PSME2_RAT
ID PSME2_RAT Reviewed; 238 AA.
AC Q63798; Q4QR96;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Proteasome activator complex subunit 2;
DE AltName: Full=11S regulator complex subunit beta;
DE Short=REG-beta;
DE AltName: Full=Activator of multicatalytic protease subunit 2;
DE AltName: Full=Proteasome activator 28 subunit beta;
DE Short=PA28b;
DE Short=PA28beta;
GN Name=Psme2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7789512; DOI=10.1016/0014-5793(95)00492-r;
RA Ahn J.Y., Tanahashi N., Akiyama K., Hisamatsu H., Noda C., Tanaka K.,
RA Chung C.H., Shibmara N., Willy P.J., Mott J.D., Slaughter C.A.,
RA DeMartino G.N.;
RT "Primary structures of two homologous subunits of PA28, a gamma-interferon-
RT inducible protein activator of the 20S proteasome.";
RL FEBS Lett. 366:37-42(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary, and Thymus;
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).
CC -!- FUNCTION: Implicated in immunoproteasome assembly and required for
CC efficient antigen processing. The PA28 activator complex enhances the
CC generation of class I binding peptides by altering the cleavage pattern
CC of the proteasome.
CC -!- SUBUNIT: Heterodimer of PSME1 and PSME2, which forms a hexameric ring.
CC -!- INDUCTION: By interferon gamma.
CC -!- SIMILARITY: Belongs to the PA28 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D45250; BAA08207.1; -; mRNA.
DR EMBL; BC058486; AAH58486.1; -; mRNA.
DR EMBL; BC097331; AAH97331.1; -; mRNA.
DR RefSeq; NP_058953.1; NM_017257.2.
DR AlphaFoldDB; Q63798; -.
DR SMR; Q63798; -.
DR STRING; 10116.ENSRNOP00000026279; -.
DR iPTMnet; Q63798; -.
DR PhosphoSitePlus; Q63798; -.
DR jPOST; Q63798; -.
DR PRIDE; Q63798; -.
DR Ensembl; ENSRNOT00000026279; ENSRNOP00000026279; ENSRNOG00000019246.
DR GeneID; 29614; -.
DR KEGG; rno:29614; -.
DR UCSC; RGD:3430; rat.
DR CTD; 5721; -.
DR RGD; 3430; Psme2.
DR eggNOG; KOG4470; Eukaryota.
DR GeneTree; ENSGT00950000183098; -.
DR HOGENOM; CLU_062515_0_1_1; -.
DR InParanoid; Q63798; -.
DR OMA; KKPPKCG; -.
DR OrthoDB; 1251022at2759; -.
DR PhylomeDB; Q63798; -.
DR TreeFam; TF106236; -.
DR Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-RNO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-RNO-4641257; Degradation of AXIN.
DR Reactome; R-RNO-4641258; Degradation of DVL.
DR Reactome; R-RNO-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-RNO-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-RNO-5632684; Hedgehog 'on' state.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR Reactome; R-RNO-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-RNO-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-5689603; UCH proteinases.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-68867; Assembly of the pre-replicative complex.
DR Reactome; R-RNO-68949; Orc1 removal from chromatin.
DR Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-RNO-69481; G2/M Checkpoints.
DR Reactome; R-RNO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-RNO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-RNO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-RNO-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-RNO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q63798; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000019246; Expressed in spleen and 20 other tissues.
DR Genevisible; Q63798; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR GO; GO:0061133; F:endopeptidase activator activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019884; P:antigen processing and presentation of exogenous antigen; ISO:RGD.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Phosphoprotein; Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UL46"
FT CHAIN 2..238
FT /note="Proteasome activator complex subunit 2"
FT /id="PRO_0000161788"
FT REGION 65..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL46"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL46"
SQ SEQUENCE 238 AA; 26857 MW; AFA0F013CECE1CD3 CRC64;
MAKPCGVRLS GEARKQVDAF RQNLFQEAED FLCTFLPRKI ISLSQLLQED SLNVADLSSL
RAPLDIPIPD PPPKDDEMET EQEKKEVPKC GFLPGNEKLL ALLALVKPEV WTLKEKCILV
ITWIQHLIPK IEDGNDFGVA IQEKVLERVN AVKTKVEAFQ TAISKYFSER GDAVAKASKD
THVMDYRALV HERDEAAYGA LRAMVLDLRA FYAELHHIIS SNLEKIVNPK GEEKPSMY
