PSB6_HUMAN
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 03-AUG-2022, entry version 223.
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).
RN [23]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH AKIRIN2,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=34711951; DOI=10.1038/s41586-021-04035-8;
RA de Almeida M., Hinterndorfer M., Brunner H., Grishkovskaya I., Singh K.,
RA Schleiffer A., Jude J., Deswal S., Kalis R., Vunjak M., Lendl T., Imre R.,
RA Roitinger E., Neumann T., Kandolf S., Schutzbier M., Mechtler K.,
RA Versteeg G.A., Haselbach D., Zuber J.;
RT "AKIRIN2 controls the nuclear import of proteasomes in vertebrates.";
RL Nature 599:491-496(2021).
CC -!- FUNCTION: 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:34711951,
CC 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,
CC ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345,
CC ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into
CC the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000269|PubMed:34711951}.
CC -!- INDUCTION: 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 PDB; 7LXV; EM; 3.40 A; N/b=35-239.
DR PDB; 7NHT; EM; 2.80 A; N=1-239.
DR PDB; 7PG9; EM; 3.70 A; H/V=35-239.
DR PDB; 7V5G; EM; 4.47 A; A/H=35-239.
DR PDB; 7V5M; EM; 3.88 A; H/V=35-239.
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 PDBsum; 7LXV; -.
DR PDBsum; 7NHT; -.
DR PDBsum; 7PG9; -.
DR PDBsum; 7V5G; -.
DR PDBsum; 7V5M; -.
DR AlphaFoldDB; P28072; -.
DR SMR; P28072; -.
DR BioGRID; 111667; 166.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P28072; -.
DR DIP; DIP-33847N; -.
DR IntAct; P28072; 50.
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 GlyGen; P28072; 1 site, 1 O-linked glycan (1 site).
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; 154 antibodies from 28 providers.
DR DNASU; 5694; -.
DR Ensembl; ENST00000270586.8; ENSP00000270586.3; ENSG00000142507.10.
DR GeneID; 5694; -.
DR KEGG; hsa:5694; -.
DR MANE-Select; ENST00000270586.8; ENSP00000270586.3; NM_002798.3; NP_002789.1.
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; -.
DR eggNOG; KOG0174; Eukaryota.
DR GeneTree; ENSGT00940000155114; -.
DR HOGENOM; CLU_035750_5_2_1; -.
DR InParanoid; P28072; -.
DR OMA; HKQAYAI; -.
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-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P28072; -.
DR SIGNOR; P28072; -.
DR BioGRID-ORCS; 5694; 756 hits in 1091 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 212 other tissues.
DR ExpressionAtlas; P28072; baseline and differential.
DR Genevisible; P28072; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO: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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
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
