Full text data of PSMB4
PSMB4
(PROS26)
[Confidence: high (present in two of the MS resources)]
Proteasome subunit beta type-4; 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; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit beta type-4; 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; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00291936
IPI00291936 Proteasome subunit beta type 4 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00291936 Proteasome subunit beta type 4 Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P28070
ID PSB4_HUMAN Reviewed; 264 AA.
AC P28070; B2R9L3; P31148; Q5SZS5; Q6IBI4; Q969L6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 4.
DT 22-JAN-2014, entry version 158.
DE RecName: Full=Proteasome subunit beta type-4;
DE EC=3.4.25.1;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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-
RT peptide 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
RT proteinase, 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
RT partial 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
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [12]
RP INTERACTION WITH HTLV-1 TAX.
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 [13]
RP INTERACTION WITH HIV-1 NEF.
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
RT type 1 Nef protein.";
RL Virology 237:33-45(1997).
RN [14]
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
RT proteins.";
RL J. Biol. Chem. 276:46533-46543(2001).
RN [15]
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
RT transduction pathway of the bone morphogenetic proteins (BMPs).";
RL BMC Cell Biol. 3:15-15(2002).
RN [16]
RP INTERACTION WITH HIV-1 TAT.
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 [17]
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.,
RA Katinger H., Grillari J.;
RT "Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of
RT the 20 S proteasome.";
RL Biochem. J. 388:593-603(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [19]
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
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [20]
RP INDUCTION.
RX PubMed=17367606; DOI=10.1016/j.humpath.2006.07.019;
RA Kannangai R., Vivekanandan P., Martinez-Murillo F., Choti M.,
RA Torbenson M.;
RT "Fibrolamellar carcinomas show overexpression of genes in the RAS,
RT MAPK, PIK3, and xenobiotic degradation pathways.";
RL Hum. Pathol. 38:639-644(2007).
RN [21]
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.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [22]
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.,
RA Buerckstuemmer T., 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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex
CC which is characterized by its ability to cleave peptides with Arg,
CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. Mediates the lipopolysaccharide-induced signal
CC macrophage proteasome (By similarity). SMAD1/OAZ1/PSMB4 complex
CC mediates the degradation of the CREBBP/EP300 repressor SNIP1.
CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC specificity.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC two 19S regulatory subunits. The 20S proteasome core is composed
CC of 28 subunits that are arranged in four stacked rings, resulting
CC in a barrel-shaped structure. The two end rings are each formed by
CC seven alpha subunits, and the two central rings are each formed by
CC seven beta subunits. The catalytic chamber with the active sites
CC is on the inside of the barrel. Interacts with HIV-1 TAT and HIV-1
CC NEF proteins. Interaction with HTLV-1 TAX protein favors NFKB1
CC activation. Interacts with bacterial lipopolysaccharide (LPS) (By
CC similarity). Forms a ternary complex with SMAD1 and OAZ1 before
CC PSMB4 is incorporated into the 20S proteasome. Interacts with
CC PRPF19.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- INDUCTION: Up-regulated in fibrolamellar carcinomas.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC -!- CAUTION: A report observed N-glycosylation at Asn-83
CC (PubMed:19139490). However, as the protein does not localize in an
CC extracellular compartment of the cell, additional evidences are
CC required to confirm this result.
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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; CAI16806.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53442.1; -; Genomic_DNA.
DR EMBL; S71381; AAB31085.1; -; mRNA.
DR PIR; S08186; S08186.
DR PIR; S45719; S45719.
DR PIR; S50147; S50147.
DR RefSeq; NP_002787.2; NM_002796.2.
DR UniGene; Hs.89545; -.
DR ProteinModelPortal; P28070; -.
DR SMR; P28070; 46-262.
DR IntAct; P28070; 17.
DR MINT; MINT-1192686; -.
DR STRING; 9606.ENSP00000290541; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.987; -.
DR PhosphoSite; P28070; -.
DR DMDM; 116242733; -.
DR DOSAC-COBS-2DPAGE; P28070; -.
DR OGP; P28070; -.
DR REPRODUCTION-2DPAGE; IPI00555956; -.
DR SWISS-2DPAGE; P28070; -.
DR PaxDb; P28070; -.
DR PeptideAtlas; P28070; -.
DR PRIDE; P28070; -.
DR DNASU; 5692; -.
DR Ensembl; ENST00000290541; ENSP00000290541; ENSG00000159377.
DR GeneID; 5692; -.
DR KEGG; hsa:5692; -.
DR UCSC; uc001eyc.1; human.
DR CTD; 5692; -.
DR GeneCards; GC01P151372; -.
DR HGNC; HGNC:9541; PSMB4.
