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P04202

- TGFB1_MOUSE

UniProt

P04202 - TGFB1_MOUSE

Protein

Transforming growth factor beta-1

Gene

Tgfb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 1 (20 Mar 1987)
      Previous versions | rss
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    Functioni

    Multifunctional protein that controls proliferation, differentiation and other functions in many cell types. Many cells synthesize TGFB1 and have specific receptors for it. It positively and negatively regulates many other growth factors. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. transforming growth factor beta receptor binding Source: MGI
    3. type II transforming growth factor beta receptor binding Source: UniProtKB

    GO - Biological processi

    1. adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains Source: BHF-UCL
    2. aging Source: Ensembl
    3. ATP biosynthetic process Source: UniProtKB
    4. branch elongation involved in mammary gland duct branching Source: MGI
    5. cell activation Source: MGI
    6. cell-cell junction organization Source: UniProtKB
    7. cell cycle arrest Source: UniProtKB
    8. cell growth Source: InterPro
    9. cell proliferation Source: MGI
    10. cellular calcium ion homeostasis Source: MGI
    11. cellular response to dexamethasone stimulus Source: Ensembl
    12. cellular response to growth factor stimulus Source: MGI
    13. cellular response to organic cyclic compound Source: UniProtKB
    14. cellular response to transforming growth factor beta stimulus Source: MGI
    15. chondrocyte differentiation Source: UniProtKB
    16. common-partner SMAD protein phosphorylation Source: UniProtKB
    17. defense response Source: MGI
    18. defense response to fungus, incompatible interaction Source: Ensembl
    19. digestive tract development Source: Ensembl
    20. embryo development Source: Ensembl
    21. endoderm development Source: MGI
    22. epidermal growth factor receptor signaling pathway Source: UniProtKB
    23. epithelial to mesenchymal transition Source: Ensembl
    24. evasion or tolerance of host defenses by virus Source: UniProtKB
    25. extracellular matrix assembly Source: BHF-UCL
    26. extrinsic apoptotic signaling pathway Source: BHF-UCL
    27. face morphogenesis Source: UniProtKB
    28. female pregnancy Source: Ensembl
    29. frontal suture morphogenesis Source: Ensembl
    30. germ cell migration Source: MGI
    31. hematopoietic progenitor cell differentiation Source: UniProtKB
    32. hyaluronan catabolic process Source: UniProtKB
    33. inflammatory response Source: MGI
    34. inner ear development Source: Ensembl
    35. lens fiber cell differentiation Source: MGI
    36. lipopolysaccharide-mediated signaling pathway Source: UniProtKB
    37. lymph node development Source: MGI
    38. mammary gland branching involved in thelarche Source: MGI
    39. mammary gland development Source: MGI
    40. MAPK cascade Source: UniProtKB
    41. mitotic cell cycle checkpoint Source: UniProtKB
    42. mononuclear cell proliferation Source: MGI
    43. myelination Source: Ensembl
    44. myeloid dendritic cell differentiation Source: MGI
    45. negative regulation of blood vessel endothelial cell migration Source: UniProtKB
    46. negative regulation of cell-cell adhesion Source: UniProtKB
    47. negative regulation of cell cycle Source: UniProtKB
    48. negative regulation of cell growth Source: BHF-UCL
    49. negative regulation of cell proliferation Source: UniProtKB
    50. negative regulation of DNA replication Source: UniProtKB
    51. negative regulation of epithelial cell proliferation Source: UniProtKB
    52. negative regulation of fat cell differentiation Source: UniProtKB
    53. negative regulation of hyaluronan biosynthetic process Source: UniProtKB
    54. negative regulation of immune response Source: Ensembl
    55. negative regulation of macrophage cytokine production Source: Ensembl
    56. negative regulation of mitotic cell cycle Source: UniProtKB
    57. negative regulation of myoblast differentiation Source: UniProtKB
    58. negative regulation of neuroblast proliferation Source: Ensembl
    59. negative regulation of ossification Source: MGI
    60. negative regulation of phagocytosis Source: Ensembl
    61. negative regulation of protein phosphorylation Source: UniProtKB
    62. negative regulation of release of sequestered calcium ion into cytosol Source: Ensembl
    63. negative regulation of skeletal muscle tissue development Source: UniProtKB
    64. negative regulation of T cell activation Source: MGI
    65. negative regulation of T cell proliferation Source: MGI
    66. negative regulation of transcription, DNA-templated Source: UniProtKB
    67. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    68. organ morphogenesis Source: MGI
    69. organ regeneration Source: Ensembl
    70. ossification involved in bone remodeling Source: Ensembl
    71. pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
    72. phosphate-containing compound metabolic process Source: UniProtKB
    73. positive regulation of apoptotic process Source: Ensembl
    74. positive regulation of blood vessel endothelial cell migration Source: UniProtKB
    75. positive regulation of bone mineralization Source: Ensembl
    76. positive regulation of branching involved in ureteric bud morphogenesis Source: Ensembl
    77. positive regulation of cell cycle arrest Source: MGI
    78. positive regulation of cell division Source: UniProtKB-KW
    79. positive regulation of cell migration Source: UniProtKB
    80. positive regulation of cell proliferation Source: MGI
    81. positive regulation of cellular protein metabolic process Source: UniProtKB
    82. positive regulation of chemotaxis Source: UniProtKB
    83. positive regulation of collagen biosynthetic process Source: BHF-UCL
    84. positive regulation of epithelial cell proliferation Source: Ensembl
    85. positive regulation of epithelial to mesenchymal transition Source: MGI
    86. positive regulation of exit from mitosis Source: Ensembl
    87. positive regulation of fibroblast migration Source: UniProtKB
    88. positive regulation of gene expression Source: MGI
    89. positive regulation of histone acetylation Source: MGI
    90. positive regulation of histone deacetylation Source: MGI
    91. positive regulation of interleukin-17 production Source: BHF-UCL
    92. positive regulation of isotype switching to IgA isotypes Source: MGI
    93. positive regulation of MAP kinase activity Source: UniProtKB
    94. positive regulation of NAD+ ADP-ribosyltransferase activity Source: UniProtKB
    95. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    96. positive regulation of odontogenesis Source: MGI
    97. positive regulation of pathway-restricted SMAD protein phosphorylation Source: UniProtKB
    98. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
    99. positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
    100. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    101. positive regulation of protein complex assembly Source: UniProtKB
    102. positive regulation of protein dephosphorylation Source: UniProtKB
    103. positive regulation of protein kinase B signaling Source: UniProtKB
    104. positive regulation of protein localization to nucleus Source: MGI
    105. positive regulation of protein phosphorylation Source: UniProtKB
    106. positive regulation of protein secretion Source: UniProtKB
    107. positive regulation of SMAD protein import into nucleus Source: Ensembl
    108. positive regulation of smooth muscle cell differentiation Source: MGI
    109. positive regulation of superoxide anion generation Source: UniProtKB
    110. positive regulation of transcription, DNA-templated Source: MGI
    111. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    112. positive regulation of transcription regulatory region DNA binding Source: UniProtKB
    113. protein export from nucleus Source: UniProtKB
    114. protein import into nucleus, translocation Source: UniProtKB
    115. protein kinase B signaling Source: UniProtKB
    116. protein phosphorylation Source: MGI
    117. receptor catabolic process Source: UniProtKB
    118. regulation of actin cytoskeleton reorganization Source: MGI
    119. regulation of binding Source: MGI
    120. regulation of branching involved in mammary gland duct morphogenesis Source: MGI
    121. regulation of cartilage development Source: MGI
    122. regulation of cell proliferation Source: MGI
    123. regulation of DNA binding Source: MGI
    124. regulation of protein import into nucleus Source: MGI
    125. regulation of sodium ion transport Source: MGI
    126. regulation of striated muscle tissue development Source: MGI
    127. regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
    128. regulatory T cell differentiation Source: MGI
    129. response to cholesterol Source: UniProtKB
    130. response to drug Source: Ensembl
    131. response to estradiol Source: UniProtKB
    132. response to glucose Source: Ensembl
    133. response to hypoxia Source: Ensembl
    134. response to laminar fluid shear stress Source: Ensembl
    135. response to progesterone Source: UniProtKB
    136. response to radiation Source: Ensembl
    137. response to vitamin D Source: Ensembl
    138. salivary gland morphogenesis Source: Ensembl
    139. skeletal muscle tissue development Source: MGI
    140. skeletal system development Source: MGI
    141. SMAD protein complex assembly Source: UniProtKB
    142. SMAD protein import into nucleus Source: UniProtKB
    143. T cell activation Source: MGI
    144. T cell differentiation Source: MGI
    145. T cell homeostasis Source: MGI
    146. tolerance induction to self antigen Source: MGI
    147. transforming growth factor beta receptor signaling pathway Source: MGI
    148. ureteric bud development Source: UniProtKB
    149. wound healing Source: Ensembl

