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P36897 (TGFR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TGF-beta receptor type-1

Short name=TGFR-1
EC=2.7.11.30
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 names
Name:TGFBR1
Synonyms:ALK5, SKR4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11 Ref.12 Ref.15 Ref.22 Ref.23 Ref.25

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Enzyme regulation

Kept in an inactive conformation by FKBP1A preventing receptor activation in absence of ligand. CD109 is another inhibitor of the receptor. Ref.13

Subunit structure

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. Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.31

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cell junctiontight junction Ref.10 Ref.17 Ref.22.

Tissue specificity

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

Post-translational modification

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. Ref.10 Ref.31

N-Glycosylated. Ref.7

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. Ref.18 Ref.19 Ref.21 Ref.28

Involvement in disease

Loeys-Dietz syndrome 1A (LDS1A) [MIM:609192]: An aortic aneurysm syndrome with widespread systemic involvement. The disorder is characterized by arterial tortuosity and aneurysms, craniosynostosis, hypertelorism, and bifid uvula or cleft palate. Other findings include exotropy, micrognathia and retrognathia, structural brain abnormalities, intellectual deficit, congenital heart disease, translucent skin, joint hyperlaxity and aneurysm with dissection throughout the arterial tree.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38 Ref.40 Ref.41 Ref.45 Ref.46

Loeys-Dietz syndrome 2A (LDS2A) [MIM:608967]: An aortic aneurysm syndrome with widespread systemic involvement. Physical findings include diffuse arterial aneurysms and dissections, 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. Loeys-Dietz syndrome type 2 is characterized by the absence of craniofacial abnormalities with the exception of bifid uvula that can be present in some patients.
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) (Ref.41). This phenotype, also known as thoracic aortic aneurysms type 5 (AAT5), is distinguised from LDS2A 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 LDS2A by the OMIM resource. Ref.41 Ref.42

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.47

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.

Contains 1 GS domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Differentiation
Growth regulation
   Cellular componentCell junction
Cell membrane
Membrane
Tight junction
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAortic aneurysm
Craniosynostosis
Disease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPKK activity

Inferred from direct assay PubMed 18625725. Source: BHF-UCL

angiogenesis

Inferred from electronic annotation. Source: Ensembl

anterior/posterior pattern specification

Inferred from sequence or structural similarity. Source: BHF-UCL

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

artery morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

blastocyst development

Inferred from electronic annotation. Source: Ensembl

cell cycle arrest

Traceable author statement Ref.26. Source: UniProtKB

cell motility

Inferred from mutant phenotype PubMed 18625725. Source: BHF-UCL

cellular response to transforming growth factor beta stimulus

Inferred from direct assay PubMed 19494318. Source: BHF-UCL

collagen fibril organization

Inferred from sequence or structural similarity. Source: BHF-UCL

embryonic cranial skeleton morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

epithelial to mesenchymal transition

Inferred from direct assay Ref.22. Source: UniProtKB

extracellular structure organization

Traceable author statement Ref.26. Source: UniProtKB

germ cell migration

Inferred from sequence or structural similarity. Source: BHF-UCL

heart development

Inferred from sequence or structural similarity. Source: BHF-UCL

in utero embryonic development

Inferred from sequence or structural similarity. Source: BHF-UCL

kidney development

Inferred from sequence or structural similarity. Source: BHF-UCL

lens development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

mesenchymal cell differentiation

Traceable author statement Ref.26. Source: UniProtKB

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of chondrocyte differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 18625725. Source: BHF-UCL

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

neuron fate commitment

Inferred from sequence or structural similarity. Source: BHF-UCL

palate development

Inferred from sequence or structural similarity. Source: BHF-UCL

parathyroid gland development

Inferred from sequence or structural similarity. Source: BHF-UCL

pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 11157754PubMed 12015308PubMed 18625725PubMed 19736306. Source: BHF-UCL

peptidyl-serine phosphorylation

Inferred from direct assay Ref.22. Source: UniProtKB

peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 19736306. Source: BHF-UCL

pharyngeal system development

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of SMAD protein import into nucleus

Inferred from direct assay PubMed 9389648. Source: BHF-UCL

positive regulation of apoptotic signaling pathway

Inferred from direct assay Ref.25. Source: UniProtKB

positive regulation of cell growth

Inferred from direct assay PubMed 18625725. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 14633705. Source: HGNC

positive regulation of cellular component movement

Inferred from mutant phenotype PubMed 18625725. Source: BHF-UCL

positive regulation of filopodium assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from direct assay Ref.14PubMed 9389648. Source: BHF-UCL

positive regulation of protein kinase B signaling

Inferred from direct assay PubMed 18625725. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.14PubMed 9389648. Source: BHF-UCL

