PSB10_HUMAN
ID PSB10_HUMAN Reviewed; 273 AA.
AC P40306; B2R5J4; Q5U098;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Proteasome subunit beta type-10;
DE EC=3.4.25.1;
DE AltName: Full=Low molecular mass protein 10;
DE AltName: Full=Macropain subunit MECl-1;
DE AltName: Full=Multicatalytic endopeptidase complex subunit MECl-1;
DE AltName: Full=Proteasome MECl-1;
DE AltName: Full=Proteasome subunit beta-2i;
DE Flags: Precursor;
GN Name=PSMB10; Synonyms=LMP10, MECL1;
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 [GENOMIC DNA].
RX PubMed=8268911; DOI=10.1093/hmg/2.10.1589;
RA Larsen F., Solheim J., Kristensen T., Kolstoe A.-B., Prydz H.;
RT "A tight cluster of five unrelated human genes on chromosome 16q22.1.";
RL Hum. Mol. Genet. 2:1589-1595(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9551082; DOI=10.1016/s0167-4889(97)00152-3;
RA Foss G.S., Larsen F., Solheim J., Prydz H.;
RT "Constitutive and interferon-gamma-induced expression of the human
RT proteasome subunit multicatalytic endopeptidase complex-like 1.";
RL Biochim. Biophys. Acta 1402:17-28(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, and Lymph;
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 [7]
RP INDUCTION BY IFNG.
RX PubMed=8666937; DOI=10.1084/jem.183.4.1807;
RA Hisamatsu H., Shimbara N., Saito Y., Kristensen P., Hendil K.B.,
RA Fujiwara T., Takahashi E., Tanahashi N., Tamura T., Ichihara A., Tanaka K.;
RT "Newly identified pair of proteasomal subunits regulated reciprocally by
RT interferon gamma.";
RL J. Exp. Med. 183:1807-1816(1996).
RN [8]
RP INDUCTION BY IFNG AND IRF1.
RX PubMed=10575004; DOI=10.1074/jbc.274.49.35196;
RA Foss G.S., Prydz H.;
RT "Interferon regulatory factor 1 mediates the interferon-gamma induction of
RT the human immunoproteasome subunit multicatalytic endopeptidase complex-
RT like 1.";
RL J. Biol. Chem. 274:35196-35202(1999).
RN [9]
RP INDUCTION BY TNF AND IFNG.
RX PubMed=11493458; DOI=10.1182/blood.v98.4.1108;
RA Hallermalm K., Seki K., Wei C., Castelli C., Rivoltini L., Kiessling R.,
RA Levitskaya J.;
RT "Tumor necrosis factor-alpha induces coordinated changes in major
RT histocompatibility class I presentation pathway, resulting in increased
RT stability of class I complexes at the cell surface.";
RL Blood 98:1108-1115(2001).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=11717192; DOI=10.1093/intimm/13.12.1515;
RA Li J., Schuler-Thurner B., Schuler G., Huber C., Seliger B.;
RT "Bipartite regulation of different components of the MHC class I antigen-
RT processing machinery during dendritic cell maturation.";
RL Int. Immunol. 13:1515-1523(2001).
RN [11]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RX PubMed=14550573; DOI=10.1016/s0014-5793(03)01025-1;
RA Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA Mayer R.J., Krueger E.;
RT "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT proteasomal alpha and beta subunits.";
RL FEBS Lett. 553:200-204(2003).
RN [12]
RP INDUCTION BY TETRODOTOXIN.
RX PubMed=15501285; DOI=10.1016/j.toxicon.2004.07.018;
RA Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.;
RT "Potential effects of tetrodotoxin exposure to human glial cells postulated
RT using microarray approach.";
RL Toxicon 44:597-608(2004).
RN [13]
RP INDUCTION BY IFNG 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 [14]
RP INDUCTION.
