# PSMB9

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Protein found in humans

PSMB9 Identifiers Aliases PSMB9, LMP2, PSMB6i, RING12, beta1i, proteasome subunit beta 9, PRAAS3, proteasome 20S subunit beta 9 External IDs OMIM: 177045; MGI: 1346526; HomoloGene: 2094; GeneCards: PSMB9; OMA:PSMB9 - orthologs Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p21.32 Start 32,844,136 bp[1] End 32,859,851 bp[1] Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17 B1|17 17.98 cM Start 34,400,961 bp[2] End 34,406,738 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte monocyte lymph node appendix blood spleen duodenum mucosa of transverse colon olfactory zone of nasal mucosa right lung Top expressed in spleen thymus mesenteric lymph nodes granulocyte duodenum jejunum mucous cell of stomach intestinal villus blood lactiferous gland More reference expression data BioGPS More reference expression data Gene ontology Molecular function endopeptidase activity peptidase activity protein binding threonine-type endopeptidase activity hydrolase activity Cellular component spermatoproteasome complex nucleoplasm proteasome complex extracellular exosome nucleus proteasome core complex cytoplasm cytosol proteasome core complex, beta-subunit complex Biological process regulation of cellular amino acid metabolic process antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent regulation of mRNA stability regulation of cysteine-type endopeptidase activity positive regulation of canonical Wnt signaling pathway immune system process protein polyubiquitination stimulatory C-type lectin receptor signaling pathway tumor necrosis factor-mediated signaling pathway MAPK cascade proteolysis Fc-epsilon receptor signaling pathway NIK/NF-kappaB signaling anaphase-promoting complex-dependent catabolic process proteolysis involved in cellular protein catabolic process T cell receptor signaling pathway negative regulation of canonical Wnt signaling pathway proteasome-mediated ubiquitin-dependent protein catabolic process viral process Wnt signaling pathway, planar cell polarity pathway negative regulation of G2/M transition of mitotic cell cycle protein deubiquitination SCF-dependent proteasomal ubiquitin-dependent protein catabolic process transmembrane transport regulation of transcription from RNA polymerase II promoter in response to hypoxia post-translational protein modification regulation of hematopoietic stem cell differentiation proteasomal protein catabolic process proteasomal ubiquitin-independent protein catabolic process interleukin-1-mediated signaling pathway regulation of mitotic cell cycle phase transition Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 5698 16912 Ensembl ENSG00000240118 ENSG00000243067 ENSG00000240065 ENSG00000240508 ENSG00000242711 ENSG00000243594 ENSG00000243958 ENSG00000239836 ENSMUSG00000096727 UniProt P28065 P28076 RefSeq (mRNA) NM_002800 NM_148954 NM_013585 RefSeq (protein) NP_002791 NP_038613 Location (UCSC) Chr 6: 32.84 – 32.86 Mb Chr 17: 34.4 – 34.41 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Proteasome subunit beta type-9** as known as **20S proteasome subunit beta-1i** is a [protein](/source/Protein) that in humans is encoded by the *PSMB9* [gene](/source/Gene).[5][6][7]

This protein is one of the 17 essential subunits (alpha subunits 1-7, constitutive beta subunits 1-7, and inducible subunits including **beta1i**, [beta2i](/source/PSMB10), [beta5i](/source/PSMB8)) that contributes to the complete assembly of 20S [proteasome](/source/Proteasome) complex. In particular, proteasome subunit beta type-5, along with other beta subunits, assemble into two heptameric rings and subsequently a proteolytic chamber for substrate degradation. This protein contains "Trypsin-like" activity and is capable of cleaving after basic residues of peptide.[8] The eukaryotic [proteasome](/source/Proteasome) recognized degradable proteins, including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes. The constitutive subunit beta1, beta2, and beta 5 (systematic nomenclature) can be replaced by their inducible counterparts beta1i, 2i, and 5i when cells are under the treatment of interferon-γ. The resulting proteasome complex becomes the so-called immunoproteasome. An essential function of the modified proteasome complex, the immunoproteasome, is the processing of numerous MHC class-I restricted T cell epitopes.[9]

## Structure

### Gene

The gene *PSMB9* encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. This gene is located in the class II region of the [MHC](/source/Major_histocompatibility_complex) (major histocompatibility complex). Expression of this gene is induced by [gamma interferon](/source/Gamma_interferon) and this gene product replaces catalytic subunit 1 (proteasome beta 6 subunit) in the immunoproteasome. Proteolytic processing is required to generate a mature subunit. Two alternative transcripts encoding different isoforms have been identified; both isoforms are processed to yield the same mature subunit.[7] The human PSMB9 gene has 6 exons and locates at chromosome band 6p21.3.

### Protein

The human protein proteasome subunit beta type-9 is 21 kDa in size and composed of 199 amino acids. The calculated theoretical pI of this protein is 4.80.

### Complex assembly

The [proteasome](/source/Proteasome) is a multicatalytic proteinase complex with a highly ordered 20S core structure. This barrel-shaped core structure is composed of 4 axially stacked rings of 28 non-identical subunits: the two end rings are each formed by 7 alpha subunits, and the two central rings are each formed by 7 beta subunits. Three beta subunits ([beta1](/source/PSMB1), [beta2](/source/PSMB2), [beta5](/source/PSMB5)) each contains a proteolytic active site and has distinct substrate preferences. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an [ATP](/source/Adenosine_triphosphate)/[ubiquitin](/source/Ubiquitin)-dependent process in a non-[lysosomal](/source/Lysosomal) pathway.[10][11]

## Function

Protein functions are supported by its tertiary structure and its interaction with associating partners. As one of 28 subunits of 20S proteasome, protein proteasome subunit beta type-2 contributes to form a proteolytic environment for substrate degradation. Evidences of the crystal structures of isolated 20S proteasome complex demonstrate that the two rings of beta subunits form a proteolytic chamber and maintain all their active sites of proteolysis within the chamber.[11] Concomitantly, the rings of alpha subunits form the entrance for substrates entering the proteolytic chamber. In an inactivated 20S proteasome complex, the gate into the internal proteolytic chamber are guarded by the [N-terminal](/source/N-terminal) tails of specific alpha-subunit. This unique structure design prevents random encounter between proteolytic active sites and protein substrate, which makes protein degradation a well-regulated process.[12][13] 20S proteasome complex, by itself, is usually functionally inactive. The proteolytic capacity of 20S core particle (CP) can be activated when CP associates with one or two regulatory particles (RP) on one or both side of alpha rings. These regulatory particles include 19S proteasome complexes, 11S proteasome complex, etc. Following the CP-RP association, the confirmation of certain alpha subunits will change and consequently cause the opening of substrate entrance gate. Besides RPs, the 20S proteasomes can also be effectively activated by other mild chemical treatments, such as exposure to low levels of sodium dodecylsulfate (SDS) or NP-14.[13][14]

The 20S proteasome subunit beta-5i (systematic nomenclature) is originally expressed as a precursor with 276 amino acids. The fragment of 72 amino acids at peptide N-terminal is essential for proper protein folding and subsequent complex assembly. At the end-stage of complex assembly, the N-terminal fragment of beta5 subunit is cleaved, forming the mature beta5i subunit of 20S complex.[15] During the basal assembly, and [proteolytic processing](/source/Proteolysis) is required to generate a mature subunit. The subunit beta5i only presents in the immunoproteasome and is replaced by subunit beta5(proteasome beta 5 subunit) in constitutive 20S proteasome complex.

## 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](/source/Ubiquitin%E2%80%93proteasome_system) (UPS) [16] and corresponding cellular Protein Quality Control (PQC). Protein [ubiquitination](/source/Ubiquitination) and subsequent [proteolysis](/source/Proteolysis) and degradation by the proteasome are important mechanisms in the regulation of the [cell cycle](/source/Cell_cycle), [cell growth](/source/Cell_growth) and differentiation, gene transcription, signal transduction and [apoptosis](/source/Apoptosis).[17] 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,[18][19] cardiovascular diseases,[20][21][22] inflammatory responses and autoimmune diseases,[23] and systemic DNA damage responses leading to [malignancies](/source/Malignancies).[24]

