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Entry version 220 (31 Jul 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Mothers against decapentaplegic homolog 2

Gene

SMAD2

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

Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.5 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 bindingi74ZincBy similarity1
Metal bindingi149ZincBy similarity1
Metal bindingi161ZincBy similarity1
Metal bindingi166ZincBy similarity1

<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

GO - Biological processi

<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

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Reactomei
R-HSA-1181150 Signaling by NODAL
R-HSA-1502540 Signaling by Activin
R-HSA-2173788 Downregulation of TGF-beta receptor signaling
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-3304356 SMAD2/3 Phosphorylation Motif Mutants in Cancer
R-HSA-3311021 SMAD4 MH2 Domain Mutants in Cancer
R-HSA-3315487 SMAD2/3 MH2 Domain Mutants in Cancer
R-HSA-3656532 TGFBR1 KD Mutants in Cancer
R-HSA-452723 Transcriptional regulation of pluripotent stem cells
R-HSA-5689880 Ub-specific processing proteases
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

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SignaLinki
Q15796

SIGNOR Signaling Network Open Resource

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SIGNORi
Q15796

<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 2
Short name:
MAD homolog 2
Short name:
Mothers against DPP homolog 2
Alternative name(s):
JV18-1
Mad-related protein 2
Short name:
hMAD-2
SMAD family member 2
Short name:
SMAD 2
Short name:
Smad2
Short name:
hSMAD2
<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:SMAD2
Synonyms:MADH2, MADR2
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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

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HGNCi
HGNC:6768 SMAD2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601366 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q15796

<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

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>Mutagenesisi19K → R: Loss of acetylation. 1 Publication1
Mutagenesisi20K → R: No effect on acetylation. 1 Publication1
Mutagenesisi221 – 225Missing : Loss of binding to SMURF2. 1 Publication5
Mutagenesisi368W → A: Loss of interaction with PMEPA1. 1 Publication1
Mutagenesisi381N → S: Loss of binding to SARA. 1 Publication1
Mutagenesisi398V → R: Increased binding to PPM1A. 1 Publication1
Mutagenesisi464S → A: Loss of phosphorylation by TGFBR1; when associated with A-465 and A-467. 1 Publication1
Mutagenesisi465 – 467SMS → AMA: Binds RANBP3. 1 Publication3
Mutagenesisi465 – 467SMS → DMD: Greatly reduced RANBP2 binding. 1 Publication3
Mutagenesisi465S → A: No change in binding to PPM1A. Loss of phosphorylation by TGFBR1; when associated with A-464 and A-467. 2 Publications1
Mutagenesisi465S → D: No change in binding to PPM1A. 2 Publications1
Mutagenesisi467S → A: No change in binding to PPM1A. Loss of phosphorylation by TGFBR1; when associated with A-464 and A-465. 2 Publications1
Mutagenesisi467S → D: No change in binding to PPM1A. 2 Publications1

Organism-specific databases

DisGeNET

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DisGeNETi
4087

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

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GeneReviewsi
SMAD2

Open Targets

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OpenTargetsi
ENSG00000175387

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134959722

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2396512

Drug and drug target database

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DrugBanki
DB04522 Phosphonoserine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
SMAD2

Domain mapping of disease mutations (DMDM)

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DMDMi
13633914

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<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_00000908522 – 467Mothers against decapentaplegic homolog 2Add BLAST466

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 residuei2N-acetylserineCombined sources1 Publication1
Modified residuei8Phosphothreonine; by MAPK3Combined sources1 Publication1
Modified residuei19N6-acetyllysine1 Publication1
Modified residuei220Phosphothreonine1 Publication1
Modified residuei240Phosphoserine; by CAMK2PROSITE-ProRule annotation1 Publication1
Modified residuei245Phosphoserine1 Publication1
Modified residuei250Phosphoserine1 Publication1
Modified residuei255Phosphoserine1 Publication1
Modified residuei458PhosphoserineCombined sources1
Modified residuei460PhosphoserineCombined sources1
Modified residuei464PhosphoserinePROSITE-ProRule annotation1 Publication1
Modified residuei465Phosphoserine; by TGFBR1PROSITE-ProRule annotation4 Publications1
Modified residuei467Phosphoserine; by TGFBR1PROSITE-ProRule annotation4 Publications1

