Full text data of PSMA6
PSMA6
(PROS27)
[Confidence: high (present in two of the MS resources)]
Proteasome subunit alpha type-6; 3.4.25.1 (27 kDa prosomal protein; PROS-27; p27K; Macropain iota chain; Multicatalytic endopeptidase complex iota chain; Proteasome iota chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit alpha type-6; 3.4.25.1 (27 kDa prosomal protein; PROS-27; p27K; Macropain iota chain; Multicatalytic endopeptidase complex iota chain; Proteasome iota chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00029623
IPI00029623 Proteasome subunit alpha type 6 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
IPI00029623 Proteasome subunit alpha type 6 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
P60900
ID PSA6_HUMAN Reviewed; 246 AA.
AC P60900; B2R7J9; P34062; Q6IB60;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-APR-2004, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Proteasome subunit alpha type-6;
DE EC=3.4.25.1;
DE AltName: Full=27 kDa prosomal protein;
DE Short=PROS-27;
DE Short=p27K;
DE AltName: Full=Macropain iota chain;
DE AltName: Full=Multicatalytic endopeptidase complex iota chain;
DE AltName: Full=Proteasome iota chain;
GN Name=PSMA6; Synonyms=PROS27;
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=7681138; DOI=10.1007/BF00282801;
RA Bey F., Pereira I.S., Coux O., Viegas-Pequignot E., Targa F.R.,
RA Nothwang H.G., Dutrillaux B., Scherrer K.;
RT "The prosomal RNA-binding protein p27K is a member of the alpha-type
RT human prosomal gene family.";
RL Mol. Gen. Genet. 237:193-205(1993).
RN [2]
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lymph, Skeletal muscle, and Skin;
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 [6]
RP PROTEIN SEQUENCE OF 12-43; 60-88; 105-116; 154-164; 172-181 AND
RP 229-246, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-246, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1888762; DOI=10.1016/0167-4838(91)90020-Z;
RA DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z.,
RA Moomaw C.R., Dawson P.A., Slaughter C.A.;
RT "The primary structures of four subunits of the human, high-molecular-
RT weight proteinase, macropain (proteasome), are distinct but
RT homologous.";
RL Biochim. Biophys. Acta 1079:29-38(1991).
RN [8]
RP PARTIAL PROTEIN SEQUENCE.
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 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 [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-59, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-104, 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 [12]
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 [13]
RP INTERACTION WITH ALKBH4.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M.,
RA Meza-Zepeda L.A., Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(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.
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. Interacts with ALKBH4.
CC -!- INTERACTION:
CC P25787:PSMA2; NbExp=5; IntAct=EBI-357793, EBI-603262;
CC P25788:PSMA3; NbExp=4; IntAct=EBI-357793, EBI-348380;
CC P25789:PSMA4; NbExp=4; IntAct=EBI-357793, EBI-359310;
CC O14818:PSMA7; NbExp=11; IntAct=EBI-357793, EBI-603272;
CC Q9Y5K5:UCHL5; NbExp=4; IntAct=EBI-357793, EBI-1051183;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body (By
CC similarity). Note=Colocalizes with TRIM5 in the cytoplasmic bodies
CC (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; X59417; CAA42052.1; -; mRNA.
DR EMBL; CR456944; CAG33225.1; -; mRNA.
DR EMBL; AK313011; BAG35846.1; -; mRNA.
DR EMBL; CH471078; EAW65877.1; -; Genomic_DNA.
DR EMBL; BC002979; AAH02979.1; -; mRNA.
DR EMBL; BC017882; AAH17882.1; -; mRNA.
DR EMBL; BC022354; AAH22354.1; -; mRNA.
DR EMBL; BC023659; AAH23659.1; -; mRNA.
DR EMBL; BC070137; AAH70137.1; -; mRNA.
DR EMBL; X61972; CAA43964.1; -; mRNA.
DR PIR; S30274; S30274.
DR RefSeq; NP_001269161.1; NM_001282232.1.
DR RefSeq; NP_002782.1; NM_002791.2.
DR UniGene; Hs.446260; -.
DR ProteinModelPortal; P60900; -.
DR SMR; P60900; 2-245.
DR DIP; DIP-29367N; -.
DR IntAct; P60900; 28.
DR MINT; MINT-5001118; -.
DR STRING; 9606.ENSP00000261479; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.971; -.
DR PhosphoSite; P60900; -.
DR DMDM; 46397659; -.
DR REPRODUCTION-2DPAGE; IPI00029623; -.
DR SWISS-2DPAGE; P60900; -.
DR UCD-2DPAGE; P60900; -.
DR PaxDb; P60900; -.
DR PeptideAtlas; P60900; -.
DR PRIDE; P60900; -.
DR DNASU; 5687; -.
DR Ensembl; ENST00000261479; ENSP00000261479; ENSG00000100902.
DR GeneID; 5687; -.
DR KEGG; hsa:5687; -.
DR UCSC; uc001wtd.3; human.
DR CTD; 5687; -.
DR GeneCards; GC14P035747; -.
DR HGNC; HGNC:9535; PSMA6.
DR HPA; HPA003049; -.
DR MIM; 602855; gene.
DR neXtProt; NX_P60900; -.
DR PharmGKB; PA33880; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091084; -.
DR HOVERGEN; HBG107363; -.
DR InParanoid; P60900; -.
DR KO; K02730; -.
DR PhylomeDB; P60900; -.
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; PSMA6; -.
DR GenomeRNAi; 5687; -.
DR NextBio; 22090; -.
DR PRO; PR:P60900; -.
DR ArrayExpress; P60900; -.
DR Bgee; P60900; -.
DR CleanEx; HS_PSMA6; -.
DR Genevestigator; P60900; -.
DR GO; GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005844; C:polysome; IDA:BHF-UCL.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:BHF-UCL.
DR GO; GO:0030017; C:sarcomere; ISS:BHF-UCL.
DR GO; GO:0004175; F:endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0035639; F:purine ribonucleoside triphosphate binding; NAS:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; NAS: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: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:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
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:0050727; P:regulation of inflammatory response; IC:BHF-UCL.
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 Glycoprotein; Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein;
KW Polymorphism; Protease; Proteasome; Reference proteome;
KW Threonine protease; Ubl conjugation.
FT CHAIN 1 246 Proteasome subunit alpha type-6.
FT /FTId=PRO_0000124130.
FT MOD_RES 102 102 N6-acetyllysine.
FT MOD_RES 104 104 N6-acetyllysine.
FT MOD_RES 159 159 Phosphotyrosine (By similarity).
FT CARBOHYD 5 5 O-linked (GlcNAc) (By similarity).
FT CROSSLNK 59 59 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VARIANT 233 233 A -> S (in dbSNP:rs15434).
FT /FTId=VAR_051546.
FT CONFLICT 59 59 K -> C (in Ref. 7; CAA43964).
SQ SEQUENCE 246 AA; 27399 MW; 94D1FD3C0A7CC72A CRC64;
MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL
LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD
ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY CGFKATAAGV KQTESTSFLE
KKVKKKFDWT FEQTVETAIT CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV
ALAERD
//
ID PSA6_HUMAN Reviewed; 246 AA.
AC P60900; B2R7J9; P34062; Q6IB60;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-APR-2004, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Proteasome subunit alpha type-6;
DE EC=3.4.25.1;
DE AltName: Full=27 kDa prosomal protein;
DE Short=PROS-27;
DE Short=p27K;
DE AltName: Full=Macropain iota chain;
DE AltName: Full=Multicatalytic endopeptidase complex iota chain;
DE AltName: Full=Proteasome iota chain;
GN Name=PSMA6; Synonyms=PROS27;
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=7681138; DOI=10.1007/BF00282801;
RA Bey F., Pereira I.S., Coux O., Viegas-Pequignot E., Targa F.R.,
RA Nothwang H.G., Dutrillaux B., Scherrer K.;
RT "The prosomal RNA-binding protein p27K is a member of the alpha-type
RT human prosomal gene family.";
RL Mol. Gen. Genet. 237:193-205(1993).
