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P36897

- TGFR1_HUMAN

UniProt

P36897 - TGFR1_HUMAN

Protein

TGF-beta receptor type-1

Gene

TGFBR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 174 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation.7 Publications

    Catalytic activityi

    ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

    Cofactori

    Magnesium or manganese.By similarity

    Enzyme regulationi

    Kept in an inactive conformation by FKBP1A preventing receptor activation in absence of ligand. CD109 is another inhibitor of the receptor.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei232 – 2321ATPPROSITE-ProRule annotation
    Active sitei333 – 3331Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi211 – 2199ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: HGNC
    2. I-SMAD binding Source: BHF-UCL
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. protein kinase activity Source: BHF-UCL
    6. protein serine/threonine kinase activity Source: BHF-UCL
    7. receptor signaling protein serine/threonine kinase activity Source: InterPro
    8. SMAD binding Source: BHF-UCL
    9. transforming growth factor beta-activated receptor activity Source: BHF-UCL
    10. transforming growth factor beta binding Source: BHF-UCL
    11. transforming growth factor beta receptor activity, type I Source: BHF-UCL
    12. type II transforming growth factor beta receptor binding Source: BHF-UCL

    GO - Biological processi

    1. activation of MAPKK activity Source: BHF-UCL
    2. angiogenesis Source: Ensembl
    3. anterior/posterior pattern specification Source: BHF-UCL
    4. apoptotic process Source: UniProtKB-KW
    5. artery morphogenesis Source: BHF-UCL
    6. blastocyst development Source: Ensembl
    7. cell cycle arrest Source: UniProtKB
    8. cell motility Source: BHF-UCL
    9. cellular response to transforming growth factor beta stimulus Source: BHF-UCL
    10. collagen fibril organization Source: BHF-UCL
    11. embryonic cranial skeleton morphogenesis Source: BHF-UCL
    12. endothelial cell migration Source: Ensembl
    13. epithelial to mesenchymal transition Source: UniProtKB
    14. extracellular structure organization Source: UniProtKB
    15. germ cell migration Source: BHF-UCL
    16. heart development Source: BHF-UCL
    17. in utero embryonic development Source: BHF-UCL
    18. kidney development Source: BHF-UCL
    19. lens development in camera-type eye Source: Ensembl
    20. mesenchymal cell differentiation Source: UniProtKB
    21. negative regulation of apoptotic process Source: Ensembl
    22. negative regulation of chondrocyte differentiation Source: BHF-UCL
    23. negative regulation of endothelial cell proliferation Source: Ensembl
    24. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    25. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
    26. neuron fate commitment Source: BHF-UCL
    27. palate development Source: BHF-UCL
    28. parathyroid gland development Source: BHF-UCL
    29. pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
    30. peptidyl-serine phosphorylation Source: UniProtKB
    31. peptidyl-threonine phosphorylation Source: BHF-UCL
    32. pharyngeal system development Source: BHF-UCL
    33. positive regulation of apoptotic signaling pathway Source: UniProtKB
    34. positive regulation of cell growth Source: BHF-UCL
    35. positive regulation of cell proliferation Source: HGNC
    36. positive regulation of cellular component movement Source: BHF-UCL
    37. positive regulation of filopodium assembly Source: Ensembl
    38. positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
    39. positive regulation of protein kinase B signaling Source: BHF-UCL
    40. positive regulation of SMAD protein import into nucleus Source: BHF-UCL
    41. positive regulation of transcription, DNA-templated Source: BHF-UCL
    42. post-embryonic development Source: Ensembl
    43. protein phosphorylation Source: BHF-UCL
    44. regulation of protein binding Source: Ensembl
    45. regulation of protein ubiquitination Source: UniProtKB
    46. regulation of transcription, DNA-templated Source: HGNC
    47. response to cholesterol Source: BHF-UCL
    48. signal transduction Source: HGNC
    49. skeletal system development Source: BHF-UCL
    50. skeletal system morphogenesis Source: BHF-UCL
    51. thymus development Source: BHF-UCL
    52. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    53. wound healing Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Receptor, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Differentiation, Growth regulation

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    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_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_169165. SMAD2/3 MH2 Domain 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.
    SignaLinkiP36897.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TGF-beta receptor type-1 (EC:2.7.11.30)
    Short name:
    TGFR-1
    Alternative name(s):
    Activin A receptor type II-like protein kinase of 53kD
    Activin receptor-like kinase 5
    Short name:
    ALK-5
    Short name:
    ALK5
    Serine/threonine-protein kinase receptor R4
    Short name:
    SKR4
    TGF-beta type I receptor
    Transforming growth factor-beta receptor type I
    Short name:
    TGF-beta receptor type I
    Short name:
    TbetaR-I
    Gene namesi
    Name:TGFBR1
    Synonyms:ALK5, SKR4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:11772. TGFBR1.

