Full text data of PSMA3
PSMA3
(HC8, PSC8)
[Confidence: high (present in two of the MS resources)]
Proteasome subunit alpha type-3; 3.4.25.1 (Macropain subunit C8; Multicatalytic endopeptidase complex subunit C8; Proteasome component C8)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit alpha type-3; 3.4.25.1 (Macropain subunit C8; Multicatalytic endopeptidase complex subunit C8; Proteasome component C8)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00171199
IPI00171199 Proteasome subunit alpha type 3 (EC 3.4.25.1) (Proteasome component C8) (Macropain subunit C8) (Multicatalytic endopeptidase com 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
IPI00171199 Proteasome subunit alpha type 3 (EC 3.4.25.1) (Proteasome component C8) (Macropain subunit C8) (Multicatalytic endopeptidase com 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
P25788
ID PSA3_HUMAN Reviewed; 255 AA.
AC P25788; B2RCK6; Q86U83; Q8N1D8; Q9BS70;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 161.
DE RecName: Full=Proteasome subunit alpha type-3;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit C8;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C8;
DE AltName: Full=Proteasome component C8;
GN Name=PSMA3; Synonyms=HC8, PSC8;
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] (ISOFORM 1).
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] (ISOFORMS 1 AND 2).
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Pancreas, and Urinary bladder;
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 116-130.
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 [7]
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 [8]
RP FUNCTION, AND INTERACTION WITH CDKN1A.
RX PubMed=11350925; DOI=10.1093/emboj/20.10.2367;
RA Touitou R., Richardson J., Bose S., Nakanishi M., Rivett J.,
RA Allday M.J.;
RT "A degradation signal located in the C-terminus of p21WAF1/CIP1 is a
RT binding site for the C8 alpha-subunit of the 20S proteasome.";
RL EMBO J. 20:2367-2375(2001).
RN [9]
RP ACETYLATION AT SER-2, AND PHOSPHORYLATION AT SER-250.
RX PubMed=12376572; DOI=10.1074/mcp.M200030-MCP200;
RA Claverol S., Burlet-Schiltz O., Girbal-Neuhauser E., Gairin J.E.,
RA Monsarrat B.;
RT "Mapping and structural dissection of human 20 s proteasome using
RT proteomic approaches.";
RL Mol. Cell. Proteomics 1:567-578(2002).
RN [10]
RP INDUCTION.
RX PubMed=12472671; DOI=10.1046/j.1365-3083.2002.01179.x;
RA Matsunaga T., Ishida T., Takekawa M., Nishimura S., Adachi M.,
RA Imai K.;
RT "Analysis of gene expression during maturation of immature dendritic
RT cells derived from peripheral blood monocytes.";
RL Scand. J. Immunol. 56:593-601(2002).
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 INTERACTION WITH AURKB.
RX PubMed=14674694; DOI=10.1023/A:1027317014159;
RA Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C.,
RA Zhao S., Yu L.;
RT "Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes
RT degradation in a proteasome-dependent manner.";
RL Mol. Cell. Biochem. 254:157-162(2003).
RN [13]
RP INTERACTION WITH EBNA3.
RX PubMed=15831937; DOI=10.1099/vir.0.80763-0;
RA Touitou R., O'Nions J., Heaney J., Allday M.J.;
RT "Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of
RT the 20S proteasome and are degraded by 20S proteasomes in vitro, but
RT are very stable in latently infected B cells.";
RL J. Gen. Virol. 86:1269-1277(2005).
RN [14]
RP INTERACTION WITH MDM2 AND RB1.
RX PubMed=16337594; DOI=10.1016/j.molcel.2005.10.017;
RA Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R.,
RA Allday M.J., Xiao Z.X.;
RT "MDM2 promotes proteasome-dependent ubiquitin-independent degradation
RT of retinoblastoma protein.";
RL Mol. Cell 20:699-708(2005).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [17]
RP INDUCTION BY BO-653.