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](/source/Alzheimer's_disease),[25] [Parkinson's disease](/source/Parkinson's_disease)[26] and [Pick's disease](/source/Pick's_disease),[27] [Amyotrophic lateral sclerosis](/source/Amyotrophic_lateral_sclerosis) (ALS),[27] [Huntington's disease](/source/Huntington's_disease),[26] [Creutzfeldt–Jakob disease](/source/Creutzfeldt%E2%80%93Jakob_disease),[28] and motor neuron diseases, polyglutamine (PolyQ) diseases, [Muscular dystrophies](/source/Muscular_dystrophies)[29] and several rare forms of neurodegenerative diseases associated with [dementia](/source/Dementia).[30] As part of the [Ubiquitin-Proteasome System (UPS)](/source/Proteasome), the proteasome maintains cardiac protein homeostasis and thus plays a significant role in cardiac [Ischemic](/source/Ischemic) injury,[31] [ventricular hypertrophy](/source/Ventricular_hypertrophy)[32] and [heart failure](/source/Heart_failure).[33] 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](/source/Transcription_factors), such as [p53](/source/P53), [c-jun](/source/C-jun), [c-Fos](/source/C-Fos), [NF-κB](/source/NF-%CE%BAB), [c-Myc](/source/C-Myc), HIF-1α, MATα2, [STAT3](/source/STAT3), sterol-regulated element-binding proteins and [androgen receptors](/source/Androgen_receptors) are all controlled by the UPS and thus involved in the development of various malignancies.[34] Moreover, the UPS regulates the degradation of tumor suppressor gene products such as [adenomatous polyposis coli](/source/Adenomatous_polyposis_coli) ([APC](/source/Adenomatous_polyposis_coli)) in colorectal cancer, [retinoblastoma](/source/Retinoblastoma) (Rb). and [von Hippel–Lindau tumor suppressor](/source/Von_Hippel%E2%80%93Lindau_tumor_suppressor) (VHL), as well as a number of [proto-oncogenes](/source/Proto-oncogenes) ([Raf](/source/Raf_kinase), [Myc](/source/Myc), [Myb](/source/MYB_(gene)), [Rel](/source/NF-%CE%BAB), [Src](/source/Src_(gene)), [Mos](/source/MOS_(gene)), [Abl](/source/Abl_(gene))). 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](/source/Cytokines) such as [TNF-α](/source/TNF-%CE%B1), IL-β, [IL-8](/source/Interleukin_8), [adhesion molecules](/source/Adhesion_molecules) ([ICAM-1](/source/ICAM-1), [VCAM-1](/source/VCAM-1), [P-selectin](/source/P-selectin)) and [prostaglandins](/source/Prostaglandins) and [nitric oxide](/source/Nitric_oxide) (NO).[23] 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](/source/Cyclin-dependent_kinase) inhibitors.[35] Lastly, [autoimmune disease](/source/Autoimmune_disease) patients with [SLE](/source/Systemic_lupus_erythematosus), [Sjögren syndrome](/source/Sj%C3%B6gren_syndrome) and [rheumatoid arthritis](/source/Rheumatoid_arthritis) (RA) predominantly exhibit circulating proteasomes which can be applied as clinical biomarkers.[36]

During the antigen processing for the major histocompatibility complex (MHC) class-I, the proteasome is the major degradation machinery that degrades the antigen and present the resulting peptides to cytotoxic T lymphocytes.[37][38] The immunoproteasome has been considered playing a critical role in improving the quality and quantity of generated class-I ligands.

The clinical relevance of the PSMB9 protein can be found mostly in the areas of [infectious diseases](/source/Infectious_diseases), [autoimmune diseases](/source/Autoimmune_disease) and [oncology](/source/Oncology). For instance, it has been verified that mRNA coding for PSMB9 (together with [CFD](/source/Complement_factor_D), [MAGED1](/source/MAGED1), [PRDX4](/source/PRDX4) and [FCGR3B](/source/FCGR3B)) is differentially expressed between patients who developed clinical symptoms associated with the mild disease type of [Dengue](/source/Dengue) fever, and patients who showed clinical symptoms associated with severe Dengue. The study suggests that this gene expression panel may serve as biomarkers of clinical prognosis in Dengue hemorrhagic fever.[39] Further studies also indicate a role for PMSB9, in a panel with 9 other genes (Zbp1, Mx2, Irf7, Lfi47, Tapbp, Timp1, Trafd1, Tap2) in the development of [influenza](/source/Influenza) [vaccines](/source/Vaccines),[40] and in the diagnosis of autoimmune disease [Sjögren syndrome](/source/Sj%C3%B6gren_syndrome) in conjunction with 18 other genes ([EPSTI1](/source/Epithelial_stromal_interaction_1), IFI44, IFI44L, [IFIT1](/source/IFIT1), [IFIT2](/source/IFIT2), [IFIT3](/source/IFIT3), [MX1](/source/MX1), [OAS1](/source/OAS1), SAMD9L, [STAT1](/source/STAT1), [HERC5](/source/HERC5), EV12B, [CD53](/source/CD53), [SELL](/source/SELL), [HLA-DQA1](/source/HLA-DQA1), [PTPRC](/source/PTPRC), [B2M](/source/Beta-2_microglobulin), and [TAP2](/source/TAP2)).[41] With regards to oncology, PSMB9 in conjunction with other genes that are involved with immune response processes ([TAP1](/source/TAP1), [PSMB8](/source/PSMB8), PSMB9, [HLA-DQB1](/source/HLA-DQB1), [HLA-DQB2](/source/HLA-DQB2), [HLA-DMA](/source/HLA-DMA), and [HLA-DOA](/source/HLA-DOA)) may form a comprehensive assessment of the clinical outcome in epithelial ovarian carcinoma tumor [methylation](/source/Methylation) assessments. The study suggest that an epigenetically mediated immune response is a predictor of recurrence and, possibly, treatment response for high-grade [serous](/source/Serous) [epithelial](/source/Epithelial) [ovarian](/source/Ovarian) [carcinomas](/source/Carcinomas).[42]

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1. **[^](#cite_ref-22)** Wang ZV, Hill JA (Feb 2015). ["Protein quality control and metabolism: bidirectional control in the heart"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4317573). *Cell Metabolism*. **21** (2): 215–26. [doi](/source/Doi_(identifier)):[10.1016/j.cmet.2015.01.016](https://doi.org/10.1016%2Fj.cmet.2015.01.016). [PMC](/source/PMC_(identifier)) [4317573](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4317573). [PMID](/source/PMID_(identifier)) [25651176](https://pubmed.ncbi.nlm.nih.gov/25651176).

1. ^ [***a***](#cite_ref-Karin_M_2000_23-0) [***b***](#cite_ref-Karin_M_2000_23-1) 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](/source/Doi_(identifier)):[10.1006/smim.2000.0210](https://doi.org/10.1006%2Fsmim.2000.0210). [PMID](/source/PMID_(identifier)) [10723801](https://pubmed.ncbi.nlm.nih.gov/10723801).

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1. ^ [***a***](#cite_ref-ReferenceC_26-0) [***b***](#cite_ref-ReferenceC_26-1) 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](/source/Doi_(identifier)):[10.1016/s0166-2236(00)01998-6](https://doi.org/10.1016%2Fs0166-2236%2800%2901998-6). [PMID](/source/PMID_(identifier)) [11881748](https://pubmed.ncbi.nlm.nih.gov/11881748). [S2CID](/source/S2CID_(identifier)) [2211658](https://api.semanticscholar.org/CorpusID:2211658).

1. ^ [***a***](#cite_ref-IkedaAkiyama2002_27-0) [***b***](#cite_ref-IkedaAkiyama2002_27-1) 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](/source/Doi_(identifier)):[10.1007/s00401-001-0513-5](https://doi.org/10.1007%2Fs00401-001-0513-5). [PMID](/source/PMID_(identifier)) [12070660](https://pubmed.ncbi.nlm.nih.gov/12070660). [S2CID](/source/S2CID_(identifier)) [22396490](https://api.semanticscholar.org/CorpusID:22396490).

