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P97471

- SMAD4_MOUSE

UniProt

P97471 - SMAD4_MOUSE

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Protein

Mothers against decapentaplegic homolog 4

Gene

Smad4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for syngernistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity). Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (PubMed:15329343). In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi71 – 711ZincBy similarity
Metal bindingi115 – 1151ZincBy similarity
Metal bindingi127 – 1271ZincBy similarity
Metal bindingi132 – 1321ZincBy similarity
Sitei514 – 5141Necessary for heterotrimerizationBy similarity

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. collagen binding Source: MGI
  3. core promoter proximal region sequence-specific DNA binding Source: Ensembl
  4. DNA binding Source: MGI
  5. metal ion binding Source: UniProtKB-KW
  6. RNA polymerase II transcription factor binding Source: BHF-UCL
  7. RNA polymerase II transcription factor binding transcription factor activity Source: BHF-UCL
  8. sequence-specific DNA binding transcription factor activity Source: MGI
  9. transforming growth factor beta receptor, common-partner cytoplasmic mediator activity Source: Ensembl

GO - Biological processi

  1. anterior/posterior pattern specification Source: MGI
  2. atrioventricular canal development Source: BHF-UCL
  3. atrioventricular valve formation Source: BHF-UCL
  4. axon guidance Source: MGI
  5. BMP signaling pathway Source: Ensembl
  6. brainstem development Source: MGI
  7. branching involved in ureteric bud morphogenesis Source: MGI
  8. cardiac septum development Source: BHF-UCL
  9. cell proliferation Source: MGI
  10. developmental growth Source: MGI
  11. endocardial cell differentiation Source: BHF-UCL
  12. endoderm development Source: MGI
  13. endothelial cell activation Source: BHF-UCL
  14. epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
  15. formation of anatomical boundary Source: MGI
  16. gastrulation Source: MGI
  17. gastrulation with mouth forming second Source: MGI
  18. in utero embryonic development Source: MGI
  19. kidney development Source: MGI
  20. mesoderm development Source: MGI
  21. metanephric mesenchyme morphogenesis Source: UniProtKB
  22. negative regulation of cell death Source: UniProtKB
  23. negative regulation of cell growth Source: Ensembl
  24. negative regulation of cell proliferation Source: MGI
  25. negative regulation of protein catabolic process Source: Ensembl
  26. negative regulation of transcription, DNA-templated Source: Ensembl
  27. nephrogenic mesenchyme morphogenesis Source: UniProtKB
  28. neural crest cell differentiation Source: MGI
  29. neuron fate commitment Source: MGI
  30. palate development Source: BHF-UCL
  31. positive regulation of BMP signaling pathway Source: Ensembl
  32. positive regulation of cell proliferation involved in heart valve morphogenesis Source: BHF-UCL
  33. positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  34. positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  35. positive regulation of SMAD protein import into nucleus Source: BHF-UCL
  36. positive regulation of transcription, DNA-templated Source: MGI
  37. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  38. positive regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  39. regulation of binding Source: MGI
  40. regulation of cell proliferation Source: MGI
  41. regulation of hair follicle development Source: MGI
  42. regulation of transcription from RNA polymerase II promoter Source: MGI
  43. regulation of transforming growth factor beta2 production Source: Ensembl
  44. response to hypoxia Source: Ensembl
  45. sebaceous gland development Source: MGI
  46. SMAD protein complex assembly Source: Ensembl
  47. SMAD protein signal transduction Source: Ensembl
  48. somite rostral/caudal axis specification Source: MGI
  49. tissue morphogenesis Source: MGI
  50. transcription from RNA polymerase II promoter Source: GOC
  51. transforming growth factor beta receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_202264. SMAD4 MH2 Domain Mutants in Cancer.
REACT_203510. TGF-beta receptor signaling activates SMADs.
REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_216222. Transcriptional regulation of pluripotent stem cells.
REACT_216258. Signaling by Activin.
REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_220505. Signaling by BMP.
REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_220645. Signaling by NODAL.

Names & Taxonomyi

Protein namesi
Recommended name:
Mothers against decapentaplegic homolog 4
Short name:
MAD homolog 4
Short name:
Mothers against DPP homolog 4
Alternative name(s):
Deletion target in pancreatic carcinoma 4 homolog
SMAD family member 4
Short name:
SMAD 4
Short name:
Smad4
Gene namesi
Name:Smad4
Synonyms:Dpc4, Madh4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:894293. Smad4.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with R-SMAD. PDPK1 prevents its nuclear translocation (By similarity).By similarity

GO - Cellular componenti

  1. activin responsive factor complex Source: Ensembl
  2. centrosome Source: Ensembl
  3. cytoplasm Source: BHF-UCL
  4. nuclear chromatin Source: Ensembl
  5. nucleus Source: BHF-UCL
  6. SMAD protein complex Source: Ensembl
  7. transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Conditional knockout in muscle leads to muscle atrophy and weakness. Mutant mice loose significantly more muscle mass after denervation as compared to wild-type animals and show excessive proteolysis in denervated muscle. The loss of maximal absolute force after fasting is greater in mutant mice than in controls.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Mothers against decapentaplegic homolog 4PRO_0000090862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371N6-acetyllysineBy similarity
Modified residuei427 – 4271N6-acetyllysineBy similarity
Modified residuei506 – 5061N6-acetyllysineBy similarity
Cross-linki518 – 518Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Phosphorylated by PDPK1.By similarity
Monoubiquitinated on Lys-518 by E3 ubiquitin-protein ligase TRIM33. Monoubiquitination hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade. Deubiqitination by USP9X restores its competence to mediate TGF-beta signaling (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP97471.
PaxDbiP97471.
PRIDEiP97471.

PTM databases

PhosphoSiteiP97471.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP97471.
CleanExiMM_SMAD4.
ExpressionAtlasiP97471. baseline and differential.
GenevestigatoriP97471.

Interactioni

Subunit structurei

Monomer (By similarity). Heterotrimer; with a C-terminally phosphorylated R-SMAD molecule and to form the transcriptionally active SMAD2/3-SMAD4 complex (By similarity). Found in a ternary complex composed of SMAD4, STK11/LKB1 and STK11IP. Interacts with ATF2, COPS5, DACH1, MSG1, SKI, STK11/LKB1, STK11IP and TRIM33. Associates with ZNF423 or ZNF521 in response to BMP2 leading to activate transcription of BMP target genes. Interacts with USP9X. Interacts with RBPMS. Interacts with WWTR1 (via coiled-coil domain). Interacts with CITED1 and CITED2 (By similarity). Interacts with PDPK1 (via PH domain) (By similarity). Interacts with VPS39; this interaction affects heterodimer formation with SMAD3, but not with SMAD2, and leads to inhibition of SMAD3-dependent transcription activation (By similarity). Interactions with VPS39 and SMAD2 may be mutually exclusive (By similarity). Found in a complex with SMAD1 and YY1.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Smad2Q624323EBI-5259270,EBI-2337932
Smad3Q8BUN55EBI-5259270,EBI-2337983

Protein-protein interaction databases

BioGridi201277. 27 interactions.
DIPiDIP-29718N.
IntActiP97471. 5 interactions.
MINTiMINT-261841.

Structurei

Secondary structure

1
551
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 249
Helixi33 – 4715
Helixi51 – 6212
Turni63 – 653
Beta strandi73 – 753
Beta strandi82 – 843
Beta strandi87 – 893
Helixi91 – 999
Beta strandi109 – 1113
Helixi119 – 1213
Beta strandi124 – 1274
Helixi130 – 1323
Beta strandi133 – 1353

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QSVX-ray2.71A/B/C/D9-140[»]
ProteinModelPortaliP97471.
SMRiP97471. Positions 10-138, 284-551.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97471.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 142125MH1PROSITE-ProRule annotationAdd
BLAST
Domaini322 – 551230MH2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni274 – 31946SADAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi450 – 46516Poly-AlaAdd
BLAST

Domaini

The MH1 domain is required for DNA binding.
The MH2 domain is required for both homomeric and heteromeric interactions and for transcriptional regulation. Sufficient for nuclear import (By similarity).By similarity

Sequence similaritiesi

Belongs to the dwarfin/SMAD family.Curated
Contains 1 MH1 (MAD homology 1) domain.PROSITE-ProRule annotation
Contains 1 MH2 (MAD homology 2) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG286923.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000286019.
HOVERGENiHBG053353.
InParanoidiP97471.
KOiK04501.
OMAiPTEGHSI.
OrthoDBiEOG712TW5.
TreeFamiTF314923.

Family and domain databases

Gene3Di2.60.200.10. 1 hit.
3.90.520.10. 1 hit.
InterProiIPR013790. Dwarfin.
IPR003619. MAD_homology1_Dwarfin-type.
IPR013019. MAD_homology_MH1.
IPR017855. SMAD_dom-like.
IPR001132. SMAD_dom_Dwarfin-type.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR13703. PTHR13703. 1 hit.
PfamiPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTiSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 1 hit.
PROSITEiPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97471-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDNMSITNTP TSNDACLSIV HSLMCHRQGG ESETFAKRAI ESLVKKLKEK
60 70 80 90 100
KDELDSLITA ITTNGAHPSK CVTIQRTLDG RLQVAGRKGF PHVIYARLWR
110 120 130 140 150
WPDLHKNELK HVKYCQYAFD LKCDSVCVNP YHYERVVSPG IDLSGLTLQS
160 170 180 190 200
NAPSMLVKDE YVHDFEGQPS LPTEGHSIQT IQHPPSNRAS TETYSAPALL
210 220 230 240 250
APAESNATST TNFPNIPVAS TSQPASILAG SHSEGLLQIA SGPQPGQQQN
260 270 280 290 300
GFTAQPATYH HNSTTTWTGS RTAPYTPNLP HHQNGHLQHH PPMPPHPGHY
310 320 330 340 350
WPVHNELAFQ PPISNHPAPE YWCSIAYFEM DVQVGETFKV PSSCPVVTVD
360 370 380 390 400
GYVDPSGGDR FCLGQLSNVH RTEAIERARL HIGKGVQLEC KGEGDVWVRC
410 420 430 440 450
LSDHAVFVQS YYLDREAGRA PGDAVHKIYP SAYIKVFDLR QCHRQMQQQA
460 470 480 490 500
ATAQAAAAAQ AAAVAGNIPG PGSVGGIAPA ISLSAAAGIG VDDLRRLCIL
510 520 530 540 550
RMSFVKGWGP DYPRQSIKET PCWIEIHLHR ALQLLDEVLH TMPIADPQPL

D
Length:551
Mass (Da):60,342
Last modified:July 27, 2011 - v2
Checksum:i4FBDF5DED4442F86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571A → S in AAB57905. (PubMed:9166592)Curated
Sequence conflicti292 – 2921P → R in AAB57905. (PubMed:9166592)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U79748 mRNA. Translation: AAB57905.1.
CH466528 Genomic DNA. Translation: EDL09560.1.
BC046584 mRNA. Translation: AAH46584.1.
AK004804 mRNA. Translation: BAB23576.1.
CCDSiCCDS29337.1.
RefSeqiNP_032566.2. NM_008540.2.
UniGeneiMm.100399.

