PSB11_HUMAN
ID PSB11_HUMAN Reviewed; 300 AA.
AC A5LHX3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
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 (By similarity). Plays a
CC pivotal role in development of CD8-positive T cells (By similarity).
CC {ECO:0000250}.
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 -!- INTERACTION:
CC A5LHX3; Q9H1Y0: ATG5; NbExp=3; IntAct=EBI-19951687, EBI-1047414;
CC A5LHX3; O14964: HGS; NbExp=3; IntAct=EBI-19951687, EBI-740220;
CC A5LHX3; P78337: PITX1; NbExp=3; IntAct=EBI-19951687, EBI-748265;
CC A5LHX3; O75360: PROP1; NbExp=5; IntAct=EBI-19951687, EBI-9027467;
CC A5LHX3; O43711: TLX3; NbExp=3; IntAct=EBI-19951687, EBI-3939165;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; AB299437; BAF63540.1; -; mRNA.
DR EMBL; AL132780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS41923.1; -.
DR RefSeq; NP_001093250.1; NM_001099780.1.
DR AlphaFoldDB; A5LHX3; -.
DR SMR; A5LHX3; -.
DR BioGRID; 125789; 5.
DR IntAct; A5LHX3; 5.
DR STRING; 9606.ENSP00000386212; -.
DR BindingDB; A5LHX3; -.
DR ChEMBL; CHEMBL2364701; -.
DR ChEMBL; CHEMBL3831201; -.
DR MEROPS; T01.016; -.
DR PhosphoSitePlus; A5LHX3; -.
DR BioMuta; PSMB11; -.
DR EPD; A5LHX3; -.
DR jPOST; A5LHX3; -.
DR MassIVE; A5LHX3; -.
DR PaxDb; A5LHX3; -.
DR PeptideAtlas; A5LHX3; -.
DR PRIDE; A5LHX3; -.
DR Antibodypedia; 47235; 97 antibodies from 22 providers.
DR DNASU; 122706; -.
DR Ensembl; ENST00000408907.5; ENSP00000386212.2; ENSG00000222028.5.
DR GeneID; 122706; -.
DR KEGG; hsa:122706; -.
DR MANE-Select; ENST00000408907.5; ENSP00000386212.2; NM_001099780.2; NP_001093250.1.
DR UCSC; uc010ake.2; human.
DR CTD; 122706; -.
DR GeneCards; PSMB11; -.
DR HGNC; HGNC:31963; PSMB11.
DR HPA; ENSG00000222028; Tissue enriched (lymphoid).
DR MIM; 611137; gene.
DR neXtProt; NX_A5LHX3; -.
DR OpenTargets; ENSG00000222028; -.
DR PharmGKB; PA162400222; -.
DR VEuPathDB; HostDB:ENSG00000222028; -.
DR eggNOG; KOG0175; Eukaryota.
DR GeneTree; ENSGT00940000162200; -.
DR HOGENOM; CLU_035750_7_3_1; -.
DR InParanoid; A5LHX3; -.
DR OMA; KVIPVHR; -.
DR OrthoDB; 929961at2759; -.
DR PhylomeDB; A5LHX3; -.
DR TreeFam; TF106223; -.
DR PathwayCommons; A5LHX3; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; A5LHX3; -.
DR BioGRID-ORCS; 122706; 19 hits in 1068 CRISPR screens.
DR GenomeRNAi; 122706; -.
DR Pharos; A5LHX3; Tbio.
DR PRO; PR:A5LHX3; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; A5LHX3; protein.
DR Bgee; ENSG00000222028; Expressed in left testis.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
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; IDA: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; IEA:Ensembl.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
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; Protease; Proteasome; Reference proteome;
KW Threonine protease; Zymogen.
FT PROPEP 1..49
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000300011"
FT CHAIN 50..300
FT /note="Proteasome subunit beta type-11"
FT /id="PRO_0000300012"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 50
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT VARIANT 49
FT /note="G -> S (in dbSNP:rs34457782)"
FT /id="VAR_051550"
SQ SEQUENCE 300 AA; 32530 MW; 234ECBD1D230A7E8 CRC64;
MALQDVCKWQ SPDTQGPSPH LPRAGGWAVP RGCDPQTFLQ IHGPRLAHGT TTLAFRFRHG
VIAAADTRSS CGSYVACPAS CKVIPVHQHL LGTTSGTSAD CATWYRVLQR ELRLRELREG
QLPSVASAAK LLSAMMSQYR GLDLCVATAL CGWDRSGPEL FYVYSDGTRL QGDIFSVGSG
SPYAYGVLDR GYRYDMSTQE AYALARCAVA HATHRDAYSG GSVDLFHVRE SGWEHVSRSD
ACVLYVELQK LLEPEPEEDA SHAHPEPATA HRAAEDRELS VGPGEVTPGD SRMPAGTETV
