Full text data of PSMB10
PSMB10
(LMP10, MECL1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Proteasome subunit beta type-10; 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; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit beta type-10; 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; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P40306
ID PSB10_HUMAN Reviewed; 273 AA.
AC P40306; B2R5J4; Q5U098;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1995, sequence version 1.
DT 22-JAN-2014, entry version 141.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Tanaka K.;
RT "Newly identified pair of proteasomal subunits regulated reciprocally
RT by 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
RT induction of the human immunoproteasome subunit multicatalytic
RT endopeptidase complex-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.,
RA Kiessling R., Levitskaya J.;
RT "Tumor necrosis factor-alpha induces coordinated changes in major
RT histocompatibility class I presentation pathway, resulting in
RT increased 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
RT antigen-processing machinery during dendritic cell maturation.";
RL Int. Immunol. 13:1515-1523(2001).
RN [11]
RP INTERACTION WITH HIV-1 TAT.
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
RT postulated 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.,
RA Tsuchiya K., Okamoto R., Kanai T., Watanabe M.;
RT "IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted
RT expression 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
RT ulcerative colitis from endoscopic pinch biopsies: insights into
RT distinctive 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
RT in carcinomas via the coordinated action of NF-kappaB and of NF-
RT kappaB-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.,
RA Buerckstuemmer T., 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 MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex
CC which is characterized by its ability to cleave peptides with Arg,
CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. This subunit is involved in antigen processing to
CC generate class I binding peptides.
CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC specificity.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC two 19S regulatory subunits. The 20S proteasome core is composed
CC of 28 subunits that are arranged in four stacked rings, resulting
CC in a barrel-shaped structure. The two end rings are each formed by
CC seven alpha subunits, and the two central rings are each formed by
CC seven beta subunits. The catalytic chamber with the active sites
CC is on the inside of the barrel. This subunit is part of the
CC immunoproteasome where it displaces the equivalent houskeeping
CC subunit PSMB7. Component of the spermatoproteasome, a form of the
CC proteasome specifically found in testis. Interacts with HIV-1 TAT
CC protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- DEVELOPMENTAL STAGE: Highly expressed in immature dendritic cells
CC (at protein level).
CC -!- INDUCTION: Up-regulated by IFNG/IFN-gamma (at protein level). Up-
CC regulated by IRF1. Up-regulated by TNF (at protein level). Up-
CC regulated by tetrodotoxin (TTX) in glial cells. Up-regulated in
CC Crohn's bowel disease (CD). Up-regulated by CD40L via the NFKB1
CC pathway in cancer cells.
CC -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the
CC mature subunit is responsible for the nucleophile proteolytic
CC activity (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 PIR; I38135; I38135.
DR RefSeq; NP_002792.1; NM_002801.3.
DR UniGene; Hs.9661; -.
DR ProteinModelPortal; P40306; -.
DR SMR; P40306; 40-258.
DR IntAct; P40306; 7.
DR STRING; 9606.ENSP00000351314; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.014; -.
DR PhosphoSite; P40306; -.
DR DMDM; 730376; -.
DR OGP; P40306; -.
DR SWISS-2DPAGE; P40306; -.
DR PaxDb; P40306; -.
DR PeptideAtlas; P40306; -.
DR PRIDE; P40306; -.
DR DNASU; 5699; -.
DR Ensembl; ENST00000358514; ENSP00000351314; ENSG00000205220.
DR GeneID; 5699; -.
DR KEGG; hsa:5699; -.
DR UCSC; uc002eux.2; human.
DR CTD; 5699; -.
DR GeneCards; GC16M067968; -.
DR HGNC; HGNC:9538; PSMB10.
DR HPA; HPA030225; -.
DR MIM; 176847; gene.
DR neXtProt; NX_P40306; -.
DR PharmGKB; PA33883; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000182856; -.
DR HOVERGEN; HBG093416; -.
DR InParanoid; P40306; -.
DR KO; K02733; -.
DR OMA; QYRFAPG; -.
DR OrthoDB; EOG7CRTQJ; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMB10; human.
DR GeneWiki; PSMB10; -.
DR GenomeRNAi; 5699; -.
DR NextBio; 22142; -.
DR PRO; PR:P40306; -.
DR ArrayExpress; P40306; -.
DR Bgee; P40306; -.
DR CleanEx; HS_PSMB10; -.
DR Genevestigator; P40306; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
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 Pfam; PF12465; Pr_beta_C; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Host-virus interaction;
KW Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW Threonine protease; Zymogen.
FT PROPEP 1 39 Removed in mature form (By similarity).
FT /FTId=PRO_0000026651.
FT CHAIN 40 273 Proteasome subunit beta type-10.
FT /FTId=PRO_0000026652.
FT ACT_SITE 40 40 Nucleophile (By similarity).
