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Database: UniProt
Entry: P28072
LinkDB: P28072
Original site: P28072 
ID   PSB6_HUMAN              Reviewed;         239 AA.
AC   P28072; Q96J55;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 4.
DT   02-JUN-2021, entry version 219.
DE   RecName: Full=Proteasome subunit beta type-6;
DE            EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
DE   AltName: Full=Macropain delta chain;
DE   AltName: Full=Multicatalytic endopeptidase complex delta chain;
DE   AltName: Full=Proteasome delta chain;
DE   AltName: Full=Proteasome subunit Y;
DE   Flags: Precursor;
GN   Name=PSMB6; Synonyms=LMPY, Y;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=8066462; DOI=10.1126/science.8066462;
RA   Akiyama K.-Y., Yokota K.-Y., Kagawa S., Shimbara N., Tamura T., Akioka H.,
RA   Nothwang H.G., Noda C., Tanaka K., Ichihara A.;
RT   "cDNA cloning and interferon gamma down-regulation of proteasomal subunits
RT   X and Y.";
RL   Science 265:1231-1234(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cervix;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-9; 54-63 AND 210-230, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Colon carcinoma;
RA   Bienvenut W.V., Zebisch A., Kolch W.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 60-239, AND PROTEIN SEQUENCE OF 35-75; 80-110
RP   AND 210-233.
RX   PubMed=1888762; DOI=10.1016/0167-4838(91)90020-z;
RA   DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R.,
RA   Dawson P.A., Slaughter C.A.;
RT   "The primary structures of four subunits of the human, high-molecular-
RT   weight proteinase, macropain (proteasome), are distinct but homologous.";
RL   Biochim. Biophys. Acta 1079:29-38(1991).
RN   [5]
RP   PROTEIN SEQUENCE OF 35-60.
RX   PubMed=2306472; DOI=10.1016/0167-4838(90)90165-c;
RA   Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N.,
RA   Slaughter C.A.;
RT   "Relationships among the subunits of the high molecular weight proteinase,
RT   macropain (proteasome).";
RL   Biochim. Biophys. Acta 1037:178-185(1990).
RN   [6]
RP   PROTEIN SEQUENCE OF 157-178, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Vishwanath V.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [7]
RP   SUBUNIT.
RX   PubMed=8163024; DOI=10.1016/0014-5793(94)80612-8;
RA   Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M., Kristensen P.,
RA   Hendil K.B., Tanaka K., Ichihara A.;
RT   "Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by
RT   interferon-gamma for acquirement of the functional diversity responsible
RT   for antigen processing.";
RL   FEBS Lett. 343:85-88(1994).
RN   [8]
RP   FUNCTION IN ANTIGEN PRESENTATION.
RX   PubMed=8610016; DOI=10.1038/381166a0;
RA   Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H.,
RA   Rammensee H.G., Koszinowski U.H., Kloetzel P.M.;
RT   "A role for the proteasome regulator PA28alpha in antigen presentation.";
RL   Nature 381:166-168(1996).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12181345; DOI=10.1091/mbc.e02-03-0122;
RA   Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D.,
RA   Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.;
RT   "Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes,
RT   ubiquitin, and protein substrates of proteasome.";
RL   Mol. Biol. Cell 13:2771-2782(2002).
RN   [10]
RP   INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RX   PubMed=14550573; DOI=10.1016/s0014-5793(03)01025-1;
RA   Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA   Mayer R.J., Krueger E.;
RT   "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT   proteasomal alpha and beta subunits.";
RL   FEBS Lett. 553:200-204(2003).
RN   [11]
RP   FUNCTION.
RX   PubMed=15244466; DOI=10.1021/bm049957a;
RA   Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
RT   "20S proteasome prevents aggregation of heat-denatured proteins without
RT   PA700 regulatory subcomplex like a molecular chaperone.";
RL   Biomacromolecules 5:1465-1469(2004).
RN   [12]
RP   INDUCTION.
RX   PubMed=15613457; DOI=10.1677/erc.1.00818;
RA   Onda M., Emi M., Yoshida A., Miyamoto S., Akaishi J., Asaka S.,
RA   Mizutani K., Shimizu K., Nagahama M., Ito K., Tanaka T., Tsunoda T.;
RT   "Comprehensive gene expression profiling of anaplastic thyroid cancers with
RT   cDNA microarray of 25 344 genes.";
RL   Endocr. Relat. Cancer 11:843-854(2004).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17323924; DOI=10.1021/bi061994u;
RA   Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT   "Mass spectrometric characterization of the affinity-purified human 26S
RT   proteasome complex.";
RL   Biochemistry 46:3553-3565(2007).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [17]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=27176742; DOI=10.1515/hsz-2016-0176;
RA   Rut W., Drag M.;
RT   "Human 20S proteasome activity towards fluorogenic peptides of various
RT   chain lengths.";
RL   Biol. Chem. 397:921-926(2016).
RN   [18]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
RX   PubMed=26133119; DOI=10.1038/ncomms8573;
RA   da Fonseca P.C., Morris E.P.;
RT   "Cryo-EM reveals the conformation of a substrate analogue in the human 20S
RT   proteasome core.";
RL   Nat. Commun. 6:7573-7573(2015).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 35-236, SUBUNIT, AND ACTIVE SITE.
RX   PubMed=25599644; DOI=10.1016/j.str.2014.11.017;
RA   Harshbarger W., Miller C., Diedrich C., Sacchettini J.;
RT   "Crystal structure of the human 20S proteasome in complex with
RT   carfilzomib.";
RL   Structure 23:418-424(2015).
RN   [20]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
RX   PubMed=27428775; DOI=10.1038/nsmb.3273;
RA   Huang X., Luan B., Wu J., Shi Y.;
RT   "An atomic structure of the human 26S proteasome.";
RL   Nat. Struct. Mol. Biol. 23:778-785(2016).
RN   [21]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), AND SUBUNIT.
RX   PubMed=27342858; DOI=10.1073/pnas.1608050113;
RA   Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
RA   Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
RT   "Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX   PubMed=27493187; DOI=10.1126/science.aaf8993;
RA   Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
RA   Stark H., Bourenkov G., Chari A.;
RT   "The inhibition mechanism of human 20S proteasomes enables next-generation
RT   inhibitor design.";
RL   Science 353:594-598(2016).
CC   -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC       proteolytic degradation of most intracellular proteins. This complex
CC       plays numerous essential roles within the cell by associating with
CC       different regulatory particles. Associated with two 19S regulatory
CC       particles, forms the 26S proteasome and thus participates in the ATP-
CC       dependent degradation of ubiquitinated proteins. The 26S proteasome
CC       plays a key role in the maintenance of protein homeostasis by removing
CC       misfolded or damaged proteins that could impair cellular functions, and
CC       by removing proteins whose functions are no longer required. Associated
CC       with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC       independent protein degradation. This type of proteolysis is required
CC       in several pathways including spermatogenesis (20S-PA200 complex) or
CC       generation of a subset of MHC class I-presented antigenic peptides
CC       (20S-PA28 complex). Within the 20S core complex, PSMB6 displays a
CC       peptidylglutamyl-hydrolizing activity also termed postacidic or
CC       caspase-like activity, meaning that the peptides bond hydrolysis occurs
CC       directly after acidic residues. {ECO:0000269|PubMed:15244466,
CC       ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1; Evidence={ECO:0000269|PubMed:27176742};
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC       complex made of 28 subunits that are arranged in four stacked rings.
CC       The two outer rings are each formed by seven alpha subunits, and the
CC       two inner rings are formed by seven beta subunits. The proteolytic
CC       activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
CC       {ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119,
CC       ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC       ECO:0000269|PubMed:27493187, ECO:0000269|PubMed:8163024}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 protein Tat.
CC       {ECO:0000269|PubMed:14550573}.
