homo sapiens,Human,Macropain iota chain,Multicatalytic endopeptidase complex iota chain,p27K,PROS27,PROS-27,Proteasome iota chain,Proteasome subunit alpha type-6,PSMA6
10-288-22044F Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 0.1 mg
10-288-22044F Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 0.05 mg
18-003-44181 Proteasome subunit alpha type-1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.05 mg Aff Pur

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP542: Electron Transport Chain
WP1566: Citrate cycle (TCA cycle)
WP1224: EBV LMP1 signaling
WP1502: Mitochondrial biogenesis
WP1571: EBV LMP1 signaling
WP1626: Benzoate degradation via CoA ligation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1655: Geraniol degradation
WP1665: Limonene and pinene degradation
WP1673: Naphthalene and anthracene degradation
WP210: Cytoplasmic Ribosomal Proteins
WP2218: sGC
WP262: EBV LMP1 signaling
WP1002: Electron Transport Chain
WP1045: TGF-beta Receptor Signaling Pathway
WP1048: TGF Beta Signaling Pathway
WP105: Fatty Acid Beta Oxidation 2
WP1058: Senescence and Autophagy
WP1061: Fatty Acid Beta Oxidation
WP1106: Keap1-Nrf2
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP111: Electron Transport Chain
WP1119: Electron Transport Chain
WP113: TGF Beta Signaling Pathway

Related Genes :
[PSMB4 PROS26] 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)
[PSMA6 PROS27] Proteasome subunit alpha type-6 (EC 3.4.25.1) (27 kDa prosomal protein) (PROS-27) (p27K) (Macropain iota chain) (Multicatalytic endopeptidase complex iota chain) (Proteasome iota chain)
[Psmb4 Lmp3] Proteasome subunit beta type-4 (EC 3.4.25.1) (Low molecular mass protein 3) (Macropain beta chain) (Multicatalytic endopeptidase complex beta chain) (Proteasome beta chain) (Proteasome chain 3)
[PSMA1 HC2 NU PROS30 PSC2] Proteasome subunit alpha type-1 (EC 3.4.25.1) (30 kDa prosomal protein) (PROS-30) (Macropain subunit C2) (Multicatalytic endopeptidase complex subunit C2) (Proteasome component C2) (Proteasome nu chain)
[PSMB2] Proteasome subunit beta type-2 (EC 3.4.25.1) (Macropain subunit C7-I) (Multicatalytic endopeptidase complex subunit C7-I) (Proteasome component C7-I)
[PSMB5 LMPX MB1 X] Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain epsilon chain) (Multicatalytic endopeptidase complex epsilon chain) (Proteasome chain 6) (Proteasome epsilon chain) (Proteasome subunit MB1) (Proteasome subunit X)
[PSMB9 LMP2 PSMB6i RING12] Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
[PSMB3] Proteasome subunit beta type-3 (EC 3.4.25.1) (Proteasome chain 13) (Proteasome component C10-II) (Proteasome theta chain)
[Psmb9 Lmp2 Ring12] Proteasome subunit beta type-9 (EC 3.4.25.1) (LMP-2d) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
[Psmb9 Lmp2 Ring12] Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
[PSMB6 LMPY Y] Proteasome subunit beta type-6 (EC 3.4.25.1) (Macropain delta chain) (Multicatalytic endopeptidase complex delta chain) (Proteasome delta chain) (Proteasome subunit Y)
[Psmb9 Lmp2 Ring12] Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
[Psmb9 Lmp2 Ring12] Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
[Psmb9 Lmp2 Ring12] Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
[Psmb5] Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain epsilon chain) (Multicatalytic endopeptidase complex epsilon chain) (Proteasome chain 6) (Proteasome epsilon chain) (Proteasome subunit X)
[Psmb6 Lmp19] Proteasome subunit beta type-6 (EC 3.4.25.1) (Low molecular mass protein 19) (Macropain delta chain) (Multicatalytic endopeptidase complex delta chain) (Proteasome delta chain) (Proteasome subunit Y)
[PSMB1 PSC5] Proteasome subunit beta type-1 (EC 3.4.25.1) (Macropain subunit C5) (Multicatalytic endopeptidase complex subunit C5) (Proteasome component C5) (Proteasome gamma chain)
[PSMB7 Z] Proteasome subunit beta type-7 (EC 3.4.25.1) (Macropain chain Z) (Multicatalytic endopeptidase complex chain Z) (Proteasome subunit Z)
[Psmb8 Lmp7 Mc13] Proteasome subunit beta type-8 (EC 3.4.25.1) (Low molecular mass protein 7) (Macropain subunit C13) (Multicatalytic endopeptidase complex subunit C13) (Proteasome component C13) (Proteasome subunit beta-5i)
[Psmb1] Proteasome subunit beta type-1 (EC 3.4.25.1) (Macropain subunit C5) (Multicatalytic endopeptidase complex subunit C5) (Proteasome component C5) (Proteasome gamma chain)
[PSMB10 LMP10 MECL1] Proteasome subunit beta type-10 (EC 3.4.25.1) (Low molecular mass protein 10) (Macropain subunit MECl-1) (Multicatalytic endopeptidase complex subunit MECl-1) (Proteasome MECl-1) (Proteasome subunit beta-2i)
[Psma6] Proteasome subunit alpha type-6 (EC 3.4.25.1) (Macropain iota chain) (Multicatalytic endopeptidase complex iota chain) (Proteasome iota chain)
[PSMB8 LMP7 PSMB5i RING10 Y2] Proteasome subunit beta type-8 (EC 3.4.25.1) (Low molecular mass protein 7) (Macropain subunit C13) (Multicatalytic endopeptidase complex subunit C13) (Proteasome component C13) (Proteasome subunit beta-5i) (Really interesting new gene 10 protein)
[Psmb10 Lmp10 Mecl1] Proteasome subunit beta type-10 (EC 3.4.25.1) (Low molecular mass protein 10) (Macropain subunit MECl-1) (Multicatalytic endopeptidase complex subunit MECl-1) (Proteasome MECl-1) (Proteasome subunit beta-2i)
[PSMA5] Proteasome subunit alpha type-5 (EC 3.4.25.1) (Macropain zeta chain) (Multicatalytic endopeptidase complex zeta chain) (Proteasome zeta chain)
[Psmb9 Lmp2 Ring12] Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
[PRE4 YFR050C] Proteasome subunit beta type-7 (EC 3.4.25.1) (Macropain subunit PRE4) (Multicatalytic endopeptidase complex subunit PRE4) (Proteasome component PRE4) (Proteinase YSCE subunit PRE4)
[PRE3 YJL001W J1407] Proteasome subunit beta type-1 (EC 3.4.25.1) (Macropain subunit PRE3) (Multicatalytic endopeptidase complex subunit PRE3) (Proteasome component PRE3) (Proteinase YSCE subunit PRE3)
[PRE1 YER012W] Proteasome subunit beta type-4 (EC 3.4.25.1) (Macropain subunit C11) (Multicatalytic endopeptidase complex subunit C11) (Proteasome component C11) (Proteinase YSCE subunit 11)
[Psma1] Proteasome subunit alpha type-1 (EC 3.4.25.1) (Macropain subunit C2) (Multicatalytic endopeptidase complex subunit C2) (Proteasome component C2) (Proteasome nu chain)

Bibliography :
?>