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P35638

- DDIT3_HUMAN

UniProt

P35638 - DDIT3_HUMAN

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Protein

DNA damage-inducible transcript 3 protein

Gene

DDIT3

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

Functioni

Multifunctional transcription factor in ER stress response. 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. Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes. 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. Positively regulates the transcription of TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and ERO1L. 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). Inhibits the canonical Wnt signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding properties and repressing its transcriptional activity. 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.9 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. sequence-specific DNA binding Source: InterPro
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc
  4. transcription corepressor activity Source: ProtInc
  5. transcription factor binding Source: BHF-UCL

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. blood vessel maturation Source: Ensembl
  3. cell cycle arrest Source: UniProtKB-KW
  4. cell redox homeostasis Source: MGI
  5. cellular protein metabolic process Source: Reactome
  6. cellular response to DNA damage stimulus Source: ProtInc
  7. endoplasmic reticulum unfolded protein response Source: Reactome
  8. ER overload response Source: Ensembl
  9. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
  10. mRNA transcription from RNA polymerase II promoter Source: MGI
  11. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
  12. negative regulation of determination of dorsal identity Source: BHF-UCL
  13. negative regulation of myoblast differentiation Source: Ensembl
  14. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  15. negative regulation of transcription, DNA-templated Source: UniProtKB
  16. positive regulation of interleukin-8 production Source: UniProtKB
  17. positive regulation of neuron apoptotic process Source: Ensembl
  18. positive regulation of transcription, DNA-templated Source: UniProtKB
  19. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  20. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  21. regulation of DNA-templated transcription in response to stress Source: BHF-UCL
  22. regulation of transcription, DNA-templated Source: UniProtKB
  23. regulation of transcription involved in anterior/posterior axis specification Source: BHF-UCL
  24. release of sequestered calcium ion into cytosol Source: Ensembl
  25. response to endoplasmic reticulum stress Source: UniProtKB
  26. response to starvation Source: Ensembl
  27. response to unfolded protein Source: UniProtKB
  28. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Apoptosis, Cell cycle, Growth arrest, Stress response, Transcription, Transcription regulation, Unfolded protein response, Wnt signaling pathway

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_18355. ATF4 activates genes.
REACT_18423. ATF6-alpha activates chaperone genes.
SignaLinkiP35638.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA damage-inducible transcript 3 protein
Short name:
DDIT-3
Alternative name(s):
C/EBP zeta
C/EBP-homologous protein
Short name:
CHOP
C/EBP-homologous protein 10
Short name:
CHOP-10
CCAAT/enhancer-binding protein homologous protein
Growth arrest and DNA damage-inducible protein GADD153
Gene namesi
Name:DDIT3
Synonyms:CHOP, CHOP10, GADD153
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:2726. DDIT3.

Subcellular locationi

Cytoplasm. Nucleus
Note: Present in the cytoplasm under non-stressed conditions and ER stress leads to its nuclear accumulation.

GO - Cellular componenti

  1. late endosome Source: Ensembl
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
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).1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

MIMi613488. phenotype.
Orphaneti99967. Myxoid/round cell liposarcoma.
PharmGKBiPA27193.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 169169DNA damage-inducible transcript 3 proteinPRO_0000076642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine; by CK2By similarity
Modified residuei15 – 151Phosphoserine; by CK2By similarity
Modified residuei30 – 301Phosphoserine; by CK2By similarity
Modified residuei31 – 311Phosphoserine; by CK2By similarity
Modified residuei79 – 791Phosphoserine; by MAPK14By similarity
Modified residuei82 – 821Phosphoserine; by MAPK14By similarity

Post-translational modificationi

Ubiquitinated, leading to its degradation by the proteasome.1 Publication
Phosphorylation at serine residues by MAPK14 enhances its transcriptional activation activity while phosphorylation at serine residues by CK2 inhibits its transcriptional activation activity.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP35638.
PaxDbiP35638.
PRIDEiP35638.

PTM databases

PhosphoSiteiP35638.

Expressioni

Inductioni

By oxidative stress, amino-acid deprivation, hypoxia and ER stress. During ER stress, induced by a EIF2AK3/ATF4 pathway and/or ERN1/ATF6 pathway. Expression is suppressed by TLR-TRIF signaling pathway during prolonged ER stress.2 Publications

Gene expression databases

BgeeiP35638.
CleanExiHS_DDIT3.
ExpressionAtlasiP35638. baseline and differential.
GenevestigatoriP35638.

Interactioni

Subunit structurei

Heterodimer. Interacts with TCF7L2/TCF4, EP300/P300, HDAC1, HDAC5 and HDAC6. Interacts with TRIB3 which blocks its association with EP300/P300. Interacts with FOXO3, CEBPB and ATF4.6 Publications

Protein-protein interaction databases

BioGridi108016. 58 interactions.
IntActiP35638. 15 interactions.
MINTiMINT-1434413.
STRINGi9606.ENSP00000340671.

Structurei

3D structure databases

DisProtiDP00624.
ProteinModelPortaliP35638.
SMRiP35638. Positions 95-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 16264bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 2617N-terminalAdd
BLAST
Regioni10 – 189Interaction with TRIB3
Regioni101 – 13030Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni134 – 14815Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi93 – 975Poly-Glu

Domaini

The N-terminal region is necessary for its proteasomal degradation, transcriptional activity and interaction with EP300/P300.

Sequence similaritiesi

Belongs to the bZIP family.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG279524.
GeneTreeiENSGT00390000006305.
HOGENOMiHOG000089934.
HOVERGENiHBG051328.
InParanoidiP35638.
KOiK04452.
OMAiDRMVNLH.
OrthoDBiEOG7QC7Z1.
PhylomeDBiP35638.
TreeFamiTF105006.

Family and domain databases

InterProiIPR004827. bZIP.
IPR016670. DNA_damage_induc_transcript_3.
[Graphical view]
PANTHERiPTHR16833. PTHR16833. 1 hit.
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFiPIRSF016571. C/EBPzeta_CHOP_DDIT3. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35638-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAESLPFSF GTLSSWELEA WYEDLQEVLS SDENGGTYVS PPGNEEEESK
60 70 80 90 100
IFTTLDPASL AWLTEEEPEP AEVTSTSQSP HSPDSSQSSL AQEEEEEDQG
110 120 130 140 150
RTRKRKQSGH SPARAGKQRM KEKEQENERK VAQLAEENER LKQEIERLTR
160
EVEATRRALI DRMVNLHQA
Length:169
Mass (Da):19,175
Last modified:June 1, 1994 - v1
Checksum:i31905293FB1FBBE2
GO
Isoform 2 (identifier: P35638-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MELVPATPHYPADVLFQTDPTAEM

Show »
Length:192
Mass (Da):21,700
Checksum:i1C569DBC247612EB
GO

Sequence cautioni

The sequence AAB27103.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 145FGTLS → SDTV in AAB22646. (PubMed:1339368)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151A → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036000

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MELVPATPHYPADVLFQTDP TAEM in isoform 2. 1 PublicationVSP_047277

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S40706 mRNA. Translation: AAB22646.1.
S62138 mRNA. Translation: AAB27103.1. Sequence problems.
AY461580 mRNA. No translation available.
AY880949 Genomic DNA. Translation: AAW56077.1.
AC022506 Genomic DNA. No translation available.
BC003637 mRNA. Translation: AAH03637.1.
CCDSiCCDS55838.1. [P35638-2]
CCDS8943.1. [P35638-1]
PIRiJC1169.
S33798.
RefSeqiNP_001181982.1. NM_001195053.1. [P35638-2]
NP_001181983.1. NM_001195054.1. [P35638-2]
NP_001181984.1. NM_001195055.1. [P35638-2]
NP_001181986.1. NM_001195057.1. [P35638-1]
NP_004074.2. NM_004083.5. [P35638-1]
UniGeneiHs.505777.