CC   -!- INTERACTION:
CC       P28072; P42858: HTT; NbExp=3; IntAct=EBI-359288, EBI-466029;
CC       P28072; Q9UHB4: NDOR1; NbExp=3; IntAct=EBI-359288, EBI-10249760;
CC       P28072; Q99436: PSMB7; NbExp=3; IntAct=EBI-359288, EBI-603319;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus
CC       {ECO:0000269|PubMed:12181345}.
CC   -!- INDUCTION: Down-regulated by IFNG/IFN-gamma (at protein level). Up-
CC       regulated in anaplastic thyroid cancer cell lines.
CC       {ECO:0000269|PubMed:15613457, ECO:0000269|PubMed:8066462}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; D29012; BAA06098.1; -; mRNA.
DR   EMBL; BC000835; AAH00835.1; -; mRNA.
DR   EMBL; X61971; CAA43963.1; -; mRNA.
DR   CCDS; CCDS11056.1; -.
DR   PIR; B54589; B54589.
DR   PIR; S17522; S17522.
DR   RefSeq; NP_002789.1; NM_002798.2.
DR   PDB; 4R3O; X-ray; 2.60 A; H/V=35-236.
DR   PDB; 4R67; X-ray; 2.89 A; H/V/j/x=35-236.
DR   PDB; 5A0Q; EM; 3.50 A; H/V=35-239.
DR   PDB; 5GJQ; EM; 4.50 A; a/o=1-239.
DR   PDB; 5GJR; EM; 3.50 A; a/o=1-239.
DR   PDB; 5L4G; EM; 4.02 A; 6/Z=1-239.
DR   PDB; 5LE5; X-ray; 1.80 A; N/b=35-239.
DR   PDB; 5LEX; X-ray; 2.20 A; N/b=35-239.
DR   PDB; 5LEY; X-ray; 1.90 A; N/b=35-239.
DR   PDB; 5LEZ; X-ray; 2.19 A; N/b=35-239.
DR   PDB; 5LF0; X-ray; 2.41 A; N/b=35-239.
DR   PDB; 5LF1; X-ray; 2.00 A; N/b=35-239.
DR   PDB; 5LF3; X-ray; 2.10 A; N/b=36-239.
DR   PDB; 5LF4; X-ray; 1.99 A; N/b=35-239.
DR   PDB; 5LF6; X-ray; 2.07 A; N/b=35-239.
DR   PDB; 5LF7; X-ray; 2.00 A; N/b=35-239.
DR   PDB; 5LN3; EM; 6.80 A; 1=1-239.
DR   PDB; 5M32; EM; 3.80 A; N/b=1-239.
DR   PDB; 5T0C; EM; 3.80 A; AN/BN=2-239.
DR   PDB; 5T0G; EM; 4.40 A; N=2-239.
DR   PDB; 5T0H; EM; 6.80 A; N=2-239.
DR   PDB; 5T0I; EM; 8.00 A; N=2-239.
DR   PDB; 5T0J; EM; 8.00 A; N=2-239.
DR   PDB; 5VFO; EM; 3.50 A; N/n=35-225.
DR   PDB; 5VFP; EM; 4.20 A; N/n=35-225.
DR   PDB; 5VFQ; EM; 4.20 A; N/n=35-225.
DR   PDB; 5VFR; EM; 4.90 A; N/n=35-225.
DR   PDB; 5VFS; EM; 3.60 A; N/n=35-225.
DR   PDB; 5VFT; EM; 7.00 A; N/n=35-225.
DR   PDB; 5VFU; EM; 5.80 A; N/n=35-225.
DR   PDB; 6KWY; EM; 2.72 A; N/b=1-239.
DR   PDB; 6MSB; EM; 3.00 A; N/n=2-239.
DR   PDB; 6MSD; EM; 3.20 A; N/n=2-239.
DR   PDB; 6MSE; EM; 3.30 A; N/n=2-239.
DR   PDB; 6MSG; EM; 3.50 A; N/n=2-239.
DR   PDB; 6MSH; EM; 3.60 A; N/n=2-239.
