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Entry version 127 (17 Jun 2020)
Sequence version 2 (03 Oct 2012)
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Protein

Cell death activator CIDE-3

Gene

Cidec

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

Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression.4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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 functionActivator
Biological processApoptosis, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-8964572 Lipid particle organization

<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:
Cell death activator CIDE-3
Alternative name(s):
Cell death-inducing DFFA-like effector protein C
Fat-specific protein FSP27
<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:Cidec
Synonyms:Fsp27
<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 6

Organism-specific databases

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

More...
MGIi
MGI:95585 Cidec

<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

Endoplasmic reticulum, Lipid droplet, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant animals are born in a Mendelian ratio and appear physically normal at birth. The body weights of wild-type and mutant mice fed a standard diet do not differ up to 14 weeks of age, nor does food intake. From 16 weeks of age, the body weight of mutant mice significantly decreases compared with that of wild-type mice. When animals are fed a high-fat diet, the gain in body weight is significantly smaller for mutant mice than for wild-type. Under these feeding conditions, mutant mice are also protected from insulin resistance and from accumulation of fat in the liver. The body temperature do not differ significantly between mutant and wild-type mice maintained at room temperature, but the basal rate of oxygen consumption is significantly increased in mutants.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi46R → E: Abolishes CIDE-N/CIDE-N interaction between the 2 homodimer subunits. 1 Publication1
Mutagenesisi53K → A: Slightly inhibits interaction with PLIN1. 1 Publication1
Mutagenesisi55R → E: Abolishes CIDE-N/CIDE-N interaction between the 2 homodimer subunits. 1 Publication1
Mutagenesisi75K → A: Inhibits interaction with PLIN1; when associated with A-77. 1 Publication1
Mutagenesisi77K → A: Inhibits interaction with PLIN1; when associated with A-75. 1 Publication1
Mutagenesisi86 – 88EED → QQN: Abolishes CIDE-N/CIDE-N interaction between the 2 homodimer subunits and inhibits lipid droplet enlargement. No effect on homodimerization. 1 Publication3
Mutagenesisi87 – 88ED → QN: Reduces CIDE-N/CIDE-N interaction between the 2 homodimer subunits and inhibits lipid droplet enlargement. 1 Publication2
Mutagenesisi112K → A: Slightly inhibits interaction with PLIN1; when associated with A-115. 1 Publication1
Mutagenesisi115K → A: Slightly inhibits interaction with PLIN1; when associated with A-112 or A-117. 1 Publication1
Mutagenesisi117K → A: Slightly inhibits interaction with PLIN1; when associated with A-115. 1 Publication1
Mutagenesisi182K → A: Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-186 and A-190. 1 Publication1
Mutagenesisi186K → A: Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-182 and A-190. 1 Publication1
Mutagenesisi190R → A: Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-182 and A-186. 1 Publication1
Mutagenesisi224K → A: No effect on protein stability; when associated with A-226. Drastically increased protein stability and decreased ubiquitination; when associated with A-226 and A-236. 1 Publication1
Mutagenesisi226K → A: No effect on protein stability; when associated with A-226. Drastically increased protein stability and decreased ubiquitination; when associated with A-224 and A-236. 1 Publication1
Mutagenesisi236K → A: No effect on protein stability. Drastically increased protein stability and decreased ubiquitination; when associated with A-224 and A-226. 1 Publication1

<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_00001447231 – 239Cell death activator CIDE-3Add BLAST239

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated and targeted to proteasomal degradation, resulting in a short half-life (about 15 minutes in 3T3-L1 cells). Protein stability depends on triaclyglycerol synthesis, fatty acid availability and lipid droplet formation.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

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

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PaxDbi
P56198

PRoteomics IDEntifications database

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PRIDEi
P56198

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P56198

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

More...
PhosphoSitePlusi
P56198

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed almost exclusively in adipose tissue, including subcutaneous and epididymal white adipose tissue (at protein level). Although abundantly present in brown adipose tissue at the mRNA level, the protein is almost undetectable in this tissue (PubMed:18654663), or at moderate levels (PubMed:22245780, PubMed:12910269). Expressed in the mammary gland, in stromal adipose tissue, but becomes undetectable at the end of pregnancy and during lactation (at protein level). Expressed at low levels in skeletal muscle and heart.5 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Up-regulated during differentiation into adipocytes in various cell lines, including TA1 and 3T3-L1. Decreases in the mammary gland during pregnancy from day 14.5 until 18.5, when it becomes hardly detectable, and during lactation.4 Publications

<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 under conditions that enhance triacylglycerol deposition, including rosiglitazone treatment and high-fat diet. This up-regulation is mediated by PPARG. Up-regulated by isoproterenol, a beta-agonist, and oleic acid treatment. This induction is due to protein stabilization. Down-regulated upon hypertonic conditions.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000030278 Expressed in epididymal fat pad and 97 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P56198 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P56198 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

Homodimer.

Interacts with CIDEA.