<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 on one or several of Thr-220, Ser-245, Ser-250, and Ser-255. In response to TGF-beta, phosphorylated on Ser-465/467 by TGF-beta and activin type 1 receptor kinases. TGF-beta-induced Ser-465/467 phosphorylation declines progressively in a KMT5A-dependent manner. Able to interact with SMURF2 when phosphorylated on Ser-465/467, recruiting other proteins, such as SNON, for degradation. In response to decorin, the naturally occurring inhibitor of TGF-beta signaling, phosphorylated on Ser-240 by CaMK2. Phosphorylated by MAPK3 upon EGF stimulation; which increases transcriptional activity and stability, and is blocked by calmodulin. Phosphorylated by PDPK1.8 Publications
In response to TGF-beta, ubiquitinated by NEDD4L; which promotes its degradation. Monoubiquitinated, leading to prevent DNA-binding (By similarity). Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes (PubMed:21947082). Ubiquitinated by RNF111, leading to its degradation: only SMAD2 proteins that are 'in use' are targeted by RNF111, RNF111 playing a key role in activating SMAD2 and regulating its turnover (By similarity).By similarity1 Publication
Acetylated on Lys-19 by coactivators in response to TGF-beta signaling, which increases transcriptional activity. Isoform short: Acetylation increases DNA binding activity in vitro and enhances its association with target promoters in vivo. Acetylation in the nucleus by EP300 is enhanced by TGF-beta.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q15796

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q15796

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

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PaxDbi
Q15796

PeptideAtlas

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PeptideAtlasi
Q15796

PRoteomics IDEntifications database

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PRIDEi
Q15796

ProteomicsDB human proteome resource

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ProteomicsDBi
60764 [Q15796-1]
60765 [Q15796-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q15796

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

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PhosphoSitePlusi
Q15796

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed at high levels in skeletal muscle, endothelial cells, heart and placenta.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000175387 Expressed in 233 organ(s), highest expression level in kidney

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q15796 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q15796 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB025507
CAB073546
HPA067203

<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

Monomer; the absence of TGF-beta. Heterodimer; in the presence of TGF-beta.

Forms a heterodimer with co-SMAD, SMAD4, in the nucleus to form the transactivation complex SMAD2/SMAD4.

Interacts with AIP1, HGS, PML and WWP1 (By similarity).

Interacts with NEDD4L in response to TGF-beta (By similarity).

Found in a complex with SMAD3 and TRIM33 upon addition of TGF-beta.

Interacts with ACVR1B, SMAD3 and TRIM33.

Interacts (via the MH2 domain) with ZFYVE9; may form trimers with the SMAD4 co-SMAD.

Interacts with FOXH1, homeobox protein TGIF, PEBP2-alpha subunit, CREB-binding protein (CBP), EP300, SKI and SNW1.

Interacts with SNON; when phosphorylated at Ser-465/467.

Interacts with SKOR1 and SKOR2.

Interacts with PRDM16.

Interacts (via MH2 domain) with LEMD3.

Interacts with RBPMS.

Interacts with WWP1.

Interacts (dephosphorylated form, via the MH1 and MH2 domains) with RANBP3 (via its C-terminal R domain); the interaction results in the export of dephosphorylated SMAD3 out of the nucleus and termination of the TGF-beta signaling.

Interacts with PDPK1 (via PH domain).

Interacts with DAB2; the interactions are enhanced upon TGF-beta stimulation.

Interacts with USP15.

Interacts with PPP5C.

Interacts with ZNF580.

Interacts with LDLRAD4 (via the SMAD interaction motif).

Interacts (via MH2 domain) with PMEPA1 (via the SMAD interaction motif).

Interacts with ZFHX3.

Interacts with ZNF451 (PubMed:24324267).

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

Interacts weakly with ZNF8 (By similarity).

Interacts (when phosphorylated) with RNF111; RNF111 acts as an enhancer of the transcriptional responses by mediating ubiquitination and degradation of SMAD2 inhibitors (By similarity).

By similarity28 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110262, 274 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1 SMAD2-SMAD3-SMAD4 complex
CPX-11 SMAD2 homotrimer
CPX-3208 SMAD2-SMAD4 complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q15796

Database of interacting proteins

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DIPi
DIP-29716N

Protein interaction database and analysis system

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IntActi
Q15796, 225 interactors

Molecular INTeraction database

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MINTi
Q15796

STRING: functional protein association networks

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STRINGi
9606.ENSP00000262160

<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

1467
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

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SMRi
Q15796

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q15796

<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>Domaini10 – 176MH1PROSITE-ProRule annotationAdd BLAST167
Domaini274 – 467MH2PROSITE-ProRule annotationAdd BLAST194

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi221 – 225PY-motif5

<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

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eggNOGi
KOG3701 Eukaryota
ENOG410XQKU LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153499

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000286018

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q15796

KEGG Orthology (KO)

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KOi
K04500

Identification of Orthologs from Complete Genome Data

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OMAi
DEICINP

Database of Orthologous Groups

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OrthoDBi
608001at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q15796