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 12015308. Source: BHF-UCL

regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

regulation of protein ubiquitination

Inferred from direct assay Ref.25. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 14517293. Source: HGNC

response to cholesterol

Inferred from direct assay PubMed 17878231. Source: BHF-UCL

signal transduction

Inferred from direct assay PubMed 14633705. Source: HGNC

skeletal system development

Inferred from sequence or structural similarity. Source: BHF-UCL

skeletal system morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

thymus development

Inferred from sequence or structural similarity. Source: BHF-UCL

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 11157754PubMed 9389648. Source: BHF-UCL

wound healing

Traceable author statement Ref.26. Source: UniProtKB

   Cellular_componentplasma membrane

Inferred from direct assay PubMed 17878231. Source: BHF-UCL

receptor complex

Inferred from direct assay PubMed 8774881. Source: BHF-UCL

tight junction

Inferred from direct assay Ref.22. Source: UniProtKB

transforming growth factor beta receptor homodimeric complex

Inferred by curator PubMed 1326540. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from direct assay PubMed 12065756. Source: HGNC

I-SMAD binding

Inferred from physical interaction Ref.19. Source: BHF-UCL

SMAD binding

Inferred from direct assay PubMed 18625725. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase activity

Inferred from direct assay PubMed 19736306. Source: BHF-UCL

protein serine/threonine kinase activity

Inferred from direct assay PubMed 18625725. Source: BHF-UCL

transforming growth factor beta binding

Inferred from direct assay PubMed 11157754. Source: BHF-UCL

transforming growth factor beta receptor activity, type I

Inferred from direct assay Ref.11. Source: BHF-UCL

transforming growth factor beta-activated receptor activity

Inferred from direct assay PubMed 12015308. Source: BHF-UCL

type II transforming growth factor beta receptor binding

Inferred from direct assay PubMed 11157754. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q99IB85EBI-1027557,EBI-6858501From a different organism.
TGFB1P011372EBI-1027557,EBI-779636
YWHAZP631044EBI-1027557,EBI-347088

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P36897-1)

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.
Isoform 2 (identifier: P36897-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     114-114: T → TGPFS
Isoform 3 (identifier: P36897-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Ref.7
Chain34 – 503470TGF-beta receptor type-1
PRO_0000024423

Regions

Topological domain34 – 12693Extracellular Potential
Transmembrane127 – 14721Helical; Potential
Topological domain148 – 503356Cytoplasmic Potential
Domain175 – 20430GS
Domain205 – 495291Protein kinase
Nucleotide binding211 – 2199ATP By similarity
Motif193 – 1942FKBP1A-binding

Sites

Active site3331Proton acceptor By similarity
Binding site2321ATP By similarity

Amino acid modifications

Modified residue1651Phosphoserine Ref.27
Modified residue1851Phosphothreonine; by TGFBR2 Ref.10
Modified residue1861Phosphothreonine; by TGFBR2 Ref.10
Modified residue1871Phosphoserine; by TGFBR2 Ref.10
Modified residue1891Phosphoserine; by TGFBR2 Ref.10
Modified residue1911Phosphoserine; by TGFBR2 Ref.10
Glycosylation451N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 54 Ref.34 Ref.35
Disulfide bond38 ↔ 41 Ref.34 Ref.35
Disulfide bond48 ↔ 71 Ref.34 Ref.35
Disulfide bond86 ↔ 100 Ref.34 Ref.35
Disulfide bond101 ↔ 106 Ref.34 Ref.35
Cross-link391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1141T → TGPFS in isoform 2.
VSP_041326
Alternative sequence115 – 19177Missing in isoform 3.
VSP_041327
Natural variant24 – 263Missing in allele TGFBR1*6A; could be a tumor susceptibility allele.
VAR_022342
Natural variant261A → AA in allele TGFBR1*10A; rare polymorphism. Ref.7
VAR_022343
Natural variant411C → Y in MSSE; hypomorphic mutation. Ref.47
VAR_065826
Natural variant451N → S in MSSE; hypomorphic mutation. Ref.47
VAR_065827
Natural variant521G → R in MSSE; hypomorphic mutation. Ref.47
VAR_065828
Natural variant831P → L in MSSE; hypomorphic mutation. Ref.47
VAR_065829
Natural variant1391I → V. Ref.44
VAR_054160
Natural variant1531V → I. Ref.43
Corresponds to variant rs56014374 [ dbSNP | Ensembl ].
VAR_041412
Natural variant2001T → I in LDS1A. Ref.38
VAR_022344
Natural variant2321K → E in LDS2A. Ref.42
VAR_029481
Natural variant2411S → L in LDS1A. Ref.40 Ref.41
VAR_029482
Natural variant2661D → Y in LDS1A. Ref.46
VAR_066720
Natural variant2671N → H in a patient with Marfan syndrome. Ref.41
VAR_029483
Natural variant2911Y → C. Ref.43
Corresponds to variant rs35974499 [ dbSNP | Ensembl ].
VAR_041413
Natural variant3181M → R in LDS1A. Ref.38
VAR_022345
Natural variant3511D → G in LDS1A. Ref.45
VAR_066721
Natural variant3751T → I in LDS1A. Ref.46
VAR_066722
Natural variant4001D → G in LDS1A. Ref.38
VAR_022346
Natural variant4871R → P in LDS1A and LDS2A. Ref.38 Ref.42
VAR_022347
Natural variant4871R → Q in LDS1A and LDS2A. Ref.41 Ref.42 Ref.46
VAR_029484
Natural variant4871R → W in LDS2A. Ref.42
VAR_029485

