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Protein

26S proteasome non-ATPase regulatory subunit 10

Gene

Psmd10

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

Functioni

Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module (By similarity). Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pahway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.By similarity1 Publication
Acts as an oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Apoptosis

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 proteasome non-ATPase regulatory subunit 10
Alternative name(s):
26S proteasome regulatory subunit p28
Gankyrin
Gene namesi
Name:Psmd10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1858898. Psmd10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23123126S proteasome non-ATPase regulatory subunit 10PRO_0000067046Add
BLAST

Proteomic databases

EPDiQ9Z2X2.
MaxQBiQ9Z2X2.
PaxDbiQ9Z2X2.
PeptideAtlasiQ9Z2X2.
PRIDEiQ9Z2X2.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2X2.

PTM databases

iPTMnetiQ9Z2X2.
PhosphoSiteiQ9Z2X2.

Expressioni

Inductioni

Up-regulated by activated HRAS.1 Publication

Gene expression databases

BgeeiENSMUSG00000031429.
ExpressionAtlasiQ9Z2X2. baseline and differential.
GenevisibleiQ9Z2X2. MM.

Interactioni

Subunit structurei

Part of transient complex containing PSMD10, PSMC4, PSMC5 and PAAF1 formed during the assembly of the 26S proteasome. Stays associated throughout the assembly of the PA700/19S RC and is released upon association with the 20S core. Interacts with PSMC4. Interacts with RB1. Interacts with CDK4. Interacts with MDM2. Interacts with RELA. Associates with a CDK4:CCND2 serine/threonine kinase complex (By similarity). Interacts with ARHGDIA and increases the interaction between ARHGDIA and RHOA, hence promotes ARHGDIA inactivation of RHOA and ROCK (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207302. 4 interactions.
DIPiDIP-29273N.
IntActiQ9Z2X2. 2 interactions.
MINTiMINT-4108931.
STRINGi10090.ENSMUSP00000033805.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi9 – 168Combined sources
Helixi19 – 2810Combined sources
Helixi30 – 345Combined sources
Helixi43 – 508Combined sources
Helixi53 – 619Combined sources
Helixi76 – 838Combined sources
Helixi86 – 949Combined sources
Helixi109 – 1157Combined sources
Helixi119 – 1279Combined sources
Helixi142 – 1498Combined sources
Helixi152 – 1609Combined sources
Helixi175 – 1817Combined sources
Helixi185 – 1939Combined sources
Helixi208 – 2114Combined sources
Helixi214 – 22916Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DVWX-ray2.30A1-231[»]
2DWZX-ray2.40A/C1-231[»]
3AJIX-ray2.05A/C1-231[»]
ProteinModelPortaliQ9Z2X2.
SMRiQ9Z2X2. Positions 3-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z2X2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati3 – 3634ANK 1Add
BLAST
Repeati37 – 6933ANK 2Add
BLAST
Repeati70 – 10233ANK 3Add
BLAST
Repeati103 – 13533ANK 4Add
BLAST
Repeati136 – 16833ANK 5Add
BLAST
Repeati169 – 20133ANK 6Add
BLAST
Repeati202 – 22625ANK 7Add
BLAST

Sequence similaritiesi

Contains 7 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG4412. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129743.
HOGENOMiHOG000158359.
HOVERGENiHBG053737.
InParanoidiQ9Z2X2.
KOiK06694.
OMAiCSAGHTN.
OrthoDBiEOG091G0KEZ.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z2X2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGCVSNIMI CNLAYSGKLD ELKERILADK SLATRTDQDS RTALHWACSA
60 70 80 90 100
GHTEIVEFLL QLGVPVNDKD DAGWSPLHIA ASAGRDEIVK ALLVKGAHVN
110 120 130 140 150
AVNQNGCTPL HYAASKNRHE IAVMLLEGGA NPDAKDHYDA TAMHRAAAKG
160 170 180 190 200
NLKMVHILLF YKASTNIQDT EGNTPLHLAC DEERVEEAKF LVTQGASIYI
210 220 230
ENKEEKTPLQ VAKGGLGLIL KRLAESEEAS M
Length:231
Mass (Da):25,084
Last modified:January 9, 2013 - v3
Checksum:iBCE7B9A79C91358B
GO

