ID   PSD7_HUMAN              Reviewed;         324 AA.
AC   P51665; Q6PKI2; Q96E97;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 2.
DT   07-JUL-2009, entry version 83.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 7;
DE   AltName: Full=26S proteasome regulatory subunit rpn8;
DE   AltName: Full=26S proteasome regulatory subunit S12;
DE   AltName: Full=Proteasome subunit p40;
DE   AltName: Full=Mov34 protein homolog;
GN   Name=PSMD7; Synonyms=MOV34L;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95275316; PubMed=7755639; DOI=10.1006/bbrc.1995.1701;
RA   Tsurumi C., DeMartino G.N., Slaughter C., Shimbara N., Tanaka K.;
RT   "cDNA cloning of p40, a regulatory subunit of the human 26S
RT   proteasome, and a homolog of the Mov-34 gene product.";
RL   Biochem. Biophys. Res. Commun. 210:600-608(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186, CLEAVAGE OF
RP   INITIATOR METHIONINE, 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   [4]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-180, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18781797; DOI=10.1021/pr800468j;
RA   Meierhofer D., Wang X., Huang L., Kaiser P.;
RT   "Quantitative analysis of global ubiquitination in HeLa cells by mass
RT   spectrometry.";
RL   J. Proteome Res. 7:4566-4576(2008).
RN   [5]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which
CC       is involved in the ATP-dependent degradation of ubiquitinated
CC       proteins.
CC   -!- INTERACTION:
CC       Q9BRP4:PAAF1; NbExp=1; IntAct=EBI-357659, EBI-1056358;
CC       P43686:PSMC4; NbExp=1; IntAct=EBI-357659, EBI-743997;
CC       O75832:PSMD10; NbExp=1; IntAct=EBI-357659, EBI-752185;
CC       Q15008:PSMD6; NbExp=1; IntAct=EBI-357659, EBI-359701;
CC   -!- SIMILARITY: Belongs to the peptidase M67A family.
CC   -!- SIMILARITY: Contains 1 MPN (JAB/Mov34) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH00338.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; D50063; BAA08780.1; -; mRNA.
DR   EMBL; BC000338; AAH00338.1; ALT_SEQ; mRNA.
DR   EMBL; BC012606; AAH12606.1; -; mRNA.
DR   IPI; IPI00019927; -.
DR   PIR; JC4154; JC4154.
DR   PIR; S65491; S65491.
DR   RefSeq; NP_002802.2; -.
DR   UniGene; Hs.440604; -.
DR   PDB; 2O95; X-ray; 1.95 A; A/B=1-186.
DR   PDB; 2O96; X-ray; 3.00 A; A/B=1-177.
DR   PDBsum; 2O95; -.
DR   PDBsum; 2O96; -.
DR   DIP; DIP:27572N; -.
DR   IntAct; P51665; 10.
DR   MEROPS; M67.973; -.
DR   PhosphoSite; P51665; -.
DR   PeptideAtlas; P51665; -.
DR   PRIDE; P51665; -.
DR   Ensembl; ENSG00000103035; Homo sapiens.
DR   GeneID; 5713; -.
DR   KEGG; hsa:5713; -.
DR   UCSC; uc002fcq.1; human.
DR   GeneCards; GC16P072888; -.
DR   H-InvDB; HIX0013230; -.
DR   HGNC; HGNC:9565; PSMD7.
DR   MIM; 157970; gene.
DR   PharmGKB; PA33911; -.
DR   HOGENOM; P51665; -.
DR   HOVERGEN; P51665; -.
DR   OMA; P51665; MLVVYLA.
DR   Reactome; REACT_11045; Signaling by Wnt.
DR   Reactome; REACT_13; Metabolism of amino acids.
DR   Reactome; REACT_13635; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   Reactome; REACT_383; DNA Replication.
DR   Reactome; REACT_578; Apoptosis.
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   NextBio; 22194; -.
DR   ArrayExpress; P51665; -.
DR   Bgee; P51665; -.
DR   CleanEx; HS_PSMD7; -.
DR   GermOnline; ENSG00000103035; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-KW.
DR   GO; GO:0005838; C:proteasome regulatory particle; 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; IPR000555; Mov34_MPN_PAD1.
DR   Pfam; PF01398; Mov34; 1.
DR   ProDom; PD363422; Mov34-1; 1.
DR   SMART; SM00232; JAB_MPN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Isopeptide bond; Phosphoprotein;
KW   Proteasome; Ubl conjugation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    324       26S proteasome non-ATPase regulatory
FT                                subunit 7.
FT                                /FTId=PRO_0000213943.
FT   DOMAIN        4    118       MPN.
FT   COMPBIAS    286    324       Glu/Lys-rich.
FT   MOD_RES     186    186       Phosphothreonine.
FT   CROSSLNK    180    180       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CONFLICT     27     27       G -> V (in Ref. 1; BAA08780).
FT   CONFLICT    144    145       VH -> DQ (in Ref. 1; BAA08780).
FT   CONFLICT    216    216       A -> G (in Ref. 1; BAA08780).
FT   STRAND        7     11
FT   HELIX        13     28
FT   STRAND       36     56
FT   STRAND       58     60
FT   STRAND       67     70
FT   HELIX        72     83
FT   STRAND       86     88
FT   STRAND       90     96
FT   HELIX       105    112
FT   TURN        113    115
FT   STRAND      120    124
FT   STRAND      134    143
FT   STRAND      152    164
FT   HELIX       166    178
SQ   SEQUENCE   324 AA;  37025 MW;  3F7B343996B102B7 CRC64;
     MPELAVQKVV VHPLVLLSVV DHFNRIGKVG NQKRVVGVLL GSWQKKVLDV SNSFAVPFDE
     DDKDDSVWFL DHDYLENMYG MFKKVNARER IVGWYHTGPK LHKNDIAINE LMKRYCPNSV
     LVIIDVKPKD LGLPTEAYIS VEEVHDDGTP TSKTFEHVTS EIGAEEAEEV GVEHLLRDIK
     DTTVGTLSQR ITNQVHGLKG LNSKLLDIRS YLEKVATGKL PINHQIIYQL QDVFNLLPDV
     SLQEFVKAFY LKTNDQMVVV YLASLIRSVV ALHNLINNKI ANRDAEKKEG QEKEESKKDR
     KEDKEKDKDK EKSDVKKEEK KEKK
//