Full text data of PSMC1
PSMC1
[Confidence: high (present in two of the MS resources)]
26S protease regulatory subunit 4; P26s4 (26S proteasome AAA-ATPase subunit RPT2; Proteasome 26S subunit ATPase 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S protease regulatory subunit 4; P26s4 (26S proteasome AAA-ATPase subunit RPT2; Proteasome 26S subunit ATPase 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00011126
IPI00011126 26S protease regulatory subunit 4 The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins 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
IPI00011126 26S protease regulatory subunit 4 The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins 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
P62191
ID PRS4_HUMAN Reviewed; 440 AA.
AC P62191; P49014; Q03527; Q6IAW0; Q6NW36; Q96AZ3;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=26S protease regulatory subunit 4;
DE Short=P26s4;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT2;
DE AltName: Full=Proteasome 26S subunit ATPase 1;
GN Name=PSMC1;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1429620;
RA Dubiel W., Ferrell K., Pratt G., Rechsteiner M.C.;
RT "Subunit 4 of the 26 S protease is a member of a novel eukaryotic
RT ATPase family.";
RL J. Biol. Chem. 267:22699-22702(1992).
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=Bone marrow, Brain, Lung, and Prostate;
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 [4]
RP INTERACTION WITH SCA7.
RX PubMed=11734547; DOI=10.1093/hmg/10.24.2821;
RA Matilla A., Gorbea C., Einum D.D., Townsend J., Michalik A.,
RA van Broeckhoven C., Jensen C.C., Murphy K.J., Ptacek L.J., Fu Y.H.;
RT "Association of ataxin-7 with the proteasome subunit S4 of the 19S
RT regulatory complex.";
RL Hum. Mol. Genet. 10:2821-2831(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP INTERACTION WITH NGLY1.
RX PubMed=15358861; DOI=10.1073/pnas.0405663101;
RA Katiyar S., Li G., Lennarz W.J.;
RT "A complex between peptide:N-glycanase and two proteasome-linked
RT proteins suggests a mechanism for the degradation of misfolded
RT glycoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004).
RN [7]
RP INTERACTION WITH PAAF1.
RX PubMed=15831487; DOI=10.1128/MCB.25.9.3842-3853.2005;
RA Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
RT "Proteasomal ATPase-associated factor 1 negatively regulates
RT proteasome activity by interacting with proteasomal ATPases.";
RL Mol. Cell. Biol. 25:3842-3853(2005).
RN [8]
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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-237, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-258, AND 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 [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).
CC -!- FUNCTION: The 26S protease is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the
CC 26S complex.
CC -!- SUBUNIT: Interacts with SCA7. Interacts with NGLY1. Interacts with
CC PAAF1.
CC -!- INTERACTION:
CC O60341:KDM1A; NbExp=2; IntAct=EBI-357598, EBI-710124;
CC P35998:PSMC2; NbExp=4; IntAct=EBI-357598, EBI-359710;
CC P62333:PSMC6; NbExp=3; IntAct=EBI-357598, EBI-357669;
CC Q13200:PSMD2; NbExp=6; IntAct=EBI-357598, EBI-357648;
CC O43463:SUV39H1; NbExp=2; IntAct=EBI-357598, EBI-349968;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L02426; AAA35484.1; -; mRNA.
DR EMBL; CR457044; CAG33325.1; -; mRNA.
DR EMBL; BC000512; AAH00512.1; -; mRNA.
DR EMBL; BC016368; AAH16368.1; -; mRNA.
DR EMBL; BC067741; AAH67741.1; -; mRNA.
DR EMBL; BC073818; AAH73818.1; -; mRNA.
DR PIR; A44468; A44468.
DR RefSeq; NP_002793.2; NM_002802.2.
DR UniGene; Hs.356654; -.
DR ProteinModelPortal; P62191; -.
DR SMR; P62191; 78-440.
DR IntAct; P62191; 29.