    Keywords - Molecular functioni

    Growth factor, Mitogen

    Enzyme and pathway databases

    ReactomeiREACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_196606. ECM proteoglycans.
    REACT_196644. Syndecan interactions.
    REACT_198998. Molecules associated with elastic fibres.
    REACT_203510. TGF-beta receptor signaling activates SMADs.
    REACT_209370. TGFBR2 MSI Frameshift Mutants in Cancer.
    REACT_215733. Downregulation of TGF-beta receptor signaling.
    REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_217958. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_224217. TGFBR1 LBD Mutants in Cancer.
    REACT_224787. TGFBR2 Kinase Domain Mutants in Cancer.
    REACT_224802. TGFBR1 KD Mutants in Cancer.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transforming growth factor beta-1
    Short name:
    TGF-beta-1
    Cleaved into the following chain:
    Gene namesi
    Name:Tgfb1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:98725. Tgfb1.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cell surface Source: BHF-UCL
    3. cytoplasm Source: UniProtKB
    4. extracellular matrix Source: MGI
    5. extracellular space Source: BHF-UCL
    6. microvillus Source: Ensembl
    7. neuronal cell body Source: Ensembl
    8. nucleus Source: UniProtKB
    9. proteinaceous extracellular matrix Source: MGI
    10. secretory granule Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929By similarityAdd
    BLAST
    Chaini30 – 278249Latency-associated peptidePRO_0000033766Add
    BLAST
    Chaini279 – 390112Transforming growth factor beta-1PRO_0000033767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi33 – 33Interchain (with C-1350 or C-1375 in LTBP1); in inactive formBy similarity
    Glycosylationi82 – 821N-linked (GlcNAc...)By similarity
    Glycosylationi136 – 1361N-linked (GlcNAc...)By similarity
    Glycosylationi176 – 1761N-linked (GlcNAc...)By similarity
    Disulfide bondi223 – 223Interchain (with C-225)By similarity
    Disulfide bondi225 – 225Interchain (with C-223)By similarity
    Disulfide bondi285 ↔ 294By similarity
    Disulfide bondi293 ↔ 356By similarity
    Disulfide bondi322 ↔ 387By similarity
    Disulfide bondi326 ↔ 389By similarity
    Disulfide bondi355 – 355InterchainBy similarity

    Post-translational modificationi

    Glycosylated.By similarity
    The precursor is cleaved into mature TGF-beta-1 and LAP, which remains non-covalently linked to mature TGF-beta-1 rendering it inactive.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP04202.
    PRIDEiP04202.

    PTM databases

    PhosphoSiteiP04202.

    Miscellaneous databases

    PMAP-CutDBP04202.

    Expressioni

    Gene expression databases

    ArrayExpressiP04202.
    BgeeiP04202.
    CleanExiMM_TGFB1.
    GenevestigatoriP04202.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked, or heterodimer with TGFB2 By similarity. Secreted and stored as a biologically inactive form in the extracellular matrix in a 290 kDa complex (large latent TGF-beta1 complex) containing the TGFB1 homodimer, the latency-associated peptide (LAP), and the latent TGFB1 binding protein-1 (LTBP1). The complex without LTBP1 is known as the'small latent TGF-beta1 complex'. Dissociation of the TGFB1 from LAP is required for growth factor activation and biological activity. Release of the large latent TGF-beta1 complex from the extracellular matrix is carried out by the matrix metalloproteinase MMP3 By similarity. Interacts with CD109 and DPT. Interacts with ASPN By similarity. May interact with THSD4; this interaction may lead to sequestration by FBN1 microfibril assembly and attenuation of TGFB signaling. Interacts with the serine proteases, HTRA1 and HTRA3: the interaction with either inhibits TGFB1-mediated signaling. The HTRA protease activity is required for this inhibition. Latency-associated peptide interacts with NREP; the interaction results in a decrease in TGFB1 autoinduction.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi204157. 4 interactions.
    DIPiDIP-48640N.
    STRINGi10090.ENSMUSP00000002678.

    Structurei

    3D structure databases

    ProteinModelPortaliP04202.
    SMRiP04202. Positions 30-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 7445Straightjacket domainBy similarityAdd
    BLAST
    Regioni75 – 271197Arm domainBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi244 – 2463Cell attachment siteSequence Analysis

    Domaini

    The 'straitjacket' and 'arm' domains encircle the growth factor monomers and are fastened together by strong bonding between Lys-56 and Tyr-103/Tyr-104. Activation of TGF-beta1 requires the binding of integrin alpha-V to an RGD sequence in the prodomain and exertion of force on this domain, which is held in the extracellular matrix by latent TGF-beta binding proteins. The sheer physical force unfastens the straitjacket and releases the active growth factor dimer By similarity.By similarity

    Sequence similaritiesi

    Belongs to the TGF-beta family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG279949.
    HOGENOMiHOG000290198.
    HOVERGENiHBG074115.
    InParanoidiP04202.
    KOiK13375.
    OMAiSHSIYMF.
    OrthoDBiEOG70GMFT.
    PhylomeDBiP04202.
    TreeFamiTF318514.

    Family and domain databases

    Gene3Di2.10.90.10. 1 hit.
    InterProiIPR029034. Cystine-knot_cytokine.
    IPR001839. TGF-b_C.
    IPR001111. TGF-b_N.
    IPR016319. TGF-beta.
    IPR015615. TGF-beta-rel.
    IPR003939. TGFb1.
    IPR017948. TGFb_CS.
    [Graphical view]
    PANTHERiPTHR11848. PTHR11848. 1 hit.
    PfamiPF00019. TGF_beta. 1 hit.
    PF00688. TGFb_propeptide. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001787. TGF-beta. 1 hit.
    PRINTSiPR01423. TGFBETA.
    PR01424. TGFBETA1.
    SMARTiSM00204. TGFB. 1 hit.
    [Graphical view]
    SUPFAMiSSF57501. SSF57501. 1 hit.
    PROSITEiPS00250. TGF_BETA_1. 1 hit.
    PS51362. TGF_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P04202-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPSGLRLLP LLLPLPWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR    50
    GQILSKLRLA SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESADPEPEPE 100
    ADYYAKEVTR VLMVDRNNAI YEKTKDISHS IYMFFNTSDI REAVPEPPLL 150
    SRAELRLQRL KSSVEQHVEL YQKYSNNSWR YLGNRLLTPT DTPEWLSFDV 200
    TGVVRQWLNQ GDGIQGFRFS AHCSCDSKDN KLHVEINGIS PKRRGDLGTI 250
    HDMNRPFLLL MATPLERAQH LHSSRHRRAL DTNYCFSSTE KNCCVRQLYI 300
    DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA 350
    SASPCCVPQA LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS 390
    Length:390
    Mass (Da):44,310
    Last modified:March 20, 1987 - v1
    Checksum:i4381A51B711D689E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13177 mRNA. Translation: AAA40423.1.
    L42462
    , L42456, L42457, L42458, L42459, L42460, L42461 Genomic DNA. Translation: AAB00138.1.
    AJ009862 mRNA. Translation: CAA08900.1.
    BC013738 mRNA. Translation: AAH13738.1.
    CCDSiCCDS20993.1.
    PIRiA01396. WFMS2.
    RefSeqiNP_035707.1. NM_011577.1.
    UniGeneiMm.248380.

    Genome annotation databases

    EnsembliENSMUST00000002678; ENSMUSP00000002678; ENSMUSG00000002603.
    GeneIDi21803.
    KEGGimmu:21803.
    UCSCiuc009ftq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13177 mRNA. Translation: AAA40423.1 .
    L42462
    , L42456 , L42457 , L42458 , L42459 , L42460 , L42461 Genomic DNA. Translation: AAB00138.1 .
    AJ009862 mRNA. Translation: CAA08900.1 .
    BC013738 mRNA. Translation: AAH13738.1 .
    CCDSi CCDS20993.1.
    PIRi A01396. WFMS2.
    RefSeqi NP_035707.1. NM_011577.1.
    UniGenei Mm.248380.

    3D structure databases

    ProteinModelPortali P04202.
    SMRi P04202. Positions 30-390.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204157. 4 interactions.
    DIPi DIP-48640N.
    STRINGi 10090.ENSMUSP00000002678.

    PTM databases

    PhosphoSitei P04202.

