PSMD10

PSMD10
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1QYM, 1TR4, 1UOH, 4NIK
Identifiers
Aliases	PSMD10 , dJ889N15.2, p28, p28(GANK), proteasome 26S subunit, non-ATPase 10
External IDs	OMIM: 300880 MGI: 1858898 HomoloGene: 94517 GeneCards: PSMD10
Gene location (Human) Chr. X chromosome (human) [1] Band Xq22.3 Start 108,084,207 bp [1] End 108,091,549 bp [1]
Gene location (Mouse) Chr. X chromosome (mouse) [2] Band X|X F1 Start 139,849,178 bp [2] End 139,857,477 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in hypothalamus islet of Langerhans palpebral conjunctiva tibia bronchial epithelial cell ganglionic eminence germinal epithelium corpus callosum substantia nigra corpus epididymis Top expressed in yolk sac proximal tubule secondary oocyte ileum lens neural tube stomach jejunum lung kidney More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transcription factor binding protein binding Cellular component intermediate filament cytoskeleton cytoplasm nucleoplasm proteasome regulatory particle, base subcomplex nucleus proteasome regulatory particle proteasome complex cytosol Biological process negative regulation of release of cytochrome c from mitochondria cytoplasmic sequestering of NF-kappaB positive regulation of cyclin-dependent protein serine/threonine kinase activity positive regulation of cell growth negative regulation of transcription by RNA polymerase II negative regulation of MAPK cascade negative regulation of DNA damage response, signal transduction by p53 class mediator proteasome regulatory particle assembly positive regulation of protein ubiquitination negative regulation of NF-kappaB transcription factor activity positive regulation of proteasomal ubiquitin-dependent protein catabolic process negative regulation of apoptotic process apoptotic process protein deubiquitination post-translational protein modification MAPK cascade protein polyubiquitination stimulatory C-type lectin receptor signaling pathway antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent regulation of cellular amino acid metabolic process negative regulation of G2/M transition of mitotic cell cycle anaphase-promoting complex-dependent catabolic process SCF-dependent proteasomal ubiquitin-dependent protein catabolic process tumor necrosis factor-mediated signaling pathway NIK/NF-kappaB signaling Fc-epsilon receptor signaling pathway proteasome-mediated ubiquitin-dependent protein catabolic process regulation of mRNA stability T cell receptor signaling pathway transmembrane transport Wnt signaling pathway, planar cell polarity pathway regulation of transcription from RNA polymerase II promoter in response to hypoxia interleukin-1-mediated signaling pathway negative regulation of canonical Wnt signaling pathway positive regulation of canonical Wnt signaling pathway regulation of mitotic cell cycle phase transition regulation of hematopoietic stem cell differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5716 53380 Ensembl ENSG00000101843 ENSMUSG00000031429 UniProt O75832 Q9Z2X2 RefSeq (mRNA) NM_170750 NM_002814 NM_001164177 NM_016883 RefSeq (protein) NP_002805 NP_736606 NP_001157649 NP_058579 Location (UCSC) Chr X: 108.08 – 108.09 Mb Chr X: 139.85 – 139.86 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

26S proteasome non-ATPase regulatory subunit 10 or gankyrin is an enzyme that in humans is encoded by the PSMD10 gene. ^[5] First isolated in 1998 by Tanaka et al.; Gankyrin is an oncoprotein that is a component of the 19S regulatory cap of the proteasome. ^{[6] [7]} Structurally, it contains a 33-amino acid ankyrin repeat that forms a series of alpha helices. ^[8] 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. ^[9] Gankyrin also has an anti-apoptotic effect and is overexpressed in certain types of tumor cells such as hepatocellular carcinoma. ^[10]

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. ^[11]

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) ^[12] 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. ^[13] 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, ^{[14] [15]} cardiovascular diseases, ^{[16] [17] [18]} inflammatory responses and autoimmune diseases, ^[19] and systemic DNA damage responses leading to malignancies. ^[20]

