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PSMD10

{{cs1 config|name-list-style=vanc}}

{{Short description|Enzyme found in humans}}

{{Infobox_gene}}

26S proteasome non-ATPase regulatory subunit 10 or gankyrin is an enzyme that in humans is encoded by the PSMD10 gene.{{cite journal | vauthors = Hori T, Kato S, Saeki M, DeMartino GN, Slaughter CA, Takeuchi J, Toh-e A, Tanaka K | title = cDNA cloning and functional analysis of p28 (Nas6p) and p40.5 (Nas7p), two novel regulatory subunits of the 26S proteasome | journal = Gene | volume = 216 | issue = 1 | pages = 113–22 | date = Aug 1998 | pmid = 9714768 | doi = 10.1016/S0378-1119(98)00309-6 }} First isolated in 1998 by Tanaka et al.; Gankyrin is an oncoprotein that is a component of the 19S regulatory cap of the proteasome.{{Cite journal |last1=Lozano |first1=Guillermina |last2=Zambetti |first2=Gerard P. |date=2005-07-01 |title=Gankyrin: An intriguing name for a novel regulator of p53 and RB |journal=Cancer Cell |volume=8 |issue=1 |pages=3–4 |doi=10.1016/j.ccr.2005.06.014 |pmid=16023592 |issn=1535-6108|doi-access=free }}{{Cite journal |last1=Hori |first1=Tomoko |last2=Kato |first2=Seishi |last3=Saeki |first3=Mihoro |last4=DeMartino |first4=George N. |last5=Slaughter |first5=Clive A. |last6=Takeuchi |first6=Junko |last7=Toh-e |first7=Akio |last8=Tanaka |first8=Keiji |date=1998-08-17 |title=cDNA cloning and functional analysis of p28 (Nas6p) and p40.5 (Nas7p), two novel regulatory subunits of the 26S proteasome1The nucleotide sequence data reported in this paper will appear in the GSDB, DDBJ, EMBL and NCBI Nucleotide Sequence Databases with the following accession numbers: p28 (AB009619) and p40.5 (AB009398).1 |url=https://www.sciencedirect.com/science/article/pii/S0378111998003096 |journal=Gene |language=en |volume=216 |issue=1 |pages=113–122 |doi=10.1016/S0378-1119(98)00309-6 |pmid=9714768 |issn=0378-1119}} Structurally, it contains a 33-amino acid ankyrin repeat that forms a series of alpha helices.{{cite journal | vauthors = Krzywda S, Brzozowski AM, Higashitsuji H, Fujita J, Welchman R, Dawson S, Mayer RJ, Wilkinson AJ | title = The crystal structure of gankyrin, an oncoprotein found in complexes with cyclin-dependent kinase 4, a 19 S proteasomal ATPase regulator, and the tumor suppressors Rb and p53 | journal = The Journal of Biological Chemistry | volume = 279 | issue = 2 | pages = 1541–5 | year = 2004 | pmid = 14573599 | doi = 10.1074/jbc.M310265200 | doi-access = free }} It plays a key role in regulating the cell cycle via protein-protein interactions with the cyclin-dependent kinase CDK4. It also binds closely to the E3 ubiquitin ligase MDM2, which is a regulator of the degradation of p53 and retinoblastoma protein, both transcription factors involved in tumor suppression and found mutated in many cancers.{{cite journal | vauthors = Krzywda S, Brzozowski AM, Al-Safty R, Welchman R, Mee M, Dawson S, Fujita J, Higashitsuji H, Mayer RJ, Wilkinson AJ | title = Crystallization of gankyrin, an oncoprotein that interacts with CDK4 and the S6b (rpt3) ATPase of the 19S regulator of the 26S proteasome | journal = Acta Crystallographica Section D | volume = 59 | issue = Pt 7 | pages = 1294–5 | year = 2003 | pmid = 12832791 | doi = 10.1107/S0907444903009892 }} Gankyrin also has an anti-apoptotic effect and is overexpressed in certain types of tumor cells such as hepatocellular carcinoma.{{cite journal | vauthors = Higashitsuji H, Liu Y, Mayer RJ, Fujita J | title = The oncoprotein gankyrin negatively regulates both p53 and RB by enhancing proteasomal degradation | journal = Cell Cycle | volume = 4 | issue = 10 | pages = 1335–7 | year = 2005 | pmid = 16177571 | doi = 10.4161/cc.4.10.2107 | s2cid = 1722598 | doi-access = }}

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. This gene encodes a non-ATPase subunit of the 19S regulator. Two transcripts encoding different isoforms have been described. Pseudogenes have been identified on chromosomes 3 and 20.{{cite web | title = Entrez Gene: PSMD10 proteasome (prosome, macropain) 26S subunit, non-ATPase, 10| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5716}}

Clinical significance

The proteasome and its subunits are of clinical significance for at least two reasons: (1) a compromised complex assembly or a dysfunctional proteasome can be associated with the underlying pathophysiology of specific diseases, and (2) they can be exploited as drug targets for therapeutic interventions. More recently, more effort has been made to consider the proteasome for the development of novel diagnostic markers and strategies. An improved and comprehensive understanding of the pathophysiology of the proteasome should lead to clinical applications in the future.

The proteasomes form a pivotal component for the ubiquitin–proteasome system (UPS) {{cite journal | vauthors = Kleiger G, Mayor T | title = Perilous journey: a tour of the ubiquitin–proteasome system | journal = Trends in Cell Biology | volume = 24 | issue = 6 | pages = 352–9 | date = Jun 2014 | pmid = 24457024 | pmc = 4037451 | doi = 10.1016/j.tcb.2013.12.003 }} and corresponding cellular Protein Quality Control (PQC). Protein ubiquitination and subsequent proteolysis and degradation by the proteasome are important mechanisms in the regulation of the cell cycle, cell growth and differentiation, gene transcription, signal transduction and apoptosis.{{cite journal | vauthors = Goldberg AL, Stein R, Adams J | title = New insights into proteasome function: from archaebacteria to drug development | journal = Chemistry & Biology | volume = 2 | issue = 8 | pages = 503–8 | date = Aug 1995 | pmid = 9383453 | doi=10.1016/1074-5521(95)90182-5| doi-access = free }} Subsequently, a compromised proteasome complex assembly and function lead to reduced proteolytic activities and the accumulation of damaged or misfolded protein species. Such protein accumulation may contribute to the pathogenesis and phenotypic characteristics in neurodegenerative diseases,{{cite journal | vauthors = Sulistio YA, Heese K | title = The Ubiquitin–Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease | journal = Molecular Neurobiology | date = Jan 2015 | pmid = 25561438 | doi = 10.1007/s12035-014-9063-4 | volume=53 | issue = 2 | pages=905–31| s2cid = 14103185 }}{{cite journal | vauthors = Ortega Z, Lucas JJ | title = Ubiquitin-proteasome system involvement in Huntington's disease | journal = Frontiers in Molecular Neuroscience | volume = 7 | pages = 77 | date = 2014 | pmid = 25324717 | pmc = 4179678 | doi = 10.3389/fnmol.2014.00077 | doi-access = free }} cardiovascular diseases,{{cite journal | vauthors = Sandri M, Robbins J | title = Proteotoxicity: an underappreciated pathology in cardiac disease | journal = Journal of Molecular and Cellular Cardiology | volume = 71 | pages = 3–10 | date = Jun 2014 | pmid = 24380730 | pmc = 4011959 | doi = 10.1016/j.yjmcc.2013.12.015 }}{{cite journal | vauthors = Drews O, Taegtmeyer H | title = Targeting the ubiquitin–proteasome system in heart disease: the basis for new therapeutic strategies | journal = Antioxidants & Redox Signaling | volume = 21 | issue = 17 | pages = 2322–43 | date = Dec 2014 | pmid = 25133688 | pmc = 4241867 | doi = 10.1089/ars.2013.5823 }}{{cite journal | vauthors = Wang ZV, Hill JA | title = Protein quality control and metabolism: bidirectional control in the heart | journal = Cell Metabolism | volume = 21 | issue = 2 | pages = 215–26 | date = Feb 2015 | pmid = 25651176 | pmc = 4317573 | doi = 10.1016/j.cmet.2015.01.016 }} inflammatory responses and autoimmune diseases,{{cite journal | vauthors = Karin M, Delhase M | title = The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signalling | journal = Seminars in Immunology | volume = 12 | issue = 1 | pages = 85–98 | date = Feb 2000 | pmid = 10723801 | doi = 10.1006/smim.2000.0210 }} and systemic DNA damage responses leading to malignancies.{{cite journal | vauthors = Ermolaeva MA, Dakhovnik A, Schumacher B | title = Quality control mechanisms in cellular and systemic DNA damage responses | journal = Ageing Research Reviews | volume = 23 | issue = Pt A | pages = 3–11 | date = Sep 2015 | pmid = 25560147 | doi = 10.1016/j.arr.2014.12.009 | pmc=4886828}}

