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Q62432 (SMAD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mothers against decapentaplegic homolog 2

Short name=MAD homolog 2
Short name=Mothers against DPP homolog 2
Alternative name(s):
Mad-related protein 2
Short name=mMad2
SMAD family member 2
Short name=SMAD 2
Short name=Smad2
Gene names
Name:Smad2
Synonyms:Madh2, Madr2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

General annotation (Comments)

Function

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 By similarity. Ref.7

Subunit structure

Momomer; the absence of TGF-beta By similarity. Interacts with ZNF580 By similarity. Heterodimer; in the presence of TGF-beta. Forms a heterodimer with co-SMAD, SMAD4, in the nucleus to form the transactivation complex SMAD2/SMAD4 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 (via PY-motif) with SMURF2. Interacts with SKOR1 and SKOR2. Interacts with PRDM16. Interacts (via MH2 domain) with LEMD3. Interacts with RBPMS. 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 ot the TGF-beta signaling By similarity. Interacts with NEDD4L in response to TGF-beta. Interacts with WWP1, AIP1 and HGS. Interacts with PML. Interacts with PDPK1 (via PH domain). Interacts with DAB2; the interactions are enhanced upon TGF-beta stimulation. Interacts with USP15. Interacts with PPP5C. Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4. On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1 By similarity. Ref.14

Post-translational modification

In response to TGF-beta, phosphorylated on the C-terminal SXS motif by TGF-beta and activin type 1 receptor kinases, phosphorylation declines progressively in a SETD8-dependent manner. Phosphorylation in this motif is required for interaction with a number of proteins including SMURF2, SNON and SMAD4 in response to TGF-beta. Dephosphorylated in this motif by PPM1A leading to disruption of the SMAD2/3-SMAD4 complex, nuclear export and termination of the TGF-beta signaling. 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. Ref.7 Ref.10

In response to TGF-beta, ubiquitinated by NEDD4L; which promotes its degradation. Monoubiquitinated, leading to prevent DNA-binding. Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes By similarity.

Acetylated on Lys-19 by coactivators in response to TGF-beta signaling, which increases transcriptional activity By similarity.

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 processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
Metal-binding
Zinc
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSMAD protein complex assembly

Inferred from electronic annotation. Source: Ensembl

anterior/posterior pattern specification

Inferred from mutant phenotype PubMed 11418863PubMed 12842913PubMed 9529255. Source: MGI

cell fate commitment

Inferred from mutant phenotype PubMed 12842913. Source: MGI

common-partner SMAD protein phosphorylation

Inferred from sequence orthology PubMed 16806156. Source: MGI

developmental growth

Inferred from genetic interaction PubMed 15183723. Source: MGI

embryonic cranial skeleton morphogenesis

Inferred from genetic interaction PubMed 15183723. Source: MGI

embryonic foregut morphogenesis

Inferred from genetic interaction PubMed 15183723. Source: MGI

embryonic pattern specification

Inferred from genetic interaction PubMed 15183723. Source: MGI

endoderm development

Inferred from genetic interaction PubMed 15183723. Source: MGI

endoderm formation

Inferred from mutant phenotype PubMed 21822279. Source: MGI

gastrulation

Inferred from genetic interaction PubMed 15183723. Source: MGI

heart development

Inferred from genetic interaction PubMed 17849440. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 17849440. Source: MGI

insulin secretion

Inferred from genetic interaction PubMed 17849440. Source: MGI

intracellular signal transduction

Inferred from direct assay PubMed 14749725. Source: MGI

lung development

Inferred from genetic interaction PubMed 17849440. Source: MGI

mesoderm formation

Inferred from mutant phenotype PubMed 15084457. Source: MGI

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

nodal signaling pathway

Inferred from electronic annotation. Source: Ensembl

organ growth

Inferred from genetic interaction PubMed 17849440. Source: MGI

palate development

Inferred from mutant phenotype PubMed 14691138. Source: BHF-UCL

pancreas development

Inferred from genetic interaction PubMed 17849440. Source: MGI

paraxial mesoderm morphogenesis

Inferred from mutant phenotype PubMed 15084457. Source: MGI

pattern specification process

Inferred from genetic interaction PubMed 17849440. Source: MGI

pericardium development

Inferred from genetic interaction PubMed 15183723. Source: MGI

positive regulation of BMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 14691138. Source: BHF-UCL

positive regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 9702197. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 14691138. Source: BHF-UCL

post-embryonic development

Inferred from genetic interaction PubMed 17849440. Source: MGI

protein phosphorylation

Inferred from direct assay PubMed 18990706. Source: MGI

regulation of binding

Inferred from direct assay PubMed 15282343. Source: MGI

regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

response to cholesterol

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from genetic interaction PubMed 17849440. Source: MGI

signal transduction involved in regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 11557747PubMed 14749725. Source: MGI

ureteric bud development

Inferred from expression pattern PubMed 14656760. Source: UniProtKB

zygotic specification of dorsal/ventral axis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentSMAD protein complex

