P36897 (TGFR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 junction › tight 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 abbrogates 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 process	Apoptosis Differentiation Growth regulation
Cellular component	Cell junction Cell membrane Membrane Tight junction
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Aortic aneurysm Craniosynostosis Disease mutation
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Disulfide bond Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of MAPKK activity Inferred from direct assay PubMed 18625725. Source: BHF-UCL angiogenesis Inferred from electronic annotation. Source: Compara 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: Compara cell cycle arrest Traceable author statement Ref.26. Source: UniProtKB 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: Compara epithelial to mesenchymal transition Inferred from direct assay Ref.22. 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 induction of apoptosis Inferred from electronic annotation. Source: Compara kidney development Inferred from sequence or structural similarity. Source: BHF-UCL lens development in camera-type eye Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from mutant phenotype PubMed 18625725. Source: BHF-UCL 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: Compara 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 12015308PubMed 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 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: Compara 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 cascade Inferred from direct assay PubMed 18625725. Source: BHF-UCL positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.14PubMed 9389648. Source: BHF-UCL post-embryonic development Inferred from electronic annotation. Source: Compara regulation of protein binding Inferred from electronic annotation. Source: Compara regulation of protein ubiquitination Inferred from direct assay Ref.25. Source: UniProtKB response to cholesterol Inferred from direct assay PubMed 17878231. 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_component	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_function	ATP binding Inferred from direct assay PubMed 12065756. Source: HGNC SMAD binding Inferred from direct assay PubMed 18625725. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 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
TGFB1	P01137	2	EBI-1027557,EBI-779636
YWHAZ	P63104	4	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 33

33

Ref.7

Chain

34 – 503

470

TGF-beta receptor type-1

PRO_0000024423

Regions

Topological domain

34 – 126

93

Extracellular Potential

Transmembrane

127 – 147

21

Helical; Potential

Topological domain

148 – 503

356

Cytoplasmic Potential

Domain

175 – 204

30

GS

Domain

205 – 495

291

Protein kinase

Nucleotide binding

211 – 219

9

ATP By similarity

Motif

193 – 194

2

FKBP1A-binding

Sites

Active site

333

1

Proton acceptor By similarity

Binding site

232

1

ATP By similarity

Amino acid modifications

Modified residue

165

1

Phosphoserine Ref.27

Modified residue

185

1

Phosphothreonine; by TGFBR2 Ref.10

Modified residue

186

1

Phosphothreonine; by TGFBR2 Ref.10

Modified residue

187

1

Phosphoserine; by TGFBR2 Ref.10

Modified residue

189

1

Phosphoserine; by TGFBR2 Ref.10

Modified residue

191

1

Phosphoserine; by TGFBR2 Ref.10

Glycosylation

45

1

N-linked (GlcNAc...) Potential

Disulfide bond

36 ↔ 54

Ref.34 Ref.35

Disulfide bond

38 ↔ 41

Ref.34 Ref.35

Disulfide bond

48 ↔ 71

Ref.34 Ref.35

Disulfide bond

86 ↔ 100

Ref.34 Ref.35

Disulfide bond

101 ↔ 106

Ref.34 Ref.35

Cross-link

391

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence

114

1

T → TGPFS in isoform 2.

VSP_041326

Alternative sequence

115 – 191

77

Missing in isoform 3.

VSP_041327

Natural variant

24 – 26

3

Missing in allele TGFBR1*6A; could be a tumor susceptibility allele.

VAR_022342

Natural variant

26

1

A → AA in allele TGFBR1*10A; rare polymorphism. Ref.7

VAR_022343

Natural variant

41

1

C → Y in MSSE; hypomorphic mutation. Ref.47

VAR_065826

Natural variant

45

1

N → S in MSSE; hypomorphic mutation. Ref.47

VAR_065827

Natural variant

52

1

G → R in MSSE; hypomorphic mutation. Ref.47

VAR_065828

Natural variant

83

1

P → L in MSSE; hypomorphic mutation. Ref.47

VAR_065829

Natural variant

139

1

I → V. Ref.44

VAR_054160

Natural variant

153

1

V → I. Ref.43
Corresponds to variant rs56014374 [ dbSNP | Ensembl ].