RX PubMed=16298756; DOI=10.1080/10715760500354430;
RA Takabe W., Matsukawa N., Kodama T., Tanaka K., Noguchi N.;
RT "Chemical structure-dependent gene expression of proteasome subunits
RT via regulation of the antioxidant response element.";
RL Free Radic. Res. 40:21-30(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-250, AND
RP MASS SPECTROMETRY.
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [21]
RP FUNCTION, AND INTERACTION WITH TBXA2R.
RX PubMed=17499743; DOI=10.1016/j.prostaglandins.2006.12.001;
RA Sasaki M., Sukegawa J., Miyosawa K., Yanagisawa T., Ohkubo S.,
RA Nakahata N.;
RT "Low expression of cell-surface thromboxane A2 receptor beta-isoform
RT through the negative regulation of its membrane traffic by
RT proteasomes.";
RL Prostaglandins Other Lipid Mediat. 83:237-249(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [26]
RP INTERACTION WITH HCV F PROTEIN.
RX PubMed=18971267; DOI=10.1128/JVI.00832-08;
RA Yuksek K., Chen W.-L., Chien D., Ou J.-H.;
RT "Ubiquitin-independent degradation of hepatitis C virus F protein.";
RL J. Virol. 83:612-621(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-206 AND LYS-230, AND
RP MASS 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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, 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. Binds to the C-terminus of CDKN1A and thereby mediates
CC its degradation. Negatively regulates the membrane trafficking of
CC the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.
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 AURKB. Interacts
CC with CDKN1A. Interacts with HIV-1 TAT protein. Interacts with
CC hepatitis C virus (HCV) F protein. Interacts with Epstein-Barr
CC virus EBNA3 proteins. Interacts with MDM2 and RB1. Interacts with
CC the C-terminus of TBXA2R isoform 2.
CC -!- INTERACTION:
CC Q00987:MDM2; NbExp=2; IntAct=EBI-348380, EBI-389668;
CC P29590:PML; NbExp=2; IntAct=EBI-348380, EBI-295890;
CC P25786:PSMA1; NbExp=3; IntAct=EBI-348380, EBI-359352;
CC P25789:PSMA4; NbExp=4; IntAct=EBI-348380, EBI-359310;
CC P60900:PSMA6; NbExp=4; IntAct=EBI-348380, EBI-357793;
CC O14818:PSMA7; NbExp=6; IntAct=EBI-348380, EBI-603272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P25788-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P25788-2; Sequence=VSP_005280;
CC -!- INDUCTION: Down-regulated by antioxidants BO-653 and probucol. Up-
CC regulated by bacterial lipopolysaccharides (LPS) and TNF.
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; D00762; BAA00659.1; -; mRNA.
DR EMBL; BT006711; AAP35357.1; -; mRNA.
DR EMBL; BT019715; AAV38520.1; -; mRNA.
DR EMBL; AK315158; BAG37603.1; -; mRNA.
DR EMBL; CH471061; EAW80719.1; -; Genomic_DNA.
DR EMBL; BC005265; AAH05265.1; -; mRNA.
DR EMBL; BC029402; AAH29402.1; -; mRNA.
DR EMBL; BC038990; AAH38990.1; -; mRNA.
DR PIR; S15971; SNHUC8.
DR RefSeq; NP_002779.1; NM_002788.3.
DR RefSeq; NP_687033.1; NM_152132.2.
DR UniGene; Hs.558799; -.
DR ProteinModelPortal; P25788; -.
DR SMR; P25788; 2-246.
DR IntAct; P25788; 43.
DR MINT; MINT-1035201; -.
DR STRING; 9606.ENSP00000216455; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.977; -.
DR PhosphoSite; P25788; -.
DR DMDM; 130859; -.
DR OGP; P25788; -.
DR REPRODUCTION-2DPAGE; IPI00171199; -.
DR PaxDb; P25788; -.
DR PRIDE; P25788; -.
DR DNASU; 5684; -.
DR Ensembl; ENST00000216455; ENSP00000216455; ENSG00000100567.
DR Ensembl; ENST00000412908; ENSP00000390491; ENSG00000100567.
DR GeneID; 5684; -.
DR KEGG; hsa:5684; -.
DR UCSC; uc001xdj.2; human.
DR CTD; 5684; -.
DR GeneCards; GC14P058711; -.
DR H-InvDB; HIX0155215; -.
DR HGNC; HGNC:9532; PSMA3.
DR HPA; HPA000905; -.
DR MIM; 176843; gene.
DR MIM; 176845; gene.
DR neXtProt; NX_P25788; -.
DR PharmGKB; PA33877; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091086; -.
DR HOVERGEN; HBG105566; -.
DR InParanoid; P25788; -.
DR KO; K02727; -.
DR OMA; VPDGRHF; -.
DR OrthoDB; EOG73JKW6; -.
DR PhylomeDB; P25788; -.
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; PSMA3; -.
DR GenomeRNAi; 5684; -.
DR NextBio; 22072; -.
DR PRO; PR:P25788; -.
DR ArrayExpress; P25788; -.
DR Bgee; P25788; -.
DR CleanEx; HS_PSMA3; -.
DR Genevestigator; P25788; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; IDA:BHF-UCL.
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: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: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; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Hydrolase; Nucleus;
KW Phosphoprotein; Protease; Proteasome; Reference proteome;
KW Threonine protease.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 255 Proteasome subunit alpha type-3.
FT /FTId=PRO_0000124091.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 57 57 N6-acetyllysine.
FT MOD_RES 206 206 N6-acetyllysine.
FT MOD_RES 230 230 N6-acetyllysine.
FT MOD_RES 243 243 Phosphoserine.
FT MOD_RES 250 250 Phosphoserine.
FT VAR_SEQ 136 142 Missing (in isoform 2).
FT /FTId=VSP_005280.
FT CONFLICT 91 91 I -> M (in Ref. 5; AAH29402).
SQ SEQUENCE 255 AA; 28433 MW; A1854ED3C0650FB1 CRC64;
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE
EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV
HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL
QMKEMTCRDI VKEVAKIIYI VHDEVKDKAF ELELSWVGEL TNGRHEIVPK DIREEAEKYA
KESLKEEDES DDDNM
//
ID PSA3_HUMAN Reviewed; 255 AA.
AC P25788; B2RCK6; Q86U83; Q8N1D8; Q9BS70;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 161.
DE RecName: Full=Proteasome subunit alpha type-3;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit C8;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C8;
DE AltName: Full=Proteasome component C8;
GN Name=PSMA3; Synonyms=HC8, PSC8;
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] (ISOFORM 1).
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] (ISOFORMS 1 AND 2).
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Pancreas, and Urinary bladder;
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 116-130.
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 [7]
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 [8]
RP FUNCTION, AND INTERACTION WITH CDKN1A.
RX PubMed=11350925; DOI=10.1093/emboj/20.10.2367;
RA Touitou R., Richardson J., Bose S., Nakanishi M., Rivett J.,
RA Allday M.J.;
RT "A degradation signal located in the C-terminus of p21WAF1/CIP1 is a
RT binding site for the C8 alpha-subunit of the 20S proteasome.";
RL EMBO J. 20:2367-2375(2001).
RN [9]
RP ACETYLATION AT SER-2, AND PHOSPHORYLATION AT SER-250.
RX PubMed=12376572; DOI=10.1074/mcp.M200030-MCP200;
RA Claverol S., Burlet-Schiltz O., Girbal-Neuhauser E., Gairin J.E.,
RA Monsarrat B.;
RT "Mapping and structural dissection of human 20 s proteasome using
RT proteomic approaches.";
RL Mol. Cell. Proteomics 1:567-578(2002).
RN [10]
RP INDUCTION.
RX PubMed=12472671; DOI=10.1046/j.1365-3083.2002.01179.x;
RA Matsunaga T., Ishida T., Takekawa M., Nishimura S., Adachi M.,
RA Imai K.;
RT "Analysis of gene expression during maturation of immature dendritic
RT cells derived from peripheral blood monocytes.";
RL Scand. J. Immunol. 56:593-601(2002).
