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Proteasome subunit beta type-8 (EC 3.4.25.1) (Low molecular mass protein 7) (Macropain subunit C13) (Multicatalytic endopeptidase complex subunit C13) (Proteasome component C13) (Proteasome subunit beta-5i) (Really interesting new gene 10 protein)

 PSB8_HUMAN              Reviewed;         276 AA.
P28062; B0UZC0; Q29824; Q5JNW6; Q5QNR8; Q96J48;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
31-MAY-2011, sequence version 3.
22-NOV-2017, entry version 203.
RecName: Full=Proteasome subunit beta type-8;
EC=3.4.25.1;
AltName: Full=Low molecular mass protein 7;
AltName: Full=Macropain subunit C13;
AltName: Full=Multicatalytic endopeptidase complex subunit C13;
AltName: Full=Proteasome component C13;
AltName: Full=Proteasome subunit beta-5i;
AltName: Full=Really interesting new gene 10 protein;
Flags: Precursor;
Name=PSMB8; Synonyms=LMP7, PSMB5i, RING10, Y2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8458375; DOI=10.1002/eji.1830230414;
Glynne R., Kerr L.A., Mockridge I., Beck S., Kelly A., Trowsdale J.;
"The major histocompatibility complex-encoded proteasome component
LMP7: alternative first exons and post-translational processing.";
Eur. J. Immunol. 23:860-866(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1453454; DOI=10.1016/0022-2836(92)90832-5;
Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P.,
Trowsdale J.;
"DNA sequence analysis of 66 kb of the human MHC class II region
encoding a cluster of genes for antigen processing.";
J. Mol. Biol. 228:433-441(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1922342; DOI=10.1038/353357a0;
Glynne R., Powis S.H., Beck S., Kelly A., Kerr L.A., Trowsdale J.;
"A proteasome-related gene between the two ABC transporter loci in the
class II region of the human MHC.";
Nature 353:357-360(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1429565;
Fruh K., Yang Y., Arnold D., Chambers J., Wu L., Waters J.B.,
Spies T., Peterson P.A.;
"Alternative exon usage and processing of the major histocompatibility
complex-encoded proteasome subunits.";
J. Biol. Chem. 267:22131-22140(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8344725; DOI=10.1007/BF00210482;
Meinhardt T., Graf U., Hammerling G.J.;
"Different genomic structure of mouse and human Lmp7 genes:
characterization of MHC-encoded proteasome genes.";
Immunogenetics 38:373-379(1993).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8568858; DOI=10.1006/jmbi.1996.0001;
Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G.,
Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P.,
Radley E., Thorpe K.L., Trowsdale J.;
"Evolutionary dynamics of non-coding sequences within the class II
region of the human MHC.";
J. Mol. Biol. 255:1-13(1996).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE LMP7C), AND VARIANT LYS-49.
Maksymowych W.P.;
"Sequence analysis of the HLA-linked LMP7 gene.";
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-269.
TISSUE=Blood;
PubMed=9157092; DOI=10.1016/0198-8859(95)00172-7;
Kim T.G., Lee Y.H., Choi H.B., Han H.;
"Two newly discovered alleles of major histocompatibility complex-
encoded LMP7 in Korean populations.";
Hum. Immunol. 46:61-64(1996).
[12]
FUNCTION.
PubMed=8163024; DOI=10.1016/0014-5793(94)80612-8;
Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M.,
Kristensen P., Hendil K.B., Tanaka K., Ichihara A.;
"Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced
by interferon-gamma for acquirement of the functional diversity
responsible for antigen processing.";
FEBS Lett. 343:85-88(1994).
[13]
INDUCTION.
PubMed=8663318; DOI=10.1074/jbc.271.29.17275;
Gaczynska M., Goldberg A.L., Tanaka K., Hendil K.B., Rock K.L.;
"Proteasome subunits X and Y alter peptidase activities in opposite
ways to the interferon-gamma-induced subunits LMP2 and LMP7.";
J. Biol. Chem. 271:17275-17280(1996).
[14]
INDUCTION BY TNF AND IFNG.