Several experimental and clinical studies have indicated that aberrations and deregulations of the UPS contribute to the pathogenesis of several neurodegenerative and myodegenerative disorders, including Alzheimer's disease,{{cite journal | vauthors = Checler F, da Costa CA, Ancolio K, Chevallier N, Lopez-Perez E, Marambaud P | title = Role of the proteasome in Alzheimer's disease | journal = Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease | volume = 1502 | issue = 1 | pages = 133–8 | date = Jul 2000 | pmid = 10899438 | doi=10.1016/s0925-4439(00)00039-9| doi-access = }} Parkinson's disease{{cite journal | vauthors = Chung KK, Dawson VL, Dawson TM | title = The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders | journal = Trends in Neurosciences | volume = 24 | issue = 11 Suppl | pages = S7–14 | date = Nov 2001 | pmid = 11881748 | doi=10.1016/s0166-2236(00)01998-6| s2cid = 2211658 }} and Pick's disease,{{cite journal | vauthors = Ikeda K, Akiyama H, Arai T, Ueno H, Tsuchiya K, Kosaka K | title = Morphometrical reappraisal of motor neuron system of Pick's disease and amyotrophic lateral sclerosis with dementia | journal = Acta Neuropathologica | volume = 104 | issue = 1 | pages = 21–8 | date = Jul 2002 | pmid = 12070660 | doi = 10.1007/s00401-001-0513-5 | s2cid = 22396490 }} Amyotrophic lateral sclerosis (ALS), Huntington's disease, Creutzfeldt–Jakob disease,{{cite journal | vauthors = Manaka H, Kato T, Kurita K, Katagiri T, Shikama Y, Kujirai K, Kawanami T, Suzuki Y, Nihei K, Sasaki H | title = Marked increase in cerebrospinal fluid ubiquitin in Creutzfeldt–Jakob disease | journal = Neuroscience Letters | volume = 139 | issue = 1 | pages = 47–9 | date = May 1992 | pmid = 1328965 | doi=10.1016/0304-3940(92)90854-z | s2cid = 28190967 }} and motor neuron diseases, polyglutamine (PolyQ) diseases, Muscular dystrophies{{cite journal | vauthors = Mathews KD, Moore SA | title = Limb-girdle muscular dystrophy | journal = Current Neurology and Neuroscience Reports | volume = 3 | issue = 1 | pages = 78–85 | date = Jan 2003 | pmid = 12507416 | doi=10.1007/s11910-003-0042-9| s2cid = 5780576 }} and several rare forms of neurodegenerative diseases associated with dementia.{{cite journal | vauthors = Mayer RJ | title = From neurodegeneration to neurohomeostasis: the role of ubiquitin | journal = Drug News & Perspectives | volume = 16 | issue = 2 | pages = 103–8 | date = Mar 2003 | pmid = 12792671 | doi=10.1358/dnp.2003.16.2.829327}} As part of the ubiquitin–proteasome system (UPS), the proteasome maintains cardiac protein homeostasis and thus plays a significant role in cardiac ischemic injury,{{cite journal | vauthors = Calise J, Powell SR | title = The ubiquitin proteasome system and myocardial ischemia | journal = American Journal of Physiology. Heart and Circulatory Physiology | volume = 304 | issue = 3 | pages = H337–49 | date = Feb 2013 | pmid = 23220331 | pmc = 3774499 | doi = 10.1152/ajpheart.00604.2012 }} ventricular hypertrophy{{cite journal | vauthors = Predmore JM, Wang P, Davis F, Bartolone S, Westfall MV, Dyke DB, Pagani F, Powell SR, Day SM | title = Ubiquitin proteasome dysfunction in human hypertrophic and dilated cardiomyopathies | journal = Circulation | volume = 121 | issue = 8 | pages = 997–1004 | date = Mar 2010 | pmid = 20159828 | pmc = 2857348 | doi = 10.1161/CIRCULATIONAHA.109.904557 }} and heart failure.{{cite journal | vauthors = Powell SR | title = The ubiquitin–proteasome system in cardiac physiology and pathology | journal = American Journal of Physiology. Heart and Circulatory Physiology | volume = 291 | issue = 1 | pages = H1–H19 | date = Jul 2006 | pmid = 16501026 | doi = 10.1152/ajpheart.00062.2006 | s2cid = 7073263 }} Additionally, evidence is accumulating that the UPS plays an essential role in malignant transformation. UPS proteolysis plays a major role in responses of cancer cells to stimulatory signals that are critical for the development of cancer. Accordingly, gene expression by degradation of transcription factors, such as p53, c-jun, c-Fos, NF-κB, c-Myc, HIF-1α, MATα2, STAT3, sterol-regulated element-binding proteins and androgen receptors are all controlled by the UPS and thus involved in the development of various malignancies.{{cite journal | vauthors = Adams J | title = Potential for proteasome inhibition in the treatment of cancer | journal = Drug Discovery Today | volume = 8 | issue = 7 | pages = 307–15 | date = Apr 2003 | pmid = 12654543 | doi=10.1016/s1359-6446(03)02647-3}} Moreover, the UPS regulates the degradation of tumor suppressor gene products such as adenomatous polyposis coli (APC) in colorectal cancer, retinoblastoma (Rb). and von Hippel–Lindau tumor suppressor (VHL), as well as a number of proto-oncogenes (Raf, Myc, Myb, Rel, Src, Mos, ABL). The UPS is also involved in the regulation of inflammatory responses. This activity is usually attributed to the role of proteasomes in the activation of NF-κB which further regulates the expression of pro inflammatory cytokines such as TNF-α, IL-β, IL-8, adhesion molecules (ICAM-1, VCAM-1, P-selectin) and prostaglandins and nitric oxide (NO). Additionally, the UPS also plays a role in inflammatory responses as regulators of leukocyte proliferation, mainly through proteolysis of cyclines and the degradation of CDK inhibitors.{{cite journal | vauthors = Ben-Neriah Y | title = Regulatory functions of ubiquitination in the immune system | journal = Nature Immunology | volume = 3 | issue = 1 | pages = 20–6 | date = Jan 2002 | pmid = 11753406 | doi = 10.1038/ni0102-20 | s2cid = 26973319 }} Lastly, autoimmune disease patients with SLE, Sjögren syndrome and rheumatoid arthritis (RA) predominantly exhibit circulating proteasomes which can be applied as clinical biomarkers.{{cite journal | vauthors = Egerer K, Kuckelkorn U, Rudolph PE, Rückert JC, Dörner T, Burmester GR, Kloetzel PM, Feist E | title = Circulating proteasomes are markers of cell damage and immunologic activity in autoimmune diseases | journal = The Journal of Rheumatology | volume = 29 | issue = 10 | pages = 2045–52 | date = Oct 2002 | pmid = 12375310 }}