FT SITE 39 40 Cleavage; by autocatalysis (By
FT similarity).
FT MOD_RES 1 1 N-acetylmethionine.
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
//
ID PSB10_HUMAN Reviewed; 273 AA.
AC P40306; B2R5J4; Q5U098;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1995, sequence version 1.
DT 22-JAN-2014, entry version 141.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Tanaka K.;
RT "Newly identified pair of proteasomal subunits regulated reciprocally
RT by 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
RT induction of the human immunoproteasome subunit multicatalytic
RT endopeptidase complex-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.,
RA Kiessling R., Levitskaya J.;
RT "Tumor necrosis factor-alpha induces coordinated changes in major
RT histocompatibility class I presentation pathway, resulting in
RT increased 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
RT antigen-processing machinery during dendritic cell maturation.";
RL Int. Immunol. 13:1515-1523(2001).
RN [11]
RP INTERACTION WITH HIV-1 TAT.
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
RT postulated 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.,
RA Tsuchiya K., Okamoto R., Kanai T., Watanabe M.;
RT "IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted
RT expression 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
RT ulcerative colitis from endoscopic pinch biopsies: insights into
RT distinctive 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
RT in carcinomas via the coordinated action of NF-kappaB and of NF-
RT kappaB-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.,
RA Buerckstuemmer T., 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 MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex
CC which is characterized by its ability to cleave peptides with Arg,
CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. This subunit is involved in antigen processing to
CC generate class I binding peptides.
CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC specificity.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC two 19S regulatory subunits. The 20S proteasome core is composed
CC of 28 subunits that are arranged in four stacked rings, resulting
CC in a barrel-shaped structure. The two end rings are each formed by
CC seven alpha subunits, and the two central rings are each formed by
CC seven beta subunits. The catalytic chamber with the active sites
CC is on the inside of the barrel. This subunit is part of the
CC immunoproteasome where it displaces the equivalent houskeeping
CC subunit PSMB7. Component of the spermatoproteasome, a form of the
CC proteasome specifically found in testis. Interacts with HIV-1 TAT
CC protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- DEVELOPMENTAL STAGE: Highly expressed in immature dendritic cells
CC (at protein level).
CC -!- INDUCTION: Up-regulated by IFNG/IFN-gamma (at protein level). Up-
CC regulated by IRF1. Up-regulated by TNF (at protein level). Up-
CC regulated by tetrodotoxin (TTX) in glial cells. Up-regulated in
CC Crohn's bowel disease (CD). Up-regulated by CD40L via the NFKB1
CC pathway in cancer cells.
CC -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the
CC mature subunit is responsible for the nucleophile proteolytic
CC activity (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 PIR; I38135; I38135.
DR RefSeq; NP_002792.1; NM_002801.3.
DR UniGene; Hs.9661; -.
DR ProteinModelPortal; P40306; -.
DR SMR; P40306; 40-258.
DR IntAct; P40306; 7.
DR STRING; 9606.ENSP00000351314; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.014; -.
DR PhosphoSite; P40306; -.
DR DMDM; 730376; -.
DR OGP; P40306; -.
DR SWISS-2DPAGE; P40306; -.
DR PaxDb; P40306; -.
DR PeptideAtlas; P40306; -.
DR PRIDE; P40306; -.
DR DNASU; 5699; -.
DR Ensembl; ENST00000358514; ENSP00000351314; ENSG00000205220.
DR GeneID; 5699; -.
DR KEGG; hsa:5699; -.
DR UCSC; uc002eux.2; human.
DR CTD; 5699; -.
DR GeneCards; GC16M067968; -.
DR HGNC; HGNC:9538; PSMB10.
DR HPA; HPA030225; -.
DR MIM; 176847; gene.
DR neXtProt; NX_P40306; -.
DR PharmGKB; PA33883; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000182856; -.
DR HOVERGEN; HBG093416; -.
DR InParanoid; P40306; -.
DR KO; K02733; -.
DR OMA; QYRFAPG; -.
DR OrthoDB; EOG7CRTQJ; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMB10; human.
DR GeneWiki; PSMB10; -.
DR GenomeRNAi; 5699; -.
DR NextBio; 22142; -.
DR PRO; PR:P40306; -.
DR ArrayExpress; P40306; -.
DR Bgee; P40306; -.
DR CleanEx; HS_PSMB10; -.
DR Genevestigator; P40306; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
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 Pfam; PF12465; Pr_beta_C; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Host-virus interaction;
KW Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW Threonine protease; Zymogen.
FT PROPEP 1 39 Removed in mature form (By similarity).
FT /FTId=PRO_0000026651.
FT CHAIN 40 273 Proteasome subunit beta type-10.
FT /FTId=PRO_0000026652.
