PSB11_MOUSE
ID PSB11_MOUSE Reviewed; 302 AA.
AC Q8BG41; Q149K8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Proteasome subunit beta type-11;
DE EC=3.4.25.1;
DE AltName: Full=Proteasome subunit beta-5t;
DE Flags: Precursor;
GN Name=Psmb11;
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], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17540904; DOI=10.1126/science.1141915;
RA Murata S., Sasaki K., Kishimoto T., Niwa S., Hayashi H., Takahama Y.,
RA Tanaka K.;
RT "Regulation of CD8+ T cell development by thymus-specific proteasomes.";
RL Science 316:1349-1353(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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).
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.
CC Incorporated instead of PSMB5 or PSMB8, this unit reduces the
CC chymotrypsin-like activity of the proteasome. Plays a pivotal role in
CC development of CD8-positive T-cells. {ECO:0000269|PubMed:17540904}.
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. Incorporated instead of PSMB5 and PSMB8.
CC {ECO:0000269|PubMed:17540904}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in cortical thymic epithelial
CC cells. {ECO:0000269|PubMed:17540904}.
CC -!- DISRUPTION PHENOTYPE: Displays defective development of CD8-positive T-
CC cells in the thymus. {ECO:0000269|PubMed:17540904}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; AB299436; BAF63539.1; -; mRNA.
DR EMBL; AK041393; BAC30929.1; -; mRNA.
DR EMBL; AK162727; BAE37039.1; -; mRNA.
DR EMBL; AK037368; BAC29796.1; -; mRNA.
DR EMBL; BC117732; AAI17733.1; -; mRNA.
DR EMBL; BC117733; AAI17734.1; -; mRNA.
DR CCDS; CCDS49491.1; -.
DR RefSeq; NP_780413.1; NM_175204.4.
DR AlphaFoldDB; Q8BG41; -.
DR SMR; Q8BG41; -.
DR STRING; 10090.ENSMUSP00000132140; -.
DR MEROPS; T01.016; -.
DR iPTMnet; Q8BG41; -.
DR PhosphoSitePlus; Q8BG41; -.
DR MaxQB; Q8BG41; -.
DR PaxDb; Q8BG41; -.
DR PRIDE; Q8BG41; -.
DR ProteomicsDB; 291760; -.
DR Antibodypedia; 47235; 97 antibodies from 22 providers.
DR DNASU; 73902; -.
DR Ensembl; ENSMUST00000097177; ENSMUSP00000132140; ENSMUSG00000072423.
DR GeneID; 73902; -.
DR KEGG; mmu:73902; -.
DR UCSC; uc007twn.2; mouse.
DR CTD; 122706; -.
DR MGI; MGI:1921152; Psmb11.
DR VEuPathDB; HostDB:ENSMUSG00000072423; -.
DR eggNOG; KOG0175; Eukaryota.
DR GeneTree; ENSGT00940000162200; -.
DR HOGENOM; CLU_035750_7_3_1; -.
DR InParanoid; Q8BG41; -.
DR OMA; KVIPVHR; -.
DR OrthoDB; 929961at2759; -.
DR PhylomeDB; Q8BG41; -.
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-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-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-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-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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 73902; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Psmb11; mouse.
DR PRO; PR:Q8BG41; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BG41; protein.
DR Bgee; ENSMUSG00000072423; Expressed in thymus and 16 other tissues.
DR Genevisible; Q8BG41; 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:0005839; C:proteasome core complex; IDA:MGI.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043374; P:CD8-positive, alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR034385; Proteasome_beta11.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF48; PTHR11599:SF48; 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 Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protease; Proteasome;
KW Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..49
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000300013"
FT CHAIN 50..302
FT /note="Proteasome subunit beta type-11"
FT /id="PRO_0000300014"
FT ACT_SITE 50
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 266
FT /note="Y -> H (in Ref. 3; AAI17734/AAI17733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 33220 MW; CAF08F2E3E914A13 CRC64;
MALQDVCKWQ TPDTPRPSIH LPQAGGWAVP RGCDPQTFLQ IHGPRLAHGT TTLAFRFRHG
VIAAADTRSS CGSYVACPAS RKVIPVHQRL LGTTSGTSAD CATWYRVLRR ELRLRELREG
QLPSVAGTAK LLAAMMSCYR GLDLCVATAL CGWDHSGPAL FYVYSDGTCL QGDIFSVGSG
SPYAYGVLDR GYHYDMTIQE AYTLARCAVA HATHRDAYSG GSVDLFHVRE SGWEYVSRSD
ACVLYRELQK ARSLEQELEA KACGIYPEPA TPQGARECKE LFVEQEEVTP EDCAIIMKTE
TM
