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Search results 301 to 400 out of 526 for Smad6

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Hits by Pathway

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Hits by Strain

Type Details Score
GXD Expression
GXD Expression
Probe: MGI:1314968
Assay Type: Immunohistochemistry
Annotation Date: 2021-08-26
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1860123
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:6753287
Age: embryonic day 15.5
Image: 2V,V',V'''
Note: Expression in smooth muscle. No overlap with Smad6 expression.
Specimen Label: 2V,V',V'''
Detected: true
Specimen Num: 1
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Interaction Experiment
Shen R (2006)
Description: Smad6 interacts with Runx2 and mediates Smad ubiquitin regulatory factor 1-induced Runx2 degradation.
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Interaction Experiment
Chen YL (2009)
Description: Smad6 inhibits the transcriptional activity of Tbx6 by mediating its degradation.
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DO Term
DOID:0080334 | aortic valve disease 2
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GXD Expression
GXD Expression
Probe: MGI:3581531
Assay Type: Immunohistochemistry
Annotation Date: 2021-08-26
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3518227
Pattern: Regionally restricted
Stage: TS27
Assay Id: MGI:6753288
Age: postnatal day 3
Image: 2W
Note: Expression in pericytes and smooth muscle. No overlap with Smad6 expression.
Specimen Label: 2W
Detected: true
Specimen Num: 2
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GXD Expression
GXD Expression
Probe: MGI:3581531
Assay Type: Immunohistochemistry
Annotation Date: 2021-08-26
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1860123
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:6753288
Age: embryonic day 15.5
Image: 2V
Note: Expression in pericytes and smooth muscle. No overlap with Smad6 expression.
Specimen Label: 2V
Detected: true
Specimen Num: 1
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Protein
O35182
Organism: Mus musculus/domesticus
Length: 495  
Fragment?: false
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Publication
16951688 | -
First Author: Choi KC
Year: 2006
Journal: Nat Immunol
Title: Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor signaling through direct interaction with the adaptor Pellino-1.
Volume: 7
Issue: 10
Pages: 1057-65
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Allele
Rr49<em1Axvi> | MGI:7489586
Name: regulatory region 49; endonuclease-mediated mutation 1, Axel Visel
Allele Type: Endonuclease-mediated
Attribute String: Modified regulatory region
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Strain
MGI:7489906 | FVB-Rr49<em1Axvi>
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
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Strain
MGI:6348304 | FVB/NCrl-Rr49<em1Axvi>/Mmucd
Attribute String: mutant strain, coisogenic, endonuclease-mediated mutation
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Genotype
Genotype
Symbol: Rr49/Rr49
Background: FVB-Rr49
Zygosity: hm
Has Mutant Allele: true
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Gene
1482 | NKX2-5
Type: gene
Organism: human
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DO Term
DOID:0060912 | craniosynostosis 7
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Gene
79068 | FTO
Type: gene
Organism: human
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Publication
10393693 | J:56152
First Author: Nakao A
Year: 1999
Journal: J Clin Invest
Title: Transient gene transfer and expression of Smad7 prevents bleomycin-induced lung fibrosis in mice.
Volume: 104
Issue: 1
Pages: 5-11
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Publication
16641368 | J:112732
First Author: Wang C
Year: 2006
Journal: Mol Biol Cell
Title: Cell aggregation-induced FGF8 elevation is essential for P19 cell neural differentiation.
Volume: 17
Issue: 7
Pages: 3075-84
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Publication
28694257 | J:243415
First Author: Stantzou A
Year: 2017
Journal: Development
Title: BMP signaling regulates satellite cell-dependent postnatal muscle growth.
Volume: 144
Issue: 15
Pages: 2737-2747
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Publication
29749927 | J:356872
   
First Author: Schlereth K
Year: 2018
Journal: Elife
Title: The transcriptomic and epigenetic map of vascular quiescence in the continuous lung endothelium.
Volume: 7
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Publication
23071089 | J:192861
First Author: Takahashi A
Year: 2012
Journal: Mol Cell Biol
Title: Tob2 inhibits peroxisome proliferator-activated receptor γ2 expression by sequestering Smads and C/EBPα during adipocyte differentiation.
Volume: 32
Issue: 24
Pages: 5067-77
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Publication
29521016 | J:271967
First Author: Hayata T
Year: 2018
Journal: Genes Cells
Title: Dullard deficiency causes hemorrhage in the adult ovarian follicles.
