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Protein

26S proteasome non-ATPase regulatory subunit 3

Gene

PSMD3

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 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:HS03089-MONOMER.
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-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 3
Alternative name(s):
26S proteasome regulatory subunit RPN3
26S proteasome regulatory subunit S3
Proteasome subunit p58
Gene namesi
Name:PSMD3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9560. PSMD3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • proteasome accessory complex Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome regulatory particle, lid subcomplex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5709.
OpenTargetsiENSG00000108344.
PharmGKBiPA38123.

Polymorphism and mutation databases

BioMutaiPSMD3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001738161 – 53426S proteasome non-ATPase regulatory subunit 3Add BLAST534

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei418PhosphoserineCombined sources1
Modified residuei430PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO43242.
MaxQBiO43242.
PaxDbiO43242.
PeptideAtlasiO43242.
PRIDEiO43242.

PTM databases

iPTMnetiO43242.
PhosphoSitePlusiO43242.
SwissPalmiO43242.

Expressioni

Gene expression databases

BgeeiENSG00000108344.
CleanExiHS_PSMD3.
ExpressionAtlasiO43242. baseline and differential.
GenevisibleiO43242. HS.

Organism-specific databases

HPAiCAB017038.
HPA048972.

Interactioni

Subunit structurei

The 26S proteasome is composed of a core protease, known as the 20S proteasome, capped at one or both ends by the 19S regulatory complex (RC). The RC is composed of at least 18 different subunits in two subcomplexes, the base and the lid, which form the portions proximal and distal to the 20S proteolytic core, respectively (By similarity). Interacts with UBQLN1 (via ubiquitin-like domain).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP44Q9C0F13EBI-357622,EBI-744115
PLCG2P168852EBI-357622,EBI-617403
SHFM1P608963EBI-357622,EBI-79819
ZBTB43O432985EBI-357622,EBI-740718

Protein-protein interaction databases

BioGridi111682. 128 interactors.
DIPiDIP-27571N.
IntActiO43242. 43 interactors.
MINTiMINT-5003834.
STRINGi9606.ENSP00000264639.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GJQelectron microscopy4.50S1-534[»]
5GJRelectron microscopy3.506/S1-525[»]
5L4Kelectron microscopy4.50S1-534[»]
5T0Celectron microscopy3.80AV/BV2-534[»]
5T0Gelectron microscopy4.40V2-534[»]
5T0Helectron microscopy6.80V2-534[»]
5T0Ielectron microscopy8.00V2-534[»]
5T0Jelectron microscopy8.00V2-534[»]
ProteinModelPortaliO43242.
SMRiO43242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini358 – 462PCIAdd BLAST105

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi26 – 32Poly-Pro7

Sequence similaritiesi

Belongs to the proteasome subunit S3 family.Curated
Contains 1 PCI domain.Curated

Phylogenomic databases

eggNOGiKOG2581. Eukaryota.
ENOG410XS40. LUCA.
GeneTreeiENSGT00490000043406.
HOGENOMiHOG000193909.
HOVERGENiHBG000703.
InParanoidiO43242.
KOiK03033.
OMAiEKKNQDV.
OrthoDBiEOG091G05QN.
PhylomeDBiO43242.
TreeFamiTF106110.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProiIPR013586. 26S_Psome_reg_C.
IPR000717. PCI_dom.
IPR011990. TPR-like_helical_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
PF08375. Rpn3_C. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43242-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKQEGSARRR GADKAKPPPG GGEQEPPPPP APQDVEMKEE AATGGGSTGE
60 70 80 90 100
ADGKTAAAAA EHSQRELDTV TLEDIKEHVK QLEKAVSGKE PRFVLRALRM
110 120 130 140 150
LPSTSRRLNH YVLYKAVQGF FTSNNATRDF LLPFLEEPMD TEADLQFRPR
160 170 180 190 200
TGKAASTPLL PEVEAYLQLL VVIFMMNSKR YKEAQKISDD LMQKISTQNR
210 220 230 240 250
RALDLVAAKC YYYHARVYEF LDKLDVVRSF LHARLRTATL RHDADGQATL
260 270 280 290 300
LNLLLRNYLH YSLYDQAEKL VSKSVFPEQA NNNEWARYLY YTGRIKAIQL
310 320 330 340 350
EYSEARRTMT NALRKAPQHT AVGFKQTVHK LLIVVELLLG EIPDRLQFRQ
360 370 380 390 400
PSLKRSLMPY FLLTQAVRTG NLAKFNQVLD QFGEKFQADG TYTLIIRLRH
410 420 430 440 450
NVIKTGVRMI SLSYSRISLA DIAQKLQLDS PEDAEFIVAK AIRDGVIEAS
460 470 480 490 500
INHEKGYVQS KEMIDIYSTR EPQLAFHQRI SFCLDIHNMS VKAMRFPPKS
510 520 530
YNKDLESAEE RREREQQDLE FAKEMAEDDD DSFP
Length:534
Mass (Da):60,978
Last modified:May 10, 2002 - v2
Checksum:i3B3FB5593542C078
GO
Isoform 2 (identifier: O43242-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.
     493-534: AMRFPPKSYNKDLESAEERREREQQDLEFAKEMAEDDDDSFP → GW