DR MINT; MINT-1141832; -.
DR STRING; 9606.ENSP00000261303; -.
DR PhosphoSite; P62191; -.
DR DMDM; 49065817; -.
DR PaxDb; P62191; -.
DR PeptideAtlas; P62191; -.
DR PRIDE; P62191; -.
DR DNASU; 5700; -.
DR Ensembl; ENST00000261303; ENSP00000261303; ENSG00000100764.
DR GeneID; 5700; -.
DR KEGG; hsa:5700; -.
DR UCSC; uc001xyf.3; human.
DR CTD; 5700; -.
DR GeneCards; GC14P090722; -.
DR H-InvDB; HIX0030744; -.
DR HGNC; HGNC:9547; PSMC1.
DR HPA; HPA000872; -.
DR MIM; 602706; gene.
DR neXtProt; NX_P62191; -.
DR PharmGKB; PA33892; -.
DR eggNOG; COG1222; -.
DR HOGENOM; HOG000225143; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P62191; -.
DR KO; K03062; -.
DR OMA; ATNKIES; -.
DR OrthoDB; EOG7F24ST; -.
DR PhylomeDB; P62191; -.
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; PSMC1; -.
DR GenomeRNAi; 5700; -.
DR NextBio; 22146; -.
DR PRO; PR:P62191; -.
DR ArrayExpress; P62191; -.
DR Bgee; P62191; -.
DR CleanEx; HS_PSMC1; -.
DR Genevestigator; P62191; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR005937; 26S_Psome_P45.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Lipoprotein; Myristate;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 440 26S protease regulatory subunit 4.
FT /FTId=PRO_0000084677.
FT NP_BIND 226 233 ATP (Potential).
FT MOD_RES 4 4 Phosphoserine.
FT MOD_RES 258 258 N6-acetyllysine.
FT MOD_RES 439 439 Phosphotyrosine.
FT LIPID 2 2 N-myristoyl glycine (By similarity).
FT CROSSLNK 237 237 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CONFLICT 19 19 K -> E (in Ref. 1; AAA35484).
FT CONFLICT 70 70 D -> G (in Ref. 3; AAH67741).
FT CONFLICT 120 120 H -> R (in Ref. 3; AAH16368).
SQ SEQUENCE 440 AA; 49185 MW; ACA80782F4F96F49 CRC64;
MGQSQSGGHG PGGGKKDDKD KKKKYEPPVP TRVGKKKKKT KGPDAASKLP LVTPHTQCRL
KLLKLERIKD YLLMEEEFIR NQEQMKPLEE KQEEERSKVD DLRGTPMSVG TLEEIIDDNH
AIVSTSVGSE HYVSILSFVD KDLLEPGCSV LLNHKVHAVI GVLMDDTDPL VTVMKVEKAP
QETYADIGGL DNQIQEIKES VELPLTHPEY YEEMGIKPPK GVILYGPPGT GKTLLAKAVA
NQTSATFLRV VGSELIQKYL GDGPKLVREL FRVAEEHAPS IVFIDEIDAI GTKRYDSNSG
GEREIQRTML ELLNQLDGFD SRGDVKVIMA TNRIETLDPA LIRPGRIDRK IEFPLPDEKT
KKRIFQIHTS RMTLADDVTL DDLIMAKDDL SGADIKAICT EAGLMALRER RMKVTNEDFK
KSKENVLYKK QEGTPEGLYL
//
ID PRS4_HUMAN Reviewed; 440 AA.
AC P62191; P49014; Q03527; Q6IAW0; Q6NW36; Q96AZ3;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=26S protease regulatory subunit 4;
DE Short=P26s4;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT2;
DE AltName: Full=Proteasome 26S subunit ATPase 1;
GN Name=PSMC1;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1429620;
RA Dubiel W., Ferrell K., Pratt G., Rechsteiner M.C.;
RT "Subunit 4 of the 26 S protease is a member of a novel eukaryotic
RT ATPase family.";
RL J. Biol. Chem. 267:22699-22702(1992).
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=Bone marrow, Brain, Lung, and Prostate;
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 [4]
RP INTERACTION WITH SCA7.
RX PubMed=11734547; DOI=10.1093/hmg/10.24.2821;
RA Matilla A., Gorbea C., Einum D.D., Townsend J., Michalik A.,
RA van Broeckhoven C., Jensen C.C., Murphy K.J., Ptacek L.J., Fu Y.H.;
RT "Association of ataxin-7 with the proteasome subunit S4 of the 19S
RT regulatory complex.";
RL Hum. Mol. Genet. 10:2821-2831(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP INTERACTION WITH NGLY1.
RX PubMed=15358861; DOI=10.1073/pnas.0405663101;
RA Katiyar S., Li G., Lennarz W.J.;
RT "A complex between peptide:N-glycanase and two proteasome-linked
RT proteins suggests a mechanism for the degradation of misfolded
RT glycoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004).
RN [7]
RP INTERACTION WITH PAAF1.
RX PubMed=15831487; DOI=10.1128/MCB.25.9.3842-3853.2005;
RA Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
RT "Proteasomal ATPase-associated factor 1 negatively regulates
RT proteasome activity by interacting with proteasomal ATPases.";
RL Mol. Cell. Biol. 25:3842-3853(2005).
RN [8]
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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-237, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-258, AND 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 [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).
CC -!- FUNCTION: The 26S protease is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the
CC 26S complex.
CC -!- SUBUNIT: Interacts with SCA7. Interacts with NGLY1. Interacts with
CC PAAF1.
CC -!- INTERACTION:
CC O60341:KDM1A; NbExp=2; IntAct=EBI-357598, EBI-710124;
CC P35998:PSMC2; NbExp=4; IntAct=EBI-357598, EBI-359710;
CC P62333:PSMC6; NbExp=3; IntAct=EBI-357598, EBI-357669;
CC Q13200:PSMD2; NbExp=6; IntAct=EBI-357598, EBI-357648;
CC O43463:SUV39H1; NbExp=2; IntAct=EBI-357598, EBI-349968;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L02426; AAA35484.1; -; mRNA.
DR EMBL; CR457044; CAG33325.1; -; mRNA.
DR EMBL; BC000512; AAH00512.1; -; mRNA.
DR EMBL; BC016368; AAH16368.1; -; mRNA.
DR EMBL; BC067741; AAH67741.1; -; mRNA.
DR EMBL; BC073818; AAH73818.1; -; mRNA.
DR PIR; A44468; A44468.
DR RefSeq; NP_002793.2; NM_002802.2.
DR UniGene; Hs.356654; -.
DR ProteinModelPortal; P62191; -.
DR SMR; P62191; 78-440.
DR IntAct; P62191; 29.
DR MINT; MINT-1141832; -.
DR STRING; 9606.ENSP00000261303; -.
DR PhosphoSite; P62191; -.
DR DMDM; 49065817; -.
DR PaxDb; P62191; -.
DR PeptideAtlas; P62191; -.
DR PRIDE; P62191; -.
DR DNASU; 5700; -.
DR Ensembl; ENST00000261303; ENSP00000261303; ENSG00000100764.
DR GeneID; 5700; -.
DR KEGG; hsa:5700; -.
DR UCSC; uc001xyf.3; human.
DR CTD; 5700; -.
DR GeneCards; GC14P090722; -.
DR H-InvDB; HIX0030744; -.
DR HGNC; HGNC:9547; PSMC1.
DR HPA; HPA000872; -.
DR MIM; 602706; gene.
DR neXtProt; NX_P62191; -.
DR PharmGKB; PA33892; -.
DR eggNOG; COG1222; -.
DR HOGENOM; HOG000225143; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P62191; -.
DR KO; K03062; -.
DR OMA; ATNKIES; -.