Inferred from electronic annotation. Source: Ensembl

activin responsive factor complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 14691138. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 11160896. Source: UniProtKB

transcription factor complex

Inferred from direct assay PubMed 17568773PubMed 9702197. Source: MGI

   Molecular_functionSMAD binding

Inferred from physical interaction PubMed 11160896. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 15657445PubMed 16619037. Source: MGI

double-stranded DNA binding

Inferred from direct assay PubMed 15282343. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 22442258. Source: IntAct

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

transcription factor binding

Inferred from physical interaction PubMed 11937490PubMed 9702197. Source: UniProtKB

transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Smad4P974713EBI-2337932,EBI-5259270

Alternative products

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

Note: mRNA corresponding to the isoform Long is approximately 20-fold more abundant. Both forms are coexpressed throughout mouse development.
Isoform Long (identifier: Q62432-1)

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: Q62432-2)

Also known as: Deltaexon3;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 467466Mothers against decapentaplegic homolog 2
PRO_0000090853

Regions

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

Sites

Metal binding741Zinc By similarity
Metal binding1491Zinc By similarity
Metal binding1611Zinc By similarity
Metal binding1661Zinc By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue81Phosphothreonine By similarity
Modified residue191N6-acetyllysine By similarity
Modified residue2401Phosphoserine; by CAMK2 By similarity
Modified residue4581Phosphoserine By similarity
Modified residue4601Phosphoserine By similarity
Modified residue4641Phosphoserine By similarity
Modified residue4651Phosphoserine; by TGFBR1 By similarity
Modified residue4671Phosphoserine; by TGFBR1 By similarity

Natural variations

Alternative sequence79 – 10830Missing in isoform Short.
VSP_021571

Experimental info

Sequence conflict421E → Q in AAB03612. Ref.1
Sequence conflict421E → Q in AAB62269. Ref.2

Sequences

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

Last modified November 14, 2006. Version 2.
Checksum: 31A2A36D463DB3E9

FASTA46752,266
        10         20         30         40         50         60 
MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK KLKKTGRLDE 

        70         80         90        100        110        120 
LEKAITTQNC NTKCVTIPST CSEIWGLSTA NTVDQWDTTG 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 (Deltaexon3) [UniParc].

Checksum: 0E2FF38B009D2F9E
Show »

