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Protein

26S proteasome regulatory subunit 6A

Gene

PSMC3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. PSMC3 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi227 – 234ATPSequence analysis8

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • proteasome-activating ATPase activity Source: GO_Central
  • TBP-class protein binding Source: GO_Central

GO - Biological processi

Keywordsi

Biological processHost-virus interaction
LigandATP-binding, Nucleotide-binding

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-446652. Interleukin-1 family signaling.
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-8941858. Regulation of RUNX3 expression and activity.
R-HSA-8948751. Regulation of PTEN stability and activity.
R-HSA-8951664. Neddylation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome regulatory subunit 6A
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT5
Proteasome 26S subunit ATPase 3
Proteasome subunit P50
Tat-binding protein 1
Short name:
TBP-1
Gene namesi
Name:PSMC3
Synonyms:TBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000165916.8.
HGNCiHGNC:9549. PSMC3.

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

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5702.
OpenTargetsiENSG00000165916.
PharmGKBiPA33894.

Chemistry databases

ChEMBLiCHEMBL2364701.

Polymorphism and mutation databases

BioMutaiPSMC3.
DMDMi20532406.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000846981 – 43926S proteasome regulatory subunit 6AAdd BLAST439

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei9PhosphoserineCombined sources1
Modified residuei376PhosphoserineCombined sources1

Post-translational modificationi

Sumoylated by UBE2I in response to MEKK1-mediated stimuli.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP17980.
MaxQBiP17980.
PaxDbiP17980.
PeptideAtlasiP17980.
PRIDEiP17980.

2D gel databases

REPRODUCTION-2DPAGEiIPI00018398.

PTM databases

iPTMnetiP17980.
PhosphoSitePlusiP17980.
SwissPalmiP17980.

Miscellaneous databases

PMAP-CutDBiP17980.

Expressioni

Gene expression databases

BgeeiENSG00000165916.
CleanExiHS_PSMC3.
ExpressionAtlasiP17980. baseline and differential.
GenevisibleiP17980. HS.

Organism-specific databases

HPAiHPA006065.

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, a base containing 6 ATPases including PSMC3 and few additional components (PubMed:27428775, PubMed:27342858). Interacts with PAAF1 (PubMed:15831487). Interacts with HIV-1 Tat (PubMed:2194290).4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • TBP-class protein binding Source: GO_Central

Protein-protein interaction databases

BioGridi111675. 191 interactors.
CORUMiP17980.
DIPiDIP-27555N.
IntActiP17980. 50 interactors.
MINTiMINT-1149785.
STRINGi9606.ENSP00000298852.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GJQelectron microscopy4.50M1-439[»]
5GJRelectron microscopy3.500/M1-439[»]
5L4Gelectron microscopy4.02M1-439[»]
5LN3electron microscopy6.80M1-439[»]
5M32electron microscopy3.80g1-439[»]
5T0Celectron microscopy3.80AF/BF1-439[»]
5T0Gelectron microscopy4.40F1-439[»]
5T0Helectron microscopy6.80F1-439[»]
5T0Ielectron microscopy8.00F1-439[»]
5T0Jelectron microscopy8.00F1-439[»]
5VGZelectron microscopy3.70F53-167[»]
5VHFelectron microscopy5.70F53-432[»]
5VHHelectron microscopy6.10F53-432[»]
5VHIelectron microscopy6.80F53-432[»]
5VHJelectron microscopy8.50F166-432[»]
5VHMelectron microscopy8.30F166-432[»]
5VHNelectron microscopy7.30F166-432[»]
5VHOelectron microscopy8.30F166-432[»]
5VHPelectron microscopy7.90F166-432[»]
5VHQelectron microscopy8.90F166-432[»]
5VHRelectron microscopy7.70F166-432[»]
5VHSelectron microscopy8.80F53-432[»]
ProteinModelPortaliP17980.
SMRiP17980.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0652. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00730000111070.
HOVERGENiHBG000109.
InParanoidiP17980.
KOiK03065.
OMAiRACAAQS.
OrthoDBiEOG091G07E0.
PhylomeDBiP17980.
TreeFamiTF105648.

Family and domain databases

InterProiView protein in InterPro
IPR005937. 26S_Psome_P45-like.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
IPR035254. PSMC3.
PANTHERiPTHR23073:SF7. PTHR23073:SF7. 1 hit.
PfamiView protein in Pfam
PF00004. AAA. 1 hit.
SMARTiView protein in SMART
SM00382. AAA. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiView protein in PROSITE
PS00674. AAA. 1 hit.

Sequencei

Sequence statusi: Complete.

P17980-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLLPNIESP VTRQEKMATV WDEAEQDGIG EEVLKMSTEE IIQRTRLLDS
60 70 80 90 100
EIKIMKSEVL RVTHELQAMK DKIKENSEKI KVNKTLPYLV SNVIELLDVD
110 120 130 140 150
PNDQEEDGAN IDLDSQRKGK CAVIKTSTRQ TYFLPVIGLV DAEKLKPGDL
160 170 180 190 200
VGVNKDSYLI LETLPTEYDS RVKAMEVDER PTEQYSDIGG LDKQIQELVE
210 220 230 240 250
AIVLPMNHKE KFENLGIQPP KGVLMYGPPG TGKTLLARAC AAQTKATFLK
260 270 280 290 300
LAGPQLVQMF IGDGAKLVRD AFALAKEKAP SIIFIDELDA IGTKRFDSEK
310 320 330 340 350
AGDREVQRTM LELLNQLDGF QPNTQVKVIA ATNRVDILDP ALLRSGRLDR
360 370 380 390 400
KIEFPMPNEE ARARIMQIHS RKMNVSPDVN YEELARCTDD FNGAQCKAVC
410 420 430
VEAGMIALRR GATELTHEDY MEGILEVQAK KKANLQYYA
Length:439
Mass (Da):49,204
Last modified:May 10, 2002 - v3
Checksum:i0E443465DDDEBB0B
GO

Sequence cautioni

P17980: The sequence AAI07805 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti356M → T in BAD96205 (Ref. 5) Curated1
Sequence conflicti409R → A in AAA36666 (PubMed:2194290).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK313518 mRNA. Translation: BAG36298.1.
CH471064 Genomic DNA. Translation: EAW67916.1.
BC008713 mRNA. Translation: AAH08713.4.
BC073165 mRNA. Translation: AAH73165.3.
BC106920 mRNA. Translation: AAI06921.1.
BC107804 mRNA. Translation: AAI07805.1. Different initiation.
AK222485 mRNA. Translation: BAD96205.1.
M34079 mRNA. Translation: AAA36666.1.
CR456731 mRNA. Translation: CAG33012.1.
CCDSiCCDS7935.1.
PIRiA34832.
RefSeqiNP_002795.2. NM_002804.4.
UniGeneiHs.250758.

Genome annotation databases

EnsembliENST00000298852; ENSP00000298852; ENSG00000165916.
ENST00000619920; ENSP00000481029; ENSG00000165916.
GeneIDi5702.
KEGGihsa:5702.
UCSCiuc001nfh.2. human.

Similar proteinsi

Entry informationi

Entry nameiPRS6A_HUMAN
AccessioniPrimary (citable) accession number: P17980
Secondary accession number(s): B2R8V1
, Q3B757, Q3B865, Q53HU5, Q6GPG8, Q6IBS1, Q96HD3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 10, 2002
Last modified: October 25, 2017
This is version 195 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. SIMILARITY comments
    Index of protein domains and families