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 INTERACTION WITH AURKB.
RX PubMed=14674694; DOI=10.1023/A:1027317014159;
RA Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C.,
RA Zhao S., Yu L.;
RT "Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes
RT degradation in a proteasome-dependent manner.";
RL Mol. Cell. Biochem. 254:157-162(2003).
RN [13]
RP INTERACTION WITH EBNA3.
RX PubMed=15831937; DOI=10.1099/vir.0.80763-0;
RA Touitou R., O'Nions J., Heaney J., Allday M.J.;
RT "Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of
RT the 20S proteasome and are degraded by 20S proteasomes in vitro, but
RT are very stable in latently infected B cells.";
RL J. Gen. Virol. 86:1269-1277(2005).
RN [14]
RP INTERACTION WITH MDM2 AND RB1.
RX PubMed=16337594; DOI=10.1016/j.molcel.2005.10.017;
RA Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R.,
RA Allday M.J., Xiao Z.X.;
RT "MDM2 promotes proteasome-dependent ubiquitin-independent degradation
RT of retinoblastoma protein.";
RL Mol. Cell 20:699-708(2005).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [17]
RP INDUCTION BY BO-653.
RX PubMed=16298756; DOI=10.1080/10715760500354430;
RA Takabe W., Matsukawa N., Kodama T., Tanaka K., Noguchi N.;
RT "Chemical structure-dependent gene expression of proteasome subunits
RT via regulation of the antioxidant response element.";
RL Free Radic. Res. 40:21-30(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-250, AND
RP MASS SPECTROMETRY.
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [21]
RP FUNCTION, AND INTERACTION WITH TBXA2R.
RX PubMed=17499743; DOI=10.1016/j.prostaglandins.2006.12.001;
RA Sasaki M., Sukegawa J., Miyosawa K., Yanagisawa T., Ohkubo S.,
RA Nakahata N.;
RT "Low expression of cell-surface thromboxane A2 receptor beta-isoform
RT through the negative regulation of its membrane traffic by
RT proteasomes.";
RL Prostaglandins Other Lipid Mediat. 83:237-249(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [26]
RP INTERACTION WITH HCV F PROTEIN.
RX PubMed=18971267; DOI=10.1128/JVI.00832-08;
RA Yuksek K., Chen W.-L., Chien D., Ou J.-H.;
RT "Ubiquitin-independent degradation of hepatitis C virus F protein.";
RL J. Virol. 83:612-621(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-206 AND LYS-230, AND
RP MASS 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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, 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. Binds to the C-terminus of CDKN1A and thereby mediates
CC its degradation. Negatively regulates the membrane trafficking of
CC the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.
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 AURKB. Interacts
CC with CDKN1A. Interacts with HIV-1 TAT protein. Interacts with
CC hepatitis C virus (HCV) F protein. Interacts with Epstein-Barr
CC virus EBNA3 proteins. Interacts with MDM2 and RB1. Interacts with
CC the C-terminus of TBXA2R isoform 2.
CC -!- INTERACTION:
CC Q00987:MDM2; NbExp=2; IntAct=EBI-348380, EBI-389668;
CC P29590:PML; NbExp=2; IntAct=EBI-348380, EBI-295890;
CC P25786:PSMA1; NbExp=3; IntAct=EBI-348380, EBI-359352;
CC P25789:PSMA4; NbExp=4; IntAct=EBI-348380, EBI-359310;
CC P60900:PSMA6; NbExp=4; IntAct=EBI-348380, EBI-357793;
CC O14818:PSMA7; NbExp=6; IntAct=EBI-348380, EBI-603272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P25788-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P25788-2; Sequence=VSP_005280;
CC -!- INDUCTION: Down-regulated by antioxidants BO-653 and probucol. Up-
CC regulated by bacterial lipopolysaccharides (LPS) and TNF.
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; D00762; BAA00659.1; -; mRNA.
DR EMBL; BT006711; AAP35357.1; -; mRNA.
DR EMBL; BT019715; AAV38520.1; -; mRNA.
