Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

26S proteasome non-ATPase regulatory subunit 7

Gene

PSMD7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
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_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_263873. degradation of AXIN.
REACT_263883. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
REACT_264438. degradation of DVL.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264605. Hedgehog ligand biogenesis.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268156. Degradation of GLI1 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_268718. Hedgehog 'on' state.
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_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:9565. PSMD7.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome regulatory particle Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33911.

Polymorphism and mutation databases

BioMutaiPSMD7.
DMDMi20532412.

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-acetyllysineBy similarity
Modified residuei317 – 3171N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP51665.
PaxDbiP51665.
PeptideAtlasiP51665.
PRIDEiP51665.

PTM databases

PhosphoSiteiP51665.

Expressioni

Gene expression databases

BgeeiP51665.
CleanExiHS_PSMD7.
ExpressionAtlasiP51665. baseline and differential.
GenevisibleiP51665. HS.

Organism-specific databases

HPAiCAB019379.
HPA049824.
HPA056069.

Interactioni

Subunit structurei

Homodimer. Interacts with TRIM5.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMD14O004875EBI-357659,EBI-722193

Protein-protein interaction databases

BioGridi111685. 85 interactions.
DIPiDIP-27572N.
IntActiP51665. 32 interactions.
MINTiMINT-5002613.
STRINGi9606.ENSP00000219313.

Structurei

Secondary structure

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

3D structure databases

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

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.Curated
Contains 1 MPN (JAB/Mov34) domain.Curated

Phylogenomic databases

eggNOGiCOG1310.
GeneTreeiENSGT00530000063075.
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

        10         20         30         40         50
MPELAVQKVV VHPLVLLSVV DHFNRIGKVG NQKRVVGVLL GSWQKKVLDV
60 70 80 90 100
SNSFAVPFDE DDKDDSVWFL DHDYLENMYG MFKKVNARER IVGWYHTGPK
110 120 130 140 150
LHKNDIAINE LMKRYCPNSV LVIIDVKPKD LGLPTEAYIS VEEVHDDGTP
160 170 180 190 200
TSKTFEHVTS EIGAEEAEEV GVEHLLRDIK DTTVGTLSQR ITNQVHGLKG
210 220 230 240 250
LNSKLLDIRS YLEKVATGKL PINHQIIYQL QDVFNLLPDV SLQEFVKAFY
260 270 280 290 300
LKTNDQMVVV YLASLIRSVV ALHNLINNKI ANRDAEKKEG QEKEESKKDR
310 320
KEDKEKDKDK EKSDVKKEEK KEKK
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.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271G → V in BAA08780 (PubMed:7755639).Curated
Sequence conflicti144 – 1452VH → DQ in BAA08780 (PubMed:7755639).Curated
Sequence conflicti216 – 2161A → G in BAA08780 (PubMed:7755639).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi111685. 85 interactions.
DIPiDIP-27572N.
IntActiP51665. 32 interactions.
MINTiMINT-5002613.
STRINGi9606.ENSP00000219313.

Protein family/group databases

MEROPSiM67.973.

PTM databases

PhosphoSiteiP51665.

Polymorphism and mutation databases

BioMutaiPSMD7.
DMDMi20532412.

Proteomic databases

MaxQBiP51665.
PaxDbiP51665.
PeptideAtlasiP51665.
PRIDEiP51665.

Protocols and materials databases

DNASUi5713.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5713.
GeneCardsiGC16P074330.
HGNCiHGNC:9565. PSMD7.
HPAiCAB019379.
HPA049824.
HPA056069.
MIMi157970. gene.
neXtProtiNX_P51665.
PharmGKBiPA33911.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1310.
GeneTreeiENSGT00530000063075.
HOGENOMiHOG000209236.
HOVERGENiHBG035951.
InParanoidiP51665.
KOiK03038.
OMAiDHNYVES.
OrthoDBiEOG7B8S4G.
PhylomeDBiP51665.

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
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_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_263873. degradation of AXIN.
REACT_263883. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
REACT_264438. degradation of DVL.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264605. Hedgehog ligand biogenesis.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268156. Degradation of GLI1 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_268718. Hedgehog 'on' state.
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_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
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

ChiTaRSiPSMD7. human.
EvolutionaryTraceiP51665.
GeneWikiiPSMD7.
GenomeRNAii5713.
NextBioi22194.
PROiP51665.
SOURCEiSearch...

Gene expression databases

BgeeiP51665.
CleanExiHS_PSMD7.
ExpressionAtlasiP51665. baseline and differential.
GenevisibleiP51665. HS.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "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: June 24, 2015
This is version 145 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.