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Q62432

- SMAD2_MOUSE

UniProt

Q62432 - SMAD2_MOUSE

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Protein

Mothers against decapentaplegic homolog 2

Gene

Smad2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi74 – 741ZincBy similarity
Metal bindingi149 – 1491ZincBy similarity
Metal bindingi161 – 1611ZincBy similarity
Metal bindingi166 – 1661ZincBy similarity

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. double-stranded DNA binding Source: MGI
  3. metal ion binding Source: UniProtKB-KW
  4. sequence-specific DNA binding transcription factor activity Source: InterPro
  5. SMAD binding Source: UniProtKB
  6. transcription factor binding Source: UniProtKB
  7. transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity Source: Ensembl

GO - Biological processi

  1. anterior/posterior pattern specification Source: MGI
  2. cell fate commitment Source: MGI
  3. common-partner SMAD protein phosphorylation Source: MGI
  4. developmental growth Source: MGI
  5. embryonic cranial skeleton morphogenesis Source: MGI
  6. embryonic foregut morphogenesis Source: MGI
  7. embryonic pattern specification Source: MGI
  8. endoderm development Source: MGI
  9. endoderm formation Source: MGI
  10. gastrulation Source: MGI
  11. heart development Source: MGI
  12. insulin secretion Source: MGI
  13. intracellular signal transduction Source: MGI
  14. in utero embryonic development Source: MGI
  15. lung development Source: MGI
  16. mesoderm formation Source: MGI
  17. negative regulation of cell proliferation Source: Ensembl
  18. negative regulation of gene expression Source: MGI
  19. negative regulation of transcription, DNA-templated Source: Ensembl
  20. nodal signaling pathway Source: Ensembl
  21. organ growth Source: MGI
  22. palate development Source: BHF-UCL
  23. pancreas development Source: MGI
  24. paraxial mesoderm morphogenesis Source: MGI
  25. pattern specification process Source: MGI
  26. pericardium development Source: MGI
  27. positive regulation of BMP signaling pathway Source: Ensembl
  28. positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  29. positive regulation of gene expression Source: MGI
  30. positive regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry Source: Ensembl
  31. positive regulation of transcription, DNA-templated Source: BHF-UCL
  32. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  33. post-embryonic development Source: MGI
  34. protein phosphorylation Source: MGI
  35. regulation of binding Source: MGI
  36. regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  37. response to cholesterol Source: Ensembl
  38. response to glucose Source: MGI
  39. signal transduction involved in regulation of gene expression Source: Ensembl
  40. SMAD protein complex assembly Source: Ensembl
  41. SMAD protein signal transduction Source: MGI
  42. transcription, DNA-templated Source: UniProtKB-KW
  43. transforming growth factor beta receptor signaling pathway Source: MGI
  44. ureteric bud development Source: UniProtKB
  45. zygotic specification of dorsal/ventral axis Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_202264. SMAD4 MH2 Domain Mutants in Cancer.
REACT_203510. TGF-beta receptor signaling activates SMADs.
REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_215733. Downregulation of TGF-beta receptor signaling.
REACT_216222. Transcriptional regulation of pluripotent stem cells.
REACT_216258. Signaling by Activin.
REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_217958. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_220645. Signaling by NODAL.
REACT_224802. TGFBR1 KD Mutants in Cancer.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Smad2
Synonyms:Madh2, Madr2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:108051. Smad2.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. activin responsive factor complex Source: Ensembl
  2. cytoplasm Source: BHF-UCL
  3. nuclear chromatin Source: Ensembl
  4. nucleus Source: UniProtKB
  5. SMAD2-SMAD3 protein complex Source: Ensembl
  6. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 467466Mothers against decapentaplegic homolog 2PRO_0000090853Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei8 – 81PhosphothreonineBy similarity
Modified residuei19 – 191N6-acetyllysineBy similarity
Modified residuei240 – 2401Phosphoserine; by CAMK2PROSITE-ProRule annotation
Modified residuei458 – 4581PhosphoserinePROSITE-ProRule annotation
Modified residuei460 – 4601PhosphoserinePROSITE-ProRule annotation
Modified residuei464 – 4641PhosphoserinePROSITE-ProRule annotation
Modified residuei465 – 4651Phosphoserine; by TGFBR1PROSITE-ProRule annotation
Modified residuei467 – 4671Phosphoserine; by TGFBR1PROSITE-ProRule annotation

Post-translational modificationi

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 PDPK1.2 Publications
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).By similarity
Acetylated on Lys-19 by coactivators in response to TGF-beta signaling, which increases transcriptional activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ62432.
PaxDbiQ62432.
PRIDEiQ62432.