    Proteomic databases

    PaxDbi P04202.
    PRIDEi P04202.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000002678 ; ENSMUSP00000002678 ; ENSMUSG00000002603 .
    GeneIDi 21803.
    KEGGi mmu:21803.
    UCSCi uc009ftq.1. mouse.

    Organism-specific databases

    CTDi 7040.
    MGIi MGI:98725. Tgfb1.

    Phylogenomic databases

    eggNOGi NOG279949.
    HOGENOMi HOG000290198.
    HOVERGENi HBG074115.
    InParanoidi P04202.
    KOi K13375.
    OMAi SHSIYMF.
    OrthoDBi EOG70GMFT.
    PhylomeDBi P04202.
    TreeFami TF318514.

    Enzyme and pathway databases

    Reactomei REACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_196606. ECM proteoglycans.
    REACT_196644. Syndecan interactions.
    REACT_198998. Molecules associated with elastic fibres.
    REACT_203510. TGF-beta receptor signaling activates SMADs.
    REACT_209370. TGFBR2 MSI Frameshift Mutants in Cancer.
    REACT_215733. Downregulation of TGF-beta receptor signaling.
    REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_217958. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_224217. TGFBR1 LBD Mutants in Cancer.
    REACT_224787. TGFBR2 Kinase Domain Mutants in Cancer.
    REACT_224802. TGFBR1 KD Mutants in Cancer.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Miscellaneous databases

    NextBioi 301176.
    PMAP-CutDB P04202.
    PROi P04202.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04202.
    Bgeei P04202.
    CleanExi MM_TGFB1.
    Genevestigatori P04202.

    Family and domain databases

    Gene3Di 2.10.90.10. 1 hit.
    InterProi IPR029034. Cystine-knot_cytokine.
    IPR001839. TGF-b_C.
    IPR001111. TGF-b_N.
    IPR016319. TGF-beta.
    IPR015615. TGF-beta-rel.
    IPR003939. TGFb1.
    IPR017948. TGFb_CS.
    [Graphical view ]
    PANTHERi PTHR11848. PTHR11848. 1 hit.
    Pfami PF00019. TGF_beta. 1 hit.
    PF00688. TGFb_propeptide. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001787. TGF-beta. 1 hit.
    PRINTSi PR01423. TGFBETA.
    PR01424. TGFBETA1.
    SMARTi SM00204. TGFB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57501. SSF57501. 1 hit.
    PROSITEi PS00250. TGF_BETA_1. 1 hit.
    PS51362. TGF_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The murine transforming growth factor-beta precursor."
      Derynck R., Jarrett J.A., Chen E.Y., Goeddel D.V.
      J. Biol. Chem. 261:4377-4379(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular organization of the gene encoding murine transforming growth factor beta 1."
      Guron C., Sudarshan C., Raghow R.
      Gene 165:325-326(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
    3. "Transforming growth factor-beta 1 sequence and expression: no difference between NOD/Lt and C57Bl/6 mouse strains."
      Poirot L., Benoist C., Mathis D.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 and NOD/LT.
      Tissue: Spleen.
    4. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    5. "P311 binds to the latency associated protein and downregulates the expression of TGF-beta1 and TGF-beta2."
      Paliwal S., Shi J., Dhru U., Zhou Y., Schuger L.
      Biochem. Biophys. Res. Commun. 315:1104-1109(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NREP.
    6. "Developmentally regulated expression of mouse HtrA3 and its role as an inhibitor of TGF-beta signaling."
      Tocharus J., Tsuchiya A., Kajikawa M., Ueta Y., Oka C., Kawaichi M.
      Dev. Growth Differ. 46:257-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTRA3.
    7. Cited for: INTERACTION WITH HTRA1.
    8. "ADAMTSL6beta protein rescues fibrillin-1 microfibril disorder in a Marfan syndrome mouse model through the promotion of fibrillin-1 assembly."
      Saito M., Kurokawa M., Oda M., Oshima M., Tsutsui K., Kosaka K., Nakao K., Ogawa M., Manabe R., Suda N., Ganjargal G., Hada Y., Noguchi T., Teranaka T., Sekiguchi K., Yoneda T., Tsuji T.
      J. Biol. Chem. 286:38602-38613(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THSD4.
    9. "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: FUNCTION.

    Entry informationi

    Entry nameiTGFB1_MOUSE
    AccessioniPrimary (citable) accession number: P04202
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: March 20, 1987
    Last modified: October 1, 2014
    This is version 161 of the entry and version 1 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