Publication for PSMB8 and PSMB10

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	PSMB8	proteasome 20S subunit beta 8	5696			[link]
hsa	PSMB10	proteasome 20S subunit beta 10	5699

Pubmed ID	Priority	Text
26344735	0.98	MECL-1 (beta2i), and LMP7 (beta5i), respectively.
	0.97	LMP7 and MECL-1 immunoproteasome subunits have reduced cell survival under conditions of oxidative stress and ER stress (Figure 10).
	0.95	LMP7 and MECL-1 (L7M1) immunoproteasome subunits.
	0.92	MECL-1, LMP7) catalytic subunits, or a mixture of both types of catalytic subunits.
25329802	0.98	LMP7 possess chymotrypsin-like (ChTL) activity, subunits Y and LMP2 possess caspase-like activity, and subunits Z and MECL1- trypsin-like activity.
	0.97	LMP7(beta5i), LMP2(beta1i), and LMP10(MECL1, beta2i) instead of constitutive protease subunits X(beta5), Y(beta1), and Z(beta2) of constitutive proteasomes.
	0.96	MECL1 is known to be integrated into assembling proteasomes jointly with subunit LMP2 but independently from subunit LMP7.
26474164	0.98	PSMB8, PSMB9, and PSMB10 have been found to be induced by interferon-gamma as secondary-responsive IFNgamma-inducible genes.
	0.94	PSMB8, PSMB9, and PSMB10 are all components of the immunoproteasome that replace the constitutive catalytic proteasome subunits beta1, beta2, and beta5 upon treatment with interferon-gamma.
	0.92	PSMB8, PSMB10) have greater fold changes that range from 3.5- to >76,000-fold increases in DBA patients relative to healthy donors.
20812720	0.98	MECL1/beta2i, and LMP7/beta5i, which replace the constitutive proteasome counterparts Y/beta1, Z/beta2, and X/beta5, respectively, to create the immunoproteasome.
	0.96	MECL1/beta2i and LMP7/beta5i.
26885372	0.98	PSMB8, PSMB9, PSMB10, and thymus restricted subunit PSMB11
	0.95	PSMB8 [Swiss-Prot:P28062], PSMB9 [Swiss-Prot:P28065], PSMB10 [Swiss-Prot:P40306]) in our database of 55 melanoma cell lines by gene expression array analysis (Fig. 1).
26876939	0.98	beta2i (MECL1) and beta5i (LMP7) - that replace the c-proteasomal beta1, beta2 and beta5 to form immunoproteasomes (i-proteasomes, the term used here for any type of proteasomes that contains at least one of the three i-proteasome-specific beta (ibeta) subunits).
23932981	0.97	LMP7 and MECL-1 was observed after 4 and 12 h following stimulation.
	0.96	LMP7 and MECL-1 beta subunits forming the immunoproteasome and enhancing antigen presentation to MHC class I molecules.
	0.91	LMP7 and MECL-1 have experienced different evolutionary pressures leading to complex phylogenetic relationships with the rest of the vertebrate immunoproteasome subunits.
	0.91	LMP7 and MECL-1 expression in both lung and kidney cells indicating an important role of these molecules in immune response against viral infections in lungfish and shedding light on the evolution of lung immunity.
	0.86	LMP7 and MECL-1 in a sarcopterygian fish, the Nigerian spotted lungfish (Protopterus dolloi)
	0.85	LMP7 and MECL-1 expression in both tissues.
	0.83	LMP7) and 4 times lower (MECL-1) than those found in the kidney.
	0.78	MECL-1 or PSMB10) and beta5i (LMP7 or PSMB8) are constitutively expressed in a number of hematopoietic cells (such as dendritic cells (DCs) and monocyte-derived cells) and are induced in other cell types after exposure to type I interferon.
	0.78	LMP7 and MECL-1 were constitutively expressed in all the tissues examined with the highest expression found in the kidney and post-pyloric spleen.
	0.65	LMP7 and MECL-1 genes at 4 and 12 h following stimulation indicating that the fish was able to mount an immune response against viral infection.