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, ^[21] Parkinson's disease ^[22] and Pick's disease, ^[23] Amyotrophic lateral sclerosis (ALS), ^[23] Huntington's disease, ^[22] Creutzfeldt–Jakob disease, ^[24] and motor neuron diseases, polyglutamine (PolyQ) diseases, Muscular dystrophies ^[25] and several rare forms of neurodegenerative diseases associated with dementia. ^[26] As part of the ubiquitin–proteasome system (UPS), the proteasome maintains cardiac protein homeostasis and thus plays a significant role in cardiac ischemic injury, ^[27] ventricular hypertrophy ^[28] and heart failure. ^[29] 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. ^[30] 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). ^[19] 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. ^[31] Lastly, autoimmune disease patients with SLE, Sjögren syndrome and rheumatoid arthritis (RA) predominantly exhibit circulating proteasomes which can be applied as clinical biomarkers. ^[32]

Interactions

PSMD10 has been shown to interact with:

• Mdm2, ^[33]
• PAAF1, ^[34] and
• PSMC4. ^{[34] [35] [36]}

References

1. GRCh38: Ensembl release 89: ENSG00000101843 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031429 - Ensembl, 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. Hori T, Kato S, Saeki M, DeMartino GN, Slaughter CA, Takeuchi J, Toh-e A, Tanaka K (Aug 1998). "cDNA cloning and functional analysis of p28 (Nas6p) and p40.5 (Nas7p), two novel regulatory subunits of the 26S proteasome". Gene. 216 (1): 113–22. doi:10.1016/S0378-1119(98)00309-6. PMID   9714768.
6. Lozano G, Zambetti GP (2005-07-01). "Gankyrin: An intriguing name for a novel regulator of p53 and RB". Cancer Cell. 8 (1): 3–4. doi: 10.1016/j.ccr.2005.06.014 . ISSN   1535-6108. PMID   16023592.
7. Hori T, Kato S, Saeki M, DeMartino GN, Slaughter CA, Takeuchi J, Toh-e A, Tanaka K (1998-08-17). "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". Gene. 216 (1): 113–122. doi:10.1016/S0378-1119(98)00309-6. ISSN   0378-1119. PMID   9714768.
8. Krzywda S, Brzozowski AM, Higashitsuji H, Fujita J, Welchman R, Dawson S, Mayer RJ, Wilkinson AJ (2004). "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". The Journal of Biological Chemistry. 279 (2): 1541–5. doi: 10.1074/jbc.M310265200 . PMID   14573599.
9. Krzywda S, Brzozowski AM, Al-Safty R, Welchman R, Mee M, Dawson S, Fujita J, Higashitsuji H, Mayer RJ, Wilkinson AJ (2003). "Crystallization of gankyrin, an oncoprotein that interacts with CDK4 and the S6b (rpt3) ATPase of the 19S regulator of the 26S proteasome". Acta Crystallographica Section D. 59 (Pt 7): 1294–5. doi:10.1107/S0907444903009892. PMID   12832791.
10. Higashitsuji H, Liu Y, Mayer RJ, Fujita J (2005). "The oncoprotein gankyrin negatively regulates both p53 and RB by enhancing proteasomal degradation". Cell Cycle. 4 (10): 1335–7. doi:10.4161/cc.4.10.2107. PMID   16177571. S2CID   1722598.
11. "Entrez Gene: PSMD10 proteasome (prosome, macropain) 26S subunit, non-ATPase, 10".
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15. Ortega Z, Lucas JJ (2014). "Ubiquitin-proteasome system involvement in Huntington's disease". Frontiers in Molecular Neuroscience. 7: 77. doi: 10.3389/fnmol.2014.00077 . PMC   4179678 . PMID   25324717.
16. Sandri M, Robbins J (Jun 2014). "Proteotoxicity: an underappreciated pathology in cardiac disease". Journal of Molecular and Cellular Cardiology. 71: 3–10. doi:10.1016/j.yjmcc.2013.12.015. PMC   4011959 . PMID   24380730.
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18. Wang ZV, Hill JA (Feb 2015). "Protein quality control and metabolism: bidirectional control in the heart". Cell Metabolism. 21 (2): 215–26. doi:10.1016/j.cmet.2015.01.016. PMC   4317573 . PMID   25651176.
19. Karin M, Delhase M (Feb 2000). "The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signalling". Seminars in Immunology. 12 (1): 85–98. doi:10.1006/smim.2000.0210. PMID   10723801.
