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P01137

- TGFB1_HUMAN

UniProt

P01137 - TGFB1_HUMAN

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Protein
Transforming growth factor beta-1
Gene
TGFB1, TGFB
Organism
Homo sapiens (Human)
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.

GO - Molecular functioni

  1. antigen binding Source: UniProt
  2. cytokine activity Source: AgBase
  3. enzyme binding Source: BHF-UCL
  4. glycoprotein binding Source: UniProt
  5. protein binding Source: UniProtKB
  6. type II transforming growth factor beta receptor binding Source: BHF-UCL

GO - Biological processi

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

Keywords - Molecular functioni

Growth factor, Mitogen

Enzyme and pathway databases

ReactomeiREACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_120850. TGF-beta receptor signaling activates SMADs.
REACT_150331. Molecules associated with elastic fibres.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_169165. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_169192. TGFBR2 MSI Frameshift Mutants in Cancer.
REACT_169263. TGFBR1 KD Mutants in Cancer.
REACT_169440. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_169445. TGFBR1 LBD Mutants in Cancer.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_6213. Influenza Virus Induced Apoptosis.
SignaLinkiP01137.

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
Synonyms:TGFB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:11766. TGFB1.

Subcellular locationi

Secretedextracellular spaceextracellular matrix 1 Publication

GO - Cellular componenti

  1. Golgi lumen Source: Reactome
  2. axon Source: Ensembl
  3. blood microparticle Source: UniProt
  4. cell surface Source: BHF-UCL
  5. cytoplasm Source: BHF-UCL
  6. extracellular region Source: Reactome
  7. extracellular space Source: BHF-UCL
  8. neuronal cell body Source: Ensembl
  9. nucleus Source: BHF-UCL
  10. plasma membrane Source: Reactome
  11. platelet alpha granule lumen Source: Reactome
  12. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Camurati-Engelmann disease (CE) [MIM:131300]: Autosomal dominant disorder characterized by hyperostosis and sclerosis of the diaphyses of long bones. The disease typically presents in early childhood with pain, muscular weakness and waddling gait, and in some cases other features such as exophthalmos, facial paralysis, hearing difficulties and loss of vision.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti81 – 811Y → H in CE; leads to TGF-beta-1 intracellular accumulation. 2 Publications
VAR_017607
Natural varianti218 – 2181R → C in CE; higher levels of active TGF-beta-1 in the culture medium; enhances osteoclast formation in vitro. 4 Publications
VAR_017608
Natural varianti218 – 2181R → H in CE. 1 Publication
VAR_017609
Natural varianti222 – 2221H → D in CE; sporadic case; higher levels of active TGF-beta-1 in the culture medium. 1 Publication
VAR_017610
Natural varianti223 – 2231C → G in CE. 1 Publication
VAR_067303
Natural varianti223 – 2231C → R in CE. 1 Publication
VAR_067304
Natural varianti225 – 2251C → R in CE; higher levels of active TGF-beta-1 in the culture medium. 3 Publications
VAR_017611

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi131300. phenotype.
Orphaneti1328. Camurati-Engelmann disease.
586. Cystic fibrosis.
PharmGKBiPA350.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 Publication
Add
BLAST
Chaini30 – 278249Latency-associated peptide
PRO_0000033762Add
BLAST
Chaini279 – 390112Transforming growth factor beta-1
PRO_0000033763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 – 33Interchain (with C-1359 or C-1384 in LTBP1); in inactive form By similarity
Glycosylationi82 – 821N-linked (GlcNAc...)2 Publications
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
Disulfide bondi293 ↔ 356
Disulfide bondi322 ↔ 387
Disulfide bondi326 ↔ 389
Disulfide bondi355 – 355Interchain

Post-translational modificationi

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

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP01137.
PaxDbiP01137.
PRIDEiP01137.

2D gel databases

OGPiP01137.

PTM databases

PhosphoSiteiP01137.

