ID PSB1_HUMAN Reviewed; 241 AA. AC P20618; B5BU76; Q9BWA8; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 2. DT 11-MAY-2016, entry version 178. DE RecName: Full=Proteasome subunit beta type-1; DE EC=3.4.25.1; DE AltName: Full=Macropain subunit C5; DE AltName: Full=Multicatalytic endopeptidase complex subunit C5; DE AltName: Full=Proteasome component C5; DE AltName: Full=Proteasome gamma chain; DE Flags: Precursor; GN Name=PSMB1; Synonyms=PSC5; 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]. RX PubMed=2025653; DOI=10.1016/0167-4781(91)90090-9; RA Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., RA Tanaka K., Ichihara A.; RT "Molecular cloning and sequence analysis of cDNAs for five major RT subunits of human proteasomes (multi-catalytic proteinase RT complexes)."; RL Biochim. Biophys. Acta 1089:95-102(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., RA Isogai T., Imai J., Watanabe S., Nomura N.; RT "Human protein factory for converting the transcriptome into an in RT vitro-expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-11. RC TISSUE=Brain, and Lung; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 29-52. 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 [7] 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 [8] RP INTERACTION WITH SERPINB2. RX PubMed=14732874; DOI=10.1093/abbs/36.1.42; RA Fan J., Zhang Y.Q., Li P., Hou M., Tan L., Wang X., Zhu Y.S.; RT "Interaction of plasminogen activator inhibitor-2 and proteasome RT subunit, beta type 1."; RL Acta Biochim. Biophys. Sin. 36:42-46(2004). RN [9] 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] 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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [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., 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). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). 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. 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 SERPINB2. Interacts CC with HIV-1 TAT protein. {ECO:0000269|PubMed:14550573, CC ECO:0000269|PubMed:14732874}. CC -!- INTERACTION: CC Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-372273, EBI-2125614; CC A1A4E9:KRT13; NbExp=3; IntAct=EBI-372273, EBI-10171552; CC P19012:KRT15; NbExp=3; IntAct=EBI-372273, EBI-739566; CC Q9UPY8:MAPRE3; NbExp=3; IntAct=EBI-372273, EBI-726739; CC P28074:PSMB5; NbExp=3; IntAct=EBI-372273, EBI-357828; CC Q99436:PSMB7; NbExp=8; IntAct=EBI-372273, EBI-603319; CC Q13077:TRAF1; NbExp=3; IntAct=EBI-372273, EBI-359224; CC P14373:TRIM27; NbExp=3; IntAct=EBI-372273, EBI-719493; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- SIMILARITY: Belongs to the peptidase T1B family. CC {ECO:0000255|PROSITE-ProRule:PRU00809}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; D00761; BAA00658.1; -; mRNA. DR EMBL; BT019720; AAV38525.1; -; mRNA. DR EMBL; AB451312; BAG70126.1; -; mRNA. DR EMBL; AB451442; BAG70256.1; -; mRNA. DR EMBL; AL031259; CAA20287.1; -; Genomic_DNA. DR EMBL; BC000508; AAH00508.1; -; mRNA. DR EMBL; BC020807; AAH20807.1; -; mRNA. DR CCDS; CCDS34577.1; -. DR PIR; S15973; SNHUC5. DR RefSeq; NP_002784.1; NM_002793.3. DR UniGene; Hs.352768; -. DR PDB; 4R3O; X-ray; 2.60 A; 1/M=29-241. DR PDB; 4R67; X-ray; 2.89 A; 1/M/a/o=29-241. DR PDB; 5A0Q; EM; 3.50 A; M/a=29-241. DR PDBsum; 4R3O; -. DR PDBsum; 4R67; -. DR PDBsum; 5A0Q; -. DR ProteinModelPortal; P20618; -. DR SMR; P20618; 29-241. DR BioGrid; 111662; 124. DR DIP; DIP-31193N; -. DR IntAct; P20618; 31. DR MINT; MINT-3009312; -. DR STRING; 9606.ENSP00000262193; -. DR BindingDB; P20618; -. DR ChEMBL; CHEMBL2364701; -. DR DrugBank; DB00188; Bortezomib. DR DrugBank; DB08889; Carfilzomib. DR GuidetoPHARMACOLOGY; 2404; -. DR MEROPS; T01.986; -. DR iPTMnet; P20618; -. DR PhosphoSite; P20618; -. DR SwissPalm; P20618; -. DR BioMuta; PSMB1; -. DR DMDM; 130853; -. DR REPRODUCTION-2DPAGE; IPI00025019; -. DR UCD-2DPAGE; P20618; -. DR EPD; P20618; -. DR MaxQB; P20618; -. DR PaxDb; P20618; -. DR PeptideAtlas; P20618; -. DR PRIDE; P20618; -. DR TopDownProteomics; P20618; -. DR DNASU; 5689; -. DR Ensembl; ENST00000262193; ENSP00000262193; ENSG00000008018. DR GeneID; 5689; -. DR KEGG; hsa:5689; -. DR UCSC; uc011ehe.3; human. DR CTD; 5689; -. DR GeneCards; PSMB1; -. DR HGNC; HGNC:9537; PSMB1. DR HPA; CAB033911; -. DR HPA; HPA029635; -. DR HPA; HPA029637; -. DR MIM; 602017; gene. DR neXtProt; NX_P20618; -. DR PharmGKB; PA33882; -. DR eggNOG; KOG0179; Eukaryota. DR eggNOG; COG0638; LUCA. DR GeneTree; ENSGT00550000075035; -. DR HOGENOM; HOG000091081; -. DR HOVERGEN; HBG000961; -. DR InParanoid; P20618; -. DR KO; K02732; -. DR OMA; EHRFNPY; -. DR OrthoDB; EOG7WHHBB; -. DR PhylomeDB; P20618; -. DR TreeFam; TF106218; -. DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells. 