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Protein Page:
Smad4 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Smad4 transcription factor that mediates signal transduction by the transforming growth factor superfamily. The common smad (co-smad). Binds directly to consensus DNA-binding elements in the promoters of target genes. Promotes binding of the Smad2/Smad4/Fast-1 complex to DNA and provides an activation function required for Smad1 or Smad2 to stimulate transcription. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein; Transcription, coactivator/corepressor
Cellular Component: nucleoplasm; centrosome; transcription factor complex; cytoplasm; nuclear chromatin; nucleolus; cytosol; nucleus
Molecular Function: collagen binding; identical protein binding; protein binding; protein homodimerization activity; transforming growth factor beta receptor, common-partner cytoplasmic mediator activity; DNA binding; sequence-specific DNA binding; metal ion binding; chromatin binding; transcription factor activity
Biological Process: developmental growth; axon guidance; positive regulation of transcription, DNA-dependent; sebaceous gland development; palate development; negative regulation of transcription from RNA polymerase II promoter; BMP signaling pathway; negative regulation of cell proliferation; regulation of transforming growth factor beta receptor signaling pathway; transforming growth factor beta receptor signaling pathway; mesoderm development; neural crest cell differentiation; positive regulation of BMP signaling pathway; transcription initiation from RNA polymerase II promoter; regulation of transforming growth factor-beta2 production; regulation of binding; transcription, DNA-dependent; in utero embryonic development; positive regulation of transforming growth factor beta receptor signaling pathway; neuron fate commitment; gastrulation with mouth forming second; somite rostral/caudal axis specification; SMAD protein complex assembly; formation of anatomical boundary; endothelial cell activation; cell proliferation; ureteric bud branching; response to hypoxia; positive regulation of transcription from RNA polymerase II promoter; gene expression; negative regulation of cell growth; regulation of hair follicle development; negative regulation of protein catabolic process; negative regulation of transcription, DNA-dependent; endoderm development
Reference #:  Q13485 (UniProtKB)
Alt. Names/Synonyms: deleted in pancreatic carcinoma locus 4; Deletion target in pancreatic carcinoma 4; DPC4; hSMAD4; JIP; MAD homolog 4; MAD, mothers against decapentaplegic homolog 4; MADH4; Mothers against decapentaplegic homolog 4; mothers against decapentaplegic, Drosophila, homolog of, 4; Mothers against DPP homolog 4; SMAD 4; SMAD family member 4; SMAD, mothers against DPP homolog 4; SMAD4
Gene Symbols: SMAD4
Molecular weight: 60,439 Da
Basal Isoelectric point: 6.5  Predict pI for various phosphorylation states
CST Pathways:  ESC Pluripotency and Differentiation  |  G1/S Checkpoint  |  SAPK/JNK Signaling Cascades  |  TGF-├č Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Smad4

Protein Structure Not Found.


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Sites Implicated In
transcription, altered: T77‑p
molecular association, regulation: T77‑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


 SS 

SS: 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.


 MS 

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


       human

 
1 1 T9-p DNMSITNtPTSNDAC
0 1 S22-p ACLSIVHsLMCHRQG
0 1 S32-p CHRQGGEsETFAkRA
0 1 K37-ac GEsETFAkRAIESLV
0 1 K45-ac RAIESLVkKLkEKKD
0 1 K45 RAIESLVKKLkEKKD
0 1 K46 AIESLVkKLkEKKDE
0 6 K48-ac ESLVkKLkEKKDELD
0 2 K70-ub TNGAHPSkCVTIQRt
1 0 T77-p kCVTIQRtLDGRLQV
0 1 Y95-p KGFPHVIyARLWRWP
0 1 K106-ac WRWPDLHkNELKHVk
0 3 K113-ub kNELKHVkYCQYAFD
4 0 K113-sm kNELKHVkYCQYAFD
1 0 S138-p YHYERVVsPGIDLSG
6 0 K159-sm APSSMMVkDEYVHDF
0 1 S178-p SLSTEGHsIQTIQHP
1 0 T277 GSRTAPYTPNLPHHQ
1 0 S343-p GETFKVPsSCPIVTV
0 1 K428-ac APGDAVHkIYPSAYI
0 1 S504-p RLCILRMsFVkGWGP
0 2 K507-ac ILRMsFVkGWGPDYP
1 0 K507-ub ILRMsFVkGWGPDYP
1 1 K519-ub DYPRQSIkETPCWIE
  mouse

 
T9 DNMSITNTPTSNDAC
S22 ACLSIVHSLMCHRQG
S32 CHRQGGESETFAKRA
K37 GESETFAKRAIESLV
K45 RAIESLVKkLkEKKD
K45-ub RAIESLVkkLkEKKD
K46-ac AIESLVkkLkEKKDE
K48-ac ESLVkkLkEKKDELD
K70 TNGAHPSKCVTIQRT
T77 KCVTIQRTLDGRLQV
Y95 KGFPHVIYARLWRWP
K106 WRWPDLHKNELKHVk
K113-ub KNELKHVkYCQYAFD
K113 KNELKHVKYCQYAFD
S138 YHYERVVSPGIDLSG
K158 NAPSMLVKDEYVHDF
S177 SLPTEGHSIQTIQHP
T276-p GSRTAPYtPNLPHHQ
S342 GETFKVPSSCPVVTV
K427 APGDAVHKIYPSAYI
S503 RLCILRMSFVKGWGP
K506 ILRMSFVKGWGPDYP
K506 ILRMSFVKGWGPDYP
K518 DYPRQSIKETPCWIE
  rat

 
T9 DNMSITNTPTSNDAC
S22 ACLSIVHSLMCHRQG
S32 CHRQGGESETFAKRA
K37 GESETFAKRAIESLV
K45-ac RAIESLVkKLKEKKD
K45 RAIESLVKKLKEKKD
K46 AIESLVkKLKEKKDE
K48 ESLVkKLKEKKDELD
K70 TNGAHPSKCVTIQRT
T77 KCVTIQRTLDGRLQV
Y95 KGFPHVIYARLWRWP
K106 WRWPDLHKNELKHVK
K113 KNELKHVKYCQYAFD
K113 KNELKHVKYCQYAFD
S138 YHYERVVSPGIDLSG
K159 APPSMLVKDEYVHDF
S178 SLPTEGHSIQTIQHP
T277 GSRTAPYTPNLPHHQ
S343 GETFKVPSSCPIVTV
K428-ac APGDAVHkIYPSAYI
S504 RLCILRMSFVKGWGP
K507 ILRMSFVKGWGPDYP
K507 ILRMSFVKGWGPDYP
K519 DYPRQSIKETPCWIE
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