DR OrthoDB; EOG7F24ST; -.
DR PhylomeDB; P62191; -.
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; PSMC1; -.
DR GenomeRNAi; 5700; -.
DR NextBio; 22146; -.
DR PRO; PR:P62191; -.
DR ArrayExpress; P62191; -.
DR Bgee; P62191; -.
DR CleanEx; HS_PSMC1; -.
DR Genevestigator; P62191; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR005937; 26S_Psome_P45.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Lipoprotein; Myristate;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 440 26S protease regulatory subunit 4.
FT /FTId=PRO_0000084677.
FT NP_BIND 226 233 ATP (Potential).
FT MOD_RES 4 4 Phosphoserine.
FT MOD_RES 258 258 N6-acetyllysine.
FT MOD_RES 439 439 Phosphotyrosine.
FT LIPID 2 2 N-myristoyl glycine (By similarity).
FT CROSSLNK 237 237 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CONFLICT 19 19 K -> E (in Ref. 1; AAA35484).
FT CONFLICT 70 70 D -> G (in Ref. 3; AAH67741).
FT CONFLICT 120 120 H -> R (in Ref. 3; AAH16368).
SQ SEQUENCE 440 AA; 49185 MW; ACA80782F4F96F49 CRC64;
MGQSQSGGHG PGGGKKDDKD KKKKYEPPVP TRVGKKKKKT KGPDAASKLP LVTPHTQCRL
KLLKLERIKD YLLMEEEFIR NQEQMKPLEE KQEEERSKVD DLRGTPMSVG TLEEIIDDNH
AIVSTSVGSE HYVSILSFVD KDLLEPGCSV LLNHKVHAVI GVLMDDTDPL VTVMKVEKAP
QETYADIGGL DNQIQEIKES VELPLTHPEY YEEMGIKPPK GVILYGPPGT GKTLLAKAVA
NQTSATFLRV VGSELIQKYL GDGPKLVREL FRVAEEHAPS IVFIDEIDAI GTKRYDSNSG
GEREIQRTML ELLNQLDGFD SRGDVKVIMA TNRIETLDPA LIRPGRIDRK IEFPLPDEKT
KKRIFQIHTS RMTLADDVTL DDLIMAKDDL SGADIKAICT EAGLMALRER RMKVTNEDFK
KSKENVLYKK QEGTPEGLYL
//
MIM
602706
*RECORD*
*FIELD* NO
602706
*FIELD* TI
*602706 PROTEASOME 26S SUBUNIT, ATPase, 1; PSMC1
;;PROTEASE 26S, SUBUNIT 4; S4
*FIELD* TX
read more
DESCRIPTION
Ubiquitinated proteins are degraded by a 26S ATP-dependent protease. The
protease is composed of a 20S catalytic proteasome and 2 PA700
regulatory modules. The PA700 complex is composed of multiple subunits,
including at least 6 related ATPases, including PSMC1, and approximately
15 non-ATPase polypeptides. Each of the 6 ATPases, namely PSMC1, PSMC2
(154365), PSMC3 (186852), PSMC4 (602707), PSMC5 (601681), and PSMC6
(602708), contains an AAA (ATPases associated with diverse cellular
activities) domain (summary by Tanahashi et al., 1998).
CLONING
Dubiel et al. (1992) cloned cDNAs encoding subunit 4 (S4) of the 26S
protease by screening a HeLa cell cDNA library with probes that were
produced using the protein sequence. The 440-amino acid protein has a
molecular mass of 51 kD by SDS-PAGE.
Hoyle and Fisher (1996) found that the human and mouse PSMC1 proteins
have 99% amino acid identity.
GENE FUNCTION
Spinocerebellar ataxia type 7 (SCA7; 164500) is a neurodegenerative
disorder characterized by ataxia and selective neuronal cell loss caused
by the expansion of a translated CAG repeat encoding a polyglutamine
tract in ataxin-7, the SCA7 gene product. Matilla et al. (2001) used a
2-hybrid assay to show that ataxin-7 interacts with the ATPase subunit
S4 of the 19S regulatory complex of the 26S proteasome. The ataxin-7/S4
association was modulated by the length of the polyglutamine tract,
whereby S4 showed a stronger association with the wildtype allele of
ataxin-7. Endogenous ataxin-7 localized to discrete nuclear foci that
also contained additional components of the proteasomal complex.
Immunohistochemical analyses suggested alterations either of the
distribution or the levels of S4 immunoreactivity in neurons that
degenerate in SCA7 brains. Immunoblot analyses demonstrated reduced
levels of S4 in SCA7 cerebella without evident alterations in the levels
of other proteasome subunits. The authors suggested a role for S4 and
ubiquitin-mediated proteasomal proteolysis in the molecular pathogenesis
of SCA7.
MAPPING
By fluorescence in situ hybridization, Tanahashi et al. (1998) mapped
the human PSMC1 gene to chromosome 19p13.3. However, Gross (2011) mapped
the PSMC1 gene to chromosome 14q32.11 based on an alignment of the PSMC1
sequence (GenBank GENBANK BT009826) with the genomic sequence (GRCh37).
By analysis of an interspecific backcross, Hoyle and Fisher (1996)
mapped the mouse Psmc1 gene to chromosome 12.
NOMENCLATURE
The PSMC1 gene product, which Dubiel et al. (1992) called subunit 4
(S4), is distinct from the PSMC4 (602707) gene product.
*FIELD* RF
1. Dubiel, W.; Ferrell, K.; Pratt, G.; Rechsteiner, M.: Subunit 4
of the 26 S protease is a member of a novel eukaryotic ATPase family. J.
Biol. Chem. 267: 22699-22702, 1992.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 2/17/2011.
3. Hoyle, J.; Fisher, E. M. C.: Genomic organization and mapping
of the mouse P26s4 ATPase gene: a member of the remarkably conserved
AAA gene family. Genomics 31: 115-118, 1996.
4. Matilla, A.; Gorbea, C.; Einum, D. D.; Townsend, J.; Michalik,
A.; van Broeckhoven, C.; Jensen, C. C.; Murphy, K. J.; Ptacek, L.
J.; Fu, Y.-H.: Association of ataxin-7 with the proteasome subunit
S4 of the 19S regulatory complex. Hum. Molec. Genet. 10: 2821-2831,
2001.
5. Tanahashi, N.; Suzuki, M.; Fujiwara, T.; Takahashi, E.; Shimbara,
N.; Chung, C. H.; Tanaka, K.: Chromosomal localization and immunological
analysis of a family of human 26S proteasomal ATPases. Biochem. Biophys.
Res. Commun. 243: 229-232, 1998.
*FIELD* CN
Matthew B. Gross - updated: 02/17/2011
George E. Tiller - updated: 6/11/2002
*FIELD* CD
Rebekah S. Rasooly: 6/10/1998
*FIELD* ED
mgross: 02/17/2011
cwells: 6/12/2002
cwells: 6/11/2002
psherman: 6/11/1998
*RECORD*
*FIELD* NO
602706
*FIELD* TI
*602706 PROTEASOME 26S SUBUNIT, ATPase, 1; PSMC1
;;PROTEASE 26S, SUBUNIT 4; S4
*FIELD* TX
read more
DESCRIPTION
Ubiquitinated proteins are degraded by a 26S ATP-dependent protease. The
protease is composed of a 20S catalytic proteasome and 2 PA700
regulatory modules. The PA700 complex is composed of multiple subunits,
including at least 6 related ATPases, including PSMC1, and approximately
15 non-ATPase polypeptides. Each of the 6 ATPases, namely PSMC1, PSMC2
(154365), PSMC3 (186852), PSMC4 (602707), PSMC5 (601681), and PSMC6
(602708), contains an AAA (ATPases associated with diverse cellular
activities) domain (summary by Tanahashi et al., 1998).
