PSME3: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +))
 
m (Bot: HTTP→HTTPS)
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Proteasome activator complex subunit 3''' is a [[protein]] that in humans is encoded by the ''PSME3'' [[gene]].<ref name="pmid7951316">{{cite journal | vauthors = Albertsen HM, Smith SA, Mazoyer S, Fujimoto E, Stevens J, Williams B, Rodriguez P, Cropp CS, Slijepcevic P, Carlson M | title = A physical map and candidate genes in the BRCA1 region on chromosome 17q12-21 | journal = Nat Genet | volume = 7 | issue = 4 | pages = 472–9 | date = Dec 1994 | pmid = 7951316 | pmc =  | doi = 10.1038/ng0894-472 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PSME3 proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10197| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki)
| HGNCid = 9570
| Symbol = PSME3
| AltSymbols =; Ki; PA28-gamma; PA28G; REG-GAMMA
| OMIM = 605129
| ECnumber = 
| Homologene = 2111
| MGIid = 1096366
| GeneAtlas_image1 = PBB_GE_PSME3_200988_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSME3_200987_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_PSME3_209852_x_at_tn.png
| Function = {{GNF_GO|id=GO:0008538 |text = proteasome activator activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0008537 |text = proteasome activator complex}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10197
    | Hs_Ensembl = ENSG00000131467
    | Hs_RefseqProtein = NP_005780
    | Hs_RefseqmRNA = NM_005789
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 38238949
    | Hs_GenLoc_end = 38249301
    | Hs_Uniprot = P61289
    | Mm_EntrezGene = 19192
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_011192
    | Mm_RefseqProtein = NP_035322
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki)''', also known as '''PSME3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSME3 proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10197| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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 gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring. Two transcript variants encoding different isoforms have been identified.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = 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 gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring. Two transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: PSME3 proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10197| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
PSME3 has been shown to [[Protein-protein interaction|interact]] with [[P53]]<ref name=pmid18309296>{{cite journal | vauthors = Zhang Z, Zhang R | title = Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradation | journal = EMBO J. | volume = 27 | issue = 6 | pages = 852–64 | date = Mar 2008 | pmid = 18309296 | pmc = 2265109 | doi = 10.1038/emboj.2008.25 }}</ref> and [[Mdm2]].<ref name=pmid18309296/>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Coux O, Tanaka K, Goldberg AL | title = Structure and functions of the 20S and 26S proteasomes | journal = Annu. Rev. Biochem. | volume = 65 | issue =  | pages = 801–47 | year = 1996 | pmid = 8811196 | doi = 10.1146/annurev.bi.65.070196.004101 }}
| citations =
* {{cite journal | vauthors = Goff SP | title = Death by deamination: a novel host restriction system for HIV-1 | journal = Cell | volume = 114 | issue = 3 | pages = 281–3 | year = 2003 | pmid = 12914693 | doi = 10.1016/S0092-8674(03)00602-0 }}
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue=  |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
* {{cite journal | vauthors = Nikaido T, Shimada K, Shibata M, Hata M, Sakamoto M, Takasaki Y, Sato C, Takahashi T, Nishida Y | title = Cloning and nucleotide sequence of cDNA for Ki antigen, a highly conserved nuclear protein detected with sera from patients with systemic lupus erythematosus | journal = Clin. Exp. Immunol. | volume = 79 | issue = 2 | pages = 209–14 | year = 1990 | pmid = 1968796 | pmc = 1534747 | doi = 10.1111/j.1365-2249.1990.tb05180.x }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
* {{cite journal | vauthors = Miki Y, Swensen J, Shattuck-Eidens D, Futreal PA, Harshman K, Tavtigian S, Liu Q, Cochran C, Bennett LM, Ding W | title = A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1 | journal = Science | volume = 266 | issue = 5182 | pages = 66–71 | year = 1994 | pmid = 7545954 | doi = 10.1126/science.7545954 | bibcode = 1994Sci...266...66M }}