RX PubMed=17262812; DOI=10.1002/ibd.20110;
RA Wu F., Dassopoulos T., Cope L., Maitra A., Brant S.R., Harris M.L.,
RA Bayless T.M., Parmigiani G., Chakravarti S.;
RT "Genome-wide gene expression differences in Crohn's disease and ulcerative
RT colitis from endoscopic pinch biopsies: insights into distinctive
RT pathogenesis.";
RL Inflamm. Bowel Dis. 13:807-821(2007).
RN [15]
RP INDUCTION BY CD40L.
RX PubMed=18694960; DOI=10.1128/mcb.00611-08;
RA Moschonas A., Kouraki M., Knox P.G., Thymiakou E., Kardassis D.,
RA Eliopoulos A.G.;
RT "CD40 induces antigen transporter and immunoproteasome gene expression in
RT carcinomas via the coordinated action of NF-kappaB and of NF-kappaB-
RT mediated de novo synthesis of IRF-1.";
RL Mol. Cell. Biol. 28:6208-6222(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP INVOLVEMENT IN PRAAS5, VARIANT PRAAS5 SER-14, AND CHARACTERIZATION OF
RP VARIANT PRAAS5 SER-14.
RX PubMed=31783057; DOI=10.1016/j.jaci.2019.11.024;
RA Sarrabay G., Mechin D., Salhi A., Boursier G., Rittore C., Crow Y.,
RA Rice G., Tran T.A., Cezar R., Duffy D., Bondet V., Boudhane L., Broca C.,
RA Kant B.P., VanGijn M., Grandemange S., Richard E., Apparailly F.,
RA Touitou I.;
RT "PSMB10, the last immunoproteasome gene missing for PRAAS.";
RL J. Allergy Clin. Immunol. 145:1015-1017(2020).
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.
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 PSMB7. Component of the
CC spermatoproteasome, a form of the proteasome specifically found in
CC testis. {ECO:0000269|PubMed:14550573}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 TAT protein.
CC {ECO:0000269|PubMed:14550573}.
CC -!- INTERACTION:
CC P40306; O95273: CCNDBP1; NbExp=5; IntAct=EBI-603329, EBI-748961;
CC P40306; O43186: CRX; NbExp=3; IntAct=EBI-603329, EBI-748171;
CC P40306; G5E9A7: DMWD; NbExp=3; IntAct=EBI-603329, EBI-10976677;
CC P40306; P28799: GRN; NbExp=3; IntAct=EBI-603329, EBI-747754;
CC P40306; P50222: MEOX2; NbExp=3; IntAct=EBI-603329, EBI-748397;
CC P40306; O60260-5: PRKN; NbExp=3; IntAct=EBI-603329, EBI-21251460;
CC P40306; P49720: PSMB3; NbExp=3; IntAct=EBI-603329, EBI-603340;
CC P40306; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-603329, EBI-396669;
CC P40306; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-603329, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in immature dendritic cells (at
CC protein level). {ECO:0000269|PubMed:11717192}.
CC -!- INDUCTION: Up-regulated by IFNG/IFN-gamma (at protein level). Up-
CC regulated by IRF1. Up-regulated by TNF (at protein level). Up-regulated
CC by tetrodotoxin (TTX) in glial cells. Up-regulated in Crohn's bowel
CC disease (CD). Up-regulated by CD40L via the NFKB1 pathway in cancer
CC cells. {ECO:0000269|PubMed:10575004, ECO:0000269|PubMed:11493458,
CC ECO:0000269|PubMed:15501285, ECO:0000269|PubMed:15907481,
CC ECO:0000269|PubMed:17262812, ECO:0000269|PubMed:18694960,
CC ECO:0000269|PubMed:8666937}.
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 -!- DISEASE: Proteasome-associated autoinflammatory syndrome 5 (PRAAS5)
CC [MIM:619175]: An autosomal recessive, autoinflammatory disorder
CC characterized by recurrent, polymorphic disseminated cutaneous rash
CC with annular lesions, non-specific lymphocytic infiltration in the
CC skin, fever, failure to thrive, and persistent hepatosplenomegaly.
