Reviewed, UniProtKB/Swiss-Prot Q15796 (SMAD2_HUMAN)

Names and origin

Protein names

Recommended name:
    Mothers against decapentaplegic homolog 2
      Short name=Mothers against DPP homolog 2
Alternative name(s):
    Mad-related protein 2
      Short name=hMAD-2
    SMAD 2
    hSMAD2
    JV18-1

Gene names

Name:	SMAD2
Synonyms:	MADH2, MADR2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	467 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transcriptional modulator activated by TGF-beta and activin type 1 receptor kinase. SMAD2 is a receptor-regulated SMAD (R-SMAD). May act as a tumor suppressor in colorectal carcinoma.
Subunit structure	Found in a complex with SMAD3 and TRIM33 upon addition of TGF-beta. Interacts with SMAD3 and TRIM33. Interacts with SARA (SMAD anchor for receptor activation); may form trimers with the SMAD4 co-SMAD. Interacts with FOXH1, homeobox protein TGIF, PEBP2-alpha subunit, CREB-binding protein (CBP), EP300 and SKI. Interacts with SNON; when phosphorylated at Ser-465/467. Interacts (via PY-motif) with SMURF2. Interacts with AIP1 and HGS. Interacts with NEDD4L in response to TGF-beta By similarity. Interacts with LBXCOR1 and CORL2.
Subcellular location	Cytoplasm. Nucleus. Note: Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4.
Tissue specificity	Expressed at high levels in skeletal muscle, heart and placenta.
Post-translational modification	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. 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. Ref.9 Ref.10 Ref.13 Ref.14 Ref.17 Ref.20 Ref.21 In response to TGF-beta, ubiquitinated by NEDD4L; which promotes its degradation By similarity. 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.
Involvement in disease	Defects in SMAD2 are found in sporadic cases of colorectal carcinoma.
Sequence similarities	Belongs to the dwarfin/SMAD family. Contains 1 MH1 (MAD homology 1) domain. Contains 1 MH2 (MAD homology 2) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	SMAD protein complex assembly Inferred from direct assay. Source: UniProtKB anterior/posterior pattern formation Inferred from sequence or structural similarity. Source: UniProtKB cell fate commitment Inferred from sequence or structural similarity. Source: UniProtKB intracellular signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB mesoderm formation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from mutant phenotype. Source: UniProtKB palate development Inferred from sequence or structural similarity. Source: UniProtKB paraxial mesoderm morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of epithelial to mesenchymal transition Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of gene-specific transcription Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB primary microRNA processing Traceable author statement. Source: UniProtKB regulation of binding Inferred from sequence or structural similarity. Source: UniProtKB regulation of transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW zygotic determination of dorsal/ventral axis Inferred from mutant phenotype. Source: UniProtKB
Cellular component	activin responsive factor complex Ref.4 Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome
Molecular function	R-SMAD binding Inferred from physical interaction. Source: UniProtKB co-SMAD binding Inferred from physical interaction. Source: UniProtKB double-stranded DNA binding Inferred from sequence or structural similarity. Source: UniProtKB phosphate binding Ref.3 Inferred from physical interaction. Source: UniProtKB promoter binding Inferred from direct assay. Source: UniProtKB transcription activator activity Inferred from sequence or structural similarity. Source: UniProtKB transcription factor activity Ref.4 Inferred from direct assay. Source: UniProtKB transcription factor binding Ref.11 Inferred from physical interaction. Source: UniProtKB transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity Ref.4 Inferred from direct assay. Source: UniProtKB type I transforming growth factor beta receptor binding Inferred from physical interaction. Source: UniProtKB ubiquitin binding Inferred from physical interaction. Source: UniProtKB ubiquitin protein ligase binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q15796-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: Q15796-2)

Also known as: Smad2Deltaexon3;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 467

466

Mothers against decapentaplegic homolog 2

PRO_0000090852

Regions

Domain

10 – 176

167

MH1

Domain

274 – 467

194

MH2

Motif

221 – 225

5

PY-motif

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.7

Modified residue

8

1

Phosphothreonine; by MAPK3 Ref.14 Ref.17 Ref.20

Modified residue

19

1

N6-acetyllysine Ref.18

Modified residue

220

1

Phosphothreonine Probable

Modified residue

240

1

Phosphoserine; by CAMK2 Ref.13

Modified residue

245

1

Phosphoserine Probable

Modified residue

250

1

Phosphoserine Probable

Modified residue

255

1

Phosphoserine Probable

Modified residue

458

1

Phosphoserine Ref.20 Ref.21

Modified residue

465

1

Phosphoserine Ref.9 Ref.10

Modified residue

467

1

Phosphoserine Ref.9 Ref.10

Natural variations

Alternative sequence

79 – 108

30

Missing in isoform Short.