1. **[^](#cite_ref-28)** 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](/source/Doi_(identifier)):[10.1016/0304-3940(92)90854-z](https://doi.org/10.1016%2F0304-3940%2892%2990854-z). [PMID](/source/PMID_(identifier)) [1328965](https://pubmed.ncbi.nlm.nih.gov/1328965). [S2CID](/source/S2CID_(identifier)) [28190967](https://api.semanticscholar.org/CorpusID:28190967).

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1. **[^](#cite_ref-30)** Mayer RJ (Mar 2003). "From neurodegeneration to neurohomeostasis: the role of ubiquitin". *Drug News & Perspectives*. **16** (2): 103–8. [doi](/source/Doi_(identifier)):[10.1358/dnp.2003.16.2.829327](https://doi.org/10.1358%2Fdnp.2003.16.2.829327). [PMID](/source/PMID_(identifier)) [12792671](https://pubmed.ncbi.nlm.nih.gov/12792671).

1. **[^](#cite_ref-31)** Calise J, Powell SR (Feb 2013). ["The ubiquitin proteasome system and myocardial ischemia"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3774499). *American Journal of Physiology. Heart and Circulatory Physiology*. **304** (3): H337–49. [doi](/source/Doi_(identifier)):[10.1152/ajpheart.00604.2012](https://doi.org/10.1152%2Fajpheart.00604.2012). [PMC](/source/PMC_(identifier)) [3774499](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3774499). [PMID](/source/PMID_(identifier)) [23220331](https://pubmed.ncbi.nlm.nih.gov/23220331).

1. **[^](#cite_ref-32)** 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"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2857348). *Circulation*. **121** (8): 997–1004. [doi](/source/Doi_(identifier)):[10.1161/CIRCULATIONAHA.109.904557](https://doi.org/10.1161%2FCIRCULATIONAHA.109.904557). [PMC](/source/PMC_(identifier)) [2857348](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2857348). [PMID](/source/PMID_(identifier)) [20159828](https://pubmed.ncbi.nlm.nih.gov/20159828).

1. **[^](#cite_ref-33)** 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](/source/Doi_(identifier)):[10.1152/ajpheart.00062.2006](https://doi.org/10.1152%2Fajpheart.00062.2006). [PMID](/source/PMID_(identifier)) [16501026](https://pubmed.ncbi.nlm.nih.gov/16501026). [S2CID](/source/S2CID_(identifier)) [7073263](https://api.semanticscholar.org/CorpusID:7073263).

1. **[^](#cite_ref-34)** Adams J (Apr 2003). "Potential for proteasome inhibition in the treatment of cancer". *Drug Discovery Today*. **8** (7): 307–15. [doi](/source/Doi_(identifier)):[10.1016/s1359-6446(03)02647-3](https://doi.org/10.1016%2Fs1359-6446%2803%2902647-3). [PMID](/source/PMID_(identifier)) [12654543](https://pubmed.ncbi.nlm.nih.gov/12654543).

1. **[^](#cite_ref-35)** Ben-Neriah Y (Jan 2002). "Regulatory functions of ubiquitination in the immune system". *Nature Immunology*. **3** (1): 20–6. [doi](/source/Doi_(identifier)):[10.1038/ni0102-20](https://doi.org/10.1038%2Fni0102-20). [PMID](/source/PMID_(identifier)) [11753406](https://pubmed.ncbi.nlm.nih.gov/11753406). [S2CID](/source/S2CID_(identifier)) [26973319](https://api.semanticscholar.org/CorpusID:26973319).

1. **[^](#cite_ref-36)** 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](/source/PMID_(identifier)) [12375310](https://pubmed.ncbi.nlm.nih.gov/12375310).

1. **[^](#cite_ref-37)** Basler M, Lauer C, Beck U, Groettrup M (Nov 2009). ["The proteasome inhibitor bortezomib enhances the susceptibility to viral infection"](https://doi.org/10.4049%2Fjimmunol.0901596). *Journal of Immunology*. **183** (10): 6145–50. [doi](/source/Doi_(identifier)):[10.4049/jimmunol.0901596](https://doi.org/10.4049%2Fjimmunol.0901596). [PMID](/source/PMID_(identifier)) [19841190](https://pubmed.ncbi.nlm.nih.gov/19841190).

