Full text data of PSMD7
PSMD7
(MOV34L)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
26S proteasome non-ATPase regulatory subunit 7 (26S proteasome regulatory subunit RPN8; 26S proteasome regulatory subunit S12; Mov34 protein homolog; Proteasome subunit p40)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S proteasome non-ATPase regulatory subunit 7 (26S proteasome regulatory subunit RPN8; 26S proteasome regulatory subunit S12; Mov34 protein homolog; Proteasome subunit p40)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00019927
IPI00019927 26S proteasome non-ATPase regulatory subunit 7 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
IPI00019927 26S proteasome non-ATPase regulatory subunit 7 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
P51665
ID PSMD7_HUMAN Reviewed; 324 AA.
AC P51665; D3DWS9; Q6PKI2; Q96E97;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 128.
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=Mov34 protein homolog;
DE AltName: Full=Proteasome subunit p40;
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 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 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 [3]
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 [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-214, 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 [6]
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 [7]
RP INTERACTION WITH TRIM5.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in
RT complex with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-186, SUBUNIT, AND LACK OF
RP METAL-BINDING.
RX PubMed=17559875; DOI=10.1016/j.jmb.2007.04.084;
RA Sanches M., Alves B.S.C., Zanchin N.I.T., Guimaraes B.G.;
RT "The crystal structure of the human Mov34 MPN domain reveals a metal-
RT free dimer.";
RL J. Mol. Biol. 370:846-855(2007).
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 -!- SUBUNIT: Homodimer. Interacts with TRIM5.
CC -!- MISCELLANEOUS: Does not bind a metal ion.
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;
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; D50063; BAA08780.1; -; mRNA.
DR EMBL; CH471166; EAW59162.1; -; Genomic_DNA.
DR EMBL; CH471166; EAW59163.1; -; Genomic_DNA.
DR EMBL; BC000338; AAH00338.1; ALT_SEQ; mRNA.
DR EMBL; BC012606; AAH12606.1; -; mRNA.
DR PIR; JC4154; JC4154.
DR PIR; S65491; S65491.
DR RefSeq; NP_002802.2; NM_002811.4.
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 ProteinModelPortal; P51665; -.
DR SMR; P51665; 1-215.
DR DIP; DIP-27572N; -.
DR IntAct; P51665; 30.
DR MINT; MINT-5002613; -.
DR STRING; 9606.ENSP00000219313; -.
DR MEROPS; M67.973; -.
DR PhosphoSite; P51665; -.
DR DMDM; 20532412; -.
DR PaxDb; P51665; -.
DR PeptideAtlas; P51665; -.
DR PRIDE; P51665; -.
DR DNASU; 5713; -.
DR Ensembl; ENST00000219313; ENSP00000219313; ENSG00000103035.
DR GeneID; 5713; -.
DR KEGG; hsa:5713; -.
DR UCSC; uc002fcq.3; human.
DR CTD; 5713; -.
DR GeneCards; GC16P074330; -.
DR HGNC; HGNC:9565; PSMD7.
DR HPA; CAB019379; -.
DR MIM; 157970; gene.
DR neXtProt; NX_P51665; -.
DR PharmGKB; PA33911; -.
DR eggNOG; COG1310; -.
DR HOGENOM; HOG000209236; -.
DR HOVERGEN; HBG035951; -.
DR InParanoid; P51665; -.
DR KO; K03038; -.
DR OMA; DAYFAVE; -.
DR OrthoDB; EOG7B8S4G; -.
DR PhylomeDB; P51665; -.
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; PSMD7; human.
DR EvolutionaryTrace; P51665; -.
DR GeneWiki; PSMD7; -.
DR GenomeRNAi; 5713; -.
DR NextBio; 22194; -.
DR PRO; PR:P51665; -.
DR ArrayExpress; P51665; -.
DR Bgee; P51665; -.
DR CleanEx; HS_PSMD7; -.
DR Genevestigator; P51665; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
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:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000555; JAB_MPN_dom.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Isopeptide bond;
KW Proteasome; Reference proteome; Ubl conjugation.
FT CHAIN 1 324 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 204 204 N6-acetyllysine.
FT MOD_RES 214 214 N6-acetyllysine.
FT MOD_RES 316 316 N6-acetyllysine (By similarity).