Volume: 23
Issue: 5
Pages: 345-356
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Publication
18433296 | J:150160
First Author: Sabatakos G
Year: 2008
Journal: J Bone Miner Res
Title: Doubly truncated FosB isoform (Delta2DeltaFosB) induces osteosclerosis in transgenic mice and modulates expression and phosphorylation of Smads in osteoblasts independent of intrinsic AP-1 activity.
Volume: 23
Issue: 5
Pages: 584-95
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Publication
10564272 | J:299435
First Author: Fujii M
Year: 1999
Journal: Mol Biol Cell
Title: Roles of bone morphogenetic protein type I receptors and Smad proteins in osteoblast and chondroblast differentiation.
Volume: 10
Issue: 11
Pages: 3801-13
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Publication
10906784 | J:63719
First Author: Zwijsen A
Year: 2000
Journal: Dev Dyn
Title: Expression of the inhibitory Smad7 in early mouse development and upregulation during embryonic vasculogenesis.
Volume: 218
Issue: 4
Pages: 663-70
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Publication
10224044 | J:54891
First Author: Yanagi Y
Year: 1999
Journal: J Biol Chem
Title: Positive and negative modulation of vitamin D receptor function by transforming growth factor-beta signaling through smad proteins.
Volume: 274
Issue: 19
Pages: 12971-4
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Publication
16905540 | J:117274
First Author: Hirao M
Year: 2006
Journal: J Biol Chem
Title: Oxygen tension regulates chondrocyte differentiation and function during endochondral ossification.
Volume: 281
Issue: 41
Pages: 31079-92
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Publication
17397798 | J:121620
First Author: Mukai T
Year: 2007
Journal: Biochem Biophys Res Commun
Title: TNF-alpha inhibits BMP-induced osteoblast differentiation through activating SAPK/JNK signaling.
Volume: 356
Issue: 4
Pages: 1004-10
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Publication
22072987 | J:177989
First Author: Kaneda A
Year: 2011
Journal: PLoS Genet
Title: Activation of Bmp2-Smad1 signal and its regulation by coordinated alteration of H3K27 trimethylation in Ras-induced senescence.
Volume: 7
Issue: 11
Pages: e1002359
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Publication
26055326 | J:317620
First Author: Ha Thi HT
Year: 2015
Journal: Mol Cell Biol
Title: Smad7 Modulates Epidermal Growth Factor Receptor Turnover through Sequestration of c-Cbl.
Volume: 35
Issue: 16
Pages: 2841-50
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Publication
37081156 | J:335096
First Author: Rajderkar S
Year: 2023
Journal: Commun Biol
Title: Topologically associating domain boundaries are required for normal genome function.
Volume: 6
Issue: 1
Pages: 435
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Publication
12588853 | J:81774
First Author: Bell E
Year: 2003
Journal: Development
Title: Cell fate specification and competence by Coco, a maternal BMP, TGFbeta and Wnt inhibitor.
Volume: 130
Issue: 7
Pages: 1381-9
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Protein Domain
IPR017855 | SMAD-like_dom_sf
Type: Homologous_superfamily
Description: This superfamily represents SMAD (Mothers against decapentaplegic (MAD) homolog) (also called MH2 for MAD homology 2) domains as well as their structural homologues, such as the transactivation domain of interferon regulatory protein 3 (IRF3), both of which have a β-sandwich structural fold.SMAD domains are found at the carboxy terminus of MAD related proteins such as Smads. SMAD domain proteins are found in a range of species from nematodes to humans. These highly conserved proteins contain an N-terminal MH1 domain that contacts DNA, and is separated by a short linker region from the C-terminal MH2 domain, the later showing a striking similarity to FHA domains. SMAD proteins mediate signalling by the TGF-beta/activin/BMP-2/4 cytokines from receptor Ser/Thr protein kinases at the cell surface to the nucleus. SMAD proteins fall into three functional classes: the receptor-regulated SMADs (R-SMADs), including SMAD1, -2, -3, -5, and -8, each of which is involved in a ligand-specific signalling pathway []; the co-mediator SMADs (co-SMADs), including SMAD4, which interact with R-SMADs to participate in signalling []; and the inhibitory SMADs (I-SMADs), including SMAD6 and -7, which block the activation of R-SMADs and Co-SMADs, thereby negatively regulating signalling pathways [].