PTM databases

PhosphoSiteiQ62432.

Expressioni

Gene expression databases

BgeeiQ62432.
CleanExiMM_SMAD2.
ExpressionAtlasiQ62432. baseline and differential.
GenevestigatoriQ62432.

Interactioni

Subunit structurei

Momomer; the absence of TGF-beta. Interacts with ZNF580. Heterodimer; in the presence of TGF-beta. Forms a heterodimer with co-SMAD, SMAD4, in the nucleus to form the transactivation complex SMAD2/SMAD4. 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 of the TGF-beta signaling. 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. Interacts with LDLRAD4 (via the SMAD interaction motif). Interacts (via MH2 domain) with PMEPA1 (via the SMAD interaction motif).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Smad4P974713EBI-2337932,EBI-5259270

Protein-protein interaction databases

BioGridi201275. 35 interactions.
IntActiQ62432. 4 interactions.
MINTiMINT-99148.

Structurei

3D structure databases

ProteinModelPortaliQ62432.
SMRiQ62432. Positions 7-172, 265-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 176167MH1PROSITE-ProRule annotationAdd
BLAST
Domaini274 – 467194MH2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi221 – 2255PY-motifBy similarity

Sequence similaritiesi

Belongs to the dwarfin/SMAD family.Curated
Contains 1 MH1 (MAD homology 1) domain.PROSITE-ProRule annotation
Contains 1 MH2 (MAD homology 2) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG320700.
GeneTreeiENSGT00760000119091.
HOGENOMiHOG000286018.
HOVERGENiHBG053353.
InParanoidiQ62432.
KOiK04500.
OMAiMNQSMDT.
OrthoDBiEOG7W1540.
PhylomeDBiQ62432.
TreeFamiTF314923.

Family and domain databases

Gene3Di2.60.200.10. 1 hit.
3.90.520.10. 1 hit.
InterProiIPR013790. 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]
PANTHERiPTHR13703. PTHR13703. 1 hit.
PfamiPF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view]
SMARTiSM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 2 hits.
PROSITEiPS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

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) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK
60 70 80 90 100
KLKKTGRLDE LEKAITTQNC NTKCVTIPST CSEIWGLSTA NTVDQWDTTG
110 120 130 140 150
LYSFSEQTRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELKAIENCE
160 170 180 190 200
YAFNLKKDEV CVNPYHYQRV ETPVLPPVLV PRHTEILTEL PPLDDYTHSI
210 220 230 240 250
PENTNFPAGI EPQSNYIPET PPPGYISEDG ETSDQQLNQS MDTGSPAELS
260 270 280 290 300
PTTLSPVNHS LDLQPVTYSE PAFWCSIAYY ELNQRVGETF HASQPSLTVD
310 320 330 340 350
GFTDPSNSER FCLGLLSNVN RNATVEMTRR HIGRGVRLYY IGGEVFAECL
360 370 380 390 400
SDSAIFVQSP NCNQRYGWHP ATVCKIPPGC NLKIFNNQEF AALLAQSVNQ
410 420 430 440 450
GFEAVYQLTR MCTIRMSFVK GWGAEYRRQT VTSTPCWIEL HLNGPLQWLD
460
KVLTQMGSPS VRCSSMS
Length:467
Mass (Da):52,266
Last modified:November 14, 2006 - v2
Checksum:i31A2A36D463DB3E9
GO
Isoform Short (identifier: Q62432-2) [UniParc]FASTAAdd to Basket

Also known as: Deltaexon3

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

Show »
Length:437
Mass (Da):48,956
Checksum:i0E2FF38B009D2F9E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421E → Q in AAB03612. (PubMed:8756346)Curated
Sequence conflicti42 – 421E → Q in AAB62269. (PubMed:9328171)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei79 – 10830Missing in isoform Short. 1 PublicationVSP_021571Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29350.1. [Q62432-1]
RefSeqiNP_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]
UniGeneiMm.152699.
Mm.490934.

