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Protein Page:
CHOP (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CHOP a transcriptional-regulatory protein of the bZIP family. Inhibits the DNA-binding activity of C/EBP and LAP by forming heterodimers that cannot bind DNA. May play an important role in melanoma progression. CK2-mediated phosphorylation inhibits its transcriptional activity. Up-regulates IL-6 transcription by trapping negative regulating NF-IL6 isoform. Note: This description may include information from UniProtKB.
Protein type: Transcription factor; Oncoprotein; Autophagy; DNA-binding
Chromosomal Location of Human Ortholog: 12q13.1-q13.2
Cellular Component: cytosol; nucleoplasm; nucleus
Molecular Function: cAMP response element binding protein binding; DNA binding; leucine zipper domain binding; protein binding; protein heterodimerization activity; protein homodimerization activity; transcription corepressor activity; transcription factor activity; transcription factor binding
Biological Process: cell cycle arrest; cell redox homeostasis; inhibition of CREB transcription factor; mRNA transcription from RNA polymerase II promoter; negative regulation of protein kinase B signaling cascade; negative regulation of transcription factor activity; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; positive regulation of interleukin-8 production; positive regulation of neuron apoptosis; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; proteasomal ubiquitin-dependent protein catabolic process; regulation of transcription in response to stress; regulation of transcription, DNA-dependent; response to DNA damage stimulus; response to unfolded protein
Disease: Myxoid Liposarcoma
Reference #:  P35638 (UniProtKB)
Alt. Names/Synonyms: C/EBP homologous protein; C/EBP zeta; C/EBP-homologous protein; C/EBP-homologous protein 10; CCAAT/enhancer-binding protein homologous protein; CEBPZ; CHOP; CHOP-10; CHOP10; DDIT-3; DDIT3; DNA damage-inducible transcript 3 protein; DNA-damage-inducible transcript 3; GADD153; Growth arrest and DNA damage-inducible protein GADD153; growth arrest- and DNA damage-inducible; MGC4154
Gene Symbols: DDIT3
Molecular weight: 19,175 Da
Basal Isoelectric point: 4.61  Predict pI for various phosphorylation states
CST Pathways:  Regulation of P38 MAPKs
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CHOP

Protein Structure Not Found.


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Sites Implicated In
transcription, altered: S79‑p, S82‑p
transcription, inhibited: S14‑p, S15‑p, S30‑p, S31‑p
activity, inhibited: S14‑p, S15‑p, S30‑p, S31‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 S14‑p PFSFGTLssWELEAW
1 0 S15‑p FSFGTLssWELEAWY
1 0 S30‑p EDLQEVLssDENGGT
1 0 S31‑p DLQEVLssDENGGTY
0 1 S49‑p PGNEEEEsKIFTtLD
0 1 T54‑p EEsKIFTtLDPASLA
0 1 T64‑p PASLAWLtEEEPEPA
1 1 S79‑p EVTSTSQsPHsPDSS
1 1 S82‑p STSQsPHsPDSSQSS
0 1 S108 RTRKRKQSGHSPARA
0 1 K121 RAGKQRMKEKEQENE
  mouse

 
S14 PFTLETVSSWELEAW
S15 FTLETVSSWELEAWY
S30 EDLQEVLSSDEIGGT
S31 DLQEVLSSDEIGGTY
S49 PGNEEEESKTFTTLD
T54 EESKTFTTLDPASLA
T64 PASLAWLTEEPGPTE
S78‑p EVTRTSQsPRsPDSS
S81‑p RTSQsPRsPDSSQSS
S107‑p RTRKRKQsGQCPARP
K120‑ub RPGKQRMkEKEQENE
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