	0.65	LMP7 lungfish (KF241954), human (CAA47026), Xenopus (NP_001084323), trout (BAD89554), zebrafish (AAB87679), coelacanth (ENSLACG00000014047) and shark (BAA10933); MECL-1 lungfish (KF241955), human (CAG33263), Xenopus (NP_001079861), trout (ADM95869), zebrafish (AAI65548), coelacanth (ENSLACG00000013849) and shark (DR783428).
	0.60	MECL-1, differentially from LMP2 and LMP7, closely clusters with the coelacanth MECL-1 sequence and groups with shark and tetrapod sequences whilst teleost MECL-1 form a different group.
	0.55	LMP7 and MECL-1 display different levels of divergence when compared to their corresponding vertebrate sequences.
	0.54	LMP7 and MECL-1 sequences, a multiple alignment was performed (Fig 2) showing the presence of a conserved proteasome beta type domain in each sequence (beta type 6, 5 and 7 respectively) and a signal peptide.
10662796	0.97	LMP7, encoded in the MHC class II region, and MECL-1 (multicatalytic endopeptidase complex-like 1; for review see references 8 and 9).
	0.97	MECL-1 active site subunits, as the presence of the constitutive subunits in these positions results in a relatively poor antigenic peptide liberation (compare T2 LMP7 and T2 LMP2[/MECL-1]+7 in Table ).
	0.96	MECL-1 and LMP7 had only minor effects on the generation of the antigenic peptide, the concerted presence of LMP2, MECL-1, and LMP7 dramatically enhanced the production of the relevant peptides.
	0.86	LMP7, and MECL-1 are constitutively highly expressed in many cells of lymphoid origin, probably including APCs.
	0.78	LMP7, and MECL-1 (multicatalytic endopeptidase complex-like 1), leading to the formation of immunoproteasomes.
	0.74	MECL-1 or LMP7 alone was sufficient to induce the production of small amounts of antigenic peptide.
	0.73	MECL-1 and also, to a lesser extent, LMP7 incorporate interdependently into proteasomes 34 37 48.
	0.63	LMP7, and MECL-1 with proteasomes changes the cleavage site specificity and enhances the frequency of cleavages, leading to efficient production of HBcAg141-151 CTL epitopes.
	0.56	LMP7 influences the structural features of 20S proteasomes, thereby enhancing the activity of the LMP2 and MECL-1 catalytic sites, which provide cleavage specificity.
25749172	0.97	LMP10 expression were stained by immunohistochemistry for TAP1, TAP2, LMP2, and LMP7.
	0.96	LMP7, their potential interrelationships, as well as possible association to HLA class I and LMP10 expression, using previously obtained data on HLA class I and LMP10 expression in TSCC and BOTSCC.
	0.95	LMP7, and LMP10 are subunits of the immunoproteasome, responsible for the processing of proteins to peptides, while TAP1 and TAP2 transport peptides from the cytoplasm to the endoplasmic reticulum.
	0.93	LMP7, LMP10, TAP1, and TAP2, affecting the formation of peptide presenting HLA-b2m complexes, seemed of importance.
	0.87	LMP7, and LMP10 also play a role with regard to cell survival and proliferation and protect cells against oxidative damage.
	0.79	LMP7 expression, similar to HLA class I and LMP10, was common in TSCC and BOTSCC, irrespective of HPV status.
27833096	0.97	beta2i/MECL-1 and beta5i/LMP7 in non-infected cells but did not alter the standard proteasome subunit beta5 expression and abundance of the non-replaceable subunit alpha4 (Figure 1b).
	0.87	beta2i/MECL-1 and beta5i/LMP7), standard proteasome subunits (alpha4 and beta5), the HCV core and tubulin.
	0.82	beta2i/MECL-1 and beta5i/LMP7 (Figure 5d).
	0.81	beta2i/MECL-1 and beta5i/LMP7) and standard proteasome subunits (alpha4 and beta5) (d).
	0.73	beta2i/MECL-1 and beta5i/LMP7 did not differ between the uninfected cells and HCV-infected cells (Figure 4b).
	0.73	beta2i/MECL-1 and beta5i/LMP7), standard proteasome subunits (alpha4 and beta5), the HCV core and tubulin (b).
25098831	0.97	proteasome subunit beta type 8-PSMB8, proteasome subunit beta type 9-PSMB9 and proteasome subunit beta type 10-PSMB10 respectively, leading to the formation of the so-called immunoproteasome.
	0.95	PSMB8/PSMB5, PSMB9/PSMB6 and PSMB10/PSMB7) in IM [1.79, 0.35 and 0.42, respectively] compared to non-inflammatory biopsies [0.94, 0.1 and 0.18, respectively] indicate an imbalance and suggest substitution of constitutive by immunoproteasomal subunits in patients with IIM.
	0.92	PSMB8, PSMB9 and/or PSMB10 in all investigated cellular subsets except CD4+ (figure 1).
	0.50	PSMB8 [0.302+-0.139 and 0.075+-0.041] and about 5-fold increase for PSMB9 [0.049+-0.029 and 0.009+-0.002] but less than 2-fold for PSMB10 [0.065+-0.064 and 0.036+-0.022].
22037302	0.97	LMP7, and LMP10 are interchanged with the three components of the 20S catalytic core to form the immunoproteasome in the instance of IFN-gamma induction.
	0.95	LMP7, and LMP10 can lead to a decrease in MHC class I-restricted peptide presentation, and cause an escape from immune surveillance, leading to cancer.
	0.76	LMP7, and LMP10 yields more types of peptides expressed on the cell surface.
28438776	0.97	Psmb8, Psmb9 nor Psmb10 suggests that IL-1beta upregulates Egr1, also known as Zif268 (zinc finger protein 225) or NGFI-A (nerve growth factor-induced protein A), which are known to suppress the response of the Psmb9 promoter to NFkappaB. Indeed, Egr1 is highly expressed in pancreatic islets and beta cells (2016) and upregulated after 4-8 h by cytokines in INS-1E cells in an NO independent manner, suggesting that the cGMP/cAMP -PKA/G-CREB pathways are not involved in regulating the beta-cell immunoproteasome in contrast to endothelial cells that have a high basal expression of the immunoproteasome.
	0.93	PSMB8, PSMB9 and PSMB10 was examined in human islets exposed to a) a combination of IL-1beta and IFNgamma (black bars) or b) only IL-1beta (grey bars) or IFNgamma (black bars).
	0.88	Psmb10/MECL-1 and Psmb8/LMP7, respectively).
29240645	0.97	LMP7, LMP2 and LMP10 catalytic proteasome subunits, which are encoded by PSMB8, PSMB9 and PSMB10 genes, respectively.
	0.95	LMP7 (beta5i), LMP2 (beta1i) and LMP10 (beta2i) after priming with pro-inflammatory cytokines, or LPS with an increase in CT-like and T-like activities.
	0.95	LMP7, LMP2 and LMP10 subunits, for example PR-924 and ONX-0914 are LMP7-selective, while carfilzomib and oprozomib actively inhibit both X and LMP7 subunits.
29182146	0.97	MECL-1 (ibeta2), and LMP7 (ibeta5) - that share respectively 62%, 59%, and 71% sequence identity with their cP counterparts.
	0.86	LMP7) and trypsin-like subunits (beta2 and MECL-1) cleave many more peptide bonds than the beta1 and LMP2 subunits of the cP and iP, respectively.
30761219	0.97	MECL-1 (multicatalytic endopeptidase complex-like-1, beta2i), and LMP7 (beta5i).
	0.82	LMP7 and MECL-1 immuno-subunits display essentially the same cleavage specificity as their constitutive counterparts, but LMP2 shows more chymotrypsin-like activity than the caspase-like activity of beta1.
11854353	0.97	beta2i (MECL1), and beta5i (LMP7).
19443843	0.97	MECL1 and LMP7 deficient T cells suggests that T cell proliferation is also affected by immunoproteasome activity.
20888811	0.97	LMP7 (Fig 3D) and MECL-1 (Fig 3E).
21887316	0.97	beta2i/MECL-1-/- beta5i/LMP7-/- and RAG1-/- mice to define their maturation status.
22134332	0.97	LMP-7, LMP-10, MB-1, Delta, and Z. Lysates of the cultured human esophageal cancer cell lines (TE2, 4, 5, 6, 8, 9, 10, 13, 14, HEC46, and SGF7) and homogenized normal human esophageal mucosa tissue (NHET) were subjected to Western blot analysis.
