Full text data of PSMA2
PSMA2
(HC3, PSC3)
[Confidence: high (present in two of the MS resources)]
Proteasome subunit alpha type-2; 3.4.25.1 (Macropain subunit C3; Multicatalytic endopeptidase complex subunit C3; Proteasome component C3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit alpha type-2; 3.4.25.1 (Macropain subunit C3; Multicatalytic endopeptidase complex subunit C3; Proteasome component C3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00219622
IPI00219622 Proteasome alPha 2 subunit Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00219622 Proteasome alPha 2 subunit Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P25787
ID PSA2_HUMAN Reviewed; 234 AA.
AC P25787; Q6ICS6; Q9BU45;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 150.
DE RecName: Full=Proteasome subunit alpha type-2;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit C3;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C3;
DE AltName: Full=Proteasome component C3;
GN Name=PSMA2; Synonyms=HC3, PSC3;
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 [MRNA].
RX PubMed=2025653; DOI=10.1016/0167-4781(91)90090-9;
RA Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H.,
RA Tanaka K., Ichihara A.;
RT "Molecular cloning and sequence analysis of cDNAs for five major
RT subunits of human proteasomes (multi-catalytic proteinase
RT complexes).";
RL Biochim. Biophys. Acta 1089:95-102(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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=Lung, and Uterus;
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 PROTEIN SEQUENCE OF 5-39; 71-84; 93-113 AND 178-196, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 5-14.
RX PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
RA Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
RT "Human proteasome subunits from 2-dimensional gels identified by
RT partial sequencing.";
RL Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
RN [9]
RP INDUCTION BY BO-653 AND PROBUCOL.
RX PubMed=11521686;
RA Takabe W., Mataki C., Wada Y., Ishii M., Izumi A., Aburatani H.,
RA Hamakubo T., Niki E., Kodama T., Noguchi N.;
RT "Gene expression induced by BO-653, probucol and BHQ in human
RT endothelial cells.";
RL J. Atheroscler. Thromb. 7:223-230(2000).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-229, AND MASS SPECTROMETRY.
RC TISSUE=Pituitary adenoma;
RX PubMed=16777052; DOI=10.1016/j.ab.2006.05.024;
RA Zhan X., Desiderio D.M.;
RT "Nitroproteins from a human pituitary adenoma tissue discovered with a
RT nitrotyrosine affinity column and tandem mass spectrometry.";
RL Anal. Biochem. 354:279-289(2006).
RN [12]
RP INDUCTION, AND MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
RT reveal differential cellular gene expression in response to
RT enterovirus 71 infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-171, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
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 [16]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-110.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
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. PSMA2 may have a potential regulatory effect on another
CC component(s) of the proteasome complex through tyrosine
CC phosphorylation.
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.
CC -!- INTERACTION:
CC P25786:PSMA1; NbExp=5; IntAct=EBI-603262, EBI-359352;
CC P25789:PSMA4; NbExp=7; IntAct=EBI-603262, EBI-359310;
CC P60900:PSMA6; NbExp=5; IntAct=EBI-603262, EBI-357793;
CC O14818:PSMA7; NbExp=5; IntAct=EBI-603262, EBI-603272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body (By
CC similarity). Note=Colocalizes with TRIM5 in the cytoplasmic bodies
CC (By similarity).
CC -!- INDUCTION: Down-regulated by antioxidants BO-653 and probucol.
CC Down-regulated in response to enterovirus 71 (EV71) infection (at
CC protein level).
CC -!- PTM: Phosphorylated on tyrosine residues; which may be important
CC for nuclear import (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; D00760; BAA00657.1; -; mRNA.
DR EMBL; AK290654; BAF83343.1; -; mRNA.
DR EMBL; CR450317; CAG29313.1; -; mRNA.
DR EMBL; CH236951; EAL24005.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW94152.1; -; Genomic_DNA.
DR EMBL; BC002900; AAH02900.2; -; mRNA.
DR EMBL; BC047697; AAH47697.1; -; mRNA.
