ID PSME2_MOUSE Reviewed; 239 AA. AC P97372; O35562; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 02-SEP-2026, entry version 187. 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; Synonyms=Pa28b1; 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=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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129; RX PubMed=9914329; DOI=10.1007/s002510050476; RA Li Y., Chambers J., Pang J., Ngo K., Peterson P.A., Leung W.P., Yang Y.; RT "Characterization of the mouse proteasome regulator PA28b gene."; RL Immunogenetics 49:149-157(1999). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=11345588; DOI=10.1007/s002510100308; RA Yawata M., Murata S., Tanaka K., Ishigatsubo Y., Kasahara M.; RT "Nucleotide sequence analysis of the ~35-kb segment containing interferon- RT gamma-inducible mouse proteasome activator genes."; RL Immunogenetics 53:119-129(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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: 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; U60329; AAC53296.1; -; mRNA. DR EMBL; AB007138; BAA28837.1; -; Genomic_DNA. DR EMBL; AF060195; AAC83999.1; -; Genomic_DNA. DR EMBL; AB053120; BAB47405.1; -; Genomic_DNA. DR EMBL; AK012344; BAB28175.1; -; mRNA. DR EMBL; BC005680; AAH05680.1; -; mRNA. DR EMBL; BC057859; AAH57859.1; -; mRNA. DR CCDS; CCDS49494.1; -. DR RefSeq; NP_001025026.1; NM_001029855.1. DR RefSeq; NP_035320.1; NM_011190.3. DR PDB; 5MSK; X-ray; 3.60 A; A/B/C/D/E/F/G=1-239. DR PDB; 5MX5; X-ray; 2.90 A; B/D/F/I/K/M=1-239. DR AlphaFoldDB; P97372; -. DR SMR; P97372; -. DR BioGRID; 202433; 39. DR BioGRID; 548745; 1. DR FunCoup; P97372; 1287. DR IntAct; P97372; 3. DR STRING; 10090.ENSMUSP00000100564; -. DR GlyGen; P97372; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P97372; -. DR PhosphoSitePlus; P97372; -. DR SwissPalm; P97372; -. DR CPTAC; non-CPTAC-3942; -. DR jPOST; P97372; -. DR PaxDb; 10090-ENSMUSP00000100564; -. DR PeptideAtlas; P97372; -. DR ProteomicsDB; 301991; -. DR Pumba; P97372; -. DR DNASU; 19188; -. DR Ensembl; ENSMUST00000104958.2; ENSMUSP00000100564.2; ENSMUSG00000078153.4. DR Ensembl; ENSMUST00000161807.8; ENSMUSP00000123798.2; ENSMUSG00000079197.11. DR GeneID; 19188; -. DR KEGG; mmu:19188; -. DR KEGG; mmu:621823; -. DR UCSC; uc007tzg.1; mouse. DR AGR; MGI:1096365; -. DR CTD; 5721; -. DR MGI; MGI:1096365; Psme2. DR VEuPathDB; HostDB:ENSMUSG00000078153; -. DR VEuPathDB; HostDB:ENSMUSG00000079197; -. DR eggNOG; KOG4470; Eukaryota. DR GeneTree; ENSGT00950000183098; -. DR HOGENOM; CLU_062515_0_1_1; -. DR InParanoid; P97372; -. DR OMA; KKPPKCG; -. DR OrthoDB; 6591885at2759; -. DR PhylomeDB; P97372; -. DR Reactome; R-MMU-1236974; ER-Phagosome pathway. DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-MMU-9907900; Proteasome assembly. DR Reactome; R-MMU-9912633; Antigen processing: Ub, ATP-independent proteasomal degradation. DR BioGRID-ORCS; 19188; 5 hits in 80 CRISPR screens. DR BioGRID-ORCS; 621823; 1 hit in 56 CRISPR screens. DR PRO; PR:P97372; -. DR Proteomes; UP000000589; Chromosome 11. DR Proteomes; UP000000589; Chromosome 14. DR RNAct; P97372; protein. DR Bgee; ENSMUSG00000078153; Expressed in spleen and 55 other cell types or tissues. DR ExpressionAtlas; P97372; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central. DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro. DR GO; GO:0000502; C:proteasome complex; ISO:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0019884; P:antigen processing and presentation of exogenous antigen; IMP:MGI. 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:GO_Central. DR FunFam; 1.20.120.180:FF:000002; Proteasome activator complex subunit 1; 1. DR FunFam; 1.20.5.120:FF:000002; proteasome activator complex subunit 2; 1. DR Gene3D; 1.20.120.180; Proteasome activator pa28, C-terminal domain; 1. DR Gene3D; 1.20.5.120; Proteasome activator pa28, N-terminal domain; 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:SF6; PROTEASOME ACTIVATOR COMPLEX SUBUNIT 2; 1. DR PANTHER; PTHR10660; PROTEASOME REGULATOR PA28; 1. DR Pfam; PF02252; PA28_C; 1. DR Pfam; PF02251; PA28_N; 1. DR SUPFAM; SSF47216; Proteasome activator; 1. DR PDBsum; 5MSK; -. DR PDBsum; 5MX5; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Phosphoprotein; Proteasome; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q9UL46" FT CHAIN 2..239 FT /note="Proteasome activator complex subunit 2" FT /id="PRO_0000161786" FT REGION 65..87 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..87 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" FT CONFLICT 152 FT /note="A -> P (in Ref. 2; AAC53296)" FT /evidence="ECO:0000305" FT HELIX 11..30 FT /evidence="ECO:0007829|PDB:5MX5" FT HELIX 31..35 FT /evidence="ECO:0007829|PDB:5MX5" FT HELIX 36..47 FT /evidence="ECO:0007829|PDB:5MX5" FT TURN 50..52 FT /evidence="ECO:0007829|PDB:5MX5" FT HELIX 57..60 FT /evidence="ECO:0007829|PDB:5MX5" FT HELIX 66..71 FT /evidence="ECO:0007829|PDB:5MX5" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:5MX5" FT HELIX 98..128 FT /evidence="ECO:0007829|PDB:5MX5" FT HELIX 138..180 FT /evidence="ECO:0007829|PDB:5MX5" FT STRAND 181..184 FT /evidence="ECO:0007829|PDB:5MX5" FT HELIX 186..222 FT /evidence="ECO:0007829|PDB:5MX5" FT HELIX 224..228 FT /evidence="ECO:0007829|PDB:5MX5" SQ SEQUENCE 239 AA; 27057 MW; D8BB90F78CB0DD7C CRC64; MAKPCGVRLS GEARKQVDVF RQNLFQEADD FLCTFLPRKI ISLSQLLQED SLNVADLSSL RAPLDIPIPD PPPKDDEMET DKQEKKEVPK CGYLPGNEKL LALLALVKPE VWTLKEKCIL VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK DTHVMDYRAL VHERDEAAYG ALRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY //