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Q15796

- SMAD2_HUMAN

UniProt

Q15796 - SMAD2_HUMAN

Protein

Mothers against decapentaplegic homolog 2

Gene

SMAD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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.5 Publications

    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. activating transcription factor binding Source: UniProtKB
    2. chromatin binding Source: Ensembl
    3. co-SMAD binding Source: BHF-UCL
    4. double-stranded DNA binding Source: UniProtKB
    5. enhancer binding Source: BHF-UCL
    6. I-SMAD binding Source: BHF-UCL
    7. metal ion binding Source: UniProtKB-KW
    8. phosphatase binding Source: UniProtKB
    9. protein binding Source: UniProtKB
    10. R-SMAD binding Source: BHF-UCL
    11. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    12. SMAD binding Source: UniProtKB
    13. transcription factor binding Source: UniProtKB
    14. transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity Source: BHF-UCL
    15. transforming growth factor beta receptor binding Source: BHF-UCL
    16. type I transforming growth factor beta receptor binding Source: BHF-UCL
    17. ubiquitin protein ligase binding Source: BHF-UCL

    GO - Biological processi

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

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_111057. Signaling by NODAL.
    REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_120850. TGF-beta receptor signaling activates SMADs.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_150238. Signaling by Activin.
    REACT_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_169107. SMAD4 MH2 Domain Mutants in Cancer.
    REACT_169165. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_169263. TGFBR1 KD Mutants in Cancer.
    REACT_200812. Transcriptional regulation of pluripotent stem cells.
    SignaLinkiQ15796.

    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):
    JV18-1
    Mad-related protein 2
    Short name:
    hMAD-2
    SMAD family member 2
    Short name:
    SMAD 2
    Short name:
    Smad2
    Short name:
    hSMAD2
    Gene namesi
    Name:SMAD2
    Synonyms:MADH2, MADR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:6768. SMAD2.

    Subcellular locationi

    Cytoplasm. Nucleus
    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.

    GO - Cellular componenti

    1. activin responsive factor complex Source: BHF-UCL
    2. cytoplasm Source: BHF-UCL
    3. cytosol Source: Reactome
    4. nuclear chromatin Source: BHF-UCL
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProtKB
    7. SMAD2-SMAD3 protein complex Source: BHF-UCL
    8. SMAD protein complex Source: UniProtKB
    9. transcription factor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191K → R: Loss of acetylation. 1 Publication
    Mutagenesisi20 – 201K → R: No effect on acetylation. 1 Publication
    Mutagenesisi221 – 2255Missing: Loss of binding to SMURF2.
    Mutagenesisi368 – 3681W → A: Loss of interaction with PMEPA1. 1 Publication
    Mutagenesisi381 – 3811N → S: Loss of binding to SARA. 1 Publication
    Mutagenesisi398 – 3981V → R: Increased binding to PPM1A. 1 Publication
    Mutagenesisi464 – 4641S → A: Loss of phosphorylation by TGFBR1; when associated with A-465 and A-467. 1 Publication
    Mutagenesisi465 – 4673SMS → AMA: Binds RANBP3. 2 Publications
    Mutagenesisi465 – 4673SMS → DMD: Greatly reduced RANBP2 binding. 2 Publications
    Mutagenesisi465 – 4651S → A: No change in binding to PPM1A. Loss of phosphorylation by TGFBR1; when associated with A-464 and A-467. 2 Publications
    Mutagenesisi465 – 4651S → D: No change in binding to PPM1A. 2 Publications
    Mutagenesisi467 – 4671S → A: No change in binding to PPM1A. Loss of phosphorylation by TGFBR1; when associated with A-464 and A-465. 2 Publications
    Mutagenesisi467 – 4671S → D: No change in binding to PPM1A. 2 Publications