*{{cite journal | author=Nikaido T, Shimada K, Shibata M, ''et al.'' |title=Cloning and nucleotide sequence of cDNA for Ki antigen, a highly conserved nuclear protein detected with sera from patients with systemic lupus erythematosus. |journal=Clin. Exp. Immunol. |volume=79 |issue= 2 |pages= 209-14 |year= 1990 |pmid= 1968796 |doi= }}
* {{cite journal | vauthors = Harshman K, Bell R, Rosenthal J, Katcher H, Miki Y, Swenson J, Gholami Z, Frye C, Ding W, Dayananth P | title = Comparison of the positional cloning methods used to isolate the BRCA1 gene | journal = Hum. Mol. Genet. | volume = 4 | issue = 8 | pages = 1259–66 | year = 1995 | pmid = 7581362 | doi = 10.1093/hmg/4.8.1259 }}
*{{cite journal | author=Miki Y, Swensen J, Shattuck-Eidens D, ''et al.'' |title=A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1. |journal=Science |volume=266 |issue= 5182 |pages= 66-71 |year= 1994 |pmid= 7545954 |doi= }}
* {{cite journal | vauthors = Jacob A, Kandpal G, Patanjali SR, Kandpal RP | title = Molecular cloning and expression pattern of genes from a 470 Kb region near BRCA1 locus on chromosome 17q21 | journal = Oncogene | volume = 11 | issue = 5 | pages = 981–6 | year = 1995 | pmid = 7675458 | doi =  }}
*{{cite journal | author=Harshman K, Bell R, Rosenthal J, ''et al.'' |title=Comparison of the positional cloning methods used to isolate the BRCA1 gene. |journal=Hum. Mol. Genet. |volume=4 |issue= 8 |pages= 1259-66 |year= 1995 |pmid= 7581362 |doi= }}
* {{cite journal | vauthors = Seeger M, Ferrell K, Frank R, Dubiel W | title = HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation | journal = J. Biol. Chem. | volume = 272 | issue = 13 | pages = 8145–8 | year = 1997 | pmid = 9079628 | doi = 10.1074/jbc.272.13.8145 }}
*{{cite journal | author=Jacob A, Kandpal G, Patanjali SR, Kandpal RP |title=Molecular cloning and expression pattern of genes from a 470 Kb region near BRCA1 locus on chromosome 17q21. |journal=Oncogene |volume=11 |issue= 5 |pages= 981-6 |year= 1995 |pmid= 7675458 |doi=  }}
* {{cite journal | vauthors = Kandil E, Kohda K, Ishibashi T, Tanaka K, Kasahara M | title = PA28 subunits of the mouse proteasome: primary structures and chromosomal localization of the genes | journal = Immunogenetics | volume = 46 | issue = 4 | pages = 337–44 | year = 1997 | pmid = 9218537 | doi = 10.1007/s002510050281 }}
*{{cite journal | author=Albertsen HM, Smith SA, Mazoyer S, ''et al.'' |title=A physical map and candidate genes in the BRCA1 region on chromosome 17q12-21. |journal=Nat. Genet. |volume=7 |issue= 4 |pages= 472-9 |year= 1994 |pmid= 7951316 |doi= 10.1038/ng0894-472 }}
* {{cite journal | vauthors = McCusker D, Jones T, Sheer D, Trowsdale J | title = Genetic relationships of the genes encoding the human proteasome beta subunits and the proteasome PA28 complex | journal = Genomics | volume = 45 | issue = 2 | pages = 362–7 | year = 1998 | pmid = 9344661 | doi = 10.1006/geno.1997.4948 }}
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
* {{cite journal | vauthors = Knowlton JR, Johnston SC, Whitby FG, Realini C, Zhang Z, Rechsteiner M, Hill CP | title = Structure of the proteasome activator REGalpha (PA28alpha) | journal = Nature | volume = 390 | issue = 6660 | pages = 639–43 | year = 1998 | pmid = 9403698 | doi = 10.1038/37670 | bibcode = 1997Natur.390..639K }}
*{{cite journal | author=Kandil E, Kohda K, Ishibashi T, ''et al.'' |title=PA28 subunits of the mouse proteasome: primary structures and chromosomal localization of the genes. |journal=Immunogenetics |volume=46 |issue= 4 |pages= 337-44 |year= 1997 |pmid= 9218537 |doi= }}
* {{cite journal | vauthors = Kohda K, Ishibashi T, Shimbara N, Tanaka K, Matsuda Y, Kasahara M | title = Characterization of the mouse PA28 activator complex gene family: complete organizations of the three member genes and a physical map of the approximately 150-kb region containing the alpha- and beta-subunit genes | journal = J. Immunol. | volume = 160 | issue = 10 | pages = 4923–35 | year = 1998 | pmid = 9590240 | doi = }}
*{{cite journal | author=McCusker D, Jones T, Sheer D, Trowsdale J |title=Genetic relationships of the genes encoding the human proteasome beta subunits and the proteasome PA28 complex. |journal=Genomics |volume=45 |issue= 2 |pages= 362-7 |year= 1998 |pmid= 9344661 |doi= 10.1006/geno.1997.4948 }}
* {{cite journal | vauthors = Madani N, Kabat D | title = An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein | journal = J. Virol. | volume = 72 | issue = 12 | pages = 10251–5 | year = 1998 | pmid = 9811770 | pmc = 110608 | doi =  }}
*{{cite journal | author=Knowlton JR, Johnston SC, Whitby FG, ''et al.'' |title=Structure of the proteasome activator REGalpha (PA28alpha). |journal=Nature |volume=390 |issue= 6660 |pages= 639-43 |year= 1998 |pmid= 9403698 |doi= 10.1038/37670 }}
* {{cite journal | vauthors = Wójcik C, Tanaka K, Paweletz N, Naab U, Wilk S | title = Proteasome activator (PA28) subunits, alpha, beta and gamma (Ki antigen) in NT2 neuronal precursor cells and HeLa S3 cells | journal = Eur. J. Cell Biol. | volume = 77 | issue = 2 | pages = 151–60 | year = 1999 | pmid = 9840465 | doi = 10.1016/s0171-9335(98)80083-6 }}
*{{cite journal | author=Kohda K, Ishibashi T, Shimbara N, ''et al.'' |title=Characterization of the mouse PA28 activator complex gene family: complete organizations of the three member genes and a physical map of the approximately 150-kb region containing the alpha- and beta-subunit genes. |journal=J. Immunol. |volume=160 |issue= 10 |pages= 4923-35 |year= 1998 |pmid= 9590240 |doi=  }}
* {{cite journal | vauthors = Simon JH, Gaddis NC, Fouchier RA, Malim MH | title = Evidence for a newly discovered cellular anti-HIV-1 phenotype | journal = Nat. Med. | volume = 4 | issue = 12 | pages = 1397–400 | year = 1998 | pmid = 9846577 | doi = 10.1038/3987 }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
* {{cite journal | vauthors = Mulder LC, Muesing MA | title = Degradation of HIV-1 integrase by the N-end rule pathway | journal = J. Biol. Chem. | volume = 275 | issue = 38 | pages = 29749–53 | year = 2000 | pmid = 10893419 | doi = 10.1074/jbc.M004670200 }}
*{{cite journal | author=Wójcik C, Tanaka K, Paweletz N, ''et al.'' |title=Proteasome activator (PA28) subunits, alpha, beta and gamma (Ki antigen) in NT2 neuronal precursor cells and HeLa S3 cells. |journal=Eur. J. Cell Biol. |volume=77 |issue= 2 |pages= 151-60 |year= 1999 |pmid= 9840465 |doi= }}
* {{cite journal | vauthors = Araya R, Takahashi R, Nomura Y | title = Yeast two-hybrid screening using constitutive-active caspase-7 as bait in the identification of PA28gamma as an effector caspase substrate | journal = Cell Death Differ. | volume = 9 | issue = 3 | pages = 322–8 | year = 2002 | pmid = 11859414 | doi = 10.1038/SJ.CDD.4400949 }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
* {{cite journal | vauthors = Sheehy AM, Gaddis NC, Choi JD, Malim MH | title = Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein | journal = Nature | volume = 418 | issue = 6898 | pages = 646–50 | year = 2002 | pmid = 12167863 | doi = 10.1038/nature00939 | bibcode = 2002Natur.418..646S }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
* {{cite journal | vauthors = Huang X, Seifert U, Salzmann U, Henklein P, Preissner R, Henke W, Sijts AJ, Kloetzel PM, Dubiel W | title = 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 | journal = J. Mol. Biol. | volume = 323 | issue = 4 | pages = 771–82 | year = 2002 | pmid = 12419264 | doi = 10.1016/S0022-2836(02)00998-1 }}
*{{cite journal | author=Araya R, Takahashi R, Nomura Y |title=Yeast two-hybrid screening using constitutive-active caspase-7 as bait in the identification of PA28gamma as an effector caspase substrate. |journal=Cell Death Differ. |volume=9 |issue= 3 |pages= 322-8 |year= 2002 |pmid= 11859414 |doi= 10.1038/sj/cdd/4400949 }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
*{{cite journal  | author=Huang X, Seifert U, Salzmann U, ''et al.'' |title=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. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771-82 |year= 2002 |pmid= 12419264 |doi=  }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* {{UCSC genome browser|PSME3}}
* {{UCSC gene details|PSME3}}
 
{{Proteasome subunits}}
 
{{gene-17-stub}}

Latest revision as of 18:53, 7 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Proteasome activator complex subunit 3 is a protein that in humans is encoded by the PSME3 gene.[1][2]

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 gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring. Two transcript variants encoding different isoforms have been identified.[2]

Interactions

PSME3 has been shown to interact with P53[3] and Mdm2.[3]

References

  1. ↑ Albertsen HM, Smith SA, Mazoyer S, Fujimoto E, Stevens J, Williams B, Rodriguez P, Cropp CS, Slijepcevic P, Carlson M (Dec 1994). "A physical map and candidate genes in the BRCA1 region on chromosome 17q12-21". Nat Genet. 7 (4): 472–9. doi:10.1038/ng0894-472. PMID 7951316.
  2. ↑ 2.0 2.1 "Entrez Gene: PSME3 proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki)".
  3. ↑ 3.0 3.1 Zhang Z, Zhang R (Mar 2008). "Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradation". EMBO J. 27 (6): 852–64. doi:10.1038/emboj.2008.25. PMC 2265109. PMID 18309296.

Further reading

External links

Retrieved from "https://www.wikidoc.org/index.php?title=PSME3&oldid=1417932"