TreeFam database of animal gene trees

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TreeFami
TF314923

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.200.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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PANTHERi
PTHR13703 PTHR13703, 1 hit

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49879 SSF49879, 1 hit
SSF56366 SSF56366, 1 hit

PROSITE; a protein domain and family database

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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>Sequences (2+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform Long (identifier: Q15796-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK
60 70 80 90 100
KLKKTGRLDE LEKAITTQNC NTKCVTIPST CSEIWGLSTP NTIDQWDTTG
110 120 130 140 150
LYSFSEQTRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELKAIENCE
160 170 180 190 200
YAFNLKKDEV CVNPYHYQRV ETPVLPPVLV PRHTEILTEL PPLDDYTHSI
210 220 230 240 250
PENTNFPAGI EPQSNYIPET PPPGYISEDG ETSDQQLNQS MDTGSPAELS
260 270 280 290 300
PTTLSPVNHS LDLQPVTYSE PAFWCSIAYY ELNQRVGETF HASQPSLTVD
310 320 330 340 350
GFTDPSNSER FCLGLLSNVN RNATVEMTRR HIGRGVRLYY IGGEVFAECL
360 370 380 390 400
SDSAIFVQSP NCNQRYGWHP ATVCKIPPGC NLKIFNNQEF AALLAQSVNQ
410 420 430 440 450
GFEAVYQLTR MCTIRMSFVK GWGAEYRRQT VTSTPCWIEL HLNGPLQWLD
460
KVLTQMGSPS VRCSSMS
Length:467
Mass (Da):52,306
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:i95406DB5FC0AA4C9
GO
Isoform Short (identifier: Q15796-2) [UniParc]FASTAAdd to basket
Also known as: Smad2Deltaexon3

The sequence of this isoform differs from the canonical sequence as follows:
     79-108: Missing.

Show »
Length:437
Mass (Da):48,956
Checksum:i0E2FF38B009D2F9E
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B7Z5N5B7Z5N5_HUMAN
Mothers against decapentaplegic hom...
SMAD2
431Annotation 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>
K7ERC7K7ERC7_HUMAN
Mothers against decapentaplegic hom...
SMAD2
137Annotation 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>
K7ESI8K7ESI8_HUMAN
Mothers against decapentaplegic hom...
SMAD2
108Annotation 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>
K7EL92K7EL92_HUMAN
Mothers against decapentaplegic hom...
SMAD2
109Annotation 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>
K7EJX0K7EJX0_HUMAN
Mothers against decapentaplegic hom...
SMAD2
217Annotation 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
<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_011375133R → C in a colorectal carcinoma sample. 1 Publication1
Natural variantiVAR_036473300D → V in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_011376344 – 358Missing in a colorectal carcinoma sample. 1 PublicationAdd BLAST15
Natural variantiVAR_011377440L → R in a colorectal carcinoma sample. 1 Publication1
Natural variantiVAR_011378445P → H in a colorectal carcinoma sample. 1 Publication1
Natural variantiVAR_011379450D → E in a colorectal carcinoma sample. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_00617879 – 108Missing in isoform Short. CuratedAdd BLAST30

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
U59911 mRNA Translation: AAC50789.1
U68018 mRNA Translation: AAB17087.1
U65019 mRNA Translation: AAB17054.1
AF027964 mRNA Translation: AAC51918.1
U78733
, U78727, U78728, U78729, U78730, U78731, U78732 Genomic DNA Translation: AAC39657.1
BC014840 mRNA Translation: AAH14840.1
BC025699 mRNA Translation: AAH25699.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11934.1 [Q15796-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
S71797

NCBI Reference Sequences

More...
RefSeqi
NP_001003652.1, NM_001003652.3 [Q15796-1]
NP_005892.1, NM_005901.5 [Q15796-1]
XP_005258316.1, XM_005258259.3 [Q15796-1]
XP_006722514.1, XM_006722451.3 [Q15796-1]
XP_016881234.1, XM_017025745.1 [Q15796-1]
XP_016881235.1, XM_017025746.1 [Q15796-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000262160; ENSP00000262160; ENSG00000175387 [Q15796-1]
ENST00000356825; ENSP00000349282; ENSG00000175387 [Q15796-2]
ENST00000402690; ENSP00000384449; ENSG00000175387 [Q15796-1]
ENST00000586040; ENSP00000466193; ENSG00000175387 [Q15796-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4087

