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UniProtKB - Q13485 (SMAD4_HUMAN)

Entry version 223 (16 Oct 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Mothers against decapentaplegic homolog 4

Gene

SMAD4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (By similarity). Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling (PubMed:25514493). Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi71ZincBy similarity1
Metal bindingi115ZincBy similarity1
Metal bindingi127ZincBy similarity1
Metal bindingi132ZincBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei515Necessary for heterotrimerization1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1181150 Signaling by NODAL
R-HSA-1502540 Signaling by Activin
R-HSA-201451 Signaling by BMP
R-HSA-2173789 TGF-beta receptor signaling activates SMADs
R-HSA-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-3311021 SMAD4 MH2 Domain Mutants in Cancer
R-HSA-3315487 SMAD2/3 MH2 Domain Mutants in Cancer
R-HSA-452723 Transcriptional regulation of pluripotent stem cells
R-HSA-5689880 Ub-specific processing proteases
R-HSA-8941326 RUNX2 regulates bone development
R-HSA-8941855 RUNX3 regulates CDKN1A transcription
R-HSA-8952158 RUNX3 regulates BCL2L11 (BIM) transcription
R-HSA-9615017 FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes
R-HSA-9617828 FOXO-mediated transcription of cell cycle genes

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q13485

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q13485

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Mothers against decapentaplegic homolog 4
Short name:
MAD homolog 4
Short name:
Mothers against DPP homolog 4
Alternative name(s):
Deletion target in pancreatic carcinoma 4
SMAD family member 4
Short name:
SMAD 4
Short name:
Smad4
Short name:
hSMAD4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SMAD4
Synonyms:DPC4, MADH4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 18

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:6770 SMAD4

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600993 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q13485

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Pancreatic cancer (PNCA)1 Publication
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA malignant neoplasm of the pancreas. Tumors can arise from both the exocrine and endocrine portions of the pancreas, but 95% of them develop from the exocrine portion, including the ductal epithelium, acinar cells, connective tissue, and lymphatic tissue.
Related information in OMIM
Juvenile polyposis syndrome (JPS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant gastrointestinal hamartomatous polyposis syndrome in which patients are at risk for developing gastrointestinal cancers. The lesions are typified by a smooth histological appearance, predominant stroma, cystic spaces and lack of a smooth muscle core. Multiple juvenile polyps usually occur in a number of Mendelian disorders. Sometimes, these polyps occur without associated features as in JPS; here, polyps tend to occur in the large bowel and are associated with an increased risk of colon and other gastrointestinal cancers.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022833330E → G in JPS. 1 PublicationCorresponds to variant dbSNP:rs281875324EnsemblClinVar.1
Natural variantiVAR_019571352G → R in JP/HHT and JPS. 2 PublicationsCorresponds to variant dbSNP:rs121912581EnsemblClinVar.1
Natural variantiVAR_019572361R → C in JPS. 1 PublicationCorresponds to variant dbSNP:rs80338963EnsemblClinVar.1
Juvenile polyposis/hereditary hemorrhagic telangiectasia syndrome (JP/HHT)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionJP/HHT syndrome phenotype consists of the coexistence of juvenile polyposis (JIP) and hereditary hemorrhagic telangiectasia (HHT) [MIM:187300] in a single individual. JIP and HHT are autosomal dominant disorders with distinct and non-overlapping clinical features. The former, an inherited gastrointestinal malignancy predisposition, is caused by mutations in SMAD4 or BMPR1A, and the latter is a vascular malformation disorder caused by mutations in ENG or ACVRL1. All four genes encode proteins involved in the transforming-growth-factor-signaling pathway. Although there are reports of patients and families with phenotypes of both disorders combined, the genetic etiology of this association is unknown.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_019571352G → R in JP/HHT and JPS. 2 PublicationsCorresponds to variant dbSNP:rs121912581EnsemblClinVar.1
Natural variantiVAR_019573386G → D in JP/HHT. 1 PublicationCorresponds to variant dbSNP:rs121912580EnsemblClinVar.1
Colorectal cancer (CRC)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionA complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
Related information in OMIM
SMAD4 variants may be associated with susceptibility to pulmonary hypertension, a disorder characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure, and death. The disease can occur from infancy throughout life and it has a mean age at onset of 36 years. Penetrance is reduced. Although familial pulmonary hypertension is rare, cases secondary to known etiologies are more common and include those associated with the appetite-suppressant drugs.1 Publication
Myhre syndrome (MYHRS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by pre- and postnatal growth deficiency, mental retardation, generalized muscle hypertrophy and striking muscular build, decreased joint mobility, cryptorchidism, and unusual facies. Dysmorphic facial features include microcephaly, midface hypoplasia, prognathism, and blepharophimosis. Typical skeletal anomalies are short stature, square body shape, broad ribs, iliac hypoplasia, brachydactyly, flattened vertebrae, and thickened calvaria. Other features, such as congenital heart disease, may also occur.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_067602500I → M in MYHRS. 1 PublicationCorresponds to variant dbSNP:rs281875320EnsemblClinVar.1
Natural variantiVAR_067603500I → T in MYHRS; there is an enhanced levels of SMAD4 protein with lower levels of ubiquitinated SMAD4 fibroblasts compared to controls suggesting stabilization of the mutant protein; 8-fold increase in phosphorylated SMAD2 and SMAD3; 11-fold increase in phosphorylated SMAD1, SMAD5 and SMAD8 in cell nuclei compared to controls. 2 PublicationsCorresponds to variant dbSNP:rs281875321EnsemblClinVar.1
Natural variantiVAR_067604500I → V in MYHRS. 2 PublicationsCorresponds to variant dbSNP:rs281875322EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi416R → S: No effect on heterotrimerization. Partially diminished transcriptional activation. 1 Publication1
Mutagenesisi496R → S: No effect on heterotrimerization. Partially diminished transcriptional activation. 1
Mutagenesisi502R → S: No effect on heterotrimerization. Greatly reduced transcriptional activation. 1 Publication1
Mutagenesisi515R → S: Reduced heterotrimerization. 1 Publication1
Mutagenesisi519K → R: Abolishes ubiquitination. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		4089

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		SMAD4

MalaCards human disease database

More...MalaCardsi		SMAD4
MIMi114500 phenotype
139210 phenotype
174900 phenotype
175050 phenotype
260350 phenotype

Open Targets

More...OpenTargetsi		ENSG00000141646

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		1333 Familial pancreatic carcinoma
329971 Generalized juvenile polyposis/juvenile polyposis coli
774 Hereditary hemorrhagic telangiectasia
2588 Myhre syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30527

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q13485

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		SMAD4

Domain mapping of disease mutations (DMDM)

More...DMDMi		13959561

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000908611 – 552Mothers against decapentaplegic homolog 4Add BLAST552

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei37N6-acetyllysineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei428N6-acetyllysineCombined sources1
Modified residuei507N6-acetyllysineCombined sources1
Cross-linki519Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by PDPK1.1 Publication
Monoubiquitinated on Lys-519 by E3 ubiquitin-protein ligase TRIM33. Monoubiquitination hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade. Deubiquitination by USP9X restores its competence to mediate TGF-beta signaling.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-1268
CPTAC-1269

Encyclopedia of Proteome Dynamics

More...EPDi		Q13485

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q13485

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q13485

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q13485

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q13485

PeptideAtlas

More...PeptideAtlasi		Q13485

PRoteomics IDEntifications database

More...PRIDEi		Q13485

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		59479

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q13485

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q13485

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q13485

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000141646 Expressed in 224 organ(s), highest expression level in kidney

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q13485 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q13485 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA019154

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Found in a complex with SMAD1 and YY1 (By similarity).

