HUMAN:SMAD2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	SMAD2 (synonyms: MADH2, MADR2)
Protein Name(s)	Mothers against decapentaplegic homolog 2 MAD homolog 2 Mothers against DPP homolog 2 JV18-1 Mad-related protein 2 hMAD-2 SMAD family member 2 SMAD 2 Smad2 hSMAD2
External Links
UniProt	Q15796
EMBL	U59911 U68018 U65019 AF027964 U78733 U78727 U78728 U78729 U78730 U78731 U78732 BC014840 BC025699
CCDS	CCDS11934.1
PIR	S71797
RefSeq	NP_001003652.1 NP_005892.1 XP_005258316.1 XP_006722514.1 XP_011524285.1
UniGene	Hs.12253 Hs.705764 Hs.741342
PDB	1DEV 1KHX 1U7V 2LB3
PDBsum	1DEV 1KHX 1U7V 2LB3
ProteinModelPortal	Q15796
SMR	Q15796
BioGrid	110262
DIP	DIP-29716N
IntAct	Q15796
MINT	MINT-5006109
STRING	9606.ENSP00000262160
ChEMBL	CHEMBL2396512
PhosphoSite	Q15796
BioMuta	SMAD2
DMDM	13633914
MaxQB	Q15796
PaxDb	Q15796
PRIDE	Q15796
DNASU	4087
Ensembl	ENST00000262160 ENST00000356825 ENST00000402690 ENST00000586040
GeneID	4087
KEGG	hsa:4087
UCSC	uc002lcy.4 uc010xdc.3
CTD	4087
GeneCards	GC18M045357
HGNC	HGNC:6768
HPA	CAB025507
MIM	601366
neXtProt	NX_Q15796
PharmGKB	PA134959722
eggNOG	NOG320700
GeneTree	ENSGT00760000119091
HOGENOM	HOG000286018
HOVERGEN	HBG053353
InParanoid	Q15796
KO	K04500
OMA	NYPDQTR
OrthoDB	EOG7W1540
PhylomeDB	Q15796
TreeFam	TF314923
Reactome	REACT_111057 REACT_120727 REACT_120734 REACT_120850 REACT_121111 REACT_150238 REACT_169103 REACT_169107 REACT_169165 REACT_169263 REACT_263856
SignaLink	Q15796
ChiTaRS	SMAD2
EvolutionaryTrace	Q15796
GeneWiki	Mothers_against_decapentaplegic_homolog_2
GenomeRNAi	4087
NextBio	16020
PRO	PR:Q15796
Proteomes	UP000005640
Bgee	Q15796
CleanEx	HS_SMAD2
ExpressionAtlas	Q15796
Genevisible	Q15796
GO	GO:0032444 GO:0005737 GO:0005829 GO:0000790 GO:0005654 GO:0005634 GO:0071141 GO:0071144 GO:0005667 GO:0033613 GO:0003682 GO:0070410 GO:0003690 GO:0035326 GO:0070411 GO:0046872 GO:0019902 GO:0070412 GO:0000978 GO:0001077 GO:0003700 GO:0046332 GO:0008134 GO:0005160 GO:0030618 GO:0034713 GO:0031625 GO:0032924 GO:0009952 GO:0045165 GO:0007182 GO:0048701 GO:0048617 GO:0001706 GO:0007369 GO:0010467 GO:0001701 GO:0030073 GO:0035556 GO:0030324 GO:0001707 GO:0000122 GO:0045892 GO:0030512 GO:0038092 GO:0035265 GO:0060021 GO:0031016 GO:0048340 GO:0060039 GO:0030513 GO:0010718 GO:1900224 GO:0045944 GO:0045893 GO:0009791 GO:0031053 GO:0051098 GO:0017015 GO:0070723 GO:0009749 GO:0007183 GO:0060395 GO:0035019 GO:0006367 GO:0006351 GO:0007179 GO:0001657 GO:0007352
Gene3D	2.60.200.10 3.90.520.10
InterPro	IPR013790 IPR003619 IPR013019 IPR017855 IPR001132 IPR008984
PANTHER	PTHR13703
Pfam	PF03165 PF03166
SMART	SM00523 SM00524
SUPFAM	SSF49879 SSF56366
PROSITE	PS51075 PS51076

