PSB3_HUMAN
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 03-AUG-2022, entry version 220.
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).
RN [24]
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: 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 ECO:0000269|PubMed:34711951}.
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,
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: 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 PDB; 7AWE; X-ray; 2.29 A; J/X=2-205.
DR PDB; 7B12; X-ray; 2.43 A; J/X=2-205.
DR PDB; 7LXV; EM; 3.40 A; I/W=1-205.
DR PDB; 7NHT; EM; 2.80 A; I=1-205.
DR PDB; 7PG9; EM; 3.70 A; J/X=1-205.
DR PDB; 7V5G; EM; 4.47 A; C/J=1-205.
DR PDB; 7V5M; EM; 3.88 A; J/X=1-205.
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 PDBsum; 7AWE; -.
DR PDBsum; 7B12; -.
DR PDBsum; 7LXV; -.
DR PDBsum; 7NHT; -.
DR PDBsum; 7PG9; -.
DR PDBsum; 7V5G; -.
DR PDBsum; 7V5M; -.
DR AlphaFoldDB; P49720; -.
DR SMR; P49720; -.
DR BioGRID; 111664; 148.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P49720; -.
DR DIP; DIP-33846N; -.
DR IntAct; P49720; 86.
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 GlyGen; P49720; 1 site, 1 O-linked glycan (1 site).
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; 138 antibodies from 32 providers.
DR DNASU; 5691; -.
DR Ensembl; ENST00000619426.5; ENSP00000483688.1; ENSG00000277791.5.
DR Ensembl; ENST00000619951.2; ENSP00000483956.1; ENSG00000275903.2.
DR GeneID; 5691; -.
DR KEGG; hsa:5691; -.
DR MANE-Select; ENST00000619426.5; ENSP00000483688.1; NM_002795.4; NP_002786.2.
DR UCSC; uc002hqr.5; human.
DR CTD; 5691; -.
DR DisGeNET; 5691; -.
DR GeneCards; PSMB3; -.
DR HGNC; HGNC:9540; PSMB3.
DR HPA; ENSG00000277791; Low tissue specificity.
DR MIM; 602176; gene.
DR neXtProt; NX_P49720; -.
DR OpenTargets; ENSG00000277791; -.
DR PharmGKB; PA33885; -.
DR VEuPathDB; HostDB:ENSG00000277791; -.
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-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; P49720; -.
DR SIGNOR; P49720; -.
DR BioGRID-ORCS; 5691; 825 hits in 1063 CRISPR screens.
DR ChiTaRS; PSMB3; human.
DR GeneWiki; PSMB3; -.
DR GenomeRNAi; 5691; -.
DR Pharos; P49720; Tbio.
DR PRO; PR:P49720; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P49720; protein.
DR Bgee; ENSG00000277791; Expressed in monocyte and 98 other tissues.
DR ExpressionAtlas; P49720; baseline and differential.
DR Genevisible; P49720; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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; 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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
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