21400024	0.96	beta2i (LMP7) and beta 5i (MECL1, LMP10), which results in proteasomes with higher chymotrypsin-like activity.
	0.88	LMP10 (left), LMP2 (center) and LMP7 (right).
	0.86	LMP10, and LMP7) in K562 cells.
	0.66	LMP10, and LMP7.
	0.57	LMP10) and later induction of LMP7 in K562 cells after 1-5 days (D1-D5) of treatment with interferon-gamma.
27648699	0.96	LMP10, but did not express LMP7 proteasome subunits (Figure 1A, lane 1).
	0.89	LMP7 (Figure 1B) and, in fact, contained proteasomes with immuno-subunits LMP2, LMP7 and LMP10, but no detectable X, Y, or Z subunits.
	0.85	LMP7, LMP2, and LMP10 subunits after 4h and 24h of second LPS tolerance treatment in PMA-treated THP-1 cells.
	0.61	LMP7, but not LMP10, X, Y, and Z (Figure 1C).
22216088	0.96	MECL1 levels and a reduction in the expression of beta5 and LMP7, though the levels of these subunits remained elevated as compared to parental cells.
	0.94	LMP7, LMP2, and MECL1) as analyzed by western blotting and quantitatively confirmed by ProCISE, an active site probe-based proteasome subunit ELISA (Figure 1B-C).
	0.82	LMP7 and MECL1, as beta1 is capable of forming hybrid proteasomes with immunoproteasome subunits.
23386784	0.96	beta2i (MECL1), and beta5i (LMP7), are expressed in response to the exposure to proinflammatory signals, such as cytokines, in particular, interferon gamma.
	0.95	LMP7) as well as dose-dependent inhibition of MECL1 and LMP2.
	0.92	LMP7, MECL1, and LMP2).
27071340	0.96	LMP7 and MECL1 were assessed.
	0.95	LMP7 occupancy, regardless of whether carfilzomib was administered as a 2- to 10-min infusion or as a 30-min infusion, while a dose-dependent increase in MECL1 and LMP2 occupancy was observed at doses of up to 45 mg/m2 (Figure S3).
	0.94	LMP7, MECL1 and LMP2 was increased by 7 9%, 23 1% and 33 6%, respectively, relative to patients receiving 15 or 20 mg/m2 (see Fig 3A and B; P < 0 05, P <0 001 and P < 0 01, respectively).
27264839	0.96	LMP7 and LMP10), respectively.
	0.81	LMP7, LMP10, TAP1, TAP2, Tapasin, Calreticulin, Calnexin, ERp57, beta2-microglobulin) and HLA class I loci (HLA-A, HLA-B and HLA-C).
	0.52	LMP7; PSMB10, LMP10.
17145306	0.96	LMP7 and MECL1 subunits and downregulating the LMP2 subunit, leading to an increased presentation of cryptic and subdominant CTL epitopes.
	0.83	LMP7, and MECL1 are incorporated into nascent proteasomes, replacing their endogenous counterparts and constituting the so-called immunoproteasome.
28051153	0.96	PSMB8, PSMB9 and PSMB10), proteasome activators PSME1 and PSME2 and transporter genes TAP1 and TAP2 across cancer cells, and eight datasets representing breast cancer tumour tissue's.
	0.92	PSMB8 and PSMB10 were increased (Fig. 8C-E) consistent with a role for retinoid-related signalling in IP induction.
29451304	0.96	PSMB8, PSMB9, PSMB10 and PSMB2).
	0.65	PSMB 8, PSMB 2, PSMB 9 and PSMB 10.
20919990	0.96	Mecl-1), and beta5i (or Lmp7).
21748441	0.96	beta2i (MECL-1), and beta5i (LMP7), in place of beta1, beta2, and beta5 subunits, respectively.
22349260	0.96	MECL1 and LMP7, as indicated.
24712303	0.96	beta2i (MECL-1) and beta5i (LMP7; Fig.1).
25412285	0.96	MECL-1 (beta2i) and LMP7 (beta5i), are expressed and incorporated into the proteasome in place of their constitutive counterparts, beta1, beta2 and beta5, to form another particle called the immunoproteasome (Figure 1A).