1. **[^](#cite_ref-38)** Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL (Sep 1994). "Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules". *Cell*. **78** (5): 761–71. [doi](/source/Doi_(identifier)):[10.1016/s0092-8674(94)90462-6](https://doi.org/10.1016%2Fs0092-8674%2894%2990462-6). [PMID](/source/PMID_(identifier)) [8087844](https://pubmed.ncbi.nlm.nih.gov/8087844). [S2CID](/source/S2CID_(identifier)) [22262916](https://api.semanticscholar.org/CorpusID:22262916).

1. **[^](#cite_ref-39)** Silva MM, Gil LH, Marques ET, Calzavara-Silva CE (Sep 2013). ["Potential biomarkers for the clinical prognosis of severe dengue"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3970693). *Memórias do Instituto Oswaldo Cruz*. **108** (6): 755–62. [doi](/source/Doi_(identifier)):[10.1590/0074-0276108062013012](https://doi.org/10.1590%2F0074-0276108062013012). [PMC](/source/PMC_(identifier)) [3970693](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3970693). [PMID](/source/PMID_(identifier)) [24037198](https://pubmed.ncbi.nlm.nih.gov/24037198).

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## Further reading

- Coux O, Tanaka K, Goldberg AL (1996). "Structure and functions of the 20S and 26S proteasomes". *Annual Review of Biochemistry*. **65**: 801–47. [doi](/source/Doi_(identifier)):[10.1146/annurev.bi.65.070196.004101](https://doi.org/10.1146%2Fannurev.bi.65.070196.004101). [PMID](/source/PMID_(identifier)) [8811196](https://pubmed.ncbi.nlm.nih.gov/8811196).

- Goff SP (Aug 2003). ["Death by deamination: a novel host restriction system for HIV-1"](https://doi.org/10.1016%2FS0092-8674%2803%2900602-0). *Cell*. **114** (3): 281–3. [doi](/source/Doi_(identifier)):[10.1016/S0092-8674(03)00602-0](https://doi.org/10.1016%2FS0092-8674%2803%2900602-0). [PMID](/source/PMID_(identifier)) [12914693](https://pubmed.ncbi.nlm.nih.gov/12914693). [S2CID](/source/S2CID_(identifier)) [16340355](https://api.semanticscholar.org/CorpusID:16340355).

- Früh K, Yang Y, Arnold D, Chambers J, Wu L, Waters JB, Spies T, Peterson PA (Nov 1992). ["Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits"](https://doi.org/10.1016%2FS0021-9258%2818%2941645-6). *The Journal of Biological Chemistry*. **267** (31): 22131–40. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(18)41645-6](https://doi.org/10.1016%2FS0021-9258%2818%2941645-6). [PMID](/source/PMID_(identifier)) [1429565](https://pubmed.ncbi.nlm.nih.gov/1429565).

- Beck S, Kelly A, Radley E, Khurshid F, Alderton RP, Trowsdale J (Nov 1992). "DNA sequence analysis of 66 kb of the human MHC class II region encoding a cluster of genes for antigen processing". *Journal of Molecular Biology*. **228** (2): 433–41. [doi](/source/Doi_(identifier)):[10.1016/0022-2836(92)90832-5](https://doi.org/10.1016%2F0022-2836%2892%2990832-5). [PMID](/source/PMID_(identifier)) [1453454](https://pubmed.ncbi.nlm.nih.gov/1453454).

- Martinez CK, Monaco JJ (Oct 1991). "Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene". *Nature*. **353** (6345): 664–7. [Bibcode](/source/Bibcode_(identifier)):[1991Natur.353..664M](https://ui.adsabs.harvard.edu/abs/1991Natur.353..664M). [doi](/source/Doi_(identifier)):[10.1038/353664a0](https://doi.org/10.1038%2F353664a0). [PMID](/source/PMID_(identifier)) [1681432](https://pubmed.ncbi.nlm.nih.gov/1681432). [S2CID](/source/S2CID_(identifier)) [4251139](https://api.semanticscholar.org/CorpusID:4251139).