RN [2]
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lymph, Skeletal muscle, and Skin;
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 [6]
RP PROTEIN SEQUENCE OF 12-43; 60-88; 105-116; 154-164; 172-181 AND
RP 229-246, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-246, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1888762; DOI=10.1016/0167-4838(91)90020-Z;
RA DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z.,
RA Moomaw C.R., Dawson P.A., Slaughter C.A.;
RT "The primary structures of four subunits of the human, high-molecular-
RT weight proteinase, macropain (proteasome), are distinct but
RT homologous.";
RL Biochim. Biophys. Acta 1079:29-38(1991).
RN [8]
RP PARTIAL PROTEIN SEQUENCE.
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 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 [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-59, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-104, 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 [12]
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 [13]
RP INTERACTION WITH ALKBH4.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M.,
RA Meza-Zepeda L.A., Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(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.
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. Interacts with ALKBH4.
CC -!- INTERACTION:
CC P25787:PSMA2; NbExp=5; IntAct=EBI-357793, EBI-603262;
CC P25788:PSMA3; NbExp=4; IntAct=EBI-357793, EBI-348380;
CC P25789:PSMA4; NbExp=4; IntAct=EBI-357793, EBI-359310;
CC O14818:PSMA7; NbExp=11; IntAct=EBI-357793, EBI-603272;
CC Q9Y5K5:UCHL5; NbExp=4; IntAct=EBI-357793, EBI-1051183;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body (By
CC similarity). Note=Colocalizes with TRIM5 in the cytoplasmic bodies
CC (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; X59417; CAA42052.1; -; mRNA.
DR EMBL; CR456944; CAG33225.1; -; mRNA.
DR EMBL; AK313011; BAG35846.1; -; mRNA.
DR EMBL; CH471078; EAW65877.1; -; Genomic_DNA.
DR EMBL; BC002979; AAH02979.1; -; mRNA.
DR EMBL; BC017882; AAH17882.1; -; mRNA.
DR EMBL; BC022354; AAH22354.1; -; mRNA.
DR EMBL; BC023659; AAH23659.1; -; mRNA.
DR EMBL; BC070137; AAH70137.1; -; mRNA.
DR EMBL; X61972; CAA43964.1; -; mRNA.
DR PIR; S30274; S30274.
DR RefSeq; NP_001269161.1; NM_001282232.1.
DR RefSeq; NP_002782.1; NM_002791.2.
DR UniGene; Hs.446260; -.
DR ProteinModelPortal; P60900; -.
DR SMR; P60900; 2-245.
DR DIP; DIP-29367N; -.
DR IntAct; P60900; 28.
DR MINT; MINT-5001118; -.
DR STRING; 9606.ENSP00000261479; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.971; -.
DR PhosphoSite; P60900; -.
DR DMDM; 46397659; -.
DR REPRODUCTION-2DPAGE; IPI00029623; -.
DR SWISS-2DPAGE; P60900; -.
DR UCD-2DPAGE; P60900; -.
DR PaxDb; P60900; -.
DR PeptideAtlas; P60900; -.
DR PRIDE; P60900; -.
DR DNASU; 5687; -.
DR Ensembl; ENST00000261479; ENSP00000261479; ENSG00000100902.
DR GeneID; 5687; -.
DR KEGG; hsa:5687; -.
DR UCSC; uc001wtd.3; human.
DR CTD; 5687; -.
DR GeneCards; GC14P035747; -.
DR HGNC; HGNC:9535; PSMA6.
DR HPA; HPA003049; -.
DR MIM; 602855; gene.
DR neXtProt; NX_P60900; -.
DR PharmGKB; PA33880; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091084; -.
DR HOVERGEN; HBG107363; -.
DR InParanoid; P60900; -.
DR KO; K02730; -.
DR PhylomeDB; P60900; -.
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; PSMA6; -.
DR GenomeRNAi; 5687; -.
DR NextBio; 22090; -.
DR PRO; PR:P60900; -.
DR ArrayExpress; P60900; -.
DR Bgee; P60900; -.
DR CleanEx; HS_PSMA6; -.
DR Genevestigator; P60900; -.
DR GO; GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005844; C:polysome; IDA:BHF-UCL.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:BHF-UCL.
DR GO; GO:0030017; C:sarcomere; ISS:BHF-UCL.