FT MOD_RES 317 317 N6-acetyllysine (By similarity).
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 152 162
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
//
ID PSMD7_HUMAN Reviewed; 324 AA.
AC P51665; D3DWS9; Q6PKI2; Q96E97;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 128.
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=Mov34 protein homolog;
DE AltName: Full=Proteasome subunit p40;
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 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 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 [3]
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 [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-214, 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 [6]
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 [7]
RP INTERACTION WITH TRIM5.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in
RT complex with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-186, SUBUNIT, AND LACK OF
RP METAL-BINDING.
RX PubMed=17559875; DOI=10.1016/j.jmb.2007.04.084;
RA Sanches M., Alves B.S.C., Zanchin N.I.T., Guimaraes B.G.;
RT "The crystal structure of the human Mov34 MPN domain reveals a metal-
RT free dimer.";
RL J. Mol. Biol. 370:846-855(2007).
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 -!- SUBUNIT: Homodimer. Interacts with TRIM5.
CC -!- MISCELLANEOUS: Does not bind a metal ion.
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;
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; D50063; BAA08780.1; -; mRNA.
DR EMBL; CH471166; EAW59162.1; -; Genomic_DNA.
DR EMBL; CH471166; EAW59163.1; -; Genomic_DNA.
DR EMBL; BC000338; AAH00338.1; ALT_SEQ; mRNA.
DR EMBL; BC012606; AAH12606.1; -; mRNA.
DR PIR; JC4154; JC4154.
DR PIR; S65491; S65491.
DR RefSeq; NP_002802.2; NM_002811.4.
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 ProteinModelPortal; P51665; -.
DR SMR; P51665; 1-215.
DR DIP; DIP-27572N; -.
DR IntAct; P51665; 30.
DR MINT; MINT-5002613; -.
DR STRING; 9606.ENSP00000219313; -.
DR MEROPS; M67.973; -.
DR PhosphoSite; P51665; -.
DR DMDM; 20532412; -.
DR PaxDb; P51665; -.
DR PeptideAtlas; P51665; -.
DR PRIDE; P51665; -.
DR DNASU; 5713; -.
DR Ensembl; ENST00000219313; ENSP00000219313; ENSG00000103035.
DR GeneID; 5713; -.
DR KEGG; hsa:5713; -.
DR UCSC; uc002fcq.3; human.
DR CTD; 5713; -.
DR GeneCards; GC16P074330; -.
DR HGNC; HGNC:9565; PSMD7.
DR HPA; CAB019379; -.
DR MIM; 157970; gene.
DR neXtProt; NX_P51665; -.
DR PharmGKB; PA33911; -.
DR eggNOG; COG1310; -.
DR HOGENOM; HOG000209236; -.
DR HOVERGEN; HBG035951; -.
DR InParanoid; P51665; -.
DR KO; K03038; -.
DR OMA; DAYFAVE; -.
DR OrthoDB; EOG7B8S4G; -.
DR PhylomeDB; P51665; -.
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; PSMD7; human.
DR EvolutionaryTrace; P51665; -.
DR GeneWiki; PSMD7; -.
DR GenomeRNAi; 5713; -.
DR NextBio; 22194; -.
DR PRO; PR:P51665; -.
DR ArrayExpress; P51665; -.
DR Bgee; P51665; -.
DR CleanEx; HS_PSMD7; -.
DR Genevestigator; P51665; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
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:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000555; JAB_MPN_dom.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Isopeptide bond;
KW Proteasome; Reference proteome; Ubl conjugation.
FT CHAIN 1 324 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 204 204 N6-acetyllysine.
FT MOD_RES 214 214 N6-acetyllysine.
FT MOD_RES 316 316 N6-acetyllysine (By similarity).
FT MOD_RES 317 317 N6-acetyllysine (By similarity).
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 152 162
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
//
MIM
157970
*RECORD*
*FIELD* NO
157970
*FIELD* TI
*157970 PROTEASOME 26S SUBUNIT, NON-ATPase, 7; PSMD7
;;MOLONEY LEUKEMIA VIRUS 34 PROVIRAL INTEGRATION SITE GENE, MOUSE, HOMOLOG
read moreOF; MOV34;;
RPN8
*FIELD* TX
CLONING
Gridley et al. (1990) stated that the Mov34 mutation is a recessive
embryonic lethal mutation caused by retroviral integration into the
murine germline. This integration disrupts a transcription unit,
designated Mov34, that appears to encode a novel protein. Gridley et al.