28763764	0.96	PSMB10, LMP10, or MECL-1, for "multicatalytic endopeptidase complex-like 1"), and ibeta5 (PSMB8 or LMP7).
32119722	0.96	beta2i (LMP10) and beta5i (LMP7) the so-called immune subunits, respectively.
21256843	0.95	LMP7, MECL-1 or PA28beta.
	0.88	MECL-1, LMP2 and LMP7.
	0.77	LMP7, and MECL-1 occurred in the non-neoplastic part of a liver removed for hepatocellular carcinoma (Fig 3).
	0.75	LMP7 and MECL-1 cause the formation of the immunoproteasome, and consequently decrease the 26S proteasome activity.
	0.75	LMP7 and MECL-1 (Fig 7).
	0.65	LMP7 and MECL-1 were also found around the mitochondria.
14970191	0.95	LMP7, PSMB10, PSME1, and PSME2, which are up-regulated by IFNgamma, and the PSMB7, COL1A1, and LMNA genes, which are down-regulated by IFNgamma.
25889583	0.95	PSMB8, LMP7), beta1i (PSMB9, LMP2) and beta2i (PSMB10, MECL1) and to assemble immunoproteasomes, along with PA28 as regulatory cap (Figure 2B).
29321020	0.95	PSMB8, PSMB9 and PSMB10), and Intravenous Immunoglobulin (IVIg), which targets three DEGs (C5, FCGR2A and FCGR3A) as either a receptor binder or antagonist.
29587858	0.95	PSMB8 (LMP7), PSMB9 (LMP2), PSMB10 (LMP10).
19756593	0.94	LMP7, LMP10, HLA class I heavy chain, tapasin, TAP1, TAP2 and ERp57) and MHC class I-related antigen (MICA).
	0.91	LMP7 and LMP10 than low-stage UC.
	0.90	LMP7 and LMP10, were found in high-stage carcinomas when compared with low-stage tumors.
	0.87	LMP7 and LMP10 has been reported in malignant melanoma, and carcinomas of breast, colorectum, cervix and kidney.
	0.74	LMP7 and LMP10, the TAP subunits TAP1 and TAP2, and tapasin.
	0.64	LMP7 and LMP10 than the deeper urothelial layer.
	0.63	LMP7 and LMP10]; the latter is induced by the action of inflammatory cytokines such as interferon-gamma and TNF-alpha.
30675634	0.94	PSMB8, PSMB9 and PSMB10 arose from PSMB6, PSMB5 and PSMB7, respectively, not by individual duplications, but by 2R-GWD (Fig. 3).
	0.59	beta2i (also known as MECL1, PSMB10) and beta5i (also known as LMP7, PSMB8) subunits instead of beta1, beta2 and beta5 subunits, respectively, have distinct cleavage specificities and produce peptides with C-terminal hydrophobic residues that fit well in the groove of MHC class I molecules more efficiently than standard 20S proteasomes.
28677774	0.94	PSMB8 mutants can be expected, as beta5i is required for the maturation of immunoproteasomes by processing and incorporation of the beta1i and beta2i subunits.
31236277	0.94	beta2i (MECL-1), and beta5i (LMP7) instead of the constitutive counterparts in the core particle to form the immunoproteasome.3, 4, 5 In particular monocytes and lymphocytes have been shown to contain immunoproteasome proteins.6, 7, 8 It is believed that cells upregulate immunoproteasomes to maintain protein homeostasis to cope with cellular stress thereby altering antigen processing for the generation of major histocompatibility (MHC) class I-restricted epitopes.9, 10
21114484	0.93	LMP7 (beta5i), LMP2 (beta1i) and MECL1 (beta2i), which are thought to play a role in presentation of antigens on major histocompatability complex 1.
24590311	0.93	LMP7 (12-25.3%) relative to MECL1 (2.2-15.2%) and LMP2 (1.2-18.6%).
29259686	0.93	beta2i (coded by PSMB10), and beta5i (coded by PSMB8) subunits instead of the beta1, beta2, and beta5 subunits of the standard proteasome, respectively.