PubMed=11493458; DOI=10.1182/blood.V98.4.1108;
Hallermalm K., Seki K., Wei C., Castelli C., Rivoltini L.,
Kiessling R., Levitskaya J.;
"Tumor necrosis factor-alpha induces coordinated changes in major
histocompatibility class I presentation pathway, resulting in
increased stability of class I complexes at the cell surface.";
Blood 98:1108-1115(2001).
[15]
DEVELOPMENTAL STAGE.
PubMed=11717192; DOI=10.1093/intimm/13.12.1515;
Li J., Schuler-Thurner B., Schuler G., Huber C., Seliger B.;
"Bipartite regulation of different components of the MHC class I
antigen-processing machinery during dendritic cell maturation.";
Int. Immunol. 13:1515-1523(2001).
[16]
INTERACTION WITH HIV-1 TAT.
PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
Mayer R.J., Krueger E.;
"Human immunodeficiency virus-1 Tat protein interacts with distinct
proteasomal alpha and beta subunits.";
FEBS Lett. 553:200-204(2003).
[17]
INDUCTION BY TETRODOTOXIN.
PubMed=15501285; DOI=10.1016/j.toxicon.2004.07.018;
Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.;
"Potential effects of tetrodotoxin exposure to human glial cells
postulated using microarray approach.";
Toxicon 44:597-608(2004).
[18]
INDUCTION BY IFNG AND IRF1.
PubMed=15907481; DOI=10.1016/j.febslet.2005.04.012;
Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y.,
Tsuchiya K., Okamoto R., Kanai T., Watanabe M.;
"IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted
expression of immunosubunits of the proteasome.";
FEBS Lett. 579:2781-2787(2005).
[19]
INTERACTION WITH TAP1.
PubMed=15488952; DOI=10.1016/j.molimm.2004.07.005;
Begley G.S., Horvath A.R., Taylor J.C., Higgins C.F.;
"Cytoplasmic domains of the transporter associated with antigen
processing and P-glycoprotein interact with subunits of the
proteasome.";
Mol. Immunol. 42:137-141(2005).
[20]
INTERACTION WITH POMP.
PubMed=15944226; DOI=10.1073/pnas.0501711102;
Heink S., Ludwig D., Kloetzel P.-M., Krueger E.;
"IFN-gamma-induced immune adaptation of the proteasome system is an
accelerated and transient response.";
Proc. Natl. Acad. Sci. U.S.A. 102:9241-9246(2005).
[21]
FUNCTION.
PubMed=16423992; DOI=10.1158/0008-5472.CAN-05-2872;
Heink S., Fricke B., Ludwig D., Kloetzel P.M., Krueger E.;
"Tumor cell lines expressing the proteasome subunit isoform LMP7E1
exhibit immunoproteasome deficiency.";
Cancer Res. 66:649-652(2006).
[22]
INDUCTION BY HEAT SHOCK.
PubMed=17142736; DOI=10.4049/jimmunol.177.12.8393;
Callahan M.K., Wohlfert E.A., Menoret A., Srivastava P.K.;
"Heat shock up-regulates lmp2 and lmp7 and enhances presentation of
immunoproteasome-dependent epitopes.";
J. Immunol. 177:8393-8399(2006).
[23]
INDUCTION.
PubMed=17262812; DOI=10.1002/ibd.20110;
Wu F., Dassopoulos T., Cope L., Maitra A., Brant S.R., Harris M.L.,
Bayless T.M., Parmigiani G., Chakravarti S.;
"Genome-wide gene expression differences in Crohn's disease and
ulcerative colitis from endoscopic pinch biopsies: insights into
distinctive pathogenesis.";
Inflamm. Bowel Dis. 13:807-821(2007).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
INDUCTION BY IFNG, AND FUNCTION.
PubMed=19443843; DOI=10.1161/ATVBAHA.109.189407;
Yang Z., Gagarin D., St Laurent G. III, Hammell N., Toma I., Hu C.A.,
Iwasa A., McCaffrey T.A.;
"Cardiovascular inflammation and lesion cell apoptosis: a novel
connection via the interferon-inducible immunoproteasome.";
Arterioscler. Thromb. Vasc. Biol. 29:1213-1219(2009).
[26]
INDUCTION.
PubMed=19619915; DOI=10.1016/j.imbio.2009.06.020;
Eisemann J., Prechtel A.T., Muehl-Zuerbes P., Steinkasserer A.,
Kummer M.;
"Herpes simplex virus type I infection of mature dendritic cells leads
to reduced LMP7-mRNA-expression levels.";
Immunobiology 214:861-867(2009).