Interactions

PSMD10 has been shown to interact with:

  • Mdm2,{{cite journal | vauthors = Qiu W, Wu J, Walsh EM, Zhang Y, Chen CY, Fujita J, Xiao ZX | title = Retinoblastoma protein modulates gankyrin-MDM2 in regulation of p53 stability and chemosensitivity in cancer cells | journal = Oncogene | volume = 27 | issue = 29 | pages = 4034–43 | date = Jul 2008 | pmid = 18332869 | doi = 10.1038/onc.2008.43 | s2cid = 7815368 | doi-access = }}
  • PAAF1,{{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Mol. Syst. Biol. | volume = 3 | pages = 89 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 | year = 2007 }} and
  • PSMC4.{{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 | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | bibcode = 2005Natur.437.1173R | s2cid = 4427026 }}{{cite journal | vauthors = Dawson S, Apcher S, Mee M, Higashitsuji H, Baker R, Uhle S, Dubiel W, Fujita J, Mayer RJ | title = Gankyrin is an ankyrin-repeat oncoprotein that interacts with CDK4 kinase and the S6 ATPase of the 26 S proteasome | journal = J. Biol. Chem. | volume = 277 | issue = 13 | pages = 10893–902 | date = Mar 2002 | pmid = 11779854 | doi = 10.1074/jbc.M107313200 | doi-access = free }}