25127410	0.92	PSMB10/beta2i and PSMB8/beta5i in the 20S chamber (Figure 1B, blue-colored subunits) alters peptidase activities, thus resulting in a higher efficiency in the generation of selected major histocompatibility complex class I epitopes.
26527367	0.92	beta2i/MECL (Multicatalytic Endopeptidase Complex-Like)-1, beta5i/LMP7, the regulatory cap PA28 and ERAP (ER-associated AminoPeptidase-associated with antigen Processing) amongst others especially within immune cells in healthy individuals.
27260006	0.92	Proteasome subunit beta type-8 (PSMB8) gene, that encodes for the beta5i subunit of the proteasome; beta5i is one of the three catalytic subunits (together with beta1i and beta2i) that are isoforms constitutionally expressed in the hematopoietic lineages and induced in non-hematopoietic cells by inflammatory cytokines such as IFN-gamma.
29510614	0.92	LMP10 (PSMB10)/beta2i, and LMP7 (PSMB8)/beta5i, respectively, to form the immunoproteasome (IP).
26636107	0.91	LMP7 has been associated with human disease, although no association has been found with the other immunoproteasome subunits (LMP2, LMP10, PA28alpha, and PA28beta).
9584142	0.90	LMP7 (ibeta5), and Z (beta2) by MECL-1 (ibeta2) results in changes of the hydrolytic activities as monitored with short fluorogenic peptide substrates.
31119134	0.89	beta2i (MECL-1), and beta5i (LMP7), which correspond to beta1, beta2, and beta5, respectively.
29930882	0.88	MECL-1 coimmunoprecipitated with proteasomes in GEM-treated cells, LMP7 was also present in this fraction.
30657666	0.88	beta2i (MECL-1), and beta5i (LMP7), yielding the so-called immunoproteasome particles (iCPs) that preferentially generate antigenic peptides with high affinity for major histocompatibility complex (MHC) class I receptors.
21804012	0.85	LMP7&beta2i/MECL-1-deficient (ko) recipients were reconstituted with T cell-depleted BM cells of beta5i/LMP7&beta2i/MECL-1-deficient donor mice (A, C) or with BM of either wt or ko donor mice as indicated (B).
22363101	0.82	LMP 7 by western blot and of MECL-1 by 2-D gelelectrophoresis it remains unclear whether it is pure immunoproteasome and/or intermediate-type proteasomes that are found in the extracellular alveolar space of ARDS patients.
	0.55	beta 2i (MECL-1), and beta 5i (LMP7) that are incorporated into a newly synthesized intermediate type and/or immunoproteasome.
29606130	0.79	LMP7 (24%), LMP2 (44%), and LMP10 (37%; P < 0.001) decreased significantly as shown in Fig. 8c, d. These data suggest that expression of proteasome LMP subunits and TNF-alpha were significantly down regulated after delta-tocotrienol treatment.
	0.72	LMP7, LMP2, LMP10 (24% - 44%) decreased significantly after delta-tocotrienol treatment.
	0.66	LMP7, LMP2, LMP10), ICAM-1, VCAM-1, and TNF-alpha using total RNAs derived from plasmas of hepatitis C patients was investigated.
22677907	0.77	MECL1/beta2i and LMP7/beta5i in non-haematopoietic cells, which replace their constitutive proteasome counterparts Y/beta1, Z/beta2 and X/beta5, respectively, to form the immunoproteasome.
19065646	0.73	LMP7, and MECL1) both at immature and mature stages.
22970293	0.72	LMP7 and MECL-1 (Figure 4B) indicating the switching over from constitutive proteasome to immunoproteasome.
28381880	0.69	LMP7, beta2: PSMB6 and LMP10, beta1: PSMB7 and LMP2).
17622526	0.67	LMP7 and LMP10 subunits); and transported from the cytoplasm to the endoplasmic reticulum by TAP (transporter associated with antigen presentation) which is composed of TAP1 and TAP2 subunits.
27659694	0.66	PSMB8, PSMB9 and PSMB10.
27098648	0.54	LMP7, and eventually the multicatalytic endopeptidase complex 1 (MECL-1) genes, were discovered and identified as interferon-gamma inducible subunits that are incorporated into a specialized form of the 20S Proteasome called the Immunoproteasome.