    Subcellular locationi

    GO - Cellular componenti

    1. plasma membrane Source: BHF-UCL
    2. receptor complex Source: BHF-UCL
    3. tight junction Source: UniProtKB
    4. transforming growth factor beta receptor homodimeric complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Tight junction

    Pathology & Biotechi

    Involvement in diseasei

    Loeys-Dietz syndrome 1 (LDS1) [MIM:609192]: An aortic aneurysm syndrome with widespread systemic involvement, characterized by arterial tortuosity and aneurysms, hypertelorism, and bifid uvula or cleft palate. Physical findings include prominent joint laxity, easy bruising, wide and atrophic scars, velvety and translucent skin with easily visible veins, spontaneous rupture of the spleen or bowel, and catastrophic complications of pregnancy, including rupture of the gravid uterus and the arteries, either during pregnancy or in the immediate postpartum period. Some patients have craniosynostosis, exotropy, micrognathia and retrognathia, structural brain abnormalities, and intellectual deficit.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. TGFBR1 mutation Gln-487 has been reported to be associated with thoracic aortic aneurysms and dissection (TAAD) (PubMed:16791849). This phenotype, also known as thoracic aortic aneurysms type 5 (AAT5), is distinguised from LDS1 by having aneurysms restricted to thoracic aorta. It is unclear, however, if this condition is fulfilled in individuals bearing Gln-487 mutation, that is why they are considered as LDS1 by the OMIM resource.1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti200 – 2001T → I in LDS1. 1 Publication
    VAR_022344
    Natural varianti232 – 2321K → E in LDS1. 1 Publication
    VAR_029481
    Natural varianti241 – 2411S → L in LDS1. 2 Publications
    VAR_029482
    Natural varianti266 – 2661D → Y in LDS1. 1 Publication
    VAR_066720
    Natural varianti318 – 3181M → R in LDS1. 1 Publication
    VAR_022345
    Natural varianti351 – 3511D → G in LDS1. 1 Publication
    VAR_066721
    Natural varianti375 – 3751T → I in LDS1. 1 Publication
    VAR_066722
    Natural varianti400 – 4001D → G in LDS1. 1 Publication
    VAR_022346
    Natural varianti487 – 4871R → P in LDS1. 2 Publications
    VAR_022347
    Natural varianti487 – 4871R → Q in LDS1. 3 Publications
    VAR_029484
    Natural varianti487 – 4871R → W in LDS1. 1 Publication
    VAR_029485
    Multiple self-healing squamous epithelioma (MSSE) [MIM:132800]: A disorder characterized by multiple skin tumors that undergo spontaneous regression. Tumors appear most often on sun-exposed regions, are locally invasive, and undergo spontaneous resolution over a period of months leaving pitted scars.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411C → Y in MSSE; hypomorphic mutation. 1 Publication
    VAR_065826
    Natural varianti45 – 451N → S in MSSE; hypomorphic mutation. 1 Publication
    VAR_065827
    Natural varianti52 – 521G → R in MSSE; hypomorphic mutation. 1 Publication
    VAR_065828
    Natural varianti83 – 831P → L in MSSE; hypomorphic mutation. 1 Publication
    VAR_065829

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi185 – 1862TT → VV: Loss of phosphorylation on threonine residues. Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with A-187; A-189 and A-191.
    Mutagenesisi187 – 1871S → A: Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-189 and A-191. 1 Publication
    Mutagenesisi189 – 1891S → A: Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-187 and A-191. 1 Publication
    Mutagenesisi191 – 1911S → A: Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-187 and A-189. 1 Publication
    Mutagenesisi193 – 1931L → G: Loss of interaction with FKBP1A. 1 Publication
    Mutagenesisi194 – 1941P → K: Loss of interaction with FKBP1A. 1 Publication
    Mutagenesisi200 – 2001T → D: Loss of response to TGF-beta. 1 Publication
    Mutagenesisi200 – 2001T → V: Loss of phosphorylation. Loss of response to TGF-beta. 1 Publication
    Mutagenesisi204 – 2041T → D: Constitutive activation. 1 Publication
    Mutagenesisi204 – 2041T → V: Reduced phosphorylation. Reduced response to TGF-beta. 1 Publication

