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Proteasome subunit beta type-3 (EC 3.4.25.1) (Proteasome chain 13) (Proteasome component C10-II) (Proteasome theta chain)

 PSB3_HUMAN              Reviewed;         205 AA.
P49720; P31147; Q0P6J7; Q96E27;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
10-MAY-2002, sequence version 2.
28-MAR-2018, entry version 190.
RecName: Full=Proteasome subunit beta type-3;
EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
AltName: Full=Proteasome chain 13;
AltName: Full=Proteasome component C10-II;
AltName: Full=Proteasome theta chain;
Name=PSMB3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-34.
PubMed=7918633; DOI=10.1016/0167-4781(94)90060-4;
Nothwang H.G., Tamura T., Tanaka K., Ichihara A.;
"Sequence analyses and inter-species comparisons of three novel human
proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential
proteolytic active-site residues.";
Biochim. Biophys. Acta 1219:361-368(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 2-15; 28-41; 49-66; 71-77; 100-115 AND 178-192,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
Submitted (JUL-2008) to UniProtKB.
[4]
PROTEIN SEQUENCE OF 29-42; 50-67 AND 101-116, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 49-66 AND 99-111.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[6]
PROTEIN SEQUENCE OF 100-115.
TISSUE=Placenta;
PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
"Human proteasome subunits from 2-dimensional gels identified by
partial sequencing.";
Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
[7]
FUNCTION IN ANTIGEN PRESENTATION.
PubMed=8610016; DOI=10.1038/381166a0;
Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H.,
Rammensee H.G., Koszinowski U.H., Kloetzel P.M.;
"A role for the proteasome regulator PA28alpha in antigen
presentation.";
Nature 381:166-168(1996).
[8]
SUBCELLULAR LOCATION.
PubMed=12181345; DOI=10.1091/mbc.E02-03-0122;
Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D.,
Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.;
"Clastosome: a subtype of nuclear body enriched in 19S and 20S
proteasomes, ubiquitin, and protein substrates of proteasome.";
Mol. Biol. Cell 13:2771-2782(2002).
[9]
INTERACTION WITH HIV-1 TAT.
PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
Mayer R.J., Krueger E.;
"Human immunodeficiency virus-1 Tat protein interacts with distinct
proteasomal alpha and beta subunits.";
FEBS Lett. 553:200-204(2003).
[10]
FUNCTION.
PubMed=15244466; DOI=10.1021/bm049957a;
Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
"20S proteasome prevents aggregation of heat-denatured proteins
without PA700 regulatory subcomplex like a molecular chaperone.";
Biomacromolecules 5:1465-1469(2004).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[12]
INDUCTION.
PubMed=18281682; DOI=10.1093/humrep/den024;
Martinez-Heredia J., de Mateo S., Vidal-Taboada J.M., Ballesca J.L.,
Oliva R.;
"Identification of proteomic differences in asthenozoospermic sperm
samples.";
Hum. Reprod. 23:783-791(2008).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=27176742; DOI=10.1515/hsz-2016-0176;
Rut W., Drag M.;
"Human 20S proteasome activity towards fluorogenic peptides of various
chain lengths.";
Biol. Chem. 397:921-926(2016).
[19]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=26133119; DOI=10.1038/ncomms8573;
da Fonseca P.C., Morris E.P.;
"Cryo-EM reveals the conformation of a substrate analogue in the human
20S proteasome core.";
Nat. Commun. 6:7573-7573(2015).
[20]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), AND SUBUNIT.
PubMed=25599644; DOI=10.1016/j.str.2014.11.017;
Harshbarger W., Miller C., Diedrich C., Sacchettini J.;
"Crystal structure of the human 20S proteasome in complex with
carfilzomib.";
Structure 23:418-424(2015).
[21]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), AND SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
[23]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
PubMed=27493187; DOI=10.1126/science.aaf8993;
Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
Stark H., Bourenkov G., Chari A.;
"The inhibition mechanism of human 20S proteasomes enables next-
generation inhibitor design.";
Science 353:594-598(2016).