DR   PDB; 6MSJ; EM; 3.30 A; N/n=2-239.
DR   PDB; 6MSK; EM; 3.20 A; N/n=2-239.
DR   PDB; 6R70; EM; 3.50 A; N/b=35-237.
DR   PDB; 6REY; EM; 3.00 A; H/V=35-239.
DR   PDB; 6RGQ; EM; 2.60 A; H/V=35-239.
DR   PDB; 6WJD; EM; 4.80 A; N/n=2-239.
DR   PDB; 6WJN; EM; 5.70 A; N/n=35-225.
DR   PDB; 6XMJ; EM; 3.00 A; H=35-236.
DR   PDBsum; 4R3O; -.
DR   PDBsum; 4R67; -.
DR   PDBsum; 5A0Q; -.
DR   PDBsum; 5GJQ; -.
DR   PDBsum; 5GJR; -.
DR   PDBsum; 5L4G; -.
DR   PDBsum; 5LE5; -.
DR   PDBsum; 5LEX; -.
DR   PDBsum; 5LEY; -.
DR   PDBsum; 5LEZ; -.
DR   PDBsum; 5LF0; -.
DR   PDBsum; 5LF1; -.
DR   PDBsum; 5LF3; -.
DR   PDBsum; 5LF4; -.
DR   PDBsum; 5LF6; -.
DR   PDBsum; 5LF7; -.
DR   PDBsum; 5LN3; -.
DR   PDBsum; 5M32; -.
DR   PDBsum; 5T0C; -.
DR   PDBsum; 5T0G; -.
DR   PDBsum; 5T0H; -.
DR   PDBsum; 5T0I; -.
DR   PDBsum; 5T0J; -.
DR   PDBsum; 5VFO; -.
DR   PDBsum; 5VFP; -.
DR   PDBsum; 5VFQ; -.
DR   PDBsum; 5VFR; -.
DR   PDBsum; 5VFS; -.
DR   PDBsum; 5VFT; -.
DR   PDBsum; 5VFU; -.
DR   PDBsum; 6KWY; -.
DR   PDBsum; 6MSB; -.
DR   PDBsum; 6MSD; -.
DR   PDBsum; 6MSE; -.
DR   PDBsum; 6MSG; -.
DR   PDBsum; 6MSH; -.
DR   PDBsum; 6MSJ; -.
DR   PDBsum; 6MSK; -.
DR   PDBsum; 6R70; -.
DR   PDBsum; 6REY; -.
DR   PDBsum; 6RGQ; -.
DR   PDBsum; 6WJD; -.
DR   PDBsum; 6WJN; -.
DR   PDBsum; 6XMJ; -.
DR   SMR; P28072; -.
DR   BioGRID; 111667; 147.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P28072; -.
DR   DIP; DIP-33847N; -.
DR   IntAct; P28072; 42.
DR   MINT; P28072; -.
DR   STRING; 9606.ENSP00000270586; -.
DR   BindingDB; P28072; -.
DR   ChEMBL; CHEMBL1944496; -.
DR   DrugBank; DB08515; (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE.
DR   MEROPS; T01.010; -.
DR   iPTMnet; P28072; -.
DR   PhosphoSitePlus; P28072; -.
DR   SwissPalm; P28072; -.
DR   BioMuta; PSMB6; -.
DR   DMDM; 20532407; -.
DR   OGP; P28072; -.
DR   SWISS-2DPAGE; P28072; -.
DR   EPD; P28072; -.
DR   jPOST; P28072; -.
DR   MassIVE; P28072; -.
DR   PaxDb; P28072; -.
DR   PeptideAtlas; P28072; -.
DR   PRIDE; P28072; -.
DR   ProteomicsDB; 54447; -.
DR   Antibodypedia; 11325; 149 antibodies.
DR   DNASU; 5694; -.
DR   Ensembl; ENST00000270586; ENSP00000270586; ENSG00000142507.
DR   GeneID; 5694; -.