DR GO; GO:0004175; F:endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0035639; F:purine ribonucleoside triphosphate binding; NAS:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; NAS: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: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:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
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:0050727; P:regulation of inflammatory response; IC:BHF-UCL.
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 Glycoprotein; Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein;
KW Polymorphism; Protease; Proteasome; Reference proteome;
KW Threonine protease; Ubl conjugation.
FT CHAIN 1 246 Proteasome subunit alpha type-6.
FT /FTId=PRO_0000124130.
FT MOD_RES 102 102 N6-acetyllysine.
FT MOD_RES 104 104 N6-acetyllysine.
FT MOD_RES 159 159 Phosphotyrosine (By similarity).
FT CARBOHYD 5 5 O-linked (GlcNAc) (By similarity).
FT CROSSLNK 59 59 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VARIANT 233 233 A -> S (in dbSNP:rs15434).
FT /FTId=VAR_051546.
FT CONFLICT 59 59 K -> C (in Ref. 7; CAA43964).
SQ SEQUENCE 246 AA; 27399 MW; 94D1FD3C0A7CC72A CRC64;
MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL
LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD
ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY CGFKATAAGV KQTESTSFLE
KKVKKKFDWT FEQTVETAIT CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV
ALAERD
//
MIM
602855
*RECORD*
*FIELD* NO
602855
*FIELD* TI
*602855 PROTEASOME SUBUNIT, ALPHA-TYPE, 6; PSMA6
;;PROTEASOME SUBUNIT IOTA;;
PROS27;;
read morep27K
*FIELD* TX
CLONING
DeMartino et al. (1991) cloned a partial sequence of a novel proteasomal
subunit, PSMA6, which they termed 'iota.' Bey et al. (1993) cloned the
PSMA6 cDNA encoding a protein that they termed p27K. The deduced
246-amino acid polypeptide contains an RNA-binding motif, a putative
nuclear localization signal, and phosphorylation sites. PSMA6 binds to a
specific HeLa cell RNA of approximately 120 nucleotides. Northern blot
analysis showed PSMA6 expression as a 1.1-kb mRNA in HeLa cells.
Southern blot analysis showed a pattern suggesting that PSMA6 is a
single-copy gene.
Coux et al. (1996) reviewed the structures and functions of the 20S
proteasome subunits. The alpha subunits comprise the outer rings of the
proteasome. Some alpha subunits contain a functional nuclear
localization signal; proteasomes are found in both the nuclear and
cytoplasmic compartments of the cell. Alpha subunits may constitute a
physical barrier that limits access of cytosolic proteins into the inner
proteolytic chamber.
MAPPING
Bey et al. (1993) mapped the PSMA6 gene to chromosome 14q13 by
fluorescence in situ hybridization.
MOLECULAR GENETICS
Because inflammation is critical in the pathogenesis of myocardial
infarction (608446) and because one of the mechanisms regulating the
inflammatory process is the ubiquitin-proteasome system, Ozaki et al.
(2006) investigated whether variants of the 20S proteasome are
associated with susceptibility to myocardial infarction. They identified
a common SNP (dbSNP rs1048990; minor allele frequency of 0.35) in the
PSMA6 gene (602855.0001) that was significantly associated with
myocardial infarction in the Japanese population. The SNP enhanced the
transcription of PSMA6. Moreover, suppression of PSMA6 expression using
short interfering RNA in cultured cells reduced activation of the
transcription factor NF-kappa-B (see 164011) by stabilizing
phosphorylated I-kappa-B (see 164008).
*FIELD* AV
.0001
MYOCARDIAL INFARCTION, SUSCEPTIBILITY TO
PSMA6, -8C-G, 5-PRIME UTR (dbSNP rs1048990)
Ozaki et al. (2006) found a significant association of susceptibility to
myocardial infarction (608446) in the Japanese population with a -8C-G
SNP (dbSNP rs1048990) in the 5-prime UTR of exon 1 of the PSMA6 gene.
The SNP enhanced the transcription of PSMA6.