DR PIR; S15970; SNHUC3.
DR RefSeq; NP_002778.1; NM_002787.4.
DR UniGene; Hs.333786; -.
DR ProteinModelPortal; P25787; -.
DR SMR; P25787; 2-234.
DR IntAct; P25787; 24.
DR MINT; MINT-1178435; -.
DR STRING; 9606.ENSP00000223321; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.972; -.
DR PhosphoSite; P25787; -.
DR DMDM; 130850; -.
DR OGP; P25787; -.
DR REPRODUCTION-2DPAGE; IPI00219622; -.
DR PaxDb; P25787; -.
DR PeptideAtlas; P25787; -.
DR PRIDE; P25787; -.
DR DNASU; 5683; -.
DR Ensembl; ENST00000223321; ENSP00000223321; ENSG00000106588.
DR GeneID; 5683; -.
DR KEGG; hsa:5683; -.
DR UCSC; uc003thy.3; human.
DR CTD; 5683; -.
DR GeneCards; GC07M042956; -.
DR HGNC; HGNC:9531; PSMA2.
DR HPA; HPA008188; -.
DR MIM; 176842; gene.
DR neXtProt; NX_P25787; -.
DR PharmGKB; PA33876; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091085; -.
DR HOVERGEN; HBG003005; -.
DR InParanoid; P25787; -.
DR KO; K02726; -.
DR OMA; WKATALG; -.
DR OrthoDB; EOG71VSTG; -.
DR PhylomeDB; P25787; -.
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 GeneWiki; PSMA2; -.
DR GenomeRNAi; 5683; -.
DR NextBio; 22068; -.
DR PRO; PR:P25787; -.
DR ArrayExpress; P25787; -.
DR Bgee; P25787; -.
DR CleanEx; HS_PSMA2; -.
DR Genevestigator; P25787; -.
DR GO; GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
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:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro.
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: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: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:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR023332; Proteasome_suA-type.
DR InterPro; IPR001353; Proteasome_sua/b.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Nitration; Nucleus; Phosphoprotein; Polymorphism; Protease;
KW Proteasome; Reference proteome; Threonine protease.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 234 Proteasome subunit alpha type-2.
FT /FTId=PRO_0000124077.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT MOD_RES 70 70 N6-acetyllysine.
FT MOD_RES 76 76 Phosphotyrosine (By similarity).
FT MOD_RES 171 171 N6-acetyllysine.
FT MOD_RES 229 229 Nitrated tyrosine.
FT VARIANT 110 110 L -> V (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036278.
SQ SEQUENCE 234 AA; 25899 MW; 63CB56A233583836 CRC64;
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER
SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE
YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE
DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVKDYL AAIA
//
ID PSA2_HUMAN Reviewed; 234 AA.
AC P25787; Q6ICS6; Q9BU45;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 150.
DE RecName: Full=Proteasome subunit alpha type-2;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit C3;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C3;
DE AltName: Full=Proteasome component C3;
GN Name=PSMA2; Synonyms=HC3, PSC3;
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 [MRNA].
RX PubMed=2025653; DOI=10.1016/0167-4781(91)90090-9;
RA Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H.,
RA Tanaka K., Ichihara A.;
RT "Molecular cloning and sequence analysis of cDNAs for five major
RT subunits of human proteasomes (multi-catalytic proteinase
RT complexes).";
RL Biochim. Biophys. Acta 1089:95-102(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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=Lung, and Uterus;
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 PROTEIN SEQUENCE OF 5-39; 71-84; 93-113 AND 178-196, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 5-14.
RX PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
RA Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
RT "Human proteasome subunits from 2-dimensional gels identified by
RT partial sequencing.";
RL Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
RN [9]
RP INDUCTION BY BO-653 AND PROBUCOL.
RX PubMed=11521686;
RA Takabe W., Mataki C., Wada Y., Ishii M., Izumi A., Aburatani H.,
RA Hamakubo T., Niki E., Kodama T., Noguchi N.;
RT "Gene expression induced by BO-653, probucol and BHQ in human
RT endothelial cells.";
RL J. Atheroscler. Thromb. 7:223-230(2000).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-229, AND MASS SPECTROMETRY.