Note: No experimental confirmation available.
Show »
Length:356
Mass (Da):41,184
Checksum:i62E7EA02B14DAE1B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti60A → V in BAA23651 (PubMed:9017604).Curated1
Sequence conflicti157 – 158TP → NT in AAH12302 (PubMed:15489334).Curated2
Sequence conflicti304E → V in AAH12302 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0563621 – 138Missing in isoform 2. 1 PublicationAdd BLAST138
Alternative sequenceiVSP_056363493 – 534AMRFP…DDSFP → GW in isoform 2. 1 PublicationAdd BLAST42

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D67025 mRNA. Translation: BAA23651.1.
BT007217 mRNA. Translation: AAP35881.1.
AK022896 mRNA. Translation: BAG51131.1.
AK300081 mRNA. Translation: BAG61884.1.
AC090844 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60625.1.
BC000074 mRNA. Translation: AAH00074.1.
BC004859 mRNA. Translation: AAH04859.1.
BC012302 mRNA. Translation: AAH12302.1.
BC020518 mRNA. Translation: AAH20518.1.
BC025686 mRNA. Translation: AAH25686.1.
CCDSiCCDS11356.1. [O43242-1]
RefSeqiNP_002800.2. NM_002809.3. [O43242-1]
UniGeneiHs.12970.

Genome annotation databases

EnsembliENST00000264639; ENSP00000264639; ENSG00000108344. [O43242-1]
GeneIDi5709.
KEGGihsa:5709.
UCSCiuc002htn.3. human. [O43242-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D67025 mRNA. Translation: BAA23651.1.
BT007217 mRNA. Translation: AAP35881.1.
AK022896 mRNA. Translation: BAG51131.1.
AK300081 mRNA. Translation: BAG61884.1.
AC090844 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60625.1.
BC000074 mRNA. Translation: AAH00074.1.
BC004859 mRNA. Translation: AAH04859.1.
BC012302 mRNA. Translation: AAH12302.1.
BC020518 mRNA. Translation: AAH20518.1.
BC025686 mRNA. Translation: AAH25686.1.
CCDSiCCDS11356.1. [O43242-1]
RefSeqiNP_002800.2. NM_002809.3. [O43242-1]
UniGeneiHs.12970.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GJQelectron microscopy4.50S1-534[»]
5GJRelectron microscopy3.506/S1-525[»]
5L4Kelectron microscopy4.50S1-534[»]
5T0Celectron microscopy3.80AV/BV2-534[»]
5T0Gelectron microscopy4.40V2-534[»]
5T0Helectron microscopy6.80V2-534[»]
5T0Ielectron microscopy8.00V2-534[»]
5T0Jelectron microscopy8.00V2-534[»]
ProteinModelPortaliO43242.
SMRiO43242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111682. 128 interactors.
DIPiDIP-27571N.
IntActiO43242. 43 interactors.
MINTiMINT-5003834.
STRINGi9606.ENSP00000264639.

PTM databases

iPTMnetiO43242.
PhosphoSitePlusiO43242.
SwissPalmiO43242.

Polymorphism and mutation databases

BioMutaiPSMD3.

Proteomic databases

EPDiO43242.
MaxQBiO43242.
PaxDbiO43242.
PeptideAtlasiO43242.
PRIDEiO43242.

Protocols and materials databases

DNASUi5709.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264639; ENSP00000264639; ENSG00000108344. [O43242-1]
GeneIDi5709.
KEGGihsa:5709.
UCSCiuc002htn.3. human. [O43242-1]

Organism-specific databases

CTDi5709.
DisGeNETi5709.
GeneCardsiPSMD3.
HGNCiHGNC:9560. PSMD3.
HPAiCAB017038.
HPA048972.
neXtProtiNX_O43242.
OpenTargetsiENSG00000108344.
PharmGKBiPA38123.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2581. Eukaryota.
ENOG410XS40. LUCA.
GeneTreeiENSGT00490000043406.
HOGENOMiHOG000193909.
HOVERGENiHBG000703.
InParanoidiO43242.
KOiK03033.
OMAiEKKNQDV.
OrthoDBiEOG091G05QN.
PhylomeDBiO43242.
TreeFamiTF106110.

Enzyme and pathway databases

BioCyciZFISH:HS03089-MONOMER.
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-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPSMD3. human.
GeneWikiiPSMD3.
GenomeRNAii5709.
PROiO43242.

Gene expression databases

BgeeiENSG00000108344.
CleanExiHS_PSMD3.
ExpressionAtlasiO43242. baseline and differential.
GenevisibleiO43242. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProiIPR013586. 26S_Psome_reg_C.
IPR000717. PCI_dom.
IPR011990. TPR-like_helical_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
PF08375. Rpn3_C. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPSMD3_HUMAN
AccessioniPrimary (citable) accession number: O43242
Secondary accession number(s): B3KMW9
, B4DT72, Q96EI2, Q9BQA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 10, 2002
Last modified: November 30, 2016
This is version 162 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.