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DNA damage-inducible transcript 3 protein (DDIT-3) (C/EBP zeta) (C/EBP-homologous protein) (CHOP) (C/EBP-homologous protein 10) (CHOP-10) (CCAAT/enhancer-binding protein homologous protein) (Growth arrest and DNA damage-inducible protein GADD153)

 DDIT3_HUMAN             Reviewed;         169 AA.
P35638; F8VS99;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
25-OCT-2017, entry version 175.
RecName: Full=DNA damage-inducible transcript 3 protein;
Short=DDIT-3;
AltName: Full=C/EBP zeta;
AltName: Full=C/EBP-homologous protein;
Short=CHOP;
AltName: Full=C/EBP-homologous protein 10;
Short=CHOP-10;
AltName: Full=CCAAT/enhancer-binding protein homologous protein;
AltName: Full=Growth arrest and DNA damage-inducible protein GADD153;
Name=DDIT3; Synonyms=CHOP, CHOP10, GADD153;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1339368; DOI=10.1016/0378-1119(92)90523-R;
Park J.S., Luethy J.D., Wang M.G., Fargnoli J., Fornace A.J. Jr.,
McBride O.W., Holbrook N.J.;
"Isolation, characterization and chromosomal localization of the human
GADD153 gene.";
Gene 116:259-267(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8510758; DOI=10.1038/363640a0;
Crozat A., Aman P., Mandahl N., Ron D.;
"Fusion of CHOP to a novel RNA-binding protein in human myxoid
liposarcoma.";
Nature 363:640-644(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN MXLIPO, AND
CHROMOSOMAL TRANSLOCATION WITH FUS.
PubMed=7503811; DOI=10.1038/ng0693-175;
Rabbitts T.H., Forster A., Larson R., Nathan P.;
"Fusion of the dominant negative transcription regulator CHOP with a
novel gene FUS by translocation t(12;16) in malignant liposarcoma.";
Nat. Genet. 4:175-180(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Li X., Xie Y., Mao Y.;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
REVIEW.
PubMed=14685163; DOI=10.1038/sj.cdd.4401373;
Oyadomari S., Mori M.;
"Roles of CHOP/GADD153 in endoplasmic reticulum stress.";
Cell Death Differ. 11:381-389(2004).
[9]
FUNCTION.
PubMed=15322075; DOI=10.1074/jbc.M406933200;
Yamaguchi H., Wang H.G.;
"CHOP is involved in endoplasmic reticulum stress-induced apoptosis by
enhancing DR5 expression in human carcinoma cells.";
J. Biol. Chem. 279:45495-45502(2004).
[10]
FUNCTION, AND INTERACTION WITH TRIB3.
PubMed=15775988; DOI=10.1038/sj.emboj.7600596;
Ohoka N., Yoshii S., Hattori T., Onozaki K., Hayashi H.;
"TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP
pathway and is involved in cell death.";
EMBO J. 24:1243-1255(2005).
[11]
FUNCTION, AND INTERACTION WITH TCF7L2.
PubMed=16434966; DOI=10.1038/sj.onc.1209380;
Horndasch M., Lienkamp S., Springer E., Schmitt A., Pavenstaedt H.,
Walz G., Gloy J.;
"The C/EBP homologous protein CHOP (GADD153) is an inhibitor of
Wnt/TCF signals.";
Oncogene 25:3397-3407(2006).
[12]
N-TERMINAL REGION, SUBCELLULAR LOCATION, INTERACTION WITH TRIB3;
EP300; HDAC1; HDAC5 AND HDAC6, UBIQUITINATION, AND PROTEASOMAL
DEGRADATION.
PubMed=17872950; DOI=10.1074/jbc.M703735200;
Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.;
"Critical and functional regulation of CHOP (C/EBP homologous protein)
through the N-terminal portion.";
J. Biol. Chem. 282:35687-35694(2007).
[13]
FUNCTION.
PubMed=17709599; DOI=10.1165/rcmb.2007-0197OC;
Vij N., Amoako M.O., Mazur S., Zeitlin P.L.;
"CHOP transcription factor mediates IL-8 signaling in cystic fibrosis
bronchial epithelial cells.";
Am. J. Respir. Cell Mol. Biol. 38:176-184(2008).
[14]
FUNCTION, AND INTERACTION WITH ATF4.
PubMed=18940792; DOI=10.1074/jbc.M806874200;
Su N., Kilberg M.S.;
"C/EBP homology protein (CHOP) interacts with activating transcription
factor 4 (ATF4) and negatively regulates the stress-dependent
induction of the asparagine synthetase gene.";
J. Biol. Chem. 283:35106-35117(2008).
[15]
INDUCTION.
