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Reviewed, UniProtKB/Swiss-Prot Q15796 (SMAD2_HUMAN)

Last modified January 19, 2010. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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. Interacts with PRDM16. Interacts (via MH2 domain) with LEMD3. Interacts with RBPMS; the interaction is direct. Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.22 Ref.27 Ref.28

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.19 Ref.23 Ref.24 Ref.26

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.

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Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processSMAD 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

response to cholesterol

Inferred from direct assay. Source: UniProtKB

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway Ref.3 Ref.4

Inferred from direct assay. Source: UniProtKB

zygotic specification of dorsal/ventral axis

Inferred from mutant phenotype. Source: UniProtKB

   Cellular componentactivin responsive factor complex Ref.4

Inferred from direct assay. Source: UniProtKB

cytosol

Inferred from Experiment. Source: Reactome

   Molecular functionR-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

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 protein ligase binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

SMAD4Q134852EBI-1040141,EBI-347263
TP63Q9H3D41EBI-1040141,EBI-2337775
TRIM33Q9UPN91EBI-1040141,EBI-2214398

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 467466Mothers against decapentaplegic homolog 2
PRO_0000090852

Regions

Domain10 – 176167MH1
Domain274 – 467194MH2
Motif221 – 2255PY-motif

Amino acid modifications

Modified residue21N-acetylserine Ref.7
Modified residue81Phosphothreonine; by MAPK3 Ref.14 Ref.19 Ref.23 Ref.26
Modified residue191N6-acetyllysine Ref.20
Modified residue2201Phosphothreonine Probable
Modified residue2401Phosphoserine; by CAMK2 Ref.13
Modified residue2451Phosphoserine Probable
Modified residue2501Phosphoserine Probable
Modified residue2551Phosphoserine Probable
Modified residue4581Phosphoserine Ref.23 Ref.24
Modified residue4651Phosphoserine Ref.9 Ref.10
Modified residue4671Phosphoserine Ref.9 Ref.10

Natural variations

Alternative sequence79 – 10830Missing in isoform Short.
VSP_006178
Natural variant1331R → C in colorectal carcinoma. Ref.3
VAR_011375
Natural variant3001D → V in a colorectal cancer sample; somatic mutation. Ref.33
VAR_036473
Natural variant344 – 35815Missing in colorectal carcinoma.
VAR_011376
Natural variant4401L → R in colorectal carcinoma. Ref.3
VAR_011377
Natural variant4451P → H in colorectal carcinoma. Ref.3
VAR_011378
Natural variant4501D → E in colorectal carcinoma. Ref.3
VAR_011379

Experimental info

Mutagenesis191K → R: Loss of acetylation. Ref.20
Mutagenesis201K → R: No effect on acetylation. Ref.20
Mutagenesis221 – 2255Missing: Loss of binding to SMURF2. Ref.12
Mutagenesis3811N → S: Loss of binding to SARA. Ref.28

Secondary structure

1 ..................................... 467
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 95406DB5FC0AA4C9

FASTA46752,306
        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

« Hide

Isoform Short (Smad2Deltaexon3).

Checksum: 0E2FF38B009D2F9E
Show »

