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Database: UniProt
Entry: P49720
LinkDB: P49720
Original site: P49720 
ID   PSB3_HUMAN              Reviewed;         205 AA.
AC   P49720; P31147; Q0P6J7; Q96E27;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 2.
DT   02-JUN-2021, entry version 216.
DE   RecName: Full=Proteasome subunit beta type-3;
DE   AltName: Full=Proteasome chain 13;
DE   AltName: Full=Proteasome component C10-II;
DE   AltName: Full=Proteasome theta chain;
GN   Name=PSMB3;
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 VARIANT LEU-34.
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].
RC   TISSUE=Muscle;
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 2-15; 28-41; 49-66; 71-77; 100-115 AND 178-192,
RP   CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Ovarian carcinoma;
RA   Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL   Submitted (JUL-2008) to UniProtKB.
RN   [4]
RP   PROTEIN SEQUENCE OF 29-42; 50-67 AND 101-116, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Vishwanath V.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   PROTEIN SEQUENCE OF 49-66 AND 99-111.
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 protein
RT   database of normal human epidermal keratinocytes.";
RL   Electrophoresis 13:960-969(1992).
RN   [6]
RP   PROTEIN SEQUENCE OF 100-115.
RC   TISSUE=Placenta;
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 partial
RT   sequencing.";
RL   Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
RN   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
RP   INDUCTION.
RX   PubMed=18281682; DOI=10.1093/humrep/den024;
RA   Martinez-Heredia J., de Mateo S., Vidal-Taboada J.M., Ballesca J.L.,
RA   Oliva R.;
RT   "Identification of proteomic differences in asthenozoospermic sperm
RT   samples.";
RL   Hum. Reprod. 23:783-791(2008).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   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   [15]
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   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18]
RP   FUNCTION.
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   [19]
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   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), AND SUBUNIT.
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   [21]
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   [22]
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   [23]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
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: Non-catalytic component of the 20S core proteasome complex
CC       involved in the proteolytic degradation of most intracellular proteins.
CC       This complex plays numerous essential roles within the cell by
CC       associating with different regulatory particles. Associated with two
CC       19S regulatory particles, forms the 26S proteasome and thus
CC       participates in the ATP-dependent degradation of ubiquitinated
CC       proteins. The 26S proteasome plays a key role in the maintenance of
CC       protein homeostasis by removing misfolded or damaged proteins that
CC       could impair cellular functions, and by removing proteins whose
CC       functions are no longer required. Associated with the PA200 or PA28,
CC       the 20S proteasome mediates ubiquitin-independent protein degradation.
CC       This type of proteolysis is required in several pathways including
CC       spermatogenesis (20S-PA200 complex) or generation of a subset of MHC
CC       class I-presented antigenic peptides (20S-PA28 complex).
CC       {ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:27176742,
CC       ECO:0000269|PubMed:8610016}.
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:14550573, ECO:0000269|PubMed:25599644,
CC       ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858,
CC       ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 TAT protein.
CC       {ECO:0000269|PubMed:14550573}.
CC   -!- INTERACTION:
CC       P49720; Q8N4Y2-3: CRACR2B; NbExp=3; IntAct=EBI-603340, EBI-11982645;
CC       P49720; Q9NW38: FANCL; NbExp=3; IntAct=EBI-603340, EBI-2339898;
CC       P49720; P42858: HTT; NbExp=3; IntAct=EBI-603340, EBI-466029;
CC       P49720; Q9Y244: POMP; NbExp=3; IntAct=EBI-603340, EBI-696895;
CC       P49720; O14818: PSMA7; NbExp=3; IntAct=EBI-603340, EBI-603272;
CC       P49720; P20618: PSMB1; NbExp=3; IntAct=EBI-603340, EBI-372273;
CC       P49720; P40306: PSMB10; NbExp=3; IntAct=EBI-603340, EBI-603329;
CC       P49720; P49721: PSMB2; NbExp=5; IntAct=EBI-603340, EBI-359335;
CC       P49720; P28074: PSMB5; NbExp=3; IntAct=EBI-603340, EBI-357828;
CC       P49720; O00560: SDCBP; NbExp=3; IntAct=EBI-603340, EBI-727004;
CC       P49720; P14373: TRIM27; NbExp=6; IntAct=EBI-603340, EBI-719493;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus
CC       {ECO:0000269|PubMed:12181345}.
CC   -!- INDUCTION: Up-regulated in asthenozoospermic sperm.
CC       {ECO:0000269|PubMed:18281682}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; D26598; BAA05645.1; -; mRNA.
DR   EMBL; BC013008; AAH13008.1; -; mRNA.
DR   CCDS; CCDS11328.1; -.
DR   PIR; S55041; S55041.
DR   RefSeq; NP_002786.2; NM_002795.3.
DR   PDB; 4R3O; X-ray; 2.60 A; J/X=2-205.
DR   PDB; 4R67; X-ray; 2.89 A; J/X/l/z=2-205.
DR   PDB; 5A0Q; EM; 3.50 A; J/X=2-205.
DR   PDB; 5GJQ; EM; 4.50 A; c/q=1-205.
DR   PDB; 5GJR; EM; 3.50 A; c/q=1-205.
DR   PDB; 5L4G; EM; 4.02 A; 3/W=1-205.
DR   PDB; 5LE5; X-ray; 1.80 A; I/W=1-205.
DR   PDB; 5LEX; X-ray; 2.20 A; I/W=1-205.
DR   PDB; 5LEY; X-ray; 1.90 A; I/W=1-205.
DR   PDB; 5LEZ; X-ray; 2.19 A; I/W=1-205.
DR   PDB; 5LF0; X-ray; 2.41 A; I/W=1-205.
DR   PDB; 5LF1; X-ray; 2.00 A; I/W=1-205.
DR   PDB; 5LF3; X-ray; 2.10 A; I/W=1-205.
DR   PDB; 5LF4; X-ray; 1.99 A; I/W=1-205.
DR   PDB; 5LF6; X-ray; 2.07 A; I/W=1-205.
DR   PDB; 5LF7; X-ray; 2.00 A; I/W=1-205.
DR   PDB; 5LN3; EM; 6.80 A; 3=1-205.
DR   PDB; 5M32; EM; 3.80 A; I/W=1-205.
DR   PDB; 5T0C; EM; 3.80 A; AP/BP=2-205.
DR   PDB; 5T0G; EM; 4.40 A; P=2-205.
DR   PDB; 5T0H; EM; 6.80 A; P=2-205.
DR   PDB; 5T0I; EM; 8.00 A; P=2-205.
DR   PDB; 5T0J; EM; 8.00 A; P=2-205.
DR   PDB; 5VFO; EM; 3.50 A; P/p=2-205.
DR   PDB; 5VFP; EM; 4.20 A; P/p=2-205.
DR   PDB; 5VFQ; EM; 4.20 A; P/p=2-205.
DR   PDB; 5VFR; EM; 4.90 A; P/p=2-205.
DR   PDB; 5VFS; EM; 3.60 A; P/p=2-205.
DR   PDB; 5VFT; EM; 7.00 A; P/p=2-205.
DR   PDB; 5VFU; EM; 5.80 A; P/p=2-205.
DR   PDB; 6AVO; EM; 3.80 A; U/Y=1-205.
DR   PDB; 6E5B; X-ray; 2.77 A; I/W=1-205.
DR   PDB; 6KWY; EM; 2.72 A; I/W=1-205.
DR   PDB; 6MSB; EM; 3.00 A; P/p=2-205.
DR   PDB; 6MSD; EM; 3.20 A; P/p=2-205.
DR   PDB; 6MSE; EM; 3.30 A; d=142-193.
DR   PDB; 6MSG; EM; 3.50 A; P/p=2-205.
DR   PDB; 6MSH; EM; 3.60 A; P/p=2-205.
DR   PDB; 6MSJ; EM; 3.30 A; P/p=2-205.
DR   PDB; 6MSK; EM; 3.20 A; P/p=2-205.
DR   PDB; 6R70; EM; 3.50 A; I/W=2-205.
DR   PDB; 6REY; EM; 3.00 A; J/X=1-205.
DR   PDB; 6RGQ; EM; 2.60 A; J/X=1-205.
DR   PDB; 6WJD; EM; 4.80 A; P/p=2-205.
DR   PDB; 6WJN; EM; 5.70 A; P/p=2-205.
DR   PDB; 6XMJ; EM; 3.00 A; J=2-205.
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; 6AVO; -.
DR   PDBsum; 6E5B; -.
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; P49720; -.
DR   BioGRID; 111664; 133.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P49720; -.