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:19274049^[1]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:19274049^[1]	ECO:0000255	match to sequence model evidence used in manual assertion	InterPro:IPR001132 InterPro:IPR003619 InterPro:IPR013019 InterPro:IPR013790	F		Seeded From UniProt	complete
enables	GO:0048156	tau protein binding	PMID:24964035^[2]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	F		Seeded From UniProt	complete
enables	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	PMID:24964035^[2]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	F	has_input:(ENSEMBL:ENSG00000127445) occurs_at:(SO:0000170)	Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	GO_REF:0000113	ECO:0005556	multiple sequence alignment evidence used in manual assertion	UniProtKB:P97454	F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:15231848^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0097718	disordered domain specific binding	PMID:15231848^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95405	F		Seeded From UniProt	complete
enables	GO:0070878	primary miRNA binding	PMID:18548003^[4]	ECO:0000353	physical interaction evidence used in manual assertion	RNAcentral:URS000018AA08_9606	F	part_of:(GO:0007179)	Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	PMID:18548003^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:25893292^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	PMID:9389648^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_at:(SO:0001952)	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:9389648^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	PMID:9389648^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1900224	positive regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry	PMID:17239842^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0071144	heteromeric SMAD protein complex	PMID:21828274^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002322)	Seeded From UniProt	complete
involved_in	GO:0070723	response to cholesterol	PMID:17878231^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0070412	R-SMAD binding	PMID:9311995^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P84022	F		Seeded From UniProt	complete
enables	GO:0070411	I-SMAD binding	PMID:9256479^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O43541	F		Seeded From UniProt	complete
enables	GO:0070410	co-SMAD binding	PMID:9311995^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13485	F		Seeded From UniProt	complete
enables	GO:0070410	co-SMAD binding	PMID:9111321^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13485	F		Seeded From UniProt	complete
involved_in	GO:0062009	secondary palate development	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:14555988^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:9389648^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:9732876^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:9311995^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:14555988^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0038092	nodal signaling pathway	PMID:15150278^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0035326	enhancer binding	PMID:21828274^[8]	ECO:0000305	curator inference used in manual assertion	GO:0000790	F	part_of:(CL:0002322) has_input:(ENSEMBL:ENSG00000243709)	Seeded From UniProt	complete
enables	GO:0034713	type I transforming growth factor beta receptor binding	PMID:8980228^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P36897	F		Seeded From UniProt	complete
involved_in	GO:0032924	activin receptor signaling pathway	PMID:15150278^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032444	activin responsive factor complex	PMID:9389648^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:19122240^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HAU4	F		Seeded From UniProt	complete
enables	GO:0030618	transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity	PMID:9256479^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0030618	transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity	PMID:9389648^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0030513	positive regulation of BMP signaling pathway	PMID:19366699^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0017015	regulation of transforming growth factor beta receptor signaling pathway	PMID:14555988^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010718	positive regulation of epithelial to mesenchymal transition	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	P		Seeded From UniProt	complete
involved_in	GO:0007352	zygotic specification of dorsal/ventral axis	PMID:9436979^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007183	SMAD protein complex assembly	PMID:9111321^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	PMID:8980228^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	PMID:9389648^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	PMID:9732876^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	PMID:8752209^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9389648^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9311995^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12411310^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005667	transcription factor complex	PMID:17438144^[22]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9389648^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9311995^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:8980228^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:12411310^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005160	transforming growth factor beta receptor binding	PMID:9311995^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P36897	F		Seeded From UniProt	complete
contributes_to	GO:0003700	DNA-binding transcription factor activity	PMID:17438144^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	PMID:9389648^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
contributes_to	GO:0003677	DNA binding	PMID:9389648^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0000790	nuclear chromatin	PMID:21828274^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000925)\|part_of:(CL:0002322)	Seeded From UniProt	complete
part_of	GO:0071141	SMAD protein complex	PMID:18832382^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051098	regulation of binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	P		Seeded From UniProt	complete
