Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - O35593 (PSDE_MOUSE)

Entry version 162 (02 Dec 2020)
Sequence version 2 (31 Aug 2004)
Previous versions | rss
Add a publicationFeedback
Protein

26S proteasome non-ATPase regulatory subunit 14

Gene

Psmd14

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

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. The PSMD14 subunit is a metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi113Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi115Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi126Zinc; catalyticPROSITE-ProRule annotation1

<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 - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHydrolase, Metalloprotease, Protease
Biological processDNA damage, DNA repair, Ubl conjugation pathway
LigandMetal-binding, Zinc

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-5689901, Metalloprotease DUBs
R-MMU-6798695, Neutrophil degranulation
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-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

Protein family/group databases

MEROPS protease database

More...MEROPSi		M67.001

<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 14 (EC:3.4.19.-)
Alternative name(s):
26S proteasome regulatory subunit RPN11
MAD1
<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:Psmd14
Synonyms:Pad1
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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 2

Organism-specific databases

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

More...MGIi		MGI:1913284, Psmd14

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Proteasome

<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_00002139531 – 31026S proteasome non-ATPase regulatory subunit 14Add BLAST310

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei150PhosphoserineBy similarity1
Modified residuei224PhosphoserineBy similarity1
Modified residuei266PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O35593

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O35593

MaxQB - The MaxQuant DataBase

More...MaxQBi		O35593

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

More...PaxDbi		O35593

PeptideAtlas

More...PeptideAtlasi		O35593

PRoteomics IDEntifications database

More...PRIDEi		O35593

Consortium for Top Down Proteomics

More...TopDownProteomicsi		O35593

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		O35593

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O35593

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

More...PhosphoSitePlusi		O35593

SwissPalm database of S-palmitoylation events

More...SwissPalmi		O35593

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000026914, Expressed in olfactory bulb and 312 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O35593, 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

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 including PSMD4, a base containing 6 ATPases and few additional components. Within the complex, PSMD4 interacts with subunit PSMD7 through their respective MPN domain.

Interacts with TXNL1.

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		208496, 61 interactors

Protein interaction database and analysis system

More...IntActi		O35593, 45 interactors

Molecular INTeraction database

More...MINTi		O35593

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000028278

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O35593, 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

3D structure databases

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

More...SMRi		O35593

Database of comparative protein structure models

More...ModBasei		Search...

<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 <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini31 – 166MPNPROSITE-ProRule annotationAdd BLAST136

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi113 – 126JAMM motifPROSITE-ProRule annotationAdd BLAST14

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M67A family. PSMD14 subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1555, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00730000111116

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_052991_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O35593

Identification of Orthologs from Complete Genome Data

More...OMAi		KTGRHEM

Database of Orthologous Groups

More...OrthoDBi		1031881at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O35593

TreeFam database of animal gene trees

More...TreeFami		TF105748

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000555, JAMM/MPN+_dom
IPR037518, MPN
IPR035299, PSMD14
IPR024969, Rpn11/EIF3F_C

The PANTHER Classification System

More...PANTHERi		PTHR10410:SF22, PTHR10410:SF22, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01398, JAB, 1 hit
PF13012, MitMem_reg, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00232, JAB_MPN, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50249, MPN, 1 hit

<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>Sequencei

<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.

O35593-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDRLLRLGGG MPGLGQGPPT DAPAVDTAEQ VYISSLALLK MLKHGRAGVP 
        60         70         80         90        100
MEVMGLMLGE FVDDYTVRVI DVFAMPQSGT GVSVEAVDPV FQAKMLDMLK 
       110        120        130        140        150
QTGRPEMVVG WYHSHPGFGC WLSGVDINTQ QSFEALSERA VAVVVDPIQS 
       160        170        180        190        200
VKGKVVIDAF RLINANMMVL GHEPRQTTSN LGHLNKPSIQ ALIHGLNRHY 
       210        220        230        240        250
YSITINYRKN ELEQKMLLNL HKKSWMEGLT LQDYSEHCKH NESVVKEMLE 
       260        270        280        290        300
LAKNYNKAVE EEDKMTPEQL AIKNVGKQDP KRHLEEHVDV LMTSNIVQCL 
       310
AAMLDTVVFK
Length:310
Mass (Da):34,577
Last modified:August 31, 2004 - v2
<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:i18ACE876C7682039
GO

