PSB8_MOUSE
ID PSB8_MOUSE Reviewed; 276 AA.
AC P28063; Q3UK42; Q64300; Q792S8; Q7TMX9; Q91VH7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Proteasome subunit beta type-8;
DE EC=3.4.25.1;
DE AltName: Full=Low molecular mass protein 7;
DE AltName: Full=Macropain subunit C13;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C13;
DE AltName: Full=Proteasome component C13;
DE AltName: Full=Proteasome subunit beta-5i;
DE Flags: Precursor;
GN Name=Psmb8; Synonyms=Lmp7, Mc13;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lymphoma;
RX PubMed=1633842; DOI=10.1016/0014-5793(92)80420-l;
RA Frentzel S., Graef U., Haemmerling G., Kloetzel P.-M.;
RT "Isolation and characterization of the MHC linked beta-type proteasome
RT subunit MC13 cDNA.";
RL FEBS Lett. 302:121-125(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lymphoma;
RX PubMed=8344725; DOI=10.1007/bf00210482;
RA Meinhardt T., Graf U., Hammerling G.J.;
RT "Different genomic structure of mouse and human Lmp7 genes:
RT characterization of MHC-encoded proteasome genes.";
RL Immunogenetics 38:373-379(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=8406612; DOI=10.1007/bf00184520;
RA Zanelli E.H., Zhou P., Hong C., Smart M.K., David C.S.;
RT "Genomic organization and tissue expression of the mouse proteasome gene
RT Lmp-7.";
RL Immunogenetics 38:400-407(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS
RP LMP7K/LMP7S/LMPF/LMP7R/LMPCAS4/LMPG7 ARG-272 AND LMP7Q SER-275.
RC STRAIN=A.CA, B10.BR, B10.CAS4, B10.RIII, BALB/cJ, DBA/1J, NOD, and SJL/J;
RC TISSUE=Splenocyte, and Thymocyte;
RX PubMed=8854085;
RA Nandi D., Iyer M.N., Monaco J.J.;
RT "Molecular and serological analysis of polymorphisms in the murine major
RT histocompatibility complex-encoded proteasome subunits, LMP-2 and LMP-7.";
RL Exp. Clin. Immunogenet. 13:20-29(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Bone marrow, Medulla oblongata, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Rowen L., Qin S., Ahearn M.E., Loretz C., Faust J., Lasky S., Mahairas G.,
RA Hood L.;
RT "Sequence of the mouse major histocompatibility locus class II region.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT
RP LMP7K/LMP7S/LMPF/LMP7R/LMPCAS4/LMPG7 ARG-272.
RC STRAIN=C57BL/6NCr, and NMRI;
RC TISSUE=Hematopoietic stem cell, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION.
RX PubMed=8066463; DOI=10.1126/science.8066463;
RA Fehling H.J., Swat W., Laplace C., Kuehn R., Rajewsky K., Mueller U.,
RA von Boehmer H.;
RT "MHC class I expression in mice lacking the proteasome subunit LMP-7.";
RL Science 265:1234-1237(1994).
RN [9]
RP INDUCTION BY DEOXYNIVALENOL.
RX PubMed=15371230; DOI=10.1080/15287390490483827;
RA Kinser S., Jia Q., Li M., Laughter A., Cornwell P., Corton J.C., Pestka J.;
RT "Gene expression profiling in spleens of deoxynivalenol-exposed mice:
RT immediate early genes as primary targets.";
RL J. Toxicol. Environ. Health Part A 67:1423-1441(2004).
RN [10]
RP INDUCTION BY INTERFERON GAMMA AND IRF1.
RX PubMed=15907481; DOI=10.1016/j.febslet.2005.04.012;
RA Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y., Tsuchiya K.,
RA Okamoto R., Kanai T., Watanabe M.;
RT "IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted expression
RT of immunosubunits of the proteasome.";
RL FEBS Lett. 579:2781-2787(2005).
RN [11]
RP INDUCTION BY HEAT SHOCK.
RX PubMed=17142736; DOI=10.4049/jimmunol.177.12.8393;
RA Callahan M.K., Wohlfert E.A., Menoret A., Srivastava P.K.;
RT "Heat shock up-regulates lmp2 and lmp7 and enhances presentation of
RT immunoproteasome-dependent epitopes.";
RL J. Immunol. 177:8393-8399(2006).
RN [12]
RP INDUCTION BY EGR1.
RX PubMed=16452686; DOI=10.1523/jneurosci.4199-05.2006;
RA James A.B., Conway A.M., Morris B.J.;
RT "Regulation of the neuronal proteasome by Zif268 (Egr1).";
RL J. Neurosci. 26:1624-1634(2006).
RN [13]
RP IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [14]
RP INDUCTION BY PR-957.
RX PubMed=19525961; DOI=10.1038/nm.1978;
RA Muchamuel T., Basler M., Aujay M.A., Suzuki E., Kalim K.W., Lauer C.,
RA Sylvain C., Ring E.R., Shields J., Jiang J., Shwonek P., Parlati F.,
RA Demo S.D., Bennett M.K., Kirk C.J., Groettrup M.;
RT "A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine
RT production and attenuates progression of experimental arthritis.";
RL Nat. Med. 15:781-787(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [16]
RP FUNCTION IN ADIPOCYTE DIFFERENTIATION.
RX PubMed=21881205; DOI=10.1172/jci58414;
RA Kitamura A., Maekawa Y., Uehara H., Izumi K., Kawachi I., Nishizawa M.,
RA Toyoshima Y., Takahashi H., Standley D.M., Tanaka K., Hamazaki J.,
RA Murata S., Obara K., Toyoshima I., Yasutomo K.;
RT "A mutation in the immunoproteasome subunit PSMB8 causes autoinflammation
RT and lipodystrophy in humans.";
RL J. Clin. Invest. 121:4150-4160(2011).
RN [17]
RP IDENTIFICATION IN THE SPERMATOPROTEASOME.
RX PubMed=23706739; DOI=10.1016/j.cell.2013.04.032;
RA Qian M.X., Pang Y., Liu C.H., Haratake K., Du B.Y., Ji D.Y., Wang G.F.,
RA Zhu Q.Q., Song W., Yu Y., Zhang X.X., Huang H.T., Miao S., Chen L.B.,
RA Zhang Z.H., Liang Y.N., Liu S., Cha H., Yang D., Zhai Y., Komatsu T.,
RA Tsuruta F., Li H., Cao C., Li W., Li G.H., Cheng Y., Chiba T., Wang L.,
RA Goldberg A.L., Shen Y., Qiu X.B.;
RT "Acetylation-mediated proteasomal degradation of core histones during DNA
RT repair and spermatogenesis.";
RL Cell 153:1012-1024(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME IN COMPLEX
RP WITH SYNTHETIC INHIBITOR, SUBUNIT, FUNCTION, TISSUE SPECIFICITY, ACTIVE
RP SITE, AND AUTOCLEAVAGE.
RX PubMed=22341445; DOI=10.1016/j.cell.2011.12.030;
RA Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M.,
RA Groll M.;
RT "Immuno- and constitutive proteasome crystal structures reveal differences
RT in substrate and inhibitor specificity.";
RL Cell 148:727-738(2012).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity. This
CC subunit is involved in antigen processing to generate class I binding
CC peptides. May participate in the inflammatory response pathway.
CC Required for adipocyte differentiation (PubMed:21881205,
CC PubMed:22341445, PubMed:8066463). May be involved in the generation of
CC spliced peptides resulting from the ligation of two separate
CC proteasomal cleavage products that are not contiguous in the parental
CC protein (By similarity). {ECO:0000250|UniProtKB:P28062,
CC ECO:0000269|PubMed:21881205, ECO:0000269|PubMed:22341445,
CC ECO:0000269|PubMed:8066463}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1;
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. Component of the immunoproteasome, where it displaces
CC the equivalent housekeeping subunit PSMB5. Component of the
CC spermatoproteasome, a form of the proteasome specifically found in
CC testis. Directly interacts with POMP. Interacts with TAP1.
CC {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445,
CC ECO:0000269|PubMed:23706739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level). Expressed in
CC spleen, thymus, lung, liver, heart and, at a very low level, in kidney.
CC Not expressed in brain nor testis. {ECO:0000269|PubMed:22341445,
CC ECO:0000269|PubMed:8406612}.
CC -!- INDUCTION: Up-regulated by interferon gamma (at protein level). Up-
CC regulated by IRF1. Down-regulated in spleen by deoxynivalenol (DON), a
CC mycotoxin that alters immune functions. Down-regulated by the selective
CC inhibitor PR-957. Up-regulated by heat shock treatment. Down-regulated
CC by EGR1 in neuronal cells. {ECO:0000269|PubMed:15371230,
CC ECO:0000269|PubMed:15907481, ECO:0000269|PubMed:16452686,
CC ECO:0000269|PubMed:17142736, ECO:0000269|PubMed:19525961}.
CC -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the mature
CC subunit is responsible for the nucleophile proteolytic activity.
CC {ECO:0000250|UniProtKB:O35955}.
CC -!- POLYMORPHISM: The allele, LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7 found in
CC strains NMRI, B10.BR, SJL, A.CA, B10.RIII, B10.cas4 and NOD may be
CC post-translationally modified. Allele LMP7q is found in strain DBA/1J.
CC {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8854085}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA45780.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X64449; CAA45779.1; -; mRNA.
DR EMBL; X64449; CAA45780.1; ALT_INIT; mRNA.
DR EMBL; L11145; AAB46392.1; -; mRNA.
DR EMBL; Z21847; CAB60065.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U22031; AAA75033.1; -; mRNA.
DR EMBL; U22032; AAA75034.1; -; mRNA.
DR EMBL; U22033; AAA75035.1; -; mRNA.
DR EMBL; U22034; AAA75036.1; -; mRNA.
DR EMBL; U22035; AAA75037.1; -; mRNA.
DR EMBL; AK031801; BAC27555.1; -; mRNA.
DR EMBL; AK050627; BAE20682.1; -; mRNA.
DR EMBL; AK146182; BAE26960.1; -; mRNA.
DR EMBL; AK150674; BAE29756.1; -; mRNA.
DR EMBL; AK159971; BAE35524.1; -; mRNA.
DR EMBL; AF027865; AAB81532.1; -; Genomic_DNA.
DR EMBL; BC013785; AAH13785.1; -; mRNA.
DR EMBL; BC051450; AAH51450.1; -; mRNA.
DR CCDS; CCDS50073.1; -.
DR PIR; I54513; I54513.
DR RefSeq; NP_034854.2; NM_010724.2.
DR PDB; 3UNF; X-ray; 2.90 A; K/Y=73-276.
DR PDB; 3UNH; X-ray; 3.20 A; K/Y=73-276.
DR PDB; 5L65; X-ray; 2.90 A; K/Y=73-210.
DR PDB; 5L66; X-ray; 2.80 A; K/Y=73-210.
DR PDB; 5L67; X-ray; 2.60 A; K/Y=73-210.
DR PDB; 5L68; X-ray; 2.80 A; K/Y=73-210.
DR PDB; 5L69; X-ray; 2.70 A; K/Y=73-210.
DR PDB; 5L6A; X-ray; 2.80 A; K/Y=73-210.
DR PDB; 5L6B; X-ray; 2.60 A; K/Y=73-210.
DR PDB; 5L6C; X-ray; 2.60 A; K/Y=73-210.
DR PDBsum; 3UNF; -.
DR PDBsum; 3UNH; -.
DR PDBsum; 5L65; -.
DR PDBsum; 5L66; -.
DR PDBsum; 5L67; -.
DR PDBsum; 5L68; -.
DR PDBsum; 5L69; -.
DR PDBsum; 5L6A; -.
DR PDBsum; 5L6B; -.
DR PDBsum; 5L6C; -.
DR AlphaFoldDB; P28063; -.