CLONING
Dubiel et al. (1992) cloned cDNAs encoding subunit 4 (S4) of the 26S
protease by screening a HeLa cell cDNA library with probes that were
produced using the protein sequence. The 440-amino acid protein has a
molecular mass of 51 kD by SDS-PAGE.
Hoyle and Fisher (1996) found that the human and mouse PSMC1 proteins
have 99% amino acid identity.
GENE FUNCTION
Spinocerebellar ataxia type 7 (SCA7; 164500) is a neurodegenerative
disorder characterized by ataxia and selective neuronal cell loss caused
by the expansion of a translated CAG repeat encoding a polyglutamine
tract in ataxin-7, the SCA7 gene product. Matilla et al. (2001) used a
2-hybrid assay to show that ataxin-7 interacts with the ATPase subunit
S4 of the 19S regulatory complex of the 26S proteasome. The ataxin-7/S4
association was modulated by the length of the polyglutamine tract,
whereby S4 showed a stronger association with the wildtype allele of
ataxin-7. Endogenous ataxin-7 localized to discrete nuclear foci that
also contained additional components of the proteasomal complex.
Immunohistochemical analyses suggested alterations either of the
distribution or the levels of S4 immunoreactivity in neurons that
degenerate in SCA7 brains. Immunoblot analyses demonstrated reduced
levels of S4 in SCA7 cerebella without evident alterations in the levels
of other proteasome subunits. The authors suggested a role for S4 and
ubiquitin-mediated proteasomal proteolysis in the molecular pathogenesis
of SCA7.
MAPPING
By fluorescence in situ hybridization, Tanahashi et al. (1998) mapped
the human PSMC1 gene to chromosome 19p13.3. However, Gross (2011) mapped
the PSMC1 gene to chromosome 14q32.11 based on an alignment of the PSMC1
sequence (GenBank GENBANK BT009826) with the genomic sequence (GRCh37).
By analysis of an interspecific backcross, Hoyle and Fisher (1996)
mapped the mouse Psmc1 gene to chromosome 12.
NOMENCLATURE
The PSMC1 gene product, which Dubiel et al. (1992) called subunit 4
(S4), is distinct from the PSMC4 (602707) gene product.
*FIELD* RF
1. Dubiel, W.; Ferrell, K.; Pratt, G.; Rechsteiner, M.: Subunit 4
of the 26 S protease is a member of a novel eukaryotic ATPase family. J.
Biol. Chem. 267: 22699-22702, 1992.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 2/17/2011.
3. Hoyle, J.; Fisher, E. M. C.: Genomic organization and mapping
of the mouse P26s4 ATPase gene: a member of the remarkably conserved
AAA gene family. Genomics 31: 115-118, 1996.
4. Matilla, A.; Gorbea, C.; Einum, D. D.; Townsend, J.; Michalik,
A.; van Broeckhoven, C.; Jensen, C. C.; Murphy, K. J.; Ptacek, L.
J.; Fu, Y.-H.: Association of ataxin-7 with the proteasome subunit
S4 of the 19S regulatory complex. Hum. Molec. Genet. 10: 2821-2831,
2001.
5. Tanahashi, N.; Suzuki, M.; Fujiwara, T.; Takahashi, E.; Shimbara,
N.; Chung, C. H.; Tanaka, K.: Chromosomal localization and immunological
analysis of a family of human 26S proteasomal ATPases. Biochem. Biophys.
Res. Commun. 243: 229-232, 1998.
*FIELD* CN
Matthew B. Gross - updated: 02/17/2011
George E. Tiller - updated: 6/11/2002
*FIELD* CD
Rebekah S. Rasooly: 6/10/1998
*FIELD* ED
mgross: 02/17/2011
cwells: 6/12/2002
cwells: 6/11/2002
psherman: 6/11/1998