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P35638 (DDIT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DDIT3
Synonyms:CHOP, CHOP10, GADD153
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length169 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20

Subunit structure

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. Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.20

Subcellular location

Cytoplasm. Nucleus. Note: Present in the cytoplasm under non-stressed conditions and ER stress leads to its nuclear accumulation. Ref.12 Ref.17 Ref.20

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. Ref.15 Ref.17

Domain

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

Post-translational modification

Ubiquitinated, leading to its degradation by the proteasome. Ref.12

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.

Involvement in 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.
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 (Ref.3). Ref.3

Sequence similarities

Belongs to the bZIP family.

Contains 1 bZIP (basic-leucine zipper) domain.

Sequence caution

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

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Growth arrest
Stress response
Transcription
Transcription regulation
Unfolded protein response
Wnt signaling pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER overload response

Inferred from electronic annotation. Source: Ensembl

Wnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

blood vessel maturation

Inferred from electronic annotation. Source: Ensembl

cell cycle arrest

Inferred from electronic annotation. Source: UniProtKB-KW

cell redox homeostasis

Inferred from direct assay PubMed 14667815. Source: MGI

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to DNA damage stimulus

Traceable author statement Ref.1. Source: ProtInc

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from direct assay Ref.14Ref.17. Source: UniProtKB

mRNA transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 14667815. Source: MGI

negative regulation of canonical Wnt signaling pathway

Inferred from sequence or structural similarity Ref.11. Source: BHF-UCL

negative regulation of determination of dorsal identity

Inferred from direct assay Ref.11. Source: BHF-UCL

negative regulation of myoblast differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.11. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of interleukin-8 production

Inferred from mutant phenotype Ref.17. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 22065586. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of DNA-templated transcription in response to stress

Traceable author statement PubMed 19816510. Source: BHF-UCL

regulation of transcription involved in anterior/posterior axis specification

Inferred from sequence or structural similarity Ref.11. Source: BHF-UCL

regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.12Ref.20. Source: UniProtKB

release of sequestered calcium ion into cytosol

Inferred from electronic annotation. Source: Ensembl

response to endoplasmic reticulum stress

Inferred from direct assay Ref.14Ref.17. Source: UniProtKB

response to starvation

Inferred from electronic annotation. Source: Ensembl

response to unfolded protein

Inferred from direct assay Ref.14. Source: UniProtKB

   Cellular_componentlate endosome

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.17Ref.20. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay Ref.14. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Non-traceable author statement Ref.2. Source: ProtInc

transcription corepressor activity

Traceable author statement Ref.3. Source: ProtInc

transcription factor binding

Inferred from physical interaction Ref.11. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35638-1)

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.
Isoform 2 (identifier: P35638-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 169169DNA damage-inducible transcript 3 protein
PRO_0000076642

Regions

Domain99 – 16264bZIP
Region10 – 2617N-terminal
Region10 – 189Interaction with TRIB3
Region101 – 13030Basic motif By similarity
Region134 – 14815Leucine-zipper By similarity
Compositional bias93 – 975Poly-Glu

Amino acid modifications

Modified residue141Phosphoserine; by CK2 By similarity
Modified residue151Phosphoserine; by CK2 By similarity
Modified residue301Phosphoserine; by CK2 By similarity
Modified residue311Phosphoserine; by CK2 By similarity
Modified residue791Phosphoserine; by MAPK14 By similarity
Modified residue821Phosphoserine; by MAPK14 By similarity

Natural variations

Alternative sequence11M → MELVPATPHYPADVLFQTDP TAEM in isoform 2.
VSP_047277
Natural variant1151A → V in a colorectal cancer sample; somatic mutation. Ref.21
VAR_036000

Experimental info

Sequence conflict10 – 145FGTLS → SDTV in AAB22646. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 31905293FB1FBBE2

FASTA16919,175
        10         20         30         40         50         60 
MAAESLPFSF GTLSSWELEA WYEDLQEVLS SDENGGTYVS PPGNEEEESK IFTTLDPASL 

        70         80         90        100        110        120 
AWLTEEEPEP AEVTSTSQSP HSPDSSQSSL AQEEEEEDQG RTRKRKQSGH SPARAGKQRM 

       130        140        150        160 
KEKEQENERK VAQLAEENER LKQEIERLTR EVEATRRALI DRMVNLHQA 

« Hide

Isoform 2 [UniParc].

Checksum: 1C569DBC247612EB
Show »

FASTA19221,700

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-115.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC1169.
S33798.
RefSeqNP_001181982.1. NM_001195053.1.
NP_001181983.1. NM_001195054.1.
NP_001181984.1. NM_001195055.1.
NP_001181986.1. NM_001195057.1.
NP_004074.2. NM_004083.5.
UniGeneHs.505777.

3D structure databases

DisProtDP00624.
ProteinModelPortalP35638.
SMRP35638. Positions 116-160.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108016. 56 interactions.
IntActP35638. 15 interactions.
MINTMINT-1434413.
STRING9606.ENSP00000340671.

PTM databases

PhosphoSiteP35638.

Polymorphism databases

DMDM544022.

Proteomic databases

PaxDbP35638.
PRIDEP35638.

Protocols and materials databases

DNASU1649.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346473; ENSP00000340671; ENSG00000175197. [P35638-1]
ENST00000547303; ENSP00000447188; ENSG00000175197. [P35638-1]
ENST00000551116; ENSP00000448665; ENSG00000175197. [P35638-2]
ENST00000552740; ENSP00000447803; ENSG00000175197. [P35638-2]
GeneID1649.
KEGGhsa:1649.
UCSCuc001soi.3. human. [P35638-1]

Organism-specific databases

CTD1649.
GeneCardsGC12M057910.
HGNCHGNC:2726. DDIT3.
MIM126337. gene.
613488. phenotype.
neXtProtNX_P35638.
Orphanet99967. Myxoid/round cell liposarcoma.
PharmGKBPA27193.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279524.
HOGENOMHOG000089934.
HOVERGENHBG051328.
InParanoidP35638.
KOK04452.
OMADRMVNLH.
OrthoDBEOG7QC7Z1.
PhylomeDBP35638.
TreeFamTF105006.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
SignaLinkP35638.

Gene expression databases

ArrayExpressP35638.
BgeeP35638.
CleanExHS_DDIT3.
GenevestigatorP35638.

Family and domain databases

InterProIPR004827. bZIP.
IPR016670. DNA_damage_induc_transcript_3.
[Graphical view]
PANTHERPTHR16833. PTHR16833. 1 hit.
PfamPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFPIRSF016571. C/EBPzeta_CHOP_DDIT3. 1 hit.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDDIT3. human.
GeneWikiDNA_damage-inducible_transcript_3.
GenomeRNAi1649.
NextBio6792.
PROP35638.
SOURCESearch...

Entry information

Entry nameDDIT3_HUMAN
AccessionPrimary (citable) accession number: P35638
Secondary accession number(s): F8VS99
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM