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 27-NOV-2024, entry version 224. 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 {ECO:0000303|PubMed:38503300}; 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). RN [21] RP INVOLVEMENT IN IMD121, AND VARIANTS IMD121 HIS-56 AND ARG-201. RX PubMed=38503300; DOI=10.1016/j.ajhg.2024.02.013; RA van der Made C.I., Kersten S., Chorin O., Engelhardt K.R., Ramakrishnan G., RA Griffin H., Schim van der Loeff I., Venselaar H., Rothschild A.R., RA Segev M., Schuurs-Hoeijmakers J.H.M., Mantere T., Essers R., Esteki M.Z., RA Avital A.L., Loo P.S., Simons A., Pfundt R., Warris A., Seyger M.M., RA van de Veerdonk F.L., Netea M.G., Slatter M.A., Flood T., Gennery A.R., RA Simon A.J., Lev A., Frizinsky S., Barel O., van der Burg M., Somech R., RA Hambleton S., Henriet S.S.V., Hoischen A.; RT "Expanding the PRAAS spectrum: De novo mutations of immunoproteasome RT subunit beta-type 10 in six infants with SCID-Omenn syndrome."; RL Am. J. Hum. Genet. 111:791-804(2024). 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=5; 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 -!- DISEASE: Immunodeficiency 121 with autoinflammation (IMD121) CC [MIM:620807]: An autosomal dominant immunologic disorder characterized CC by severe combined immunodeficiency with T- and B-cell lymphopenia and CC low-normal NK cell numbers, failure to thrive, diarrhea, alopecia, and CC desquamating erythematous rash. Remaining T cells have limited T-cell CC receptor repertoires, a skewed memory phenotype, and an elevated CC CD4/CD8 ratio. Bone marrow examination indicates severely impaired B- CC cell maturation with limited V(D)J recombination. CC {ECO:0000269|PubMed:38503300}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE- CC ProRule:PRU00809}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 9FSV; X-ray; 2.75 A; H/V=43-92. 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 PDBsum; 9FSV; -. DR AlphaFoldDB; P40306; -. DR EMDB; EMD-60139; -. DR EMDB; EMD-7010; -. DR SMR; P40306; -. DR BioGRID; 111672; 91. DR ComplexPortal; CPX-9003; 20S immunoproteasome complex. DR ComplexPortal; CPX-9004; 20S thymoproteasome complex. DR IntAct; P40306; 78. DR MINT; P40306; -. DR STRING; 9606.ENSP00000351314; -. DR BindingDB; P40306; -. DR ChEMBL; CHEMBL3317334; -. DR DrugBank; DB08889; Carfilzomib. DR DrugCentral; P40306; -. 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 jPOST; P40306; -. DR MassIVE; P40306; -. DR PaxDb; 9606-ENSP00000351314; -. DR PeptideAtlas; P40306; -. DR ProteomicsDB; 55360; -. DR Pumba; P40306; -. DR Antibodypedia; 29677; 234 antibodies from 34 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 AGR; HGNC:9538; -. 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 MIM; 620807; 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; GRYHFAP; -. DR OrthoDB; 5485745at2759; -. 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-9824272; Somitogenesis. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; P40306; -. DR SIGNOR; P40306; -. DR BioGRID-ORCS; 5699; 21 hits in 1174 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 97 other cell types or tissues. DR ExpressionAtlas; P40306; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl. DR CDD; cd03763; proteasome_beta_type_7; 1. DR FunFam; 3.60.20.10:FF:000005; Proteasome subunit beta type-2; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR000243; Pept_T1A_subB. 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; PTHR32194; METALLOPROTEASE TLDD; 1. DR PANTHER; PTHR32194:SF4; PROTEASOME SUBUNIT BETA TYPE-7; 1. DR Pfam; PF12465; Pr_beta_C; 1. DR Pfam; PF00227; Proteasome; 1. DR PRINTS; PR00141; PROTEASOME. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 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; Disease variant; KW Host-virus interaction; Hydrolase; Nucleus; Phosphoprotein; Protease; KW Proteasome; Proteomics identification; 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; uncertain significance; impaired FT autocleavage and maturation; dbSNP:rs2058265858)" FT /evidence="ECO:0000269|PubMed:31783057" FT /id="VAR_085404" FT VARIANT 56 FT /note="D -> H (in IMD121; uncertain significance)" FT /evidence="ECO:0000269|PubMed:38503300" FT /id="VAR_089741" FT VARIANT 201 FT /note="G -> R (in IMD121; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:38503300" FT /id="VAR_089742" 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 //