Interacts with CITED2 (By similarity). Monomer; in the absence of TGF-beta activation. Heterodimer; on TGF-beta activation. Composed of two molecules of a C-terminally phosphorylated R-SMAD molecule, SMAD2 or SMAD3, and one molecule of SMAD4 to form the transcriptional active SMAD2/SMAD3-SMAD4 complex.

Found in a ternary complex composed of SMAD4, STK11/LKB1 and STK11IP.

Interacts with ATF2, COPS5, DACH1, MSG1, SKI, STK11/LKB1, STK11IP and TRIM33.

Interacts with ZNF423; the interaction takes place in response to BMP2 leading to activation of transcription of BMP target genes.

Interacts with ZNF521; the interaction takes place in response to BMP2 leading to activation of transcription of BMP target genes.

Interacts with USP9X.

Interacts (via the MH1 and MH2 domains) with RBPMS.

Interacts with WWTR1 (via coiled-coil domain).

Component of the multimeric complex SMAD3/SMAD4/JUN/FOS which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta.

Interacts with CITED1.

Interacts with PDPK1 (via PH domain) (By similarity).

Interacts with VPS39; this interaction affects heterodimer formation with SMAD3, but not with SMAD2, and leads to inhibition of SMAD3-dependent transcription activation. Interactions with VPS39 and SMAD2 may be mutually exclusive.

Interacts with ZC3H3 (By similarity).

Interacts (via MH2 domain) with ZNF451 (via N-terminal zinc-finger domains) (PubMed:24324267).

Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and SMAD4 (PubMed:24324267).

Interacts weakly with ZNF8 (PubMed:12370310).

Interacts with NUP93 and IPO7; translocates SMAD4 to the nucleus through the NPC upon BMP7 stimulation resulting in activation of SMAD4 signaling (PubMed:26878725).

Interacts with CREB3L1, the interaction takes place upon TGFB1 induction and SMAD4 acts as CREB3L1 coactivator to induce the expression of genes involved in the assembly of collagen extracellular matrix (PubMed:25310401).

Interacts with DLX1 (PubMed:14671321).

Interacts with ZBTB7A; the interaction is direct and stimulated by TGFB1 (PubMed:25514493).

Interacts with CREBBP; the recruitment of this transcriptional coactivator is negatively regulated by ZBTB7A (PubMed:25514493).

Interacts with EP300; the interaction with this transcriptional coactivator is negatively regulated by ZBTB7A (PubMed:25514493).

Interacts with HDAC1 (PubMed:25514493).

By similarity22 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		110264, 230 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1 SMAD2-SMAD3-SMAD4 complex
CPX-3208 SMAD2-SMAD4 complex
CPX-3252 SMAD3-SMAD4 complex
CPX-54 SMAD1-SMAD4 complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q13485

Database of interacting proteins

More...DIPi		DIP-31512N

Protein interaction database and analysis system

More...IntActi		Q13485, 123 interactors

Molecular INTeraction database

More...MINTi		Q13485

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000341551

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q13485

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q13485

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini18 – 142MH1PROSITE-ProRule annotationAdd BLAST125
Domaini323 – 552MH2PROSITE-ProRule annotationAdd BLAST230

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 322Mediates interaction with ZBTB7A1 PublicationAdd BLAST322
Regioni275 – 320SADAdd BLAST46

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi451 – 466Poly-AlaAdd BLAST16

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the dwarfin/SMAD family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3701 Eukaryota
ENOG410XQKU LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157435

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000286019

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q13485

KEGG Orthology (KO)

More...KOi		K04501

Identification of Orthologs from Complete Genome Data

More...OMAi		PQMGPGT

Database of Orthologous Groups

More...OrthoDBi		905048at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q13485

TreeFam database of animal gene trees

More...TreeFami		TF314923

Family and domain databases

Database of protein disorder

More...DisProti		DP00464

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.200.10, 1 hit
3.90.520.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013790 Dwarfin
IPR003619 MAD_homology1_Dwarfin-type
IPR013019 MAD_homology_MH1
IPR017855 SMAD-like_dom_sf
IPR001132 SMAD_dom_Dwarfin-type
IPR008984 SMAD_FHA_dom_sf
IPR036578 SMAD_MH1_sf

