SMAD2 SMAD family member 2 [Homo sapiens (human)] - Gene

Summary

Official Symbol: SMAD2provided by HGNC
Official Full Name: SMAD family member 2provided by HGNC
Primary source: HGNC:HGNC:6768
See related: Ensembl:ENSG00000175387 MIM:601366
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: JV18; MADH2; MADR2; JV18-1; hMAD-2; hSMAD2
Summary: The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signal of the transforming growth factor (TGF)-beta, and thus regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. The phosphorylation induces the dissociation of this protein with SARA and the association with the family member SMAD4. The association with SMAD4 is important for the translocation of this protein into the nucleus, where it binds to target promoters and forms a transcription repressor complex with other cofactors. This protein can also be phosphorylated by activin type 1 receptor kinase, and mediates the signal from the activin. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, May 2012]
Expression: Ubiquitous expression in thyroid (RPKM 6.6), testis (RPKM 4.0) and 25 other tissues See more
Orthologs: mouse all

Genomic context

Location:: 18q21.1

Exon count:: 18

Annotation release	Status	Assembly	Chr	Location
109.20200815	current	GRCh38.p13 (GCF_000001405.39)	18	NC_000018.10 (47808957..47931188, complement)
105	previous assembly	GRCh37.p13 (GCF_000001405.25)	18	NC_000018.9 (45359466..45457564, complement)

Chromosome 18 - NC_000018.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Long non-coding RNA SNHG16 regulates human aortic smooth muscle cell proliferation and migration via sponging miR-205 and modulating Smad2.
Title: Long non-coding RNA SNHG16 regulates human aortic smooth muscle cell proliferation and migration via sponging miR-205 and modulating Smad2.
Expression analysis of selected miR-206 targets from the transforming growth factor-beta signaling pathway in breast cancer.
Title: Expression analysis of selected miR-206 targets from the transforming growth factor-β signaling pathway in breast cancer.
Nagilactone D ameliorates experimental pulmonary fibrosis in vitro and in vivo via modulating TGF-beta/Smad signaling pathway.
Title: Nagilactone D ameliorates experimental pulmonary fibrosis in vitro and in vivo via modulating TGF-β/Smad signaling pathway.
miR-145-5p arrests the development of fibrogenesis and decreases hypertrophic scar formation by reducing the expression of Smad2/3.
Title: miR-145-5p attenuates hypertrophic scar via reducing Smad2/Smad3 expression.
Smad2 is glycosylated, and this post-translational modification was modulated by 17beta-estradiol but not by TGFbeta1.
Title: Glycosylation is a novel TGFβ1-independent post-translational modification of Smad2.
Silencing tetraspanin 1 (TSPAN1) promotes the phosphorylation of Smad2 protein (Smad2)/Smad3 protein (Smad3) and stabilizes beta-catenin protein.
Title: Tetraspanin 1 as a mediator of fibrosis inhibits EMT process and Smad2/3 and beta-catenin pathway in human pulmonary fibrosis.
Treatment with apocynin of human VSMCs stimulated ROS production and the phosphorylation of TGFBR1 and subsequent activation of TGFBR1 signalling leading to the formation of phosphorylated Smad2 which consequently upregulates the mRNA expression of glycosaminoglycan synthesizing enzyme
Title: ROS directly activates transforming growth factor β type 1 receptor signalling in human vascular smooth muscle cells.
our data suggest that heterozygous loss-of-function SMAD2 variants can cause a wide spectrum of autosomal dominant aortic and arterial aneurysmal disease, combined with connective tissue findings reminiscent of MFS and LDS.
Title: Novel pathogenic <i>SMAD2</i> variants in five families with arterial aneurysm and dissection: further delineation of the phenotype.
HMMR activates the TGF-beta/Smad2 signaling pathway, which was required for the HMMR-mediated oncogenic effects and exhibited significant clinical relevance with HMMR expression. These findings reveal a critical role for HMMR in the chemoresistance of gastric cancer.
Title: Hyaluronan-mediated motility receptor confers resistance to chemotherapy <i>via</i> TGFβ/Smad2-induced epithelial-mesenchymal transition in gastric cancer.
this study also identified miR-125b as a downstream target of HOXA-AS2 and revealed the downregulation of miR-125b by HOXA-AS2 as well as the involvement of HOXA-AS2/miR-125b/Smad2 interactions in the functional role of HOXA-AS2 in mediating the migration, invasion and stemness of bladder cancer cells
Title: Long non-coding RNA HOXA-AS2 promotes the migration, invasion and stemness of bladder cancer via regulating miR-125b/Smad2 axis.