PubMed=19855386; DOI=10.1038/ncb1996;
Woo C.W., Cui D., Arellano J., Dorweiler B., Harding H.,
Fitzgerald K.A., Ron D., Tabas I.;
"Adaptive suppression of the ATF4-CHOP branch of the unfolded protein
response by toll-like receptor signalling.";
Nat. Cell Biol. 11:1473-1480(2009).
[16]
FUNCTION.
PubMed=19672300; DOI=10.1371/journal.pone.0006618;
Oliveira S.J., Pinto J.P., Picarote G., Costa V.M., Carvalho F.,
Rangel M., de Sousa M., de Almeida S.F.;
"ER stress-inducible factor CHOP affects the expression of hepcidin by
modulating C/EBPalpha activity.";
PLoS ONE 4:E6618-E6618(2009).
[17]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CEBPB, AND INDUCTION.
PubMed=20829347; DOI=10.1074/jbc.M110.136259;
Park S.H., Choi H.J., Yang H., Do K.H., Kim J., Lee D.W., Moon Y.;
"Endoplasmic reticulum stress-activated C/EBP homologous protein
enhances nuclear factor-kappaB signals via repression of peroxisome
proliferator-activated receptor gamma.";
J. Biol. Chem. 285:35330-35339(2010).
[18]
FUNCTION.
PubMed=20876114; DOI=10.1073/pnas.1011736107;
Goodall J.C., Wu C., Zhang Y., McNeill L., Ellis L., Saudek V.,
Gaston J.S.;
"Endoplasmic reticulum stress-induced transcription factor, CHOP, is
crucial for dendritic cell IL-23 expression.";
Proc. Natl. Acad. Sci. U.S.A. 107:17698-17703(2010).
[19]
REVIEW.
PubMed=22210905; DOI=10.1093/jb/mvr143;
Nishitoh H.;
"CHOP is a multifunctional transcription factor in the ER stress
response.";
J. Biochem. 151:217-219(2012).
[20]
FUNCTION, INTERACTION WITH FOXO3, AND SUBCELLULAR LOCATION.
PubMed=22761832; DOI=10.1371/journal.pone.0039586;
Ghosh A.P., Klocke B.J., Ballestas M.E., Roth K.A.;
"CHOP potentially co-operates with FOXO3a in neuronal cells to
regulate PUMA and BIM expression in response to ER stress.";
PLoS ONE 7:E39586-E39586(2012).
[21]
VARIANT [LARGE SCALE ANALYSIS] VAL-115.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: 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.
{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}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:15775988, ECO:0000269|PubMed:16434966,
ECO:0000269|PubMed:17872950, ECO:0000269|PubMed:18940792,
ECO:0000269|PubMed:20829347, ECO:0000269|PubMed:22761832}.
-!- INTERACTION:
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-10173632, EBI-10187270;
P18847:ATF3; NbExp=4; IntAct=EBI-742651, EBI-712767;
P18848:ATF4; NbExp=3; IntAct=EBI-742651, EBI-492498;
Q8N5M1:ATPAF2; NbExp=3; IntAct=EBI-10173632, EBI-1166928;
Q16520:BATF; NbExp=6; IntAct=EBI-742651, EBI-749503;
Q9NR55:BATF3; NbExp=4; IntAct=EBI-742651, EBI-10312707;
Q86SX3:C14orf80; NbExp=2; IntAct=EBI-742651, EBI-3247115;
Q494R4:CCDC153; NbExp=3; IntAct=EBI-10173632, EBI-10241443;
P49715:CEBPA; NbExp=2; IntAct=EBI-742651, EBI-1172054;
P17676:CEBPB; NbExp=2; IntAct=EBI-742651, EBI-969696;
P49716:CEBPD; NbExp=2; IntAct=EBI-742651, EBI-7962058;
P53567:CEBPG; NbExp=3; IntAct=EBI-742651, EBI-740209;
Q9BSW2:CRACR2A; NbExp=4; IntAct=EBI-742651, EBI-739773;
Q7Z589:EMSY; NbExp=3; IntAct=EBI-10173632, EBI-6598631;
P15408:FOSL2; NbExp=5; IntAct=EBI-742651, EBI-3893419;
Q9BPX1:HSD17B14; NbExp=5; IntAct=EBI-742651, EBI-742664;
P25791:LMO2; NbExp=3; IntAct=EBI-10173632, EBI-739696;
Q8TBB1:LNX1; NbExp=4; IntAct=EBI-742651, EBI-739832;
O75971:SNAPC5; NbExp=3; IntAct=EBI-10173632, EBI-749483;
Q4ACW9:TWEAK; NbExp=3; IntAct=EBI-10173632, EBI-10241785;
Q86VQ3:TXNDC2; NbExp=4; IntAct=EBI-742651, EBI-1220595;
A5D8V6:VPS37C; NbExp=3; IntAct=EBI-10173632, EBI-2559305;
P24278:ZBTB25; NbExp=3; IntAct=EBI-10173632, EBI-739899;
Q6PJT7:ZC3H14; NbExp=3; IntAct=EBI-10173632, EBI-740660;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Present in the
cytoplasm under non-stressed conditions and ER stress leads to its
nuclear accumulation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P35638-1; Sequence=Displayed;
Name=2;
IsoId=P35638-2; Sequence=VSP_047277;
-!- INDUCTION: 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.
