HUMAN:SMAD3

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	SMAD3 (synonyms: MADH3)
Protein Name(s)	Mothers against decapentaplegic homolog 3 MAD homolog 3 Mad3 Mothers against DPP homolog 3 hMAD-3 JV15-2 SMAD family member 3 SMAD 3 Smad3 hSMAD3
External Links
UniProt	P84022
EMBL	U68019 U76622 AB004930 AF025300 AF025293 AF025294 AF025295 AF025296 AF025297 AF025298 AF025299 AK290881 AK298139 AK300614 AK316017 AC012568 AC087482 CH471082 BC050743
CCDS	CCDS10222.1 CCDS45288.1 CCDS53950.1 CCDS53951.1
PIR	S71798
RefSeq	NP_001138574.1 NP_001138575.1 NP_001138576.1 NP_005893.1
UniGene	Hs.727986 Hs.742270
PDB	1MHD 1MJS 1MK2 1OZJ 1U7F 2LAJ 2LB2
PDBsum	1MHD 1MJS 1MK2 1OZJ 1U7F 2LAJ 2LB2
ProteinModelPortal	P84022
SMR	P84022
BioGrid	110263
DIP	DIP-29720N
IntAct	P84022
MINT	MINT-193987
STRING	9606.ENSP00000332973
BindingDB	P84022
ChEMBL	CHEMBL1293258
PhosphoSite	P84022
BioMuta	SMAD3
DMDM	51338669
MaxQB	P84022
PaxDb	P84022
PRIDE	P84022
DNASU	4088
Ensembl	ENST00000327367 ENST00000439724 ENST00000537194 ENST00000540846
GeneID	4088
KEGG	hsa:4088
UCSC	uc002aqj.3 uc010ujs.2
CTD	4088
GeneCards	GC15P067358
GeneReviews	SMAD3
HGNC	HGNC:6769
HPA	CAB008094 HPA046386
MIM	114500 603109 613795
neXtProt	NX_P84022
Orphanet	284984 91387
PharmGKB	PA30526
eggNOG	NOG320700
GeneTree	ENSGT00760000119091
HOGENOM	HOG000286018
HOVERGEN	HBG053353
InParanoid	P84022
KO	K04500
OMA	AVELCEY
PhylomeDB	P84022
TreeFam	TF314923
Reactome	REACT_111057 REACT_120727 REACT_120734 REACT_120850 REACT_121111 REACT_150238 REACT_169103 REACT_169107 REACT_169165 REACT_169263
SignaLink	P84022
ChiTaRS	SMAD3
EvolutionaryTrace	P84022
GeneWiki	Mothers_against_decapentaplegic_homolog_3
GenomeRNAi	4088
NextBio	16026
PRO	PR:P84022
Proteomes	UP000005640
Bgee	P84022
CleanEx	HS_SMAD3
ExpressionAtlas	P84022
Genevisible	P84022
GO	GO:0005737 GO:0005829 GO:0000790 GO:0005637 GO:0005654 GO:0005634 GO:0005886 GO:0043235 GO:0071141 GO:0071144 GO:0005667 GO:0008013 GO:0043425 GO:0031490 GO:0070410 GO:0000987 GO:0003690 GO:0035326 GO:0042802 GO:0019902 GO:0042803 GO:0019901 GO:0070412 GO:0001102 GO:0000978 GO:0000983 GO:0043565 GO:0003700 GO:0008134 GO:0044212 GO:0005160 GO:0030618 GO:0043130 GO:0031625 GO:0008270 GO:0006919 GO:0097296 GO:0032924 GO:0007050 GO:0045216 GO:0048589 GO:0048701 GO:0048617 GO:0009880 GO:0007492 GO:0019049 GO:0097191 GO:0010467 GO:0001947 GO:0006955 GO:0002520 GO:0001701 GO:0035556 GO:0070306 GO:0001889 GO:0001707 GO:0043066 GO:0030308 GO:0050728 GO:0045930 GO:0045668 GO:0033689 GO:0042177 GO:0001933 GO:0000122 GO:0030512 GO:0061045 GO:0038092 GO:0002076 GO:0048340 GO:0060039 GO:0010694 GO:0030501 GO:0090263 GO:0035413 GO:0030335 GO:0032332 GO:0010718 GO:1901203 GO:0051894 GO:0010628 GO:0032731 GO:0050927 GO:0051496 GO:0042993 GO:0045944 GO:0045893 GO:0032916 GO:0031053 GO:0050821 GO:0051098 GO:0050678 GO:0050776 GO:0016202 GO:0006357 GO:0017015 GO:0032909 GO:0001666 GO:0023019 GO:0007183 GO:0060395 GO:0001756 GO:0042110 GO:0030878 GO:0006367 GO:0006351 GO:0060290 GO:0007179 GO:0006810 GO:0001657 GO:0042060
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:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	PMID:24964035^[2]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8BUN5	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
involved_in	GO:0051481	negative regulation of cytosolic calcium ion concentration	PMID:27038547^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0000192) occurs_in:(UBERON:0002012)\|occurs_in:(CL:0000115) occurs_in:(UBERON:0002012)	Seeded From UniProt	complete
involved_in	GO:0045429	positive regulation of nitric oxide biosynthetic process	PMID:27038547^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0000192) occurs_in:(UBERON:0002012)\|occurs_in:(CL:0000115) occurs_in:(UBERON:0002012)	Seeded From UniProt	complete
enables	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	PMID:26311719^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	occurs_in:(CL:0002591) part_of:(GO:0071560) has_direct_input:(ENSEMBL:ENSG00000249669) has_direct_input:(ENSEMBL:ENSG00000276365) occurs_at:(SO:0001952)	Seeded From UniProt	complete
involved_in	GO:1902895	positive regulation of pri-miRNA transcription by RNA polymerase II	PMID:26311719^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	regulates_transcription_of:(ENSEMBL:ENSG00000276365) regulates_transcription_of:(ENSEMBL:ENSG00000249669) occurs_in:(CL:0002591) part_of:(GO:0071560)	Seeded From UniProt	complete
enables	GO:0035259	glucocorticoid receptor binding	PMID:12902338^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04150	F		Seeded From UniProt	complete
enables	GO:0070878	primary miRNA binding	PMID:18548003^[6]	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^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0017151	DEAD/H-box RNA helicase binding	PMID:18548003^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P17844	F		Seeded From UniProt	complete
enables	GO:0031962	mineralocorticoid receptor binding	PMID:12902338^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P22199	F		Seeded From UniProt	complete
involved_in	GO:0071560	cellular response to transforming growth factor beta stimulus	PMID:12902338^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045599	negative regulation of fat cell differentiation	PMID:19816956^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:25893292^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16007207^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:21947082^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006357	regulation of transcription by RNA polymerase II	PMID:21947082^[10]	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:21947082^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:21307346^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P02751)	Seeded From UniProt	complete
enables	GO:0070412	R-SMAD binding	PMID:20129061^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P84022	F		Seeded From UniProt	complete
involved_in	GO:0042307	positive regulation of protein import into nucleus	PMID:15799969^[13]	ECO:0000303	author statement without traceable support used in manual assertion		P	regulates_transport_of:(UniProtKB:Q13485)	Seeded From UniProt	complete
involved_in	GO:1901203	positive regulation of extracellular matrix assembly	PMID:21307346^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097191	extrinsic apoptotic signaling pathway	PMID:15334054^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0071144	heteromeric SMAD protein complex	PMID:21828274^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002322)	Seeded From UniProt	complete
enables	GO:0070412	R-SMAD binding	PMID:9311995^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q15796	F		Seeded From UniProt	complete
enables	GO:0070410	co-SMAD binding	PMID:9732876^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13485	F		Seeded From UniProt	complete
enables	GO:0070410	co-SMAD binding	PMID:9111321^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13485	F		Seeded From UniProt	complete
enables	GO:0070410	co-SMAD binding	PMID:9311995^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13485	F		Seeded From UniProt	complete
enables	GO:0070410	co-SMAD binding	PMID:8774881^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13485	F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:14555988^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P38936)\|has_regulation_target:(UniProtKB:P42772)\|has_regulation_target:(UniProtKB:P21980)\|has_regulation_target:(UniProtKB:P09601)\|has_regulation_target:(UniProtKB:P84022)	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:8774881^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045930	negative regulation of mitotic cell cycle	PMID:14555988^[20]	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:9732876^[17]	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:9111321^[18]	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^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045216	cell-cell junction organization	PMID:18505915^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0044212	transcription regulatory region DNA binding	PMID:9732876^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	PMID:10823886^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043425	bHLH transcription factor binding	PMID:21828274^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q99081	F	occurs_in:(CL:0002322)	Seeded From UniProt	complete
part_of	GO:0043235	receptor complex	PMID:8774881^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051091	positive regulation of DNA-binding transcription factor activity	PMID:15799969^[13]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:8774881^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P84022	F		Seeded From UniProt	complete
involved_in	GO:0038092	nodal signaling pathway	PMID:15150278^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0035326	enhancer binding	PMID:21828274^[15]	ECO:0000305	curator inference used in manual assertion	GO:0000790	F	part_of:(CL:0002322) has_input:(ENSEMBL:ENSG00000243709)	Seeded From UniProt	complete
involved_in	GO:0032924	activin receptor signaling pathway	PMID:15150278^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032909	regulation of transforming growth factor beta2 production	PMID:12411310^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:11278251^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HCE7	F		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:19122240^[26]	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:9111321^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0030308	negative regulation of cell growth	PMID:8774881^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019049	evasion or tolerance of host defenses by virus	PMID:15334054^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0017015	regulation of transforming growth factor beta receptor signaling pathway	PMID:8774881^[19]	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	PMID:18505915^[21]	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	PMID:21307346^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:21828274^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O75593	F	occurs_in:(CL:0002322)	Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:9732876^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P05412	F		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:9732876^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P01100	F		Seeded From UniProt	complete
involved_in	GO:0007183	SMAD protein complex assembly	PMID:9111321^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007183	SMAD protein complex assembly	PMID:10823886^[22]	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^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007050	cell cycle arrest	PMID:14555988^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006955	immune response	PMID:16886151^[27]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	PMID:15107418^[28]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060395	SMAD protein signal transduction	PMID:15799969^[13]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9311995^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12446380^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9311995^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:12446380^[29]	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^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P36897	F		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	PMID:9732876^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
