PSME3_MOUSE
ID PSME3_MOUSE Reviewed; 254 AA.
AC P61290; O35563; P97373; Q12920; Q13172; Q9BQD9;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Proteasome activator complex subunit 3;
DE AltName: Full=11S regulator complex subunit gamma;
DE Short=REG-gamma;
DE AltName: Full=Activator of multicatalytic protease subunit 3;
DE AltName: Full=Ki nuclear autoantigen;
DE AltName: Full=Proteasome activator 28 subunit gamma;
DE Short=PA28g;
DE Short=PA28gamma;
GN Name=Psme3;
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=C57BL/6J; TISSUE=Spleen;
RX PubMed=9218537; DOI=10.1007/s002510050281;
RA Kandil E., Kohda K., Ishibashi T., Tanaka K., Kasahara M.;
RT "PA28 subunits of the mouse proteasome: primary structures and chromosomal
RT localization of the genes.";
RL Immunogenetics 46:337-344(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B10.BR;
RX PubMed=9162094; DOI=10.1007/s002510050246;
RA Jiang H., Monaco J.J.;
RT "Sequence and expression of mouse proteasome activator PA28 and the related
RT autoantigen Ki.";
RL Immunogenetics 46:93-98(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9590240;
RA Kohda K., Ishibashi T., Shimbara N., Tanaka K., Matsuda Y., Kasahara M.;
RT "Characterization of the mouse PA28 activator complex gene family: complete
RT organizations of the three member genes and a physical map of the
RT approximately 150-kb region containing the alpha- and beta-subunit genes.";
RL J. Immunol. 160:4923-4935(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=10608895; DOI=10.1074/jbc.274.53.38211;
RA Murata S., Kawahara H., Tohma S., Yamamoto K., Kasahara M., Nabeshima Y.,
RA Tanaka K., Chiba T.;
RT "Growth retardation in mice lacking the proteasome activator PA28gamma.";
RL J. Biol. Chem. 274:38211-38215(1999).
RN [6]
RP INTERACTION WITH MAP3K3, PHOSPHORYLATION BY MAP3K3, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12650640; DOI=10.1042/bj20021758;
RA Hagemann C., Patel R., Blank J.L.;
RT "MEKK3 interacts with the PA28 gamma regulatory subunit of the
RT proteasome.";
RL Biochem. J. 373:71-79(2003).
RN [7]
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).
CC -!- FUNCTION: Subunit of the 11S REG-gamma (also called PA28-gamma)
CC proteasome regulator, a doughnut-shaped homoheptamer which associates
CC with the proteasome. 11S REG-gamma activates the trypsin-like catalytic
CC subunit of the proteasome but inhibits the chymotrypsin-like and
CC postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53
CC interaction which promotes ubiquitination- and MDM2-dependent
CC proteasomal degradation of p53/TP53, limiting its accumulation and
CC resulting in inhibited apoptosis after DNA damage. May also be involved
CC in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1
CC inhibition (By similarity). {ECO:0000250|UniProtKB:P61289}.
CC -!- SUBUNIT: Homoheptamer; the stability of the heptamer is essential for
CC the specific activation of the trypsine-like subunit and inhibition of
CC the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits of
CC the proteasome (By similarity). Interacts with p53/TP53 and MDM2 (By
CC similarity). Interacts with MAP3K3 (PubMed:12650640). Associates with
CC the proteasome (By similarity). Interacts with CCAR2 (By similarity).
CC Interacts with PSME3IP1 (via C-terminus); the interaction is direct and
CC promotes the association of PSME3 with the 20S proteasome (By
CC similarity). Interacts with COIL; the interaction is inhibited by
CC PSME3IP1 (By similarity). {ECO:0000250|UniProtKB:P61289,
CC ECO:0000269|PubMed:12650640}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12650640}. Cytoplasm
CC {ECO:0000269|PubMed:12650640}. Note=Localizes to the cytoplasm during
CC mitosis following nuclear envelope breakdown at this distinct stage of
CC the cell cycle which allows its interaction with MAP3K3 kinase.
CC -!- DOMAIN: The C-terminal sequences affect heptamer stability and
CC proteasome affinity. {ECO:0000250}.
CC -!- PTM: Phosphorylated by MAP3K3. Phosphorylation at Ser-247 promotes its
CC association with CCAR2 (By similarity). {ECO:0000250|UniProtKB:P61289,
CC ECO:0000269|PubMed:12650640}.
CC -!- PTM: Acetylation at the major site Lys-195 is important for
CC oligomerization and ability to degrade its target substrates.
CC Deacetylated by SIRT1 (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Growth retardation, small body size, and reduces
CC significantly the percentage of cells that enter the S phase.
CC {ECO:0000269|PubMed:10608895}.