DR   DIP; DIP-33846N; -.
DR   IntAct; P49720; 82.
DR   MINT; P49720; -.
DR   STRING; 9606.ENSP00000483688; -.
DR   BindingDB; P49720; -.
DR   ChEMBL; CHEMBL3308923; -.
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; T01.983; -.
DR   iPTMnet; P49720; -.
DR   MetOSite; P49720; -.
DR   PhosphoSitePlus; P49720; -.
DR   SwissPalm; P49720; -.
DR   BioMuta; PSMB3; -.
DR   DMDM; 20532411; -.
DR   OGP; P49720; -.
DR   REPRODUCTION-2DPAGE; IPI00028004; -.
DR   EPD; P49720; -.
DR   jPOST; P49720; -.
DR   MassIVE; P49720; -.
DR   MaxQB; P49720; -.
DR   PaxDb; P49720; -.
DR   PeptideAtlas; P49720; -.
DR   PRIDE; P49720; -.
DR   ProteomicsDB; 56056; -.
DR   TopDownProteomics; P49720; -.
DR   Antibodypedia; 73543; 135 antibodies.
DR   DNASU; 5691; -.
DR   Ensembl; ENST00000619426; ENSP00000483688; ENSG00000277791.
DR   Ensembl; ENST00000619951; ENSP00000483956; ENSG00000275903.
DR   GeneID; 5691; -.
DR   KEGG; hsa:5691; -.
DR   UCSC; uc002hqr.5; human.
DR   CTD; 5691; -.
DR   DisGeNET; 5691; -.
DR   GeneCards; PSMB3; -.
DR   HGNC; HGNC:9540; PSMB3.
DR   HPA; ENSG00000277791; Tissue enhanced (blood).
DR   MIM; 602176; gene.
DR   neXtProt; NX_P49720; -.
DR   OpenTargets; ENSG00000277791; -.
DR   PharmGKB; PA33885; -.
DR   VEuPathDB; HostDB:ENSG00000277791.4; -.
DR   eggNOG; KOG0180; Eukaryota.
DR   GeneTree; ENSGT00550000074820; -.
DR   HOGENOM; CLU_035750_10_0_1; -.
DR   InParanoid; P49720; -.
DR   OMA; GWGAIVH; -.
DR   OrthoDB; 1170036at2759; -.
DR   PhylomeDB; P49720; -.
DR   TreeFam; TF106216; -.
DR   PathwayCommons; P49720; -.
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; P49720; -.
DR   BioGRID-ORCS; 5691; 809 hits in 970 CRISPR screens.
DR   ChiTaRS; PSMB3; human.
DR   GeneWiki; PSMB3; -.
DR   GenomeRNAi; 5691; -.
DR   Pharos; P49720; Tdark.
DR   PRO; PR:P49720; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P49720; protein.
DR   Bgee; ENSG00000277791; Expressed in left adrenal gland and 246 other tissues.
DR   ExpressionAtlas; P49720; baseline and differential.
DR   Genevisible; P49720; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
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   CDD; cd03759; proteasome_beta_type_3; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR033811; Proteasome_beta_3.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF62; PTHR11599:SF62; 1.
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; Cytoplasm; Direct protein sequencing;
KW   Host-virus interaction; Nucleus; Proteasome; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   CHAIN           2..205
FT                   /note="Proteasome subunit beta type-3"
FT                   /id="PRO_0000148057"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   MOD_RES         77
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VARIANT         34
FT                   /note="M -> L (in dbSNP:rs4907)"
FT                   /evidence="ECO:0000269|PubMed:7918633"
FT                   /id="VAR_034415"
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          10..15
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          20..25
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          42..46
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           57..78
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           84..97
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   TURN            98..100
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          104..112
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          130..140
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           143..153
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           160..175
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          177..181
FT                   /evidence="ECO:0007829|PDB:6RGQ"
FT   STRAND          185..190
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          192..200
FT                   /evidence="ECO:0007829|PDB:5LE5"
SQ   SEQUENCE   205 AA;  22949 MW;  624972384C0112FD CRC64;
     MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY IGLAGLATDV
     QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF GPYYTEPVIA GLDPKTFKPF
     ICSLDLIGCP MVTDDFVVSG TCAEQMYGMC ESLWEPNMDP DHLFETISQA MLNAVDRDAV
     SGMGVIVHII EKDKITTRTL KARMD
//
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