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Proteasome subunit beta type-10 (EC 3.4.25.1) (Low molecular mass protein 10) (Macropain subunit MECl-1) (Multicatalytic endopeptidase complex subunit MECl-1) (Proteasome MECl-1) (Proteasome subunit beta-2i)

 PSB10_HUMAN             Reviewed;         273 AA.
P40306; B2R5J4; Q5U098;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
25-OCT-2017, entry version 181.
RecName: Full=Proteasome subunit beta type-10;
EC=3.4.25.1;
AltName: Full=Low molecular mass protein 10;
AltName: Full=Macropain subunit MECl-1;
AltName: Full=Multicatalytic endopeptidase complex subunit MECl-1;
AltName: Full=Proteasome MECl-1;
AltName: Full=Proteasome subunit beta-2i;
Flags: Precursor;
Name=PSMB10; Synonyms=LMP10, MECL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8268911; DOI=10.1093/hmg/2.10.1589;
Larsen F., Solheim J., Kristensen T., Kolstoe A.-B., Prydz H.;
"A tight cluster of five unrelated human genes on chromosome
16q22.1.";
Hum. Mol. Genet. 2:1589-1595(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9551082; DOI=10.1016/S0167-4889(97)00152-3;
Foss G.S., Larsen F., Solheim J., Prydz H.;
"Constitutive and interferon-gamma-induced expression of the human
proteasome subunit multicatalytic endopeptidase complex-like 1.";
Biochim. Biophys. Acta 1402:17-28(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=B-cell, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INDUCTION BY IFNG.
PubMed=8666937; DOI=10.1084/jem.183.4.1807;
Hisamatsu H., Shimbara N., Saito Y., Kristensen P., Hendil K.B.,
Fujiwara T., Takahashi E., Tanahashi N., Tamura T., Ichihara A.,
Tanaka K.;
"Newly identified pair of proteasomal subunits regulated reciprocally
by interferon gamma.";
J. Exp. Med. 183:1807-1816(1996).
[8]
INDUCTION BY IFNG AND IRF1.
PubMed=10575004; DOI=10.1074/jbc.274.49.35196;
Foss G.S., Prydz H.;
"Interferon regulatory factor 1 mediates the interferon-gamma
induction of the human immunoproteasome subunit multicatalytic
endopeptidase complex-like 1.";
J. Biol. Chem. 274:35196-35202(1999).
[9]
INDUCTION BY TNF AND IFNG.
PubMed=11493458; DOI=10.1182/blood.V98.4.1108;
Hallermalm K., Seki K., Wei C., Castelli C., Rivoltini L.,
Kiessling R., Levitskaya J.;
"Tumor necrosis factor-alpha induces coordinated changes in major
histocompatibility class I presentation pathway, resulting in
increased stability of class I complexes at the cell surface.";
Blood 98:1108-1115(2001).
[10]
DEVELOPMENTAL STAGE.
PubMed=11717192; DOI=10.1093/intimm/13.12.1515;
Li J., Schuler-Thurner B., Schuler G., Huber C., Seliger B.;
"Bipartite regulation of different components of the MHC class I
antigen-processing machinery during dendritic cell maturation.";
Int. Immunol. 13:1515-1523(2001).
[11]
INTERACTION WITH HIV-1 TAT.
PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
Mayer R.J., Krueger E.;
"Human immunodeficiency virus-1 Tat protein interacts with distinct
proteasomal alpha and beta subunits.";
FEBS Lett. 553:200-204(2003).
[12]
INDUCTION BY TETRODOTOXIN.
PubMed=15501285; DOI=10.1016/j.toxicon.2004.07.018;
Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.;
"Potential effects of tetrodotoxin exposure to human glial cells
postulated using microarray approach.";
Toxicon 44:597-608(2004).
[13]
INDUCTION BY IFNG AND IRF1.
PubMed=15907481; DOI=10.1016/j.febslet.2005.04.012;
Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y.,
Tsuchiya K., Okamoto R., Kanai T., Watanabe M.;
"IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted
expression of immunosubunits of the proteasome.";
FEBS Lett. 579:2781-2787(2005).
[14]
INDUCTION.
PubMed=17262812; DOI=10.1002/ibd.20110;
Wu F., Dassopoulos T., Cope L., Maitra A., Brant S.R., Harris M.L.,
Bayless T.M., Parmigiani G., Chakravarti S.;
"Genome-wide gene expression differences in Crohn's disease and
ulcerative colitis from endoscopic pinch biopsies: insights into
distinctive pathogenesis.";
Inflamm. Bowel Dis. 13:807-821(2007).
[15]
INDUCTION BY CD40L.
PubMed=18694960; DOI=10.1128/MCB.00611-08;
Moschonas A., Kouraki M., Knox P.G., Thymiakou E., Kardassis D.,
Eliopoulos A.G.;
"CD40 induces antigen transporter and immunoproteasome gene expression
in carcinomas via the coordinated action of NF-kappaB and of NF-
kappaB-mediated de novo synthesis of IRF-1.";
Mol. Cell. Biol. 28:6208-6222(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: The proteasome is a multicatalytic proteinase complex
which is characterized by its ability to cleave peptides with Arg,
Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
slightly basic pH. The proteasome has an ATP-dependent proteolytic
activity. This subunit is involved in antigen processing to
generate class I binding peptides.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is composed
of 28 subunits that are arranged in four stacked rings, resulting
in a barrel-shaped structure. The two end rings are each formed by
seven alpha subunits, and the two central rings are each formed by
seven beta subunits. The catalytic chamber with the active sites
is on the inside of the barrel. Component of the immunoproteasome,
where it displaces the equivalent houskeeping subunit PSMB7.