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-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 that don't undergo autocatalytic processing 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-5687128; MAPK6/MAPK4 signaling. 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-69229; Ubiquitin-dependent degradation of Cyclin D1. DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR ChiTaRS; PSMB1; human. DR GeneWiki; PSMB1; -. DR GenomeRNAi; 5689; -. DR NextBio; 22098; -. DR PRO; PR:P20618; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; P20618; -. DR CleanEx; HS_PSMB1; -. DR Genevisible; P20618; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. 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; ISS:UniProtKB. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome. DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; 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:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0034641; P:cellular nitrogen compound metabolic 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:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; 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:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome. DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome. DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome. DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome. DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome. DR GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome. DR GO; GO:0006595; P:polyamine metabolic process; TAS:Reactome. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome. DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome. DR GO; GO:0012501; P:programmed cell death; TAS:Reactome. DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome. DR GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome. DR GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome. DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome. DR GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome. DR GO; GO:0051439; P:regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome. DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. DR GO; GO:0044281; P:small molecule metabolic 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:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome. DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; TAS:Reactome. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR Pfam; PF00227; Proteasome; 1. 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; Complete proteome; Cytoplasm; KW Direct protein sequencing; Glycoprotein; Host-virus interaction; KW Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Protease; KW Proteasome; Reference proteome; Threonine protease. FT PROPEP 1 28 {ECO:0000269|PubMed:2306472}. FT /FTId=PRO_0000259623. FT CHAIN 29 241 Proteasome subunit beta type-1. FT /FTId=PRO_0000148030. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:22814378}. FT MOD_RES 150 150 Phosphotyrosine. FT {ECO:0000250|UniProtKB:O09061}. FT MOD_RES 204 204 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT CARBOHYD 58 58 O-linked (GlcNAc). {ECO:0000250}. FT CARBOHYD 209 209 O-linked (GlcNAc). {ECO:0000250}. FT VARIANT 11 11 P -> A (in dbSNP:rs12717). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_051547. FT VARIANT 208 208 I -> N (in dbSNP:rs10541). FT /FTId=VAR_051548. FT STRAND 39 44 {ECO:0000244|PDB:4R3O}. FT STRAND 49 54 {ECO:0000244|PDB:4R3O}. FT STRAND 57 59 {ECO:0000244|PDB:4R3O}. FT STRAND 62 66 {ECO:0000244|PDB:4R3O}. FT STRAND 71 73 {ECO:0000244|PDB:4R3O}. FT STRAND 75 84 {ECO:0000244|PDB:4R3O}. FT HELIX 86 107 {ECO:0000244|PDB:4R3O}. FT HELIX 113 125 {ECO:0000244|PDB:4R3O}. FT TURN 126 129 {ECO:0000244|PDB:4R3O}. FT STRAND 134 141 {ECO:0000244|PDB:4R3O}. FT STRAND 147 152 {ECO:0000244|PDB:4R3O}. FT STRAND 158 167 {ECO:0000244|PDB:4R3O}. FT HELIX 170 180 {ECO:0000244|PDB:4R3O}. FT HELIX 196 213 {ECO:0000244|PDB:4R3O}. FT STRAND 214 217 {ECO:0000244|PDB:4R3O}. FT STRAND 219 227 {ECO:0000244|PDB:4R3O}. FT STRAND 230 237 {ECO:0000244|PDB:4R3O}. SQ SEQUENCE 241 AA; 26489 MW; AE8FC42799F39157 CRC64; MLSSTAMYSA PGRDLGMEPH RAAGPLQLRF SPYVFNGGTI LAIAGEDFAI VASDTRLSEG FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL KMYKHSNNKA MTTGAIAAML STILYSRRFF PYYVYNIIGG LDEEGKGAVY SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ VGFKNMQNVE HVPLSLDRAM RLVKDVFISA AERDVYTGDA LRICIVTKEG IREETVSLRK D //