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{{Short description|Protein found in humans}}
{{PBB|geneid=5721}}
{{Infobox_gene}}
'''Proteasome activator complex subunit 2''' is a [[protein]] that in humans is encoded by the ''PSME2'' [[gene]].<ref name="pmid7789512">{{cite journal | author = Ahn JY | title = Primary structures of two homologous subunits of PA28, a gamma-interferon-inducible protein activator of the 20S proteasome | journal = FEBS Lett | volume = 366 | issue = 1 | pages = 37–42 |date=Jul 1995 | pmid = 7789512 | pmc = | doi =10.1016/0014-5793(95)00492-R | author-separator = , | author2 = Tanahashi N | author3 = Akiyama K | author4 = Hisamatsu H | author5 = Noda C | author6 = Tanaka K | author7 = Chung CH | author8 = Shibmara N | author9 = Willy PJ | display-authors = 10 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PSME2 proteasome (prosome, macropain) activator subunit 2 (PA28 beta)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5721| accessdate = }}</ref>
'''Proteasome activator complex subunit 2''' is a [[protein]] that in humans is encoded by the ''PSME2'' [[gene]].<ref name="pmid7789512">{{cite journal | vauthors = Ahn JY, Tanahashi N, Akiyama K, Hisamatsu H, Noda C, Tanaka K, Chung CH, Shibmara N, Willy PJ, Mott JD | title = Primary structures of two homologous subunits of PA28, a gamma-interferon-inducible protein activator of the 20S proteasome | journal = FEBS Lett | volume = 366 | issue = 1 | pages = 37–42 | date = Jul 1995 | pmid = 7789512 | doi = 10.1016/0014-5793(95)00492-R | doi-access = free }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PSME2 proteasome (prosome, macropain) activator subunit 2 (PA28 beta)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5721}}</ref>


== Function ==
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{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 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.<ref name="entrez" />
}}


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.<ref name="entrez" />
==Interactions==
PSME2 has been shown to [[Protein-protein interaction|interact]] with [[PSME1]].<ref name=pmid16189514>{{cite journal |last=Rual |first=Jean-François |authorlink= |coauthors=Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc |date=Oct 2005 |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=[[Nature (journal)|Nature]] |volume=437 |issue=7062 |pages=1173–8 |publisher= |location = England| pmid = 16189514 |doi = 10.1038/nature04209 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid8663520>{{cite journal |last=Ahn |first=K |authorlink= |coauthors=Erlander M, Leturcq D, Peterson P A, Früh K, Yang Y |date=Jul 1996 |title=In vivo characterization of the proteasome regulator PA28 |journal=J. Biol. Chem. |volume=271 |issue=30 |pages=18237–42 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 8663520 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.271.30.18237 }}</ref>


==References==
== Interactions ==

PSME2 has been shown to [[Protein-protein interaction|interact]] with [[PSME1]].<ref name=pmid16189514>{{cite journal | vauthors = 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 | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = [[Nature (journal)|Nature]] | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | bibcode = 2005Natur.437.1173R | s2cid = 4427026 }}</ref><ref name=pmid8663520>{{cite journal | vauthors = Ahn K, Erlander M, Leturcq D, Peterson PA, Früh K, Yang Y | title = In vivo characterization of the proteasome regulator PA28 | journal = J. Biol. Chem. | volume = 271 | issue = 30 | pages = 18237–42 | date = Jul 1996 | pmid = 8663520 | doi = 10.1074/jbc.271.30.18237 | doi-access = free }}</ref>