Component of the spermatoproteasome, a form of the proteasome
specifically found in testis. Interacts with HIV-1 TAT protein.
{ECO:0000269|PubMed:14550573}.
-!- INTERACTION:
O95273:CCNDBP1; NbExp=4; IntAct=EBI-603329, EBI-748961;
O43186:CRX; NbExp=3; IntAct=EBI-603329, EBI-748171;
P50222:MEOX2; NbExp=3; IntAct=EBI-603329, EBI-748397;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-
ProRule:PRU00809}. Nucleus {ECO:0000250}.
-!- DEVELOPMENTAL STAGE: Highly expressed in immature dendritic cells
(at protein level). {ECO:0000269|PubMed:11717192}.
-!- INDUCTION: Up-regulated by IFNG/IFN-gamma (at protein level). Up-
regulated by IRF1. Up-regulated by TNF (at protein level). Up-
regulated by tetrodotoxin (TTX) in glial cells. Up-regulated in
Crohn's bowel disease (CD). Up-regulated by CD40L via the NFKB1
pathway in cancer cells. {ECO:0000269|PubMed:10575004,
ECO:0000269|PubMed:11493458, ECO:0000269|PubMed:15501285,
ECO:0000269|PubMed:15907481, ECO:0000269|PubMed:17262812,
ECO:0000269|PubMed:18694960, ECO:0000269|PubMed:8666937}.
-!- PTM: Autocleaved. The resulting N-terminal Thr residue of the
mature subunit is responsible for the nucleophile proteolytic
activity. {ECO:0000250|UniProtKB:O35955}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
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EMBL; X71874; CAA50709.1; -; Genomic_DNA.
EMBL; Y13640; CAA73982.1; -; mRNA.
EMBL; BT019723; AAV38528.1; -; mRNA.
EMBL; BT019724; AAV38529.1; -; mRNA.
EMBL; AK312208; BAG35141.1; -; mRNA.
EMBL; CH471092; EAW83187.1; -; Genomic_DNA.
EMBL; BC017198; AAH17198.1; -; mRNA.
EMBL; BC052369; AAH52369.1; -; mRNA.
CCDS; CCDS10853.1; -.
PIR; I38135; I38135.
RefSeq; NP_002792.1; NM_002801.3.
UniGene; Hs.9661; -.
ProteinModelPortal; P40306; -.
SMR; P40306; -.
BioGrid; 111672; 23.
IntAct; P40306; 11.
STRING; 9606.ENSP00000351314; -.
BindingDB; P40306; -.
ChEMBL; CHEMBL3317334; -.
DrugBank; DB08889; Carfilzomib.
MEROPS; T01.014; -.
iPTMnet; P40306; -.
PhosphoSitePlus; P40306; -.
BioMuta; PSMB10; -.
DMDM; 730376; -.
OGP; P40306; -.
SWISS-2DPAGE; P40306; -.
EPD; P40306; -.
MaxQB; P40306; -.
PaxDb; P40306; -.
PeptideAtlas; P40306; -.
PRIDE; P40306; -.
DNASU; 5699; -.
Ensembl; ENST00000358514; ENSP00000351314; ENSG00000205220.
GeneID; 5699; -.
KEGG; hsa:5699; -.
UCSC; uc002eux.3; human.
CTD; 5699; -.
DisGeNET; 5699; -.
EuPathDB; HostDB:ENSG00000205220.11; -.
GeneCards; PSMB10; -.
HGNC; HGNC:9538; PSMB10.
HPA; CAB034384; -.
HPA; HPA030224; -.
HPA; HPA030225; -.
MIM; 176847; gene.
neXtProt; NX_P40306; -.
OpenTargets; ENSG00000205220; -.
PharmGKB; PA33883; -.
eggNOG; KOG0173; Eukaryota.
eggNOG; COG0638; LUCA.
GeneTree; ENSGT00510000046533; -.
HOGENOM; HOG000182856; -.
HOVERGEN; HBG093416; -.
InParanoid; P40306; -.
KO; K02733; -.
OMA; QTLFRYR; -.
OrthoDB; EOG091G0E5S; -.
PhylomeDB; P40306; -.
TreeFam; TF106222; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSMB10; human.
GeneWiki; PSMB10; -.
GenomeRNAi; 5699; -.
PRO; PR:P40306; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000205220; -.
CleanEx; HS_PSMB10; -.
ExpressionAtlas; P40306; baseline and differential.
Genevisible; P40306; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000502; C:proteasome complex; TAS:ProtInc.
GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000243; Pept_T1A_subB.
InterPro; IPR034384; Proteasome_beta10.
InterPro; IPR024689; Proteasome_bsu_C.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF41; PTHR11599:SF41; 1.
Pfam; PF12465; Pr_beta_C; 1.
Pfam; PF00227; Proteasome; 1.
PRINTS; PR00141; PROTEASOME.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Host-virus interaction;
Hydrolase; Nucleus; Phosphoprotein; Protease; Proteasome;
Reference proteome; Threonine protease; Zymogen.
PROPEP 1 39 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000026651.
CHAIN 40 273 Proteasome subunit beta type-10.
/FTId=PRO_0000026652.
ACT_SITE 40 40 Nucleophile. {ECO:0000250}.
SITE 39 40 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:O35955}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
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


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