Submit: New GeneRIF Correction See all GeneRIFs (321)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Copy number response

Description
Copy number response Haploinsufficency No evidence available (Last evaluated (2018-06-28) ClinGen Genome Curation Page Triplosensitivity No evidence available (Last evaluated (2018-06-28) ClinGen Genome Curation Page

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
HIV-1 replication is restricted by TGFB1 and SMAD2 in Langerhans cells	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	HIV-1 gp120 and p300 synergistically increase TGF-beta, ATF-2 and activating protein-1 (AP-1) expression leading to tubular cell apoptosis; in addition, HIV-1 gp120 treatment causes phosphorylation of Smad2 and downregulation of c-Jun	PubMed
Tat	tat	HIV-1 Tat-treated pulmonary arterial smooth muscle cells downregulate levels of phosphorylated SMAD2/3 proteins and SMAD2/3-SMAD4 protein complex, which are repressed by cocaine exposure	PubMed
	tat	HIV-1 Tat enhances binding of SMAD2, -3 and -4 and their binding partner Fast1 to the JCV DNA control region (CR) to stimulate JCV gene transcription in living cells	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH18445 (e-PCR)
- UniSTS:62505

RH69774 (e-PCR)
- UniSTS:6449

MARC_10275-10276:998924078:1 (e-PCR)
- UniSTS:267092

L18426 (e-PCR)
- UniSTS:34648

Smad2 (e-PCR), detects polymorphism
- UniSTS:466570

WIAF-1471 (e-PCR)
- UniSTS:59533

D11S3114 (e-PCR)
- UniSTS:152207

RH12141 (e-PCR)
- UniSTS:39578

SHGC-148706 (e-PCR)
- UniSTS:176569

SHGC-64255 (e-PCR)
- UniSTS:82363

RH47015 (e-PCR)
- UniSTS:52667

RH98251 (e-PCR)
- UniSTS:86211

D18S1312 (e-PCR)
- UniSTS:31430

SHGC-16176 (e-PCR)
- UniSTS:68808

MADH2_1658 (e-PCR)
- UniSTS:277460

RH66619 (e-PCR)
- UniSTS:53990

RH17857 (e-PCR)
- UniSTS:72445

Homology

Homologs of the SMAD2 gene: The SMAD2 gene is conserved in chimpanzee, Rhesus monkey, dog, cow, mouse, rat, chicken, zebrafish, and frog.
Orthologs from Annotation Pipeline: 304 organisms have orthologs with human gene SMAD2
Orthologs