Expressioni

Tissue specificityi

Highly expressed in bone. Abundantly expressed in articular cartilage and chondrocytes and is increased in osteoarthritis (OA). Colocalizes with ASPN in chondrocytes within OA lesions of articular cartilage.2 Publications

Inductioni

Activated in vitro at pH below 3.5 and over 12.5.

Gene expression databases

ArrayExpressiP01137.
BgeeiP01137.
CleanExiHS_TGFB1.
GenevestigatoriP01137.

Organism-specific databases

HPAiCAB000361.
HPA047516.

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. 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 By similarity. Latency-associated peptide interacts with NREP; the interaction results in a decrease in TGFB1 autoinduction By similarity. Interacts with CD109, DPT and ASPN.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPP050672EBI-779636,EBI-77613
DIP2AQ146892EBI-779636,EBI-2564275
ENGP178132EBI-779636,EBI-2834630
FSTL1Q128412EBI-779636,EBI-2349801
TGFBR1P368972EBI-779636,EBI-1027557
TGFBR2P371736EBI-779636,EBI-296151
TGFBR3Q031672EBI-779636,EBI-2852679
TGFBR3Q909982EBI-779636,EBI-6620843From a different organism.
THBS1P079962EBI-779636,EBI-2530274

Protein-protein interaction databases

BioGridi112898. 32 interactions.
DIPiDIP-5934N.
IntActiP01137. 18 interactions.
MINTiMINT-6806111.
STRINGi9606.ENSP00000221930.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi282 – 2854
Beta strandi291 – 2966
Beta strandi299 – 3013
Helixi302 – 3065
Beta strandi311 – 3133
Beta strandi315 – 3184
Beta strandi321 – 3244
Beta strandi330 – 3323
Helixi335 – 34612
Beta strandi347 – 3493
Beta strandi356 – 37015
Beta strandi373 – 38917

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KLANMR-A/B279-390[»]
1KLCNMR-A/B279-390[»]
1KLDNMR-A/B279-390[»]
3KFDX-ray3.00A/B/C/D279-390[»]
ProteinModelPortaliP01137.
SMRiP01137. Positions 30-390.

Miscellaneous databases

EvolutionaryTraceiP01137.

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.
InParanoidiP01137.
KOiK13375.
PhylomeDBiP01137.
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.

P01137-1 [UniParc]FASTAAdd to Basket

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MPPSGLRLLL LLLPLLWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR    50
GQILSKLRLA SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESAEPEPEPE 100
ADYYAKEVTR VLMVETHNEI YDKFKQSTHS IYMFFNTSEL REAVPEPVLL 150
SRAELRLLRL KLKVEQHVEL YQKYSNNSWR YLSNRLLAPS DSPEWLSFDV 200
TGVVRQWLSR GGEIEGFRLS AHCSCDSRDN TLQVDINGFT TGRRGDLATI 250
HGMNRPFLLL MATPLERAQH LQSSRHRRAL DTNYCFSSTE KNCCVRQLYI 300
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA 350
SAAPCCVPQA LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS 390
Length:390
Mass (Da):44,341
Last modified:February 1, 1991 - v2
Checksum:i75391614250288FE
GO

Polymorphismi

In post-menopausal Japanese women, the frequency of Leu-10 is higher in subjects with osteoporosis than in controls.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101L → P Associated with higher bone mineral density and lower frequency of vertebral fractures in Japanese post-menopausal women. 3 Publications
Corresponds to variant rs1800470 [ dbSNP | Ensembl ].
VAR_016171
Natural varianti25 – 251R → P.1 Publication
Corresponds to variant rs1800471 [ dbSNP | Ensembl ].
VAR_016172
Natural varianti81 – 811Y → H in CE; leads to TGF-beta-1 intracellular accumulation. 2 Publications
VAR_017607
Natural varianti218 – 2181R → C in CE; higher levels of active TGF-beta-1 in the culture medium; enhances osteoclast formation in vitro. 4 Publications
VAR_017608
Natural varianti218 – 2181R → H in CE. 1 Publication
VAR_017609
Natural varianti222 – 2221H → D in CE; sporadic case; higher levels of active TGF-beta-1 in the culture medium. 1 Publication
VAR_017610
Natural varianti223 – 2231C → G in CE. 1 Publication
VAR_067303
Natural varianti223 – 2231C → R in CE. 1 Publication
VAR_067304
Natural varianti225 – 2251C → R in CE; higher levels of active TGF-beta-1 in the culture medium. 3 Publications
VAR_017611
Natural varianti263 – 2631T → I.
Corresponds to variant rs1800472 [ dbSNP | Ensembl ].
VAR_016173

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591R → RR in CAA26580. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05839
, X05840, X05843, X05844, X05849, X05850 Genomic DNA. Translation: CAA29283.1.
X02812 mRNA. Translation: CAA26580.1.
BT007245 mRNA. Translation: AAP35909.1.
AK291907 mRNA. Translation: BAF84596.1.
CH471126 Genomic DNA. Translation: EAW57032.1.
BC001180 mRNA. Translation: AAH01180.1.
BC000125 mRNA. Translation: AAH00125.1.
BC022242 mRNA. Translation: AAH22242.1.
M38449 mRNA. Translation: AAA36735.1.
CCDSiCCDS33031.1.
PIRiA27513. WFHU2.
RefSeqiNP_000651.3. NM_000660.5.
UniGeneiHs.645227.

Genome annotation databases

EnsembliENST00000221930; ENSP00000221930; ENSG00000105329.
GeneIDi7040.
KEGGihsa:7040.
UCSCiuc002oqh.2. human.

Polymorphism databases

DMDMi135674.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

TGF beta-1 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05839
, X05840 , X05843 , X05844 , X05849 , X05850 Genomic DNA. Translation: CAA29283.1 .
X02812 mRNA. Translation: CAA26580.1 .
BT007245 mRNA. Translation: AAP35909.1 .
AK291907 mRNA. Translation: BAF84596.1 .
CH471126 Genomic DNA. Translation: EAW57032.1 .
BC001180 mRNA. Translation: AAH01180.1 .
BC000125 mRNA. Translation: AAH00125.1 .
BC022242 mRNA. Translation: AAH22242.1 .
M38449 mRNA. Translation: AAA36735.1 .
CCDSi CCDS33031.1.
PIRi A27513. WFHU2.
RefSeqi NP_000651.3. NM_000660.5.
UniGenei Hs.645227.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KLA NMR - A/B 279-390 [» ]
1KLC NMR - A/B 279-390 [» ]
1KLD NMR - A/B 279-390 [» ]
3KFD X-ray 3.00 A/B/C/D 279-390 [» ]
ProteinModelPortali P01137.
SMRi P01137. Positions 30-390.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112898. 32 interactions.
DIPi DIP-5934N.
IntActi P01137. 18 interactions.
MINTi MINT-6806111.
STRINGi 9606.ENSP00000221930.

Chemistry

BindingDBi P01137.
ChEMBLi CHEMBL1795178.
DrugBanki DB00070. Hyaluronidase.

PTM databases

PhosphoSitei P01137.

Polymorphism databases

DMDMi 135674.

2D gel databases

OGPi P01137.

Proteomic databases

MaxQBi P01137.
PaxDbi P01137.
PRIDEi P01137.

Protocols and materials databases

DNASUi 7040.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000221930 ; ENSP00000221930 ; ENSG00000105329 .
GeneIDi 7040.
KEGGi hsa:7040.
UCSCi uc002oqh.2. human.

Organism-specific databases

CTDi 7040.
GeneCardsi GC19M041837.
GeneReviewsi TGFB1.
H-InvDB HIX0015152.
HGNCi HGNC:11766. TGFB1.
HPAi CAB000361.
HPA047516.
MIMi 131300. phenotype.
190180. gene.
neXtProti NX_P01137.
Orphaneti 1328. Camurati-Engelmann disease.
586. Cystic fibrosis.
PharmGKBi PA350.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG279949.
HOGENOMi HOG000290198.
HOVERGENi HBG074115.
InParanoidi P01137.
KOi K13375.
PhylomeDBi P01137.
TreeFami TF318514.