The PANTHER Classification System

More...PANTHERi		PTHR13703 PTHR13703, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03165 MH1, 1 hit
PF03166 MH2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00523 DWA, 1 hit
SM00524 DWB, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49879 SSF49879, 1 hit
SSF56366 SSF56366, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51075 MH1, 1 hit
PS51076 MH2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 9 potential isoforms that are computationally mapped.Show allAlign All

Q13485-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDNMSITNTP TSNDACLSIV HSLMCHRQGG ESETFAKRAI ESLVKKLKEK 
        60         70         80         90        100
KDELDSLITA ITTNGAHPSK CVTIQRTLDG RLQVAGRKGF PHVIYARLWR 
       110        120        130        140        150
WPDLHKNELK HVKYCQYAFD LKCDSVCVNP YHYERVVSPG IDLSGLTLQS 
       160        170        180        190        200
NAPSSMMVKD EYVHDFEGQP SLSTEGHSIQ TIQHPPSNRA STETYSTPAL 
       210        220        230        240        250
LAPSESNATS TANFPNIPVA STSQPASILG GSHSEGLLQI ASGPQPGQQQ 
       260        270        280        290        300
NGFTGQPATY HHNSTTTWTG SRTAPYTPNL PHHQNGHLQH HPPMPPHPGH 
       310        320        330        340        350
YWPVHNELAF QPPISNHPAP EYWCSIAYFE MDVQVGETFK VPSSCPIVTV 
       360        370        380        390        400
DGYVDPSGGD RFCLGQLSNV HRTEAIERAR LHIGKGVQLE CKGEGDVWVR 
       410        420        430        440        450
CLSDHAVFVQ SYYLDREAGR APGDAVHKIY PSAYIKVFDL RQCHRQMQQQ 
       460        470        480        490        500
AATAQAAAAA QAAAVAGNIP GPGSVGGIAP AISLSAAAGI GVDDLRRLCI 
       510        520        530        540        550
LRMSFVKGWG PDYPRQSIKE TPCWIEIHLH RALQLLDEVL HTMPIADPQP 

LD
Length:552
Mass (Da):60,439
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7EE3C4647712DA90
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EIU8K7EIU8_HUMAN
Mothers against decapentaplegic hom...
SMAD4
456Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ES96K7ES96_HUMAN
Mothers against decapentaplegic hom...
SMAD4
320Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EIJ2K7EIJ2_HUMAN
Mothers against decapentaplegic hom...
SMAD4
140Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EL15K7EL15_HUMAN
Mothers against decapentaplegic hom...
SMAD4
120Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EL18K7EL18_HUMAN
Mothers against decapentaplegic hom...
SMAD4
126Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ENG8K7ENG8_HUMAN
Mothers against decapentaplegic hom...
SMAD4
151Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ENG1K7ENG1_HUMAN
Mothers against decapentaplegic hom...
SMAD4
90Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WUF3A0A087WUF3_HUMAN
Mothers against decapentaplegic hom...
SMAD4
220Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ELK2K7ELK2_HUMAN
Mothers against decapentaplegic hom...
SMAD4
82Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06687013N → S Rare variant; found in a patient with pulmonary hypertension; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs281875323EnsemblClinVar.1
Natural variantiVAR_036475130P → S in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1555685186EnsemblClinVar.1
Natural variantiVAR_022833330E → G in JPS. 1 PublicationCorresponds to variant dbSNP:rs281875324EnsemblClinVar.1
Natural variantiVAR_036476351D → N in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1057519739EnsemblClinVar.1
Natural variantiVAR_019571352G → R in JP/HHT and JPS. 2 PublicationsCorresponds to variant dbSNP:rs121912581EnsemblClinVar.1
Natural variantiVAR_019572361R → C in JPS. 1 PublicationCorresponds to variant dbSNP:rs80338963EnsemblClinVar.1
Natural variantiVAR_036477361R → H in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs377767347EnsemblClinVar.1
Natural variantiVAR_019573386G → D in JP/HHT. 1 PublicationCorresponds to variant dbSNP:rs121912580EnsemblClinVar.1
Natural variantiVAR_011380493D → H in pancreatic carcinoma. 1 PublicationCorresponds to variant dbSNP:rs121912578EnsemblClinVar.1
Natural variantiVAR_067602500I → M in MYHRS. 1 PublicationCorresponds to variant dbSNP:rs281875320EnsemblClinVar.1
Natural variantiVAR_067603500I → T in MYHRS; there is an enhanced levels of SMAD4 protein with lower levels of ubiquitinated SMAD4 fibroblasts compared to controls suggesting stabilization of the mutant protein; 8-fold increase in phosphorylated SMAD2 and SMAD3; 11-fold increase in phosphorylated SMAD1, SMAD5 and SMAD8 in cell nuclei compared to controls. 2 PublicationsCorresponds to variant dbSNP:rs281875321EnsemblClinVar.1
Natural variantiVAR_067604500I → V in MYHRS. 2 PublicationsCorresponds to variant dbSNP:rs281875322EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF045447
, AF045438, AF045439, AF045440, AF045441, AF045442, AF045443, AF045444, AF045445, AF045446 Genomic DNA Translation: AAC03051.1
U44378 mRNA Translation: AAA91041.1
AK290770 mRNA Translation: BAF83459.1
CH471096 Genomic DNA Translation: EAW62985.1
BC002379 mRNA Translation: AAH02379.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS11950.1