VAR_041412

Natural variant

200

1

T → I in LDS1A. Ref.38

VAR_022344

Natural variant

232

1

K → E in LDS2A. Ref.42

VAR_029481

Natural variant

241

1

S → L in LDS1A. Ref.40 Ref.41

VAR_029482

Natural variant

266

1

D → Y in LDS1A. Ref.46

VAR_066720

Natural variant

267

1

N → H in a patient with Marfan syndrome. Ref.41

VAR_029483

Natural variant

291

1

Y → C. Ref.43
Corresponds to variant rs35974499 [ dbSNP | Ensembl ].

VAR_041413

Natural variant

318

1

M → R in LDS1A. Ref.38

VAR_022345

Natural variant

351

1

D → G in LDS1A. Ref.45

VAR_066721

Natural variant

375

1

T → I in LDS1A. Ref.46

VAR_066722

Natural variant

400

1

D → G in LDS1A. Ref.38

VAR_022346

Natural variant

487

1

R → P in LDS1A and LDS2A. Ref.38 Ref.42

VAR_022347

Natural variant

487

1

R → Q in LDS1A and LDS2A. Ref.41 Ref.42 Ref.46

VAR_029484

Natural variant

487

1

R → W in LDS2A. Ref.42

VAR_029485

Experimental info

Mutagenesis

185 – 186

2

TT → 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.

Mutagenesis

187

1

S → 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

Mutagenesis

189

1

S → 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

Mutagenesis

191

1

S → 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

Mutagenesis

193

1

L → G: Loss of interaction with FKBP1A. Ref.13

Mutagenesis

194

1

P → K: Loss of interaction with FKBP1A. Ref.13

Mutagenesis

200

1

T → D: Loss of response to TGF-beta. Ref.10

Mutagenesis

200

1

T → V: Loss of phosphorylation. Loss of response to TGF-beta. Ref.10

Mutagenesis

204

1

T → D: Constitutive activation. Ref.10

Mutagenesis

204

1

T → V: Reduced phosphorylation. Reduced response to TGF-beta. Ref.10

Secondary structure

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503

Helix Strand Turn

Details...