- Kristensen P, Johnsen AH, Uerkvitz W, Tanaka K, Hendil KB (Dec 1994). "Human proteasome subunits from 2-dimensional gels identified by partial sequencing". *Biochemical and Biophysical Research Communications*. **205** (3): 1785–9. [doi](/source/Doi_(identifier)):[10.1006/bbrc.1994.2876](https://doi.org/10.1006%2Fbbrc.1994.2876). [PMID](/source/PMID_(identifier)) [7811265](https://pubmed.ncbi.nlm.nih.gov/7811265).

- Singal DP, Ye M, Quadri SA (Jan 1995). ["Major histocompatibility-encoded human proteasome LMP2. Genomic organization and a new form of mRNA"](https://doi.org/10.1074%2Fjbc.270.4.1966). *The Journal of Biological Chemistry*. **270** (4): 1966–70. [doi](/source/Doi_(identifier)):[10.1074/jbc.270.4.1966](https://doi.org/10.1074%2Fjbc.270.4.1966). [PMID](/source/PMID_(identifier)) [7829535](https://pubmed.ncbi.nlm.nih.gov/7829535).

- Beck S, Abdulla S, Alderton RP, Glynne RJ, Gut IG, Hosking LK, Jackson A, Kelly A, Newell WR, Sanseau P, Radley E, Thorpe KL, Trowsdale J (Jan 1996). "Evolutionary dynamics of non-coding sequences within the class II region of the human MHC". *Journal of Molecular Biology*. **255** (1): 1–13. [doi](/source/Doi_(identifier)):[10.1006/jmbi.1996.0001](https://doi.org/10.1006%2Fjmbi.1996.0001). [PMID](/source/PMID_(identifier)) [8568858](https://pubmed.ncbi.nlm.nih.gov/8568858).

- Hisamatsu H, Shimbara N, Saito Y, Kristensen P, Hendil KB, Fujiwara T, Takahashi E, Tanahashi N, Tamura T, Ichihara A, Tanaka K (Apr 1996). ["Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2192534). *The Journal of Experimental Medicine*. **183** (4): 1807–16. [doi](/source/Doi_(identifier)):[10.1084/jem.183.4.1807](https://doi.org/10.1084%2Fjem.183.4.1807). [PMC](/source/PMC_(identifier)) [2192534](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2192534). [PMID](/source/PMID_(identifier)) [8666937](https://pubmed.ncbi.nlm.nih.gov/8666937).

- Schmidtke G, Kraft R, Kostka S, Henklein P, Frömmel C, Löwe J, Huber R, Kloetzel PM, Schmidt M (Dec 1996). ["Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC452515). *The EMBO Journal*. **15** (24): 6887–98. [doi](/source/Doi_(identifier)):[10.1002/j.1460-2075.1996.tb01081.x](https://doi.org/10.1002%2Fj.1460-2075.1996.tb01081.x). [PMC](/source/PMC_(identifier)) [452515](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC452515). [PMID](/source/PMID_(identifier)) [9003765](https://pubmed.ncbi.nlm.nih.gov/9003765).

- Seeger M, Ferrell K, Frank R, Dubiel W (Mar 1997). ["HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation"](https://doi.org/10.1074%2Fjbc.272.13.8145). *The Journal of Biological Chemistry*. **272** (13): 8145–8. [doi](/source/Doi_(identifier)):[10.1074/jbc.272.13.8145](https://doi.org/10.1074%2Fjbc.272.13.8145). [PMID](/source/PMID_(identifier)) [9079628](https://pubmed.ncbi.nlm.nih.gov/9079628).

- Cruz M, Elenich LA, Smolarek TA, Menon AG, Monaco JJ (Nov 1997). "DNA sequence, chromosomal localization, and tissue expression of the mouse proteasome subunit lmp10 (Psmb10) gene". *Genomics*. **45** (3): 618–22. [doi](/source/Doi_(identifier)):[10.1006/geno.1997.4977](https://doi.org/10.1006%2Fgeno.1997.4977). [PMID](/source/PMID_(identifier)) [9367687](https://pubmed.ncbi.nlm.nih.gov/9367687).