Genome annotation databases

EnsembliENST00000346473; ENSP00000340671; ENSG00000175197. [P35638-1]
ENST00000547303; ENSP00000447188; ENSG00000175197. [P35638-1]
ENST00000551116; ENSP00000448665; ENSG00000175197. [P35638-2]
ENST00000552740; ENSP00000447803; ENSG00000175197. [P35638-2]
ENST00000618206; ENSP00000481270; ENSG00000175197.
GeneIDi1649.
KEGGihsa:1649.
UCSCiuc001soi.3. human. [P35638-1]
uc009zps.3. human.

Polymorphism databases

DMDMi544022.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S40706 mRNA. Translation: AAB22646.1 .
S62138 mRNA. Translation: AAB27103.1 . Sequence problems.
AY461580 mRNA. No translation available.
AY880949 Genomic DNA. Translation: AAW56077.1 .
AC022506 Genomic DNA. No translation available.
BC003637 mRNA. Translation: AAH03637.1 .
CCDSi CCDS55838.1. [P35638-2 ]
CCDS8943.1. [P35638-1 ]
PIRi JC1169.
S33798.
RefSeqi NP_001181982.1. NM_001195053.1. [P35638-2 ]
NP_001181983.1. NM_001195054.1. [P35638-2 ]
NP_001181984.1. NM_001195055.1. [P35638-2 ]
NP_001181986.1. NM_001195057.1. [P35638-1 ]
NP_004074.2. NM_004083.5. [P35638-1 ]
UniGenei Hs.505777.

3D structure databases

DisProti DP00624.
ProteinModelPortali P35638.
SMRi P35638. Positions 95-157.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108016. 58 interactions.
IntActi P35638. 15 interactions.
MINTi MINT-1434413.
STRINGi 9606.ENSP00000340671.

PTM databases

PhosphoSitei P35638.

Polymorphism databases

DMDMi 544022.

Proteomic databases

MaxQBi P35638.
PaxDbi P35638.
PRIDEi P35638.

Protocols and materials databases

DNASUi 1649.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000346473 ; ENSP00000340671 ; ENSG00000175197 . [P35638-1 ]
ENST00000547303 ; ENSP00000447188 ; ENSG00000175197 . [P35638-1 ]
ENST00000551116 ; ENSP00000448665 ; ENSG00000175197 . [P35638-2 ]
ENST00000552740 ; ENSP00000447803 ; ENSG00000175197 . [P35638-2 ]
ENST00000618206 ; ENSP00000481270 ; ENSG00000175197 .
GeneIDi 1649.
KEGGi hsa:1649.
UCSCi uc001soi.3. human. [P35638-1 ]
uc009zps.3. human.

Organism-specific databases

CTDi 1649.
GeneCardsi GC12M057910.
HGNCi HGNC:2726. DDIT3.
MIMi 126337. gene.
613488. phenotype.
neXtProti NX_P35638.
Orphaneti 99967. Myxoid/round cell liposarcoma.
PharmGKBi PA27193.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG279524.
GeneTreei ENSGT00390000006305.
HOGENOMi HOG000089934.
HOVERGENi HBG051328.
InParanoidi P35638.
KOi K04452.
OMAi DRMVNLH.
OrthoDBi EOG7QC7Z1.
PhylomeDBi P35638.
TreeFami TF105006.

Enzyme and pathway databases

Reactomei REACT_18355. ATF4 activates genes.
REACT_18423. ATF6-alpha activates chaperone genes.
SignaLinki P35638.

Miscellaneous databases

ChiTaRSi DDIT3. human.
GeneWikii DNA_damage-inducible_transcript_3.
GenomeRNAii 1649.
NextBioi 6792.
PROi P35638.
SOURCEi Search...

Gene expression databases

Bgeei P35638.
CleanExi HS_DDIT3.
ExpressionAtlasi P35638. baseline and differential.
Genevestigatori P35638.

