# PSME2

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Protein found in humans

PSME2 Identifiers Aliases PSME2, PA28B, PA28beta, REGbeta, proteasome activator subunit 2 External IDs OMIM: 602161; MGI: 1096365; HomoloGene: 86889; GeneCards: PSME2; OMA:PSME2 - orthologs Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q12 Start 24,143,362 bp[1] End 24,147,570 bp[1] Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14 C3|14 28.19 cM Start 55,824,898 bp[2] End 55,828,570 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte duodenum appendix spleen right adrenal cortex mucosa of transverse colon lymph node pituitary gland left adrenal gland left adrenal cortex Top expressed in jejunum duodenum ileum colon adrenal gland ovary uterus epiblast spleen white adipose tissue More reference expression data BioGPS More reference expression data Gene ontology Molecular function endopeptidase activator activity protein binding identical protein binding Cellular component cytoplasm cytosol membrane proteasome activator complex nucleoplasm proteasome complex extracellular exosome Biological process positive regulation of endopeptidase activity regulation of proteasomal protein catabolic process regulation of cellular amino acid metabolic process antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent regulation of mRNA stability positive regulation of canonical Wnt signaling pathway protein polyubiquitination stimulatory C-type lectin receptor signaling pathway tumor necrosis factor-mediated signaling pathway MAPK cascade Fc-epsilon receptor signaling pathway regulation of G1/S transition of mitotic cell cycle NIK/NF-kappaB signaling anaphase-promoting complex-dependent catabolic process T cell receptor signaling pathway negative regulation of canonical Wnt signaling pathway proteasome-mediated ubiquitin-dependent protein catabolic process Wnt signaling pathway, planar cell polarity pathway negative regulation of G2/M transition of mitotic cell cycle protein deubiquitination SCF-dependent proteasomal ubiquitin-dependent protein catabolic process transmembrane transport regulation of transcription from RNA polymerase II promoter in response to hypoxia post-translational protein modification interleukin-12-mediated signaling pathway regulation of hematopoietic stem cell differentiation interleukin-1-mediated signaling pathway regulation of mitotic cell cycle phase transition Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 5721 19188 Ensembl ENSG00000100911 ENSG00000284889 ENSMUSG00000079197 UniProt Q9UL46 P97372 RefSeq (mRNA) NM_002818 NM_001029855 NM_011190 RefSeq (protein) NP_002809 NP_001268401 Location (UCSC) Chr 14: 24.14 – 24.15 Mb Chr 14: 55.82 – 55.83 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Proteasome activator complex subunit 2** is a [protein](/source/Protein) that in humans is encoded by the *PSME2* [gene](/source/Gene).[5][6]

## Function

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 [ATPase](/source/ATPase) subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout [eukaryotic cells](/source/Eukaryotic_cells) at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-[lysosomal](/source/Lysosome) pathway. An essential function of a modified proteasome, the [immunoproteasome](/source/Immunoproteasome), is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the beta subunit of the 11S regulator, one of the two 11S subunits that is induced by gamma-interferon. Three beta and three alpha subunits combine to form a heterohexameric ring. Six [pseudogenes](/source/Pseudogene) have been identified on [chromosomes](/source/Chromosome) 4, 5, 8, 10 and 13.[6]

## Interactions

PSME2 has been shown to [interact](/source/Protein-protein_interaction) with [PSME1](/source/PSME1).[7][8]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [ENSG00000284889 GRCh38: Ensembl release 89: ENSG00000100911, ENSG00000284889](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000100911,) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000079197](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000079197) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=5721). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=19188). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid7789512_5-0)** Ahn JY, Tanahashi N, Akiyama K, Hisamatsu H, Noda C, Tanaka K, Chung CH, Shibmara N, Willy PJ, Mott JD (Jul 1995). ["Primary structures of two homologous subunits of PA28, a gamma-interferon-inducible protein activator of the 20S proteasome"](https://doi.org/10.1016%2F0014-5793%2895%2900492-R). *FEBS Lett*. **366** (1): 37–42. [doi](/source/Doi_(identifier)):[10.1016/0014-5793(95)00492-R](https://doi.org/10.1016%2F0014-5793%2895%2900492-R). [PMID](/source/PMID_(identifier)) [7789512](https://pubmed.ncbi.nlm.nih.gov/7789512).

1. ^ [***a***](#cite_ref-entrez_6-0) [***b***](#cite_ref-entrez_6-1) ["Entrez Gene: PSME2 proteasome (prosome, macropain) activator subunit 2 (PA28 beta)"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=5721).

1. **[^](#cite_ref-pmid16189514_7-0)** Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". *[Nature](/source/Nature_(journal))*. **437** (7062): 1173–8. [Bibcode](/source/Bibcode_(identifier)):[2005Natur.437.1173R](https://ui.adsabs.harvard.edu/abs/2005Natur.437.1173R). [doi](/source/Doi_(identifier)):[10.1038/nature04209](https://doi.org/10.1038%2Fnature04209). [PMID](/source/PMID_(identifier)) [16189514](https://pubmed.ncbi.nlm.nih.gov/16189514). [S2CID](/source/S2CID_(identifier)) [4427026](https://api.semanticscholar.org/CorpusID:4427026).

1. **[^](#cite_ref-pmid8663520_8-0)** Ahn K, Erlander M, Leturcq D, Peterson PA, Früh K, Yang Y (Jul 1996). ["In vivo characterization of the proteasome regulator PA28"](https://doi.org/10.1074%2Fjbc.271.30.18237). *J. Biol. Chem*. **271** (30): 18237–42. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.30.18237](https://doi.org/10.1074%2Fjbc.271.30.18237). [PMID](/source/PMID_(identifier)) [8663520](https://pubmed.ncbi.nlm.nih.gov/8663520).

## Further reading

- Coux O, Tanaka K, Goldberg AL (1996). "Structure and functions of the 20S and 26S proteasomes". *Annu. Rev. Biochem*. **65**: 801–47. [doi](/source/Doi_(identifier)):[10.1146/annurev.bi.65.070196.004101](https://doi.org/10.1146%2Fannurev.bi.65.070196.004101). [PMID](/source/PMID_(identifier)) [8811196](https://pubmed.ncbi.nlm.nih.gov/8811196).

- Sijts A, Sun Y, Janek K, Kral S, Paschen A, Schadendorf D, Kloetzel PM (2002). "The role of the proteasome activator PA28 in MHC class I antigen processing". *Mol. Immunol*. **39** (3–4): 165–9. [doi](/source/Doi_(identifier)):[10.1016/S0161-5890(02)00099-8](https://doi.org/10.1016%2FS0161-5890%2802%2900099-8). [PMID](/source/PMID_(identifier)) [12200048](https://pubmed.ncbi.nlm.nih.gov/12200048).

- Goff SP (2003). ["Death by deamination: a novel host restriction system for HIV-1"](https://doi.org/10.1016%2FS0092-8674%2803%2900602-0). *Cell*. **114** (3): 281–3. [doi](/source/Doi_(identifier)):[10.1016/S0092-8674(03)00602-0](https://doi.org/10.1016%2FS0092-8674%2803%2900602-0). [PMID](/source/PMID_(identifier)) [12914693](https://pubmed.ncbi.nlm.nih.gov/12914693).

- Dubiel W, Pratt G, Ferrell K, Rechsteiner M (1992). ["Purification of an 11 S regulator of the multicatalytic protease"](https://doi.org/10.1016%2FS0021-9258%2818%2941681-X). *J. Biol. Chem*. **267** (31): 22369–77. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(18)41681-X](https://doi.org/10.1016%2FS0021-9258%2818%2941681-X). [PMID](/source/PMID_(identifier)) [1429590](https://pubmed.ncbi.nlm.nih.gov/1429590).

- Mott JD, Pramanik BC, Moomaw CR, Afendis SJ, DeMartino GN, Slaughter CA (1995). ["PA28, an activator of the 20 S proteasome, is composed of two nonidentical but homologous subunits"](https://doi.org/10.1016%2FS0021-9258%2818%2931717-4). *J. Biol. Chem*. **269** (50): 31466–71. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(18)31717-4](https://doi.org/10.1016%2FS0021-9258%2818%2931717-4). [PMID](/source/PMID_(identifier)) [7989312](https://pubmed.ncbi.nlm.nih.gov/7989312).

- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". *Gene*. **138** (1–2): 171–4. [doi](/source/Doi_(identifier)):[10.1016/0378-1119(94)90802-8](https://doi.org/10.1016%2F0378-1119%2894%2990802-8). [PMID](/source/PMID_(identifier)) [8125298](https://pubmed.ncbi.nlm.nih.gov/8125298).

- Ahn K, Erlander M, Leturcq D, Peterson PA, Früh K, Yang Y (1996). ["In vivo characterization of the proteasome regulator PA28"](https://doi.org/10.1074%2Fjbc.271.30.18237). *J. Biol. Chem*. **271** (30): 18237–42. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.30.18237](https://doi.org/10.1074%2Fjbc.271.30.18237). [PMID](/source/PMID_(identifier)) [8663520](https://pubmed.ncbi.nlm.nih.gov/8663520).

- Seeger M, Ferrell K, Frank R, Dubiel W (1997). ["HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation"](https://doi.org/10.1074%2Fjbc.272.13.8145). *J. Biol. Chem*. **272** (13): 8145–8. [doi](/source/Doi_(identifier)):[10.1074/jbc.272.13.8145](https://doi.org/10.1074%2Fjbc.272.13.8145). [PMID](/source/PMID_(identifier)) [9079628](https://pubmed.ncbi.nlm.nih.gov/9079628).

- McCusker D, Jones T, Sheer D, Trowsdale J (1998). "Genetic relationships of the genes encoding the human proteasome beta subunits and the proteasome PA28 complex". *Genomics*. **45** (2): 362–7. [doi](/source/Doi_(identifier)):[10.1006/geno.1997.4948](https://doi.org/10.1006%2Fgeno.1997.4948). [PMID](/source/PMID_(identifier)) [9344661](https://pubmed.ncbi.nlm.nih.gov/9344661).

- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". *Gene*. **200** (1–2): 149–56. [doi](/source/Doi_(identifier)):[10.1016/S0378-1119(97)00411-3](https://doi.org/10.1016%2FS0378-1119%2897%2900411-3). [PMID](/source/PMID_(identifier)) [9373149](https://pubmed.ncbi.nlm.nih.gov/9373149).

- Hendil KB, Khan S, Tanaka K (1998). ["Simultaneous binding of PA28 and PA700 activators to 20 S proteasomes"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1219536). *Biochem. J*. 332 ( Pt 3) (Pt 3): 749–54. [doi](/source/Doi_(identifier)):[10.1042/bj3320749](https://doi.org/10.1042%2Fbj3320749). [PMC](/source/PMC_(identifier)) [1219536](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1219536). [PMID](/source/PMID_(identifier)) [9620878](https://pubmed.ncbi.nlm.nih.gov/9620878).

- Madani N, Kabat D (1998). ["An Endogenous Inhibitor of Human Immunodeficiency Virus in Human Lymphocytes Is Overcome by the Viral Vif Protein"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110608). *J. Virol*. **72** (12): 10251–5. [doi](/source/Doi_(identifier)):[10.1128/JVI.72.12.10251-10255.1998](https://doi.org/10.1128%2FJVI.72.12.10251-10255.1998). [PMC](/source/PMC_(identifier)) [110608](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110608). [PMID](/source/PMID_(identifier)) [9811770](https://pubmed.ncbi.nlm.nih.gov/9811770).

- Wójcik C, Tanaka K, Paweletz N, Naab U, Wilk S (1999). "Proteasome activator (PA28) subunits, alpha, beta and gamma (Ki antigen) in NT2 neuronal precursor cells and HeLa S3 cells". *Eur. J. Cell Biol*. **77** (2): 151–60. [doi](/source/Doi_(identifier)):[10.1016/s0171-9335(98)80083-6](https://doi.org/10.1016%2Fs0171-9335%2898%2980083-6). [PMID](/source/PMID_(identifier)) [9840465](https://pubmed.ncbi.nlm.nih.gov/9840465).