DR HPA; HPA006700; -.
DR MIM; 602177; gene.
DR neXtProt; NX_P28070; -.
DR PharmGKB; PA33886; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000181719; -.
DR HOVERGEN; HBG018194; -.
DR InParanoid; P28070; -.
DR KO; K02736; -.
DR OMA; RIMRVND; -.
DR OrthoDB; EOG74FF1D; -.
DR PhylomeDB; P28070; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMB4; human.
DR GeneWiki; PSMB4; -.
DR GenomeRNAi; 5692; -.
DR NextBio; 22110; -.
DR PRO; PR:P28070; -.
DR Bgee; P28070; -.
DR CleanEx; HS_PSMB4; -.
DR Genevestigator; P28070; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR016295; Proteasome_endopept_cplx_B.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR Pfam; PF00227; Proteasome; 1.
DR PIRSF; PIRSF001213; Psome_endopept_beta; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Hydrolase; Nucleus; Phosphoprotein;
KW Polymorphism; Protease; Proteasome; Reference proteome;
KW Threonine protease; Zymogen.
FT PROPEP 1 45
FT /FTId=PRO_0000026579.
FT CHAIN 46 264 Proteasome subunit beta type-4.
FT /FTId=PRO_0000026580.
FT ACT_SITE 46 46 Nucleophile (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 102 102 Phosphotyrosine.
FT VARIANT 95 95 M -> I (in dbSNP:rs1804241).
FT /FTId=VAR_012072.
FT VARIANT 234 234 I -> T (in dbSNP:rs4603).
FT /FTId=VAR_013115.
FT CONFLICT 264 264 E -> D (in Ref. 3; CAG33101).
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
//
ID PSB4_HUMAN Reviewed; 264 AA.
AC P28070; B2R9L3; P31148; Q5SZS5; Q6IBI4; Q969L6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 4.
DT 22-JAN-2014, entry version 158.
DE RecName: Full=Proteasome subunit beta type-4;
DE EC=3.4.25.1;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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-
RT peptide 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
RT proteinase, 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
RT partial 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
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [12]
RP INTERACTION WITH HTLV-1 TAX.
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 [13]
RP INTERACTION WITH HIV-1 NEF.
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
RT type 1 Nef protein.";
RL Virology 237:33-45(1997).
RN [14]
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
RT proteins.";
RL J. Biol. Chem. 276:46533-46543(2001).
RN [15]
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
RT transduction pathway of the bone morphogenetic proteins (BMPs).";
RL BMC Cell Biol. 3:15-15(2002).
RN [16]
RP INTERACTION WITH HIV-1 TAT.
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 [17]
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.,
RA Katinger H., Grillari J.;
RT "Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of
RT the 20 S proteasome.";
RL Biochem. J. 388:593-603(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [19]
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
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [20]
RP INDUCTION.
RX PubMed=17367606; DOI=10.1016/j.humpath.2006.07.019;
RA Kannangai R., Vivekanandan P., Martinez-Murillo F., Choti M.,
RA Torbenson M.;
RT "Fibrolamellar carcinomas show overexpression of genes in the RAS,
RT MAPK, PIK3, and xenobiotic degradation pathways.";
RL Hum. Pathol. 38:639-644(2007).
RN [21]
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.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [22]
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.,
RA Buerckstuemmer T., 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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex
CC which is characterized by its ability to cleave peptides with Arg,
CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. Mediates the lipopolysaccharide-induced signal
CC macrophage proteasome (By similarity). SMAD1/OAZ1/PSMB4 complex
CC mediates the degradation of the CREBBP/EP300 repressor SNIP1.
CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC specificity.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC two 19S regulatory subunits. The 20S proteasome core is composed
CC of 28 subunits that are arranged in four stacked rings, resulting
CC in a barrel-shaped structure. The two end rings are each formed by
CC seven alpha subunits, and the two central rings are each formed by
CC seven beta subunits. The catalytic chamber with the active sites
CC is on the inside of the barrel. Interacts with HIV-1 TAT and HIV-1
CC NEF proteins. Interaction with HTLV-1 TAX protein favors NFKB1
CC activation. Interacts with bacterial lipopolysaccharide (LPS) (By
CC similarity). Forms a ternary complex with SMAD1 and OAZ1 before
CC PSMB4 is incorporated into the 20S proteasome. Interacts with
CC PRPF19.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- INDUCTION: Up-regulated in fibrolamellar carcinomas.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC -!- CAUTION: A report observed N-glycosylation at Asn-83
CC (PubMed:19139490). However, as the protein does not localize in an
CC extracellular compartment of the cell, additional evidences are
CC required to confirm this result.
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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; CAI16806.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53442.1; -; Genomic_DNA.