Family and domain databases

InterProi IPR004827. bZIP.
IPR016670. DNA_damage_induc_transcript_3.
[Graphical view ]
PANTHERi PTHR16833. PTHR16833. 1 hit.
Pfami PF07716. bZIP_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF016571. C/EBPzeta_CHOP_DDIT3. 1 hit.
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
PROSITEi PS50217. BZIP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, characterization and chromosomal localization of the human GADD153 gene."
    Park J.S., Luethy J.D., Wang M.G., Fargnoli J., Fornace A.J. Jr., McBride O.W., Holbrook N.J.
    Gene 116:259-267(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma."
    Crozat A., Aman P., Mandahl N., Ron D.
    Nature 363:640-644(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Fusion of the dominant negative transcription regulator CHOP with a novel gene FUS by translocation t(12;16) in malignant liposarcoma."
    Rabbitts T.H., Forster A., Larson R., Nathan P.
    Nat. Genet. 4:175-180(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN MXLIPO, CHROMOSOMAL TRANSLOCATION WITH FUS.
  4. Li X., Xie Y., Mao Y.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. NIEHS SNPs program
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle.
  8. "Roles of CHOP/GADD153 in endoplasmic reticulum stress."
    Oyadomari S., Mori M.
    Cell Death Differ. 11:381-389(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. "CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells."
    Yamaguchi H., Wang H.G.
    J. Biol. Chem. 279:45495-45502(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death."
    Ohoka N., Yoshii S., Hattori T., Onozaki K., Hayashi H.
    EMBO J. 24:1243-1255(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRIB3.
  11. "The C/EBP homologous protein CHOP (GADD153) is an inhibitor of Wnt/TCF signals."
    Horndasch M., Lienkamp S., Springer E., Schmitt A., Pavenstaedt H., Walz G., Gloy J.
    Oncogene 25:3397-3407(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TCF7L2.
  12. "Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion."
    Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.
    J. Biol. Chem. 282:35687-35694(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: N-TERMINAL REGION, SUBCELLULAR LOCATION, INTERACTION WITH TRIB3; EP300; HDAC1; HDAC5 AND HDAC6, UBIQUITINATION, PROTEASOMAL DEGRADATION.
  13. "CHOP transcription factor mediates IL-8 signaling in cystic fibrosis bronchial epithelial cells."
    Vij N., Amoako M.O., Mazur S., Zeitlin P.L.
    Am. J. Respir. Cell Mol. Biol. 38:176-184(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "C/EBP homology protein (CHOP) interacts with activating transcription factor 4 (ATF4) and negatively regulates the stress-dependent induction of the asparagine synthetase gene."
    Su N., Kilberg M.S.
    J. Biol. Chem. 283:35106-35117(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATF4.
  15. "Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling."
    Woo C.W., Cui D., Arellano J., Dorweiler B., Harding H., Fitzgerald K.A., Ron D., Tabas I.
    Nat. Cell Biol. 11:1473-1480(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  16. "ER stress-inducible factor CHOP affects the expression of hepcidin by modulating C/EBPalpha activity."
    Oliveira S.J., Pinto J.P., Picarote G., Costa V.M., Carvalho F., Rangel M., de Sousa M., de Almeida S.F.
    PLoS ONE 4:E6618-E6618(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Endoplasmic reticulum stress-activated C/EBP homologous protein enhances nuclear factor-kappaB signals via repression of peroxisome proliferator-activated receptor gamma."
    Park S.H., Choi H.J., Yang H., Do K.H., Kim J., Lee D.W., Moon Y.
    J. Biol. Chem. 285:35330-35339(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CEBPB, INDUCTION.
  18. "Endoplasmic reticulum stress-induced transcription factor, CHOP, is crucial for dendritic cell IL-23 expression."
    Goodall J.C., Wu C., Zhang Y., McNeill L., Ellis L., Saudek V., Gaston J.S.
    Proc. Natl. Acad. Sci. U.S.A. 107:17698-17703(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "CHOP is a multifunctional transcription factor in the ER stress response."
    Nishitoh H.
    J. Biochem. 151:217-219(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  20. "CHOP potentially co-operates with FOXO3a in neuronal cells to regulate PUMA and BIM expression in response to ER stress."
    Ghosh A.P., Klocke B.J., Ballestas M.E., Roth K.A.
    PLoS ONE 7:E39586-E39586(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FOXO3, SUBCELLULAR LOCATION.
  21. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-115.

Entry informationi

Entry nameiDDIT3_HUMAN
AccessioniPrimary (citable) accession number: P35638
Secondary accession number(s): F8VS99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 144 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3