Sequence cautioni

The sequence BAB31128 differs from that shown. Reason: Frameshift at position 218. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011A → S in BAA36969 (Ref. 1) Curated
Sequence conflicti122 – 1221A → S in BAA36969 (Ref. 1) Curated
Sequence conflicti226 – 2261S → G in BAB26053 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022022 mRNA. Translation: BAA36969.1.
AK009068 mRNA. Translation: BAB26053.1.
AK018233 mRNA. Translation: BAB31128.1. Frameshift.
AK136400 mRNA. Translation: BAE22964.1.
AL672306 Genomic DNA. Translation: CAM15395.1.
CH466616 Genomic DNA. Translation: EDL23939.1.
BC026931 mRNA. Translation: AAH26931.1.
BC056196 mRNA. Translation: AAH56196.1.
CCDSiCCDS30444.1.
RefSeqiNP_001157649.1. NM_001164177.1.
NP_058579.2. NM_016883.4.
UniGeneiMm.17640.

Genome annotation databases

EnsembliENSMUST00000033805; ENSMUSP00000033805; ENSMUSG00000031429.
GeneIDi53380.
KEGGimmu:53380.
UCSCiuc009ulj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022022 mRNA. Translation: BAA36969.1.
AK009068 mRNA. Translation: BAB26053.1.
AK018233 mRNA. Translation: BAB31128.1. Frameshift.
AK136400 mRNA. Translation: BAE22964.1.
AL672306 Genomic DNA. Translation: CAM15395.1.
CH466616 Genomic DNA. Translation: EDL23939.1.
BC026931 mRNA. Translation: AAH26931.1.
BC056196 mRNA. Translation: AAH56196.1.
CCDSiCCDS30444.1.
RefSeqiNP_001157649.1. NM_001164177.1.
NP_058579.2. NM_016883.4.
UniGeneiMm.17640.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DVWX-ray2.30A1-231[»]
2DWZX-ray2.40A/C1-231[»]
3AJIX-ray2.05A/C1-231[»]
ProteinModelPortaliQ9Z2X2.
SMRiQ9Z2X2. Positions 3-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207302. 4 interactions.
DIPiDIP-29273N.
IntActiQ9Z2X2. 2 interactions.
MINTiMINT-4108931.
STRINGi10090.ENSMUSP00000033805.

PTM databases

iPTMnetiQ9Z2X2.
PhosphoSiteiQ9Z2X2.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2X2.

Proteomic databases

EPDiQ9Z2X2.
MaxQBiQ9Z2X2.
PaxDbiQ9Z2X2.
PeptideAtlasiQ9Z2X2.
PRIDEiQ9Z2X2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033805; ENSMUSP00000033805; ENSMUSG00000031429.
GeneIDi53380.
KEGGimmu:53380.
UCSCiuc009ulj.2. mouse.

Organism-specific databases

CTDi5716.
MGIiMGI:1858898. Psmd10.

Phylogenomic databases

eggNOGiKOG4412. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129743.
HOGENOMiHOG000158359.
HOVERGENiHBG053737.
InParanoidiQ9Z2X2.
KOiK06694.
OMAiCSAGHTN.
OrthoDBiEOG091G0KEZ.

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

EvolutionaryTraceiQ9Z2X2.
PROiQ9Z2X2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031429.
ExpressionAtlasiQ9Z2X2. baseline and differential.
GenevisibleiQ9Z2X2. MM.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPSD10_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2X2
Secondary accession number(s): Q8R0G2, Q9D383, Q9D7N8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: January 9, 2013
Last modified: September 7, 2016
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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