Enzyme and pathway databases

Reactomei REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_120850. TGF-beta receptor signaling activates SMADs.
REACT_150331. Molecules associated with elastic fibres.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_169165. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_169192. TGFBR2 MSI Frameshift Mutants in Cancer.
REACT_169263. TGFBR1 KD Mutants in Cancer.
REACT_169440. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_169445. TGFBR1 LBD Mutants in Cancer.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_6213. Influenza Virus Induced Apoptosis.
SignaLinki P01137.

Miscellaneous databases

ChiTaRSi TGFB1. human.
EvolutionaryTracei P01137.
GeneWikii TGF_beta_1.
GenomeRNAii 7040.
NextBioi 27507.
PROi P01137.
SOURCEi Search...

Gene expression databases

ArrayExpressi P01137.
Bgeei P01137.
CleanExi HS_TGFB1.
Genevestigatori P01137.

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. "Intron-exon structure of the human transforming growth factor-beta precursor gene."
    Derynck R., Rhee L., Chen E.Y., van Tilburg A.
    Nucleic Acids Res. 15:3188-3189(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Human transforming growth factor-beta complementary DNA sequence and expression in normal and transformed cells."
    Derynck R., Jarrett J.A., Chen E.Y., Eaton D.H., Bell J.R., Assoian R.K., Roberts A.B., Sporn M.B., Goeddel D.V.
    Nature 316:701-705(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PRO-10 AND PRO-25.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Duodenum and Eye.
  7. "Cloning and expression of the gene for human transforming growth factor-beta in Escherichia coli."
    Urushizaki Y., Niitsu Y., Terui T., Koshida Y., Mahara K., Kohgo Y., Urushizaki I., Takahashi Y., Ito H.
    Tumor Res. 22:41-55(1987)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 279-390.
    Tissue: Carcinoma.
  8. "Recombinant human transforming growth factor-beta 1: expression by Chinese hamster ovary cells, isolation, and characterization."
    Bourdrel L., Lin C.-H., Lauren S.L., Elmore R.H., Sugarman B.J., Hu S., Westcott K.R.
    Protein Expr. Purif. 4:130-140(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 279-329.
    Tissue: Urinary bladder carcinoma.
  9. "Cellular receptors for type beta transforming growth factor. Ligand binding and affinity labeling in human and rodent cell lines."
    Massague J., Like B.
    J. Biol. Chem. 260:2636-2645(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 279-301.
  10. "Latent high molecular weight complex of transforming growth factor beta 1. Purification from human platelets and structural characterization."
    Miyazono K., Hellman U., Wernstedt C., Heldin C.H.
    J. Biol. Chem. 263:6407-6415(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-42 AND 279-290, CHARACTERIZATION.
  11. "Latent transforming growth factor-beta: structural features and mechanisms of activation."
    Munger J.S., Harpel J.G., Gleizes P.E., Mazzieri R., Nunes I., Rifkin D.B.
    Kidney Int. 51:1376-1382(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  12. "Dermatopontin interacts with transforming growth factor beta and enhances its biological activity."
    Okamoto O., Fujiwara S., Abe M., Sato Y.
    Biochem. J. 337:537-541(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DPT.
  13. "Differential gene expression of cultured human osteoblasts."
    Shur I., Lokiec F., Bleiberg I., Benayahu D.
    J. Cell. Biochem. 83:547-553(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  14. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82.
    Tissue: Plasma.
  15. "Identification of CD109 as part of the TGF-beta receptor system in human keratinocytes."
    Finnson K.W., Tam B.Y.Y., Liu K., Marcoux A., Lepage P., Roy S., Bizet A.A., Philip A.
    FASEB J. 20:1525-1527(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD109.
  16. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82.
    Tissue: Platelet.
  17. "Mechanisms for asporin function and regulation in articular cartilage."
