PSME2_HUMAN
ID PSME2_HUMAN Reviewed; 239 AA.
AC Q9UL46; Q15129;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 195.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-89.
RX PubMed=10199920; DOI=10.1007/s002510050517;
RA McCusker D., Wilson M., Trowsdale J.;
RT "Organization of the genes encoding the human proteasome activators
RT PA28alpha and beta.";
RL Immunogenetics 49:438-445(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-89.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-89.
RC TISSUE=Liver, Pancreas, and Placenta;
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 PROTEIN SEQUENCE OF 2-61; 91-115; 132-145; 155-171; 181-226 AND 232-239,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 -!- INTERACTION:
CC Q9UL46; Q9BVJ7: DUSP23; NbExp=3; IntAct=EBI-741630, EBI-724940;
CC Q9UL46; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-741630, EBI-739832;
CC Q9UL46; Q06323: PSME1; NbExp=6; IntAct=EBI-741630, EBI-712149;
CC Q9UL46; Q9UL46: PSME2; NbExp=6; IntAct=EBI-741630, EBI-741630;
CC Q9UL46; O00560: SDCBP; NbExp=3; IntAct=EBI-741630, EBI-727004;
CC Q9UL46; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-741630, EBI-607755;
CC -!- INDUCTION: By IFNG/IFN-gamma.
CC -!- SIMILARITY: Belongs to the PA28 family. {ECO:0000305}.
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DR EMBL; AF079558; AAF02218.1; -; Genomic_DNA.
DR EMBL; D45248; BAA08205.1; -; mRNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004368; AAH04368.1; -; mRNA.
DR EMBL; BC019885; AAH19885.1; -; mRNA.
DR EMBL; BC072025; AAH72025.1; -; mRNA.
DR CCDS; CCDS9614.1; -.
DR PIR; I53518; I53518.
DR RefSeq; NP_002809.2; NM_002818.2.
DR PDB; 7DR6; EM; 4.10 A; A/D/F=1-239.
DR PDB; 7DRW; EM; 4.20 A; H/K/M/O/c/g=1-239.
DR PDBsum; 7DR6; -.
DR PDBsum; 7DRW; -.
DR AlphaFoldDB; Q9UL46; -.
DR SMR; Q9UL46; -.
DR BioGRID; 111693; 101.
DR CORUM; Q9UL46; -.
DR IntAct; Q9UL46; 42.
DR MINT; Q9UL46; -.
DR STRING; 9606.ENSP00000216802; -.
DR ChEMBL; CHEMBL4295982; -.
DR GlyGen; Q9UL46; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UL46; -.
DR MetOSite; Q9UL46; -.
DR PhosphoSitePlus; Q9UL46; -.
DR SwissPalm; Q9UL46; -.
DR BioMuta; PSME2; -.
DR DMDM; 296453017; -.
DR OGP; Q9UL46; -.
DR REPRODUCTION-2DPAGE; IPI00384051; -.
DR CPTAC; CPTAC-262; -.
DR CPTAC; CPTAC-263; -.
DR EPD; Q9UL46; -.
DR jPOST; Q9UL46; -.
DR MassIVE; Q9UL46; -.
DR MaxQB; Q9UL46; -.
DR PaxDb; Q9UL46; -.
DR PeptideAtlas; Q9UL46; -.
DR PRIDE; Q9UL46; -.
DR ProteomicsDB; 84947; -.
DR TopDownProteomics; Q9UL46; -.
DR Antibodypedia; 22660; 396 antibodies from 36 providers.
DR DNASU; 5721; -.
DR Ensembl; ENST00000216802.10; ENSP00000216802.5; ENSG00000100911.16.
DR Ensembl; ENST00000645325.2; ENSP00000495790.1; ENSG00000284889.2.
DR GeneID; 5721; -.
DR KEGG; hsa:5721; -.
DR MANE-Select; ENST00000216802.10; ENSP00000216802.5; NM_002818.3; NP_002809.2.
DR UCSC; uc001wmj.4; human.
DR CTD; 5721; -.
DR DisGeNET; 5721; -.
DR GeneCards; PSME2; -.
DR HGNC; HGNC:9569; PSME2.
DR HPA; ENSG00000100911; Low tissue specificity.
DR MIM; 602161; gene.
DR neXtProt; NX_Q9UL46; -.
DR OpenTargets; ENSG00000100911; -.
DR PharmGKB; PA33915; -.
DR VEuPathDB; HostDB:ENSG00000100911; -.
DR eggNOG; KOG4470; Eukaryota.
DR GeneTree; ENSGT00950000183098; -.
DR InParanoid; Q9UL46; -.
DR OMA; KKPPKCG; -.
DR OrthoDB; 1251022at2759; -.
DR PhylomeDB; Q9UL46; -.
DR TreeFam; TF106236; -.
DR PathwayCommons; Q9UL46; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9UL46; -.
DR BioGRID-ORCS; 5721; 28 hits in 1078 CRISPR screens.
DR ChiTaRS; PSME2; human.
DR GeneWiki; PSME2; -.
DR GenomeRNAi; 5721; -.
DR Pharos; Q9UL46; Tbio.
DR PRO; PR:Q9UL46; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9UL46; protein.
DR Bgee; ENSG00000100911; Expressed in granulocyte and 95 other tissues.
DR ExpressionAtlas; Q9UL46; baseline and differential.
DR Genevisible; Q9UL46; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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; TAS:ProtInc.
DR GO; GO:0061133; F:endopeptidase activator activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Phosphoprotein;
KW Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT CHAIN 2..239
FT /note="Proteasome activator complex subunit 2"
FT /id="PRO_0000161785"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 89
FT /note="H -> P (in dbSNP:rs7146672)"
FT /evidence="ECO:0000269|PubMed:10199920,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7789512"
FT /id="VAR_063111"
FT CONFLICT 229
FT /note="N -> T (in Ref. 2; BAA08205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 27402 MW; 98A30D83B3F93A91 CRC64;
MAKPCGVRLS GEARKQVEVF RQNLFQEAEE FLYRFLPQKI IYLNQLLQED SLNVADLTSL
RAPLDIPIPD PPPKDDEMET DKQEKKEVHK CGFLPGNEKV LSLLALVKPE VWTLKEKCIL
VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK
ETHVMDYRAL VHERDEAAYG ELRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY
