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Protein

26S proteasome non-ATPase regulatory subunit 7

Gene

PSMD7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.1 Publication

Miscellaneous

Does not bind a metal ion.

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6798695 Neutrophil degranulation
R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-HSA-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

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
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000103035.10
HGNCiHGNC:9565 PSMD7
MIMi157970 gene
neXtProtiNX_P51665

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5713
OpenTargetsiENSG00000103035
PharmGKBiPA33911

Chemistry databases

ChEMBLiCHEMBL2364701

Polymorphism and mutation databases

BioMutaiPSMD7
DMDMi20532412

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002139431 – 32426S proteasome non-ATPase regulatory subunit 7Add BLAST324

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki180Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei204N6-acetyllysineCombined sources1
Modified residuei214N6-acetyllysineCombined sources1
Modified residuei316N6-acetyllysineBy similarity1
Modified residuei317N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP51665
MaxQBiP51665
PaxDbiP51665
PeptideAtlasiP51665
PRIDEiP51665
ProteomicsDBi56361

PTM databases

iPTMnetiP51665
PhosphoSitePlusiP51665

Expressioni

Gene expression databases

BgeeiENSG00000103035
CleanExiHS_PSMD7
ExpressionAtlasiP51665 baseline and differential
GenevisibleiP51665 HS

Organism-specific databases

HPAiCAB019379
HPA049824
HPA056069

Interactioni

Subunit structurei

Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits including PSMD7, a base containing 6 ATPases and few additional components (PubMed:27428775, PubMed:27342858). Within the complex, PSMD7 interacts with subunit PSMD4 through their respective MPN domain. Interacts with TRIM5 (PubMed:22078707).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMD14O004878EBI-357659,EBI-722193

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi111685, 121 interactors
CORUMiP51665
DIPiDIP-27572N
IntActiP51665, 54 interactors
MINTiP51665
STRINGi9606.ENSP00000219313

Structurei

Secondary structure

1324
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Helixi13 – 28Combined sources16
Beta strandi36 – 56Combined sources21
Beta strandi58 – 60Combined sources3
Beta strandi67 – 70Combined sources4
Helixi72 – 83Combined sources12
Beta strandi86 – 88Combined sources3
Beta strandi90 – 96Combined sources7
Helixi105 – 112Combined sources8
Turni113 – 115Combined sources3
Beta strandi120 – 124Combined sources5
Beta strandi134 – 143Combined sources10
Beta strandi152 – 162Combined sources11
Helixi166 – 178Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O95X-ray1.95A/B1-186[»]
2O96X-ray3.00A/B1-177[»]
5GJQelectron microscopy4.50U1-324[»]
5GJRelectron microscopy3.508/U1-324[»]
5L4Kelectron microscopy4.50U1-324[»]
5LN3electron microscopy6.80U1-324[»]
5M32electron microscopy3.80n1-324[»]
5T0Celectron microscopy3.80AZ/BZ1-324[»]
5T0Gelectron microscopy4.40Z1-324[»]
5T0Helectron microscopy6.80Z1-324[»]
5T0Ielectron microscopy8.00Z1-324[»]
5T0Jelectron microscopy8.00Z1-324[»]
5VGZelectron microscopy3.70Z5-290[»]
5VHFelectron microscopy5.70Z5-290[»]
5VHHelectron microscopy6.10Z5-290[»]
5VHIelectron microscopy6.80Z5-290[»]
5VHSelectron microscopy8.80Z5-290[»]
ProteinModelPortaliP51665
SMRiP51665
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51665

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 144MPNPROSITE-ProRule annotationAdd BLAST136

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi286 – 324Glu/Lys-richAdd BLAST39

Sequence similaritiesi

Belongs to the peptidase M67A family.Curated

Phylogenomic databases

eggNOGiKOG1556 Eukaryota
COG1310 LUCA
GeneTreeiENSGT00530000063075
HOGENOMiHOG000209236
HOVERGENiHBG035951
InParanoidiP51665
KOiK03038
OMAiDAYFAVE
OrthoDBiEOG091G0DX6
PhylomeDBiP51665

Family and domain databases

CDDicd08062 MPN_RPN7_8, 1 hit
InterProiView protein in InterPro
IPR000555 JAMM/MPN+_dom
IPR037518 MPN
IPR033858 MPN_RPN7_8
IPR024969 Rpn11/EIF3F_C
PANTHERiPTHR10540:SF7 PTHR10540:SF7, 1 hit
PfamiView protein in Pfam
PF01398 JAB, 1 hit
PF13012 MitMem_reg, 1 hit
SMARTiView protein in SMART
SM00232 JAB_MPN, 1 hit
PROSITEiView protein in PROSITE
PS50249 MPN, 1 hit

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 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27G → V in BAA08780 (PubMed:7755639).Curated1
Sequence conflicti144 – 145VH → DQ in BAA08780 (PubMed:7755639).Curated2
Sequence conflicti216A → G in BAA08780 (PubMed:7755639).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiPSMD7_HUMAN
AccessioniPrimary (citable) accession number: P51665
Secondary accession number(s): D3DWS9, Q6PKI2, Q96E97
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2002
Last modified: June 20, 2018
This is version 176 of the entry and version 2 of the sequence. See 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

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

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