Experimental info

Mutagenesis185 – 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.
Mutagenesis1871S → 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. Ref.10
Mutagenesis1891S → 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. Ref.10
Mutagenesis1911S → 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. Ref.10
Mutagenesis1931L → G: Loss of interaction with FKBP1A. Ref.13
Mutagenesis1941P → K: Loss of interaction with FKBP1A. Ref.13
Mutagenesis2001T → D: Loss of response to TGF-beta. Ref.10
Mutagenesis2001T → V: Loss of phosphorylation. Loss of response to TGF-beta. Ref.10
Mutagenesis2041T → D: Constitutive activation. Ref.10
Mutagenesis2041T → V: Reduced phosphorylation. Reduced response to TGF-beta. Ref.10

Secondary structure

.................................................................................. 503
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 179F11404725DDCB

FASTA50355,960
        10         20         30         40         50         60 
MEAAVAAPRP RLLLLVLAAA AAAAAALLPG ATALQCFCHL CTKDNFTCVT DGLCFVSVTE 

        70         80         90        100        110        120 
TTDKVIHNSM CIAEIDLIPR DRPFVCAPSS KTGSVTTTYC CNQDHCNKIE LPTTVKSSPG 

       130        140        150        160        170        180 
LGPVELAAVI AGPVCFVCIS LMLMVYICHN RTVIHHRVPN EEDPSLDRPF ISEGTTLKDL 

       190        200        210        220        230        240 
IYDMTTSGSG SGLPLLVQRT IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER 

       250        260        270        280        290        300 
SWFREAEIYQ TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE 

       310        320        330        340        350        360 
GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA DLGLAVRHDS 

       370        380        390        400        410        420 
ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD IYAMGLVFWE IARRCSIGGI 

       430        440        450        460        470        480 
HEDYQLPYYD LVPSDPSVEE MRKVVCEQKL RPNIPNRWQS CEALRVMAKI MRECWYANGA 

       490        500 
ARLTALRIKK TLSQLSQQEG IKM 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 9EFAF4435F30E4C2
Show »

FASTA50756,348
Isoform 3 [UniParc].

Checksum: 97EA2F587AFA08F6
Show »