contributes_to	GO:0003700	DNA-binding transcription factor activity	PMID:9111321^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	PMID:10823886^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001666	response to hypoxia	PMID:12411310^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0001102	RNA polymerase II activating transcription factor binding	PMID:17251190^[30]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P26367	F		Seeded From UniProt	complete
part_of	GO:0000790	nuclear chromatin	PMID:21828274^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000925)\|part_of:(CL:0002322)	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:14555988^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:8774881^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0071141	SMAD protein complex	PMID:21947082^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0071141	SMAD protein complex	PMID:18832382^[31]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:18832382^[31]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043130	ubiquitin binding	PMID:18794808^[32]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0019902	phosphatase binding	PMID:16751101^[33]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35813	F		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:12874272^[34]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9H2X6	F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:12686552^[35]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	PMID:21947082^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21947082^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005667	transcription factor complex	PMID:21947082^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005637	nuclear inner membrane	PMID:15647271^[36]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21947082^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	PMID:21947082^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003712	transcription coregulator activity	PMID:18832382^[31]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000987	proximal promoter sequence-specific DNA binding	PMID:21947082^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000987	proximal promoter sequence-specific DNA binding	PMID:18832382^[31]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22045334^[37]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P84022	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18729074^[38]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P84022	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903243	negative regulation of cardiac muscle hypertrophy in response to stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0097296	activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0090263	positive regulation of canonical Wnt signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0061767	negative regulation of lung blood pressure	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0060290	transdifferentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0051894	positive regulation of focal adhesion assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0051496	positive regulation of stress fiber assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0050927	positive regulation of positive chemotaxis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
enables	GO:0046332	SMAD binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	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:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0045429	positive regulation of nitric oxide biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	F		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0042177	negative regulation of protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	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:P84025 ensembl:ENSRNOP00000037346	C		Seeded From UniProt	complete
involved_in	GO:0032916	positive regulation of transforming growth factor beta3 production	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0032731	positive regulation of interleukin-1 beta production	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0030501	positive regulation of bone mineralization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0030335	positive regulation of cell migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0030325	adrenal gland development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	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:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	F		Seeded From UniProt	complete
involved_in	GO:0010694	positive regulation of alkaline phosphatase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	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:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	F		Seeded From UniProt	complete
enables	GO:0008013	beta-catenin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	F		Seeded From UniProt	complete
involved_in	GO:0007183	SMAD protein complex assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	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:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	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:P84025 ensembl:ENSRNOP00000037346	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	C		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	F		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P84025 ensembl:ENSRNOP00000037346	P		Seeded From UniProt	complete