DR   KEGG; hsa:5694; -.
DR   CTD; 5694; -.
DR   DisGeNET; 5694; -.
DR   GeneCards; PSMB6; -.
DR   HGNC; HGNC:9543; PSMB6.
DR   HPA; ENSG00000142507; Low tissue specificity.
DR   MIM; 600307; gene.
DR   neXtProt; NX_P28072; -.
DR   OpenTargets; ENSG00000142507; -.
DR   PharmGKB; PA33888; -.
DR   VEuPathDB; HostDB:ENSG00000142507.9; -.
DR   eggNOG; KOG0174; Eukaryota.
DR   GeneTree; ENSGT00940000155114; -.
DR   HOGENOM; CLU_035750_5_2_1; -.
DR   InParanoid; P28072; -.
DR   OMA; HAIYHDG; -.
DR   OrthoDB; 1172133at2759; -.
DR   PhylomeDB; P28072; -.
DR   TreeFam; TF106221; -.
DR   PathwayCommons; P28072; -.
DR   Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR   Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR   Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR   Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-HSA-202424; Downstream TCR signaling.
DR   Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR   Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-HSA-4641257; Degradation of AXIN.
DR   Reactome; R-HSA-4641258; Degradation of DVL.
DR   Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR   Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR   Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR   Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR   Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-HSA-5689603; UCH proteinases.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
DR   Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR   Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-HSA-69481; G2/M Checkpoints.
DR   Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR   Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR   Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; P28072; -.
DR   BioGRID-ORCS; 5694; 748 hits in 1003 CRISPR screens.
DR   ChiTaRS; PSMB6; human.
DR   GeneWiki; PSMB6; -.
DR   GenomeRNAi; 5694; -.
DR   Pharos; P28072; Tbio.
DR   PRO; PR:P28072; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P28072; protein.
DR   Bgee; ENSG00000142507; Expressed in gastrocnemius and 248 other tissues.
DR   ExpressionAtlas; P28072; baseline and differential.
DR   Genevisible; P28072; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR   GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000243; Pept_T1A_subB.
DR   InterPro; IPR035140; Proteasome_beta6.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF46; PTHR11599:SF46; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Host-virus interaction; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW   Proteasome; Reference proteome; Threonine protease; Zymogen.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT   PROPEP          2..34
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:1888762,
FT                   ECO:0000269|PubMed:2306472"
FT                   /id="PRO_0000026613"
FT   CHAIN           35..239
FT                   /note="Proteasome subunit beta type-6"
FT                   /id="PRO_0000026614"
FT   ACT_SITE        35
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:25599644,
FT                   ECO:0000269|PubMed:27493187"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT   MOD_RES         69
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         107
FT                   /note="P -> A (in dbSNP:rs2304974)"
FT                   /id="VAR_020030"
FT   CONFLICT        145
FT                   /note="V -> G (in Ref. 1; BAA06098)"
FT                   /evidence="ECO:0000305"
FT   STRAND          37..42
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          68..72
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          75..81
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           83..104
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           110..123
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   TURN            139..141
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          142..148
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          158..163
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           164..169
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           170..176
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           183..200
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          201..203
FT                   /evidence="ECO:0007829|PDB:4R67"
FT   STRAND          208..214
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          217..223
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           225..227
FT                   /evidence="ECO:0007829|PDB:5LE5"
SQ   SEQUENCE   239 AA;  25358 MW;  7DF4081DC735930C CRC64;
     MAATLLAARG AGPAPAWGPE AFTPDWESRE VSTGTTIMAV QFDGGVVLGA DSRTTTGSYI
     ANRVTDKLTP IHDRIFCCRS GSAADTQAVA DAVTYQLGFH SIELNEPPLV HTAASLFKEM
     CYRYREDLMA GIIIAGWDPQ EGGQVYSVPM GGMMVRQSFA IGGSGSSYIY GYVDATYREG
     MTKEECLQFT ANALALAMER DGSSGGVIRL AAIAESGVER QVLLGDQIPK FAVATLPPA
//
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