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P04202

- TGFB1_MOUSE

UniProt

P04202 - TGFB1_MOUSE

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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

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929 By similarity
Add
BLAST
Chaini30 – 278249Latency-associated peptide
PRO_0000033766Add
BLAST
Chaini279 – 390112Transforming growth factor beta-1
PRO_0000033767Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 – 33Interchain (with C-1350 or C-1375 in LTBP1); in inactive form By 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 ↔ 294 By similarity
Disulfide bondi293 ↔ 356 By similarity
Disulfide bondi322 ↔ 387 By similarity
Disulfide bondi326 ↔ 389 By similarity
Disulfide bondi355 – 355Interchain By 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.4 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP04202.
SMRiP04202. Positions 30-390.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 7445Straightjacket domain By similarity
Add
BLAST
Regioni75 – 271197Arm domain By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi244 – 2463Cell attachment site Reviewed prediction

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.

Sequence similaritiesi

Belongs to the TGF-beta family.

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

« 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: September 3, 2014
This is version 160 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