RC TISSUE=Pituitary adenoma;
RX PubMed=16777052; DOI=10.1016/j.ab.2006.05.024;
RA Zhan X., Desiderio D.M.;
RT "Nitroproteins from a human pituitary adenoma tissue discovered with a
RT nitrotyrosine affinity column and tandem mass spectrometry.";
RL Anal. Biochem. 354:279-289(2006).
RN [12]
RP INDUCTION, AND MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
RT reveal differential cellular gene expression in response to
RT enterovirus 71 infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-171, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
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 [16]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-110.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
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. PSMA2 may have a potential regulatory effect on another
CC component(s) of the proteasome complex through tyrosine
CC phosphorylation.
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.
CC -!- INTERACTION:
CC P25786:PSMA1; NbExp=5; IntAct=EBI-603262, EBI-359352;
CC P25789:PSMA4; NbExp=7; IntAct=EBI-603262, EBI-359310;
CC P60900:PSMA6; NbExp=5; IntAct=EBI-603262, EBI-357793;
CC O14818:PSMA7; NbExp=5; IntAct=EBI-603262, EBI-603272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body (By
CC similarity). Note=Colocalizes with TRIM5 in the cytoplasmic bodies
CC (By similarity).
CC -!- INDUCTION: Down-regulated by antioxidants BO-653 and probucol.
CC Down-regulated in response to enterovirus 71 (EV71) infection (at
CC protein level).
CC -!- PTM: Phosphorylated on tyrosine residues; which may be important
CC for nuclear import (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; D00760; BAA00657.1; -; mRNA.
DR EMBL; AK290654; BAF83343.1; -; mRNA.
DR EMBL; CR450317; CAG29313.1; -; mRNA.
DR EMBL; CH236951; EAL24005.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW94152.1; -; Genomic_DNA.
DR EMBL; BC002900; AAH02900.2; -; mRNA.
DR EMBL; BC047697; AAH47697.1; -; mRNA.
DR PIR; S15970; SNHUC3.
DR RefSeq; NP_002778.1; NM_002787.4.
DR UniGene; Hs.333786; -.
DR ProteinModelPortal; P25787; -.
DR SMR; P25787; 2-234.
DR IntAct; P25787; 24.
DR MINT; MINT-1178435; -.
DR STRING; 9606.ENSP00000223321; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.972; -.
DR PhosphoSite; P25787; -.
DR DMDM; 130850; -.
DR OGP; P25787; -.
DR REPRODUCTION-2DPAGE; IPI00219622; -.
DR PaxDb; P25787; -.
DR PeptideAtlas; P25787; -.
DR PRIDE; P25787; -.
DR DNASU; 5683; -.
DR Ensembl; ENST00000223321; ENSP00000223321; ENSG00000106588.
DR GeneID; 5683; -.
DR KEGG; hsa:5683; -.
DR UCSC; uc003thy.3; human.
DR CTD; 5683; -.
DR GeneCards; GC07M042956; -.
DR HGNC; HGNC:9531; PSMA2.
DR HPA; HPA008188; -.
DR MIM; 176842; gene.
DR neXtProt; NX_P25787; -.
DR PharmGKB; PA33876; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091085; -.
DR HOVERGEN; HBG003005; -.
DR InParanoid; P25787; -.
DR KO; K02726; -.
DR OMA; WKATALG; -.
DR OrthoDB; EOG71VSTG; -.
DR PhylomeDB; P25787; -.
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 GeneWiki; PSMA2; -.
DR GenomeRNAi; 5683; -.
DR NextBio; 22068; -.
DR PRO; PR:P25787; -.
DR ArrayExpress; P25787; -.
DR Bgee; P25787; -.
DR CleanEx; HS_PSMA2; -.
DR Genevestigator; P25787; -.