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
contributes_to DNA binding	IDA Inferred from Direct Assay more info	PubMed
DNA-binding transcription activator activity, RNA polymerase II-specific	IBA Inferred from Biological aspect of Ancestor more info	PubMed
DNA-binding transcription activator activity, RNA polymerase II-specific	IDA Inferred from Direct Assay more info	PubMed
DNA-binding transcription activator activity, RNA polymerase II-specific	ISS Inferred from Sequence or Structural Similarity more info	PubMed
DNA-binding transcription factor activity	IDA Inferred from Direct Assay more info	PubMed
contributes_to DNA-binding transcription factor activity	IDA Inferred from Direct Assay more info	PubMed
DNA-binding transcription factor activity, RNA polymerase II-specific	ISA Inferred from Sequence Alignment more info
DNA-binding transcription factor activity, RNA polymerase II-specific	ISM Inferred from Sequence Model more info	PubMed
I-SMAD binding	IBA Inferred from Biological aspect of Ancestor more info	PubMed
I-SMAD binding	IPI Inferred from Physical Interaction more info	PubMed
R-SMAD binding	IPI Inferred from Physical Interaction more info	PubMed
RNA polymerase II proximal promoter sequence-specific DNA binding	IBA Inferred from Biological aspect of Ancestor more info	PubMed
RNA polymerase II proximal promoter sequence-specific DNA binding	IDA Inferred from Direct Assay more info	PubMed
SMAD binding	IPI Inferred from Physical Interaction more info	PubMed
activating transcription factor binding	IPI Inferred from Physical Interaction more info	PubMed
chromatin binding	IEA Inferred from Electronic Annotation more info
co-SMAD binding	IPI Inferred from Physical Interaction more info	PubMed
disordered domain specific binding	IPI Inferred from Physical Interaction more info	PubMed
double-stranded DNA binding	ISS Inferred from Sequence or Structural Similarity more info
metal ion binding	IEA Inferred from Electronic Annotation more info
phosphatase binding	IPI Inferred from Physical Interaction more info	PubMed
protein binding	IPI Inferred from Physical Interaction more info	PubMed
proximal promoter sequence-specific DNA binding	IC Inferred by Curator more info	PubMed
tau protein binding	ISS Inferred from Sequence or Structural Similarity more info	PubMed
transcription factor binding	IBA Inferred from Biological aspect of Ancestor more info	PubMed
transcription factor binding	IPI Inferred from Physical Interaction more info	PubMed
transforming growth factor beta receptor binding	IPI Inferred from Physical Interaction more info	PubMed
type I transforming growth factor beta receptor binding	IPI Inferred from Physical Interaction more info	PubMed
ubiquitin protein ligase binding	IBA Inferred from Biological aspect of Ancestor more info	PubMed
ubiquitin protein ligase binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
BMP signaling pathway	IBA Inferred from Biological aspect of Ancestor more info	PubMed
SMAD protein complex assembly	IDA Inferred from Direct Assay more info	PubMed
SMAD protein signal transduction	IBA Inferred from Biological aspect of Ancestor more info	PubMed
SMAD protein signal transduction	IEA Inferred from Electronic Annotation more info
activin receptor signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
adrenal gland development	IEA Inferred from Electronic Annotation more info
anatomical structure morphogenesis	IBA Inferred from Biological aspect of Ancestor more info	PubMed
anterior/posterior pattern specification	ISS Inferred from Sequence or Structural Similarity more info
cell differentiation	IBA Inferred from Biological aspect of Ancestor more info	PubMed
cell fate commitment	ISS Inferred from Sequence or Structural Similarity more info
common-partner SMAD protein phosphorylation	IDA Inferred from Direct Assay more info	PubMed
embryonic cranial skeleton morphogenesis	IEA Inferred from Electronic Annotation more info
embryonic foregut morphogenesis	IEA Inferred from Electronic Annotation more info
endoderm formation	IEA Inferred from Electronic Annotation more info
gastrulation	TAS Traceable Author Statement more info	PubMed
in utero embryonic development	IEA Inferred from Electronic Annotation more info
insulin secretion	IEA Inferred from Electronic Annotation more info
intracellular signal transduction	ISS Inferred from Sequence or Structural Similarity more info
lung development	IEA Inferred from Electronic Annotation more info
mesoderm formation	ISS Inferred from Sequence or Structural Similarity more info
negative regulation of cell proliferation	IEA Inferred from Electronic Annotation more info
negative regulation of transcription by RNA polymerase II	IBA Inferred from Biological aspect of Ancestor more info	PubMed
negative regulation of transcription by RNA polymerase II	TAS Traceable Author Statement more info
negative regulation of transcription, DNA-templated	IMP Inferred from Mutant Phenotype more info	PubMed
negative regulation of transforming growth factor beta receptor signaling pathway	TAS Traceable Author Statement more info
nodal signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
organ growth	IEA Inferred from Electronic Annotation more info
pancreas development	IEA Inferred from Electronic Annotation more info
paraxial mesoderm morphogenesis	ISS Inferred from Sequence or Structural Similarity more info
pericardium development	IEA Inferred from Electronic Annotation more info
positive regulation of BMP signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
positive regulation of epithelial to mesenchymal transition	ISS Inferred from Sequence or Structural Similarity more info
positive regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry	IMP Inferred from Mutant Phenotype more info	PubMed
positive regulation of transcription by RNA polymerase II	IBA Inferred from Biological aspect of Ancestor more info	PubMed
positive regulation of transcription by RNA polymerase II	IDA Inferred from Direct Assay more info	PubMed
positive regulation of transcription by RNA polymerase II	ISS Inferred from Sequence or Structural Similarity more info
positive regulation of transcription by RNA polymerase II	TAS Traceable Author Statement more info
positive regulation of transcription, DNA-templated	IDA Inferred from Direct Assay more info	PubMed
positive regulation of transcription, DNA-templated	IMP Inferred from Mutant Phenotype more info	PubMed
positive regulation of transcription, DNA-templated	ISS Inferred from Sequence or Structural Similarity more info
post-embryonic development	IEA Inferred from Electronic Annotation more info
primary miRNA processing	TAS Traceable Author Statement more info	PubMed
protein deubiquitination	TAS Traceable Author Statement more info
regulation of binding	ISS Inferred from Sequence or Structural Similarity more info
regulation of transforming growth factor beta receptor signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
response to cholesterol	IDA Inferred from Direct Assay more info	PubMed
response to glucose	IEA Inferred from Electronic Annotation more info
secondary palate development	ISS Inferred from Sequence or Structural Similarity more info
signal transduction involved in regulation of gene expression	IEA Inferred from Electronic Annotation more info
somatic stem cell population maintenance	TAS Traceable Author Statement more info
transforming growth factor beta receptor signaling pathway	IBA Inferred from Biological aspect of Ancestor more info	PubMed
transforming growth factor beta receptor signaling pathway	IDA Inferred from Direct Assay more info	PubMed
transforming growth factor beta receptor signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
transforming growth factor beta receptor signaling pathway	TAS Traceable Author Statement more info
ureteric bud development	IEA Inferred from Electronic Annotation more info
wound healing	IEA Inferred from Electronic Annotation more info
zygotic specification of dorsal/ventral axis	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
SMAD protein complex	IDA Inferred from Direct Assay more info	PubMed
activin responsive factor complex	IDA Inferred from Direct Assay more info	PubMed
cytoplasm	IBA Inferred from Biological aspect of Ancestor more info	PubMed
cytoplasm	IDA Inferred from Direct Assay more info	PubMed
cytosol	TAS Traceable Author Statement more info
heteromeric SMAD protein complex	IBA Inferred from Biological aspect of Ancestor more info	PubMed
heteromeric SMAD protein complex	IDA Inferred from Direct Assay more info	PubMed
nuclear chromatin	IDA Inferred from Direct Assay more info	PubMed
nuclear chromatin	ISA Inferred from Sequence Alignment more info
nucleoplasm	TAS Traceable Author Statement more info
nucleus	IDA Inferred from Direct Assay more info	PubMed
protein-containing complex	IMP Inferred from Mutant Phenotype more info	PubMed
transcription factor complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: mothers against decapentaplegic homolog 2

