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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.
11-DEC-2019, entry version 197.
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]
SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM ALTDDIT3), AND
SUBUNIT.
PubMed=29083303; DOI=10.7554/elife.27860;
Samandi S., Roy A.V., Delcourt V., Lucier J.F., Gagnon J., Beaudoin M.C.,
Vanderperre B., Breton M.A., Motard J., Jacques J.F., Brunelle M.,
Gagnon-Arsenault I., Fournier I., Ouangraoua A., Hunting D.J., Cohen A.A.,
Landry C.R., Scott M.S., Roucou X.;
"Deep transcriptome annotation enables the discovery and functional
characterization of cryptic small proteins.";
Elife 6:0-0(2017).
[22]
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. Interacts with
isoform AltDDIT3 of DDIT3 (PubMed:29083303).
{ECO:0000269|PubMed:15775988, ECO:0000269|PubMed:16434966,
ECO:0000269|PubMed:17872950, ECO:0000269|PubMed:18940792,
ECO:0000269|PubMed:20829347, ECO:0000269|PubMed:22761832,
ECO:0000269|PubMed:29083303}.
-!- INTERACTION:
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-10173632, EBI-10187270;
P18847:ATF3; NbExp=19; 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;
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-10173632, EBI-740209;
Q7Z589:EMSY; NbExp=3; IntAct=EBI-10173632, EBI-6598631;
P01100:FOS; NbExp=6; IntAct=EBI-742651, EBI-852851;
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;
O75971:SNAPC5; NbExp=3; IntAct=EBI-10173632, EBI-749483;
Q86SX3:TEDC1; NbExp=2; IntAct=EBI-742651, EBI-3247115;
Q4ACW9:TWEAK; NbExp=3; IntAct=EBI-10173632, EBI-10241785;
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 {ECO:0000269|PubMed:29083303}. Nucleus
{ECO:0000269|PubMed:29083303}. Note=Present in the cytoplasm under non-
stressed conditions and ER stress leads to its nuclear accumulation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Name=1;
IsoId=P35638-1; Sequence=Displayed;
Name=2;
IsoId=P35638-2; Sequence=VSP_047277;
Name=AltDDIT3;
IsoId=P0DPQ6-1; Sequence=External;
-!- 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]
SMR; P35638; -.
BioGrid; 108016; 99.
ComplexPortal; CPX-69; CHOP-C/EBPalpha complex.
ComplexPortal; CPX-70; CHOP-C/EBPbeta complex.
CORUM; P35638; -.
DIP; DIP-41589N; -.
IntAct; P35638; 51.
STRING; 9606.ENSP00000448665; -.
ChEMBL; CHEMBL3351207; -.
iPTMnet; P35638; -.
PhosphoSitePlus; P35638; -.
BioMuta; DDIT3; -.
DMDM; 544022; -.
jPOST; P35638; -.
MassIVE; P35638; -.
PaxDb; P35638; -.
PeptideAtlas; P35638; -.
PRIDE; P35638; -.
ProteomicsDB; 28566; -.
ProteomicsDB; 55121; -. [P35638-1]
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]
Ensembl; ENST00000623876; ENSP00000494844; ENSG00000175197. [P35638-1]
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; -.
InParanoid; P35638; -.
KO; K04452; -.
OMA; RKQSGQW; -.
OrthoDB; 1338770at2759; -.
PhylomeDB; P35638; -.
TreeFam; TF105006; -.
Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress.
Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
Reactome; R-HSA-9614657; FOXO-mediated transcription of cell death genes.
SignaLink; P35638; -.
SIGNOR; P35638; -.
ChiTaRS; DDIT3; human.
GeneWiki; DNA_damage-inducible_transcript_3; -.
GenomeRNAi; 1649; -.
Pharos; P35638; Tchem.
PRO; PR:P35638; -.
Proteomes; UP000005640; Chromosome 12.
RNAct; P35638; protein.
Bgee; ENSG00000175197; Expressed in 213 organ(s), highest expression level in hypothalamus.
ExpressionAtlas; P35638; baseline and differential.
Genevisible; P35638; HS.
GO; GO:0005623; C:cell; IEA:GOC.
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:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:ParkinsonsUK-UCL.
GO; GO:0005770; C:late endosome; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
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:0008140; F:cAMP response element binding protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IGI:ParkinsonsUK-UCL.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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 cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003713; F:transcription coactivator activity; ISS:ARUK-UCL.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
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: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; IBA:GO_Central.
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 by RNA polymerase II; IDA:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:BHF-UCL.
GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
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:0043433; P:negative regulation of DNA-binding transcription factor activity; 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:0000122; P:negative regulation of transcription by RNA polymerase II; 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:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:CAFA.
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:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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 complex oligomerization; IDA:CAFA.
GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
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.
DisProt; DP00624; -.
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 initiation; Alternative splicing; Apoptosis;
Cell cycle; Chromosomal rearrangement; 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
/note="DNA damage-inducible transcript 3 protein"
/id="PRO_0000076642"
DOMAIN 99..162
/note="bZIP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
REGION 10..26
/note="N-terminal"
REGION 10..18
/note="Interaction with TRIB3"
REGION 101..130
/note="Basic motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
REGION 134..148
/note="Leucine-zipper"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
COMPBIAS 93..97
/note="Poly-Glu"
MOD_RES 14
/note="Phosphoserine; by CK2"
/evidence="ECO:0000250|UniProtKB:P35639"
MOD_RES 15
/note="Phosphoserine; by CK2"
/evidence="ECO:0000250|UniProtKB:P35639"
MOD_RES 30
/note="Phosphoserine; by CK2"
/evidence="ECO:0000250|UniProtKB:P35639"
MOD_RES 31
/note="Phosphoserine; by CK2"
/evidence="ECO:0000250|UniProtKB:P35639"
MOD_RES 79
/note="Phosphoserine; by MAPK14"
/evidence="ECO:0000250|UniProtKB:P35639"
MOD_RES 82
/note="Phosphoserine; by MAPK14"
/evidence="ECO:0000250|UniProtKB:P35639"
VAR_SEQ 1
/note="M -> MELVPATPHYPADVLFQTDPTAEM (in isoform 2)"
/evidence="ECO:0000303|Ref.4"
/id="VSP_047277"
VARIANT 115
/note="A -> V (in a colorectal cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036000"
CONFLICT 10..14
/note="FGTLS -> SDTV (in Ref. 1; AAB22646)"
/evidence="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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