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P97471

- SMAD4_MOUSE

UniProt

P97471 - SMAD4_MOUSE

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Protein
Mothers against decapentaplegic homolog 4
Gene
Smad4, Dpc4, Madh4
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. 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 SMAD1/5/8.1 Publication

Sites

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

GO - Molecular functioni

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

GO - Biological processi

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

GO - Cellular componenti

  1. SMAD protein complex Source: Ensembl
  2. activin responsive factor complex Source: Ensembl
  3. centrosome Source: Ensembl
  4. cytoplasm Source: BHF-UCL
  5. nucleus Source: BHF-UCL
  6. 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 4
PRO_0000090862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371N6-acetyllysine By similarity
Modified residuei427 – 4271N6-acetyllysine By similarity
Modified residuei506 – 5061N6-acetyllysine By 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.

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP97471.
PaxDbiP97471.
PRIDEiP97471.

PTM databases

PhosphoSiteiP97471.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiP97471.
BgeeiP97471.
CleanExiMM_SMAD4.
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.1 Publication

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

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.

Miscellaneous databases

EvolutionaryTraceiP97471.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 142125MH1
Add
BLAST
Domaini322 – 551230MH2
Add
BLAST

Region

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

Compositional bias

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

Domaini

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

Sequence similaritiesi

Belongs to the dwarfin/SMAD family.

Phylogenomic databases

eggNOGiNOG286923.
GeneTreeiENSGT00600000084353.
HOGENOMiHOG000286019.
HOVERGENiHBG053353.
InParanoidiQ6GTP6.
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

MDNMSITNTP TSNDACLSIV HSLMCHRQGG ESETFAKRAI ESLVKKLKEK    50
KDELDSLITA ITTNGAHPSK CVTIQRTLDG RLQVAGRKGF PHVIYARLWR 100
WPDLHKNELK HVKYCQYAFD LKCDSVCVNP YHYERVVSPG IDLSGLTLQS 150
NAPSMLVKDE YVHDFEGQPS LPTEGHSIQT IQHPPSNRAS TETYSAPALL 200
APAESNATST TNFPNIPVAS TSQPASILAG SHSEGLLQIA SGPQPGQQQN 250
GFTAQPATYH HNSTTTWTGS RTAPYTPNLP HHQNGHLQHH PPMPPHPGHY 300
WPVHNELAFQ PPISNHPAPE YWCSIAYFEM DVQVGETFKV PSSCPVVTVD 350
GYVDPSGGDR FCLGQLSNVH RTEAIERARL HIGKGVQLEC KGEGDVWVRC 400
LSDHAVFVQS YYLDREAGRA PGDAVHKIYP SAYIKVFDLR QCHRQMQQQA 450
ATAQAAAAAQ AAAVAGNIPG PGSVGGIAPA ISLSAAAGIG VDDLRRLCIL 500
RMSFVKGWGP DYPRQSIKET PCWIEIHLHR ALQLLDEVLH TMPIADPQPL 550
D 551
Length:551
Mass (Da):60,342
Last modified:July 27, 2011 - v2
Checksum:i4FBDF5DED4442F86
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571A → S in AAB57905. 1 Publication
Sequence conflicti292 – 2921P → R in AAB57905. 1 Publication

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...

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 ENSGT00600000084353.
HOGENOMi HOG000286019.
HOVERGENi HBG053353.
InParanoidi Q6GTP6.
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

ArrayExpressi P97471.
Bgeei P97471.
CleanExi MM_SMAD4.
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. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "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: September 3, 2014
This is version 140 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

Similar proteinsi