-!- FUNCTION: Component of the 20S core proteasome complex involved in
the proteolytic degradation of most intracellular proteins. This
complex plays numerous essential roles within the cell by
associating with different regulatory particles. Associated with
two 19S regulatory particles, forms the 26S proteasome and thus
participates in the ATP-dependent degradation of ubiquitinated
proteins. The 26S proteasome plays a key role in the maintenance
of protein homeostasis by removing misfolded or damaged proteins
that could impair cellular functions, and by removing proteins
whose functions are no longer required. Associated with the PA200
or PA28, the 20S proteasome mediates ubiquitin-independent protein
degradation. This type of proteolysis is required in several
pathways including spermatogenesis (20S-PA200 complex) or
generation of a subset of MHC class I-presented antigenic peptides
(20S-PA28 complex). {ECO:0000269|PubMed:15244466,
ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000269|PubMed:27176742}.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is a barrel-
shaped complex made of 28 subunits that are arranged in four
stacked rings. The two outer rings are each formed by seven alpha
subunits, and the two inner rings are formed by seven beta
subunits. The proteolytic activity is exerted by three beta-
subunits PSMB5, PSMB6 and PSMB7. Interacts with HIV-1 TAT protein
(PubMed:14550573). {ECO:0000269|PubMed:14550573,
ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119,
ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
ECO:0000269|PubMed:27493187}.
-!- INTERACTION:
P49721:PSMB2; NbExp=4; IntAct=EBI-603340, EBI-359335;
P14373:TRIM27; NbExp=5; IntAct=EBI-603340, EBI-719493;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}.
Nucleus {ECO:0000269|PubMed:12181345}.
-!- INDUCTION: Up-regulated in asthenozoospermic sperm.
{ECO:0000269|PubMed:18281682}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
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EMBL; D26598; BAA05645.1; -; mRNA.
EMBL; BC013008; AAH13008.1; -; mRNA.
CCDS; CCDS11328.1; -.
PIR; S55041; S55041.
RefSeq; NP_002786.2; NM_002795.3.
UniGene; Hs.82793; -.
PDB; 4R3O; X-ray; 2.60 A; J/X=2-205.
PDB; 4R67; X-ray; 2.89 A; J/X/l/z=2-205.
PDB; 5A0Q; EM; 3.50 A; J/X=2-205.
PDB; 5GJQ; EM; 4.50 A; c/q=1-205.
PDB; 5GJR; EM; 3.50 A; c/q=1-205.
PDB; 5L4G; EM; 4.02 A; 3/W=1-205.
PDB; 5LE5; X-ray; 1.80 A; I/W=1-205.
PDB; 5LEX; X-ray; 2.20 A; I/W=1-205.
PDB; 5LEY; X-ray; 1.90 A; I/W=1-205.
PDB; 5LEZ; X-ray; 2.19 A; I/W=1-205.
PDB; 5LF0; X-ray; 2.41 A; I/W=1-205.
PDB; 5LF1; X-ray; 2.00 A; I/W=1-205.
PDB; 5LF3; X-ray; 2.10 A; I/W=1-205.
PDB; 5LF4; X-ray; 1.99 A; I/W=1-205.
PDB; 5LF6; X-ray; 2.07 A; I/W=1-205.
PDB; 5LF7; X-ray; 2.00 A; I/W=1-205.
PDB; 5LN3; EM; 6.80 A; 3=1-205.
PDB; 5M32; EM; 3.80 A; I/W=1-205.
PDB; 5T0C; EM; 3.80 A; AP/BP=2-205.
PDB; 5T0G; EM; 4.40 A; P=2-205.
PDB; 5T0H; EM; 6.80 A; P=2-205.
PDB; 5T0I; EM; 8.00 A; P=2-205.
PDB; 5T0J; EM; 8.00 A; P=2-205.
PDB; 6AVO; EM; 3.80 A; U/Y=1-205.
PDBsum; 4R3O; -.
PDBsum; 4R67; -.
PDBsum; 5A0Q; -.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4G; -.
PDBsum; 5LE5; -.
PDBsum; 5LEX; -.
PDBsum; 5LEY; -.
PDBsum; 5LEZ; -.
PDBsum; 5LF0; -.
PDBsum; 5LF1; -.
PDBsum; 5LF3; -.
PDBsum; 5LF4; -.
PDBsum; 5LF6; -.
PDBsum; 5LF7; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 6AVO; -.
ProteinModelPortal; P49720; -.
SMR; P49720; -.
BioGrid; 111664; 99.
CORUM; P49720; -.
DIP; DIP-33846N; -.
IntAct; P49720; 45.
MINT; P49720; -.
STRING; 9606.ENSP00000225426; -.
BindingDB; P49720; -.
ChEMBL; CHEMBL3831201; -.
MEROPS; T01.983; -.
iPTMnet; P49720; -.
PhosphoSitePlus; P49720; -.
SwissPalm; P49720; -.
BioMuta; PSMB3; -.
DMDM; 20532411; -.
OGP; P49720; -.
REPRODUCTION-2DPAGE; IPI00028004; -.
EPD; P49720; -.
MaxQB; P49720; -.
PaxDb; P49720; -.
PeptideAtlas; P49720; -.
PRIDE; P49720; -.
TopDownProteomics; P49720; -.
DNASU; 5691; -.
Ensembl; ENST00000619426; ENSP00000483688; ENSG00000277791.
Ensembl; ENST00000619951; ENSP00000483956; ENSG00000275903.
GeneID; 5691; -.
KEGG; hsa:5691; -.
UCSC; uc002hqr.5; human.
CTD; 5691; -.
EuPathDB; HostDB:ENSG00000277791.4; -.
GeneCards; PSMB3; -.
H-InvDB; HIX0030292; -.
HGNC; HGNC:9540; PSMB3.
HPA; HPA042775; -.
HPA; HPA048147; -.
MIM; 602176; gene.
neXtProt; NX_P49720; -.
OpenTargets; ENSG00000277791; -.
PharmGKB; PA33885; -.
eggNOG; KOG0180; Eukaryota.
eggNOG; ENOG410XSC8; LUCA.
GeneTree; ENSGT00550000074820; -.
HOGENOM; HOG000090523; -.
HOVERGEN; HBG004446; -.
InParanoid; P49720; -.
KO; K02735; -.
OMA; EQLFGMC; -.
OrthoDB; EOG091G0JTX; -.
PhylomeDB; P49720; -.
TreeFam; TF106216; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSMB3; human.
GeneWiki; PSMB3; -.
GenomeRNAi; 5691; -.
PRO; PR:P49720; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000277791; -.
CleanEx; HS_PSMB3; -.
ExpressionAtlas; P49720; baseline and differential.
Genevisible; P49720; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
CDD; cd03759; proteasome_beta_type_3; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR033811; Proteasome_beta_3.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF62; PTHR11599:SF62; 1.
Pfam; PF00227; Proteasome; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Host-virus interaction; Hydrolase; Nucleus;
Polymorphism; Protease; Proteasome; Reference proteome;
Threonine protease.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.3}.
CHAIN 2 205 Proteasome subunit beta type-3.
/FTId=PRO_0000148057.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.3}.
MOD_RES 77 77 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 34 34 M -> L (in dbSNP:rs4907).
{ECO:0000269|PubMed:7918633}.
/FTId=VAR_034415.
HELIX 3 5 {ECO:0000244|PDB:5LE5}.
STRAND 10 15 {ECO:0000244|PDB:5LE5}.
STRAND 20 25 {ECO:0000244|PDB:5LE5}.
STRAND 28 30 {ECO:0000244|PDB:5LE5}.
STRAND 33 37 {ECO:0000244|PDB:5LE5}.
STRAND 42 46 {ECO:0000244|PDB:5LE5}.
STRAND 49 55 {ECO:0000244|PDB:5LE5}.
HELIX 57 78 {ECO:0000244|PDB:5LE5}.
HELIX 84 97 {ECO:0000244|PDB:5LE5}.
TURN 98 100 {ECO:0000244|PDB:5LE5}.
STRAND 104 112 {ECO:0000244|PDB:5LE5}.
TURN 114 116 {ECO:0000244|PDB:5LE5}.
STRAND 119 124 {ECO:0000244|PDB:5LE5}.
STRAND 130 140 {ECO:0000244|PDB:5LE5}.
HELIX 143 153 {ECO:0000244|PDB:5LE5}.
HELIX 160 175 {ECO:0000244|PDB:5LE5}.
STRAND 178 181 {ECO:0000244|PDB:4R67}.
STRAND 185 190 {ECO:0000244|PDB:5LE5}.
STRAND 192 200 {ECO:0000244|PDB:5LE5}.
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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