{ECO:0000269|PubMed:19855386, ECO:0000269|PubMed:20829347}.
-!- DOMAIN: The N-terminal region is necessary for its proteasomal
degradation, transcriptional activity and interaction with
EP300/P300.
-!- 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}.
-!- 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}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB27103.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DDIT3ID80.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ddit3/";
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EMBL; S40706; AAB22646.1; -; mRNA.
EMBL; S62138; AAB27103.1; ALT_SEQ; mRNA.
EMBL; AY461580; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY880949; AAW56077.1; -; Genomic_DNA.
EMBL; AC022506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003637; AAH03637.1; -; mRNA.
CCDS; CCDS55838.1; -. [P35638-2]
CCDS; CCDS8943.1; -. [P35638-1]
PIR; JC1169; JC1169.
PIR; S33798; S33798.
RefSeq; NP_001181982.1; NM_001195053.1. [P35638-2]
RefSeq; NP_001181983.1; NM_001195054.1. [P35638-2]
RefSeq; NP_001181984.1; NM_001195055.1. [P35638-2]
RefSeq; NP_001181986.1; NM_001195057.1. [P35638-1]
RefSeq; NP_004074.2; NM_004083.5. [P35638-1]
UniGene; Hs.505777; -.
DisProt; DP00624; -.
ProteinModelPortal; P35638; -.
SMR; P35638; -.
BioGrid; 108016; 72.
CORUM; P35638; -.
DIP; DIP-41589N; -.
IntAct; P35638; 51.
MINT; MINT-1434413; -.
STRING; 9606.ENSP00000447803; -.
ChEMBL; CHEMBL3351207; -.
iPTMnet; P35638; -.
PhosphoSitePlus; P35638; -.
BioMuta; DDIT3; -.
DMDM; 544022; -.
EPD; P35638; -.
PaxDb; P35638; -.
PeptideAtlas; P35638; -.
PRIDE; P35638; -.
DNASU; 1649; -.
Ensembl; ENST00000346473; ENSP00000340671; ENSG00000175197. [P35638-1]
Ensembl; ENST00000547303; ENSP00000447188; ENSG00000175197. [P35638-1]
Ensembl; ENST00000551116; ENSP00000448665; ENSG00000175197. [P35638-2]
Ensembl; ENST00000552740; ENSP00000447803; ENSG00000175197. [P35638-2]
GeneID; 1649; -.
KEGG; hsa:1649; -.
UCSC; uc009zps.4; human. [P35638-1]
CTD; 1649; -.
DisGeNET; 1649; -.
EuPathDB; HostDB:ENSG00000175197.10; -.
GeneCards; DDIT3; -.
HGNC; HGNC:2726; DDIT3.
HPA; HPA058416; -.
HPA; HPA068416; -.
MalaCards; DDIT3; -.
MIM; 126337; gene.
MIM; 613488; phenotype.
neXtProt; NX_P35638; -.
OpenTargets; ENSG00000175197; -.
Orphanet; 99967; Myxoid/round cell liposarcoma.
PharmGKB; PA27193; -.
eggNOG; ENOG410ISXY; Eukaryota.
eggNOG; ENOG41127XB; LUCA.
GeneTree; ENSGT00390000006305; -.
HOGENOM; HOG000089934; -.
HOVERGEN; HBG051328; -.
InParanoid; P35638; -.
KO; K04452; -.
OMA; WELEAWY; -.
OrthoDB; EOG091G0UKC; -.
PhylomeDB; P35638; -.
TreeFam; TF105006; -.
Reactome; R-HSA-380994; ATF4 activates genes.
Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
SignaLink; P35638; -.
SIGNOR; P35638; -.