[27]
INDUCTION BY PR-957.
PubMed=19525961; DOI=10.1038/nm.1978;
Muchamuel T., Basler M., Aujay M.A., Suzuki E., Kalim K.W., Lauer C.,
Sylvain C., Ring E.R., Shields J., Jiang J., Shwonek P., Parlati F.,
Demo S.D., Bennett M.K., Kirk C.J., Groettrup M.;
"A selective inhibitor of the immunoproteasome subunit LMP7 blocks
cytokine production and attenuates progression of experimental
arthritis.";
Nat. Med. 15:781-787(2009).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
FUNCTION IN ADIPOCYTE DIFFERENTIATION, VARIANT NKJO VAL-201, AND
CHARACTERIZATION OF VARIANT NKJO VAL-201.
PubMed=21881205; DOI=10.1172/JCI58414;
Kitamura A., Maekawa Y., Uehara H., Izumi K., Kawachi I.,
Nishizawa M., Toyoshima Y., Takahashi H., Standley D.M., Tanaka K.,
Hamazaki J., Murata S., Obara K., Toyoshima I., Yasutomo K.;
"A mutation in the immunoproteasome subunit PSMB8 causes
autoinflammation and lipodystrophy in humans.";
J. Clin. Invest. 121:4150-4160(2011).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[32]
VARIANT NKJO MET-75, AND CHARACTERIZATION OF VARIANT NKJO MET-75.
PubMed=21129723; DOI=10.1016/j.ajhg.2010.10.031;
Agarwal A.K., Xing C., DeMartino G.N., Mizrachi D., Hernandez M.D.,
Sousa A.B., Martinez de Villarreal L., dos Santos H.G., Garg A.;
"PSMB8 encoding the beta5i proteasome subunit is mutated in joint
contractures, muscle atrophy, microcytic anemia, and panniculitis-
induced lipodystrophy syndrome.";
Am. J. Hum. Genet. 87:866-872(2010).
[33]
VARIANT NKJO MET-75.
PubMed=21953331; DOI=10.1002/art.33368;
Liu Y., Ramot Y., Torrelo A., Paller A.S., Si N., Babay S., Kim P.W.,
Sheikh A., Lee C.C., Chen Y., Vera A., Zhang X., Goldbach-Mansky R.,
Zlotogorski A.;
"Mutations in proteasome subunit beta type 8 cause chronic atypical
neutrophilic dermatosis with lipodystrophy and elevated temperature
with evidence of genetic and phenotypic heterogeneity.";
Arthritis Rheum. 64:895-907(2012).
[34]
VARIANT NKJO VAL-201, AND CHARACTERIZATION OF VARIANT NKJO VAL-201.
PubMed=21852578; DOI=10.1073/pnas.1106015108;
Arima K., Kinoshita A., Mishima H., Kanazawa N., Kaneko T.,
Mizushima T., Ichinose K., Nakamura H., Tsujino A., Kawakami A.,
Matsunaka M., Kasagi S., Kawano S., Kumagai S., Ohmura K., Mimori T.,
Hirano M., Ueno S., Tanaka K., Tanaka M., Toyoshima I., Sugino H.,
Yamakawa A., Tanaka K., Niikawa N., Furukawa F., Murata S., Eguchi K.,
Ida H., Yoshiura K.;
"Proteasome assembly defect due to a proteasome subunit beta type 8
(PSMB8) mutation causes the autoinflammatory disorder, Nakajo-
Nishimura syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 108:14914-14919(2011).
[35]
VARIANTS NKJO MET-75 AND GLN-105, AND CHARACTERIZATION OF VARIANTS
NKJO MET-75.