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Protein
A0A140LJD9
Organism: Mus musculus/domesticus
Length: 103  
Fragment?: true
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Protein
O54726
Organism: Mus musculus/domesticus
Length: 83  
Fragment?: true
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Protein
A0A2I3BRM5
Organism: Mus musculus/domesticus
Length: 63  
Fragment?: true
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Protein
A0A140LJE8
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: true
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Publication
9214508 | -
First Author: Shi Y
Year: 1997
Journal: Nature
Title: A structural basis for mutational inactivation of the tumour suppressor Smad4.
Volume: 388
Issue: 6637
Pages: 87-93
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Publication
11483516 | -
First Author: Itoh F
Year: 2001
Journal: EMBO J
Title: Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads.
Volume: 20
Issue: 15
Pages: 4132-42
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Protein
A0A0J9YUT2
Organism: Mus musculus/domesticus
Length: 53  
Fragment?: false
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Protein
A0A0J9YVH5
Organism: Mus musculus/domesticus
Length: 59  
Fragment?: false
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Protein
A0A0N4SW39
Organism: Mus musculus/domesticus
Length: 44  
Fragment?: false
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Protein
A0A0J9YTV1
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
E0CXB7
Organism: Mus musculus/domesticus
Length: 48  
Fragment?: false
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Publication
11106755 | -
First Author: Durocher D
Year: 2000
Journal: Mol Cell
Title: The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms.
Volume: 6
Issue: 5
Pages: 1169-82
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Publication
12121644 | -
First Author: Stavridi ES
Year: 2002
Journal: Structure
Title: Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate.
Volume: 10
Issue: 7
Pages: 891-9
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Publication
12049740 | -
First Author: Li J
Year: 2002
Journal: Mol Cell
Title: Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2.
Volume: 9
Issue: 5
Pages: 1045-54
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Publication
11779503 | -
First Author: Wu JW
Year: 2001
Journal: Mol Cell
Title: Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling.
Volume: 8
Issue: 6
Pages: 1277-89
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Publication
14555996 | -
First Author: Qin BY
Year: 2003
Journal: Nat Struct Biol
Title: Crystal structure of IRF-3 reveals mechanism of autoinhibition and virus-induced phosphoactivation.
Volume: 10
Issue: 11
Pages: 913-21
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Protein Domain
IPR008984 | SMAD_FHA_dom_sf
Type: Homologous_superfamily
Description: FHA and SMAD (MH2) domains share a common structure consisting of a sandwich of eleven β-strands in two sheets with Greek key topology. Forkhead-associated (FHA) domains were originally identified as a sequence profile of about 75 amino acids, whereas the full-length domain is closer to about 150 amino acids. FHA domains are found in transcription factors, kinesin motors, and in a variety of other signalling molecules in organisms ranging from eubacteria to humans. FHA domains are protein-protein interaction domains that are specific for phosphoproteins. FHA-containing proteins function in maintaining cell-cycle checkpoints, DNA repair and transcriptional regulation. FHA domain proteins include the Chk2/Rad53/Cds1 family of proteins that contain one or more FHA domains, as well as a Ser/Thr kinase domain [, , ]. SMAD (Mothers against decapentaplegic (MAD) homologue) domain proteins are found in a range of species from nematodes to humans. These highly conserved proteins contain an N-terminal MH1 domain that contacts DNA, and is separated by a short linker region from the C-terminal MH2 domain, the later showing a striking similarity to FHA domains. SMAD proteins mediate signalling by the TGF-beta/activin/BMP-2/4 cytokines from receptor Ser/Thr protein kinases at the cell surface to the nucleus. SMAD proteins fall into three functional classes: the receptor-regulated SMADs (R-SMADs), including SMAD1, -2, -3, -5, and -8, each of which is involved in a ligand-specific signalling pathway []; the comediator SMADs (co-SMADs), including SMAD4, which interact with R-SMADs to participate in signalling []; and the inhibitory SMADs (I-SMADs), including SMAD6 and -7, which block the activation of R-SMADs and Co-SMADs, thereby negatively regulating signalling pathways []. Domains with this fold are also found as the transactivation domain of interferon regulatory factor 3 (IRF3), which has a weak homology to SMAD domains [], and the N-terminal domain of EssC protein in Staphylococcus aureus.
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Protein
Q8R3G1
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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Protein
A6PWD2
Organism: Mus musculus/domesticus
Length: 1420  
Fragment?: false
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Protein
Q8BUN5
Organism: Mus musculus/domesticus
Length: 425  
Fragment?: false
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Protein
E9PVX6
Organism: Mus musculus/domesticus
Length: 3177  
Fragment?: false
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Protein
Q8BIZ6
Organism: Mus musculus/domesticus
Length: 383  
Fragment?: false
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Protein
Q9JIW5
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
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Protein
Q62432
Organism: Mus musculus/domesticus
Length: 467  
Fragment?: false
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Protein
P97471
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: false
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Protein
P70340
Organism: Mus musculus/domesticus
Length: 465  
Fragment?: false
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Protein
P97454
Organism: Mus musculus/domesticus
Length: 465  
Fragment?: false
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Protein
Q99KJ5
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: false
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Protein
O35253
Organism: Mus musculus/domesticus
Length: 426  
Fragment?: false
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Protein
E3SRG8
Organism: Mus musculus/domesticus
Length: 455  
Fragment?: false
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Protein
G3XA31
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: false
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Protein
G3UZZ4
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: false
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Protein
G3UX64
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: true
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Protein
E0CY08
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: true
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Protein
A0A0G2JGX6
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: true
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Protein
Q7TQJ9
Organism: Mus musculus/domesticus
Length: 806  
Fragment?: true
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Protein
A2ADR8
Organism: Mus musculus/domesticus
Length: 350  
Fragment?: false
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Protein
E0CY69
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: true
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Protein
Q9CRR7
Organism: Mus musculus/domesticus
Length: 377  
Fragment?: true
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Protein
B2RPW6
Organism: Mus musculus/domesticus
Length: 426  
Fragment?: false
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Protein
Q811W8
Organism: Mus musculus/domesticus
Length: 545  
Fragment?: false
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Protein
E3SRH0
Organism: Mus musculus/domesticus
Length: 465  
Fragment?: false
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Protein
G3UX42
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: true
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Protein
Q0VER3
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
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Protein
Q3UUI2
Organism: Mus musculus/domesticus
Length: 536  
Fragment?: true
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Protein
Q80ZV9
Organism: Mus musculus/domesticus
Length: 495  
Fragment?: false
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Protein
E0CZ64
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: true
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Protein
Q3V3E0
Organism: Mus musculus/domesticus
Length: 371  
Fragment?: true
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Protein
Q6GQW1
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: true
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Protein
E3SRG7
Organism: Mus musculus/domesticus
Length: 402  
Fragment?: false
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Protein
E9Q1Q0
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
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Protein
E9Q3M0
Organism: Mus musculus/domesticus
Length: 434  
Fragment?: false
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Protein
A0A3Q4EC15
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: false
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Protein
A2CG44
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: true
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Protein
A0A0G2JGG6
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
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Protein
Q3UVC6
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
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Protein
E9PX68
Organism: Mus musculus/domesticus
Length: 744  
Fragment?: false
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Protein
A0A0G2JG71
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
Q8C3Y6
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
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Protein
E9Q585
Organism: Mus musculus/domesticus
Length: 715  
Fragment?: false
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Protein Domain
IPR036578 | SMAD_MH1_sf
Type: Homologous_superfamily
Description: Smad proteins are signal transducers and transcriptional comodulators of the TGF-beta superfamily of ligands, which play a central role in regulating a broad range of cellular responses, including cell growth, differentiation, and specification of developmental fate, in diverse organisms from Caenorhabditis elegans to humans. Ligand binding to specific transmembrane receptor kinases induces receptor oligomerisation and phosphorylation of the receptor specific Smad protein (R-Smad) in the cytoplasm. The R-Smad proteins regulate distinct signalling pathways. Smad1, 5 and 8 mediate the signals of bone morphogenetic proteins (BMPs), while Smad2 and 3 mediate the signals of activins and TGF-betas. Upon ligand stimulation, R-Smad proteins are phosphorylated at the conserved C-terminal tail sequence, SS*xS* (where S* denotes a site of phosphorylation). The phosphorylated states of R-Smad proteins form heteromeric complexes with Smad4 and are translocated into the nucleus. In the nucleus, the heteromeric complexes function as gene-specific transcription activators by binding to promoters and interacting with transcriptional coactivators. Smad6 and Smad7 are inhibitory Smad proteins that inhibit TGF-beta signalling by interfering with either receptor-mediated phosphorylation or hetero-oligomerisation between Smad4 and R-Smad proteins. Smad proteins comprise two conserved MAD homology domains, one in the N terminus (MH1) and one in the C terminus (MH2), separated by a more variable, proline-rich linker region. The MH1 domain has a role in DNA binding and negatively regulates the functions of MH2 domain, whereas the MH2 domain is responsible for transactivation and mediates phosphorylation-triggered heteromeric assembly between Smad4 and R-Smad [, ]. The MH1 domain adopts a compact globular fold, with four alpha helices, six short beta strands, and five loops. The N-terminal half of the sequence consists of three alpha helices, and the C-terminal half contains all six beta strands, which form two small beta sheets and one beta hairpin. The fourth alpha helix is located in the hydrophobic core of the molecule, surrounded by the N-terminal three alpha helices on one side and by the two small beta sheets and the beta hairpin on the other side. These secondary structural elements are connected with five intervening surface loops. The MH1 domain employs a novel DNA-binding motif, an 11-residue β-hairpin formed by strands B2 and B3, to contact DNA in the major groove. Two residues in the L3 loop and immediately preceding strand B2 also contribute significantly to DNA recognition. The beta hairpin appears to protrude outward from the globular MH1 core [].
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Protein Domain
IPR013019 | MAD_homology_MH1
Type: Domain
Description: Smad proteins are signal transducers and transcriptional comodulators of the TGF-beta superfamily of ligands, which play a central role in regulating a broad range of cellular responses, including cell growth, differentiation, and specification of developmental fate, in diverse organisms from Caenorhabditis elegans to humans. Ligand binding to specific transmembrane receptor kinases induces receptor oligomerisation and phosphorylation of the receptor specific Smad protein (R-Smad) in the cytoplasm. The R-Smad proteins regulate distinct signalling pathways. Smad1, 5 and 8 mediate the signals of bone morphogenetic proteins (BMPs), while Smad2 and 3 mediate the signals of activins and TGF-betas. Upon ligand stimulation, R-Smad proteins are phosphorylated at the conserved C-terminal tail sequence, SS*xS* (where S* denotes a site of phosphorylation). The phosphorylated states of R-Smad proteins form heteromeric complexes with Smad4 and are translocated into the nucleus. In the nucleus, the heteromeric complexes function as gene-specific transcription activators by binding to promoters and interacting with transcriptional coactivators. Smad6 and Smad7 are inhibitory Smad proteins that inhibit TGF-beta signalling by interfering with either receptor-mediated phosphorylation or hetero-oligomerisation between Smad4 and R-Smad proteins. Smad proteins comprise two conserved MAD homology domains, one in the N terminus (MH1) and one in the C terminus (MH2), separated by a more variable, proline-rich linker region. The MH1 domain has a role in DNA binding and negatively regulates the functions of MH2 domain, whereas the MH2 domain is responsible for transactivation and mediates phosphorylation-triggered heteromeric assembly between Smad4 and R-Smad [, ]. The MH1 domain adopts a compact globular fold, with four alpha helices, six short beta strands, and five loops. The N-terminal half of the sequence consists of three alpha helices, and the C-terminal half contains all six beta strands, which form two small beta sheets and one beta hairpin. The fourth alpha helix is located in the hydrophobic core of the molecule, surrounded by the N-terminal three alpha helices on one side and by the two small beta sheets and the beta hairpin on the other side. These secondary structural elements are connected with five intervening surface loops. The MH1 domain employs a novel DNA-binding motif, an 11-residue β-hairpin formed by strands B2 and B3, to contact DNA in the major groove. Two residues in the L3 loop and immediately preceding strand B2 also contribute significantly to DNA recognition. The beta hairpin appears to protrude outward from the globular MH1 core [].
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Protein
Q8C2P1
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: true
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Protein
Q3TZQ3
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
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Protein
E9PZV6
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: true
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Protein
G3UXH8
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
A2CG45
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: true
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Publication
9741623 | -
First Author: Shi Y
Year: 1998
Journal: Cell
Title: Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-beta signaling.
Volume: 94
Issue: 5
Pages: 585-94
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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