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Protein

Transforming growth factor beta-1

Gene

Tgfb1

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

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

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_252217. Transcriptional regulation of white adipocyte differentiation.
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. blood microparticle Source: MGI
  3. cell surface Source: BHF-UCL
  4. cytoplasm Source: UniProtKB
  5. extracellular matrix Source: MGI
  6. extracellular space Source: BHF-UCL
  7. microvillus Source: Ensembl
  8. neuronal cell body Source: Ensembl
  9. nucleus Source: UniProtKB
  10. proteinaceous extracellular matrix Source: MGI
  11. secretory granule Source: Ensembl
Complete GO annotation...

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

BgeeiP04202.
CleanExiMM_TGFB1.
ExpressionAtlasiP04202. baseline and differential.
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

        10         20         30         40         50
MPPSGLRLLP LLLPLPWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR
60 70 80 90 100
GQILSKLRLA SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESADPEPEPE
110 120 130 140 150
ADYYAKEVTR VLMVDRNNAI YEKTKDISHS IYMFFNTSDI REAVPEPPLL
160 170 180 190 200
SRAELRLQRL KSSVEQHVEL YQKYSNNSWR YLGNRLLTPT DTPEWLSFDV
210 220 230 240 250
TGVVRQWLNQ GDGIQGFRFS AHCSCDSKDN KLHVEINGIS PKRRGDLGTI
260 270 280 290 300
HDMNRPFLLL MATPLERAQH LHSSRHRRAL DTNYCFSSTE KNCCVRQLYI
310 320 330 340 350
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA
360 370 380 390
SASPCCVPQA LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS
Length:390
Mass (Da):44,310
Last modified:March 20, 1987 - v1
Checksum:i4381A51B711D689E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP04202.

Proteomic databases

PaxDbiP04202.
PRIDEiP04202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7040.
MGIiMGI:98725. Tgfb1.

Phylogenomic databases

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

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_252217. Transcriptional regulation of white adipocyte differentiation.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

NextBioi301176.
PMAP-CutDBP04202.
PROiP04202.
SOURCEiSearch...

Gene expression databases

BgeeiP04202.
CleanExiMM_TGFB1.
ExpressionAtlasiP04202. baseline and differential.
GenevestigatoriP04202.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 165 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.