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4087

UCSC genome browser

More...
UCSCi
uc010xdc.4 human [Q15796-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59911 mRNA Translation: AAC50789.1
U68018 mRNA Translation: AAB17087.1
U65019 mRNA Translation: AAB17054.1
AF027964 mRNA Translation: AAC51918.1
U78733
, U78727, U78728, U78729, U78730, U78731, U78732 Genomic DNA Translation: AAC39657.1
BC014840 mRNA Translation: AAH14840.1
BC025699 mRNA Translation: AAH25699.1
CCDSiCCDS11934.1 [Q15796-1]
PIRiS71797
RefSeqiNP_001003652.1, NM_001003652.3 [Q15796-1]
NP_005892.1, NM_005901.5 [Q15796-1]
XP_005258316.1, XM_005258259.3 [Q15796-1]
XP_006722514.1, XM_006722451.3 [Q15796-1]
XP_016881234.1, XM_017025745.1 [Q15796-1]
XP_016881235.1, XM_017025746.1 [Q15796-2]

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
1DEVX-ray2.20A/C261-456[»]
1KHXX-ray1.80A241-467[»]
1U7VX-ray2.70A/C270-467[»]
2LB3NMR-B217-224[»]
5XODX-ray1.85A262-458[»]
5ZOJX-ray2.79A/B/C262-458[»]
SMRiQ15796
ModBaseiSearch...

Protein-protein interaction databases

BioGridi110262, 274 interactors
ComplexPortaliCPX-1 SMAD2-SMAD3-SMAD4 complex
CPX-11 SMAD2 homotrimer
CPX-3208 SMAD2-SMAD4 complex
CORUMiQ15796
DIPiDIP-29716N
IntActiQ15796, 225 interactors
MINTiQ15796
STRINGi9606.ENSP00000262160

Chemistry databases

ChEMBLiCHEMBL2396512
DrugBankiDB04522 Phosphonoserine

PTM databases

iPTMnetiQ15796
PhosphoSitePlusiQ15796

Polymorphism and mutation databases

BioMutaiSMAD2
DMDMi13633914

Proteomic databases

EPDiQ15796
jPOSTiQ15796
PaxDbiQ15796
PeptideAtlasiQ15796
PRIDEiQ15796
ProteomicsDBi60764 [Q15796-1]
60765 [Q15796-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4087
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262160; ENSP00000262160; ENSG00000175387 [Q15796-1]
ENST00000356825; ENSP00000349282; ENSG00000175387 [Q15796-2]
ENST00000402690; ENSP00000384449; ENSG00000175387 [Q15796-1]
ENST00000586040; ENSP00000466193; ENSG00000175387 [Q15796-2]
GeneIDi4087
KEGGihsa:4087
UCSCiuc010xdc.4 human [Q15796-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4087
DisGeNETi4087

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SMAD2
GeneReviewsiSMAD2
HGNCiHGNC:6768 SMAD2
HPAiCAB025507
CAB073546
HPA067203
MIMi601366 gene
neXtProtiNX_Q15796
OpenTargetsiENSG00000175387
PharmGKBiPA134959722

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3701 Eukaryota
ENOG410XQKU LUCA
GeneTreeiENSGT00940000153499
HOGENOMiHOG000286018
InParanoidiQ15796
KOiK04500
OMAiDEICINP
OrthoDBi608001at2759
PhylomeDBiQ15796
TreeFamiTF314923

Enzyme and pathway databases

ReactomeiR-HSA-1181150 Signaling by NODAL
R-HSA-1502540 Signaling by Activin
R-HSA-2173788 Downregulation of TGF-beta receptor signaling
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-3304356 SMAD2/3 Phosphorylation Motif Mutants in Cancer
R-HSA-3311021 SMAD4 MH2 Domain Mutants in Cancer
R-HSA-3315487 SMAD2/3 MH2 Domain Mutants in Cancer
R-HSA-3656532 TGFBR1 KD Mutants in Cancer
R-HSA-452723 Transcriptional regulation of pluripotent stem cells
R-HSA-5689880 Ub-specific processing proteases
R-HSA-9615017 FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes
R-HSA-9617828 FOXO-mediated transcription of cell cycle genes
SignaLinkiQ15796
SIGNORiQ15796

Miscellaneous databases

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

More...
ChiTaRSi
SMAD2 human
EvolutionaryTraceiQ15796

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Mothers_against_decapentaplegic_homolog_2

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

More...
GenomeRNAii
4087

Protein Ontology

More...
PROi
PR:Q15796

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000175387 Expressed in 233 organ(s), highest expression level in kidney
ExpressionAtlasiQ15796 baseline and differential
GenevisibleiQ15796 HS

Family and domain databases

Gene3Di2.60.200.10, 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 nameiSMAD2_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: Q15796
<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: April 27, 2001
Last sequence update: November 1, 1996
Last modified: July 31, 2019
This is version 220 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, Direct protein sequencing, 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. UniProtKB entry view manual
    User manual for the UniProtKB entry view
  4. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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