VSP_006178

Natural variant

133

1

R → C in colorectal carcinoma. Ref.3

VAR_011375

Natural variant

300

1

D → V in a colorectal cancer sample; somatic mutation. Ref.28

VAR_036473

Natural variant

344 – 358

15

Missing in colorectal carcinoma. Ref.1

VAR_011376

Natural variant

440

1

L → R in colorectal carcinoma. Ref.3

VAR_011377

Natural variant

445

1

P → H in colorectal carcinoma. Ref.3

VAR_011378

Natural variant

450

1

D → E in colorectal carcinoma. Ref.3

VAR_011379

Experimental info

Mutagenesis

19

1

K → R: Loss of acetylation. Ref.18

Mutagenesis

20

1

K → R: No effect on acetylation. Ref.18

Mutagenesis

221 – 225

5

Missing: Loss of binding to SMURF2. Ref.12

Mutagenesis

381

1

N → S: Loss of binding to SARA. Ref.23

Secondary structure

1

.

.

.

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.

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467

Helix Strand Turn

Details...

Beta strand

264 – 267

4

Beta strand

275 – 281

7

Beta strand

290 – 292

3

Beta strand

294 – 301

8

Beta strand

310 – 312

3

Helix

323 – 332

10

Beta strand

336 – 341

6

Beta strand

344 – 349

6

Beta strand

351 – 353

3

Beta strand

355 – 358

4

Helix

360 – 366

7

Beta strand

374 – 376

3

Beta strand

381 – 385

5

Helix

387 – 397

11

Helix

398 – 400

3

Helix

401 – 407

7

Helix

408 – 412

5

Beta strand

413 – 419

7

Helix

431 – 433

3

Beta strand

434 – 442

9

Helix

443 – 454

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 95406DB5FC0AA4C9	FASTA	467	52,306
	10 20 30 40 50 60 MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK KLKKTGRLDE 70 80 90 100 110 120 LEKAITTQNC NTKCVTIPST CSEIWGLSTP NTIDQWDTTG LYSFSEQTRS LDGRLQVSHR 130 140 150 160 170 180 KGLPHVIYCR LWRWPDLHSH HELKAIENCE YAFNLKKDEV CVNPYHYQRV ETPVLPPVLV 190 200 210 220 230 240 PRHTEILTEL PPLDDYTHSI PENTNFPAGI EPQSNYIPET PPPGYISEDG ETSDQQLNQS 250 260 270 280 290 300 MDTGSPAELS PTTLSPVNHS LDLQPVTYSE PAFWCSIAYY ELNQRVGETF HASQPSLTVD 310 320 330 340 350 360 GFTDPSNSER FCLGLLSNVN RNATVEMTRR HIGRGVRLYY IGGEVFAECL SDSAIFVQSP 370 380 390 400 410 420 NCNQRYGWHP ATVCKIPPGC NLKIFNNQEF AALLAQSVNQ GFEAVYQLTR MCTIRMSFVK 430 440 450 460 GWGAEYRRQT VTSTPCWIEL HLNGPLQWLD KVLTQMGSPS VRCSSMS
	Isoform Short (Smad2Deltaexon3). Checksum: 0E2FF38B009D2F9E	FASTA	437	48,956
	10 20 30 40 50 60 MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK KLKKTGRLDE 70 80 90 100 110 120 LEKAITTQNC NTKCVTIPRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELKAIENCE 130 140 150 160 170 180 YAFNLKKDEV CVNPYHYQRV ETPVLPPVLV PRHTEILTEL PPLDDYTHSI PENTNFPAGI 190 200 210 220 230 240 EPQSNYIPET PPPGYISEDG ETSDQQLNQS MDTGSPAELS PTTLSPVNHS LDLQPVTYSE 250 260 270 280 290 300 PAFWCSIAYY ELNQRVGETF HASQPSLTVD GFTDPSNSER FCLGLLSNVN RNATVEMTRR 310 320 330 340 350 360 HIGRGVRLYY IGGEVFAECL SDSAIFVQSP NCNQRYGWHP ATVCKIPPGC NLKIFNNQEF 370 380 390 400 410 420 AALLAQSVNQ GFEAVYQLTR MCTIRMSFVK GWGAEYRRQT VTSTPCWIEL HLNGPLQWLD 430 KVLTQMGSPS VRCSSMS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mad-related genes in the human." Riggins G.J., Thiagalingam S., Rosenblum E., Weinstein C.L., Kern S.E., Hamilton S.R., Willson J.K.V., Markowitz S.D., Kinzler K.W., Vogelstein B.V. Nat. Genet. 13:347-349(1996) [PubMed: 8673135] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT COLORECTAL CARCINOMA 344-GLU--GLN-358 DEL.
[2]	"Receptor-associated Mad homologues synergize as effectors of the TGF-beta response." Zhang Y., Feng X.-H., Wu R.-Y., Derynck R. Nature 383:168-172(1996) [PubMed: 8774881] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG). Tissue: Placenta.
[3]	"MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma." Eppert K., Scherer S.W., Ozcelik H., Pirone R., Hoodless P., Kim H., Tsui L.-C., Bapat B., Gallinger S., Andrulis I.L., Thomsen G.H., Wrana J.L., Attisano L. Cell 86:543-552(1996) [PubMed: 8752209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANTS COLORECTAL CARCINOMA CYS-133; ARG-440; HIS-445 AND GLU-450. Tissue: Kidney.
[4]	"Dual role of the Smad4/DPC4 tumor suppressor in TGFbeta-inducible transcriptional complexes." Liu F., Pouponnot C., Massague J. Genes Dev. 11:3157-3167(1997) [PubMed: 9389648] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
[5]	"Characterization of the MADH2/Smad2 gene, a human Mad homolog responsible for the transforming growth factor-beta and activin signal transduction pathway." Takenoshita S., Mogi A., Nagashima M., Yang K., Yagi K., Hanyu A., Nagamachi Y., Miyazono K., Hagiwara K. Genomics 48:1-11(1998) [PubMed: 9503010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). Tissue: Kidney, Pancreas and Spleen.
