ID   PRS4_HUMAN              Reviewed;         440 AA.
AC   P62191; P49014; Q03527; Q6IAW0; Q96AZ3;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   10-JUN-2008, entry version 51.
DE   26S protease regulatory subunit 4 (P26s4) (Proteasome 26S subunit
DE   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   MEDLINE=93054576; 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, 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   MEDLINE=21592411; 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=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   MYRISTOYLATION [LARGE SCALE ANALYSIS] AT GLY-2, AND MASS SPECTROMETRY.
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.
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).
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       P43686:PSMC4; NbExp=1; IntAct=EBI-357598, EBI-743997;
CC       O75832:PSMD10; NbExp=1; IntAct=EBI-357598, EBI-752185;
CC       Q15008:PSMD6; NbExp=1; IntAct=EBI-357598, EBI-359701;
CC       Q9BRP4:WDR71; NbExp=1; IntAct=EBI-357598, EBI-1056358;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
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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; BC073818; AAH73818.1; -; mRNA.
DR   PIR; A44468; A44468.
DR   RefSeq; NP_002793.2; -.
DR   UniGene; Hs.356654; -.
DR   HSSP; P43773; 1OFI.
DR   IntAct; P62191; -.
DR   PhosphoSite; P62191; -.
DR   PeptideAtlas; P62191; -.
DR   Ensembl; ENSG00000100764; Homo sapiens.
DR   GeneID; 5700; -.
DR   KEGG; hsa:5700; -.
DR   H-InvDB; HIX0011881; -.
DR   H-InvDB; HIX0030744; -.
DR   HGNC; HGNC:9547; PSMC1.
DR   HPA; HPA000872; -.
DR   MIM; 602706; gene.
DR   PharmGKB; PA33892; -.
DR   HOGENOM; P62191; -.
DR   HOVERGEN; P62191; -.
DR   Reactome; REACT_11045; Signaling by Wnt.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   Reactome; REACT_383; DNA Replication.
DR   Reactome; REACT_6185; HIV Infection.
DR   Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; REACT_9035; APC/C:Cdh1-mediated degradation of Skp2.
DR   LinkHub; P62191; -.
DR   ArrayExpress; P62191; -.
DR   CleanEx; HS_PSMC1; -.
DR   GermOnline; ENSG00000100764; Homo sapiens.
DR   GO; GO:0000502; C:proteasome complex; NAS:ProtInc.
DR   GO; GO:0016887; F:ATPase activity; TAS:ProtInc.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent protea...; EXP:Reactome.
DR   GO; GO:0051436; P:negative regulation of ubiquitin-protein li...; EXP:Reactome.
DR   GO; GO:0051437; P:positive regulation of ubiquitin-protein li...; EXP:Reactome.
DR   InterPro; IPR005937; 26S_proteasome_P45.
DR   InterPro; IPR003593; AAA+_ATPase_core.
DR   InterPro; IPR003959; AAA_ATPase_core.
DR   InterPro; IPR003960; AAA_ATPase_CS.
DR   Pfam; PF00004; AAA; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Lipoprotein;
KW   Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    440       26S protease regulatory subunit 4.
FT                                /FTId=PRO_0000084677.
FT   NP_BIND     226    233       ATP (Potential).
FT   MOD_RES     439    439       Phosphotyrosine.
FT   LIPID         2      2       N-myristoyl glycine.
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    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
//