20. Ermolaeva MA, Dakhovnik A, Schumacher B (Sep 2015). "Quality control mechanisms in cellular and systemic DNA damage responses". Ageing Research Reviews. 23 (Pt A): 3–11. doi:10.1016/j.arr.2014.12.009. PMC   4886828 . PMID   25560147.
21. Checler F, da Costa CA, Ancolio K, Chevallier N, Lopez-Perez E, Marambaud P (Jul 2000). "Role of the proteasome in Alzheimer's disease". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1502 (1): 133–8. doi:10.1016/s0925-4439(00)00039-9. PMID   10899438.
22. Chung KK, Dawson VL, Dawson TM (Nov 2001). "The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders". Trends in Neurosciences. 24 (11 Suppl): S7–14. doi:10.1016/s0166-2236(00)01998-6. PMID   11881748. S2CID   2211658.
23. Ikeda K, Akiyama H, Arai T, Ueno H, Tsuchiya K, Kosaka K (Jul 2002). "Morphometrical reappraisal of motor neuron system of Pick's disease and amyotrophic lateral sclerosis with dementia". Acta Neuropathologica. 104 (1): 21–8. doi:10.1007/s00401-001-0513-5. PMID   12070660. S2CID   22396490.
24. Manaka H, Kato T, Kurita K, Katagiri T, Shikama Y, Kujirai K, Kawanami T, Suzuki Y, Nihei K, Sasaki H (May 1992). "Marked increase in cerebrospinal fluid ubiquitin in Creutzfeldt–Jakob disease". Neuroscience Letters. 139 (1): 47–9. doi:10.1016/0304-3940(92)90854-z. PMID   1328965. S2CID   28190967.
25. Mathews KD, Moore SA (Jan 2003). "Limb-girdle muscular dystrophy". Current Neurology and Neuroscience Reports. 3 (1): 78–85. doi:10.1007/s11910-003-0042-9. PMID   12507416. S2CID   5780576.
26. Mayer RJ (Mar 2003). "From neurodegeneration to neurohomeostasis: the role of ubiquitin". Drug News & Perspectives. 16 (2): 103–8. doi:10.1358/dnp.2003.16.2.829327. PMID   12792671.
27. Calise J, Powell SR (Feb 2013). "The ubiquitin proteasome system and myocardial ischemia". American Journal of Physiology. Heart and Circulatory Physiology. 304 (3): H337–49. doi:10.1152/ajpheart.00604.2012. PMC   3774499 . PMID   23220331.
28. Predmore JM, Wang P, Davis F, Bartolone S, Westfall MV, Dyke DB, Pagani F, Powell SR, Day SM (Mar 2010). "Ubiquitin proteasome dysfunction in human hypertrophic and dilated cardiomyopathies". Circulation. 121 (8): 997–1004. doi:10.1161/CIRCULATIONAHA.109.904557. PMC   2857348 . PMID   20159828.
29. Powell SR (Jul 2006). "The ubiquitin–proteasome system in cardiac physiology and pathology". American Journal of Physiology. Heart and Circulatory Physiology. 291 (1): H1–H19. doi:10.1152/ajpheart.00062.2006. PMID   16501026. S2CID   7073263.
30. Adams J (Apr 2003). "Potential for proteasome inhibition in the treatment of cancer". Drug Discovery Today. 8 (7): 307–15. doi:10.1016/s1359-6446(03)02647-3. PMID   12654543.
31. Ben-Neriah Y (Jan 2002). "Regulatory functions of ubiquitination in the immune system". Nature Immunology. 3 (1): 20–6. doi:10.1038/ni0102-20. PMID   11753406. S2CID   26973319.
32. Egerer K, Kuckelkorn U, Rudolph PE, Rückert JC, Dörner T, Burmester GR, Kloetzel PM, Feist E (Oct 2002). "Circulating proteasomes are markers of cell damage and immunologic activity in autoimmune diseases". The Journal of Rheumatology. 29 (10): 2045–52. PMID   12375310.
33. Qiu W, Wu J, Walsh EM, Zhang Y, Chen CY, Fujita J, Xiao ZX (Jul 2008). "Retinoblastoma protein modulates gankyrin-MDM2 in regulation of p53 stability and chemosensitivity in cancer cells". Oncogene. 27 (29): 4034–43. doi:10.1038/onc.2008.43. PMID   18332869. S2CID   7815368.
34. 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 (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.
35. 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.
36. Dawson S, Apcher S, Mee M, Higashitsuji H, Baker R, Uhle S, Dubiel W, Fujita J, Mayer RJ (Mar 2002). "Gankyrin is an ankyrin-repeat oncoprotein that interacts with CDK4 kinase and the S6 ATPase of the 26 S proteasome". J. Biol. Chem. 277 (13): 10893–902. doi: 10.1074/jbc.M107313200 . PMID   11779854.

