Full text data of PSMA4
PSMA4
(HC9, PSC9)
[Confidence: high (present in two of the MS resources)]
Proteasome subunit alpha type-4; 3.4.25.1 (Macropain subunit C9; Multicatalytic endopeptidase complex subunit C9; Proteasome component C9; Proteasome subunit L)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit alpha type-4; 3.4.25.1 (Macropain subunit C9; Multicatalytic endopeptidase complex subunit C9; Proteasome component C9; Proteasome subunit L)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00299155
IPI00299155 Proteasome subunit alpha type 4 Proteasome subunit alpha type 4 membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 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
IPI00299155 Proteasome subunit alpha type 4 Proteasome subunit alpha type 4 membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 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
P25789
ID PSA4_HUMAN Reviewed; 261 AA.
AC P25789; D3DW86; Q53XP2; Q567Q5; Q8TBD1;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1992, sequence version 1.
DT 22-JAN-2014, entry version 148.
DE RecName: Full=Proteasome subunit alpha type-4;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit C9;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C9;
DE AltName: Full=Proteasome component C9;
DE AltName: Full=Proteasome subunit L;
GN Name=PSMA4; Synonyms=HC9, PSC9;
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] (ISOFORM 1).
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 GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
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] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, Brain, Lung, 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 18-39.
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 INTERACTION WITH HTLV-1 TAX.
RX PubMed=8692272; DOI=10.1038/381328a0;
RA Rousset R., Desbois C., Bantignies F., Jalinot P.;
RT "Effects on NF-kappa B1/p105 processing of the interaction between the
RT HTLV-1 transactivator Tax and the proteasome.";
RL Nature 381:328-331(1996).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASS
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127 AND LYS-176, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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 [13]
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).
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. Interaction with HTLV-1 TAX
CC protein favors NFKB1 activation.
CC -!- INTERACTION:
CC P25786:PSMA1; NbExp=3; IntAct=EBI-359310, EBI-359352;
CC P25787:PSMA2; NbExp=7; IntAct=EBI-359310, EBI-603262;
CC P25788:PSMA3; NbExp=4; IntAct=EBI-359310, EBI-348380;
CC P60900:PSMA6; NbExp=4; IntAct=EBI-359310, EBI-357793;
CC O14818:PSMA7; NbExp=8; IntAct=EBI-359310, 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P25789-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P25789-2; Sequence=VSP_043102;
CC Note=No experimental confirmation available;
CC -!- INDUCTION: Down-regulated by antioxidants BO-653 and probucol.
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; D00763; BAA00660.1; -; mRNA.
DR EMBL; BT009784; AAP88786.1; -; mRNA.
DR EMBL; AC027228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471136; EAW99163.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99164.1; -; Genomic_DNA.
DR EMBL; BC005361; AAH05361.1; -; mRNA.
DR EMBL; BC022445; AAH22445.1; -; mRNA.
DR EMBL; BC022817; AAH22817.2; -; mRNA.
DR EMBL; BC047667; AAH47667.1; -; mRNA.
DR EMBL; BC093069; AAH93069.1; -; mRNA.
DR PIR; S15972; SNHUC9.
DR RefSeq; NP_001096137.1; NM_001102667.1.
DR RefSeq; NP_001096138.1; NM_001102668.1.
DR RefSeq; NP_002780.1; NM_002789.4.
DR UniGene; Hs.251531; -.
DR ProteinModelPortal; P25789; -.
DR SMR; P25789; 2-237.
DR DIP; DIP-29365N; -.
DR IntAct; P25789; 19.
DR MINT; MINT-5002513; -.
DR STRING; 9606.ENSP00000044462; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.973; -.
DR PhosphoSite; P25789; -.
DR DMDM; 130861; -.
DR UCD-2DPAGE; P25789; -.
DR PaxDb; P25789; -.
DR PRIDE; P25789; -.
DR DNASU; 5685; -.
DR Ensembl; ENST00000044462; ENSP00000044462; ENSG00000041357.
DR Ensembl; ENST00000413382; ENSP00000402118; ENSG00000041357.
DR Ensembl; ENST00000559082; ENSP00000453887; ENSG00000041357.
DR GeneID; 5685; -.
DR KEGG; hsa:5685; -.
DR UCSC; uc002bdu.4; human.
DR CTD; 5685; -.
DR GeneCards; GC15P078832; -.
DR HGNC; HGNC:9533; PSMA4.
DR HPA; CAB004973; -.
DR MIM; 176846; gene.
DR neXtProt; NX_P25789; -.
DR PharmGKB; PA33878; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091085; -.
DR HOVERGEN; HBG003005; -.
DR InParanoid; P25789; -.
DR KO; K02728; -.
DR OMA; KQEYKDD; -.
DR PhylomeDB; P25789; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMA4; human.
DR GeneWiki; PSMA4; -.
DR GenomeRNAi; 5685; -.
DR NextBio; 22078; -.
DR PRO; PR:P25789; -.
DR ArrayExpress; P25789; -.
DR Bgee; P25789; -.
DR CleanEx; HS_PSMA4; -.