    Keywords - Diseasei

    Aortic aneurysm, Craniosynostosis, Disease mutation

    Organism-specific databases

    MIMi132800. phenotype.
    609192. phenotype.
    Orphaneti91387. Familial thoracic aortic aneurysm and aortic dissection.
    60030. Loeys-Dietz syndrome.
    65748. Multiple keratoacanthoma, Ferguson-Smith type.
    PharmGKBiPA36485.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 33331 PublicationAdd
    BLAST
    Chaini34 – 503470TGF-beta receptor type-1PRO_0000024423Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi36 ↔ 54
    Disulfide bondi38 ↔ 41
    Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi48 ↔ 71
    Disulfide bondi86 ↔ 100
    Disulfide bondi101 ↔ 106
    Modified residuei165 – 1651Phosphoserine2 Publications
    Modified residuei185 – 1851Phosphothreonine; by TGFBR22 Publications
    Modified residuei186 – 1861Phosphothreonine; by TGFBR22 Publications
    Modified residuei187 – 1871Phosphoserine; by TGFBR22 Publications
    Modified residuei189 – 1891Phosphoserine; by TGFBR22 Publications
    Modified residuei191 – 1911Phosphoserine; by TGFBR22 Publications
    Cross-linki391 – 391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Phosphorylated at basal levels in the absence of ligand. Activated upon phosphorylation by TGFBR2, mainly in the GS domain. Phosphorylation in the GS domain abrogates FKBP1A-binding.3 Publications
    N-Glycosylated.1 Publication
    Ubiquitinated; undergoes ubiquitination catalyzed by several E3 ubiquitin ligases including SMURF1, SMURF2 and NEDD4L2. Results in the proteasomal and/or lysosomal degradation of the receptor thereby negatively regulating its activity. Deubiquitinated by USP15, leading to stabilization of the protein and enhanced TGF-beta signal.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP36897.
    PaxDbiP36897.
    PRIDEiP36897.

    PTM databases

    PhosphoSiteiP36897.

    Expressioni

    Tissue specificityi

    Found in all tissues examined, most abundant in placenta and least abundant in brain and heart.

    Gene expression databases

    ArrayExpressiP36897.
    BgeeiP36897.
    CleanExiHS_TGFBR1.
    GenevestigatoriP36897.

    Organism-specific databases

    HPAiCAB002441.
    CAB031481.

    Interactioni

    Subunit structurei

    Homodimer; in the endoplasmic reticulum but also at the cell membrane. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands assemble a functional receptor composed of two TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The respective affinity of TGBRB1 and TGFBR2 for the ligands may modulate the kinetics of assembly of the receptor and may explain the different biological activities of TGFB1, TGFB2 and TGFB3. Interacts with CD109; inhibits TGF-beta receptor activation in keratinocytes. Interacts with RBPMS. Interacts (unphosphorylated) with FKBP1A; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation. Interacts with SMAD2, SMAD3 and ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta receptor. Interacts with TRAF6 and MAP3K7; induces MAP3K7 activation by TRAF6. Interacts with PARD6A; involved in TGF-beta induced epithelial to mesenchymal transition. Interacts with SMAD7, NEDD4L, SMURF1 and SMURF2; SMAD7 recruits NEDD4L, SMURF1 and SMURF2 to the TGF-beta receptor. Interacts with USP15 and VPS39.20 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q99IB85EBI-1027557,EBI-6858501From a different organism.
    TGFB1P011372EBI-1027557,EBI-779636
    YWHAZP631044EBI-1027557,EBI-347088

    Protein-protein interaction databases

    BioGridi112904. 172 interactions.
    DIPiDIP-5935N.
    IntActiP36897. 10 interactions.
    MINTiMINT-152959.
    STRINGi9606.ENSP00000364133.

    Structurei

    Secondary structure

    1
    503
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 373
    Turni42 – 465
    Beta strandi51 – 577
    Beta strandi61 – 633
    Beta strandi69 – 724
    Turni74 – 763
    Beta strandi77 – 826
    Turni84 – 863
    Helixi89 – 924
    Beta strandi94 – 1018
    Beta strandi102 – 1054
    Helixi107 – 1093
    Helixi177 – 1837
    Beta strandi187 – 1904
    Beta strandi191 – 1933
    Helixi202 – 2043
    Beta strandi205 – 2139
    Beta strandi215 – 22410
    Beta strandi227 – 2348
    Helixi236 – 2383
    Helixi239 – 24911
    Beta strandi251 – 2533
    Beta strandi262 – 2698
    Beta strandi271 – 28111
    Helixi288 – 2947
    Helixi299 – 31719
    Beta strandi322 – 3243
    Beta strandi328 – 3303
    Beta strandi338 – 3414
    Beta strandi347 – 3493
    Helixi352 – 3543
    Beta strandi356 – 3594
    Turni360 – 3634
    Beta strandi364 – 3663
    Helixi376 – 3783
    Helixi381 – 3844
    Helixi393 – 41321
    Beta strandi417 – 4193
    Turni427 – 4315
    Helixi438 – 4458
    Helixi456 – 4594
    Helixi462 – 47211
    Helixi479 – 4813
    Helixi485 – 49713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B6CX-ray2.60B/D/F/H162-503[»]
    1IASX-ray2.90A/B/C/D/E162-503[»]
    1PY5X-ray2.30A175-500[»]
    1RW8X-ray2.40A200-500[»]
    1TBImodel-A34-114[»]
    1VJYX-ray2.00A201-503[»]
    2L5SNMR-A31-115[»]
    2PJYX-ray3.00C33-111[»]
    2WOTX-ray1.85A200-503[»]
    2WOUX-ray2.30A200-503[»]
    2X7OX-ray3.70A/B/C/D/E162-503[»]
    3FAAX-ray3.35A/B/C/D/E162-503[»]
    3GXLX-ray1.80A201-503[»]
    3HMMX-ray1.70A201-503[»]
    3KCFX-ray2.80A/B/C/D/E162-503[»]
    3KFDX-ray3.00I/J/K/L31-115[»]
    3TZMX-ray1.70A200-503[»]
    ProteinModelPortaliP36897.
    SMRiP36897. Positions 31-115, 175-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36897.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini34 – 12693ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini148 – 503356CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei127 – 14721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini175 – 20430GSPROSITE-ProRule annotationAdd
    BLAST
    Domaini205 – 495291Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi193 – 1942FKBP1A-binding