    Organism-specific databases

    PharmGKBiPA134959722.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 467466Mothers against decapentaplegic homolog 2PRO_0000090852Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine6 Publications
    Modified residuei8 – 81Phosphothreonine; by MAPK33 Publications
    Modified residuei19 – 191N6-acetyllysine2 Publications
    Modified residuei220 – 2201Phosphothreonine1 Publication
    Modified residuei240 – 2401Phosphoserine; by CAMK21 PublicationPROSITE-ProRule annotation
    Modified residuei245 – 2451Phosphoserine1 Publication
    Modified residuei250 – 2501Phosphoserine1 Publication
    Modified residuei255 – 2551Phosphoserine1 Publication
    Modified residuei458 – 4581Phosphoserine2 PublicationsPROSITE-ProRule annotation
    Modified residuei460 – 4601Phosphoserine1 PublicationPROSITE-ProRule annotation
    Modified residuei464 – 4641Phosphoserine1 PublicationPROSITE-ProRule annotation
    Modified residuei465 – 4651Phosphoserine; by TGFBR14 PublicationsPROSITE-ProRule annotation
    Modified residuei467 – 4671Phosphoserine; by TGFBR14 PublicationsPROSITE-ProRule annotation

    Post-translational modificationi

    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. TGF-beta-induced Ser-465/467 phosphorylation declines progressively in a SETD8-dependent manner. 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. Phosphorylated by PDPK1.11 Publications
    In response to TGF-beta, ubiquitinated by NEDD4L; which promotes its degradation By similarity. Monoubiquitinated, leading to prevent DNA-binding. Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes.By similarity1 Publication
    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. Acetylation in the nucleus by EP300 is enhanced by TGF-beta.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15796.
    PaxDbiQ15796.
    PRIDEiQ15796.

    PTM databases

    PhosphoSiteiQ15796.

    Expressioni

    Tissue specificityi

    Expressed at high levels in skeletal muscle, endothelial cells, heart and placenta.1 Publication

    Gene expression databases

    ArrayExpressiQ15796.
    BgeeiQ15796.
    CleanExiHS_SMAD2.
    GenevestigatoriQ15796.

    Organism-specific databases

    HPAiCAB025507.

    Interactioni

    Subunit structurei

    Momomer; the absence of TGF-beta. Heterodimer; in the presence of TGF-beta. Forms a heterodimer with co-SMAD, SMAD4, in the nucleus to form the transactivation complex SMAD2/SMAD4. Interacts with AIP1, HGS, PML and WWP1 By similarity. Interacts with NEDD4L in response to TGF-beta 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 with SKOR1 and SKOR2. Interacts with PRDM16. Interacts (via MH2 domain) with LEMD3. Interacts with RBPMS. Interacts with WWP1. 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 PDPK1 (via PH domain). Interacts with DAB2; the interactions are enhanced upon TGF-beta stimulation. Interacts with USP15. Interacts with PPP5C. Interacts with ZNF580. Interacts with LDLRAD4 (via the SMAD interaction motif). Interacts (via MH2 domain) with PMEPA1 (via the SMAD interaction motif).By similarity26 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ANK3Q129552EBI-1040141,EBI-2691178
    CHGBP050602EBI-1040141,EBI-712619
    DAB2P980824EBI-1040141,EBI-1171238
    DOCK9Q9BZ293EBI-1040141,EBI-2695893
    MTMR4Q9NYA43EBI-1040141,EBI-1052346
    NEFMP071973EBI-1040141,EBI-1105035
    OLIG1Q8TAK62EBI-1040141,EBI-3867416
    PPM1AP358132EBI-1040141,EBI-989143
    RANBP3Q9H6Z42EBI-1040141,EBI-992681
    RHOAP615862EBI-1040141,EBI-446668
    SMAD3P840222EBI-1040141,EBI-347161
    SMAD4Q1348518EBI-1040141,EBI-347263
    SMURF2Q9HAU45EBI-1040141,EBI-396727
    SNW1Q135733EBI-1040141,EBI-632715
    TP53P046374EBI-1040141,EBI-366083
    TP63Q9H3D43EBI-1040141,EBI-2337775
    TRIM33Q9UPN96EBI-1040141,EBI-2214398
    WWP2O003084EBI-1040141,EBI-743923
    ZFRQ96KR12EBI-1040141,EBI-2513582
    ZFYVE9O954052EBI-1040141,EBI-296817

    Protein-protein interaction databases

    BioGridi110262. 256 interactions.
    DIPiDIP-29716N.
    IntActiQ15796. 207 interactions.
    MINTiMINT-5006109.
    STRINGi9606.ENSP00000262160.

    Structurei

    Secondary structure

    1
    467
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi264 – 2674
    Beta strandi274 – 2818
    Beta strandi290 – 2923
    Beta strandi294 – 3029
    Beta strandi305 – 3073
    Beta strandi310 – 3123
    Helixi313 – 3153
    Helixi323 – 3297
    Turni330 – 3345
    Beta strandi336 – 3416
    Beta strandi344 – 3496
    Beta strandi351 – 3533
    Beta strandi355 – 3584
    Helixi360 – 3656
    Beta strandi374 – 3763
    Beta strandi381 – 3866
    Helixi387 – 39711
    Helixi398 – 4003
    Helixi402 – 4065
    Helixi407 – 4126
    Beta strandi413 – 4197
    Beta strandi423 – 4275
    Helixi431 – 4333
    Beta strandi434 – 4429
    Helixi443 – 45311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DEVX-ray2.20A/C261-456[»]
    1KHXX-ray1.80A241-467[»]
    1U7VX-ray2.70A/C270-467[»]
    2LB3NMR-B217-224[»]
    ProteinModelPortaliQ15796.
    SMRiQ15796. Positions 7-172, 265-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15796.

    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-motif

    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.
    HOGENOMiHOG000286018.
    HOVERGENiHBG053353.
    InParanoidiQ15796.
    KOiK04500.
    OMAiMNQSMDT.
    OrthoDBiEOG7W1540.
    PhylomeDBiQ15796.
    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

    Isoform Long (identifier: Q15796-1) [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

    MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK    50
    KLKKTGRLDE LEKAITTQNC NTKCVTIPST CSEIWGLSTP NTIDQWDTTG 100
    LYSFSEQTRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELKAIENCE 150
    YAFNLKKDEV CVNPYHYQRV ETPVLPPVLV PRHTEILTEL PPLDDYTHSI 200
    PENTNFPAGI EPQSNYIPET PPPGYISEDG ETSDQQLNQS MDTGSPAELS 250
    PTTLSPVNHS LDLQPVTYSE PAFWCSIAYY ELNQRVGETF HASQPSLTVD 300
    GFTDPSNSER FCLGLLSNVN RNATVEMTRR HIGRGVRLYY IGGEVFAECL 350
    SDSAIFVQSP NCNQRYGWHP ATVCKIPPGC NLKIFNNQEF AALLAQSVNQ 400
    GFEAVYQLTR MCTIRMSFVK GWGAEYRRQT VTSTPCWIEL HLNGPLQWLD 450
    KVLTQMGSPS VRCSSMS 467
    Length:467
    Mass (Da):52,306
    Last modified:November 1, 1996 - v1
    Checksum:i95406DB5FC0AA4C9
    GO
    Isoform Short (identifier: Q15796-2) [UniParc]FASTAAdd to Basket

    Also known as: Smad2Deltaexon3

    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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti133 – 1331R → C in a colorectal carcinoma sample. 1 Publication
    VAR_011375
    Natural varianti300 – 3001D → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036473
    Natural varianti344 – 35815Missing in a colorectal carcinoma sample. 1 Publication
    VAR_011376Add
    BLAST
    Natural varianti440 – 4401L → R in a colorectal carcinoma sample. 1 Publication
    VAR_011377
    Natural varianti445 – 4451P → H in a colorectal carcinoma sample. 1 Publication
    VAR_011378
    Natural varianti450 – 4501D → E in a colorectal carcinoma sample. 1 Publication
    VAR_011379

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei79 – 10830Missing in isoform Short. CuratedVSP_006178Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11934.1. [Q15796-1]
    PIRiS71797.
    RefSeqiNP_001003652.1. NM_001003652.3. [Q15796-1]
    NP_005892.1. NM_005901.5. [Q15796-1]
    XP_005258316.1. XM_005258259.1. [Q15796-1]
    XP_006722514.1. XM_006722451.1. [Q15796-1]
    UniGeneiHs.12253.
    Hs.705764.
    Hs.741342.

    Genome annotation databases

    EnsembliENST00000262160; ENSP00000262160; ENSG00000175387. [Q15796-1]
    ENST00000356825; ENSP00000349282; ENSG00000175387. [Q15796-2]
    ENST00000402690; ENSP00000384449; ENSG00000175387. [Q15796-1]
    ENST00000586040; ENSP00000466193; ENSG00000175387. [Q15796-2]
    GeneIDi4087.
    KEGGihsa:4087.
    UCSCiuc002lcy.4. human. [Q15796-1]
    uc010xdc.3. human. [Q15796-2]

    Polymorphism databases

    DMDMi13633914.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11934.1. [Q15796-1 ]
    PIRi S71797.
    RefSeqi NP_001003652.1. NM_001003652.3. [Q15796-1 ]
    NP_005892.1. NM_005901.5. [Q15796-1 ]
    XP_005258316.1. XM_005258259.1. [Q15796-1 ]
    XP_006722514.1. XM_006722451.1. [Q15796-1 ]
    UniGenei Hs.12253.
    Hs.705764.
    Hs.741342.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 270-467 [» ]
    2LB3 NMR - B 217-224 [» ]
    ProteinModelPortali Q15796.
    SMRi Q15796. Positions 7-172, 265-467.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110262. 256 interactions.
    DIPi DIP-29716N.
    IntActi Q15796. 207 interactions.
    MINTi MINT-5006109.
    STRINGi 9606.ENSP00000262160.

    Chemistry

    ChEMBLi CHEMBL2396512.

    PTM databases

    PhosphoSitei Q15796.

    Polymorphism databases

    DMDMi 13633914.

    Proteomic databases

    MaxQBi Q15796.
    PaxDbi Q15796.
    PRIDEi Q15796.

    Protocols and materials databases

    DNASUi 4087.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262160 ; ENSP00000262160 ; ENSG00000175387 . [Q15796-1 ]
    ENST00000356825 ; ENSP00000349282 ; ENSG00000175387 . [Q15796-2 ]
    ENST00000402690 ; ENSP00000384449 ; ENSG00000175387 . [Q15796-1 ]
    ENST00000586040 ; ENSP00000466193 ; ENSG00000175387 . [Q15796-2 ]
    GeneIDi 4087.
    KEGGi hsa:4087.
    UCSCi uc002lcy.4. human. [Q15796-1 ]
    uc010xdc.3. human. [Q15796-2 ]

    Organism-specific databases

    CTDi 4087.
    GeneCardsi GC18M045357.
    HGNCi HGNC:6768. SMAD2.
    HPAi CAB025507.
    MIMi 601366. gene.
    neXtProti NX_Q15796.
    PharmGKBi PA134959722.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG320700.
    HOGENOMi HOG000286018.
    HOVERGENi HBG053353.
    InParanoidi Q15796.
    KOi K04500.
    OMAi MNQSMDT.
    OrthoDBi EOG7W1540.
    PhylomeDBi Q15796.
    TreeFami TF314923.

    Enzyme and pathway databases

    Reactomei REACT_111057. Signaling by NODAL.
    REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_120850. TGF-beta receptor signaling activates SMADs.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_150238. Signaling by Activin.
    REACT_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_169107. SMAD4 MH2 Domain Mutants in Cancer.
    REACT_169165. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_169263. TGFBR1 KD Mutants in Cancer.
    REACT_200812. Transcriptional regulation of pluripotent stem cells.
    SignaLinki Q15796.

    Miscellaneous databases

    ChiTaRSi SMAD2. human.
    EvolutionaryTracei Q15796.
    GeneWikii Mothers_against_decapentaplegic_homolog_2.
    GenomeRNAii 4087.
    NextBioi 16020.
    PROi Q15796.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15796.
    Bgeei Q15796.
    CleanExi HS_SMAD2.
    Genevestigatori Q15796.

    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

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT 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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PHOSPHORYLATION BY TGFBR1, VARIANTS 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Chronic myeloid leukemia cell.
    8. "MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling."
      Macias-Silva M., Abdollah S., Hoodless P.A., Pirone R., Attisano L., Wrana J.L.
      Cell 87:1215-1224(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFBR1, PHOSPHORYLATION AT SER-464; SER-465 AND SER-467, MUTAGENESIS OF SER-464; SER-465 AND SER-467.
    9. "SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor."
      Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.
      Cell 95:779-791(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZFYVE9, SUBCELLULAR LOCATION.
    10. "Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors."
      Kawabata M., Inoue H., Hanyu A., Imamura T., Miyazono K.
      EMBO J. 17:4056-4065(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    11. "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] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS LONG AND SHORT).
    12. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-465 AND SER-467.
    13. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-465 AND SER-467 BY TGFBR1.
    14. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FOXH1.
      Tissue: Colon adenocarcinoma.
    15. "Roles of pathway-specific and inhibitory Smads in activin receptor signaling."
      Lebrun J.J., Takabe K., Chen Y., Vale W.
      Mol. Endocrinol. 13:15-23(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACVR1B, FUNCTION.
    16. "The adaptor molecule Disabled-2 links the transforming growth factor beta receptors to the Smad pathway."
      Hocevar B.A., Smine A., Xu X.X., Howe P.H.
      EMBO J. 20:2789-2801(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2.
    17. "Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription."
      Leong G.M., Subramaniam N., Figueroa J., Flanagan J.L., Hayman M.J., Eisman J.A., Kouzmenko A.P.
      J. Biol. Chem. 276:18243-18248(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNW1.
    18. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMURF2, MUTAGENESIS OF 221-PRO--TYR-225.
    19. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-240.
    20. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-8; THR-220; SER-245; SER-250 AND SER-255.
    21. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LEMD3.
    22. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LEMD3.
    23. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKOR2.
    24. Cited for: INTERACTION WITH PPM1A, DEPHOSPHORYLATION, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-398; SER-465 AND SER-467.
    25. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH SMAD3 AND TRIM33, INTERACTION WITH TRIM33.
    26. "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] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-19, MUTAGENESIS OF LYS-19 AND LYS-20.
    27. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBPMS.
    28. "3-Phosphoinositide-dependent PDK1 negatively regulates transforming growth factor-beta-induced signaling in a kinase-dependent manner through physical interaction with Smad proteins."
      Seong H.A., Jung H., Kim K.T., Ha H.
      J. Biol. Chem. 282:12272-12289(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION BY PDPK1, INTERACTION WITH PDPK1.
    29. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKOR1.
    30. "Smad3 is acetylated by p300/CBP to regulate its transactivation activity."
      Inoue Y., Itoh Y., Abe K., Okamoto T., Daitoku H., Fukamizu A., Onozaki K., Hayashi H.
      Oncogene 26:500-508(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION, FUNCTION.
    31. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. "TAZ controls Smad nucleocytoplasmic shuttling and regulates human embryonic stem-cell self-renewal."
      Varelas X., Sakuma R., Samavarchi-Tehrani P., Peerani R., Rao B.M., Dembowy J., Yaffe M.B., Zandstra P.W., Wrana J.L.
      Nat. Cell Biol. 10:837-848(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WWTR1.
    33. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    34. "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] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling."
      Dai F., Lin X., Chang C., Feng X.H.
      Dev. Cell 16:345-357(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RANBP3, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF 465-SER--SER-467.
    36. Cited for: INTERACTION WITH PRDM16.
    37. "TMEPAI, a transmembrane TGF-beta-inducible protein, sequesters Smad proteins from active participation in TGF-beta signaling."
      Watanabe Y., Itoh S., Goto T., Ohnishi E., Inamitsu M., Itoh F., Satoh K., Wiercinska E., Yang W., Shi L., Tanaka A., Nakano N., Mommaas A.M., Shibuya H., Ten Dijke P., Kato M.
      Mol. Cell 37:123-134(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PMEPA1, MUTAGENESIS OF TRP-368.
    38. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-458 AND SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "ZNF580, a novel C2H2 zinc-finger transcription factor, interacts with the TGF-beta signal molecule Smad2."
      Luo Y., Hu W., Xu R., Hou B., Zhang L., Zhang W.
      Cell Biol. Int. 35:1153-1157(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF580, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    41. Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP15, DNA-BINDING, INTERACTION WITH USP15.
    42. "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.
    43. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    44. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    45. "CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration."
      Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.
      Mol. Cell 49:1147-1158(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-465 AND SER-467.
    46. Cited for: INTERACTION WITH LDLRAD4.
    47. Cited for: REVIEW.
    48. "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] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    49. Cited for: REVIEW.
    50. Cited for: REVIEW.
    51. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 261-456 IN COMPLEX WITH ZFYVE9, INTERACTION WITH SARA, MUTAGENESIS OF ASN-381.
    52. "Structural basis of heteromeric smad protein assembly in TGF-beta signaling."
      Chacko B.M., Qin B.Y., Tiwari A., Shi G., Lam S., Hayward L.J., De Caestecker M., Lin K.
      Mol. Cell 15:813-823(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 270-466 IN COMPLEX WITH SMAD4, SUBUNIT.
    53. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-300.

    Entry informationi

    Entry nameiSMAD2_HUMAN
    AccessioniPrimary (citable) accession number: Q15796
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 172 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3