DR EMBL; S71381; AAB31085.1; -; mRNA.
DR PIR; S08186; S08186.
DR PIR; S45719; S45719.
DR PIR; S50147; S50147.
DR RefSeq; NP_002787.2; NM_002796.2.
DR UniGene; Hs.89545; -.
DR ProteinModelPortal; P28070; -.
DR SMR; P28070; 46-262.
DR IntAct; P28070; 17.
DR MINT; MINT-1192686; -.
DR STRING; 9606.ENSP00000290541; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.987; -.
DR PhosphoSite; P28070; -.
DR DMDM; 116242733; -.
DR DOSAC-COBS-2DPAGE; P28070; -.
DR OGP; P28070; -.
DR REPRODUCTION-2DPAGE; IPI00555956; -.
DR SWISS-2DPAGE; P28070; -.
DR PaxDb; P28070; -.
DR PeptideAtlas; P28070; -.
DR PRIDE; P28070; -.
DR DNASU; 5692; -.
DR Ensembl; ENST00000290541; ENSP00000290541; ENSG00000159377.
DR GeneID; 5692; -.
DR KEGG; hsa:5692; -.
DR UCSC; uc001eyc.1; human.
DR CTD; 5692; -.
DR GeneCards; GC01P151372; -.
DR HGNC; HGNC:9541; PSMB4.
DR HPA; HPA006700; -.
DR MIM; 602177; gene.
DR neXtProt; NX_P28070; -.
DR PharmGKB; PA33886; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000181719; -.
DR HOVERGEN; HBG018194; -.
DR InParanoid; P28070; -.
DR KO; K02736; -.
DR OMA; RIMRVND; -.
DR OrthoDB; EOG74FF1D; -.
DR PhylomeDB; P28070; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMB4; human.
DR GeneWiki; PSMB4; -.
DR GenomeRNAi; 5692; -.
DR NextBio; 22110; -.
DR PRO; PR:P28070; -.
DR Bgee; P28070; -.
DR CleanEx; HS_PSMB4; -.
DR Genevestigator; P28070; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR016295; Proteasome_endopept_cplx_B.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR Pfam; PF00227; Proteasome; 1.
DR PIRSF; PIRSF001213; Psome_endopept_beta; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Hydrolase; Nucleus; Phosphoprotein;
KW Polymorphism; Protease; Proteasome; Reference proteome;
KW Threonine protease; Zymogen.
FT PROPEP 1 45
FT /FTId=PRO_0000026579.
FT CHAIN 46 264 Proteasome subunit beta type-4.
FT /FTId=PRO_0000026580.
FT ACT_SITE 46 46 Nucleophile (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 102 102 Phosphotyrosine.
FT VARIANT 95 95 M -> I (in dbSNP:rs1804241).
FT /FTId=VAR_012072.
FT VARIANT 234 234 I -> T (in dbSNP:rs4603).
FT /FTId=VAR_013115.
FT CONFLICT 264 264 E -> D (in Ref. 3; CAG33101).
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
//
MIM
602177
*RECORD*
*FIELD* NO
602177
*FIELD* TI
*602177 PROTEASOME SUBUNIT, BETA-TYPE, 4; PSMB4
;;PROTEASOME SUBUNIT BETA-7
*FIELD* TX
read moreSee PSMB2 (602175). McCusker et al. (1997) mapped PSMB4 to 1q21 by
fluorescence in situ hybridization.
*FIELD* RF
1. McCusker, D.; Jones, T.; Sheer, D.; Trowsdale, J.: Genetic relationships
of the genes encoding the human proteasome beta subunits and the proteasome
PA28 complex. Genomics 45: 362-367, 1997.
*FIELD* CD
Victor A. McKusick: 12/12/1997
*FIELD* ED
mgross: 06/25/2007
dkim: 7/23/1998
mark: 12/12/1997
*RECORD*
*FIELD* NO
602177
*FIELD* TI
*602177 PROTEASOME SUBUNIT, BETA-TYPE, 4; PSMB4
;;PROTEASOME SUBUNIT BETA-7
*FIELD* TX
read moreSee PSMB2 (602175). McCusker et al. (1997) mapped PSMB4 to 1q21 by
fluorescence in situ hybridization.
*FIELD* RF
1. McCusker, D.; Jones, T.; Sheer, D.; Trowsdale, J.: Genetic relationships
of the genes encoding the human proteasome beta subunits and the proteasome
PA28 complex. Genomics 45: 362-367, 1997.
*FIELD* CD
Victor A. McKusick: 12/12/1997
*FIELD* ED
mgross: 06/25/2007
dkim: 7/23/1998
mark: 12/12/1997