(1990) found that the Mov34 transcript is conserved in evolution. A
Drosophila homolog encodes a protein with 62% amino acid identity to the
murine protein.
Gridley et al. (1991) cloned a full-length cDNA encoding mouse Mov34.
The deduced 321-amino acid protein has a calculated molecular mass of 36
kD.
MAPPING
Gridley et al. (1990) found that the Mov34 gene is located on mouse
chromosome 8. By Southern analysis of rodent/human cell hybrids and by
in situ hybridization, they mapped the human homolog of Mov34 to
chromosome 16q23-q24. An evolutionarily conserved syntenic relationship
exists between these 2 regions. Mouse chromosome 8 also contains
'oligosyndactyly' (os), another recessive lethal mutation. By genetic
studies, Gridley et al. (1990) ruled out the possibility that os resides
at the same locus as the Mov34 integration.
*FIELD* RF
1. Gridley, T.; Gray, D. A.; Orr-Weaver, T.; Soriano, P.; Barton,
D. E.; Francke, U.; Jaenisch, R.: Molecular analysis of the Mov34
mutation: transcript disrupted by proviral integration in mice is
conserved in Drosophila. Development 109: 235-242, 1990.
2. Gridley, T.; Jaenisch, R.; Gendron-Maguire, M.: The murine Mov-34
gene: full-length cDNA and genomic organization. Genomics 11: 501-507,
1991.
*FIELD* CN
Matthew B. Gross - updated: 07/18/2012
*FIELD* CD
Victor A. McKusick: 12/13/1991
*FIELD* ED
mgross: 07/18/2012
psherman: 11/20/1998
alopez: 8/24/1998
supermim: 3/16/1992
carol: 12/13/1991
*RECORD*
*FIELD* NO
157970
*FIELD* TI
*157970 PROTEASOME 26S SUBUNIT, NON-ATPase, 7; PSMD7
;;MOLONEY LEUKEMIA VIRUS 34 PROVIRAL INTEGRATION SITE GENE, MOUSE, HOMOLOG
read moreOF; MOV34;;
RPN8
*FIELD* TX
CLONING
Gridley et al. (1990) stated that the Mov34 mutation is a recessive
embryonic lethal mutation caused by retroviral integration into the
murine germline. This integration disrupts a transcription unit,
designated Mov34, that appears to encode a novel protein. Gridley et al.
(1990) found that the Mov34 transcript is conserved in evolution. A
Drosophila homolog encodes a protein with 62% amino acid identity to the
murine protein.
Gridley et al. (1991) cloned a full-length cDNA encoding mouse Mov34.
The deduced 321-amino acid protein has a calculated molecular mass of 36
kD.
MAPPING
Gridley et al. (1990) found that the Mov34 gene is located on mouse
chromosome 8. By Southern analysis of rodent/human cell hybrids and by
in situ hybridization, they mapped the human homolog of Mov34 to
chromosome 16q23-q24. An evolutionarily conserved syntenic relationship
exists between these 2 regions. Mouse chromosome 8 also contains
'oligosyndactyly' (os), another recessive lethal mutation. By genetic
studies, Gridley et al. (1990) ruled out the possibility that os resides
at the same locus as the Mov34 integration.
*FIELD* RF
1. Gridley, T.; Gray, D. A.; Orr-Weaver, T.; Soriano, P.; Barton,
D. E.; Francke, U.; Jaenisch, R.: Molecular analysis of the Mov34
mutation: transcript disrupted by proviral integration in mice is
conserved in Drosophila. Development 109: 235-242, 1990.
2. Gridley, T.; Jaenisch, R.; Gendron-Maguire, M.: The murine Mov-34
gene: full-length cDNA and genomic organization. Genomics 11: 501-507,
1991.
*FIELD* CN
Matthew B. Gross - updated: 07/18/2012
*FIELD* CD
Victor A. McKusick: 12/13/1991
*FIELD* ED
mgross: 07/18/2012
psherman: 11/20/1998
alopez: 8/24/1998
supermim: 3/16/1992
carol: 12/13/1991