PubMed=26524591; DOI=10.1172/JCI81260;
Brehm A., Liu Y., Sheikh A., Marrero B., Omoyinmi E., Zhou Q.,
Montealegre G., Biancotto A., Reinhardt A., Almeida de Jesus A.,
Pelletier M., Tsai W.L., Remmers E.F., Kardava L., Hill S., Kim H.,
Lachmann H.J., Megarbane A., Chae J.J., Brady J., Castillo R.D.,
Brown D., Casano A.V., Gao L., Chapelle D., Huang Y., Stone D.,
Chen Y., Sotzny F., Lee C.C., Kastner D.L., Torrelo A.,
Zlotogorski A., Moir S., Gadina M., McCoy P., Wesley R., Rother K.,
Hildebrand P.W., Brogan P., Krueger E., Aksentijevich I.,
Goldbach-Mansky R.;
"Additive loss-of-function proteasome subunit mutations in
CANDLE/PRAAS patients promote type I IFN production.";
J. Clin. Invest. 125:4196-4211(2015).
[36]
VARIANT NKJO PRO-94.
PubMed=26567544; DOI=10.1007/s00431-015-2668-4;
Cavalcante M.P., Brunelli J.B., Miranda C.C., Novak G.V., Malle L.,
Aikawa N.E., Jesus A.A., Silva C.A.;
"CANDLE syndrome: chronic atypical neutrophilic dermatosis with
lipodystrophy and elevated temperature-a rare case with a novel
mutation.";
Eur. J. Pediatr. 175:735-740(2016).
-!- FUNCTION: The proteasome is a multicatalytic proteinase complex
which is characterized by its ability to cleave peptides with Arg,
Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
slightly basic pH. The proteasome has an ATP-dependent proteolytic
activity. This subunit is involved in antigen processing to
generate class I binding peptides. Replacement of PSMB5 by PSMB8
increases the capacity of the immunoproteasome to cleave model
peptides after hydrophobic and basic residues. Acts as a major
component of interferon gamma-induced sensitivity. Plays a key
role in apoptosis via the degradation of the apoptotic inhibitor
MCL1. May be involved in the inflammatory response pathway. In
cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1)
results in immunoproteasome deficiency. Required for the
differentiation of preadipocytes into adipocytes.
{ECO:0000269|PubMed:16423992, ECO:0000269|PubMed:19443843,
ECO:0000269|PubMed:21881205, ECO:0000269|PubMed:8163024}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is composed
of 28 subunits that are arranged in four stacked rings, resulting
in a barrel-shaped structure. The two end rings are each formed by
seven alpha subunits, and the two central rings are each formed by
seven beta subunits. The catalytic chamber with the active sites
is on the inside of the barrel. Component of the immunoproteasome,
where it displaces the equivalent housekeeping subunit PSMB5.
Component of the spermatoproteasome, a form of the proteasome
specifically found in testis. Directly interacts with POMP.
Interacts with HIV-1 TAT protein. Interacts with TAP1.
{ECO:0000269|PubMed:14550573, ECO:0000269|PubMed:15488952,
ECO:0000269|PubMed:15944226}.
-!- INTERACTION:
P27958:- (xeno); NbExp=4; IntAct=EBI-372294, EBI-3649474;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-
ProRule:PRU00809}. Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=LMP7B, LMP7-E2;
IsoId=P28062-1; Sequence=Displayed;
Name=2; Synonyms=LMP7A, LMP7-E1;
IsoId=P28062-2; Sequence=VSP_005287;
Note=Contains a phosphothreonine at position 5.
{ECO:0000244|PubMed:18669648};
-!- DEVELOPMENTAL STAGE: Highly expressed in immature dendritic cells
(at protein level). {ECO:0000269|PubMed:11717192}.
-!- INDUCTION: Up-regulated by IFNG/IFN-gamma and IRF1 (at protein
level). Up-regulated by TNF (at protein level). Up-regulated by
tetrodotoxin (TTX) in glial cells. Up-regulated in Crohn's bowel
disease (CD). Down-regulated by the selective inhibitor PR-957.
Down-regulated in mature dendritic cells by HSV-1 infection. Up-
regulated by heat shock treatment. {ECO:0000269|PubMed:11493458,
ECO:0000269|PubMed:15501285, ECO:0000269|PubMed:15907481,
ECO:0000269|PubMed:17142736, ECO:0000269|PubMed:17262812,
ECO:0000269|PubMed:19443843, ECO:0000269|PubMed:19525961,
ECO:0000269|PubMed:19619915, ECO:0000269|PubMed:8663318}.
-!- PTM: Autocleaved. The resulting N-terminal Thr residue of the
mature subunit is responsible for the nucleophile proteolytic
activity. {ECO:0000250|UniProtKB:O35955}.