Protein sequence database of the Protein Information Resource

More...PIRi		S71811

NCBI Reference Sequences

More...RefSeqi		NP_005350.1, NM_005359.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000342988; ENSP00000341551; ENSG00000141646
ENST00000398417; ENSP00000381452; ENSG00000141646

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4089

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4089

UCSC genome browser

More...UCSCi		uc010xdp.3 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Mendelian genes SMAD family member 4 (SMAD4)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF045447
, AF045438, AF045439, AF045440, AF045441, AF045442, AF045443, AF045444, AF045445, AF045446 Genomic DNA Translation: AAC03051.1
U44378 mRNA Translation: AAA91041.1
AK290770 mRNA Translation: BAF83459.1
CH471096 Genomic DNA Translation: EAW62985.1
BC002379 mRNA Translation: AAH02379.1
CCDSiCCDS11950.1
PIRiS71811
RefSeqiNP_005350.1, NM_005359.5

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DD1X-ray2.62A/B/C285-552[»]
1G88X-ray3.00A/B/C285-552[»]
1MR1X-ray2.85A/B319-552[»]
1U7FX-ray2.60B314-552[»]
1U7VX-ray2.70B314-549[»]
1YGSX-ray2.10A319-552[»]
5C4VX-ray2.60A/C/E314-549[»]
5MEYX-ray2.05A10-140[»]
5MEZX-ray2.98A/B10-140[»]
5MF0X-ray3.03A/B10-140[»]
5UWUX-ray2.24D133-149[»]
SMRiQ13485
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi110264, 230 interactors
ComplexPortaliCPX-1 SMAD2-SMAD3-SMAD4 complex
CPX-3208 SMAD2-SMAD4 complex
CPX-3252 SMAD3-SMAD4 complex
CPX-54 SMAD1-SMAD4 complex
CORUMiQ13485
DIPiDIP-31512N
IntActiQ13485, 123 interactors
MINTiQ13485
STRINGi9606.ENSP00000341551

PTM databases

iPTMnetiQ13485
PhosphoSitePlusiQ13485
SwissPalmiQ13485

Polymorphism and mutation databases

BioMutaiSMAD4
DMDMi13959561

Proteomic databases

CPTACiCPTAC-1268
CPTAC-1269
EPDiQ13485
jPOSTiQ13485
MassIVEiQ13485
MaxQBiQ13485
PaxDbiQ13485
PeptideAtlasiQ13485
PRIDEiQ13485
ProteomicsDBi59479

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		4089

Genome annotation databases

EnsembliENST00000342988; ENSP00000341551; ENSG00000141646
ENST00000398417; ENSP00000381452; ENSG00000141646
GeneIDi4089
KEGGihsa:4089
UCSCiuc010xdp.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4089
DisGeNETi4089

GeneCards: human genes, protein and diseases

More...GeneCardsi		SMAD4
GeneReviewsiSMAD4
HGNCiHGNC:6770 SMAD4
HPAiHPA019154
MalaCardsiSMAD4
MIMi114500 phenotype
139210 phenotype
174900 phenotype
175050 phenotype
260350 phenotype
600993 gene
neXtProtiNX_Q13485
OpenTargetsiENSG00000141646
Orphaneti1333 Familial pancreatic carcinoma
329971 Generalized juvenile polyposis/juvenile polyposis coli
774 Hereditary hemorrhagic telangiectasia
2588 Myhre syndrome
PharmGKBiPA30527

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3701 Eukaryota
ENOG410XQKU LUCA
GeneTreeiENSGT00940000157435
HOGENOMiHOG000286019
InParanoidiQ13485
KOiK04501
OMAiPQMGPGT
OrthoDBi905048at2759
PhylomeDBiQ13485
TreeFamiTF314923

Enzyme and pathway databases

ReactomeiR-HSA-1181150 Signaling by NODAL
R-HSA-1502540 Signaling by Activin
R-HSA-201451 Signaling by BMP
R-HSA-2173789 TGF-beta receptor signaling activates SMADs
R-HSA-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-3311021 SMAD4 MH2 Domain Mutants in Cancer
R-HSA-3315487 SMAD2/3 MH2 Domain Mutants in Cancer
R-HSA-452723 Transcriptional regulation of pluripotent stem cells
R-HSA-5689880 Ub-specific processing proteases
R-HSA-8941326 RUNX2 regulates bone development
R-HSA-8941855 RUNX3 regulates CDKN1A transcription
R-HSA-8952158 RUNX3 regulates BCL2L11 (BIM) transcription
R-HSA-9615017 FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes
R-HSA-9617828 FOXO-mediated transcription of cell cycle genes
SignaLinkiQ13485
SIGNORiQ13485

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		SMAD4 human
EvolutionaryTraceiQ13485

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Mothers_against_decapentaplegic_homolog_4

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		4089
PharosiQ13485

Protein Ontology

More...PROi		PR:Q13485

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000141646 Expressed in 224 organ(s), highest expression level in kidney
ExpressionAtlasiQ13485 baseline and differential
GenevisibleiQ13485 HS

Family and domain databases

DisProtiDP00464
Gene3Di2.60.200.10, 1 hit
3.90.520.10, 1 hit
InterProiView protein in InterPro
IPR013790 Dwarfin
IPR003619 MAD_homology1_Dwarfin-type
IPR013019 MAD_homology_MH1
IPR017855 SMAD-like_dom_sf
IPR001132 SMAD_dom_Dwarfin-type
IPR008984 SMAD_FHA_dom_sf
IPR036578 SMAD_MH1_sf
PANTHERiPTHR13703 PTHR13703, 1 hit
PfamiView protein in Pfam
PF03165 MH1, 1 hit
PF03166 MH2, 1 hit
SMARTiView protein in SMART
SM00523 DWA, 1 hit
SM00524 DWB, 1 hit
SUPFAMiSSF49879 SSF49879, 1 hit
SSF56366 SSF56366, 1 hit
PROSITEiView protein in PROSITE
PS51075 MH1, 1 hit
PS51076 MH2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSMAD4_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q13485
Secondary accession number(s): A8K405
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: November 1, 1996
Last modified: October 16, 2019
This is version 223 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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