involved_in	GO:0070306	lens fiber cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0061045	negative regulation of wound healing	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0060039	pericardium development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0050776	regulation of immune response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0050728	negative regulation of inflammatory response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0050678	regulation of epithelial cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0048589	developmental growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0045668	negative regulation of osteoblast differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	F		Seeded From UniProt	complete
involved_in	GO:0042110	T cell activation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0033689	negative regulation of osteoblast proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0032332	positive regulation of chondrocyte differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
enables	GO:0031490	chromatin DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	F		Seeded From UniProt	complete
involved_in	GO:0030878	thyroid gland development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0017015	regulation of transforming growth factor beta receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0016202	regulation of striated muscle tissue development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	F		Seeded From UniProt	complete
involved_in	GO:0007492	endoderm development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0007369	gastrulation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	C		Seeded From UniProt	complete
enables	GO:0005518	collagen binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	F		Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	F		Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	F		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	F		Seeded From UniProt	complete
involved_in	GO:0002520	immune system development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0002076	osteoblast development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0001947	heart looping	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0001889	liver development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0001756	somitogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0001707	mesoderm formation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0001649	osteoblast differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		Seeded From UniProt	complete
involved_in	GO:0001501	skeletal system development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	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:Q8BUN5 ensembl:ENSMUSP00000034973	F		Seeded From UniProt	complete
enables	GO:0000977	RNA polymerase II regulatory region sequence-specific DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	F		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8BUN5 ensembl:ENSMUSP00000034973	P		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:0042060	wound healing	PMID:19018011^[39]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031053	primary miRNA processing	PMID:19018011^[39]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071345	cellular response to cytokine stimulus	Reactome:R-HSA-9008059	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: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-9009910 Reactome:R-HSA-9008928 Reactome:R-HSA-9008692 Reactome:R-HSA-6781764 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-2187405 Reactome:R-HSA-2187401 Reactome:R-HSA-2187395 Reactome:R-HSA-2187382 Reactome:R-HSA-2187375 Reactome:R-HSA-2187368 Reactome:R-HSA-2187358 Reactome:R-HSA-2187355 Reactome:R-HSA-2106579 Reactome:R-HSA-2031355 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-8952226 Reactome:R-HSA-8878178 Reactome:R-HSA-8878143 Reactome:R-HSA-870538 Reactome:R-HSA-870449 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	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
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
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
	GO:0005634	nucleus	PMID:20097766^[40]	ECO:0000314			C		Figure 4C shows localization of wild type SMAD3 in the nucleus	complete CACAO 11864
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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
↑ 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 Liu, Y et al. (2016) MiRNA-199a-5p influences pulmonary artery hypertension via downregulating Smad3. Biochem. Biophys. Res. Commun. 473 859-866 PubMed GONUTS page
↑ ^4.0 ^4.1 Deng, L et al. (2015) MicroRNA-143 Activation Regulates Smooth Muscle and Endothelial Cell Crosstalk in Pulmonary Arterial Hypertension. Circ. Res. 117 870-883 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Li, G et al. (2003) Identification of glucocorticoid receptor domains involved in transrepression of transforming growth factor-beta action. J. Biol. Chem. 278 41779-88 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Davis, BN et al. (2008) SMAD proteins control DROSHA-mediated microRNA maturation. Nature 454 56-61 PubMed GONUTS page
↑ Kim, YJ et al. (2009) MiR-21 regulates adipogenic differentiation through the modulation of TGF-beta signaling in mesenchymal stem cells derived from human adipose tissue. Stem Cells 27 3093-102 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