CC Disease onset is in early infancy. {ECO:0000269|PubMed:31783057}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; X71874; CAA50709.1; -; Genomic_DNA.
DR EMBL; Y13640; CAA73982.1; -; mRNA.
DR EMBL; BT019723; AAV38528.1; -; mRNA.
DR EMBL; BT019724; AAV38529.1; -; mRNA.
DR EMBL; AK312208; BAG35141.1; -; mRNA.
DR EMBL; CH471092; EAW83187.1; -; Genomic_DNA.
DR EMBL; BC017198; AAH17198.1; -; mRNA.
DR EMBL; BC052369; AAH52369.1; -; mRNA.
DR CCDS; CCDS10853.1; -.
DR PIR; I38135; I38135.
DR RefSeq; NP_002792.1; NM_002801.3.
DR PDB; 6AVO; EM; 3.80 A; B/E=40-273.
DR PDB; 6E5B; X-ray; 2.77 A; H/V=1-273.
DR PDB; 6HV3; X-ray; 2.70 A; H/V=40-92.
DR PDB; 6HV4; X-ray; 3.00 A; H/V=40-92.
DR PDB; 6HV5; X-ray; 3.00 A; H/V=40-92.
DR PDB; 6HV7; X-ray; 3.40 A; H/V=40-92.
DR PDB; 6HVA; X-ray; 2.90 A; H/V=40-92.
DR PDB; 6HVR; X-ray; 2.70 A; H/V=40-92.
DR PDB; 6HVS; X-ray; 3.10 A; H/V=40-92.
DR PDB; 6HVT; X-ray; 2.90 A; H/V=40-92.
DR PDB; 6HVU; X-ray; 2.90 A; H/V=40-92.
DR PDB; 6HVV; X-ray; 2.70 A; H/V=40-92.
DR PDB; 6HVW; X-ray; 3.00 A; H/V=40-92.
DR PDB; 7AWE; X-ray; 2.29 A; I/W=40-262.
DR PDB; 7B12; X-ray; 2.43 A; i/w=40-262.
DR PDBsum; 6AVO; -.
DR PDBsum; 6E5B; -.
DR PDBsum; 6HV3; -.
DR PDBsum; 6HV4; -.
DR PDBsum; 6HV5; -.
DR PDBsum; 6HV7; -.
DR PDBsum; 6HVA; -.
DR PDBsum; 6HVR; -.
DR PDBsum; 6HVS; -.
DR PDBsum; 6HVT; -.
DR PDBsum; 6HVU; -.
DR PDBsum; 6HVV; -.
DR PDBsum; 6HVW; -.
DR PDBsum; 7AWE; -.
DR PDBsum; 7B12; -.
DR AlphaFoldDB; P40306; -.
DR SMR; P40306; -.
DR BioGRID; 111672; 29.
DR IntAct; P40306; 17.
DR MINT; P40306; -.
DR STRING; 9606.ENSP00000351314; -.
DR BindingDB; P40306; -.
DR ChEMBL; CHEMBL3317334; -.
DR DrugBank; DB08889; Carfilzomib.
DR MEROPS; T01.014; -.
DR GlyGen; P40306; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P40306; -.
DR PhosphoSitePlus; P40306; -.
DR BioMuta; PSMB10; -.
DR DMDM; 730376; -.
DR OGP; P40306; -.
DR SWISS-2DPAGE; P40306; -.
DR EPD; P40306; -.
DR jPOST; P40306; -.
DR MassIVE; P40306; -.
DR MaxQB; P40306; -.
DR PaxDb; P40306; -.
DR PeptideAtlas; P40306; -.
DR PRIDE; P40306; -.
DR ProteomicsDB; 55360; -.
DR Antibodypedia; 29677; 235 antibodies from 35 providers.
DR CPTC; P40306; 1 antibody.
DR DNASU; 5699; -.
DR Ensembl; ENST00000358514.9; ENSP00000351314.4; ENSG00000205220.12.
DR GeneID; 5699; -.
DR KEGG; hsa:5699; -.
DR MANE-Select; ENST00000358514.9; ENSP00000351314.4; NM_002801.4; NP_002792.1.
DR UCSC; uc002eux.3; human.
DR CTD; 5699; -.
DR DisGeNET; 5699; -.
DR GeneCards; PSMB10; -.
DR HGNC; HGNC:9538; PSMB10.
DR HPA; ENSG00000205220; Tissue enhanced (lymphoid).
DR MalaCards; PSMB10; -.
DR MIM; 176847; gene.
DR MIM; 619175; phenotype.
DR neXtProt; NX_P40306; -.
DR OpenTargets; ENSG00000205220; -.
DR PharmGKB; PA33883; -.
DR VEuPathDB; HostDB:ENSG00000205220; -.
DR eggNOG; KOG0173; Eukaryota.
DR GeneTree; ENSGT00940000161047; -.
DR HOGENOM; CLU_035750_3_0_1; -.
DR InParanoid; P40306; -.
DR OMA; RVSYGFY; -.
DR OrthoDB; 977476at2759; -.
DR PhylomeDB; P40306; -.
DR TreeFam; TF106222; -.
DR PathwayCommons; P40306; -.
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-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
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-187577; SCF(Skp2)-mediated degradation of p27/p21.
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-68867; Assembly of the pre-replicative complex.
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-8941858; Regulation of RUNX3 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-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P40306; -.
DR SIGNOR; P40306; -.
DR BioGRID-ORCS; 5699; 17 hits in 1088 CRISPR screens.
DR ChiTaRS; PSMB10; human.
DR GeneWiki; PSMB10; -.
DR GenomeRNAi; 5699; -.
DR Pharos; P40306; Tchem.
DR PRO; PR:P40306; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P40306; protein.
DR Bgee; ENSG00000205220; Expressed in granulocyte and 96 other tissues.
DR ExpressionAtlas; P40306; baseline and differential.
DR Genevisible; P40306; HS.
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; TAS:ProtInc.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; ISS: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:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR034384; Proteasome_beta2/10.
DR InterPro; IPR024689; Proteasome_bsu_C.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF41; PTHR11599:SF41; 1.
DR Pfam; PF12465; Pr_beta_C; 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; Acetylation; Cytoplasm; Host-virus interaction; Hydrolase;
KW Nucleus; Phosphoprotein; Protease; Proteasome; Reference proteome;
KW Threonine protease; Zymogen.
FT PROPEP 1..39
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026651"
FT CHAIN 40..273
FT /note="Proteasome subunit beta type-10"
FT /id="PRO_0000026652"
FT ACT_SITE 40
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 39..40
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O35955"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 14
FT /note="F -> S (in PRAAS5; unknown pathological
FT significance; impaired autocleavage and maturation)"
FT /evidence="ECO:0000269|PubMed:31783057"
FT /id="VAR_085404"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 59..69
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:7AWE"
FT HELIX 88..109
FT /evidence="ECO:0007829|PDB:7AWE"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:7AWE"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:7AWE"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:7AWE"
FT HELIX 187..204
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6E5B"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 221..229
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:7AWE"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:7AWE"
SQ SEQUENCE 273 AA; 28936 MW; D6728E50513A45B9 CRC64;
MLKPALEPRG GFSFENCQRN ASLERVLPGL KVPHARKTGT TIAGLVFQDG VILGADTRAT
NDSVVADKSC EKIHFIAPKI YCCGAGVAAD AEMTTRMVAS KMELHALSTG REPRVATVTR
ILRQTLFRYQ GHVGASLIVG GVDLTGPQLY GVHPHGSYSR LPFTALGSGQ DAALAVLEDR
FQPNMTLEAA QGLLVEAVTA GILGDLGSGG NVDACVITKT GAKLLRTLSS PTEPVKRSGR
YHFVPGTTAV LTQTVKPLTL ELVEETVQAM EVE