DR Genevestigator; P25789; -.
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: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; IPR016050; Proteasome_bsu_CS.
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 CHAIN 1 261 Proteasome subunit alpha type-4.
FT /FTId=PRO_0000124103.
FT MOD_RES 13 13 Phosphoserine.
FT MOD_RES 75 75 Phosphoserine.
FT MOD_RES 127 127 N6-acetyllysine.
FT MOD_RES 176 176 N6-acetyllysine.
FT VAR_SEQ 1 71 Missing (in isoform 2).
FT /FTId=VSP_043102.
SQ SEQUENCE 261 AA; 29484 MW; 7867422B1B31F3B9 CRC64;
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF
FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA
YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK
EGEMTLKSAL ALAIKVLNKT MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH
EEEEAKAERE KKEKEQKEKD K
//
ID PSA4_HUMAN Reviewed; 261 AA.
AC P25789; D3DW86; Q53XP2; Q567Q5; Q8TBD1;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1992, sequence version 1.
DT 22-JAN-2014, entry version 148.
DE RecName: Full=Proteasome subunit alpha type-4;
DE EC=3.4.25.1;
DE AltName: Full=Macropain subunit C9;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C9;
DE AltName: Full=Proteasome component C9;
DE AltName: Full=Proteasome subunit L;
GN Name=PSMA4; Synonyms=HC9, PSC9;
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] (ISOFORM 1).
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 GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
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] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, Brain, Lung, 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 18-39.
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 INTERACTION WITH HTLV-1 TAX.
RX PubMed=8692272; DOI=10.1038/381328a0;
RA Rousset R., Desbois C., Bantignies F., Jalinot P.;
RT "Effects on NF-kappa B1/p105 processing of the interaction between the
RT HTLV-1 transactivator Tax and the proteasome.";
RL Nature 381:328-331(1996).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASS
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127 AND LYS-176, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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 [13]
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).
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. Interaction with HTLV-1 TAX
CC protein favors NFKB1 activation.
CC -!- INTERACTION:
CC P25786:PSMA1; NbExp=3; IntAct=EBI-359310, EBI-359352;
CC P25787:PSMA2; NbExp=7; IntAct=EBI-359310, EBI-603262;
CC P25788:PSMA3; NbExp=4; IntAct=EBI-359310, EBI-348380;
CC P60900:PSMA6; NbExp=4; IntAct=EBI-359310, EBI-357793;
CC O14818:PSMA7; NbExp=8; IntAct=EBI-359310, 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P25789-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P25789-2; Sequence=VSP_043102;
CC Note=No experimental confirmation available;
CC -!- INDUCTION: Down-regulated by antioxidants BO-653 and probucol.
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; D00763; BAA00660.1; -; mRNA.
DR EMBL; BT009784; AAP88786.1; -; mRNA.
DR EMBL; AC027228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471136; EAW99163.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99164.1; -; Genomic_DNA.
DR EMBL; BC005361; AAH05361.1; -; mRNA.
DR EMBL; BC022445; AAH22445.1; -; mRNA.
DR EMBL; BC022817; AAH22817.2; -; mRNA.
DR EMBL; BC047667; AAH47667.1; -; mRNA.
DR EMBL; BC093069; AAH93069.1; -; mRNA.
DR PIR; S15972; SNHUC9.
DR RefSeq; NP_001096137.1; NM_001102667.1.
DR RefSeq; NP_001096138.1; NM_001102668.1.
DR RefSeq; NP_002780.1; NM_002789.4.
DR UniGene; Hs.251531; -.
DR ProteinModelPortal; P25789; -.
DR SMR; P25789; 2-237.
DR DIP; DIP-29365N; -.
DR IntAct; P25789; 19.
DR MINT; MINT-5002513; -.
DR STRING; 9606.ENSP00000044462; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.973; -.
DR PhosphoSite; P25789; -.
DR DMDM; 130861; -.
DR UCD-2DPAGE; P25789; -.
DR PaxDb; P25789; -.
DR PRIDE; P25789; -.
DR DNASU; 5685; -.
DR Ensembl; ENST00000044462; ENSP00000044462; ENSG00000041357.
DR Ensembl; ENST00000413382; ENSP00000402118; ENSG00000041357.
DR Ensembl; ENST00000559082; ENSP00000453887; ENSG00000041357.
DR GeneID; 5685; -.
DR KEGG; hsa:5685; -.
DR UCSC; uc002bdu.4; human.
DR CTD; 5685; -.
DR GeneCards; GC15P078832; -.
DR HGNC; HGNC:9533; PSMA4.
DR HPA; CAB004973; -.
DR MIM; 176846; gene.
DR neXtProt; NX_P25789; -.
DR PharmGKB; PA33878; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091085; -.
DR HOVERGEN; HBG003005; -.
DR InParanoid; P25789; -.
DR KO; K02728; -.
DR OMA; KQEYKDD; -.
DR PhylomeDB; P25789; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMA4; human.
DR GeneWiki; PSMA4; -.
DR GenomeRNAi; 5685; -.
DR NextBio; 22078; -.