DR GO; GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
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:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro.
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: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: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:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR023332; Proteasome_suA-type.
DR InterPro; IPR001353; Proteasome_sua/b.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Nitration; Nucleus; Phosphoprotein; Polymorphism; Protease;
KW Proteasome; Reference proteome; Threonine protease.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 234 Proteasome subunit alpha type-2.
FT /FTId=PRO_0000124077.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT MOD_RES 70 70 N6-acetyllysine.
FT MOD_RES 76 76 Phosphotyrosine (By similarity).
FT MOD_RES 171 171 N6-acetyllysine.
FT MOD_RES 229 229 Nitrated tyrosine.
FT VARIANT 110 110 L -> V (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036278.
SQ SEQUENCE 234 AA; 25899 MW; 63CB56A233583836 CRC64;
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER
SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE
YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE
DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVKDYL AAIA
//
MIM
176842
*RECORD*
*FIELD* NO
176842
*FIELD* TI
*176842 PROTEASOME SUBUNIT, ALPHA-TYPE, 2; PSMA2
;;HC3;;
PSC2
*FIELD* TX
Proteasomes (multicatalytic proteinase complexes) are symmetric,
read morering-shaped or cylindrical cytoplasmic particles with the unusually
large size of 20S (Mr approximately 750,000). They are composed of
polysubunits of similar sizes (Mr 21,000-32,000) but different charges.
They are ubiquitously distributed in eukaryotic cells at considerably
high concentrations, suggesting their general importance in cellular
functions. Proteasomes have been demonstrated to catalyze an
energy-dependent degradative process in a nonlysosomal pathway. Tamura
et al. (1991) reported molecular cloning and sequencing of full-length
cDNAs for 5 subunits of proteasomes which they symbolized HC2 (602854),
HC3, HC5 (602017), HC8 (176843), and HC9 (PSMA4; 176846). The
proteasomes of human liver were studied with description of their
structure and homology with the subunits of proteasomes from other
species. The 5 subunits had 263, 234, 241, 255, and 261 amino acid
residues and calculated molecular weights of 29,554, 25,897, 26,847,
28,431, and 29,482, respectively. They were encoded by single
independent genes. Most of the genes for proteasome components are
highly homologous and their proteins show approximately 30% identity in
amino acid sequence. The exception is component 5 (PSMA5; 176844), which
may have diverged in eukaryotes during evolution.
Tamura et al. (1994) isolated 2 human proteasome genes encoding the
alpha-type HC3 and the beta-type HC5 subunits. Analysis of their
promoter sequences revealed the absence of TATA and CAAT elements and
the existence of 2 or 3 GC boxes that function coordinately as promoters
of the 2 genes. Differences in the exon/intron organizations of these
genes, however, suggested that they diverged at an early stage of
evolution.
Okumura et al. (1995) mapped the PSMA2 gene to 6q27 by fluorescence in
situ hybridization.
*FIELD* RF
1. Okumura, K.; Nogami, M.; Taguchi, H.; Hisamatsu, H.; Tanaka, K.
: The genes for the alpha-type HC3 (PMSA2) and beta-type HC5 (PMSB1)
subunits of human proteasomes map to chromosomes 6q27 and 7p12-p13
by fluorescence in situ hybridization. Genomics 27: 377-379, 1995.
2. Tamura, T.; Lee, D. H.; Osaka, F.; Fujiwara, T.; Shin, S.; Chung,
C. H.; Tanaka, K.; Ichihara, A.: Molecular cloning and sequence analysis
of cDNAs for five major subunits of human proteasomes (multi-catalytic
proteinase complexes). Biochim. Biophys. Acta 1089: 95-102, 1991.
3. Tamura, T.; Osaka, F.; Kawamura, Y.; Higuti, T.; Ishida, N.; Nothwang,
H.-G.; Tsurumi, C.; Tanaka, K.; Ichihara, A.: Isolation and characterization
of alpha-type HC3 and beta-type HC5 subunit genes of human proteasomes. J.
Molec. Biol. 244: 117-124, 1994.
*FIELD* CD
Victor A. McKusick: 7/10/1991
*FIELD* ED
terry: 05/27/2010
terry: 12/17/2009
mgross: 8/28/2007
alopez: 7/16/1998
alopez: 3/18/1998
mark: 8/11/1995
supermim: 3/16/1992
carol: 7/22/1991
carol: 7/12/1991
carol: 7/10/1991
*RECORD*
*FIELD* NO
176842
*FIELD* TI
*176842 PROTEASOME SUBUNIT, ALPHA-TYPE, 2; PSMA2
;;HC3;;
PSC2
*FIELD* TX
Proteasomes (multicatalytic proteinase complexes) are symmetric,
read morering-shaped or cylindrical cytoplasmic particles with the unusually
large size of 20S (Mr approximately 750,000). They are composed of
polysubunits of similar sizes (Mr 21,000-32,000) but different charges.
They are ubiquitously distributed in eukaryotic cells at considerably
high concentrations, suggesting their general importance in cellular
functions. Proteasomes have been demonstrated to catalyze an
energy-dependent degradative process in a nonlysosomal pathway. Tamura
et al. (1991) reported molecular cloning and sequencing of full-length
cDNAs for 5 subunits of proteasomes which they symbolized HC2 (602854),
HC3, HC5 (602017), HC8 (176843), and HC9 (PSMA4; 176846). The
proteasomes of human liver were studied with description of their
structure and homology with the subunits of proteasomes from other
species. The 5 subunits had 263, 234, 241, 255, and 261 amino acid
residues and calculated molecular weights of 29,554, 25,897, 26,847,
28,431, and 29,482, respectively. They were encoded by single
independent genes. Most of the genes for proteasome components are
highly homologous and their proteins show approximately 30% identity in
amino acid sequence. The exception is component 5 (PSMA5; 176844), which
may have diverged in eukaryotes during evolution.
Tamura et al. (1994) isolated 2 human proteasome genes encoding the
alpha-type HC3 and the beta-type HC5 subunits. Analysis of their
promoter sequences revealed the absence of TATA and CAAT elements and
the existence of 2 or 3 GC boxes that function coordinately as promoters
of the 2 genes. Differences in the exon/intron organizations of these
genes, however, suggested that they diverged at an early stage of
evolution.
Okumura et al. (1995) mapped the PSMA2 gene to 6q27 by fluorescence in
situ hybridization.
*FIELD* RF
1. Okumura, K.; Nogami, M.; Taguchi, H.; Hisamatsu, H.; Tanaka, K.
: The genes for the alpha-type HC3 (PMSA2) and beta-type HC5 (PMSB1)
subunits of human proteasomes map to chromosomes 6q27 and 7p12-p13
by fluorescence in situ hybridization. Genomics 27: 377-379, 1995.
2. Tamura, T.; Lee, D. H.; Osaka, F.; Fujiwara, T.; Shin, S.; Chung,
C. H.; Tanaka, K.; Ichihara, A.: Molecular cloning and sequence analysis
of cDNAs for five major subunits of human proteasomes (multi-catalytic
proteinase complexes). Biochim. Biophys. Acta 1089: 95-102, 1991.
3. Tamura, T.; Osaka, F.; Kawamura, Y.; Higuti, T.; Ishida, N.; Nothwang,
H.-G.; Tsurumi, C.; Tanaka, K.; Ichihara, A.: Isolation and characterization
of alpha-type HC3 and beta-type HC5 subunit genes of human proteasomes. J.
Molec. Biol. 244: 117-124, 1994.
*FIELD* CD
Victor A. McKusick: 7/10/1991
*FIELD* ED
terry: 05/27/2010
terry: 12/17/2009
mgross: 8/28/2007
alopez: 7/16/1998
alopez: 3/18/1998
mark: 8/11/1995
supermim: 3/16/1992
carol: 7/22/1991
carol: 7/12/1991
carol: 7/10/1991