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Protein

26S protease regulatory subunit 6A

Gene

Psmc3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi230 – 2378ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S protease regulatory subunit 6A
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT5
Proteasome 26S subunit ATPase 3
Tat-binding protein 1
Short name:
TBP-1
Gene namesi
Name:Psmc3
Synonyms:Tbp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1098754. Psmc3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 44244226S protease regulatory subunit 6APRO_0000084699Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei379 – 3791PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO88685.
MaxQBiO88685.
PaxDbiO88685.
PeptideAtlasiO88685.
PRIDEiO88685.

PTM databases

iPTMnetiO88685.
PhosphoSiteiO88685.

Expressioni

Gene expression databases

BgeeiO88685.
ExpressionAtlasiO88685. baseline and differential.
GenevisibleiO88685. MM.

Interactioni

Subunit structurei

May form a heterodimer with a related family member. Interacts with PAAF1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202428. 7 interactions.
IntActiO88685. 3 interactions.
MINTiMINT-4108722.
STRINGi10090.ENSMUSP00000071054.

Structurei

3D structure databases

ProteinModelPortaliO88685.
SMRiO88685. Positions 55-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0652. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00730000111070.
HOVERGENiHBG000109.
InParanoidiO88685.
KOiK03065.
OrthoDBiEOG7TMZRN.
TreeFamiTF105648.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88685-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQEMNLLPTP ESPVTRQEKM ATVWDEAEQD GIGEEVLKMS TEEIVQRTRL
60 70 80 90 100
LDSEIKIMKS EVLRVTHELQ AMKDKIKENS EKIKVNKTLP YLVSNVIELL
110 120 130 140 150
DVDPNDQEED GANIDLDSQR KGKCAVIKTS TRQTYFLPVI GLVDAEKLKP
160 170 180 190 200
GDLVGVNKDS YLILETLPTE YDSRVKAMEV DERPTEQYSD IGGLDKQIQE
210 220 230 240 250
LVEAIVLPMN HKEKFENLGI QPPKGVLMYG PPGTGKTLLA RACAAQTKAT
260 270 280 290 300
FLKLAGPQLV QMFIGDGAKL VRDAFALAKE KAPSIIFIDE LDAIGTKRFD
310 320 330 340 350
SEKAGDREVQ RTMLELLNQL DGFQPNTQVK VIAATNRVDI LDPALLRSGR
360 370 380 390 400
LDRKIEFPMP NEEARARIMQ IHSRKMNVSP DVNYEELARC TDDFNGAQCK
410 420 430 440
AVCVEAGMIA LRRGATELTH EDYMEGILEV QAKKKANLQY YA
Length:442
Mass (Da):49,549
Last modified:July 27, 2011 - v2
Checksum:iAECCFD5BAFF26C5B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701E → D in BAA32559 (PubMed:9714759).Curated
Sequence conflicti170 – 1701E → D in BAB16347 (PubMed:10945464).Curated
Sequence conflicti399 – 3991C → S in BAA32559 (PubMed:9714759).Curated
Sequence conflicti399 – 3991C → S in BAB16347 (PubMed:10945464).Curated
Sequence conflicti423 – 4231Y → H in BAA32559 (PubMed:9714759).Curated
Sequence conflicti423 – 4231Y → H in BAB16347 (PubMed:10945464).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49686 mRNA. Translation: BAA32559.1.
AB040858 Genomic DNA. Translation: BAB16347.1.
AY902337 Genomic DNA. Translation: AAX90622.1.
AL691439 Genomic DNA. Translation: CAM19025.1.
BC005783 mRNA. Translation: AAH05783.1.
CCDSiCCDS16423.1.
RefSeqiNP_032974.2. NM_008948.2.
UniGeneiMm.289832.

Genome annotation databases

EnsembliENSMUST00000067663; ENSMUSP00000071054; ENSMUSG00000002102.
GeneIDi19182.
KEGGimmu:19182.
UCSCiuc008kuf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49686 mRNA. Translation: BAA32559.1.
AB040858 Genomic DNA. Translation: BAB16347.1.
AY902337 Genomic DNA. Translation: AAX90622.1.
AL691439 Genomic DNA. Translation: CAM19025.1.
BC005783 mRNA. Translation: AAH05783.1.
CCDSiCCDS16423.1.
RefSeqiNP_032974.2. NM_008948.2.
UniGeneiMm.289832.

3D structure databases

ProteinModelPortaliO88685.
SMRiO88685. Positions 55-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202428. 7 interactions.
IntActiO88685. 3 interactions.
MINTiMINT-4108722.
STRINGi10090.ENSMUSP00000071054.

PTM databases

iPTMnetiO88685.
PhosphoSiteiO88685.

Proteomic databases

EPDiO88685.
MaxQBiO88685.
PaxDbiO88685.
PeptideAtlasiO88685.
PRIDEiO88685.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067663; ENSMUSP00000071054; ENSMUSG00000002102.
GeneIDi19182.
KEGGimmu:19182.
UCSCiuc008kuf.2. mouse.

Organism-specific databases

CTDi5702.
MGIiMGI:1098754. Psmc3.

Phylogenomic databases

eggNOGiKOG0652. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00730000111070.
HOVERGENiHBG000109.
InParanoidiO88685.
KOiK03065.
OrthoDBiEOG7TMZRN.
TreeFamiTF105648.

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPsmc3. mouse.
PROiO88685.
SOURCEiSearch...

Gene expression databases

BgeeiO88685.
ExpressionAtlasiO88685. baseline and differential.
GenevisibleiO88685. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and heterogeneous in vivo expression of Tat binding protein-1 (TBP-1) in the mouse."
    Nakamura T., Tanaka T., Takagi H., Sato M.
    Biochim. Biophys. Acta 1399:93-100(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
    Tissue: Brain.
  2. "Mouse proteasomal ATPases Psmc3 and Psmc4: genomic organization and gene targeting."
    Sakao Y., Kawai T., Takeuchi O., Copeland N.G., Gilbert D.J., Jenkins N.A., Takeda K., Akira S.
    Genomics 67:1-7(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Characterization of quantitative trait loci influencing growth and adiposity using congenic mouse strains."
    Farber C.R., Corva P.M., Medrano J.F.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CAST/EiJ.
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  6. Cited for: IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "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: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPRS6A_MOUSE
AccessioniPrimary (citable) accession number: O88685
Secondary accession number(s): Q99JN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.