↑ Pavio, N et al. (2005) Hepatitis C virus core variants isolated from liver tumor but not from adjacent non-tumor tissue interact with Smad3 and inhibit the TGF-beta pathway. Oncogene 24 6119-32 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 ^10.7 ^10.8 ^10.9 Inui, M et al. (2011) USP15 is a deubiquitylating enzyme for receptor-activated SMADs. Nat. Cell Biol. 13 1368-75 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Guo, X et al. (2011) Response gene to complement 32 interacts with Smad3 to promote epithelial-mesenchymal transition of human renal tubular cells. Am. J. Physiol., Cell Physiol. 300 C1415-21 PubMed GONUTS page
↑ Watanabe, Y et al. (2010) TMEPAI, a transmembrane TGF-beta-inducible protein, sequesters Smad proteins from active participation in TGF-beta signaling. Mol. Cell 37 123-34 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Chen, HB et al. (2005) Nuclear targeting of transforming growth factor-beta-activated Smad complexes. J. Biol. Chem. 280 21329-36 PubMed GONUTS page
↑ ^14.0 ^14.1 Cheng, PL et al. (2004) Hepatitis C viral proteins interact with Smad3 and differentially regulate TGF-beta/Smad3-mediated transcriptional activation. Oncogene 23 7821-38 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 ^15.4 Yoon, SJ et al. (2011) HEB and E2A function as SMAD/FOXH1 cofactors. Genes Dev. 25 1654-61 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 Nakao, A et al. (1997) TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4. EMBO J. 16 5353-62 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 ^17.6 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
↑ ^18.0 ^18.1 ^18.2 ^18.3 ^18.4 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
↑ ^19.0 ^19.1 ^19.2 ^19.3 ^19.4 ^19.5 ^19.6 Zhang, Y et al. (1996) Receptor-associated Mad homologues synergize as effectors of the TGF-beta response. Nature 383 168-72 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 ^20.3 Kretschmer, A et al. (2003) Differential regulation of TGF-beta signaling through Smad2, Smad3 and Smad4. Oncogene 22 6748-63 PubMed GONUTS page
↑ ^21.0 ^21.1 Do, TV et al. (2008) Transforming growth factor-beta1, transforming growth factor-beta2, and transforming growth factor-beta3 enhance ovarian cancer metastatic potential by inducing a Smad3-dependent epithelial-to-mesenchymal transition. Mol. Cancer Res. 6 695-705 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 Denissova, NG et al. (2000) Transforming growth factor beta -inducible independent binding of SMAD to the Smad7 promoter. Proc. Natl. Acad. Sci. U.S.A. 97 6397-402 PubMed GONUTS page
↑ ^23.0 ^23.1 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
↑ ^24.0 ^24.1 Zhang, H et al. (2003) Cellular response to hypoxia involves signaling via Smad proteins. Blood 101 2253-60 PubMed GONUTS page
↑ Ebisawa, T et al. (2001) Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation. J. Biol. Chem. 276 12477-80 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
↑ Adewoye, AH et al. (2006) Association of polymorphisms of IGF1R and genes in the transforming growth factor- beta /bone morphogenetic protein pathway with bacteremia in sickle cell anemia. Clin. Infect. Dis. 43 593-8 PubMed GONUTS page
↑ Kim, BC et al. (2004) Activin receptor-like kinase-7 induces apoptosis through activation of MAPKs in a Smad3-dependent mechanism in hepatoma cells. J. Biol. Chem. 279 28458-65 PubMed GONUTS page
↑ ^29.0 ^29.1 Saika, S et al. (2002) TGFbeta-Smad signalling in postoperative human lens epithelial cells. Br J Ophthalmol 86 1428-33 PubMed GONUTS page
↑ Grocott, T et al. (2007) The MH1 domain of Smad3 interacts with Pax6 and represses autoregulation of the Pax6 P1 promoter. Nucleic Acids Res. 35 890-901 PubMed GONUTS page
↑ ^31.0 ^31.1 ^31.2 ^31.3 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
↑ Guo, X et al. (2008) Ligand-dependent ubiquitination of Smad3 is regulated by casein kinase 1 gamma 2, an inhibitor of TGF-beta signaling. Oncogene 27 7235-47 PubMed GONUTS page
↑ Lin, X et al. (2006) PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling. Cell 125 915-28 PubMed GONUTS page
↑ Harada, J et al. (2003) Requirement of the co-repressor homeodomain-interacting protein kinase 2 for ski-mediated inhibition of bone morphogenetic protein-induced transcriptional activation. J. Biol. Chem. 278 38998-9005 PubMed GONUTS page
↑ Chai, J et al. (2003) Features of a Smad3 MH1-DNA complex. Roles of water and zinc in DNA binding. J. Biol. Chem. 278 20327-31 PubMed GONUTS page
↑ Pan, D et al. (2005) The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines. J. Biol. Chem. 280 15992-6001 PubMed GONUTS page
↑ Tang, LY et al. (2011) Ablation of Smurf2 reveals an inhibition in TGF-β signalling through multiple mono-ubiquitination of Smad3. EMBO J. 30 4777-89 PubMed GONUTS page
↑ Brown, KA et al. (2008) Identification of novel Smad2 and Smad3 associated proteins in response to TGF-beta1. J. Cell. Biochem. 105 596-611 PubMed GONUTS page
↑ ^39.0 ^39.1 Hoover, LL & Kubalak, SW (2008) Holding their own: the noncanonical roles of Smad proteins. Sci Signal 1 pe48 PubMed GONUTS page
↑ Zhang, M et al. (2010) Smad3 prevents beta-catenin degradation and facilitates beta-catenin nuclear translocation in chondrocytes. J. Biol. Chem. 285 8703-10 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] 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:27038547-3] 3.0 ^3.1 Liu, Y et al. (2016) MiRNA-199a-5p influences pulmonary artery hypertension via downregulating Smad3. Biochem. Biophys. Res. Commun. 473 859-866 PubMed GONUTS page

[PMID:26311719-4] 4.0 ^4.1 Deng, L et al. (2015) MicroRNA-143 Activation Regulates Smooth Muscle and Endothelial Cell Crosstalk in Pulmonary Arterial Hypertension. Circ. Res. 117 870-883 PubMed GONUTS page

[PMID:12902338-5] 5.0 ^5.1 ^5.2 Li, G et al. (2003) Identification of glucocorticoid receptor domains involved in transrepression of transforming growth factor-beta action. J. Biol. Chem. 278 41779-88 PubMed GONUTS page

[PMID:18548003-6] 6.0 ^6.1 ^6.2 Davis, BN et al. (2008) SMAD proteins control DROSHA-mediated microRNA maturation. Nature 454 56-61 PubMed GONUTS page

[PMID:19816956-7] Kim, YJ et al. (2009) MiR-21 regulates adipogenic differentiation through the modulation of TGF-beta signaling in mesenchymal stem cells derived from human adipose tissue. Stem Cells 27 3093-102 PubMed GONUTS page

[PMID:25893292-8] 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:16007207-9] Pavio, N et al. (2005) Hepatitis C virus core variants isolated from liver tumor but not from adjacent non-tumor tissue interact with Smad3 and inhibit the TGF-beta pathway. Oncogene 24 6119-32 PubMed GONUTS page

[PMID:21947082-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 ^10.7 ^10.8 ^10.9 Inui, M et al. (2011) USP15 is a deubiquitylating enzyme for receptor-activated SMADs. Nat. Cell Biol. 13 1368-75 PubMed GONUTS page

[PMID:21307346-11] 11.0 ^11.1 ^11.2 Guo, X et al. (2011) Response gene to complement 32 interacts with Smad3 to promote epithelial-mesenchymal transition of human renal tubular cells. Am. J. Physiol., Cell Physiol. 300 C1415-21 PubMed GONUTS page

[PMID:20129061-12] Watanabe, Y et al. (2010) TMEPAI, a transmembrane TGF-beta-inducible protein, sequesters Smad proteins from active participation in TGF-beta signaling. Mol. Cell 37 123-34 PubMed GONUTS page

[PMID:15799969-13] 13.0 ^13.1 ^13.2 Chen, HB et al. (2005) Nuclear targeting of transforming growth factor-beta-activated Smad complexes. J. Biol. Chem. 280 21329-36 PubMed GONUTS page

[PMID:15334054-14] 14.0 ^14.1 Cheng, PL et al. (2004) Hepatitis C viral proteins interact with Smad3 and differentially regulate TGF-beta/Smad3-mediated transcriptional activation. Oncogene 23 7821-38 PubMed GONUTS page

[PMID:21828274-15] 15.0 ^15.1 ^15.2 ^15.3 ^15.4 Yoon, SJ et al. (2011) HEB and E2A function as SMAD/FOXH1 cofactors. Genes Dev. 25 1654-61 PubMed GONUTS page

[PMID:9311995-16] 16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 Nakao, A et al. (1997) TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4. EMBO J. 16 5353-62 PubMed GONUTS page

[PMID:9732876-17] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 ^17.6 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:9111321-18] 18.0 ^18.1 ^18.2 ^18.3 ^18.4 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:8774881-19] 19.0 ^19.1 ^19.2 ^19.3 ^19.4 ^19.5 ^19.6 Zhang, Y et al. (1996) Receptor-associated Mad homologues synergize as effectors of the TGF-beta response. Nature 383 168-72 PubMed GONUTS page

[PMID:14555988-20] 20.0 ^20.1 ^20.2 ^20.3 Kretschmer, A et al. (2003) Differential regulation of TGF-beta signaling through Smad2, Smad3 and Smad4. Oncogene 22 6748-63 PubMed GONUTS page

[PMID:18505915-21] 21.0 ^21.1 Do, TV et al. (2008) Transforming growth factor-beta1, transforming growth factor-beta2, and transforming growth factor-beta3 enhance ovarian cancer metastatic potential by inducing a Smad3-dependent epithelial-to-mesenchymal transition. Mol. Cancer Res. 6 695-705 PubMed GONUTS page

[PMID:10823886-22] 22.0 ^22.1 ^22.2 Denissova, NG et al. (2000) Transforming growth factor beta -inducible independent binding of SMAD to the Smad7 promoter. Proc. Natl. Acad. Sci. U.S.A. 97 6397-402 PubMed GONUTS page

[PMID:15150278-23] 23.0 ^23.1 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:12411310-24] 24.0 ^24.1 Zhang, H et al. (2003) Cellular response to hypoxia involves signaling via Smad proteins. Blood 101 2253-60 PubMed GONUTS page

[PMID:11278251-25] Ebisawa, T et al. (2001) Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation. J. Biol. Chem. 276 12477-80 PubMed GONUTS page

[PMID:19122240-26] 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:16886151-27] Adewoye, AH et al. (2006) Association of polymorphisms of IGF1R and genes in the transforming growth factor- beta /bone morphogenetic protein pathway with bacteremia in sickle cell anemia. Clin. Infect. Dis. 43 593-8 PubMed GONUTS page

[PMID:15107418-28] Kim, BC et al. (2004) Activin receptor-like kinase-7 induces apoptosis through activation of MAPKs in a Smad3-dependent mechanism in hepatoma cells. J. Biol. Chem. 279 28458-65 PubMed GONUTS page

[PMID:12446380-29] 29.0 ^29.1 Saika, S et al. (2002) TGFbeta-Smad signalling in postoperative human lens epithelial cells. Br J Ophthalmol 86 1428-33 PubMed GONUTS page

[PMID:17251190-30] Grocott, T et al. (2007) The MH1 domain of Smad3 interacts with Pax6 and represses autoregulation of the Pax6 P1 promoter. Nucleic Acids Res. 35 890-901 PubMed GONUTS page

[PMID:18832382-31] 31.0 ^31.1 ^31.2 ^31.3 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:18794808-32] Guo, X et al. (2008) Ligand-dependent ubiquitination of Smad3 is regulated by casein kinase 1 gamma 2, an inhibitor of TGF-beta signaling. Oncogene 27 7235-47 PubMed GONUTS page

[PMID:16751101-33] Lin, X et al. (2006) PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling. Cell 125 915-28 PubMed GONUTS page

[PMID:12874272-34] Harada, J et al. (2003) Requirement of the co-repressor homeodomain-interacting protein kinase 2 for ski-mediated inhibition of bone morphogenetic protein-induced transcriptional activation. J. Biol. Chem. 278 38998-9005 PubMed GONUTS page

[PMID:12686552-35] Chai, J et al. (2003) Features of a Smad3 MH1-DNA complex. Roles of water and zinc in DNA binding. J. Biol. Chem. 278 20327-31 PubMed GONUTS page

[PMID:15647271-36] Pan, D et al. (2005) The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines. J. Biol. Chem. 280 15992-6001 PubMed GONUTS page

[PMID:22045334-37] Tang, LY et al. (2011) Ablation of Smurf2 reveals an inhibition in TGF-β signalling through multiple mono-ubiquitination of Smad3. EMBO J. 30 4777-89 PubMed GONUTS page

[PMID:18729074-38] Brown, KA et al. (2008) Identification of novel Smad2 and Smad3 associated proteins in response to TGF-beta1. J. Cell. Biochem. 105 596-611 PubMed GONUTS page

[PMID:19018011-39] 39.0 ^39.1 Hoover, LL & Kubalak, SW (2008) Holding their own: the noncanonical roles of Smad proteins. Sci Signal 1 pe48 PubMed GONUTS page

[PMID:20097766-40] Zhang, M et al. (2010) Smad3 prevents beta-catenin degradation and facilitates beta-catenin nuclear translocation in chondrocytes. J. Biol. Chem. 285 8703-10 PubMed GONUTS page

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