Beta strand

35 – 37

3

Turn

42 – 46

5

Beta strand

51 – 57

7

Beta strand

61 – 63

3

Beta strand

69 – 72

4

Turn

74 – 76

3

Beta strand

77 – 82

6

Turn

84 – 86

3

Helix

89 – 92

4

Beta strand

94 – 101

8

Beta strand

102 – 105

4

Helix

107 – 109

3

Helix

177 – 183

7

Beta strand

187 – 190

4

Beta strand

191 – 193

3

Helix

202 – 204

3

Beta strand

205 – 213

9

Beta strand

215 – 224

10

Beta strand

227 – 234

8

Helix

236 – 238

3

Helix

239 – 249

11

Beta strand

251 – 253

3

Beta strand

262 – 269

8

Beta strand

271 – 281

11

Helix

288 – 294

7

Helix

299 – 317

19

Beta strand

322 – 324

3

Beta strand

328 – 330

3

Beta strand

338 – 341

4

Beta strand

347 – 349

3

Helix

352 – 354

3

Beta strand

356 – 359

4

Turn

360 – 363

4

Beta strand

364 – 366

3

Helix

376 – 378

3

Helix

381 – 384

4

Helix

393 – 413

21

Beta strand

417 – 419

3

Turn

427 – 431

5

Helix

438 – 445

8

Helix

456 – 459

4

Helix

462 – 472

11

Helix

479 – 481

3

Helix

485 – 497

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 179F11404725DDCB	FASTA	503	55,960
	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
	Isoform 2 (B) [UniParc]. Checksum: 9EFAF4435F30E4C2	FASTA	507	56,348
	10 20 30 40 50 60 MEAAVAAPRP RLLLLVLAAA AAAAAALLPG ATALQCFCHL CTKDNFTCVT DGLCFVSVTE 70 80 90 100 110 120 TTDKVIHNSM CIAEIDLIPR DRPFVCAPSS KTGSVTTTYC CNQDHCNKIE LPTTGPFSVK 130 140 150 160 170 180 SSPGLGPVEL AAVIAGPVCF VCISLMLMVY ICHNRTVIHH RVPNEEDPSL DRPFISEGTT 190 200 210 220 230 240 LKDLIYDMTT SGSGSGLPLL VQRTIARTIV LQESIGKGRF GEVWRGKWRG EEVAVKIFSS 250 260 270 280 290 300 REERSWFREA EIYQTVMLRH ENILGFIAAD NKDNGTWTQL WLVSDYHEHG SLFDYLNRYT 310 320 330 340 350 360 VTVEGMIKLA LSTASGLAHL HMEIVGTQGK PAIAHRDLKS KNILVKKNGT CCIADLGLAV 370 380 390 400 410 420 RHDSATDTID IAPNHRVGTK RYMAPEVLDD SINMKHFESF KRADIYAMGL VFWEIARRCS 430 440 450 460 470 480 IGGIHEDYQL PYYDLVPSDP SVEEMRKVVC EQKLRPNIPN RWQSCEALRV MAKIMRECWY 490 500 ANGAARLTAL RIKKTLSQLS QQEGIKM
	Isoform 3 [UniParc]. Checksum: 97EA2F587AFA08F6	FASTA	426	47,690
	10 20 30 40 50 60 MEAAVAAPRP RLLLLVLAAA AAAAAALLPG ATALQCFCHL CTKDNFTCVT DGLCFVSVTE 70 80 90 100 110 120 TTDKVIHNSM CIAEIDLIPR DRPFVCAPSS KTGSVTTTYC CNQDHCNKIE LPTTGLPLLV 130 140 150 160 170 180 QRTIARTIVL QESIGKGRFG EVWRGKWRGE EVAVKIFSSR EERSWFREAE IYQTVMLRHE 190 200 210 220 230 240 NILGFIAADN KDNGTWTQLW LVSDYHEHGS LFDYLNRYTV TVEGMIKLAL STASGLAHLH 250 260 270 280 290 300 MEIVGTQGKP AIAHRDLKSK NILVKKNGTC CIADLGLAVR HDSATDTIDI APNHRVGTKR 310 320 330 340 350 360 YMAPEVLDDS INMKHFESFK RADIYAMGLV FWEIARRCSI GGIHEDYQLP YYDLVPSDPS 370 380 390 400 410 420 VEEMRKVVCE QKLRPNIPNR WQSCEALRVM AKIMRECWYA NGAARLTALR IKKTLSQLSQ QEGIKM

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY.
[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. , 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. , 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. , 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. , 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. , 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.

Web resources

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00005733.
IPI00844074.
IPI01018344.

PIR

A49432.

RefSeq

NP_001124388.1. NM_001130916.1.
NP_004603.1. NM_004612.2.

UniGene

Hs.494622.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P36897.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5935N.

IntAct

P36897. 5 interactions.

MINT

MINT-152959.

STRING

9606.ENSP00000364133.

PTM databases

PhosphoSite

P36897.

Polymorphism databases

DMDM

547777.

Proteomic databases

PaxDb

P36897.

PRIDE

P36897.

Protocols and materials databases

DNASU

7046.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374990; ENSP00000364129; ENSG00000106799.
ENST00000374994; ENSP00000364133; ENSG00000106799.
ENST00000552516; ENSP00000447297; ENSG00000106799.

GeneID

7046.

KEGG

hsa:7046.

UCSC

uc004azc.3. human.
uc004azd.3. human.
uc004aze.3. human.

Organism-specific databases

CTD

7046.

GeneCards

GC09P101867.

HGNC

HGNC:11772. TGFBR1.

HPA

CAB002441.
CAB031481.

MIM

132800. phenotype.
190181. gene.
608967. phenotype.
609192. phenotype.

neXtProt

NX_P36897.

Orphanet

91387. Familial thoracic aortic aneurysm and aortic dissection.
60030. Loeys-Dietz syndrome type 1.
65748. Multiple keratoacanthoma, Ferguson-Smith type.

PharmGKB

PA36485.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000230587.

HOVERGEN

HBG054502.

InParanoid

P36897.

KO

K04674.

OMA

CISLMLI.

OrthoDB

EOG4JQ3XG.

PhylomeDB

P36897.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

glypican_1pathway. Glypican 1 network.
tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_111102. Signal Transduction.

SignaLink

P36897.

Gene expression databases

ArrayExpress

P36897.

Bgee

P36897.

CleanEx

HS_TGFBR1.

Genevestigator

P36897.

GermOnline

ENSG00000106799. Homo sapiens.

Family and domain databases

InterPro

IPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR003605. TGF_beta_rcpt_GS.
[Graphical view]

Pfam

PF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]

SMART

SM00467. GS. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P36897.

ChEMBL

CHEMBL4439.

ChiTaRS

TGFBR1. human.

EvolutionaryTrace

P36897.

GenomeRNAi

7046.

NextBio

27533.

SOURCE

Search...

Entry information

Entry name

TGFR1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 160 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.