== References ==
{{reflist}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
* {{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 | pages = 801–47 | year = 1996 | pmid = 8811196 | doi = 10.1146/annurev.bi.65.070196.004101 }}
{{PBB_Further_reading
* {{cite journal | vauthors = Sijts A, Sun Y, Janek K, Kral S, Paschen A, Schadendorf D, Kloetzel PM | title = The role of the proteasome activator PA28 in MHC class I antigen processing | journal = Mol. Immunol. | volume = 39 | issue = 3–4 | pages = 165–9 | year = 2002 | pmid = 12200048 | doi = 10.1016/S0161-5890(02)00099-8 }}
| citations =
*{{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 = 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 | doi-access = free }}
* {{cite journal | vauthors = Dubiel W, Pratt G, Ferrell K, Rechsteiner M | title = Purification of an 11 S regulator of the multicatalytic protease | journal = J. Biol. Chem. | volume = 267 | issue = 31 | pages = 22369–77 | year = 1992 | doi = 10.1016/S0021-9258(18)41681-X | pmid = 1429590 | doi-access = free }}
*{{cite journal | author=Sijts A |title=The role of the proteasome activator PA28 in MHC class I antigen processing |journal=Mol. Immunol. |volume=39 |issue= 3–4 |pages= 165–9 |year= 2002 |pmid= 12200048 |doi=10.1016/S0161-5890(02)00099-8 | author-separator=, | author2=Sun Y | author3=Janek K | display-authors=3 | last4=Kral | first4=Sylvie | last5=Paschen | first5=Annettte | last6=Schadendorf | first6=Dirk | last7=Kloetzel | first7=Peter-M }}
*{{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=10.1016/S0092-8674(03)00602-0 }}
* {{cite journal | vauthors = Mott JD, Pramanik BC, Moomaw CR, Afendis SJ, DeMartino GN, Slaughter CA | title = PA28, an activator of the 20 S proteasome, is composed of two nonidentical but homologous subunits | journal = J. Biol. Chem. | volume = 269 | issue = 50 | pages = 31466–71 | year = 1995 | doi = 10.1016/S0021-9258(18)31717-4 | pmid = 7989312 | doi-access = free }}
*{{cite journal | author=Dubiel W, Pratt G, Ferrell K, Rechsteiner M |title=Purification of an 11 S regulator of the multicatalytic protease |journal=J. Biol. Chem. |volume=267 |issue= 31 |pages= 22369–77 |year= 1992 |pmid= 1429590 |doi= }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Mott JD |title=PA28, an activator of the 20 S proteasome, is composed of two nonidentical but homologous subunits |journal=J. Biol. Chem. |volume=269 |issue= 50 |pages= 31466–71 |year= 1995 |pmid= 7989312 |doi= | author-separator=, | author2=Pramanik BC | author3=Moomaw CR | display-authors=3 | last4=Afendis | first4=SJ | last5=Demartino | first5=GN | last6=Slaughter | first6=CA }}
* {{cite journal | vauthors = Ahn K, Erlander M, Leturcq D, Peterson PA, Früh K, Yang Y | title = In vivo characterization of the proteasome regulator PA28 | journal = J. Biol. Chem. | volume = 271 | issue = 30 | pages = 18237–42 | year = 1996 | pmid = 8663520 | doi = 10.1074/jbc.271.30.18237 | doi-access = free }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
* {{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 | doi-access = free }}
* {{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=Ahn K |title=In vivo characterization of the proteasome regulator PA28 |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 18237–42 |year= 1996 |pmid= 8663520 |doi=10.1074/jbc.271.30.18237 | author-separator=, | author2=Erlander M | author3=Leturcq D | display-authors=3 | last4=Peterson | first4=PA | last5=Früh | first5=K | last6=Yang | first6=Y }}
*{{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=10.1074/jbc.272.13.8145 }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | year = 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{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 = Hendil KB, Khan S, Tanaka K | title = Simultaneous binding of PA28 and PA700 activators to 20 S proteasomes | journal = Biochem. J. | volume = 332 ( Pt 3) | issue = Pt 3 | pages = 749–54 | year = 1998 | doi = 10.1042/bj3320749 | pmid = 9620878 | pmc = 1219536 }}
* {{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 | doi = 10.1128/JVI.72.12.10251-10255.1998 | pmid = 9811770 | pmc = 110608 }}
*{{cite journal | author=Suzuki Y |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 | author-separator=, | author2=Yoshitomo-Nakagawa K | author3=Maruyama K | display-authors=3 | last4=Suyama | first4=Akira | last5=Sugano | first5=Sumio }}
*{{cite journal | author=Hendil KB, Khan S, Tanaka K |title=Simultaneous binding of PA28 and PA700 activators to 20 S proteasomes |journal=Biochem. J. |volume=332 ( Pt 3) |issue= Pt 3|pages= 749–54 |year= 1998 |pmid= 9620878 |doi= | pmc=1219536 }}
* {{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=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= | pmc=110608 }}
* {{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 | s2cid = 25235070 }}
* {{cite journal | vauthors = McCusker D, Wilson M, Trowsdale J | title = Organization of the genes encoding the human proteasome activators PA28alpha and beta | journal = Immunogenetics | volume = 49 | issue = 5 | pages = 438–45 | year = 1999 | pmid = 10199920 | doi = 10.1007/s002510050517 | s2cid = 40575791 }}
*{{cite journal | author=Wójcik C |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| author-separator=, | author2=Tanaka K | author3=Paweletz N | display-authors=3 | last4=Naab | first4=U | last5=Wilk | first5=S }}
*{{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 = Tanahashi N, Murakami Y, Minami Y, Shimbara N, Hendil KB, Tanaka K | title = Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis | journal = J. Biol. Chem. | volume = 275 | issue = 19 | pages = 14336–45 | year = 2000 | pmid = 10799514 | doi = 10.1074/jbc.275.19.14336 | doi-access = free }}
*{{cite journal | author=McCusker D, Wilson M, Trowsdale J |title=Organization of the genes encoding the human proteasome activators PA28alpha and beta |journal=Immunogenetics |volume=49 |issue= 5 |pages= 438–45 |year= 1999 |pmid= 10199920 |doi=10.1007/s002510050517 }}
* {{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 | doi-access = free }}
* {{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 | s2cid = 4403228 }}
*{{cite journal | author=Tanahashi N |title=Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14336–45 |year= 2000 |pmid= 10799514 |doi=10.1074/jbc.275.19.14336 | author-separator=, | author2=Murakami Y | author3=Minami Y | display-authors=3 | last4=Shimbara | first4=N | last5=Hendil | first5=KB | last6=Tanaka | first6=K }}
*{{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 | 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 }}
}}
{{refend}}
{{refend}}


{{Proteasome subunits}}
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{{gene-14-stub}}
{{gene-14-stub}}

Latest revision as of 02:03, 14 October 2022

PSME2
Identifiers
AliasesPSME2, PA28B, PA28beta, REGbeta, proteasome activator subunit 2
External IDsOMIM: 602161; MGI: 1096365; HomoloGene: 86889; GeneCards: PSME2; OMA:PSME2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002818

NM_001029855
NM_011190

RefSeq (protein)

NP_002809

NP_001268401

Location (UCSC)Chr 14: 24.14 – 24.15 MbChr 14: 55.82 – 55.83 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Proteasome activator complex subunit 2 is a protein that in humans is encoded by the PSME2 gene.[5][6]

Function

[edit]

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.[6]

Interactions

[edit]

PSME2 has been shown to interact with PSME1.[7][8]

References

[edit]
  1. ^ a b c ENSG00000284889 GRCh38: Ensembl release 89: ENSG00000100911, ENSG00000284889Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000079197Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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". FEBS Lett. 366 (1): 37–42. doi:10.1016/0014-5793(95)00492-R. PMID 7789512.
  6. ^ a b "Entrez Gene: PSME2 proteasome (prosome, macropain) activator subunit 2 (PA28 beta)".
  7. ^ 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. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  8. ^ Ahn K, Erlander M, Leturcq D, Peterson PA, Früh K, Yang Y (Jul 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.

Further reading

[edit]