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 conflicti15 – 17GQG → AR in CAA73514 (PubMed:9727008).Curated3

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
Y13071 mRNA Translation: CAA73514.1
AK012013 mRNA Translation: BAB27974.1
AK151104 mRNA Translation: BAE30114.1
AK151733 mRNA Translation: BAE30648.1
BC003742 mRNA Translation: AAH03742.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS38127.1

NCBI Reference Sequences

More...RefSeqi		NP_067501.2, NM_021526.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000028278; ENSMUSP00000028278; ENSMUSG00000026914

Database of genes from NCBI RefSeq genomes

More...GeneIDi		59029

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:59029

UCSC genome browser

More...UCSCi		uc008jvc.1, 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
Y13071 mRNA Translation: CAA73514.1
AK012013 mRNA Translation: BAB27974.1
AK151104 mRNA Translation: BAE30114.1
AK151733 mRNA Translation: BAE30648.1
BC003742 mRNA Translation: AAH03742.1
CCDSiCCDS38127.1
RefSeqiNP_067501.2, NM_021526.2

3D structure databases

SMRiO35593
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi208496, 61 interactors
IntActiO35593, 45 interactors
MINTiO35593
STRINGi10090.ENSMUSP00000028278

Protein family/group databases

MEROPSiM67.001

PTM databases

iPTMnetiO35593
PhosphoSitePlusiO35593
SwissPalmiO35593

2D gel databases

REPRODUCTION-2DPAGEiO35593

Proteomic databases

EPDiO35593
jPOSTiO35593
MaxQBiO35593
PaxDbiO35593
PeptideAtlasiO35593
PRIDEiO35593
TopDownProteomicsiO35593

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1047, 239 antibodies

Genome annotation databases

EnsembliENSMUST00000028278; ENSMUSP00000028278; ENSMUSG00000026914
GeneIDi59029
KEGGimmu:59029
UCSCiuc008jvc.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		10213
MGIiMGI:1913284, Psmd14

Phylogenomic databases

eggNOGiKOG1555, Eukaryota
GeneTreeiENSGT00730000111116
HOGENOMiCLU_052991_0_1_1
InParanoidiO35593
OMAiKTGRHEM
OrthoDBi1031881at2759
PhylomeDBiO35593
TreeFamiTF105748

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-5689901, Metalloprotease DUBs
R-MMU-6798695, Neutrophil degranulation
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-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

More...BioGRID-ORCSi		59029, 10 hits in 17 CRISPR screens

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

More...ChiTaRSi		Psmd14, mouse

Protein Ontology

More...PROi		PR:O35593
RNActiO35593, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000026914, Expressed in olfactory bulb and 312 other tissues
GenevisibleiO35593, MM

Family and domain databases

InterProiView protein in InterPro
IPR000555, JAMM/MPN+_dom
IPR037518, MPN
IPR035299, PSMD14
IPR024969, Rpn11/EIF3F_C
PANTHERiPTHR10410:SF22, PTHR10410:SF22, 1 hit
PfamiView protein in Pfam
PF01398, JAB, 1 hit
PF13012, MitMem_reg, 1 hit
SMARTiView protein in SMART
SM00232, JAB_MPN, 1 hit
PROSITEiView protein in PROSITE
PS50249, MPN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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 nameiPSDE_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: O35593
Secondary accession number(s): Q3UB50, Q9CZY6
<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: August 31, 2004
Last sequence update: August 31, 2004
Last modified: December 2, 2020
This is version 162 of the entry and version 2 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

Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again