ChiTaRS; DDIT3; human.
GeneWiki; DNA_damage-inducible_transcript_3; -.
GenomeRNAi; 1649; -.
PRO; PR:P35638; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000175197; -.
CleanEx; HS_DDIT3; -.
ExpressionAtlas; P35638; baseline and differential.
Genevisible; P35638; HS.
GO; GO:1990622; C:CHOP-ATF3 complex; IDA:ParkinsonsUK-UCL.
GO; GO:1990617; C:CHOP-ATF4 complex; IDA:ParkinsonsUK-UCL.
GO; GO:0036488; C:CHOP-C/EBP complex; ISS:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:ParkinsonsUK-UCL.
GO; GO:0005770; C:late endosome; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032993; C:protein-DNA complex; IDA:ParkinsonsUK-UCL.
GO; GO:0035976; C:transcription factor AP-1 complex; IEA:Ensembl.
GO; GO:0008140; F:cAMP response element binding protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0043522; F:leucine zipper domain binding; IDA:ParkinsonsUK-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IGI:ParkinsonsUK-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:ParkinsonsUK-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0036500; P:ATF6-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:0001955; P:blood vessel maturation; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IDA:CACAO.
GO; GO:0045454; P:cell redox homeostasis; IDA:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; TAS:ProtInc.
GO; GO:0006983; P:ER overload response; IEA:Ensembl.
GO; GO:0072655; P:establishment of protein localization to mitochondrion; IEA:Ensembl.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IDA:UniProtKB.
GO; GO:1990442; P:intrinsic apoptotic signaling pathway in response to nitrosative stress; IEA:Ensembl.
GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:BHF-UCL.
GO; GO:0032792; P:negative regulation of CREB transcription factor activity; IDA:ParkinsonsUK-UCL.
GO; GO:2000016; P:negative regulation of determination of dorsal identity; IDA:BHF-UCL.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:ParkinsonsUK-UCL.
GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:ParkinsonsUK-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0036499; P:PERK-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IC:ParkinsonsUK-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IC:ParkinsonsUK-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:CAFA.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IDA:CAFA.
GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; TAS:BHF-UCL.
GO; GO:0044324; P:regulation of transcription involved in anterior/posterior axis specification; ISS:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
GO; GO:0042594; P:response to starvation; IEA:Ensembl.
GO; GO:0006986; P:response to unfolded protein; IDA:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR004827; bZIP.
InterPro; IPR016670; DNA_damage_induc_transcript_3.
PANTHER; PTHR16833; PTHR16833; 1.
Pfam; PF07716; bZIP_2; 1.
PIRSF; PIRSF016571; C/EBPzeta_CHOP_DDIT3; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Apoptosis; Cell cycle;
Chromosomal rearrangement; Complete proteome; Cytoplasm; DNA-binding;
Growth arrest; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene;
Reference proteome; Repressor; Stress response; Transcription;
Transcription regulation; Ubl conjugation; Unfolded protein response;
Wnt signaling pathway.
CHAIN 1 169 DNA damage-inducible transcript 3
protein.
/FTId=PRO_0000076642.
DOMAIN 99 162 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 10 26 N-terminal.
REGION 10 18 Interaction with TRIB3.
REGION 101 130 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 134 148 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 93 97 Poly-Glu.
MOD_RES 14 14 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P35639}.
MOD_RES 15 15 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P35639}.
MOD_RES 30 30 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P35639}.
MOD_RES 31 31 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P35639}.
MOD_RES 79 79 Phosphoserine; by MAPK14.
{ECO:0000250|UniProtKB:P35639}.
MOD_RES 82 82 Phosphoserine; by MAPK14.
{ECO:0000250|UniProtKB:P35639}.
VAR_SEQ 1 1 M -> MELVPATPHYPADVLFQTDPTAEM (in isoform
2). {ECO:0000303|Ref.4}.
/FTId=VSP_047277.
VARIANT 115 115 A -> V (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036000.
CONFLICT 10 14 FGTLS -> SDTV (in Ref. 1; AAB22646).
{ECO:0000305}.
SEQUENCE 169 AA; 19175 MW; 31905293FB1FBBE2 CRC64;
MAAESLPFSF GTLSSWELEA WYEDLQEVLS SDENGGTYVS PPGNEEEESK IFTTLDPASL
AWLTEEEPEP AEVTSTSQSP HSPDSSQSSL AQEEEEEDQG RTRKRKQSGH SPARAGKQRM
KEKEQENERK VAQLAEENER LKQEIERLTR EVEATRRALI DRMVNLHQA


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