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. S2CID   16340355.
• Sastry L, Cao T, King CR (1997). "Multiple Grb2-protein complexes in human cancer cells". Int. J. Cancer. 70 (2): 208–13. doi: 10.1002/(SICI)1097-0215(19970117)70:2<208::AID-IJC12>3.0.CO;2-E . PMID   9009162. S2CID   10317185.
• 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.
• 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. doi:10.1128/JVI.72.12.10251-10255.1998. PMC   110608 . 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. S2CID   25235070.
• 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.
• Dawson S, Apcher S, Mee M, Higashitsuji H, Baker R, Uhle S, Dubiel W, Fujita J, Mayer RJ (2002). "Gankyrin is an ankyrin-repeat oncoprotein that interacts with CDK4 kinase and the S6 ATPase of the 26 S proteasome". J. Biol. Chem. 277 (13): 10893–902. doi: 10.1074/jbc.M107313200 . PMID   11779854.
• 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. Bibcode:2002Natur.418..646S. doi:10.1038/nature00939. PMID   12167863. S2CID   4403228.
• Fu XY, Wang HY, Tan L, Liu SQ, Cao HF, Wu MC (2002). "Overexpression of p28/gankyrin in human hepatocellular carcinoma and its clinical significance". World J. Gastroenterol. 8 (4): 638–43. doi: 10.3748/wjg.v8.i4.638 . PMC   4656312 . PMID   12174370.
• Huang X, Seifert U, Salzmann U, Henklein P, Preissner R, Henke W, Sijts AJ, Kloetzel PM, Dubiel W (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. doi:10.1016/S0022-2836(02)00998-1. PMID   12419264.
• Nagao T, Higashitsuji H, Nonoguchi K, Sakurai T, Dawson S, Mayer RJ, Itoh K, Fujita J (2003). "MAGE-A4 interacts with the liver oncoprotein gankyrin and suppresses its tumorigenic activity". J. Biol. Chem. 278 (12): 10668–74. doi: 10.1074/jbc.M206104200 . PMID   12525503.
• Gaddis NC, Chertova E, Sheehy AM, Henderson LE, Malim MH (2003). "Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions". J. Virol. 77 (10): 5810–20. doi:10.1128/JVI.77.10.5810-5820.2003. PMC   154025 . 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. S2CID   20591673.
• Zhang H, Yang B, Pomerantz RJ, Zhang C, Arunachalam SC, Gao L (2003). "The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA". Nature. 424 (6944): 94–8. Bibcode:2003Natur.424...94Z. doi:10.1038/nature01707. PMC   1350966 . PMID   12808465.
• Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D (2003). "Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts". Nature. 424 (6944): 99–103. Bibcode:2003Natur.424...99M. doi:10.1038/nature01709. PMID   12808466. S2CID   4347374.
• Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (2003). "DNA deamination mediates innate immunity to retroviral infection". Cell. 113 (6): 803–9. doi: 10.1016/S0092-8674(03)00423-9 . PMID   12809610. S2CID   544971.

External links

• gankyrin+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Overview of all the structural information available in the PDB for UniProt : O75832 (Human 26S proteasome non-ATPase regulatory subunit 10) at the PDBe-KB .
• Overview of all the structural information available in the PDB for UniProt : Q9Z2X2 (Mouse 26S proteasome non-ATPase regulatory subunit 10) at the PDBe-KB .