CC -!- SIMILARITY: Belongs to the PA28 family. {ECO:0000305}.
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DR EMBL; D87911; BAA22041.1; -; mRNA.
DR EMBL; U60330; AAC53297.1; -; mRNA.
DR EMBL; AB007139; BAA28838.1; -; Genomic_DNA.
DR EMBL; BC015255; AAH15255.1; -; mRNA.
DR CCDS; CCDS25463.1; -.
DR RefSeq; NP_035322.1; NM_011192.3.
DR AlphaFoldDB; P61290; -.
DR SMR; P61290; -.
DR BioGRID; 202435; 36.
DR IntAct; P61290; 3.
DR STRING; 10090.ENSMUSP00000019470; -.
DR iPTMnet; P61290; -.
DR PhosphoSitePlus; P61290; -.
DR REPRODUCTION-2DPAGE; P61290; -.
DR EPD; P61290; -.
DR jPOST; P61290; -.
DR PaxDb; P61290; -.
DR PeptideAtlas; P61290; -.
DR PRIDE; P61290; -.
DR ProteomicsDB; 291705; -.
DR TopDownProteomics; P61290; -.
DR Antibodypedia; 1736; 336 antibodies from 34 providers.
DR DNASU; 19192; -.
DR Ensembl; ENSMUST00000019470; ENSMUSP00000019470; ENSMUSG00000078652.
DR GeneID; 19192; -.
DR KEGG; mmu:19192; -.
DR UCSC; uc007lon.1; mouse.
DR CTD; 10197; -.
DR MGI; MGI:1096366; Psme3.
DR VEuPathDB; HostDB:ENSMUSG00000078652; -.
DR eggNOG; KOG4470; Eukaryota.
DR GeneTree; ENSGT00950000183098; -.
DR HOGENOM; CLU_062515_1_0_1; -.
DR InParanoid; P61290; -.
DR OMA; PCNKPLC; -.
DR OrthoDB; 1251022at2759; -.
DR PhylomeDB; P61290; -.
DR TreeFam; TF106236; -.
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; 19192; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Psme3; mouse.
DR PRO; PR:P61290; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P61290; protein.
DR Bgee; ENSMUSG00000078652; Expressed in blood and 270 other tissues.
DR ExpressionAtlas; P61290; baseline and differential.
DR Genevisible; P61290; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR GO; GO:0061133; F:endopeptidase activator activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0010950; P:positive regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:MGI.
DR Gene3D; 1.20.120.180; -; 1.
DR Gene3D; 1.20.5.120; -; 1.
DR InterPro; IPR003186; PA28_C.
DR InterPro; IPR036997; PA28_C_sf.
DR InterPro; IPR036996; PA28_N_sf.
DR InterPro; IPR009077; Proteasome_activ_PA28.
DR InterPro; IPR003185; Proteasome_activ_PA28_N.
DR InterPro; IPR036252; Proteasome_activ_sf.
DR PANTHER; PTHR10660; PTHR10660; 1.
DR Pfam; PF02251; PA28_alpha; 1.
DR Pfam; PF02252; PA28_beta; 1.
DR SUPFAM; SSF47216; SSF47216; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Cell cycle; Cytoplasm; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61289"
FT CHAIN 2..254
FT /note="Proteasome activator complex subunit 3"
FT /id="PRO_0000161790"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P61289"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61289"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61289"
FT MOD_RES 195
FT /note="N6-acetyllysine; by P300/CBP"
FT /evidence="ECO:0000250|UniProtKB:P61289"
FT MOD_RES 247
FT /note="Phosphoserine; by CHEK2"
FT /evidence="ECO:0000250|UniProtKB:P61289"
FT CONFLICT 2
FT /note="A -> L (in Ref. 2; AAC53297)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="Q -> L (in Ref. 2; AAC53297)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="T -> S (in Ref. 2; AAC53297)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="D -> G (in Ref. 2; AAC53297)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="A -> P (in Ref. 2; AAC53297)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="K -> G (in Ref. 2; AAC53297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 29506 MW; 116FAB47D60A26C0 CRC64;
MASLLKVDQE VKLKVDSFRE RITSEAEDLV ANFFPKKLLE LDSFLKEPIL NIHDLTQIHS
DMNLPVPDPI LLTNSHDGLD GPTYKKRRLD ECEEAFQGTK VFVMPNGMLK SNQQLVDIIE
KVKPEIRLLI EKCNTVKMWV QLLIPRIEDG NNFGVSIQEE TVAELRTVES EAASYLDQIS
RYYITRAKLV SKIAKYPHVE DYRRTVTEID EKEYISLRLI ISELRNQYVT LHDMILKNIE
KIKRPRSSNA ETLY