DR EMBL; AK315158; BAG37603.1; -; mRNA.
DR EMBL; CH471061; EAW80719.1; -; Genomic_DNA.
DR EMBL; BC005265; AAH05265.1; -; mRNA.
DR EMBL; BC029402; AAH29402.1; -; mRNA.
DR EMBL; BC038990; AAH38990.1; -; mRNA.
DR PIR; S15971; SNHUC8.
DR RefSeq; NP_002779.1; NM_002788.3.
DR RefSeq; NP_687033.1; NM_152132.2.
DR UniGene; Hs.558799; -.
DR ProteinModelPortal; P25788; -.
DR SMR; P25788; 2-246.
DR IntAct; P25788; 43.
DR MINT; MINT-1035201; -.
DR STRING; 9606.ENSP00000216455; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.977; -.
DR PhosphoSite; P25788; -.
DR DMDM; 130859; -.
DR OGP; P25788; -.
DR REPRODUCTION-2DPAGE; IPI00171199; -.
DR PaxDb; P25788; -.
DR PRIDE; P25788; -.
DR DNASU; 5684; -.
DR Ensembl; ENST00000216455; ENSP00000216455; ENSG00000100567.
DR Ensembl; ENST00000412908; ENSP00000390491; ENSG00000100567.
DR GeneID; 5684; -.
DR KEGG; hsa:5684; -.
DR UCSC; uc001xdj.2; human.
DR CTD; 5684; -.
DR GeneCards; GC14P058711; -.
DR H-InvDB; HIX0155215; -.
DR HGNC; HGNC:9532; PSMA3.
DR HPA; HPA000905; -.
DR MIM; 176843; gene.
DR MIM; 176845; gene.
DR neXtProt; NX_P25788; -.
DR PharmGKB; PA33877; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091086; -.
DR HOVERGEN; HBG105566; -.
DR InParanoid; P25788; -.
DR KO; K02727; -.
DR OMA; VPDGRHF; -.
DR OrthoDB; EOG73JKW6; -.
DR PhylomeDB; P25788; -.
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; PSMA3; -.
DR GenomeRNAi; 5684; -.
DR NextBio; 22072; -.
DR PRO; PR:P25788; -.
DR ArrayExpress; P25788; -.
DR Bgee; P25788; -.
DR CleanEx; HS_PSMA3; -.
DR Genevestigator; P25788; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; IDA:BHF-UCL.
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: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: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; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Hydrolase; Nucleus;
KW Phosphoprotein; Protease; Proteasome; Reference proteome;
KW Threonine protease.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 255 Proteasome subunit alpha type-3.
FT /FTId=PRO_0000124091.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 57 57 N6-acetyllysine.
FT MOD_RES 206 206 N6-acetyllysine.
FT MOD_RES 230 230 N6-acetyllysine.
FT MOD_RES 243 243 Phosphoserine.
FT MOD_RES 250 250 Phosphoserine.
FT VAR_SEQ 136 142 Missing (in isoform 2).
FT /FTId=VSP_005280.
FT CONFLICT 91 91 I -> M (in Ref. 5; AAH29402).
SQ SEQUENCE 255 AA; 28433 MW; A1854ED3C0650FB1 CRC64;
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE
EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV
HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL
QMKEMTCRDI VKEVAKIIYI VHDEVKDKAF ELELSWVGEL TNGRHEIVPK DIREEAEKYA
KESLKEEDES DDDNM
//
MIM
176843
*RECORD*
*FIELD* NO
176843
*FIELD* TI
*176843 PROTEASOME SUBUNIT, ALPHA-TYPE, 3; PSMA3
;;HC8;;
PSC3
*FIELD* TX
DESCRIPTION
read more
The proteasome is a multicatalytic protease complex that catalyzes an
energy-dependent, extralysosomal proteolytic pathway responsible for
selective elimination of proteins with aberrant structures and naturally
occurring short-lived proteins related to metabolic regulation and cell
cycle progression. The proteasome has a sedimentation coefficient of 26S
and is composed of a 20S catalytic core and a 22S regulatory complex.
