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P51665 (PSMD7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PSMD7
Synonyms:MOV34L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Homodimer. Interacts with TRIM5. Ref.7 Ref.8

Miscellaneous

Does not bind a metal ion.

Sequence similarities

Belongs to the peptidase M67A family.

Contains 1 MPN (JAB/Mov34) domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentProteasome
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

RNA metabolic process

Traceable author statement. Source: Reactome

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein polyubiquitination

Traceable author statement. Source: Reactome

regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of cellular amino acid metabolic process

Traceable author statement. Source: Reactome

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

proteasome complex

Traceable author statement PubMed 8811196. Source: ProtInc

proteasome regulatory particle

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionprotein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 32432426S proteasome non-ATPase regulatory subunit 7
PRO_0000213943

Regions

Domain4 – 118115MPN
Compositional bias286 – 32439Glu/Lys-rich

Amino acid modifications

Modified residue2041N6-acetyllysine Ref.5
Modified residue2141N6-acetyllysine Ref.5
Modified residue3161N6-acetyllysine By similarity
Modified residue3171N6-acetyllysine By similarity
Cross-link180Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Experimental info

Sequence conflict271G → V in BAA08780. Ref.1
Sequence conflict144 – 1452VH → DQ in BAA08780. Ref.1
Sequence conflict2161A → G in BAA08780. Ref.1

Secondary structure

............................ 324
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51665 [UniParc].

Last modified May 10, 2002. Version 2.
Checksum: 3F7B343996B102B7

FASTA32437,025
        10         20         30         40         50         60 
MPELAVQKVV VHPLVLLSVV DHFNRIGKVG NQKRVVGVLL GSWQKKVLDV SNSFAVPFDE 

        70         80         90        100        110        120 
DDKDDSVWFL DHDYLENMYG MFKKVNARER IVGWYHTGPK LHKNDIAINE LMKRYCPNSV 

       130        140        150        160        170        180 
LVIIDVKPKD LGLPTEAYIS VEEVHDDGTP TSKTFEHVTS EIGAEEAEEV GVEHLLRDIK 

       190        200        210        220        230        240 
DTTVGTLSQR ITNQVHGLKG LNSKLLDIRS YLEKVATGKL PINHQIIYQL QDVFNLLPDV 

       250        260        270        280        290        300 
SLQEFVKAFY LKTNDQMVVV YLASLIRSVV ALHNLINNKI ANRDAEKKEG QEKEESKKDR 

       310        320 
KEDKEKDKDK EKSDVKKEEK KEKK 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10910.1.
PIRJC4154.
S65491.
RefSeqNP_002802.2. NM_002811.4.
UniGeneHs.440604.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O95X-ray1.95A/B1-186[»]
2O96X-ray3.00A/B1-177[»]
ProteinModelPortalP51665.
SMRP51665. Positions 1-288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111685. 72 interactions.
DIPDIP-27572N.
IntActP51665. 31 interactions.
MINTMINT-5002613.
STRING9606.ENSP00000219313.

Protein family/group databases

MEROPSM67.973.

PTM databases

PhosphoSiteP51665.

Polymorphism databases

DMDM20532412.

Proteomic databases

MaxQBP51665.
PaxDbP51665.
PeptideAtlasP51665.
PRIDEP51665.

Protocols and materials databases

DNASU5713.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219313; ENSP00000219313; ENSG00000103035.
GeneID5713.
KEGGhsa:5713.
UCSCuc002fcq.3. human.

Organism-specific databases

CTD5713.
GeneCardsGC16P074330.
HGNCHGNC:9565. PSMD7.
HPACAB019379.
HPA049824.
HPA056069.
MIM157970. gene.
neXtProtNX_P51665.
PharmGKBPA33911.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1310.
HOGENOMHOG000209236.
HOVERGENHBG035951.
InParanoidP51665.
KOK03038.
OMADHNYVES.
OrthoDBEOG7B8S4G.
PhylomeDBP51665.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP51665.
BgeeP51665.
CleanExHS_PSMD7.
GenevestigatorP51665.

Family and domain databases

InterProIPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPSMD7. human.
EvolutionaryTraceP51665.
GeneWikiPSMD7.
GenomeRNAi5713.
NextBio22194.
PROP51665.
SOURCESearch...

Entry information

Entry namePSMD7_HUMAN
AccessionPrimary (citable) accession number: P51665
Secondary accession number(s): D3DWS9, Q6PKI2, Q96E97
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2002
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM