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Protein

Cell death activator CIDE-A

Gene

CIDEA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a CEBPB coactivator in mammary epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter (By similarity). 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 and occurs at a lower rate than that promoted by CIDEC. When overexpressed, induces apoptosis. The physiological significance of its role in apoptosis is unclear.By similarity1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell death Source: BHF-UCL
  • lipid metabolic process Source: BHF-UCL
  • lipid storage Source: BHF-UCL
  • negative regulation of cytokine secretion Source: BHF-UCL
  • negative regulation of execution phase of apoptosis Source: BHF-UCL
  • negative regulation of lipid catabolic process Source: BHF-UCL
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  • negative regulation of tumor necrosis factor production Source: BHF-UCL
  • positive regulation of sequestering of triglyceride Source: BHF-UCL
  • regulation of apoptotic DNA fragmentation Source: BHF-UCL
  • regulation of apoptotic process Source: GO_Central
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • response to stilbenoid Source: Ensembl
  • temperature homeostasis Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Cell death activator CIDE-A
Alternative name(s):
Cell death-inducing DFFA-like effector A
Gene namesi
Name:CIDEA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:1976. CIDEA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • lipid particle Source: UniProtKB-SubCell
  • mitochondrial envelope Source: BHF-UCL
  • mitochondrion Source: BHF-UCL
  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Lipid droplet, Nucleus

Pathology & Biotechi

Involvement in diseasei

In omental and subcutaneous adipose tissue of obese patients matched for BMI, expression levels correlate with insulin sensitivity. Expression is increased 5-6 fold in the group of patients with high insulin sensitivity, compared to the insulin-resistant group. This observation is consistent with the idea that triglyceride storage in adipocytes plays an important role in sequestering triglycerides and fatty acids away from the circulation and peripheral tissues, thus enhancing insulin sensitivity in liver and muscle.

Organism-specific databases

PharmGKBiPA26514.

Polymorphism and mutation databases

BioMutaiCIDEA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219Cell death activator CIDE-APRO_0000144718Add
BLAST

Proteomic databases

PaxDbiO60543.
PeptideAtlasiO60543.
PRIDEiO60543.

PTM databases

iPTMnetiO60543.

Expressioni

Tissue specificityi

Expressed in omental and subcutaneous adipose tissue (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000176194.
CleanExiHS_CIDEA.
ExpressionAtlasiO60543. baseline and differential.
GenevisibleiO60543. HS.

Interactioni

Subunit structurei

Directly interacts with CEBPB (By similarity). Interacts with CIDEC.By similarity1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi107570. 11 interactions.
IntActiO60543. 3 interactions.
MINTiMINT-7002607.
STRINGi9606.ENSP00000320209.

Structurei

Secondary structure

1
219
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 406Combined sources
Beta strandi48 – 547Combined sources
Helixi55 – 6511Combined sources
Beta strandi69 – 713Combined sources
Beta strandi73 – 775Combined sources
Turni78 – 803Combined sources
Helixi87 – 904Combined sources
Beta strandi95 – 1039Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EELNMR-A33-110[»]
ProteinModelPortaliO60543.
SMRiO60543. Positions 33-110.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60543.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 11078CIDE-NPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CIDE-N domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IVIC. Eukaryota.
ENOG4111SUV. LUCA.
GeneTreeiENSGT00390000018596.
HOGENOMiHOG000029211.
HOVERGENiHBG050961.
InParanoidiO60543.
OMAiAQITGQF.
OrthoDBiEOG091G0H6W.
PhylomeDBiO60543.
TreeFamiTF334321.

Family and domain databases

InterProiIPR032936. CIDE-A.
IPR003508. CIDE-N_dom.
[Graphical view]
PANTHERiPTHR12306:SF8. PTHR12306:SF8. 1 hit.
PfamiPF02017. CIDE-N. 1 hit.
[Graphical view]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
PROSITEiPS51135. CIDE_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60543-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAARDYAGA LIRPLTFMGS QTKRVLFTPL MHPARPFRVS NHDRSSRRGV
60 70 80 90 100
MASSLQELIS KTLDALVIAT GLVTLVLEED GTVVDTEEFF QTLGDNTHFM
110 120 130 140 150
ILEKGQKWMP GSQHVPTCSP PKRSGIARVT FDLYRLNPKD FIGCLNVKAT
160 170 180 190 200
MYEMYSVSYD IRCTGLKGLL RSLLRFLSYS AQVTGQFLIY LGTYMLRVLD
210
DKEERPSLRS QAKGRFTCG
Length:219
Mass (Da):24,687
Last modified:August 1, 1998 - v1
Checksum:i05F704823CE71C0E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151V → F.1 Publication
Corresponds to variant rs11545881 [ dbSNP | Ensembl ].
VAR_048738

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041378 mRNA. Translation: AAC34987.1.
AY364639 mRNA. Translation: AAQ65241.1.
EF444967 Genomic DNA. Translation: ACA05966.1.
CCDSiCCDS11856.1.
RefSeqiNP_001270.1. NM_001279.3.
UniGeneiHs.249129.

Genome annotation databases

EnsembliENST00000320477; ENSP00000320209; ENSG00000176194.
GeneIDi1149.
KEGGihsa:1149.
UCSCiuc002kqt.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041378 mRNA. Translation: AAC34987.1.
AY364639 mRNA. Translation: AAQ65241.1.
EF444967 Genomic DNA. Translation: ACA05966.1.
CCDSiCCDS11856.1.
RefSeqiNP_001270.1. NM_001279.3.
UniGeneiHs.249129.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EELNMR-A33-110[»]
ProteinModelPortaliO60543.
SMRiO60543. Positions 33-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107570. 11 interactions.
IntActiO60543. 3 interactions.
MINTiMINT-7002607.
STRINGi9606.ENSP00000320209.

PTM databases

iPTMnetiO60543.

Polymorphism and mutation databases

BioMutaiCIDEA.

Proteomic databases

PaxDbiO60543.
PeptideAtlasiO60543.
PRIDEiO60543.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320477; ENSP00000320209; ENSG00000176194.
GeneIDi1149.
KEGGihsa:1149.
UCSCiuc002kqt.5. human.

Organism-specific databases

CTDi1149.
GeneCardsiCIDEA.
HGNCiHGNC:1976. CIDEA.
MIMi604440. gene.
neXtProtiNX_O60543.
PharmGKBiPA26514.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IVIC. Eukaryota.
ENOG4111SUV. LUCA.
GeneTreeiENSGT00390000018596.
HOGENOMiHOG000029211.
HOVERGENiHBG050961.
InParanoidiO60543.
OMAiAQITGQF.
OrthoDBiEOG091G0H6W.
PhylomeDBiO60543.
TreeFamiTF334321.

Miscellaneous databases

EvolutionaryTraceiO60543.
GeneWikiiCIDEA.
GenomeRNAii1149.
PROiO60543.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000176194.
CleanExiHS_CIDEA.
ExpressionAtlasiO60543. baseline and differential.
GenevisibleiO60543. HS.

Family and domain databases

InterProiIPR032936. CIDE-A.
IPR003508. CIDE-N_dom.
[Graphical view]
PANTHERiPTHR12306:SF8. PTHR12306:SF8. 1 hit.
PfamiPF02017. CIDE-N. 1 hit.
[Graphical view]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
PROSITEiPS51135. CIDE_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCIDEA_HUMAN
AccessioniPrimary (citable) accession number: O60543
Secondary accession number(s): B0YIY7, Q6UPR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: September 7, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.