FASTA42647,690

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4."
Nakao A., Imamura T., Souchelnytskyi S., Kawabata M., Ishisaki A., Oeda E., Tamaki K., Hanai J., Heldin C.H., Miyazono K., ten Dijke P.
EMBO J. 16:5353-5362(1997) [PubMed] [Europe PMC] [Abstract]
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]"TGF-beta signal transduction."
Massague J.
Annu. Rev. Biochem. 67:753-791(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON PROCESSES REGULATED BY THE TGF-BETA CYTOKINES.
[27]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"No major association between TGFBR1*6A and prostate cancer."
Kaklamani V.G., Baddi L., Rosman D., Liu J., Ellis N., Oddoux C., Ostrer H., Chen Y., Ahsan H., Offit K., Pasche B.
BMC Genet. 5:28-28(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN PROSTATE CANCER.
[38]"A syndrome of altered cardiovascular, craniofacial, neurocognitive and skeletal development caused by mutations in TGFBR1 or TGFBR2."
Loeys B.L., Chen J., Neptune E.R., Judge D.P., Podowski M., Holm T., Meyers J., Leitch C.C., Katsanis N., Sharifi N., Xu F.L., Myers L.A., Spevak P.J., Cameron D.E., De Backer J.F., Hellemans J., Chen Y., Davis E.C. expand/collapse author list , Webb C.L., Kress W., Coucke P.J., Rifkin D.B., De Paepe A.M., Dietz H.C.
Nat. Genet. 37:275-281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LDS1A 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 LDS1A 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: VARIANT LDS1A LEU-241, VARIANT LDS2A GLN-487, VARIANT HIS-267.
[42]"Aneurysm syndromes caused by mutations in the TGF-beta receptor."
Loeys B.L., Schwarze U., Holm T., Callewaert B.L., Thomas G.H., Pannu H., De Backer J.F., Oswald G.L., Symoens S., Manouvrier S., Roberts A.E., Faravelli F., Greco M.A., Pyeritz R.E., Milewicz D.M., Coucke P.J., Cameron D.E., Braverman A.C. expand/collapse author list , Byers P.H., De Paepe A.M., Dietz H.C.
N. Engl. J. Med. 355:788-798(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LDS2A 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. expand/collapse author list , 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]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
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 LDS1A 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 LDS1A TYR-266; ILE-375 AND GLN-487.
[47]"Multiple self-healing squamous epithelioma is caused by a disease-specific spectrum of mutations in TGFBR1."
Goudie D.R., D'Alessandro M., Merriman B., Lee H., Szeverenyi I., Avery S., O'Connor B.D., Nelson S.F., Coats S.E., Stewart A., Christie L., Pichert G., Friedel J., Hayes I., Burrows N., Whittaker S., Gerdes A.M., Broesby-Olsen S. expand/collapse author list , Ferguson-Smith M.A., Verma C., Lunny D.P., Reversade B., Lane E.B.
Nat. Genet. 43:365-369(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MSSE TYR-41; SER-45; ARG-52 AND LEU-83.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L11695 mRNA. Translation: AAA16073.1.
AF054598 expand/collapse EMBL AC list , AF054590, AF054591, AF054592, AF054593, AF054594, AF054595, AF054596, AF054597 Genomic DNA. Translation: AAC08998.1.
AF035670 expand/collapse EMBL AC list , 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.
PIRA49432.
RefSeqNP_001124388.1. NM_001130916.1.
NP_004603.1. NM_004612.2.
XP_005252207.1. XM_005252150.1.
UniGeneHs.494622.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP36897.
SMRP36897. Positions 31-115, 175-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112904. 171 interactions.
DIPDIP-5935N.
IntActP36897. 10 interactions.
MINTMINT-152959.
STRING9606.ENSP00000364133.

Chemistry

BindingDBP36897.
ChEMBLCHEMBL4439.
GuidetoPHARMACOLOGY1788.

PTM databases

PhosphoSiteP36897.

Polymorphism databases

DMDM547777.

Proteomic databases

PaxDbP36897.
PRIDEP36897.

Protocols and materials databases

DNASU7046.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374990; ENSP00000364129; ENSG00000106799. [P36897-3]
ENST00000374994; ENSP00000364133; ENSG00000106799. [P36897-1]
ENST00000552516; ENSP00000447297; ENSG00000106799. [P36897-2]
GeneID7046.
KEGGhsa:7046.
UCSCuc004azc.3. human. [P36897-1]
uc004azd.3. human. [P36897-3]
uc004aze.3. human. [P36897-2]

Organism-specific databases

CTD7046.
GeneCardsGC09P101867.
HGNCHGNC:11772. TGFBR1.
HPACAB002441.
CAB031481.
MIM132800. phenotype.
190181. gene.
608967. phenotype.
609192. phenotype.
neXtProtNX_P36897.
Orphanet91387. Familial thoracic aortic aneurysm and aortic dissection.
60030. Loeys-Dietz syndrome type 1.
65748. Multiple keratoacanthoma, Ferguson-Smith type.
PharmGKBPA36485.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000230587.
HOVERGENHBG054502.
InParanoidP36897.
KOK04674.
OMALYICHNR.
PhylomeDBP36897.
TreeFamTF314724.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkP36897.

Gene expression databases

ArrayExpressP36897.
BgeeP36897.
CleanExHS_TGFBR1.
GenevestigatorP36897.

Family and domain databases

InterProIPR000472. 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.
[Graphical view]
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTSM00467. GS. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTGFBR1. human.
EvolutionaryTraceP36897.
GeneWikiTGF_beta_receptor_1.
GenomeRNAi7046.
NextBio27533.
PROP36897.
SOURCESearch...

Entry information

Entry nameTGFR1_HUMAN
AccessionPrimary (citable) accession number: P36897
Secondary accession number(s): Q6IR47, Q706C0, Q706C1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM