PSMD4

Proteasome (prosome, macropain) 26S subunit, non-ATPase, 4
	; PDB rendering based on 1p9c.
Available structures
PDB	1P9C, 1P9D, 1UEL, 1YX4, 1YX5, 1YX6, 2KDE, 2KDF
Identifiers
Symbols	PSMD4; AF; AF-1; ASF; MCB1; Rpn10; S5A; pUB-R5
External IDs	OMIM: 601648 MGI: 1201670 HomoloGene: 55691 GeneCards: PSMD4 Gene
Gene Ontology
Molecular function	• protein binding; • zinc ion binding;
Cellular component	• proteasome complex; • cytoplasm;
Biological process	• cell cycle checkpoint; • G1/S transition of mitotic cell cycle; • S phase of mitotic cell cycle; • M/G1 transition of mitotic cell cycle; • mitotic cell cycle; • DNA repair; • regulation of transcription, DNA-dependent; • regulation of cellular amino acid metabolic process; • apoptosis; • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; • viral reproduction; • RNA metabolic process; • mRNA metabolic process; • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; • cellular nitrogen compound metabolic process; • regulation of apoptosis; • negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; • positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; • regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs

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26S proteasome non-ATPase regulatory subunit 4 is an enzyme that in humans is encoded by the PSMD4 gene.^[1]^[2]

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. This gene encodes one of the non-ATPase subunits of the 19S regulator lid. Pseudogenes have been identified on chromosomes 10 and 21.^[2]

[edit] Interactions

PSMD4 has been shown to interact with RAD23A^[3]^[4] and RAD23B.^[3]

[edit] References

^ Ferrell K, Deveraux Q, van Nocker S, Rechsteiner M (Jul 1996). "Molecular cloning and expression of a multiubiquitin chain binding subunit of the human 26S protease". FEBS Lett 381 (1–2): 143–8. doi:10.1016/0014-5793(96)00101-9. PMID 8641424.
^ ^a ^b "Entrez Gene: PSMD4 proteasome (prosome, macropain) 26S subunit, non-ATPase, 4". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5710.
^ ^a ^b Hiyama, H; Yokoi M, Masutani C, Sugasawa K, Maekawa T, Tanaka K, Hoeijmakers J H, Hanaoka F (Sep. 1999). "Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome". J. Biol. Chem. (UNITED STATES) 274 (39): 28019–25. doi:10.1074/jbc.274.39.28019. ISSN 0021-9258. PMID 10488153.
^ Mueller, Thomas D; Feigon Juli (Sep. 2003). "Structural determinants for the binding of ubiquitin-like domains to the proteasome". EMBO J. (England) 22 (18): 4634–45. doi:10.1093/emboj/cdg467. ISSN 0261-4189. PMC 212733. PMID 12970176. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=212733.

[edit] 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.
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.
Lönnroth I, Lange S (1986). "Purification and characterization of the antisecretory factor: a protein in the central nervous system and in the gut which inhibits intestinal hypersecretion induced by cholera toxin". Biochim. Biophys. Acta 883 (1): 138–44. PMID 3524692.
Johansson E, Lönnroth I, Lange S et al. (1995). "Molecular cloning and expression of a pituitary gland protein modulating intestinal fluid secretion". J. Biol. Chem. 270 (35): 20615–20. doi:10.1074/jbc.270.35.20615. PMID 7657640.
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.
Anand G, Yin X, Shahidi AK et al. (1997). "Novel regulation of the helix-loop-helix protein Id1 by S5a, a subunit of the 26 S proteasome". J. Biol. Chem. 272 (31): 19140–51. doi:10.1074/jbc.272.31.19140. PMID 9235903.
Young P, Deveraux Q, Beal RE et al. (1998). "Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a". J. Biol. Chem. 273 (10): 5461–7. doi:10.1074/jbc.273.10.5461. PMID 9488668.
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. PMC 110608. PMID 9811770. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110608.
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.
Hiyama H, Yokoi M, Masutani C et al. (1999). "Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome". J. Biol. Chem. 274 (39): 28019–25. doi:10.1074/jbc.274.39.28019. PMID 10488153.
Tateishi K, Misumi Y, Ikehara Y et al. (1999). "Molecular cloning and expression of rat antisecretory factor and its intracellular localization". Biochem. Cell Biol. 77 (3): 223–8. doi:10.1139/bcb-77-3-223. PMID 10505793.
Tanahashi N, Murakami Y, Minami Y et al. (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.
Kawahara H, Kasahara M, Nishiyama A et al. (2000). "Developmentally regulated, alternative splicing of the Rpn10 gene generates multiple forms of 26S proteasomes". EMBO J. 19 (15): 4144–53. doi:10.1093/emboj/19.15.4144. PMC 306610. PMID 10921894. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=306610.
Connell P, Ballinger CA, Jiang J et al. (2001). "The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins". Nat. Cell Biol. 3 (1): 93–6. doi:10.1038/35050618. PMID 11146632.
Kamitani T, Kito K, Fukuda-Kamitani T, Yeh ET (2002). "Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1". J. Biol. Chem. 276 (49): 46655–60. doi:10.1074/jbc.M108636200. PMID 11585840.
Walters KJ, Kleijnen MF, Goh AM et al. (2002). "Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a". Biochemistry 41 (6): 1767–77. doi:10.1021/bi011892y. PMID 11827521.
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. doi:10.1038/nature00939. PMID 12167863.