DDIT3
entrez
1649
canonical
uniprot
P35638
canonical
ensembl
ENSG00000175197
resolver
ensp
ENSP00000340671
resolver
ensp
ENSP00000447188
resolver
ensp
ENSP00000447803
resolver
ensp
ENSP00000448665
resolver
ensp
ENSP00000669772
resolver
ensp
ENSP00000669774
resolver
genesymbol
DDIT3
resolver
genesymbol_syn
CHOP
resolver
genesymbol_syn
CHOP10
resolver
genesymbol_syn
GADD153
resolver
hgnc
HGNC:2726
resolver
uniprot
F8VS99
resolver
uniprot
Q53YD1
resolver
uniprot_entry
DDIT3_HUMAN
resolver
uniprot_entry
Q53YD1_HUMAN
resolver
uniprot_sec
F8VS99
resolver
amino_acid_sequence
MAAESLPFSFGTLSSWELEAWYEDLQEVLSSDENGGTYVSPPGNEEEESKIFTTLDPASLAWLTEEEPEPAEVTSTSQSPHSPDSSQSSLAQEEEEEDQGRTRKRKQSGHSPARAGKQRMKEKEQENERKVAQLAEENERLKQEIERLTREVEATRRALIDRMVNLHQA
uniprot
proteins
disease_involvement
DISEASE: Myxoid liposarcoma (MXLIPO) [MIM:613488]: A soft tissue tumor that tends to occur in the limbs (especially the thigh) of patients ranging in age from 35 to 55 years. It is defined by the presence of a hypocellular spindle cell proliferation set in a myxoid background, often with mucin pooling. Lipoblasts tend to be small and often monovacuolated and to cluster around vessels or at the periphery of the lesion. {ECO:0000269|PubMed:7503811}. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving DDIT3 has been found in a patient with malignant myxoid liposarcoma. Translocation t(12;16)(q13;p11) with FUS (PubMed:7503811). {ECO:0000269|PubMed:7503811}.
uniprot
proteins
function
FUNCTION: Multifunctional transcription factor in endoplasmic reticulum (ER) stress response (PubMed:15322075, PubMed:15775988, PubMed:19672300). Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress (PubMed:15322075, PubMed:15775988). Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes (By similarity). Acts as a dominant-negative regulator of C/EBP-induced transcription: dimerizes with members of the C/EBP family, impairs their association with C/EBP binding sites in the promoter regions, and inhibits the expression of C/EBP regulated genes (By similarity). Positively regulates the transcription of TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and ERO1L (PubMed:15775988, PubMed:17709599, PubMed:20876114, PubMed:22761832). Negatively regulates; expression of BCL2 and MYOD1, ATF4-dependent transcriptional activation of asparagine synthetase (ASNS), CEBPA-dependent transcriptional activation of hepcidin (HAMP) and CEBPB-mediated expression of peroxisome proliferator-activated receptor gamma (PPARG) (PubMed:18940792, PubMed:19672300, PubMed:20829347). Together with ATF4, mediates ER-mediated cell death by promoting expression of genes involved in cellular amino acid metabolic processes, mRNA translation and the unfolded protein response (UPR) in response to ER stress (By similarity). Inhibits the canonical Wnt signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding properties and repressing its transcriptional activity (PubMed:16434966). Plays a regulatory role in the inflammatory response through the induction of caspase-11 (CASP4/CASP11) which induces the activation of caspase-1 (CASP1) and both these caspases increase the activation of pro-IL1B to mature IL1B which is involved in the inflammatory response (By similarity). Acts as a major regulator of postnatal neovascularization through regulation of endothelial nitric oxide synthase (NOS3)-related signaling (By similarity). {ECO:0000250|UniProtKB:P35639, ECO:0000269|PubMed:15322075, ECO:0000269|PubMed:15775988, ECO:0000269|PubMed:16434966, ECO:0000269|PubMed:17709599, ECO:0000269|PubMed:18940792, ECO:0000269|PubMed:19672300, ECO:0000269|PubMed:20829347, ECO:0000269|PubMed:20876114, ECO:0000269|PubMed:22761832}.
uniprot
proteins
mass_dalton
19175
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated, leading to its degradation by the proteasome. {ECO:0000269|PubMed:17872950}.; PTM: Phosphorylation at serine residues by MAPK14 enhances its transcriptional activation activity while phosphorylation at serine residues by CK2 inhibits its transcriptional activation activity. {ECO:0000250}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
pubmed
1339368
uniprot
proteins
pubmed
14685163
uniprot
proteins
pubmed
15322075
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15775988
uniprot
proteins
pubmed
16434966
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17709599
uniprot
proteins
pubmed
17872950
uniprot
proteins
pubmed
18940792
uniprot
proteins
pubmed
19672300
uniprot
proteins
pubmed
19855386
uniprot
proteins
pubmed
20829347
uniprot
proteins
pubmed
20876114
uniprot
proteins
pubmed
22210905
uniprot
proteins
pubmed
22761832
uniprot
proteins
pubmed
29083303
uniprot
proteins
pubmed
33384352
uniprot
proteins
pubmed
7503811
uniprot
proteins
pubmed
8510758
uniprot
proteins
sequence_length
169
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29083303}. Nucleus {ECO:0000269|PubMed:29083303, ECO:0000269|PubMed:33384352}. Note=Present in the cytoplasm under non-stressed conditions and ER stress leads to its nuclear accumulation. {ECO:0000269|PubMed:29083303}.
uniprot
proteins