Genome annotation databases

EnsembliENSMUST00000025393; ENSMUSP00000025393; ENSMUSG00000024515.
ENSMUST00000114939; ENSMUSP00000110589; ENSMUSG00000024515.
GeneIDi17128.
KEGGimmu:17128.
UCSCiuc008fou.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U79748 mRNA. Translation: AAB57905.1 .
CH466528 Genomic DNA. Translation: EDL09560.1 .
BC046584 mRNA. Translation: AAH46584.1 .
AK004804 mRNA. Translation: BAB23576.1 .
CCDSi CCDS29337.1.
RefSeqi NP_032566.2. NM_008540.2.
UniGenei Mm.100399.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QSV X-ray 2.71 A/B/C/D 9-140 [» ]
ProteinModelPortali P97471.
SMRi P97471. Positions 10-138, 284-551.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201277. 27 interactions.
DIPi DIP-29718N.
IntActi P97471. 5 interactions.
MINTi MINT-261841.

PTM databases

PhosphoSitei P97471.

Proteomic databases

MaxQBi P97471.
PaxDbi P97471.
PRIDEi P97471.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025393 ; ENSMUSP00000025393 ; ENSMUSG00000024515 .
ENSMUST00000114939 ; ENSMUSP00000110589 ; ENSMUSG00000024515 .
GeneIDi 17128.
KEGGi mmu:17128.
UCSCi uc008fou.1. mouse.

Organism-specific databases

CTDi 4089.
MGIi MGI:894293. Smad4.

Phylogenomic databases

eggNOGi NOG286923.
GeneTreei ENSGT00760000119091.
HOGENOMi HOG000286019.
HOVERGENi HBG053353.
InParanoidi P97471.
KOi K04501.
OMAi PTEGHSI.
OrthoDBi EOG712TW5.
TreeFami TF314923.

Enzyme and pathway databases

Reactomei REACT_202264. SMAD4 MH2 Domain Mutants in Cancer.
REACT_203510. TGF-beta receptor signaling activates SMADs.
REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_216222. Transcriptional regulation of pluripotent stem cells.
REACT_216258. Signaling by Activin.
REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_220505. Signaling by BMP.
REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_220645. Signaling by NODAL.

Miscellaneous databases

EvolutionaryTracei P97471.
NextBioi 291316.
PROi P97471.
SOURCEi Search...

Gene expression databases

Bgeei P97471.
CleanExi MM_SMAD4.
ExpressionAtlasi P97471. baseline and differential.
Genevestigatori P97471.

Family and domain databases

Gene3Di 2.60.200.10. 1 hit.
3.90.520.10. 1 hit.
InterProi IPR013790. Dwarfin.
IPR003619. MAD_homology1_Dwarfin-type.
IPR013019. MAD_homology_MH1.
IPR017855. SMAD_dom-like.
IPR001132. SMAD_dom_Dwarfin-type.
IPR008984. SMAD_FHA_domain.
[Graphical view ]
PANTHERi PTHR13703. PTHR13703. 1 hit.
Pfami PF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view ]
SMARTi SM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 1 hit.
PROSITEi PS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and chromosomal mapping of the mouse homolog (Madh4) of the human DPC4/MADH4 gene."
    Anna C.H., Devereux T.R.
    Mamm. Genome 8:443-444(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: A/J.
    Tissue: Lung.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Olfactory epithelium.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-551.
    Strain: C57BL/6J.
    Tissue: Lung.
  5. "SMAD-mediated modulation of YY1 activity regulates the BMP response and cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5 enhancer."
    Lee K.H., Evans S., Ruan T.Y., Lassar A.B.
    Development 131:4709-4723(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH SMAD1 AND YY1.
  6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Structure of Smad1 MH1/DNA complex reveals distinctive rearrangements of BMP and TGF-beta effectors."
    Baburajendran N., Palasingam P., Narasimhan K., Sun W., Prabhakar S., Jauch R., Kolatkar P.R.
    Nucleic Acids Res. 38:3477-3488(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 9-140 IN COMPLEX WITH DNA, ZINC_BINDING SITES, SUBUNIT.

Entry informationi

Entry nameiSMAD4_MOUSE
AccessioniPrimary (citable) accession number: P97471
Secondary accession number(s): Q6GTP6, Q9CW56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3