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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 pathway, 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

Keywordsi

Molecular functionChaperone
Biological processApoptosis

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
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-382556. ABC-family proteins mediated transport.
R-MMU-446652. Interleukin-1 family signaling.
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-5689603. UCH proteinases.
R-MMU-5689880. Ub-specific processing proteases.
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-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-MMU-8939236. RUNX1 regulates transcription of genes involved in differentiation of HSCs.
R-MMU-8941858. Regulation of RUNX3 expression and activity.
R-MMU-8948751. Regulation of PTEN stability and activity.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1858898. Psmd10.

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000670461 – 23126S proteasome non-ATPase regulatory subunit 10Add BLAST231

Proteomic databases

EPDiQ9Z2X2.
MaxQBiQ9Z2X2.
PaxDbiQ9Z2X2.
PeptideAtlasiQ9Z2X2.
PRIDEiQ9Z2X2.

2D gel databases

REPRODUCTION-2DPAGEiQ9Z2X2.

PTM databases

iPTMnetiQ9Z2X2.
PhosphoSitePlusiQ9Z2X2.

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

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Helixi9 – 16Combined sources8
Helixi19 – 28Combined sources10
Helixi30 – 34Combined sources5
Helixi43 – 50Combined sources8
Helixi53 – 61Combined sources9
Helixi76 – 83Combined sources8
Helixi86 – 94Combined sources9
Helixi109 – 115Combined sources7
Helixi119 – 127Combined sources9
Helixi142 – 149Combined sources8
Helixi152 – 160Combined sources9
Helixi175 – 181Combined sources7
Helixi185 – 193Combined sources9
Helixi208 – 211Combined sources4
Helixi214 – 229Combined sources16

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9Z2X2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati3 – 36ANK 1Add BLAST34
Repeati37 – 69ANK 2Add BLAST33
Repeati70 – 102ANK 3Add BLAST33
Repeati103 – 135ANK 4Add BLAST33
Repeati136 – 168ANK 5Add BLAST33
Repeati169 – 201ANK 6Add BLAST33
Repeati202 – 226ANK 7Add BLAST25

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG4412. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00900000140840.
HOGENOMiHOG000158359.
HOVERGENiHBG053737.
InParanoidiQ9Z2X2.
KOiK06694.
OMAiSVNQNGC.
OrthoDBiEOG091G0KEZ.

Family and domain databases

CDDicd00204. ANK. 1 hit.
Gene3Di1.25.40.20. 3 hits.
InterProiView protein in InterPro
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR036770. Ankyrin_rpt-contain_sf.
PfamiView protein in Pfam
PF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PRINTSiPR01415. ANKYRIN.
SMARTiView protein in SMART
SM00248. ANK. 5 hits.
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiView protein in PROSITE
PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.

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

Q9Z2X2: The sequence BAB31128 differs from that shown. Reason: Frameshift at position 218.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti101A → S in BAA36969 (Ref. 1) Curated1
Sequence conflicti122A → S in BAA36969 (Ref. 1) Curated1
Sequence conflicti226S → G in BAB26053 (PubMed:16141072).Curated1

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.

Similar proteinsi

Entry informationi

Entry nameiPSD10_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2X2
Secondary accession number(s): Q8R0G2, Q9D383, Q9D7N8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: January 9, 2013
Last modified: October 25, 2017
This is version 138 of the entry and version 3 of the sequence. See 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