Eukaryotic 20S proteasomes have a molecular mass of 700 to 800 kD and
consist of a set of over 15 kinds of polypeptides of 21 to 32 kD. All
eukaryotic 20S proteasome subunits can be classified grossly into 2
subfamilies, alpha and beta, by their high similarity with either the
alpha or beta subunits of the archaebacterium Thermoplasma acidophilum
(summary by Akioka et al., 1995).
CLONING
Akioka et al. (1995) cloned a gene encoding an alpha-type subunit, HC8,
of the human 20S proteasome. They showed that its CAAT and TATA boxes
function as promoters, in contrast to the promoters of the HC3 (PSMA2;
176842) and HC5 (PSMB1; 602017) genes.
MAPPING
By fluorescence in situ hybridization, Akioka et al. (1995) mapped the
PSMA3 gene to 14q23, which differed from the chromosomal location of 9
other proteasomal subunit genes that had been mapped up to that time. In
their Table 1, they listed the chromosomal localization of 4 alpha-type
subunits and 5 beta-type subunits.
*FIELD* RF
1. Akioka, H.; Forsberg, N. E.; Ishida, N.; Okumura, K.; Nogami, M.;
Taguchi, H.; Noda, C.; Tanaka, K.: Isolation and characterization
of the HC8 subunit gene of the human proteasome. Biochem. Biophys.
Res. Commun. 207: 318-323, 1995.
*FIELD* CD
Victor A. McKusick: 7/10/1991
*FIELD* ED
carol: 09/19/2012
terry: 12/7/2001
dkim: 7/23/1998
alopez: 3/18/1998
mark: 8/11/1995
supermim: 3/16/1992
carol: 7/10/1991
*RECORD*
*FIELD* NO
176843
*FIELD* TI
*176843 PROTEASOME SUBUNIT, ALPHA-TYPE, 3; PSMA3
;;HC8;;
PSC3
*FIELD* TX
DESCRIPTION
read more
The proteasome is a multicatalytic protease complex that catalyzes an
energy-dependent, extralysosomal proteolytic pathway responsible for
selective elimination of proteins with aberrant structures and naturally
occurring short-lived proteins related to metabolic regulation and cell
cycle progression. The proteasome has a sedimentation coefficient of 26S
and is composed of a 20S catalytic core and a 22S regulatory complex.
Eukaryotic 20S proteasomes have a molecular mass of 700 to 800 kD and
consist of a set of over 15 kinds of polypeptides of 21 to 32 kD. All
eukaryotic 20S proteasome subunits can be classified grossly into 2
subfamilies, alpha and beta, by their high similarity with either the
alpha or beta subunits of the archaebacterium Thermoplasma acidophilum
(summary by Akioka et al., 1995).
CLONING
Akioka et al. (1995) cloned a gene encoding an alpha-type subunit, HC8,
of the human 20S proteasome. They showed that its CAAT and TATA boxes
function as promoters, in contrast to the promoters of the HC3 (PSMA2;
176842) and HC5 (PSMB1; 602017) genes.
MAPPING
By fluorescence in situ hybridization, Akioka et al. (1995) mapped the
PSMA3 gene to 14q23, which differed from the chromosomal location of 9
other proteasomal subunit genes that had been mapped up to that time. In
their Table 1, they listed the chromosomal localization of 4 alpha-type
subunits and 5 beta-type subunits.
*FIELD* RF
1. Akioka, H.; Forsberg, N. E.; Ishida, N.; Okumura, K.; Nogami, M.;
Taguchi, H.; Noda, C.; Tanaka, K.: Isolation and characterization
of the HC8 subunit gene of the human proteasome. Biochem. Biophys.
Res. Commun. 207: 318-323, 1995.
*FIELD* CD
Victor A. McKusick: 7/10/1991
*FIELD* ED
carol: 09/19/2012
terry: 12/7/2001
dkim: 7/23/1998
alopez: 3/18/1998
mark: 8/11/1995
supermim: 3/16/1992
carol: 7/10/1991