-!- DISEASE: Nakajo syndrome (NKJO) [MIM:256040]: An autosomal
recessive autoinflammatory disorder characterized by early
childhood onset of recurrent fever, joint stiffness and severe
contractures of the hands and feet, and erythematous skin lesions
with subsequent development of lipodystrophy and laboratory
evidence of immune dysregulation. Accompanying features may
include muscle weakness and atrophy, hepatosplenomegaly, and
microcytic anemia. {ECO:0000269|PubMed:21129723,
ECO:0000269|PubMed:21852578, ECO:0000269|PubMed:21881205,
ECO:0000269|PubMed:21953331, ECO:0000269|PubMed:26524591,
ECO:0000269|PubMed:26567544}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
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EMBL; X66401; CAA47026.1; -; Genomic_DNA.
EMBL; X62598; CAA44482.1; -; mRNA.
EMBL; Z14982; CAA78705.1; -; Genomic_DNA.
EMBL; Z14982; CAA78706.1; -; Genomic_DNA.
EMBL; L11045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X87344; CAA60786.1; -; Genomic_DNA.
EMBL; X87344; CAA60787.1; -; Genomic_DNA.
EMBL; U17496; AAA56777.1; -; mRNA.
EMBL; U17497; AAA56778.1; -; mRNA.
EMBL; AL671681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL669918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL935043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX682530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX088556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CT009502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX927138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR762476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR753889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03644.1; -; Genomic_DNA.
EMBL; CH471081; EAX03645.1; -; Genomic_DNA.
EMBL; BC001114; AAH01114.1; -; mRNA.
EMBL; U32863; AAA80235.1; -; Genomic_DNA.
EMBL; U32862; AAA80234.1; -; Genomic_DNA.
CCDS; CCDS4756.1; -. [P28062-2]
CCDS; CCDS4757.1; -. [P28062-1]
PIR; A44324; A44324.
PIR; C44324; C44324.
PIR; G01564; G01564.
PIR; G02018; G02018.
RefSeq; NP_004150.1; NM_004159.4. [P28062-2]
RefSeq; NP_683720.2; NM_148919.3. [P28062-1]
UniGene; Hs.180062; -.
PDB; 5L5A; X-ray; 2.40 A; K/Y=73-210.
PDB; 5L5B; X-ray; 2.80 A; K/Y=73-210.
PDB; 5L5D; X-ray; 2.80 A; K/Y=73-210.
PDB; 5L5E; X-ray; 2.90 A; K/Y=73-210.
PDB; 5L5F; X-ray; 2.50 A; K/Y=73-210.
PDB; 5L5H; X-ray; 2.60 A; K/Y=73-210.
PDB; 5L5I; X-ray; 2.90 A; K/Y=73-210.
PDB; 5L5J; X-ray; 2.90 A; K/Y=73-210.
PDB; 5L5O; X-ray; 2.60 A; K/Y=73-210.
PDB; 5L5P; X-ray; 2.80 A; K/Y=73-210.
PDB; 5L5Q; X-ray; 2.80 A; K/Y=73-210.
PDB; 5L5R; X-ray; 2.90 A; K/Y=73-210.
PDB; 5L5S; X-ray; 2.60 A; K/Y=73-210.
PDB; 5L5T; X-ray; 2.90 A; K/Y=73-210.
PDB; 5L5U; X-ray; 2.60 A; K/Y=73-210.
PDB; 5L5V; X-ray; 2.70 A; K/Y=73-210.
PDB; 5LTT; X-ray; 2.70 A; K/Y=73-210.
PDB; 5M2B; X-ray; 2.70 A; K/Y=73-210.
PDBsum; 5L5A; -.
PDBsum; 5L5B; -.
PDBsum; 5L5D; -.
PDBsum; 5L5E; -.
PDBsum; 5L5F; -.
PDBsum; 5L5H; -.
PDBsum; 5L5I; -.
PDBsum; 5L5J; -.
PDBsum; 5L5O; -.
PDBsum; 5L5P; -.
PDBsum; 5L5Q; -.
PDBsum; 5L5R; -.
PDBsum; 5L5S; -.
PDBsum; 5L5T; -.
PDBsum; 5L5U; -.
PDBsum; 5L5V; -.