[7]	Bienvenut W.V., von Kriegsheim A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-14 AND 170-182, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Chronic myeloid leukemia cell.
[8]	"Alternatively spliced variant of Smad2 lacking exon 3. Comparison with wild-type Smad2 and Smad3." Yagi K., Goto D., Hamamoto T., Takenoshita S., Kato M., Miyazono K. J. Biol. Chem. 274:703-709(1999) [PubMed: 9873005] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS LONG AND SHORT).
[9]	"The TGF-beta family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase." Kretzschmar M., Liu F., Hata A., Doody J., Massague J. Genes Dev. 11:984-995(1997) [PubMed: 9136927] [Abstract] Cited for: PHOSPHORYLATION AT SER-465 AND SER-467.
[10]	"TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling." Abdollah S., Macias-Silva M., Tsukazaki T., Hayashi H., Attisano L., Wrana J.L. J. Biol. Chem. 272:27678-27685(1997) [PubMed: 9346908] [Abstract] Cited for: PHOSPHORYLATION AT SER-465 AND SER-467.
[11]	"Characterization of human FAST-1, a TGF beta and activin signal transducer." Zhou S., Zawel L., Lengauer C., Kinzler K.W., Vogelstein B. Mol. Cell 2:121-127(1998) [PubMed: 9702198] [Abstract] Cited for: INTERACTION WITH FOXH1. Tissue: Colon adenocarcinoma.
[12]	"TGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation." Bonni S., Wang H.R., Causing C.G., Kavsak P., Stroschein S.L., Luo K., Wrana J.L. Nat. Cell Biol. 3:587-595(2001) [PubMed: 11389444] [Abstract] Cited for: INTERACTION WITH SMURF2, MUTAGENESIS OF 221-PRO--TYR-225.
[13]	"Decorin suppresses transforming growth factor-beta-induced expression of plasminogen activator inhibitor-1 in human mesangial cells through a mechanism that involves Ca2+-dependent phosphorylation of Smad2 at serine-240." Abdel-Wahab N., Wicks S.J., Mason R.M., Chantry A. Biochem. J. 362:643-649(2002) [PubMed: 11879191] [Abstract] Cited for: PHOSPHORYLATION AT SER-240.
[14]	"Modulation of Smad2-mediated signaling by extracellular signal-regulated kinase." Funaba M., Zimmerman C.M., Mathews L.S. J. Biol. Chem. 277:41361-41368(2002) [PubMed: 12193595] [Abstract] Cited for: PHOSPHORYLATION AT THR-8; THR-220; SER-245; SER-250 AND SER-255.
[15]	"Cloning and functional characterization of a new Ski homolog, Fussel-18, specifically expressed in neuronal tissues." Arndt S., Poser I., Schubert T., Moser M., Bosserhoff A.-K. Lab. Invest. 85:1330-1341(2005) [PubMed: 16200078] [Abstract] Cited for: INTERACTION WITH CORL2.
[16]	"Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of the TGFbeta pathway." He W., Dorn D.C., Erdjument-Bromage H., Tempst P., Moore M.A., Massague J. Cell 125:929-941(2006) [PubMed: 16751102] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SMAD3 AND TRIM33, INTERACTION WITH TRIM33.
[17]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"The DNA binding activities of Smad2 and Smad3 are regulated by coactivator-mediated acetylation." Simonsson M., Kanduri M., Gronroos E., Heldin C.H., Ericsson J. J. Biol. Chem. 281:39870-39880(2006) [PubMed: 17074756] [Abstract] Cited for: ACETYLATION AT LYS-19, MUTAGENESIS OF LYS-19 AND LYS-20.
[19]	"Fussel-15, a novel Ski/Sno homolog protein, antagonizes BMP signaling." Arndt S., Poser I., Moser M., Bosserhoff A.-K. Mol. Cell. Neurosci. 34:603-611(2007) [PubMed: 17292623] [Abstract] Cited for: INTERACTION WITH LBXCOR1.
[20]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8 AND SER-458, MASS SPECTROMETRY.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, MASS SPECTROMETRY.
[22]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[23]	"Structural basis of Smad2 recognition by the Smad anchor for receptor activation." Wu G., Chen Y.-G., Ozdamar B., Gyuricza C.A., Chong P.A., Wrana J.L., Massague J., Shi Y. Science 287:92-97(2000) [PubMed: 10615055] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 261-456 IN COMPLEX WITH ZFYVE9, INTERACTION WITH SARA, MUTAGENESIS OF ASN-381.
[24]	"TGF-beta signal transduction." Massague J. Annu. Rev. Biochem. 67:753-791(1998) [PubMed: 9759503] [Abstract] Cited for: REVIEW.
[25]	"Remarkable versatility of Smad proteins in the nucleus of transforming growth factor-beta activated cells." Verschueren K., Huylebroeck D. Cytokine Growth Factor Rev. 10:187-199(1999) [PubMed: 10647776] [Abstract] Cited for: REVIEW.
[26]	"The Smad pathway." Wrana J.L., Attisano L. Cytokine Growth Factor Rev. 11:5-13(2000) [PubMed: 10708948] [Abstract] Cited for: REVIEW.
[27]	"TGF-beta signaling by Smad proteins." Miyazono K. Cytokine Growth Factor Rev. 11:15-22(2000) [PubMed: 10708949] [Abstract] Cited for: REVIEW.
[28]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-300.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00019548.
IPI00220364.

PIR

S71797.

RefSeq

NP_001003652.1.
NP_001129409.1.
NP_005892.1.

UniGene

Hs.12253
Hs.705764

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DEV	X-ray	2.20	A/C	261-456	[»]
1KHX	X-ray	1.80	A	241-467	[»]
1U7V	X-ray	2.70	A/C	270-466	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q15796.

Proteomic databases

PRIDE

Q15796.

Genome annotation databases

Ensembl

ENSG00000175387. Homo sapiens. [Contig view]

GeneID

4087.

KEGG

hsa:4087.

Organism-specific databases

GeneCards

GC18M043621.

H-InvDB

HIX0007530.

HGNC

HGNC:6768. SMAD2.

MIM

601366. gene.

PharmGKB

PA134959722.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q15796.

HOVERGEN

Q15796.

OMA

Q15796. WKKSASG.

Enzyme and pathway databases

Pathway_Interaction_DB

glypican_1pathway. Glypican 1 network.
smad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_6844. Signaling by TGF beta.

Gene expression databases

ArrayExpress

Q15796.

Bgee

Q15796.

CleanEx

HS_SMAD2.

GermOnline

ENSG00000175387. Homo sapiens.

Family and domain databases

InterPro

IPR013790. Dwarfin.
IPR003619. MAD_homology1_Dwarfin-type.
IPR013019. MAD_homology_MH1.
IPR017855. SMAD_dom-like.
IPR001132. SMAD_dom_Dwarfin-type.
[Graphical view]

Gene3D

G3DSA:3.90.520.10. MAD_MH1. 1 hit.
G3DSA:2.60.200.10. MH2_Dwarfin-type. 1 hit.

PANTHER

PTHR13703. Dwarfin. 1 hit.

Pfam

PF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]

SMART

SM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]

PROSITE

PS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

16020.

SOURCE

Search...

Entry information

Entry name

SMAD2_HUMAN

Accession

Primary (citable) accession number: Q15796

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)