PSMD1

From Wikipedia, the free encyclopedia

Proteasome (prosome, macropain) 26S subunit, non-ATPase, 1

Identifiers

PSMD1; MGC133040; MGC133041; P112; S1

External IDs

MGI: 1917497 HomoloGene: 2100

Gene ontology
Molecular Function:	• binding
Cellular Component:	• cytosol • proteasome regulatory particle (sensu Eukaryota)
Biological Process:	• regulation of progression through cell cycle

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002807 (mRNA)
NP_002798 (protein)

NM_027357 (mRNA)
NP_081633 (protein)

Location

Chr 2: 231.63 - 231.75 Mb

Chr 1: 87.9 - 87.97 Mb

Pubmed search

[1]

[2]

Proteasome (prosome, macropain) 26S subunit, non-ATPase, 1, also known as PSMD1, is a human gene.^[1]

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 the largest non-ATPase subunit of the 19S regulator lid, which is responsible for substrate recognition and binding.^[1]

[edit] References

^ ^a ^b Entrez Gene: PSMD1 proteasome (prosome, macropain) 26S subunit, non-ATPase, 1.

[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. PMID 12914693.
Yokota K, Kagawa S, Shimizu Y, et al. (1997). "CDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p.". Mol. Biol. Cell 7 (6): 853-70. PMID 8816993.
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. PMID 9079628.
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. PMID 9811770.
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.
Lüders J, Demand J, Höhfeld J (2000). "The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome.". J. Biol. Chem. 275 (7): 4613-7. PMID 10671488.
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. doi:10.1038/nature00939. PMID 12167863.
Huang X, Seifert U, Salzmann U, et al. (2002). "The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing.". J. Mol. Biol. 323 (4): 771-82. PMID 12419264.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Gaddis NC, Chertova E, Sheehy AM, et al. (2003). "Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions.". J. Virol. 77 (10): 5810-20. PMID 12719574.
Lecossier D, Bouchonnet F, Clavel F, Hance AJ (2003). "Hypermutation of HIV-1 DNA in the absence of the Vif protein.". Science 300 (5622): 1112. doi:10.1126/science.1083338. PMID 12750511.
Zhang H, Yang B, Pomerantz RJ, et al. (2003). "The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA.". Nature 424 (6944): 94-8. doi:10.1038/nature01707. PMID 12808465.
Mangeat B, Turelli P, Caron G, et al. (2003). "Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.". Nature 424 (6944): 99-103. doi:10.1038/nature01709. PMID 12808466.
Harris RS, Bishop KN, Sheehy AM, et al. (2003). "DNA deamination mediates innate immunity to retroviral infection.". Cell 113 (6): 803-9. PMID 12809610.
Harris RS, Sheehy AM, Craig HM, et al. (2003). "DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses.". Nat. Immunol. 4 (7): 641-3. doi:10.1038/ni0703-641. PMID 12830140.
Gu Y, Sundquist WI (2003). "Good to CU.". Nature 424 (6944): 21-2. doi:10.1038/424021a. PMID 12840737.
Mariani R, Chen D, Schröfelbauer B, et al. (2003). "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.". Cell 114 (1): 21-31. PMID 12859895.