Genome annotation databases

EnsembliENSMUST00000025453; ENSMUSP00000025453; ENSMUSG00000024563. [Q62432-1]
ENSMUST00000091831; ENSMUSP00000089439; ENSMUSG00000024563. [Q62432-2]
ENSMUST00000168423; ENSMUSP00000130115; ENSMUSG00000024563. [Q62432-1]
GeneIDi17126.
KEGGimmu:17126.
UCSCiuc008fqn.2. mouse. [Q62432-1]
uc008fqo.2. mouse. [Q62432-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS29350.1. [Q62432-1 ]
RefSeqi NP_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 ]
UniGenei Mm.152699.
Mm.490934.

3D structure databases

ProteinModelPortali Q62432.
SMRi Q62432. Positions 7-172, 265-467.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201275. 35 interactions.
IntActi Q62432. 4 interactions.
MINTi MINT-99148.

PTM databases

PhosphoSitei Q62432.

Proteomic databases

MaxQBi Q62432.
PaxDbi Q62432.
PRIDEi Q62432.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025453 ; ENSMUSP00000025453 ; ENSMUSG00000024563 . [Q62432-1 ]
ENSMUST00000091831 ; ENSMUSP00000089439 ; ENSMUSG00000024563 . [Q62432-2 ]
ENSMUST00000168423 ; ENSMUSP00000130115 ; ENSMUSG00000024563 . [Q62432-1 ]
GeneIDi 17126.
KEGGi mmu:17126.
UCSCi uc008fqn.2. mouse. [Q62432-1 ]
uc008fqo.2. mouse. [Q62432-2 ]

Organism-specific databases

CTDi 4087.
MGIi MGI:108051. Smad2.

Phylogenomic databases

eggNOGi NOG320700.
GeneTreei ENSGT00760000119091.
HOGENOMi HOG000286018.
HOVERGENi HBG053353.
InParanoidi Q62432.
KOi K04500.
OMAi MNQSMDT.
OrthoDBi EOG7W1540.
PhylomeDBi Q62432.
TreeFami TF314923.

Enzyme and pathway databases

Reactomei REACT_202264. SMAD4 MH2 Domain Mutants in Cancer.
REACT_203510. TGF-beta receptor signaling activates SMADs.
REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_215733. Downregulation of TGF-beta receptor signaling.
REACT_216222. Transcriptional regulation of pluripotent stem cells.
REACT_216258. Signaling by Activin.
REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_217958. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_220645. Signaling by NODAL.
REACT_224802. TGFBR1 KD Mutants in Cancer.

Miscellaneous databases

ChiTaRSi Smad2. mouse.
NextBioi 291308.
PROi Q62432.
SOURCEi Search...

Gene expression databases

Bgeei Q62432.
CleanExi MM_SMAD2.
ExpressionAtlasi Q62432. baseline and differential.
Genevestigatori Q62432.

Family and domain databases

Gene3Di 2.60.200.10. 1 hit.
3.90.520.10. 1 hit.
InterProi IPR013790. 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 ]
PANTHERi PTHR13703. PTHR13703. 1 hit.
Pfami PF03165. MH1. 1 hit.
PF03166. MH2. 1 hit.
[Graphical view ]
SMARTi SM00523. DWA. 1 hit.
SM00524. DWB. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF56366. SSF56366. 2 hits.
PROSITEi PS51075. MH1. 1 hit.
PS51076. MH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiSMAD2_MOUSE
AccessioniPrimary (citable) accession number: Q62432
Secondary accession number(s): Q6GU18, Q6VP00, Q9D8P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 14, 2006
Last modified: November 26, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3