PSME2

PSME2
Identifiers
Aliases	PSME2, PA28B, PA28beta, REGbeta, proteasome activator subunit 2
External IDs	OMIM: 602161 MGI: 1096365 HomoloGene: 86889 GeneCards: PSME2
Gene location (Human) Chr. Chromosome 14 (human) Band 14q12 Start 24,143,362 bp End 24,147,570 bp
Gene location (Mouse) Chr. Chromosome 14 (mouse) Band 14 C3|14 28.19 cM Start 55,824,898 bp End 55,828,570 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in duodenum appendix spleen lymph node pituitary gland left adrenal gland anterior pituitary monocyte rectum right uterine tube Top expressed in jejunum duodenum ileum colon adrenal gland ovary uterus spleen white adipose tissue thymus 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
Wikidata
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Proteasome activator complex subunit 2 is a protein that in humans is encoded by the PSME2 gene.

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 subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the 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 have been identified on chromosomes 4, 5, 8, 10 and 13.

Interactions

PSME2 has been shown to interact with PSME1.

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:10.1146/annurev.bi.65.070196.004101. PMID 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:10.1016/S0161-5890(02)00099-8. PMID 12200048.
• Goff SP (2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281–3. doi:10.1016/S0092-8674(03)00602-0. PMID 12914693.
• Dubiel W, Pratt G, Ferrell K, Rechsteiner M (1992). "Purification of an 11 S regulator of the multicatalytic protease". J. Biol. Chem. 267 (31): 22369–77. doi:10.1016/S0021-9258(18)41681-X. PMID 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". J. Biol. Chem. 269 (50): 31466–71. doi:10.1016/S0021-9258(18)31717-4. PMID 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:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Ahn K, Erlander M, Leturcq D, Peterson PA, Früh K, Yang Y (1996). "In vivo characterization of the proteasome regulator PA28". J. Biol. Chem. 271 (30): 18237–42. doi:10.1074/jbc.271.30.18237. PMID 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". J. Biol. Chem. 272 (13): 8145–8. doi:10.1074/jbc.272.13.8145. PMID 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:10.1006/geno.1997.4948. PMID 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:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Hendil KB, Khan S, Tanaka K (1998). "Simultaneous binding of PA28 and PA700 activators to 20 S proteasomes". Biochem. J. 332 ( Pt 3) (Pt 3): 749–54. doi:10.1042/bj3320749. PMC 1219536. PMID 9620878.
• Madani N, Kabat D (1998). "An Endogenous Inhibitor of Human Immunodeficiency Virus in Human Lymphocytes Is Overcome by the Viral Vif Protein". J. Virol. 72 (12): 10251–5. doi:10.1128/JVI.72.12.10251-10255.1998. PMC 110608. PMID 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:10.1016/s0171-9335(98)80083-6. PMID 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:10.1038/3987. PMID 9846577. S2CID 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:10.1007/s002510050517. PMID 10199920. S2CID 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". J. Biol. Chem. 275 (19): 14336–45. doi:10.1074/jbc.275.19.14336. PMID 10799514.
• Mulder LC, Muesing MA (2000). "Degradation of HIV-1 integrase by the N-end rule pathway". J. Biol. Chem. 275 (38): 29749–53. doi:10.1074/jbc.M004670200. PMID 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:2002Natur.418..646S. doi:10.1038/nature00939. PMID 12167863. S2CID 4403228.