    Nakajima M., Kizawa H., Saitoh M., Kou I., Miyazono K., Ikegawa S.
    J. Biol. Chem. 282:32185-32192(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ASPN.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Transforming growth factor beta 1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells."
    Archer S.J., Bax A., Roberts A.B., Sporn M.B., Ogawa Y., Piez K.A., Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J., Torchia D.A.
    Biochemistry 32:1152-1163(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 279-390.
  20. "Transforming growth factor beta 1: secondary structure as determined by heteronuclear magnetic resonance spectroscopy."
    Archer S.J., Bax A., Roberts A.B., Sporn M.B., Ogawa Y., Piez K.A., Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J., Torchia D.A.
    Biochemistry 32:1164-1171(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 279-390.
  21. "Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2."
    Hinck A.P., Archer S.J., Qian S.W., Roberts A.B., Sporn M.B., Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J., Torchia D.A.
    Biochemistry 35:8517-8534(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 279-390.
  22. "Association of a polymorphism of the transforming growth factor-beta1 gene with genetic susceptibility to osteoporosis in postmenopausal Japanese women."
    Yamada Y., Miyauchi A., Goto J., Takagi Y., Okuizumi H., Kanematsu M., Hase M., Takai H., Harada A., Ikeda K.
    J. Bone Miner. Res. 13:1569-1576(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRO-10.
  23. Cited for: VARIANTS CE CYS-218; HIS-218 AND ARG-225.
  24. "Mutations in the gene encoding the latency-associated peptide of TGF-beta 1 cause Camurati-Engelmann disease."
    Janssens K., Gershoni-Baruch R., Guanabens N., Migone N., Ralston S., Bonduelle M., Lissens W., Van Maldergem L., Vanhoenacker F., Verbruggen L., Van Hul W.
    Nat. Genet. 26:273-275(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CE HIS-81; CYS-218 AND ARG-225.
  25. "A catalog of 106 single-nucleotide polymorphisms (SNPs) and 11 other types of variations in genes for transforming growth factor-beta1 (TGF-beta1) and its signaling pathway."
    Watanabe Y., Kinoshita A., Yamada T., Ohta T., Kishino T., Matsumoto N., Ishikawa M., Niikawa N., Yoshiura K.
    J. Hum. Genet. 47:478-483(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRO-10.
  26. "Transforming growth factor-beta-1 mutations in Camurati-Engelmann disease lead to increased signaling by altering either activation or secretion of the mutant protein."
    Janssens K., ten Dijke P., Ralston S.H., Bergmann C., Van Hul W.
    J. Biol. Chem. 278:7718-7724(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS CE HIS-81; CYS-218; ASP-222 AND ARG-225.
  27. "A mutation affecting the latency-associated peptide of TGFbeta1 in Camurati-Engelmann disease enhances osteoclast formation in vitro."
    McGowan N.W., MacPherson H., Janssens K., Van Hul W., Frith J.C., Fraser W.D., Ralston S.H., Helfrich M.H.
    J. Clin. Endocrinol. Metab. 88:3321-3326(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT CE CYS-218.
  28. "TGFB1 mutations in four new families with Camurati-Engelmann disease: confirmation of independently arising LAP-domain-specific mutations."
    Kinoshita A., Fukumaki Y., Shirahama S., Miyahara A., Nishimura G., Haga N., Namba A., Ueda H., Hayashi H., Ikegawa S., Seidel J., Niikawa N., Yoshiura K.
    Am. J. Med. Genet. 127A:104-107(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CE GLY-223 AND ARG-223.

Entry informationi

Entry nameiTGFB1_HUMAN
AccessioniPrimary (citable) accession number: P01137
Secondary accession number(s): A8K792, Q9UCG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1991
Last modified: September 3, 2014
This is version 197 of the entry and version 2 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 19
    Human chromosome 19: 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

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