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References

{{reflist|33em}}

Further reading

{{refbegin|33em}}

  • {{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 }}
  • {{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 | s2cid = 16340355 | doi-access = free }}
  • {{cite journal | vauthors = Sastry L, Cao T, King CR | title = Multiple Grb2-protein complexes in human cancer cells | journal = Int. J. Cancer | volume = 70 | issue = 2 | pages = 208–13 | year = 1997 | pmid = 9009162 | doi = 10.1002/(SICI)1097-0215(19970117)70:2<208::AID-IJC12>3.0.CO;2-E | s2cid = 10317185 | doi-access = free }}
  • {{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 = 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 = 10.1128/JVI.72.12.10251-10255.1998}}
  • {{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 = 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 = Dawson S, Apcher S, Mee M, Higashitsuji H, Baker R, Uhle S, Dubiel W, Fujita J, Mayer RJ | title = Gankyrin is an ankyrin-repeat oncoprotein that interacts with CDK4 kinase and the S6 ATPase of the 26 S proteasome | journal = J. Biol. Chem. | volume = 277 | issue = 13 | pages = 10893–902 | year = 2002 | pmid = 11779854 | doi = 10.1074/jbc.M107313200 | 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 | vauthors = Fu XY, Wang HY, Tan L, Liu SQ, Cao HF, Wu MC | title = Overexpression of p28/gankyrin in human hepatocellular carcinoma and its clinical significance | journal = World J. Gastroenterol. | volume = 8 | issue = 4 | pages = 638–43 | year = 2002 | pmid = 12174370 | pmc = 4656312 | doi = 10.3748/wjg.v8.i4.638 | doi-access = free }}
  • {{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 | vauthors = Nagao T, Higashitsuji H, Nonoguchi K, Sakurai T, Dawson S, Mayer RJ, Itoh K, Fujita J | title = MAGE-A4 interacts with the liver oncoprotein gankyrin and suppresses its tumorigenic activity | journal = J. Biol. Chem. | volume = 278 | issue = 12 | pages = 10668–74 | year = 2003 | pmid = 12525503 | doi = 10.1074/jbc.M206104200 | doi-access = free | hdl = 2433/148472 | hdl-access = free }}
  • {{cite journal | vauthors = Gaddis NC, Chertova E, Sheehy AM, Henderson LE, Malim MH | title = Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions | journal = J. Virol. | volume = 77 | issue = 10 | pages = 5810–20 | year = 2003 | pmid = 12719574 | pmc = 154025 | doi = 10.1128/JVI.77.10.5810-5820.2003 }}
  • {{cite journal | vauthors = Lecossier D, Bouchonnet F, Clavel F, Hance AJ | title = Hypermutation of HIV-1 DNA in the absence of the Vif protein | journal = Science | volume = 300 | issue = 5622 | pages = 1112 | year = 2003 | pmid = 12750511 | doi = 10.1126/science.1083338 | s2cid = 20591673 }}
  • {{cite journal | vauthors = Zhang H, Yang B, Pomerantz RJ, Zhang C, Arunachalam SC, Gao L | title = The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA | journal = Nature | volume = 424 | issue = 6944 | pages = 94–8 | year = 2003 | pmid = 12808465 | pmc = 1350966 | doi = 10.1038/nature01707 | bibcode = 2003Natur.424...94Z }}
  • {{cite journal | vauthors = Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D | title = Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts | journal = Nature | volume = 424 | issue = 6944 | pages = 99–103 | year = 2003 | pmid = 12808466 | doi = 10.1038/nature01709 | bibcode = 2003Natur.424...99M | s2cid = 4347374 }}
  • {{cite journal | vauthors = Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH | title = DNA deamination mediates innate immunity to retroviral infection | journal = Cell | volume = 113 | issue = 6 | pages = 803–9 | year = 2003 | pmid = 12809610 | doi = 10.1016/S0092-8674(03)00423-9 | s2cid = 544971 | doi-access = free }}

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External links

  • {{MeSH name|gankyrin+protein,+human}}
  • {{PDBe-KB2|O75832|Human 26S proteasome non-ATPase regulatory subunit 10}}
  • {{PDBe-KB2|Q9Z2X2|Mouse 26S proteasome non-ATPase regulatory subunit 10}}

{{PDB Gallery|geneid=5716}}

{{Proteasome subunits}}

Category:Proteins

Category:Oncogenes