Interacts with NFAT5; this interaction is direct and retains NFAT5 in the cytoplasm (By similarity).

Interacts with CEBPB.

Interacts with PLIN1.

By similarity2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
199749, 1 interactor

Protein interaction database and analysis system

More...
IntActi
P56198, 1 interactor

Molecular INTeraction database

More...
MINTi
P56198

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000032416

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P56198 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

1239
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

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SMRi
P56198

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Domaini41 – 118CIDE-NPROSITE-ProRule annotationAdd BLAST78

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The CIDE-N domain is involved in homodimerization which is crucial for its function in promoting lipid exchange and transfer.1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IWQS Eukaryota
ENOG4111HCT LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000018596

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_090011_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P56198

TreeFam database of animal gene trees

More...
TreeFami
TF334321

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003508 CIDE-N_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02017 CIDE-N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00266 CAD, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51135 CIDE_N, 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>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 2 potential isoforms that are computationally mapped.Show allAlign All

P56198-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDYAMKSLSL LYPRSLSRHV AVSTAVVTQQ LVSKPSRETP RARPCRVSTA
60 70 80 90 100
DRKVRKGIMA HSLEDLLNKV QDILKLKDKP FSLVLEEDGT IVETEEYFQA
110 120 130 140 150
LAKDTMFMVL LKGQKWKPPS EQRKKRAQLA LSQKPTKKID VARVTFDLYK
160 170 180 190 200
LNPQDFIGCL NVKATLYDTY SLSYDLHCYK AKRIVKEMLR WTLFSMQATG
210 220 230
HMLLGTSSYM QQFLDATEEE QPAKAKPSSL LPACLKMLQ
Length:239
Mass (Da):27,324
Last modified:October 3, 2012 - 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:i7F4E6C5D2E24A161
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9QMZ0E9QMZ0_MOUSE
Cell death activator CIDE-3
Cidec
249Annotation 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>
D3Z1A6D3Z1A6_MOUSE
Cell death activator CIDE-3
Cidec
83Annotation 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>

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 conflicti188 – 189ML → IV in M61737 (PubMed:1339452).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M61737 mRNA No translation available.
AK080133 mRNA Translation: BAC37830.1
AC153910 Genomic DNA No translation available.
BC099676 mRNA Translation: AAH99676.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS20418.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A42445

NCBI Reference Sequences

More...
RefSeqi
NP_001288224.1, NM_001301295.1
NP_848460.1, NM_178373.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000032416; ENSMUSP00000032416; ENSMUSG00000030278
ENSMUST00000113089; ENSMUSP00000108712; ENSMUSG00000030278

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
14311

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:14311

UCSC genome browser

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UCSCi
uc009dgb.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
M61737 mRNA No translation available.
AK080133 mRNA Translation: BAC37830.1
AC153910 Genomic DNA No translation available.
BC099676 mRNA Translation: AAH99676.1
CCDSiCCDS20418.1
PIRiA42445
RefSeqiNP_001288224.1, NM_001301295.1
NP_848460.1, NM_178373.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IKGX-ray1.93A39-118[»]
4MACX-ray2.00A/B32-120[»]
SMRiP56198
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi199749, 1 interactor
IntActiP56198, 1 interactor
MINTiP56198
STRINGi10090.ENSMUSP00000032416

PTM databases

iPTMnetiP56198
PhosphoSitePlusiP56198

Proteomic databases

PaxDbiP56198
PRIDEiP56198

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
10363 291 antibodies

Genome annotation databases

EnsembliENSMUST00000032416; ENSMUSP00000032416; ENSMUSG00000030278
ENSMUST00000113089; ENSMUSP00000108712; ENSMUSG00000030278
GeneIDi14311
KEGGimmu:14311
UCSCiuc009dgb.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
63924
MGIiMGI:95585 Cidec

Phylogenomic databases

eggNOGiENOG410IWQS Eukaryota
ENOG4111HCT LUCA
GeneTreeiENSGT00390000018596
HOGENOMiCLU_090011_1_0_1
InParanoidiP56198
TreeFamiTF334321

Enzyme and pathway databases

ReactomeiR-MMU-8964572 Lipid particle organization

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
14311 1 hit in 12 CRISPR screens

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

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ChiTaRSi
Cidec mouse

Protein Ontology

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PROi
PR:P56198
RNActiP56198 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000030278 Expressed in epididymal fat pad and 97 other tissues
ExpressionAtlasiP56198 baseline and differential
GenevisibleiP56198 MM

Family and domain databases

InterProiView protein in InterPro
IPR003508 CIDE-N_dom
PfamiView protein in Pfam
PF02017 CIDE-N, 1 hit
SMARTiView protein in SMART
SM00266 CAD, 1 hit
PROSITEiView protein in PROSITE
PS51135 CIDE_N, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiCIDEC_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: P56198
Secondary accession number(s): Q499X5, Q8BNV7
<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: November 1, 1997
Last sequence update: October 3, 2012
Last modified: June 17, 2020
This is version 127 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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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