Names: MAD homolog 2; SMAD, mothers against DPP homolog 2; Sma- and Mad-related protein 2; mother against DPP homolog 2

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_029946.1 RefSeqGene

Range

5546..103050

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001003652.4 → NP_001003652.1 mothers against decapentaplegic homolog 2 isoform 1

See identical proteins and their annotated locations for NP_001003652.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) represents the longest transcript and encodes the longer isoform (1). Both variants 1 and 2 encode the same isoform (1).

Source sequence(s)

AC026898, AC120349, AI453799, BC025699, DB462454

Consensus CDS

CCDS11934.1

UniProtKB/Swiss-Prot

Q15796

UniProtKB/TrEMBL

Q53XR6

Related

ENSP00000384449.1, ENST00000402690.6

Conserved Domains (2) summary

cd10491
Location:8 → 172

MH1_SMAD_2_3; N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3

cd10985
Location:266 → 456

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3
NM_001135937.3 → NP_001129409.1 mothers against decapentaplegic homolog 2 isoform 2

See identical proteins and their annotated locations for NP_001129409.1

Status: REVIEWED

Description

Transcript Variant: This variant (3, also known as SMAD2Deltaexon3) lacks an in-frame exon in the 5' coding region, compared to variant 2, resulting in an isoform (2) that is shorter than isoform 1. There are no publicly available full-length transcripts representing this variant, but it is supported by data in Taekenoshita et al. (1998; PMID: 9503010) and Yagi et al. (1999; PMID: 9873005).

Source sequence(s)

AC026898, AC120349, AI453799, AK299218, DB462454

UniProtKB/TrEMBL

B7Z5N5

Related

ENSP00000349282.4, ENST00000356825.8

Conserved Domains (2) summary

cd10491
Location:8 → 142

MH1_SMAD_2_3; N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3

cd10985
Location:236 → 426

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3
NM_005901.6 → NP_005892.1 mothers against decapentaplegic homolog 2 isoform 1

See identical proteins and their annotated locations for NP_005892.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) uses an alternate exon (1b) in the 5' UTR compared to variant 2. Both variants 1 and 2 encode the same isoform (1).