involved_in	GO:0048340	paraxial mesoderm morphogenesis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	P		Seeded From UniProt	complete
enables	GO:0046332	SMAD binding	PMID:11160896^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q06413	F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	P		Seeded From UniProt	complete
involved_in	GO:0045165	cell fate commitment	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	P		Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	P		Seeded From UniProt	complete
enables	GO:0033613	activating transcription factor binding	PMID:11160896^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q02078	F		Seeded From UniProt	complete
enables	GO:0019902	phosphatase binding	PMID:16751101^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35813	F		Seeded From UniProt	complete
involved_in	GO:0009952	anterior/posterior pattern specification	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:9702198^[26]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O75593	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21599657^[27]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16751101^[25]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	F		Seeded From UniProt	complete
involved_in	GO:0001707	mesoderm formation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q62432	P		Seeded From UniProt	complete
involved_in	GO:0007182	common-partner SMAD protein phosphorylation	PMID:16806156^[28]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O70436 ensembl:ENSRNOP00000075341	P		Seeded From UniProt	complete
involved_in	GO:0042060	wound healing	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O70436 ensembl:ENSRNOP00000075341	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O70436 ensembl:ENSRNOP00000075341	C		Seeded From UniProt	complete
involved_in	GO:0030325	adrenal gland development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O70436 ensembl:ENSRNOP00000075341	P		Seeded From UniProt	complete
involved_in	GO:0023019	signal transduction involved in regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O70436 ensembl:ENSRNOP00000075341	P		Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O70436 ensembl:ENSRNOP00000075341	P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O70436 ensembl:ENSRNOP00000075341	F		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O70436 ensembl:ENSRNOP00000075341	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O70436 ensembl:ENSRNOP00000075341	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O70436 ensembl:ENSRNOP00000075341	C		Seeded From UniProt	complete
involved_in	GO:0062009	secondary palate development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0060395	SMAD protein signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0060039	pericardium development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0051098	regulation of binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0048701	embryonic cranial skeleton morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0048617	embryonic foregut morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0048589	developmental growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0048340	paraxial mesoderm morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
enables	GO:0048156	tau protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	F		Seeded From UniProt	complete
enables	GO:0046332	SMAD binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0045165	cell fate commitment	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	F		Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0035265	organ growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0031016	pancreas development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0030324	lung development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0030073	insulin secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0010718	positive regulation of epithelial to mesenchymal transition	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0009952	anterior/posterior pattern specification	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0009880	embryonic pattern specification	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0009791	post-embryonic development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0009749	response to glucose	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	F		Seeded From UniProt	complete
involved_in	GO:0007507	heart development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0007492	endoderm development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0007389	pattern specification process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0007369	gastrulation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	C		Seeded From UniProt	complete
part_of	GO:0005667	transcription factor complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	C		Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	F		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	F		Seeded From UniProt	complete
involved_in	GO:0001707	mesoderm formation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0001706	endoderm formation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0001701	in utero embryonic development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
involved_in	GO:0001657	ureteric bud development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	P		Seeded From UniProt	complete
enables	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q62432 ensembl:ENSMUSP00000130115	F		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013019	F		Seeded From UniProt	complete
part_of	GO:0005667	transcription factor complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013019	C		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001132 InterPro:IPR003619 InterPro:IPR013019 InterPro:IPR013790	P		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013019 InterPro:IPR036578	P		Seeded From UniProt	complete