- Simon JH, Gaddis NC, Fouchier RA, Malim MH (1998). "Evidence for a newly discovered cellular anti-HIV-1 phenotype". *Nat. Med*. **4** (12): 1397–400. [doi](/source/Doi_(identifier)):[10.1038/3987](https://doi.org/10.1038%2F3987). [PMID](/source/PMID_(identifier)) [9846577](https://pubmed.ncbi.nlm.nih.gov/9846577). [S2CID](/source/S2CID_(identifier)) [25235070](https://api.semanticscholar.org/CorpusID:25235070).

- McCusker D, Wilson M, Trowsdale J (1999). "Organization of the genes encoding the human proteasome activators PA28alpha and beta". *Immunogenetics*. **49** (5): 438–45. [doi](/source/Doi_(identifier)):[10.1007/s002510050517](https://doi.org/10.1007%2Fs002510050517). [PMID](/source/PMID_(identifier)) [10199920](https://pubmed.ncbi.nlm.nih.gov/10199920). [S2CID](/source/S2CID_(identifier)) [40575791](https://api.semanticscholar.org/CorpusID:40575791).

- Tanahashi N, Murakami Y, Minami Y, Shimbara N, Hendil KB, Tanaka K (2000). ["Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis"](https://doi.org/10.1074%2Fjbc.275.19.14336). *J. Biol. Chem*. **275** (19): 14336–45. [doi](/source/Doi_(identifier)):[10.1074/jbc.275.19.14336](https://doi.org/10.1074%2Fjbc.275.19.14336). [PMID](/source/PMID_(identifier)) [10799514](https://pubmed.ncbi.nlm.nih.gov/10799514).

- Mulder LC, Muesing MA (2000). ["Degradation of HIV-1 integrase by the N-end rule pathway"](https://doi.org/10.1074%2Fjbc.M004670200). *J. Biol. Chem*. **275** (38): 29749–53. [doi](/source/Doi_(identifier)):[10.1074/jbc.M004670200](https://doi.org/10.1074%2Fjbc.M004670200). [PMID](/source/PMID_(identifier)) [10893419](https://pubmed.ncbi.nlm.nih.gov/10893419).

- Sheehy AM, Gaddis NC, Choi JD, Malim MH (2002). "Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein". *Nature*. **418** (6898): 646–50. [Bibcode](/source/Bibcode_(identifier)):[2002Natur.418..646S](https://ui.adsabs.harvard.edu/abs/2002Natur.418..646S). [doi](/source/Doi_(identifier)):[10.1038/nature00939](https://doi.org/10.1038%2Fnature00939). [PMID](/source/PMID_(identifier)) [12167863](https://pubmed.ncbi.nlm.nih.gov/12167863). [S2CID](/source/S2CID_(identifier)) [4403228](https://api.semanticscholar.org/CorpusID:4403228).

v t e Proteasome endopeptidase complex subunits (EC 3.4.25.1) A (alpha subunits) PSMA1 PSMA2 PSMA3 PSMA4 PSMA5 PSMA6 PSMA7 PSMA8 B (beta subunits) PSMB1 PSMB2 PSMB3 PSMB4 PSMB5 PSMB6 PSMB7 PSMB8 PSMB9 PSMB10 C (ATPases) PSMC1 PSMC2 PSMC3 PSMC4 PSMC5 PSMC6 D (non-ATPases) PSMD1 PSMD2 PSMD3 PSMD4 PSMD5 PSMD6 PSMD7 PSMD8 PSMD9 PSMD10 PSMD11 PSMD12 PSMD13 PSMD14 E (activator subunits) PSME1 PSME2 PSME3 PSME4 F (inhibitor subunit) PSMF1

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Adapted from the Wikipedia article [PSME2](https://en.wikipedia.org/wiki/PSME2) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/PSME2?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.