Source sequence(s)

AC026898, AC120349, AI453799, BC014840

Consensus CDS

CCDS11934.1

UniProtKB/Swiss-Prot

Q15796

UniProtKB/TrEMBL

Q53XR6

Related

ENSP00000262160.6, ENST00000262160.11

Conserved Domains (2) summary

cd10491
Location:8 → 172

MH1_SMAD_2_3; N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3

cd10985
Location:266 → 456

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3

RefSeqs of Annotated Genomes: Homo sapiens Updated Annotation Release 109.20200815

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p13 Primary Assembly

Genomic

NC_000018.10 Reference GRCh38.p13 Primary Assembly

Range

47808957..47931188 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_017025747.2 → XP_016881236.1 mothers against decapentaplegic homolog 2 isoform X4
XM_017025746.2 → XP_016881235.1 mothers against decapentaplegic homolog 2 isoform X2

UniProtKB/Swiss-Prot

Q15796

Related

ENSP00000466193.1, ENST00000586040.5

Conserved Domains (2) summary

cd10491
Location:8 → 142

MH1_SMAD_2_3; N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3

cd10985
Location:236 → 426

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3
XM_011525985.3 → XP_011524287.1 mothers against decapentaplegic homolog 2 isoform X5

Conserved Domains (2) summary

cd10985
Location:213 → 403

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3

cl00055
Location:56 → 119

MH1; N-terminal Mad Homology 1 (MH1) domain
XM_017025745.2 → XP_016881234.1 mothers against decapentaplegic homolog 2 isoform X1

UniProtKB/Swiss-Prot

Q15796

UniProtKB/TrEMBL

Q53XR6

Conserved Domains (2) summary

cd10491
Location:8 → 172

MH1_SMAD_2_3; N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3

cd10985
Location:266 → 456

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3
XM_017025750.2 → XP_016881239.1 mothers against decapentaplegic homolog 2 isoform X7

Conserved Domains (1) summary

cd10985
Location:26 → 216

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3
XM_006722451.4 → XP_006722514.1 mothers against decapentaplegic homolog 2 isoform X1

See identical proteins and their annotated locations for XP_006722514.1

UniProtKB/Swiss-Prot

Q15796

UniProtKB/TrEMBL

Q53XR6

Conserved Domains (2) summary

cd10491
Location:8 → 172

MH1_SMAD_2_3; N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3

cd10985
Location:266 → 456

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3
XM_017025748.2 → XP_016881237.1 mothers against decapentaplegic homolog 2 isoform X5

Conserved Domains (2) summary

cd10985
Location:213 → 403

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3

cl00055
Location:56 → 119

MH1; N-terminal Mad Homology 1 (MH1) domain
XM_024451173.1 → XP_024306941.1 mothers against decapentaplegic homolog 2 isoform X1

Conserved Domains (2) summary

cd10491
Location:8 → 172

MH1_SMAD_2_3; N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3

cd10985
Location:266 → 456

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3
XM_011525984.2 → XP_011524286.1 mothers against decapentaplegic homolog 2 isoform X3

Conserved Domains (2) summary

cd10985
Location:224 → 414

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3

cl00055
Location:67 → 130

MH1; N-terminal Mad Homology 1 (MH1) domain
XM_005258259.4 → XP_005258316.1 mothers against decapentaplegic homolog 2 isoform X1

See identical proteins and their annotated locations for XP_005258316.1

UniProtKB/Swiss-Prot

Q15796

UniProtKB/TrEMBL

Q53XR6

Conserved Domains (2) summary

cd10491
Location:8 → 172

MH1_SMAD_2_3; N-terminal Mad Homology 1 (MH1) domain in SMAD2 and SMAD3

cd10985
Location:266 → 456

MH2_SMAD_2_3; C-terminal Mad Homology 2 (MH2) domain in SMAD2 and SMAD3
XM_017025749.1 → XP_016881238.1 mothers against decapentaplegic homolog 2 isoform X6

Related

ENSP00000466254.1, ENST00000587269.5