DR PRO; PR:P25789; -.
DR ArrayExpress; P25789; -.
DR Bgee; P25789; -.
DR CleanEx; HS_PSMA4; -.
DR Genevestigator; P25789; -.
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: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; IPR016050; Proteasome_bsu_CS.
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 CHAIN 1 261 Proteasome subunit alpha type-4.
FT /FTId=PRO_0000124103.
FT MOD_RES 13 13 Phosphoserine.
FT MOD_RES 75 75 Phosphoserine.
FT MOD_RES 127 127 N6-acetyllysine.
FT MOD_RES 176 176 N6-acetyllysine.
FT VAR_SEQ 1 71 Missing (in isoform 2).
FT /FTId=VSP_043102.
SQ SEQUENCE 261 AA; 29484 MW; 7867422B1B31F3B9 CRC64;
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF
FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA
YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK
EGEMTLKSAL ALAIKVLNKT MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH
EEEEAKAERE KKEKEQKEKD K
//
MIM
176846
*RECORD*
*FIELD* NO
176846
*FIELD* TI
*176846 PROTEASOME SUBUNIT, ALPHA-TYPE, 4; PSMA4
;;PROTEASOME COMPONENT 9; PSC9;;
HC9
read more*FIELD* TX
DESCRIPTION
Proteasomes are multicatalytic proteinase complexes consisting of a set
of nonidentical polypeptide components, such as PSMA4 (Tamura et al.,
1991).
CLONING
By biochemical analysis and screening a liver cell line cDNA library
with rat Psma4, Tamura et al. (1991) isolated a cDNA encoding human
PSMA4, which they called HC9. The predicted 261-amino acid protein has a
calculated molecular mass of 29.5 kD. HC9 is highly homologous to HC2
(PSMA1; 602854), HC3 (PSMA2; 176842), and HC8 (PSMA3; 176843),
particularly in the N-terminal half, and is 99% identical to the rat
protein.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PSMA4
gene to chromosome 15 (TMAP WI-9202).
Amos et al. (2008) placed the CHRNA3 (118503), CHRNA5 (118505), CHRNB4
(118509), and PSMA4 genes within a 100-kb region on chromosome 15q25.1.
*FIELD* RF
1. Amos, C. I.; Wu, X.; Broderick, P.; Gorlov, I. P.; Gu, J.; Eisen,
T.; Dong, Q.; Zhang, Q.; Gu, X.; Vijayakrishnan, J.; Sullivan, K.;
Matakidou, A.; Wang, Y.; Mills, G.; Doheny, K.; Tsai, Y.-Y.; Chen,
W. V.; Shete, S.; Spitz, M. R.; Houlston, R. S.: Genome-wide association
scan of tag SNPs identifies a susceptibility locus for lung cancer
at 15q25.1. Nature Genet. 40: 616-622, 2008.
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.
*FIELD* CD
Victor A. McKusick: 8/5/1991
*FIELD* ED
alopez: 08/19/2008
mgross: 12/13/2007
supermim: 3/16/1992
carol: 8/5/1991
*RECORD*
*FIELD* NO
176846
*FIELD* TI
*176846 PROTEASOME SUBUNIT, ALPHA-TYPE, 4; PSMA4
;;PROTEASOME COMPONENT 9; PSC9;;
HC9
read more*FIELD* TX
DESCRIPTION
Proteasomes are multicatalytic proteinase complexes consisting of a set
of nonidentical polypeptide components, such as PSMA4 (Tamura et al.,
1991).
CLONING
By biochemical analysis and screening a liver cell line cDNA library
with rat Psma4, Tamura et al. (1991) isolated a cDNA encoding human
PSMA4, which they called HC9. The predicted 261-amino acid protein has a
calculated molecular mass of 29.5 kD. HC9 is highly homologous to HC2
(PSMA1; 602854), HC3 (PSMA2; 176842), and HC8 (PSMA3; 176843),
particularly in the N-terminal half, and is 99% identical to the rat
protein.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PSMA4
gene to chromosome 15 (TMAP WI-9202).
Amos et al. (2008) placed the CHRNA3 (118503), CHRNA5 (118505), CHRNB4
(118509), and PSMA4 genes within a 100-kb region on chromosome 15q25.1.
*FIELD* RF
1. Amos, C. I.; Wu, X.; Broderick, P.; Gorlov, I. P.; Gu, J.; Eisen,
T.; Dong, Q.; Zhang, Q.; Gu, X.; Vijayakrishnan, J.; Sullivan, K.;
Matakidou, A.; Wang, Y.; Mills, G.; Doheny, K.; Tsai, Y.-Y.; Chen,
W. V.; Shete, S.; Spitz, M. R.; Houlston, R. S.: Genome-wide association
scan of tag SNPs identifies a susceptibility locus for lung cancer
at 15q25.1. Nature Genet. 40: 616-622, 2008.
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.
*FIELD* CD
Victor A. McKusick: 8/5/1991
*FIELD* ED
alopez: 08/19/2008
mgross: 12/13/2007
supermim: 3/16/1992
carol: 8/5/1991