PDBsum; 5LTT; -.
PDBsum; 5M2B; -.
ProteinModelPortal; P28062; -.
SMR; P28062; -.
BioGrid; 111669; 65.
IntAct; P28062; 21.
MINT; MINT-3010850; -.
STRING; 9606.ENSP00000364016; -.
BindingDB; P28062; -.
ChEMBL; CHEMBL5620; -.
DrugBank; DB08889; Carfilzomib.
GuidetoPHARMACOLOGY; 2408; -.
MEROPS; T01.015; -.
iPTMnet; P28062; -.
PhosphoSitePlus; P28062; -.
SwissPalm; P28062; -.
BioMuta; PSMB8; -.
DMDM; 334302881; -.
EPD; P28062; -.
PaxDb; P28062; -.
PeptideAtlas; P28062; -.
PRIDE; P28062; -.
DNASU; 5696; -.
Ensembl; ENST00000374881; ENSP00000364015; ENSG00000204264. [P28062-2]
Ensembl; ENST00000374882; ENSP00000364016; ENSG00000204264. [P28062-1]
Ensembl; ENST00000383236; ENSP00000372723; ENSG00000206298. [P28062-1]
Ensembl; ENST00000383238; ENSP00000372725; ENSG00000206298. [P28062-2]
Ensembl; ENST00000416134; ENSP00000397057; ENSG00000235715. [P28062-2]
Ensembl; ENST00000416564; ENSP00000408825; ENSG00000226201. [P28062-2]
Ensembl; ENST00000421445; ENSP00000402406; ENSG00000236443. [P28062-1]
Ensembl; ENST00000429645; ENSP00000394155; ENSG00000226201. [P28062-1]
Ensembl; ENST00000435978; ENSP00000414731; ENSG00000231631. [P28062-2]
Ensembl; ENST00000436627; ENSP00000392693; ENSG00000230669. [P28062-2]
Ensembl; ENST00000438442; ENSP00000404585; ENSG00000231631. [P28062-1]
Ensembl; ENST00000441960; ENSP00000407539; ENSG00000230034. [P28062-2]
Ensembl; ENST00000452573; ENSP00000412618; ENSG00000236443. [P28062-2]
Ensembl; ENST00000455660; ENSP00000406797; ENSG00000230669. [P28062-1]
Ensembl; ENST00000457261; ENSP00000414770; ENSG00000235715. [P28062-1]
GeneID; 5696; -.
KEGG; hsa:5696; -.
UCSC; uc003ocf.4; human. [P28062-1]
CTD; 5696; -.
DisGeNET; 5696; -.
EuPathDB; HostDB:ENSG00000204264.8; -.
GeneCards; PSMB8; -.
HGNC; HGNC:9545; PSMB8.
HPA; HPA046995; -.
HPA; HPA050327; -.
MalaCards; PSMB8; -.
MIM; 177046; gene.
MIM; 256040; phenotype.
neXtProt; NX_P28062; -.
OpenTargets; ENSG00000204264; -.
Orphanet; 325004; CANDLE syndrome.
Orphanet; 324999; JMP syndrome.
Orphanet; 2615; Nakajo-Nishimura syndrome.
PharmGKB; PA33890; -.
eggNOG; KOG0175; Eukaryota.
eggNOG; ENOG410XQRP; LUCA.
GeneTree; ENSGT00510000046395; -.
HOGENOM; HOG000091082; -.
HOVERGEN; HBG108297; -.
InParanoid; P28062; -.
KO; K02740; -.
OMA; ATIRVNK; -.
OrthoDB; EOG09370H27; -.
PhylomeDB; P28062; -.
TreeFam; TF106223; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSMB8; human.
GeneWiki; PSMB8; -.
GenomeRNAi; 5696; -.
PRO; PR:P28062; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204264; -.
CleanEx; HS_PSMB8; -.
ExpressionAtlas; P28062; baseline and differential.
Genevisible; P28062; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:0052548; P:regulation of endopeptidase activity; IMP:UniProtKB.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000243; Pept_T1A_subB.
InterPro; IPR035705; Proteasome_beta8.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF53; PTHR11599:SF53; 1.
Pfam; PF00227; Proteasome; 1.
