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Protein Page:
SMAD4 (mouse)
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
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: Nuclear receptor co-regulator; DNA-binding; Transcription, coactivator/corepressor
Cellular Component: cytoplasm; intracellular; nuclear chromatin; nucleus; protein complex; transcription factor complex
Molecular Function: chromatin binding; collagen binding; DNA binding; filamin binding; identical protein binding; metal ion binding; protein binding; protein heterodimerization activity; protein homodimerization activity; sequence-specific DNA binding; SMAD binding; transcription factor activity; transforming growth factor beta receptor, common-partner cytoplasmic mediator activity
Biological Process: anterior/posterior pattern formation; axon guidance; BMP signaling pathway; cell proliferation; cellular iron ion homeostasis; developmental growth; embryonic digit morphogenesis; endoderm development; endothelial cell activation; female gonad development; formation of anatomical boundary; gastrulation; gastrulation with mouth forming second; in utero embryonic development; kidney development; male gonad development; mesoderm development; negative regulation of cell growth; negative regulation of cell proliferation; negative regulation of protein catabolic process; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; neural crest cell differentiation; neuron fate commitment; ovarian follicle development; palate development; positive regulation of BMP signaling pathway; positive regulation of follicle-stimulating hormone secretion; positive regulation of histone H3-K4 methylation; positive regulation of luteinizing hormone secretion; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; positive regulation of transforming growth factor beta receptor signaling pathway; regulation of binding; regulation of cell proliferation; regulation of hair follicle development; regulation of transcription from RNA polymerase II promoter; regulation of transcription, DNA-dependent; regulation of transforming growth factor beta receptor signaling pathway; regulation of transforming growth factor-beta2 production; response to hypoxia; sebaceous gland development; single fertilization; SMAD protein complex assembly; somite rostral/caudal axis specification; spermatogenesis; tissue morphogenesis; transcription, DNA-dependent; transforming growth factor beta receptor signaling pathway; ureteric bud branching; uterus development
Reference #:  P97471 (UniProtKB)
Alt. Names/Synonyms: AW743858; D18Wsu70e; Deletion target in pancreatic carcinoma 4 homolog; Dpc4; MAD homolog 4; MAD homolog 4 (Drosophila); Madh4; Mothers against decapentaplegic homolog 4; Mothers against DPP homolog 4; OTTMUSP00000023201; OTTMUSP00000023202; SMAD 4; SMAD family member 4; Smad4
Gene Symbols: Smad4
Molecular weight: 60,342 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-ß Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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SMAD4

Protein Structure Not Found.
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Sites Implicated In
transcription, induced: T276‑p
intracellular localization: T276‑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.


       mouse

 
1 2 T9 DNMSITNTPTSNDAC
0 1 S22 ACLSIVHSLMCHRQG
0 1 S32 CHRQGGESETFAKRA
0 1 K37 GESETFAKRAIESLV
0 3 K45 RAIESLVKkLkEKKD
0 1 K45‑ub RAIESLVkkLkEKKD
0 1 K46‑ac AIESLVkkLkEKKDE
0 6 K48‑ac ESLVkkLkEKKDELD
0 2 K70 TNGAHPSKCVTIQRT
1 0 T77 KCVTIQRTLDGRLQV
0 1 Y95 KGFPHVIYARLWRWP
0 1 K106 WRWPDLHKNELKHVk
0 3 K113‑ub KNELKHVkYCQYAFD
4 0 K113 KNELKHVKYCQYAFD
1 1 S138 YHYERVVSPGIDLSG
6 0 K158 NAPSMLVKDEYVHDF
0 1 S177 SLPTEGHSIQTIQHP
1 0 T264 ATYHHNSTTTWTGSR
1 0 T268 HNSTTTWTGSRTAPY
1 0 T272 TTWTGSRTAPYtPNL
2 0 T276‑p GSRTAPYtPNLPHHQ
1 0 S342 GETFKVPSSCPVVTV
0 1 K384 RARLHIGKGVQLECK
0 3 K427 APGDAVHKIYPSAYI
0 2 S503 RLCILRMSFVKGWGP
0 2 K506 ILRMSFVKGWGPDYP
1 0 K506 ILRMSFVKGWGPDYP
0 1 Y512 VKGWGPDYPRQSIKE
1 2 K518 DYPRQSIKETPCWIE
  human

 
T9‑p DNMSITNtPTSNDAC
S22‑p ACLSIVHsLMCHRQG
S32‑p CHRQGGEsETFAkRA
K37‑ac GEsETFAkRAIESLV
K45‑ac RAIESLVkKLkEKKD
K45 RAIESLVKKLkEKKD
K46 AIESLVkKLkEKKDE
K48‑ac ESLVkKLkEKKDELD
K70‑ub TNGAHPSkCVTIQRt
T77‑p kCVTIQRtLDGRLQV
Y95‑p KGFPHVIyARLWRWP
K106‑ac WRWPDLHkNELKHVk
K113‑ub kNELKHVkYCQYAFD
K113‑sm kNELKHVkYCQYAFD
S138‑p YHYERVVsPGIDLSG
K159‑sm APSSMMVkDEYVHDF
S178‑p SLSTEGHsIQTIQHP
T265‑p ATYHHNStTTWtGSR
T269‑p HNStTTWtGSRtAPY
T273‑p TTWtGSRtAPYtPNL
T277‑p GSRtAPYtPNLPHHQ
S343‑p GETFKVPsSCPIVTV
K385‑ub RARLHIGkGVQLECK
K428‑ac APGDAVHkIYPSAYI
S504‑p RLCILRMsFVkGWGP
K507‑ac ILRMsFVkGWGPDyP
K507‑ub ILRMsFVkGWGPDyP
Y513‑p VkGWGPDyPRQSIkE
K519‑ub 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
T265 ATYHHNSTTTWTGSR
T269 HNSTTTWTGSRTAPY
T273 TTWTGSRTAPYTPNL
T277 GSRTAPYTPNLPHHQ
S343 GETFKVPSSCPIVTV
K385 RARLHIGKGVQLECK
K428‑ac APGDAVHkIYPSAYI
S504 RLCILRMSFVKGWGP
K507 ILRMSFVKGWGPDYP
K507 ILRMSFVKGWGPDYP
Y513 VKGWGPDYPRQSIKE
K519 DYPRQSIKETPCWIE
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