    Sequence similaritiesi

    Contains 1 GS domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000230587.
    HOVERGENiHBG054502.
    InParanoidiP36897.
    KOiK04674.
    OMAiLYICHNR.
    PhylomeDBiP36897.
    TreeFamiTF314724.

    Family and domain databases

    InterProiIPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    IPR003605. TGF_beta_rcpt_GS.
    IPR000333. TGFB_receptor.
    [Graphical view]
    PANTHERiPTHR23255. PTHR23255. 1 hit.
    PfamiPF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08515. TGF_beta_GS. 1 hit.
    [Graphical view]
    SMARTiSM00467. GS. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51256. GS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P36897-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEAAVAAPRP RLLLLVLAAA AAAAAALLPG ATALQCFCHL CTKDNFTCVT    50
    DGLCFVSVTE TTDKVIHNSM CIAEIDLIPR DRPFVCAPSS KTGSVTTTYC 100
    CNQDHCNKIE LPTTVKSSPG LGPVELAAVI AGPVCFVCIS LMLMVYICHN 150
    RTVIHHRVPN EEDPSLDRPF ISEGTTLKDL IYDMTTSGSG SGLPLLVQRT 200
    IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER SWFREAEIYQ 250
    TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE 300
    GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA 350
    DLGLAVRHDS ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD 400
    IYAMGLVFWE IARRCSIGGI HEDYQLPYYD LVPSDPSVEE MRKVVCEQKL 450
    RPNIPNRWQS CEALRVMAKI MRECWYANGA ARLTALRIKK TLSQLSQQEG 500
    IKM 503
    Length:503
    Mass (Da):55,960
    Last modified:June 1, 1994 - v1
    Checksum:i179F11404725DDCB
    GO
    Isoform 2 (identifier: P36897-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         114-114: T → TGPFS

    Show »
    Length:507
    Mass (Da):56,348
    Checksum:i9EFAF4435F30E4C2
    GO
    Isoform 3 (identifier: P36897-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         115-191: Missing.

    Show »
    Length:426
    Mass (Da):47,690
    Checksum:i97EA2F587AFA08F6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti24 – 263Missing in allele TGFBR1*6A; could be a tumor susceptibility allele.
    VAR_022342
    Natural varianti26 – 261A → AA in allele TGFBR1*10A; rare polymorphism. 1 Publication
    VAR_022343
    Natural varianti41 – 411C → Y in MSSE; hypomorphic mutation. 1 Publication
    VAR_065826
    Natural varianti45 – 451N → S in MSSE; hypomorphic mutation. 1 Publication
    VAR_065827
    Natural varianti52 – 521G → R in MSSE; hypomorphic mutation. 1 Publication
    VAR_065828
    Natural varianti83 – 831P → L in MSSE; hypomorphic mutation. 1 Publication
    VAR_065829
    Natural varianti139 – 1391I → V.1 Publication
    VAR_054160
    Natural varianti153 – 1531V → I.1 Publication
    Corresponds to variant rs56014374 [ dbSNP | Ensembl ].
    VAR_041412
    Natural varianti200 – 2001T → I in LDS1. 1 Publication
    VAR_022344
    Natural varianti232 – 2321K → E in LDS1. 1 Publication
    VAR_029481
    Natural varianti241 – 2411S → L in LDS1. 2 Publications
    VAR_029482
    Natural varianti266 – 2661D → Y in LDS1. 1 Publication
    VAR_066720
    Natural varianti267 – 2671N → H in a patient with Marfan syndrome. 1 Publication
    VAR_029483
    Natural varianti291 – 2911Y → C.1 Publication
    Corresponds to variant rs35974499 [ dbSNP | Ensembl ].
    VAR_041413
    Natural varianti318 – 3181M → R in LDS1. 1 Publication
    VAR_022345
    Natural varianti351 – 3511D → G in LDS1. 1 Publication
    VAR_066721
    Natural varianti375 – 3751T → I in LDS1. 1 Publication
    VAR_066722
    Natural varianti400 – 4001D → G in LDS1. 1 Publication
    VAR_022346
    Natural varianti487 – 4871R → P in LDS1. 2 Publications
    VAR_022347
    Natural varianti487 – 4871R → Q in LDS1. 3 Publications
    VAR_029484
    Natural varianti487 – 4871R → W in LDS1. 1 Publication
    VAR_029485

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei114 – 1141T → TGPFS in isoform 2. 1 PublicationVSP_041326
    Alternative sequencei115 – 19177Missing in isoform 3. 1 PublicationVSP_041327Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11695 mRNA. Translation: AAA16073.1.
    AF054598
    , AF054590, AF054591, AF054592, AF054593, AF054594, AF054595, AF054596, AF054597 Genomic DNA. Translation: AAC08998.1.
    AF035670
    , AF035662, AF035663, AF035664, AF035665, AF035666, AF035667, AF035668, AF035669 Genomic DNA. Translation: AAD02042.1.
    AY497473 Genomic DNA. Translation: AAR32097.1.
    AL162427 Genomic DNA. No translation available.
    BC071181 mRNA. Translation: AAH71181.1.
    AJ619019 mRNA. Translation: CAF02096.2.
    AJ619020 mRNA. Translation: CAF02097.1.
    CCDSiCCDS47998.1. [P36897-3]
    CCDS6738.1. [P36897-1]
    PIRiA49432.
    RefSeqiNP_001124388.1. NM_001130916.1. [P36897-3]
    NP_004603.1. NM_004612.2. [P36897-1]
    XP_005252207.1. XM_005252150.1. [P36897-2]
    UniGeneiHs.494622.

    Genome annotation databases

    EnsembliENST00000374990; ENSP00000364129; ENSG00000106799. [P36897-3]
    ENST00000374994; ENSP00000364133; ENSG00000106799. [P36897-1]
    ENST00000552516; ENSP00000447297; ENSG00000106799. [P36897-2]
    GeneIDi7046.
    KEGGihsa:7046.
    UCSCiuc004azc.3. human. [P36897-1]
    uc004azd.3. human. [P36897-3]
    uc004aze.3. human. [P36897-2]

    Polymorphism databases

    DMDMi547777.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11695 mRNA. Translation: AAA16073.1 .
    AF054598
    , AF054590 , AF054591 , AF054592 , AF054593 , AF054594 , AF054595 , AF054596 , AF054597 Genomic DNA. Translation: AAC08998.1 .
    AF035670
    , AF035662 , AF035663 , AF035664 , AF035665 , AF035666 , AF035667 , AF035668 , AF035669 Genomic DNA. Translation: AAD02042.1 .
    AY497473 Genomic DNA. Translation: AAR32097.1 .
    AL162427 Genomic DNA. No translation available.
    BC071181 mRNA. Translation: AAH71181.1 .
    AJ619019 mRNA. Translation: CAF02096.2 .
    AJ619020 mRNA. Translation: CAF02097.1 .
    CCDSi CCDS47998.1. [P36897-3 ]
    CCDS6738.1. [P36897-1 ]
    PIRi A49432.
    RefSeqi NP_001124388.1. NM_001130916.1. [P36897-3 ]
    NP_004603.1. NM_004612.2. [P36897-1 ]
    XP_005252207.1. XM_005252150.1. [P36897-2 ]
    UniGenei Hs.494622.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B6C X-ray 2.60 B/D/F/H 162-503 [» ]
    1IAS X-ray 2.90 A/B/C/D/E 162-503 [» ]
    1PY5 X-ray 2.30 A 175-500 [» ]
    1RW8 X-ray 2.40 A 200-500 [» ]
    1TBI model - A 34-114 [» ]
    1VJY X-ray 2.00 A 201-503 [» ]
    2L5S NMR - A 31-115 [» ]
    2PJY X-ray 3.00 C 33-111 [» ]
    2WOT X-ray 1.85 A 200-503 [» ]
    2WOU X-ray 2.30 A 200-503 [» ]
    2X7O X-ray 3.70 A/B/C/D/E 162-503 [» ]
    3FAA X-ray 3.35 A/B/C/D/E 162-503 [» ]
    3GXL X-ray 1.80 A 201-503 [» ]
    3HMM X-ray 1.70 A 201-503 [» ]
    3KCF X-ray 2.80 A/B/C/D/E 162-503 [» ]
    3KFD X-ray 3.00 I/J/K/L 31-115 [» ]
    3TZM X-ray 1.70 A 200-503 [» ]
    ProteinModelPortali P36897.
    SMRi P36897. Positions 31-115, 175-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112904. 172 interactions.
    DIPi DIP-5935N.
    IntActi P36897. 10 interactions.
    MINTi MINT-152959.
    STRINGi 9606.ENSP00000364133.

    Chemistry

    BindingDBi P36897.
    ChEMBLi CHEMBL4439.
    GuidetoPHARMACOLOGYi 1788.

    PTM databases

    PhosphoSitei P36897.

    Polymorphism databases

    DMDMi 547777.

    Proteomic databases

    MaxQBi P36897.
    PaxDbi P36897.
    PRIDEi P36897.

    Protocols and materials databases

    DNASUi 7046.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374990 ; ENSP00000364129 ; ENSG00000106799 . [P36897-3 ]
    ENST00000374994 ; ENSP00000364133 ; ENSG00000106799 . [P36897-1 ]
    ENST00000552516 ; ENSP00000447297 ; ENSG00000106799 . [P36897-2 ]
    GeneIDi 7046.
    KEGGi hsa:7046.
    UCSCi uc004azc.3. human. [P36897-1 ]
    uc004azd.3. human. [P36897-3 ]
    uc004aze.3. human. [P36897-2 ]

    Organism-specific databases

    CTDi 7046.
    GeneCardsi GC09P101867.
    GeneReviewsi TGFBR1.
    HGNCi HGNC:11772. TGFBR1.
    HPAi CAB002441.
    CAB031481.
    MIMi 132800. phenotype.
    190181. gene.
    609192. phenotype.
    neXtProti NX_P36897.
    Orphaneti 91387. Familial thoracic aortic aneurysm and aortic dissection.
    60030. Loeys-Dietz syndrome.
    65748. Multiple keratoacanthoma, Ferguson-Smith type.
    PharmGKBi PA36485.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000230587.
    HOVERGENi HBG054502.
    InParanoidi P36897.
    KOi K04674.
    OMAi LYICHNR.
    PhylomeDBi P36897.
    TreeFami TF314724.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    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_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_169165. SMAD2/3 MH2 Domain 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.
    SignaLinki P36897.

    Miscellaneous databases

    ChiTaRSi TGFBR1. human.
    EvolutionaryTracei P36897.
    GeneWikii TGF_beta_receptor_1.
    GenomeRNAii 7046.
    NextBioi 27533.
    PROi P36897.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36897.
    Bgeei P36897.
    CleanExi HS_TGFBR1.
    Genevestigatori P36897.

    Family and domain databases

    InterProi IPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    IPR003605. TGF_beta_rcpt_GS.
    IPR000333. TGFB_receptor.
    [Graphical view ]
    PANTHERi PTHR23255. PTHR23255. 1 hit.
    Pfami PF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08515. TGF_beta_GS. 1 hit.
    [Graphical view ]
    SMARTi SM00467. GS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51256. GS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor."
      Franzen P., ten Dijke P., Ichijo H., Yamashita H., Schulz P., Heldin C.-H., Miyazono K.
      Cell 75:681-692(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning and genomic organization of the human transforming growth factor-beta type I receptor gene."
      Vellucci V.F., Reiss M.
      Genomics 46:278-283(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The genomic structure of the gene encoding the human transforming growth factor beta type I receptor."
      Lynch M.A., Song H., DeGroff V.L., Alam K.Y., Adams E.M., Weghorst C.M.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. NIEHS SNPs program
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 3).
      Tissue: Placenta.
    7. "Type I transforming growth factor beta receptor maps to 9q22 and exhibits a polymorphism and a rare variant within a polyalanine tract."
      Pasche B., Luo Y., Rao P.H., Nimer S.D., Dmitrovsky E., Caron P., Luzzatto L., Offit K., Cordon-Cardo C., Renault B., Satagopan J.M., Murty V.V., Massague J.
      Cancer Res. 58:2727-2732(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-40, SIGNAL SEQUENCE CLEAVAGE SITE, GLYCOSYLATION, CHARACTERIZATION OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL, VARIANT TGFBR1*10A ALA-26 INS.
    8. "Alternative splicing of TGF-betas and their high-affinity receptors T beta RI, T beta RII and T beta RIII (betaglycan) reveal new variants in human prostatic cells."
      Konrad L., Scheiber J.A., Volck-Badouin E., Keilani M.M., Laible L., Brandt H., Schmidt A., Aumuller G., Hofmann R.
      BMC Genomics 8:318-318(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 61-155 (ISOFORM 1), ALTERNATIVE SPLICING.
      Tissue: Prostate.
    9. Konrad L.
      Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION (ISOFORM 1).
    10. "GS domain mutations that constitutively activate T beta R-I, the downstream signaling component in the TGF-beta receptor complex."
      Wieser R., Wrana J.L., Massague J.
      EMBO J. 14:2199-2208(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-185; THR-186; SER-187; SER-189 AND SER-191 BY TGFBR2, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF 185-THR-THR-186; SER-187; SER-189; SER-191; THR-200 AND THR-204.
    11. "MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma."
      Eppert K., Scherer S.W., Ozcelik H., Pirone R., Hoodless P., Kim H., Tsui L.-C., Bapat B., Gallinger S., Andrulis I.L., Thomsen G.H., Wrana J.L., Attisano L.
      Cell 86:543-552(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SMAD2.
    12. "MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling."
      Macias-Silva M., Abdollah S., Hoodless P.A., Pirone R., Attisano L., Wrana J.L.
      Cell 87:1215-1224(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMAD2, FUNCTION IN PHOSPHORYLATION OF SMAD2, FUNCTION IN TRANSCRIPTION REGULATION.
    13. "Mechanism of TGFbeta receptor inhibition by FKBP12."
      Chen Y.G., Liu F., Massague J.
      EMBO J. 16:3866-3876(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FKBP1A, ENZYME REGULATION, MUTAGENESIS OF LEU-193 AND PRO-194.
    14. Cited for: INTERACTION WITH SMAD3.
    15. "TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling."
      Abdollah S., Macias-Silva M., Tsukazaki T., Hayashi H., Attisano L., Wrana J.L.
      J. Biol. Chem. 272:27678-27685(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMAD2, FUNCTION IN PHOSPHORYLATION OF SMAD2, FUNCTION IN TRANSCRIPTION REGULATION.
    16. "SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor."
      Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.
      Cell 95:779-791(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZFYVE9.
    17. "Oligomeric structure of type I and type II transforming growth factor beta receptors: homodimers form in the ER and persist at the plasma membrane."
      Gilboa L., Wells R.G., Lodish H.F., Henis Y.I.
      J. Cell Biol. 140:767-777(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION, SUBCELLULAR LOCATION.
    18. "Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF-beta receptor for degradation."
      Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H., Wrana J.L.
      Mol. Cell 6:1365-1375(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMAD7 AND SMURF2, PROTEASOMAL AND LYSOSOMAL DEGRADATION.
    19. "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
      Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
      J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMAD7 AND SMURF1, PROTEASOMAL DEGRADATION.
    20. "TLP, a novel modulator of TGF-beta signaling, has opposite effects on Smad2- and Smad3-dependent signaling."
      Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S., McNally J.G., Roberts A.B.
      EMBO J. 22:4465-4477(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VPS39.
    21. "NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-beta (transforming growth factor-beta) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta type I receptor."
      Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K., Miyazono K., Imamura T.
      Biochem. J. 386:461-470(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEDD4L, UBIQUITINATION.
    22. "Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity."
      Ozdamar B., Bose R., Barrios-Rodiles M., Wang H.R., Zhang Y., Wrana J.L.
      Science 307:1603-1609(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EPITHELIAL TO MESENCHYMAL TRANSITION, SUBCELLULAR LOCATION, INTERACTION WITH PARD6A, FUNCTION IN PHOSPHORYLATION OF PARD6A.
    23. "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: FUNCTION IN CELLULAR GROWTH INHIBITION, INTERACTION WITH CD109.
    24. "Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS."
      Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H., Ye Q.
      Nucleic Acids Res. 34:6314-6326(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBPMS.
    25. "The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner."
      Sorrentino A., Thakur N., Grimsby S., Marcusson A., von Bulow V., Schuster N., Zhang S., Heldin C.H., Landstrom M.
      Nat. Cell Biol. 10:1199-1207(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH TRAF6 AND MAP3K7.
    26. Cited for: REVIEW ON PROCESSES REGULATED BY THE TGF-BETA CYTOKINES.
    27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "USP15 stabilizes TGF-beta receptor I and promotes oncogenesis through the activation of TGF-beta signaling in glioblastoma."
      Eichhorn P.J., Rodon L., Gonzalez-Junca A., Dirac A., Gili M., Martinez-Saez E., Aura C., Barba I., Peg V., Prat A., Cuartas I., Jimenez J., Garcia-Dorado D., Sahuquillo J., Bernards R., Baselga J., Seoane J.
      Nat. Med. 18:429-435(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP15.
    29. "Extracellular domain of type I receptor for transforming growth factor-beta: molecular modelling using protectin (CD59) as a template."
      Jokiranta T.S., Tissari J., Teleman O., Meri S.
      FEBS Lett. 376:31-36(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 34-114.
    30. "Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12."
      Huse M., Chen Y.-G., Massague J., Kuriyan J.
      Cell 96:425-436(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 162-503 IN COMPLEX WITH FKBP1A.
    31. "The TGF beta receptor activation process: an inhibitor- to substrate-binding switch."
      Huse M., Muir T.W., Xu L., Chen Y.-G., Kuriyan J., Massague J.
      Mol. Cell 8:671-682(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 162-503, PHOSPHORYLATION, INTERACTION WITH SMAD2 AND FKBP1A.
    32. "Synthesis and activity of new aryl- and heteroaryl-substituted 5,6-dihydro-4H-pyrrolo[1,2-b]pyrazole inhibitors of the transforming growth factor-beta type I receptor kinase domain."
      Sawyer J.S., Beight D.W., Britt K.S., Anderson B.D., Campbell R.M., Goodson T. Jr., Herron D.K., Li H.-Y., McMillen W.T., Mort N., Parsons S., Smith E.C.R., Wagner J.R., Yan L., Zhang F., Yingling J.M.
      Bioorg. Med. Chem. Lett. 14:3581-3584(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 175-500 IN COMPLEX WITH SYNTHETIC INHIBITOR.
    33. "Identification of 1,5-naphthyridine derivatives as a novel series of potent and selective TGF-beta type I receptor inhibitors."
      Gellibert F., Woolven J., Fouchet M.-H., Mathews N., Goodland H., Lovegrove V., Laroze A., Nguyen V.-L., Sautet S., Wang R., Janson C., Smith W., Krysa G., Boullay V., De Gouville A.-C., Huet S., Hartley D.
      J. Med. Chem. 47:4494-4506(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 201-503 IN COMPLEX WITH SYNTHETIC INHIBITOR.
    34. "Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding."
      Groppe J., Hinck C.S., Samavarchi-Tehrani P., Zubieta C., Schuermann J.P., Taylor A.B., Schwarz P.M., Wrana J.L., Hinck A.P.
      Mol. Cell 29:157-168(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 33-111 IN COMPLEX WITH TGFBR2 AND TGFB3, DISULFIDE BONDS.
    35. "Ternary complex of transforming growth factor-beta1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily."
      Radaev S., Zou Z., Huang T., Lafer E.M., Hinck A.P., Sun P.D.
      J. Biol. Chem. 285:14806-14814(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 31-115 IN COMPLEX WITH TGFBR2 AND TGFB1, RECEPTOR AFFINITY FOR LIGANDS, DISULFIDE BONDS.
    36. "TGFBR1*6A and cancer risk: a meta-analysis of seven case-control studies."
      Kaklamani V.G., Hou N., Bian Y., Reich J., Offit K., Michel L.S., Rubinstein W.S., Rademaker A., Pasche B.
      J. Clin. Oncol. 21:3236-3243(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN CANCER RISK.
    37. Cited for: ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN PROSTATE CANCER.
    38. Cited for: VARIANTS LDS1 ILE-200; ARG-318; GLY-400 AND PRO-487.
    39. "TGFBR1(*)6A is not associated with prostate cancer in men of European ancestry."
      Suarez B.K., Pal P., Jin C.H., Kaushal R., Sun G., Jin L., Pasche B., Deka R., Catalona W.J.
      Prostate Cancer Prostatic Dis. 8:50-53(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN PROSTATE CANCER.
    40. "FBN1, TGFBR1, and the Marfan-craniosynostosis/mental retardation disorders revisited."
      Ades L.C., Sullivan K., Biggin A., Haan E.A., Brett M., Holman K.J., Dixon J., Robertson S., Holmes A.D., Rogers J., Bennetts B.
      Am. J. Med. Genet. A 140:1047-1058(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LDS1 LEU-241.
    41. "Identification and in silico analyses of novel TGFBR1 and TGFBR2 mutations in Marfan syndrome-related disorders."
      Matyas G., Arnold E., Carrel T., Baumgartner D., Boileau C., Berger W., Steinmann B.
      Hum. Mutat. 27:760-769(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LDS1 LEU-241 AND GLN-487, VARIANT HIS-267.
    42. Cited for: VARIANTS LDS1 GLU-232; TRP-487; PRO-487 AND GLN-487.
    43. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-153 AND CYS-291.
    44. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-139.
    45. "Loeys-Dietz syndrome type I and type II: clinical findings and novel mutations in two Italian patients."
      Drera B., Ritelli M., Zoppi N., Wischmeijer A., Gnoli M., Fattori R., Calzavara-Pinton P.G., Barlati S., Colombi M.
      Orphanet J. Rare Dis. 4:24-24(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LDS1 GLY-351.
    46. "Clinical features and genetic analysis of Korean patients with Loeys-Dietz syndrome."
      Yang J.H., Ki C.S., Han H., Song B.G., Jang S.Y., Chung T.Y., Sung K., Lee H.J., Kim D.K.
      J. Hum. Genet. 57:52-56(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LDS1 TYR-266; ILE-375 AND GLN-487.
    47. Cited for: VARIANTS MSSE TYR-41; SER-45; ARG-52 AND LEU-83.

    Entry informationi

    Entry nameiTGFR1_HUMAN
    AccessioniPrimary (citable) accession number: P36897
    Secondary accession number(s): Q6IR47, Q706C0, Q706C1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 174 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3