FASTA43748,956

References

« Hide 'large scale' references
[1]"A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway."
Baker J.C., Harland R.M.
Genes Dev. 10:1880-1889(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Strain: 129/Sv.
[2]"Smad4 (homolog of human DPC4) and Smad2 (homolog of human JV18-1): candidates for murine lung tumor resistance and suppressor genes."
Devereux T.R., Anna C.H., Patel A.C., White C.M., Festing M.F., You M.
Carcinogenesis 18:1751-1755(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Strain: A/J and BALB/c.
[3]"Both SMAD2 and SMAD3 mediate activin-stimulated expression of the follicle-stimulating hormone beta subunit in mouse gonadotrope cells."
Bernard D.J.
Mol. Endocrinol. 18:606-623(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Strain: C57BL/6J.
Tissue: Pancreas.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
[6]"Functions of mammalian Smad genes as revealed by targeted gene disruption in mice."
Weinstein M., Yang X., Deng C.-X.
Cytokine Growth Factor Rev. 11:49-58(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[7]"Cytoplasmic PML function in TGF-beta signalling."
Lin H.K., Bergmann S., Pandolfi P.P.
Nature 431:205-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH PML AND ZFYVE9/SARA.
[8]"Negative regulation of transforming growth factor-beta (TGF-beta) signaling by WW domain-containing protein 1 (WWP1)."
Komuro A., Imamura T., Saitoh M., Yoshida Y., Yamori T., Miyazono K., Miyazawa K.
Oncogene 23:6914-6923(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WWP1.
[9]"Mice exclusively expressing the short isoform of Smad2 develop normally and are viable and fertile."
Dunn N.R., Koonce C.H., Anderson D.C., Islam A., Bikoff E.K., Robertson E.J.
Genes Dev. 19:152-163(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM SHORT).
[10]"Transforming growth factor-beta 1 inhibits non-pathogenic Gram negative bacteria-induced NF-kappa B recruitment to the interleukin-6 gene promoter in intestinal epithelial cells through modulation of histone acetylation."
Haller D., Holt L., Kim S.C., Schwabe R.F., Sartor R.B., Jobin C.
J. Biol. Chem. 278:23851-23860(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-465 AND SER-467.
[11]"Identification and characterization of a PDZ protein that interacts with activin types II receptors."
Shoji H., Tsuchida K., Kishi H., Yamakawa N., Matsuzaki T., Liu Z., Nakamura T., Sugino H.
J. Biol. Chem. 275:5485-5492(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AIP1.
[12]"Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling through cooperation with SARA."
Miura S., Takeshita T., Asao H., Kimura Y., Murata K., Sasaki Y., Hanai J., Beppu H., Tsukazaki T., Wrana J.L., Miyazono K., Sugamura K.
Mol. Cell. Biol. 20:9346-9355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HGS.
[13]"NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-beta (transforming growth factor-beta) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta type I receptor."
Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K., Miyazono K., Imamura T.
Biochem. J. 386:461-470(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEDD4L, UBIQUITINATION.
[14]"Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway."
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.
Cell. Signal. 24:1999-2006(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP5C, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U60530 mRNA. Translation: AAB03612.1.
AF005743 mRNA. Translation: AAB62269.1.
AK007817 mRNA. Translation: BAB25282.1.
AY334552 mRNA. Translation: AAR00933.1.
BC021342 mRNA. Translation: AAH21342.1.
BC089184 mRNA. Translation: AAH89184.1.
CCDSCCDS29350.1. [Q62432-1]
RefSeqNP_001239410.1. NM_001252481.1. [Q62432-1]
NP_034884.2. NM_010754.5. [Q62432-1]
XP_006525762.1. XM_006525699.1. [Q62432-1]
XP_006525763.1. XM_006525700.1. [Q62432-2]
UniGeneMm.152699.
Mm.490934.

3D structure databases

ProteinModelPortalQ62432.
SMRQ62432. Positions 7-172, 265-467.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201275. 35 interactions.
IntActQ62432. 4 interactions.
MINTMINT-99148.

PTM databases

PhosphoSiteQ62432.

Proteomic databases

MaxQBQ62432.
PaxDbQ62432.
PRIDEQ62432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025453; ENSMUSP00000025453; ENSMUSG00000024563. [Q62432-1]
ENSMUST00000091831; ENSMUSP00000089439; ENSMUSG00000024563. [Q62432-2]
ENSMUST00000168423; ENSMUSP00000130115; ENSMUSG00000024563. [Q62432-1]
GeneID17126.
KEGGmmu:17126.
UCSCuc008fqn.2. mouse. [Q62432-1]
uc008fqo.2. mouse. [Q62432-2]

Organism-specific databases

CTD4087.
MGIMGI:108051. Smad2.

Phylogenomic databases

eggNOGNOG320700.
GeneTreeENSGT00600000084186.
HOGENOMHOG000286018.
HOVERGENHBG053353.
InParanoidQ62432.
KOK04500.
OMAMNQSMDT.
OrthoDBEOG7W1540.
PhylomeDBQ62432.
TreeFamTF314923.

Gene expression databases

ArrayExpressQ62432.
BgeeQ62432.
CleanExMM_SMAD2.
GenevestigatorQ62432.

Family and domain databases

Gene3D2.60.200.10. 1 hit.
3.90.520.10. 1 hit.
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]
PANTHERPTHR13703. PTHR13703. 1 hit.
PfamPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 2 hits.
PROSITEPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio291308.
PROQ62432.
SOURCESearch...

Entry information

Entry nameSMAD2_MOUSE
AccessionPrimary (citable) accession number: Q62432
Secondary accession number(s): Q6GU18, Q6VP00, Q9D8P6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 14, 2006
Last modified: July 9, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot