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Entry version 168 (23 Feb 2022)
Sequence version 3 (09 Jan 2013)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone
Biological processApoptosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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-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-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-69481, G2/M Checkpoints
R-MMU-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-MMU-75815, Ubiquitin-dependent degradation of Cyclin D
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-8932339, ROS sensing by NFE2L2
R-MMU-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-8939902, Regulation of RUNX2 expression and activity
R-MMU-8941858, Regulation of RUNX3 expression and activity
R-MMU-8948751, Regulation of PTEN stability and activity
R-MMU-8951664, Neddylation
R-MMU-9020702, Interleukin-1 signaling
R-MMU-983168, Antigen processing: Ubiquitination & Proteasome degradation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 10
Alternative name(s):
26S proteasome regulatory subunit p28
Gankyrin
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Psmd10
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1858898, Psmd10

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSMUSG00000031429

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000670461 – 23126S proteasome non-ATPase regulatory subunit 10Add BLAST231

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9Z2X2

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9Z2X2

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9Z2X2

PeptideAtlas

More...
PeptideAtlasi
Q9Z2X2

PRoteomics IDEntifications database

More...
PRIDEi
Q9Z2X2

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
291829

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
Q9Z2X2

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9Z2X2

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9Z2X2

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by activated HRAS.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000031429, Expressed in primary oocyte and 307 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9Z2X2, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9Z2X2, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
207302, 9 interactors

Database of interacting proteins

More...
DIPi
DIP-29273N

Protein interaction database and analysis system

More...
IntActi
Q9Z2X2, 3 interactors

Molecular INTeraction database

More...
MINTi
Q9Z2X2

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000033805

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q9Z2X2, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9Z2X2

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9Z2X2

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4412, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153404

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9Z2X2

Identification of Orthologs from Complete Genome Data

More...
OMAi
WAVAYNR

Database of Orthologous Groups

More...
OrthoDBi
1514637at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9Z2X2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.20, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...
IDEALi
IID50037

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002110, Ankyrin_rpt
IPR036770, Ankyrin_rpt-contain_sf
IPR039334, PSMD10-like

The PANTHER Classification System

More...
PANTHERi
PTHR24126:SF24, PTHR24126:SF24, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00023, Ank, 1 hit
PF12796, Ank_2, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01415, ANKYRIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248, ANK, 5 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48403, SSF48403, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 5 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBCE7B9A79C91358B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2AG83A2AG83_MOUSE
26S proteasome non-ATPase regulator...
Psmd10
151Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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 No translation available.
CH466616 Genomic DNA Translation: EDL23939.1
BC026931 mRNA Translation: AAH26931.1
BC056196 mRNA Translation: AAH56196.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS30444.1

NCBI Reference Sequences

More...
RefSeqi
NP_001157649.1, NM_001164177.1
NP_058579.2, NM_016883.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000033805; ENSMUSP00000033805; ENSMUSG00000031429

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
53380

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:53380

UCSC genome browser

More...
UCSCi
uc009ulj.2, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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 No translation available.
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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DVWX-ray2.30A1-231[»]
2DWZX-ray2.40A/C1-231[»]
3AJIX-ray2.05A/C1-231[»]
SMRiQ9Z2X2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi207302, 9 interactors
DIPiDIP-29273N
IntActiQ9Z2X2, 3 interactors
MINTiQ9Z2X2
STRINGi10090.ENSMUSP00000033805

PTM databases

iPTMnetiQ9Z2X2
PhosphoSitePlusiQ9Z2X2

2D gel databases

REPRODUCTION-2DPAGEiQ9Z2X2

Proteomic databases

EPDiQ9Z2X2
MaxQBiQ9Z2X2
PaxDbiQ9Z2X2
PeptideAtlasiQ9Z2X2
PRIDEiQ9Z2X2
ProteomicsDBi291829

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
496, 442 antibodies from 33 providers

The DNASU plasmid repository

More...
DNASUi
53380

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5716
MGIiMGI:1858898, Psmd10
VEuPathDBiHostDB:ENSMUSG00000031429

Phylogenomic databases

eggNOGiKOG4412, Eukaryota
GeneTreeiENSGT00940000153404
InParanoidiQ9Z2X2
OMAiWAVAYNR
OrthoDBi1514637at2759
PhylomeDBiQ9Z2X2

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-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-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-69481, G2/M Checkpoints
R-MMU-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-MMU-75815, Ubiquitin-dependent degradation of Cyclin D
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-8932339, ROS sensing by NFE2L2
R-MMU-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-8939902, Regulation of RUNX2 expression and activity
R-MMU-8941858, Regulation of RUNX3 expression and activity
R-MMU-8948751, Regulation of PTEN stability and activity
R-MMU-8951664, Neddylation
R-MMU-9020702, Interleukin-1 signaling
R-MMU-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
53380, 0 hits in 63 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Psmd10, mouse
EvolutionaryTraceiQ9Z2X2

Protein Ontology

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PROi
PR:Q9Z2X2
RNActiQ9Z2X2, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000031429, Expressed in primary oocyte and 307 other tissues
ExpressionAtlasiQ9Z2X2, baseline and differential
GenevisibleiQ9Z2X2, MM

Family and domain databases

Gene3Di1.25.40.20, 1 hit
IDEALiIID50037
InterProiView protein in InterPro
IPR002110, Ankyrin_rpt
IPR036770, Ankyrin_rpt-contain_sf
IPR039334, PSMD10-like
PANTHERiPTHR24126:SF24, PTHR24126:SF24, 1 hit
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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPSD10_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Z2X2
Secondary accession number(s): Q8R0G2, Q9D383, Q9D7N8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: January 9, 2013
Last modified: February 23, 2022
This is version 168 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
UniProt is an ELIXIR core data resource
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