PSB2_MOUSE
ID PSB2_MOUSE Reviewed; 201 AA.
AC Q9R1P3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Proteasome subunit beta type-2;
DE AltName: Full=Macropain subunit C7-I;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C7-I;
DE AltName: Full=Proteasome component C7-I;
GN Name=Psmb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B10.BR;
RX PubMed=10436176; DOI=10.1007/s002510050562;
RA Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N.,
RA Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.;
RT "The complete primary structure of mouse 20S proteasomes.";
RL Immunogenetics 49:835-842(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 71-85; 127-145 AND 171-198, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [5]
RP FUNCTION.
RX PubMed=16581775; DOI=10.1128/mcb.26.8.2999-3007.2006;
RA Khor B., Bredemeyer A.L., Huang C.-Y., Turnbull I.R., Evans R.,
RA Maggi L.B. Jr., White J.M., Walker L.M., Carnes K., Hess R.A.,
RA Sleckman B.P.;
RT "Proteasome activator PA200 is required for normal spermatogenesis.";
RL Mol. Cell. Biol. 26:2999-3007(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT,
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22341445; DOI=10.1016/j.cell.2011.12.030;
RA Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M.,
RA Groll M.;
RT "Immuno- and constitutive proteasome crystal structures reveal differences
RT in substrate and inhibitor specificity.";
RL Cell 148:727-738(2012).
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:16581775, ECO:0000269|PubMed:22341445}.
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:16857966, ECO:0000269|PubMed:22341445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49721}. Nucleus
CC {ECO:0000250|UniProtKB:P49721}. Note=Translocated from the cytoplasm
CC into the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000250|UniProtKB:P49721}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22341445}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; AF060090; AAD50535.1; -; mRNA.
DR EMBL; BC008265; AAH08265.1; -; mRNA.
DR CCDS; CCDS18657.1; -.
DR RefSeq; NP_036100.3; NM_011970.4.
DR PDB; 3UNB; X-ray; 2.90 A; J/X/l/z=1-201.
DR PDB; 3UNE; X-ray; 3.20 A; J/X/l/z=1-201.
DR PDB; 3UNF; X-ray; 2.90 A; J/X=1-201.
DR PDB; 3UNH; X-ray; 3.20 A; J/X=1-201.
DR PDBsum; 3UNB; -.
DR PDBsum; 3UNE; -.
DR PDBsum; 3UNF; -.
DR PDBsum; 3UNH; -.
DR AlphaFoldDB; Q9R1P3; -.
DR SMR; Q9R1P3; -.
DR BioGRID; 204996; 48.
DR CORUM; Q9R1P3; -.
DR IntAct; Q9R1P3; 6.
DR STRING; 10090.ENSMUSP00000030642; -.
DR BindingDB; Q9R1P3; -.
DR ChEMBL; CHEMBL3112378; -.
DR MEROPS; T01.984; -.
DR iPTMnet; Q9R1P3; -.
DR PhosphoSitePlus; Q9R1P3; -.
DR SwissPalm; Q9R1P3; -.
DR REPRODUCTION-2DPAGE; Q9R1P3; -.
DR EPD; Q9R1P3; -.
DR jPOST; Q9R1P3; -.
DR MaxQB; Q9R1P3; -.
DR PaxDb; Q9R1P3; -.
DR PeptideAtlas; Q9R1P3; -.
DR PRIDE; Q9R1P3; -.
DR ProteomicsDB; 291691; -.
DR TopDownProteomics; Q9R1P3; -.
DR Antibodypedia; 17325; 264 antibodies from 32 providers.
DR DNASU; 26445; -.
DR Ensembl; ENSMUST00000030642; ENSMUSP00000030642; ENSMUSG00000028837.
DR GeneID; 26445; -.
DR KEGG; mmu:26445; -.
DR UCSC; uc008utr.2; mouse.
DR CTD; 5690; -.
DR MGI; MGI:1347045; Psmb2.
DR VEuPathDB; HostDB:ENSMUSG00000028837; -.
DR eggNOG; KOG0177; Eukaryota.
DR GeneTree; ENSGT00640000091536; -.
DR HOGENOM; CLU_035750_12_1_1; -.
DR InParanoid; Q9R1P3; -.
DR OMA; RMCTDEL; -.
DR OrthoDB; 1392180at2759; -.
DR PhylomeDB; Q9R1P3; -.
DR TreeFam; TF106219; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 26445; 27 hits in 72 CRISPR screens.
DR ChiTaRS; Psmb2; mouse.
DR PRO; PR:Q9R1P3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9R1P3; protein.
DR Bgee; ENSMUSG00000028837; Expressed in morula and 262 other tissues.
DR Genevisible; Q9R1P3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
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:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
DR CDD; cd03758; proteasome_beta_type_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR035206; Proteasome_beta2.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF6; PTHR11599:SF6; 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; Nucleus;
KW Proteasome; Reference proteome.
FT CHAIN 1..201
FT /note="Proteasome subunit beta type-2"
FT /id="PRO_0000148044"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P49721"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 39..49
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 52..71
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 77..92
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 153..169
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3UNB"
SQ SEQUENCE 201 AA; 22906 MW; E9B3121974777958 CRC64;
MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA GDTVQFAEYI
QKNVQLYKMR NGYELSPTAA ANFTRRNLAD CLRSRTPYHV NLLLAGYDEH EGPALYYMDY
LAALAKAPFA AHGYGAFLTL SILDRYYTPT ISRERAVELL RKCLEELQKR FILNLPTFSV
RVIDKDGIHN LENIAFPKRD S