DR SMR; P28063; -.
DR BioGRID; 201182; 35.
DR CORUM; P28063; -.
DR IntAct; P28063; 5.
DR STRING; 10090.ENSMUSP00000025196; -.
DR BindingDB; P28063; -.
DR ChEMBL; CHEMBL1944492; -.
DR GuidetoPHARMACOLOGY; 2408; -.
DR MEROPS; T01.012; -.
DR iPTMnet; P28063; -.
DR PhosphoSitePlus; P28063; -.
DR SwissPalm; P28063; -.
DR EPD; P28063; -.
DR jPOST; P28063; -.
DR MaxQB; P28063; -.
DR PaxDb; P28063; -.
DR PeptideAtlas; P28063; -.
DR PRIDE; P28063; -.
DR ProteomicsDB; 291608; -.
DR Antibodypedia; 28713; 414 antibodies from 41 providers.
DR DNASU; 16913; -.
DR Ensembl; ENSMUST00000025196; ENSMUSP00000025196; ENSMUSG00000024338.
DR GeneID; 16913; -.
DR KEGG; mmu:16913; -.
DR UCSC; uc012apv.1; mouse.
DR CTD; 5696; -.
DR MGI; MGI:1346527; Psmb8.
DR VEuPathDB; HostDB:ENSMUSG00000024338; -.
DR eggNOG; KOG0175; Eukaryota.
DR GeneTree; ENSGT00940000157293; -.
DR InParanoid; P28063; -.
DR OMA; IQIEMAH; -.
DR OrthoDB; 929961at2759; -.
DR PhylomeDB; P28063; -.
DR TreeFam; TF106223; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 16913; 9 hits in 77 CRISPR screens.
DR ChiTaRS; Psmb8; mouse.
DR PRO; PR:P28063; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P28063; protein.
DR Bgee; ENSMUSG00000024338; Expressed in peripheral lymph node and 138 other tissues.
DR ExpressionAtlas; P28063; baseline and differential.
DR Genevisible; P28063; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0052548; P:regulation of endopeptidase activity; ISO:MGI.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR035705; Proteasome_beta8.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF53; PTHR11599:SF53; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Differentiation; Hydrolase; Immunity; Nucleus;
KW Protease; Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..72
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026599"
FT CHAIN 73..276
FT /note="Proteasome subunit beta type-8"
FT /id="PRO_0000026600"
FT ACT_SITE 73
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:22341445"
FT SITE 72..73
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O35955"
FT VARIANT 272
FT /note="G -> R (in LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8854085"
FT VARIANT 275
FT /note="A -> S (in LMP7q)"
FT /evidence="ECO:0000269|PubMed:8854085"
FT CONFLICT 39
FT /note="A -> R (in Ref. 3; CAB60065)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="V -> M (in Ref. 5; BAE26960)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="S -> P (in Ref. 7; AAH51450)"
FT /evidence="ECO:0000305"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:5L67"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:5L67"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5L67"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5L67"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:5L67"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:5L67"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:5L67"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:5L67"
FT TURN 162..166
FT /evidence="ECO:0007829|PDB:5L67"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:5L67"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:5L67"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5L67"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:5L67"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:5L67"
FT HELIX 221..238
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:3UNF"
SQ SEQUENCE 276 AA; 30260 MW; D9FCCF3EF83CD3C3 CRC64;
MALLDLCGAA RGQRPEWAAL DAGSGGRSDP GHYSFSAQAP ELALPRGMQP TAFLRSFGGD
QERNVQIEMA HGTTTLAFKF QHGVIVAVDS RATAGSYISS LRMNKVIEIN PYLLGTMSGC
AADCQYWERL LAKECRLYYL RNGERISVSA ASKLLSNMML QYRGMGLSMG SMICGWDKKG
PGLYYVDDNG TRLSGQMFST GSGNTYAYGV MDSGYRQDLS PEEAYDLGRR AIAYATHRDN
YSGGVVNMYH MKEDGWVKVE SSDVSDLLYK YGEAAL