involved_in	GO:0031053	primary miRNA processing	PMID:19018011^[29]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007369	gastrulation	PMID:19018011^[29]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	Reactome:R-HSA-2173796	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035019	somatic stem cell population maintenance	Reactome:R-HSA-452723	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030512	negative regulation of transforming growth factor beta receptor signaling pathway	Reactome:R-HSA-2173788	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016579	protein deubiquitination	Reactome:R-HSA-5688426	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	Reactome:R-HSA-2173789	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-6781764 Reactome:R-HSA-3713560 Reactome:R-HSA-3702186 Reactome:R-HSA-3702184 Reactome:R-HSA-3702153 Reactome:R-HSA-3656523 Reactome:R-HSA-3315483 Reactome:R-HSA-3311014 Reactome:R-HSA-3304394 Reactome:R-HSA-2187405 Reactome:R-HSA-2187401 Reactome:R-HSA-2187395 Reactome:R-HSA-2187358 Reactome:R-HSA-2187355 Reactome:R-HSA-2176452 Reactome:R-HSA-2176445 Reactome:R-HSA-2106579 Reactome:R-HSA-2031355 Reactome:R-HSA-173542 Reactome:R-HSA-173488 Reactome:R-HSA-170868 Reactome:R-HSA-170850 Reactome:R-HSA-170847 Reactome:R-HSA-170835 Reactome:R-HSA-1549526	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-NUL-9625758 Reactome:R-NUL-2186755 Reactome:R-NUL-2186736 Reactome:R-HSA-9618021 Reactome:R-HSA-9618004 Reactome:R-HSA-9617996 Reactome:R-HSA-870538 Reactome:R-HSA-870449 Reactome:R-HSA-480204 Reactome:R-HSA-2187395 Reactome:R-HSA-2187388 Reactome:R-HSA-2187330 Reactome:R-HSA-2187325 Reactome:R-HSA-2187309 Reactome:R-HSA-2186643 Reactome:R-HSA-2186607 Reactome:R-HSA-2179276 Reactome:R-HSA-2179274 Reactome:R-HSA-2176503 Reactome:R-HSA-2176502 Reactome:R-HSA-2176491 Reactome:R-HSA-2176475 Reactome:R-HSA-2127257 Reactome:R-HSA-2106579 Reactome:R-HSA-209055 Reactome:R-HSA-173545 Reactome:R-HSA-173488 Reactome:R-HSA-173481 Reactome:R-HSA-1535903 Reactome:R-HSA-1225919 Reactome:R-HSA-1112609	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	Reactome:R-HSA-2173795	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page
↑ ^2.0 ^2.1 Ueberham, U et al. (2014) Pin1 promotes degradation of Smad proteins and their interaction with phosphorylated tau in Alzheimer's disease. Neuropathol. Appl. Neurobiol. 40 815-32 PubMed GONUTS page
↑ ^3.0 ^3.1 Chong, PA et al. (2004) Disorder in a target for the smad2 mad homology 2 domain and its implications for binding and specificity. J. Biol. Chem. 279 40707-14 PubMed GONUTS page
↑ ^4.0 ^4.1 Davis, BN et al. (2008) SMAD proteins control DROSHA-mediated microRNA maturation. Nature 454 56-61 PubMed GONUTS page
↑ Hwangbo, C et al. (2016) Syntenin regulates TGF-β1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-β type I receptor internalization. Oncogene 35 389-401 PubMed GONUTS page
↑ ^6.00 ^6.01 ^6.02 ^6.03 ^6.04 ^6.05 ^6.06 ^6.07 ^6.08 ^6.09 ^6.10 Liu, F et al. (1997) Dual role of the Smad4/DPC4 tumor suppressor in TGFbeta-inducible transcriptional complexes. Genes Dev. 11 3157-67 PubMed GONUTS page
↑ Vonica, A & Brivanlou, AH (2007) The left-right axis is regulated by the interplay of Coco, Xnr1 and derrière in Xenopus embryos. Dev. Biol. 303 281-94 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Yoon, SJ et al. (2011) HEB and E2A function as SMAD/FOXH1 cofactors. Genes Dev. 25 1654-61 PubMed GONUTS page
↑ Chen, CL et al. (2007) Cholesterol suppresses cellular TGF-beta responsiveness: implications in atherogenesis. J. Cell. Sci. 120 3509-21 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Nakao, A et al. (1997) TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4. EMBO J. 16 5353-62 PubMed GONUTS page
↑ ^11.0 ^11.1 Topper, JN et al. (1997) Vascular MADs: two novel MAD-related genes selectively inducible by flow in human vascular endothelium. Proc. Natl. Acad. Sci. U.S.A. 94 9314-9 PubMed GONUTS page
↑ ^12.0 ^12.1 Wu, RY et al. (1997) Heteromeric and homomeric interactions correlate with signaling activity and functional cooperativity of Smad3 and Smad4/DPC4. Mol. Cell. Biol. 17 2521-8 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Kretschmer, A et al. (2003) Differential regulation of TGF-beta signaling through Smad2, Smad3 and Smad4. Oncogene 22 6748-63 PubMed GONUTS page
↑ ^14.0 ^14.1 Zhang, Y et al. (1998) Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-beta-induced transcription. Nature 394 909-13 PubMed GONUTS page
↑ ^15.0 ^15.1 Munir, S et al. (2004) Nodal and ALK7 inhibit proliferation and induce apoptosis in human trophoblast cells. J. Biol. Chem. 279 31277-86 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Macías-Silva, M et al. (1996) MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell 87 1215-24 PubMed GONUTS page
↑ Nakano, A et al. (2009) Pin1 down-regulates transforming growth factor-beta (TGF-beta) signaling by inducing degradation of Smad proteins. J. Biol. Chem. 284 6109-15 PubMed GONUTS page
↑ Upton, PD et al. (2009) Bone morphogenetic protein (BMP) and activin type II receptors balance BMP9 signals mediated by activin receptor-like kinase-1 in human pulmonary artery endothelial cells. J. Biol. Chem. 284 15794-804 PubMed GONUTS page
↑ Hata, A et al. (1998) Smad6 inhibits BMP/Smad1 signaling by specifically competing with the Smad4 tumor suppressor. Genes Dev. 12 186-97 PubMed GONUTS page
↑ Eppert, K et al. (1996) MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma. Cell 86 543-52 PubMed GONUTS page
↑ ^21.0 ^21.1 Zhang, H et al. (2003) Cellular response to hypoxia involves signaling via Smad proteins. Blood 101 2253-60 PubMed GONUTS page
↑ ^22.0 ^22.1 Zhang, S et al. (2007) Smad7 antagonizes transforming growth factor beta signaling in the nucleus by interfering with functional Smad-DNA complex formation. Mol. Cell. Biol. 27 4488-99 PubMed GONUTS page
↑ Thuault, S et al. (2008) HMGA2 and Smads co-regulate SNAIL1 expression during induction of epithelial-to-mesenchymal transition. J. Biol. Chem. 283 33437-46 PubMed GONUTS page
↑ ^24.0 ^24.1 Quinn, ZA et al. (2001) Smad proteins function as co-modulators for MEF2 transcriptional regulatory proteins. Nucleic Acids Res. 29 732-42 PubMed GONUTS page
↑ ^25.0 ^25.1 Lin, X et al. (2006) PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling. Cell 125 915-28 PubMed GONUTS page
↑ Zhou, S et al. (1998) Characterization of human FAST-1, a TGF beta and activin signal transducer. Mol. Cell 2 121-7 PubMed GONUTS page
↑ Luo, Y et al. (2011) ZNF580, a novel C2H2 zinc-finger transcription factor, interacts with the TGF-β signal molecule Smad2. Cell Biol. Int. 35 1153-7 PubMed GONUTS page
↑ Dudas, M et al. (2006) Epithelial and ectomesenchymal role of the type I TGF-beta receptor ALK5 during facial morphogenesis and palatal fusion. Dev. Biol. 296 298-314 PubMed GONUTS page
↑ ^29.0 ^29.1 Hoover, LL & Kubalak, SW (2008) Holding their own: the noncanonical roles of Smad proteins. Sci Signal 1 pe48 PubMed GONUTS page

[PMID:19274049-1] 1.0 ^1.1 Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page

[PMID:24964035-2] 2.0 ^2.1 Ueberham, U et al. (2014) Pin1 promotes degradation of Smad proteins and their interaction with phosphorylated tau in Alzheimer's disease. Neuropathol. Appl. Neurobiol. 40 815-32 PubMed GONUTS page

[PMID:15231848-3] 3.0 ^3.1 Chong, PA et al. (2004) Disorder in a target for the smad2 mad homology 2 domain and its implications for binding and specificity. J. Biol. Chem. 279 40707-14 PubMed GONUTS page

[PMID:18548003-4] 4.0 ^4.1 Davis, BN et al. (2008) SMAD proteins control DROSHA-mediated microRNA maturation. Nature 454 56-61 PubMed GONUTS page

[PMID:25893292-5] Hwangbo, C et al. (2016) Syntenin regulates TGF-β1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-β type I receptor internalization. Oncogene 35 389-401 PubMed GONUTS page

[PMID:9389648-6] 6.00 ^6.01 ^6.02 ^6.03 ^6.04 ^6.05 ^6.06 ^6.07 ^6.08 ^6.09 ^6.10 Liu, F et al. (1997) Dual role of the Smad4/DPC4 tumor suppressor in TGFbeta-inducible transcriptional complexes. Genes Dev. 11 3157-67 PubMed GONUTS page

[PMID:17239842-7] Vonica, A & Brivanlou, AH (2007) The left-right axis is regulated by the interplay of Coco, Xnr1 and derrière in Xenopus embryos. Dev. Biol. 303 281-94 PubMed GONUTS page

[PMID:21828274-8] 8.0 ^8.1 ^8.2 Yoon, SJ et al. (2011) HEB and E2A function as SMAD/FOXH1 cofactors. Genes Dev. 25 1654-61 PubMed GONUTS page

[PMID:17878231-9] Chen, CL et al. (2007) Cholesterol suppresses cellular TGF-beta responsiveness: implications in atherogenesis. J. Cell. Sci. 120 3509-21 PubMed GONUTS page

[PMID:9311995-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Nakao, A et al. (1997) TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4. EMBO J. 16 5353-62 PubMed GONUTS page

[PMID:9256479-11] 11.0 ^11.1 Topper, JN et al. (1997) Vascular MADs: two novel MAD-related genes selectively inducible by flow in human vascular endothelium. Proc. Natl. Acad. Sci. U.S.A. 94 9314-9 PubMed GONUTS page

[PMID:9111321-12] 12.0 ^12.1 Wu, RY et al. (1997) Heteromeric and homomeric interactions correlate with signaling activity and functional cooperativity of Smad3 and Smad4/DPC4. Mol. Cell. Biol. 17 2521-8 PubMed GONUTS page

[PMID:14555988-13] 13.0 ^13.1 ^13.2 Kretschmer, A et al. (2003) Differential regulation of TGF-beta signaling through Smad2, Smad3 and Smad4. Oncogene 22 6748-63 PubMed GONUTS page

[PMID:9732876-14] 14.0 ^14.1 Zhang, Y et al. (1998) Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-beta-induced transcription. Nature 394 909-13 PubMed GONUTS page

[PMID:15150278-15] 15.0 ^15.1 Munir, S et al. (2004) Nodal and ALK7 inhibit proliferation and induce apoptosis in human trophoblast cells. J. Biol. Chem. 279 31277-86 PubMed GONUTS page

[PMID:8980228-16] 16.0 ^16.1 ^16.2 Macías-Silva, M et al. (1996) MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell 87 1215-24 PubMed GONUTS page

[PMID:19122240-17] Nakano, A et al. (2009) Pin1 down-regulates transforming growth factor-beta (TGF-beta) signaling by inducing degradation of Smad proteins. J. Biol. Chem. 284 6109-15 PubMed GONUTS page

[PMID:19366699-18] Upton, PD et al. (2009) Bone morphogenetic protein (BMP) and activin type II receptors balance BMP9 signals mediated by activin receptor-like kinase-1 in human pulmonary artery endothelial cells. J. Biol. Chem. 284 15794-804 PubMed GONUTS page

[PMID:9436979-19] Hata, A et al. (1998) Smad6 inhibits BMP/Smad1 signaling by specifically competing with the Smad4 tumor suppressor. Genes Dev. 12 186-97 PubMed GONUTS page

[PMID:8752209-20] Eppert, K et al. (1996) MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma. Cell 86 543-52 PubMed GONUTS page

[PMID:12411310-21] 21.0 ^21.1 Zhang, H et al. (2003) Cellular response to hypoxia involves signaling via Smad proteins. Blood 101 2253-60 PubMed GONUTS page

[PMID:17438144-22] 22.0 ^22.1 Zhang, S et al. (2007) Smad7 antagonizes transforming growth factor beta signaling in the nucleus by interfering with functional Smad-DNA complex formation. Mol. Cell. Biol. 27 4488-99 PubMed GONUTS page

[PMID:18832382-23] Thuault, S et al. (2008) HMGA2 and Smads co-regulate SNAIL1 expression during induction of epithelial-to-mesenchymal transition. J. Biol. Chem. 283 33437-46 PubMed GONUTS page

[PMID:11160896-24] 24.0 ^24.1 Quinn, ZA et al. (2001) Smad proteins function as co-modulators for MEF2 transcriptional regulatory proteins. Nucleic Acids Res. 29 732-42 PubMed GONUTS page

[PMID:16751101-25] 25.0 ^25.1 Lin, X et al. (2006) PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling. Cell 125 915-28 PubMed GONUTS page

[PMID:9702198-26] Zhou, S et al. (1998) Characterization of human FAST-1, a TGF beta and activin signal transducer. Mol. Cell 2 121-7 PubMed GONUTS page

[PMID:21599657-27] Luo, Y et al. (2011) ZNF580, a novel C2H2 zinc-finger transcription factor, interacts with the TGF-β signal molecule Smad2. Cell Biol. Int. 35 1153-7 PubMed GONUTS page

[PMID:16806156-28] Dudas, M et al. (2006) Epithelial and ectomesenchymal role of the type I TGF-beta receptor ALK5 during facial morphogenesis and palatal fusion. Dev. Biol. 296 298-314 PubMed GONUTS page

[PMID:19018011-29] 29.0 ^29.1 Hoover, LL & Kubalak, SW (2008) Holding their own: the noncanonical roles of Smad proteins. Sci Signal 1 pe48 PubMed GONUTS page

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