Hinohara et al. (2009) analyzed the -8C-G polymorphism in a total of
1,330 patients with coronary artery disease (CAD) and 2,554 controls
from Japanese and Korean populations but found no evidence for
association. However, metaanalysis of data from this study and earlier
studies yielded an odds ratio of 1.08 for the G allele (p = 0.0057),
suggesting that the contribution of PSMA6 to CAD is not large enough to
be readily replicated. Hinohara et al. (2009) concluded that further
studies are required to establish the contribution of this variant in
susceptibility to CAD.
*FIELD* RF
1. Bey, F.; Silva Pereira, I.; Coux, O.; Viegas-Pequignot, E.; Recillas
Targa, F.; Nothwang, H. G.; Dutrillaux, B.; Scherrer, K.: The prosomal
RNA-binding protein p27K is a member of the alpha-type human prosomal
gene family. Molec. Gen. Genet. 237: 193-205, 1993.
2. Coux, O.; Tanaka, K.; Goldberg, A. L.: Structure and functions
of the 20S and 26S proteasomes. Ann. Rev. Biochem. 65: 801-847,
1996.
3. DeMartino, G. N.; Orth, K.; McCullough, M. L.; Lee, L. W.; Munn,
T. Z.; Moomaw, C. R.; Dawson, P. A.; Slaughter, C. A.: The primary
structures of four subunits of the human, high molecular weight proteinase,
macropain (proteasome), are distinct but homologous. Biochim. Biophys.
Acta 1079: 29-38, 1991.
4. Hinohara, K.; Nakajima, T.; Sasaoka, T.; Sawabe, M.; Lee, B.-S.;
Ban, J.; Park, J.-E.; Izumi, T.; Kimura, A.: Replication studies
for the association of PSMA6 polymorphism with coronary artery disease
in East Asian populations. J. Hum. Genet. 54: 248-251, 2009.
5. Ozaki, K.; Sato, H.; Iida, A.; Mizuno, H.; Nakamura, T.; Miyamoto,
Y.; Takahashi, A.; Tsunoda, T.; Ikegawa, S.; Kamatani, N.; Hori, M.;
Nakamura, Y.; Tanaka, T.: A functional SNP in PSMA6 confers risk
of myocardial infarction in the Japanese population. Nature Genet. 38:
921-925, 2006.
*FIELD* CN
Marla J. F. O'Neill - updated: 12/29/2009
Victor A. McKusick - updated: 8/15/2006
*FIELD* CD
Jennifer P. Macke: 7/15/1998
*FIELD* ED
carol: 11/02/2011
ckniffin: 4/8/2011
wwang: 1/20/2010
terry: 12/29/2009
carol: 3/10/2008
carol: 6/5/2007
carol: 8/16/2006
terry: 8/15/2006
kayiaros: 7/13/1999
alopez: 7/16/1998
*RECORD*
*FIELD* NO
602855
*FIELD* TI
*602855 PROTEASOME SUBUNIT, ALPHA-TYPE, 6; PSMA6
;;PROTEASOME SUBUNIT IOTA;;
PROS27;;
read morep27K
*FIELD* TX
CLONING
DeMartino et al. (1991) cloned a partial sequence of a novel proteasomal
subunit, PSMA6, which they termed 'iota.' Bey et al. (1993) cloned the
PSMA6 cDNA encoding a protein that they termed p27K. The deduced
246-amino acid polypeptide contains an RNA-binding motif, a putative
nuclear localization signal, and phosphorylation sites. PSMA6 binds to a
specific HeLa cell RNA of approximately 120 nucleotides. Northern blot
analysis showed PSMA6 expression as a 1.1-kb mRNA in HeLa cells.
Southern blot analysis showed a pattern suggesting that PSMA6 is a
single-copy gene.
Coux et al. (1996) reviewed the structures and functions of the 20S
proteasome subunits. The alpha subunits comprise the outer rings of the
proteasome. Some alpha subunits contain a functional nuclear
localization signal; proteasomes are found in both the nuclear and
cytoplasmic compartments of the cell. Alpha subunits may constitute a
physical barrier that limits access of cytosolic proteins into the inner
proteolytic chamber.
MAPPING
Bey et al. (1993) mapped the PSMA6 gene to chromosome 14q13 by
fluorescence in situ hybridization.
MOLECULAR GENETICS
Because inflammation is critical in the pathogenesis of myocardial
infarction (608446) and because one of the mechanisms regulating the
inflammatory process is the ubiquitin-proteasome system, Ozaki et al.
(2006) investigated whether variants of the 20S proteasome are
associated with susceptibility to myocardial infarction. They identified
a common SNP (dbSNP rs1048990; minor allele frequency of 0.35) in the
PSMA6 gene (602855.0001) that was significantly associated with
myocardial infarction in the Japanese population. The SNP enhanced the
transcription of PSMA6. Moreover, suppression of PSMA6 expression using
short interfering RNA in cultured cells reduced activation of the
transcription factor NF-kappa-B (see 164011) by stabilizing
phosphorylated I-kappa-B (see 164008).
*FIELD* AV
.0001
MYOCARDIAL INFARCTION, SUSCEPTIBILITY TO
PSMA6, -8C-G, 5-PRIME UTR (dbSNP rs1048990)
Ozaki et al. (2006) found a significant association of susceptibility to
myocardial infarction (608446) in the Japanese population with a -8C-G
SNP (dbSNP rs1048990) in the 5-prime UTR of exon 1 of the PSMA6 gene.
The SNP enhanced the transcription of PSMA6.
Hinohara et al. (2009) analyzed the -8C-G polymorphism in a total of
1,330 patients with coronary artery disease (CAD) and 2,554 controls
from Japanese and Korean populations but found no evidence for
association. However, metaanalysis of data from this study and earlier
studies yielded an odds ratio of 1.08 for the G allele (p = 0.0057),
suggesting that the contribution of PSMA6 to CAD is not large enough to
be readily replicated. Hinohara et al. (2009) concluded that further
studies are required to establish the contribution of this variant in
susceptibility to CAD.
*FIELD* RF
1. Bey, F.; Silva Pereira, I.; Coux, O.; Viegas-Pequignot, E.; Recillas
Targa, F.; Nothwang, H. G.; Dutrillaux, B.; Scherrer, K.: The prosomal
RNA-binding protein p27K is a member of the alpha-type human prosomal
gene family. Molec. Gen. Genet. 237: 193-205, 1993.
2. Coux, O.; Tanaka, K.; Goldberg, A. L.: Structure and functions
of the 20S and 26S proteasomes. Ann. Rev. Biochem. 65: 801-847,
1996.
3. DeMartino, G. N.; Orth, K.; McCullough, M. L.; Lee, L. W.; Munn,
T. Z.; Moomaw, C. R.; Dawson, P. A.; Slaughter, C. A.: The primary
structures of four subunits of the human, high molecular weight proteinase,
macropain (proteasome), are distinct but homologous. Biochim. Biophys.
Acta 1079: 29-38, 1991.
4. Hinohara, K.; Nakajima, T.; Sasaoka, T.; Sawabe, M.; Lee, B.-S.;
Ban, J.; Park, J.-E.; Izumi, T.; Kimura, A.: Replication studies
for the association of PSMA6 polymorphism with coronary artery disease
in East Asian populations. J. Hum. Genet. 54: 248-251, 2009.
5. Ozaki, K.; Sato, H.; Iida, A.; Mizuno, H.; Nakamura, T.; Miyamoto,
Y.; Takahashi, A.; Tsunoda, T.; Ikegawa, S.; Kamatani, N.; Hori, M.;
Nakamura, Y.; Tanaka, T.: A functional SNP in PSMA6 confers risk
of myocardial infarction in the Japanese population. Nature Genet. 38:
921-925, 2006.
*FIELD* CN
Marla J. F. O'Neill - updated: 12/29/2009
Victor A. McKusick - updated: 8/15/2006
*FIELD* CD
Jennifer P. Macke: 7/15/1998
*FIELD* ED
carol: 11/02/2011
ckniffin: 4/8/2011
wwang: 1/20/2010
terry: 12/29/2009
carol: 3/10/2008
carol: 6/5/2007
carol: 8/16/2006
terry: 8/15/2006
kayiaros: 7/13/1999
alopez: 7/16/1998