FASTA43748,956

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References

« Hide '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]"MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling."
Lin F., Morrison J.M., Wu W., Worman H.J.
Hum. Mol. Genet. 14:437-445(2005) [PubMed: 15601644] [Abstract]
Cited for: INTERACTION WITH LEMD3.
[16]"The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines."
Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S., Luo K.
J. Biol. Chem. 280:15992-16001(2005) [PubMed: 15647271] [Abstract]
Cited for: INTERACTION WITH LEMD3.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS."
Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H., Ye Q.
Nucleic Acids Res. 34:6314-6326(2006) [PubMed: 17099224] [Abstract]
Cited for: INTERACTION WITH RBPMS.
[22]"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.
[23]"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.
[24]"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.
[25]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[26]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, MASS SPECTROMETRY.
[27]"SKI and MEL1 cooperate to inhibit transforming growth factor-beta signal in gastric cancer cells."
Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M., Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M., Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K., Imamura T.
J. Biol. Chem. 284:3334-3344(2009) [PubMed: 19049980] [Abstract]
Cited for: INTERACTION WITH PRDM16.
[28]"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.
[29]"TGF-beta signal transduction."
Massague J.
Annu. Rev. Biochem. 67:753-791(1998) [PubMed: 9759503] [Abstract]
Cited for: REVIEW.
[30]"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.
[31]"The Smad pathway."
Wrana J.L., Attisano L.
Cytokine Growth Factor Rev. 11:5-13(2000) [PubMed: 10708948] [Abstract]
Cited for: REVIEW.
[32]"TGF-beta signaling by Smad proteins."
Miyazono K.
Cytokine Growth Factor Rev. 11:15-22(2000) [PubMed: 10708949] [Abstract]
Cited for: REVIEW.
[33]"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. expand/collapse author list , 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.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U59911 mRNA. Translation: AAC50789.1.
U68018 mRNA. Translation: AAB17087.1.
U65019 mRNA. Translation: AAB17054.1.
AF027964 mRNA. Translation: AAC51918.1.
U78733 expand/collapse EMBL AC list , U78727, U78728, U78729, U78730, U78731, U78732 Genomic DNA. Translation: AAC39657.1.
BC014840 mRNA. Translation: AAH14840.1.
BC025699 mRNA. Translation: AAH25699.1.
IPIIPI00019548.
IPI00220364.
PIRS71797.
RefSeqNP_001003652.1.
NP_001129409.1.
NP_005892.1.
UniGeneHs.12253
Hs.705764

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEVX-ray2.20A/C261-456[»]
1KHXX-ray1.80A241-467[»]
1U7VX-ray2.70A/C270-466[»]
SMRQ15796. Positions 7-172.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29716N.
IntActQ15796. 5 interactions.
STRINGQ15796.

PTM databases

PhosphoSiteQ15796.

Proteomic databases

PRIDEQ15796.

Genome annotation databases

EnsemblENST00000262160; ENSP00000262160; ENSG00000175387; Homo sapiens. [Genome view]
ENST00000402690; ENSP00000384449; ENSG00000175387; Homo sapiens. [Genome view]
GeneID4087.
KEGGhsa:4087.
UCSCuc002lcy.1. human.

Organism-specific databases

CTD4087.
GeneCardsGC18M043621.
H-InvDBHIX0007530.
HGNCHGNC:6768. SMAD2.
HPACAB025507.
MIM601366. gene.
PharmGKBPA134959722.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG11788.
HOGENOMHBG443554.
HOVERGENQ15796.
InParanoidQ15796.
OMAWKKSASG.
OrthoDBEOG9DRCZ7.
PhylomeDBQ15796.

Enzyme and pathway databases

Pathway_Interaction_DBglypican_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.
ReactomeREACT_6844. Signaling by TGF beta.

Gene expression databases

ArrayExpressQ15796.
BgeeQ15796.
CleanExHS_SMAD2.
GenevestigatorQ15796.
GermOnlineENSG00000175387. Homo sapiens.

Family and domain databases

InterProIPR013790. Dwarfin.
IPR003619. MAD_homology1_Dwarfin-type.
IPR013019. MAD_homology_MH1.
IPR017855. SMAD_dom-like.
IPR001132. SMAD_dom_Dwarfin-type.
IPR008984. SMAD_FHA_domain.
[Graphical view]
Gene3DG3DSA:3.90.520.10. MAD_MH1. 1 hit.
G3DSA:2.60.200.10. MH2_Dwarfin-type. 1 hit.
PANTHERPTHR13703. Dwarfin. 1 hit.
PfamPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
PROSITEPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio16020.
SOURCESearch...

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Entry information

Entry nameSMAD2_HUMAN
AccessionPrimary (citable) accession number: Q15796
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: January 19, 2010
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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