PRINTS; PR00141; PROTEASOME.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Differentiation; Disease mutation; Host-virus interaction; Hydrolase;
Immunity; Nucleus; Phosphoprotein; Polymorphism; Protease; Proteasome;
Reference proteome; Threonine protease; Zymogen.
PROPEP 1 72 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000026597.
CHAIN 73 276 Proteasome subunit beta type-8.
/FTId=PRO_0000026598.
ACT_SITE 73 73 Nucleophile. {ECO:0000250}.
SITE 72 73 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:O35955}.
VAR_SEQ 1 49 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPE
LALPRGMQ -> MLIGTPTPRDTTPSSWLTSSLLVEAAPLD
DTTLPTPVSSGCPGLE (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1922342}.
/FTId=VSP_005287.
VARIANT 8 8 G -> R (in allele LMP7C;
dbSNP:rs114772012).
/FTId=VAR_006488.
VARIANT 30 32 PGH -> RPD (in allele LPM7C).
/FTId=VAR_006489.
VARIANT 49 49 Q -> K (in dbSNP:rs2071543).
{ECO:0000269|Ref.7}.
/FTId=VAR_065204.
VARIANT 74 74 T -> S (in dbSNP:rs17220206).
/FTId=VAR_057046.
VARIANT 75 75 T -> M (in NKJO; markedly decreased
chymotrypsin-like activity consistent
with a decrease in proteasomal activity
and loss of function; some patients are
heterozygotes for this mutation and also
carry a mutation in PSMA3; patients'
cells show reduction of proteasome
content and endopeptidase activity of the
proteasome; dbSNP:rs748082671).
{ECO:0000269|PubMed:21129723,
ECO:0000269|PubMed:26524591}.
/FTId=VAR_065291.
VARIANT 94 94 A -> P (in NKJO; unknown pathological
significance).
{ECO:0000269|PubMed:26567544}.
/FTId=VAR_075256.
VARIANT 105 105 K -> Q (in NKJO; some patients are
heterozygotes for this mutation and also
carry a mutation in PSMB4).
{ECO:0000269|PubMed:26524591}.
/FTId=VAR_075257.
VARIANT 201 201 G -> V (in NKJO; affects immunoproteasome
assembly; reduced proteasome levels;
reduced chymotrypsin-like activity
consistent with a decrease in proteasomal
activity; dbSNP:rs387906680).
{ECO:0000269|PubMed:21852578,
ECO:0000269|PubMed:21881205}.
/FTId=VAR_066449.
STRAND 75 80 {ECO:0000244|PDB:5L5A}.
STRAND 83 88 {ECO:0000244|PDB:5L5A}.
STRAND 92 94 {ECO:0000244|PDB:5L5A}.
STRAND 97 101 {ECO:0000244|PDB:5L5A}.
STRAND 106 110 {ECO:0000244|PDB:5L5A}.
STRAND 113 116 {ECO:0000244|PDB:5L5A}.
HELIX 121 142 {ECO:0000244|PDB:5L5A}.
HELIX 148 161 {ECO:0000244|PDB:5L5A}.
TURN 163 166 {ECO:0000244|PDB:5L5A}.
STRAND 169 177 {ECO:0000244|PDB:5L5A}.
STRAND 180 187 {ECO:0000244|PDB:5L5A}.
STRAND 192 194 {ECO:0000244|PDB:5L5A}.
STRAND 196 201 {ECO:0000244|PDB:5L5A}.
HELIX 204 210 {ECO:0000244|PDB:5L5A}.
SEQUENCE 276 AA; 30354 MW; 4F689501677DBD44 CRC64;
MALLDVCGAP RGQRPESALP VAGSGRRSDP GHYSFSMRSP ELALPRGMQP TEFFQSLGGD
GERNVQIEMA HGTTTLAFKF QHGVIAAVDS RASAGSYISA LRVNKVIEIN PYLLGTMSGC
AADCQYWERL LAKECRLYYL RNGERISVSA ASKLLSNMMC QYRGMGLSMG SMICGWDKKG
PGLYYVDEHG TRLSGNMFST GSGNTYAYGV MDSGYRPNLS PEEAYDLGRR AIAYATHRDS
YSGGVVNMYH MKEDGWVKVE STDVSDLLHQ YREANQ


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Genprice Inc, Invoices and accounting
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