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P51665

- PSMD7_HUMAN

UniProt

P51665 - PSMD7_HUMAN

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Protein

26S proteasome non-ATPase regulatory subunit 7

Gene
PSMD7, MOV34L
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.

GO - Molecular functioni

  1. protein binding Source: UniProtKB

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  5. apoptotic process Source: Reactome
  6. cellular nitrogen compound metabolic process Source: Reactome
  7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  8. G1/S transition of mitotic cell cycle Source: Reactome
  9. gene expression Source: Reactome
  10. mitotic cell cycle Source: Reactome
  11. mRNA metabolic process Source: Reactome
  12. negative regulation of apoptotic process Source: Reactome
  13. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  14. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  15. protein polyubiquitination Source: Reactome
  16. regulation of apoptotic process Source: Reactome
  17. regulation of cellular amino acid metabolic process Source: Reactome
  18. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  19. RNA metabolic process Source: Reactome
  20. small molecule metabolic process Source: Reactome
  21. viral process Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Protein family/group databases

MEROPSiM67.973.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 7
Alternative name(s):
26S proteasome regulatory subunit RPN8
26S proteasome regulatory subunit S12
Mov34 protein homolog
Proteasome subunit p40
Gene namesi
Name:PSMD7
Synonyms:MOV34L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:9565. PSMD7.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProt
  5. proteasome complex Source: ProtInc
  6. proteasome regulatory particle Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33911.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 32432426S proteasome non-ATPase regulatory subunit 7PRO_0000213943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki180 – 180Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei204 – 2041N6-acetyllysine1 Publication
Modified residuei214 – 2141N6-acetyllysine1 Publication
Modified residuei316 – 3161N6-acetyllysine By similarity
Modified residuei317 – 3171N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP51665.
PaxDbiP51665.
PeptideAtlasiP51665.
PRIDEiP51665.

PTM databases

PhosphoSiteiP51665.

Expressioni

Gene expression databases

ArrayExpressiP51665.
BgeeiP51665.
CleanExiHS_PSMD7.
GenevestigatoriP51665.

Organism-specific databases

HPAiCAB019379.
HPA049824.
HPA056069.

Interactioni

Subunit structurei

Homodimer. Interacts with TRIM5.2 Publications

Protein-protein interaction databases

BioGridi111685. 70 interactions.
DIPiDIP-27572N.
IntActiP51665. 31 interactions.
MINTiMINT-5002613.
STRINGi9606.ENSP00000219313.

Structurei

Secondary structure

1
324
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115
Helixi13 – 2816
Beta strandi36 – 5621
Beta strandi58 – 603
Beta strandi67 – 704
Helixi72 – 8312
Beta strandi86 – 883
Beta strandi90 – 967
Helixi105 – 1128
Turni113 – 1153
Beta strandi120 – 1245
Beta strandi134 – 14310
Beta strandi152 – 16211
Helixi166 – 17813

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O95X-ray1.95A/B1-186[»]
2O96X-ray3.00A/B1-177[»]
ProteinModelPortaliP51665.
SMRiP51665. Positions 1-288.

Miscellaneous databases

EvolutionaryTraceiP51665.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 118115MPNAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi286 – 32439Glu/Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M67A family.

Phylogenomic databases

eggNOGiCOG1310.
HOGENOMiHOG000209236.
HOVERGENiHBG035951.
InParanoidiP51665.
KOiK03038.
OMAiDHNYVES.
OrthoDBiEOG7B8S4G.
PhylomeDBiP51665.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51665-1 [UniParc]FASTAAdd to Basket

« Hide

MPELAVQKVV VHPLVLLSVV DHFNRIGKVG NQKRVVGVLL GSWQKKVLDV    50
SNSFAVPFDE DDKDDSVWFL DHDYLENMYG MFKKVNARER IVGWYHTGPK 100
LHKNDIAINE LMKRYCPNSV LVIIDVKPKD LGLPTEAYIS VEEVHDDGTP 150
TSKTFEHVTS EIGAEEAEEV GVEHLLRDIK DTTVGTLSQR ITNQVHGLKG 200
LNSKLLDIRS YLEKVATGKL PINHQIIYQL QDVFNLLPDV SLQEFVKAFY 250
LKTNDQMVVV YLASLIRSVV ALHNLINNKI ANRDAEKKEG QEKEESKKDR 300
KEDKEKDKDK EKSDVKKEEK KEKK 324
Length:324
Mass (Da):37,025
Last modified:May 10, 2002 - v2
Checksum:i3F7B343996B102B7
GO

Sequence cautioni

The sequence AAH00338.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271G → V in BAA08780. 1 Publication
Sequence conflicti144 – 1452VH → DQ in BAA08780. 1 Publication
Sequence conflicti216 – 2161A → G in BAA08780. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50063 mRNA. Translation: BAA08780.1.
CH471166 Genomic DNA. Translation: EAW59162.1.
CH471166 Genomic DNA. Translation: EAW59163.1.
BC000338 mRNA. Translation: AAH00338.1. Sequence problems.
BC012606 mRNA. Translation: AAH12606.1.
CCDSiCCDS10910.1.
PIRiJC4154.
S65491.
RefSeqiNP_002802.2. NM_002811.4.
UniGeneiHs.440604.

Genome annotation databases

EnsembliENST00000219313; ENSP00000219313; ENSG00000103035.
GeneIDi5713.
KEGGihsa:5713.
UCSCiuc002fcq.3. human.

Polymorphism databases

DMDMi20532412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50063 mRNA. Translation: BAA08780.1 .
CH471166 Genomic DNA. Translation: EAW59162.1 .
CH471166 Genomic DNA. Translation: EAW59163.1 .
BC000338 mRNA. Translation: AAH00338.1 . Sequence problems.
BC012606 mRNA. Translation: AAH12606.1 .
CCDSi CCDS10910.1.
PIRi JC4154.
S65491.
RefSeqi NP_002802.2. NM_002811.4.
UniGenei Hs.440604.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2O95 X-ray 1.95 A/B 1-186 [» ]
2O96 X-ray 3.00 A/B 1-177 [» ]
ProteinModelPortali P51665.
SMRi P51665. Positions 1-288.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111685. 70 interactions.
DIPi DIP-27572N.
IntActi P51665. 31 interactions.
MINTi MINT-5002613.
STRINGi 9606.ENSP00000219313.

Protein family/group databases

MEROPSi M67.973.

PTM databases

PhosphoSitei P51665.

Polymorphism databases

DMDMi 20532412.

Proteomic databases

MaxQBi P51665.
PaxDbi P51665.
PeptideAtlasi P51665.
PRIDEi P51665.

Protocols and materials databases

DNASUi 5713.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000219313 ; ENSP00000219313 ; ENSG00000103035 .
GeneIDi 5713.
KEGGi hsa:5713.
UCSCi uc002fcq.3. human.

Organism-specific databases

CTDi 5713.
GeneCardsi GC16P074330.
HGNCi HGNC:9565. PSMD7.
HPAi CAB019379.
HPA049824.
HPA056069.
MIMi 157970. gene.
neXtProti NX_P51665.
PharmGKBi PA33911.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1310.
HOGENOMi HOG000209236.
HOVERGENi HBG035951.
InParanoidi P51665.
KOi K03038.
OMAi DHNYVES.
OrthoDBi EOG7B8S4G.
PhylomeDBi P51665.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSi PSMD7. human.
EvolutionaryTracei P51665.
GeneWikii PSMD7.
GenomeRNAii 5713.
NextBioi 22194.
PROi P51665.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51665.
Bgeei P51665.
CleanExi HS_PSMD7.
Genevestigatori P51665.

Family and domain databases

InterProi IPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view ]
Pfami PF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view ]
SMARTi SM00232. JAB_MPN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of p40, a regulatory subunit of the human 26S proteasome, and a homolog of the Mov-34 gene product."
    Tsurumi C., DeMartino G.N., Slaughter C., Shimbara N., Tanaka K.
    Biochem. Biophys. Res. Commun. 210:600-608(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Skin.
  4. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions."
    Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., Luban J., Campbell E.M.
    Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM5.
  8. "The crystal structure of the human Mov34 MPN domain reveals a metal-free dimer."
    Sanches M., Alves B.S.C., Zanchin N.I.T., Guimaraes B.G.
    J. Mol. Biol. 370:846-855(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-186, SUBUNIT, LACK OF METAL-BINDING.

Entry informationi

Entry nameiPSMD7_HUMAN
AccessioniPrimary (citable) accession number: P51665
Secondary accession number(s): D3DWS9, Q6PKI2, Q96E97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2002
Last modified: September 3, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Does not bind a metal ion.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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