FT ACT_SITE 40 40 Nucleophile (By similarity).
FT SITE 39 40 Cleavage; by autocatalysis (By
FT similarity).
FT MOD_RES 1 1 N-acetylmethionine.
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
//
MIM
176847
*RECORD*
*FIELD* NO
176847
*FIELD* TI
*176847 PROTEASOME SUBUNIT, BETA-TYPE, 10; PSMB10
;;PROTEASOME SUBUNIT MECL1;;
PROTEASOME SUBUNIT BETA-2I
read more*FIELD* TX
CLONING
CpG islands are useful landmarks in the genome for identifying genes. By
database screening, Larsen et al. (1992) found that 57% of human genes
are associated with CpG islands. Sites for rare cutting restriction
enzymes are mainly found in CpG islands. Clustered sites for at least 2
such enzymes are good indicators of a CpG island, and an estimated 78%
of island-associated genes can be located in this way. Guided by
identification of an island in a 40-kb cosmid insert, Larsen et al.
(1993) identified a cluster of 5 unrelated human genes on chromosome
16q22.1. One of the genes encodes a putative subunit of the proteasome
complex, MECL1, an intracellular, multicatalytic proteinase (Goldberg
and Rock, 1992). The derived protein sequence shares about 50% identity
with a putative yeast proteasome subunit and is similar to the sequence
of a peptide fragment from a rat proteasome subunit.
Cruz et al. (1997) characterized a full-length mouse Lmp10 cDNA and
found that Lmp10 encodes a protein of 273 amino acids with a calculated
molecular mass of 29 kD. Northern blot analysis showed that mouse Lmp2
(PSMB9; 177045), Lmp7 (PSMB8; 177046), and Lmp10 were expressed in
heart, liver, thymus, lung, and spleen, but not in brain, kidney,
skeletal muscle, or testis.
GENE FUNCTION
Cruz et al. (1997) found that mouse Lmp2, Lmp7, and Lmp10 were induced
by gamma-interferon (IFNG; 147570).
GENE STRUCTURE
Larsen et al. (1993) determined that the MECL1 gene has 8 exons, covers
2.3 kb, and is transcribed in the same direction as the LCAT gene
(606967), from which it is separated by 3.1 kb.
MAPPING
By sequence analysis, Larsen et al. (1993) mapped the PSMB10 gene to
chromosome 16q22.1. Cruz et al. (1997) found that in mice the Psmb10
gene is present in single copy localized on chromosome 8 in a region of
conserved synteny with human chromosome 16.
ANIMAL MODEL
Basler et al. (2006) generated fertile and viable Mecl1 -/- mice. Flow
cytometric analysis showed that these mice had reduced numbers of
splenic Cd8 (see 186910)-positive T cells. The cytotoxic T lymphocyte
(CTL) response to dominant epitopes of lymphocytic choriomeningitis
virus (LCMV) was impaired in Mecl1 -/- mice. The defect was not
attributable to alterations in antigen presentation, but Mecl1 -/- mice
had reduced numbers of CTLs expressing the V-beta-10 segment of the
T-cell receptor (see 186930), which was prominent in the wildtype
anti-LCMV response. Basler et al. (2006) concluded that MECL1 has a role
in determining the T-cell repertoire for an antiviral T-cell response.
*FIELD* RF
1. Basler, M.; Moebius, J.; Elenich, L.; Groettrup, M.; Monaco, J.
J.: An altered T cell repertoire in MECL-1-deficient mice. J. Immun. 176:
6665-6672, 2006.
2. Cruz, M.; Elenich, L. A.; Smolarek, T. A.; Menon, A. G.; Monaco,
J. J.: DNA sequence, chromosomal localization, and tissue expression
of the mouse proteasome subunit Lmp10 (Psmb10) gene. Genomics 45:
618-622, 1997.
3. Goldberg, A. L.; Rock, K. L.: Proteolysis, proteasomes and antigen
presentation. Nature 357: 375-379, 1992.
4. Larsen, F.; Gundersen, G.; Lopez, R.; Prydz, H.: CpG islands as
gene markers in the human genome. Genomics 13: 1095-1107, 1992.
5. Larsen, F.; Solheim, J.; Kristensen, T.; Kolsto, A.-B.; Prydz,
H.: A tight cluster of five unrelated human genes on chromosome 16q22.1. Hum.
Molec. Genet. 2: 1589-1595, 1993.
*FIELD* CN
Paul J. Converse - updated: 4/4/2007
Victor A. McKusick - updated: 12/10/1997
*FIELD* CD
Victor A. McKusick: 10/18/1993
*FIELD* ED
mgross: 06/25/2007
mgross: 4/10/2007
terry: 4/4/2007
ckniffin: 5/29/2002
dkim: 7/23/1998
mark: 12/18/1997
terry: 12/10/1997
carol: 10/20/1993
carol: 10/19/1993
carol: 10/18/1993
*RECORD*
*FIELD* NO
176847
*FIELD* TI
*176847 PROTEASOME SUBUNIT, BETA-TYPE, 10; PSMB10
;;PROTEASOME SUBUNIT MECL1;;
PROTEASOME SUBUNIT BETA-2I
read more*FIELD* TX
CLONING
CpG islands are useful landmarks in the genome for identifying genes. By
database screening, Larsen et al. (1992) found that 57% of human genes
are associated with CpG islands. Sites for rare cutting restriction
enzymes are mainly found in CpG islands. Clustered sites for at least 2
such enzymes are good indicators of a CpG island, and an estimated 78%
of island-associated genes can be located in this way. Guided by
identification of an island in a 40-kb cosmid insert, Larsen et al.
(1993) identified a cluster of 5 unrelated human genes on chromosome
16q22.1. One of the genes encodes a putative subunit of the proteasome
complex, MECL1, an intracellular, multicatalytic proteinase (Goldberg
and Rock, 1992). The derived protein sequence shares about 50% identity
with a putative yeast proteasome subunit and is similar to the sequence
of a peptide fragment from a rat proteasome subunit.
Cruz et al. (1997) characterized a full-length mouse Lmp10 cDNA and
found that Lmp10 encodes a protein of 273 amino acids with a calculated
molecular mass of 29 kD. Northern blot analysis showed that mouse Lmp2
(PSMB9; 177045), Lmp7 (PSMB8; 177046), and Lmp10 were expressed in
heart, liver, thymus, lung, and spleen, but not in brain, kidney,
skeletal muscle, or testis.
GENE FUNCTION
Cruz et al. (1997) found that mouse Lmp2, Lmp7, and Lmp10 were induced
by gamma-interferon (IFNG; 147570).
GENE STRUCTURE
Larsen et al. (1993) determined that the MECL1 gene has 8 exons, covers
2.3 kb, and is transcribed in the same direction as the LCAT gene
(606967), from which it is separated by 3.1 kb.
MAPPING
By sequence analysis, Larsen et al. (1993) mapped the PSMB10 gene to
chromosome 16q22.1. Cruz et al. (1997) found that in mice the Psmb10
gene is present in single copy localized on chromosome 8 in a region of
conserved synteny with human chromosome 16.
ANIMAL MODEL
Basler et al. (2006) generated fertile and viable Mecl1 -/- mice. Flow
cytometric analysis showed that these mice had reduced numbers of
splenic Cd8 (see 186910)-positive T cells. The cytotoxic T lymphocyte
(CTL) response to dominant epitopes of lymphocytic choriomeningitis
virus (LCMV) was impaired in Mecl1 -/- mice. The defect was not
attributable to alterations in antigen presentation, but Mecl1 -/- mice
had reduced numbers of CTLs expressing the V-beta-10 segment of the
T-cell receptor (see 186930), which was prominent in the wildtype
anti-LCMV response. Basler et al. (2006) concluded that MECL1 has a role
in determining the T-cell repertoire for an antiviral T-cell response.
*FIELD* RF
1. Basler, M.; Moebius, J.; Elenich, L.; Groettrup, M.; Monaco, J.
J.: An altered T cell repertoire in MECL-1-deficient mice. J. Immun. 176:
6665-6672, 2006.
2. Cruz, M.; Elenich, L. A.; Smolarek, T. A.; Menon, A. G.; Monaco,
J. J.: DNA sequence, chromosomal localization, and tissue expression
of the mouse proteasome subunit Lmp10 (Psmb10) gene. Genomics 45:
618-622, 1997.
3. Goldberg, A. L.; Rock, K. L.: Proteolysis, proteasomes and antigen
presentation. Nature 357: 375-379, 1992.
4. Larsen, F.; Gundersen, G.; Lopez, R.; Prydz, H.: CpG islands as
gene markers in the human genome. Genomics 13: 1095-1107, 1992.
5. Larsen, F.; Solheim, J.; Kristensen, T.; Kolsto, A.-B.; Prydz,
H.: A tight cluster of five unrelated human genes on chromosome 16q22.1. Hum.
Molec. Genet. 2: 1589-1595, 1993.
*FIELD* CN
Paul J. Converse - updated: 4/4/2007
Victor A. McKusick - updated: 12/10/1997
*FIELD* CD
Victor A. McKusick: 10/18/1993
*FIELD* ED
mgross: 06/25/2007
mgross: 4/10/2007
terry: 4/4/2007
ckniffin: 5/29/2002
dkim: 7/23/1998
mark: 12/18/1997
terry: 12/10/1997
carol: 10/20/1993
carol: 10/19/1993
carol: 10/18/1993