- Madani N, Kabat D (Dec 1998). ["An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110608). *Journal of Virology*. **72** (12): 10251–5. [doi](/source/Doi_(identifier)):[10.1128/JVI.72.12.10251-10255.1998](https://doi.org/10.1128%2FJVI.72.12.10251-10255.1998). [PMC](/source/PMC_(identifier)) [110608](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110608). [PMID](/source/PMID_(identifier)) [9811770](https://pubmed.ncbi.nlm.nih.gov/9811770).

- Simon JH, Gaddis NC, Fouchier RA, Malim MH (Dec 1998). "Evidence for a newly discovered cellular anti-HIV-1 phenotype". *Nature Medicine*. **4** (12): 1397–400. [doi](/source/Doi_(identifier)):[10.1038/3987](https://doi.org/10.1038%2F3987). [PMID](/source/PMID_(identifier)) [9846577](https://pubmed.ncbi.nlm.nih.gov/9846577). [S2CID](/source/S2CID_(identifier)) [25235070](https://api.semanticscholar.org/CorpusID:25235070).

- Schmidt M, Zantopf D, Kraft R, Kostka S, Preissner R, Kloetzel PM (Apr 1999). "Sequence information within proteasomal prosequences mediates efficient integration of beta-subunits into the 20 S proteasome complex". *Journal of Molecular Biology*. **288** (1): 117–28. [doi](/source/Doi_(identifier)):[10.1006/jmbi.1999.2660](https://doi.org/10.1006%2Fjmbi.1999.2660). [PMID](/source/PMID_(identifier)) [10329130](https://pubmed.ncbi.nlm.nih.gov/10329130).

- Elenich LA, Nandi D, Kent AE, McCluskey TS, Cruz M, Iyer MN, Woodward EC, Conn CW, Ochoa AL, Ginsburg DB, Monaco JJ (Sep 1999). "The complete primary structure of mouse 20S proteasomes". *Immunogenetics*. **49** (10): 835–42. [doi](/source/Doi_(identifier)):[10.1007/s002510050562](https://doi.org/10.1007%2Fs002510050562). [PMID](/source/PMID_(identifier)) [10436176](https://pubmed.ncbi.nlm.nih.gov/10436176). [S2CID](/source/S2CID_(identifier)) [20977116](https://api.semanticscholar.org/CorpusID:20977116).

- Mulder LC, Muesing MA (Sep 2000). ["Degradation of HIV-1 integrase by the N-end rule pathway"](https://doi.org/10.1074%2Fjbc.M004670200). *The Journal of Biological Chemistry*. **275** (38): 29749–53. [doi](/source/Doi_(identifier)):[10.1074/jbc.M004670200](https://doi.org/10.1074%2Fjbc.M004670200). [PMID](/source/PMID_(identifier)) [10893419](https://pubmed.ncbi.nlm.nih.gov/10893419).

v t e Proteasome endopeptidase complex subunits (EC 3.4.25.1) A (alpha subunits) PSMA1 PSMA2 PSMA3 PSMA4 PSMA5 PSMA6 PSMA7 PSMA8 B (beta subunits) PSMB1 PSMB2 PSMB3 PSMB4 PSMB5 PSMB6 PSMB7 PSMB8 PSMB9 PSMB10 C (ATPases) PSMC1 PSMC2 PSMC3 PSMC4 PSMC5 PSMC6 D (non-ATPases) PSMD1 PSMD2 PSMD3 PSMD4 PSMD5 PSMD6 PSMD7 PSMD8 PSMD9 PSMD10 PSMD11 PSMD12 PSMD13 PSMD14 E (activator subunits) PSME1 PSME2 PSME3 PSME4 F (inhibitor subunit) PSMF1

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Adapted from the Wikipedia article [PSMB9](https://en.wikipedia.org/wiki/PSMB9) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/PSMB9?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.