Reviewed, UniProtKB/Swiss-Prot P36897 (TGFR1_HUMAN)

Names and origin

Protein names

Recommended name:
    TGF-beta receptor type-1
    EC=2.7.11.30
Alternative name(s):
    Transforming growth factor-beta receptor type I
      Short name=TGF-beta receptor type I
    TGF-beta type I receptor
    TbetaR-I
    TGFR-1
    Serine/threonine-protein kinase receptor R4
      Short name=SKR4
    Activin receptor-like kinase 5
      Short name=ALK-5

Gene names

Name:

TGFBR1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for TGF-beta. Ref.5
Catalytic activity	ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
Cofactor	Magnesium or manganese By similarity.
Subunit structure	Interacts with CD109. The unphosphorylated protein interacts with FKBP1A and is stabilized the inactive conformation. Phosphorylation of the GS region abrogates FKBP1A binding. Interacts with SMAD2 when phosphorylated on several residues in the GS region. Ref.5 Ref.6 Ref.9
Subcellular location	Membrane; Single-pass type I membrane protein. Ref.5
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 binding. Activated by multiple phosphorylation, mainly in the GS region. Ref.5 Ref.9
Involvement in disease	Defects in TGFBR1 are the cause of Loeys-Dietz syndrome type 1A (LDS1A) [MIM:609192]; also known as Furlong syndrome or Loeys-Dietz aortic aneurysm syndrome (LDAS). LDS1 is 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. Ref.15 Ref.17 Ref.18 Defects in TGFBR1 are the cause of Loeys-Dietz syndrome type 2A (LDS2A) [MIM:608967]. LDS2 is an aortic aneurysm syndrome with widespread systemic involvement. 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, diffuse arterial aneurysms and dissections, and catastrophic complications of pregnancy, including rupture of the gravid uterus and the arteries, either during pregnancy or in the immediate postpartum period. LDS2 is characterized by the absence of craniofacial abnormalities with the exception of bifid uvula that can be present in some patients. Defects in TGFBR1 are the cause of aortic aneurysm familial thoracic type 5 (AAT5) [MIM:608967]. Aneurysms and dissections of the aorta usually result from degenerative changes in the aortic wall. Thoracic aortic aneurysms and dissections are primarily associated with a characteristic histologic appearance known as 'medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance. Ref.18
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
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Aortic aneurysm Craniosynostosis Disease mutation
Domain	Signal Transmembrane
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	activation of MAPKK activity Inferred from direct assay. Source: UniProtKB anterior/posterior pattern formation Inferred from sequence or structural similarity. Source: UniProtKB artery morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB collagen fibril organization Inferred from sequence or structural similarity. Source: UniProtKB embryonic cranial skeleton morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB germ cell migration Inferred from sequence or structural similarity. Source: UniProtKB heart development Inferred from sequence or structural similarity. Source: UniProtKB in utero embryonic development Inferred from sequence or structural similarity. Source: UniProtKB kidney development Inferred from sequence or structural similarity. Source: UniProtKB neuron fate commitment Inferred from sequence or structural similarity. Source: UniProtKB palate development Inferred from sequence or structural similarity. Source: UniProtKB parathyroid gland development Inferred from sequence or structural similarity. Source: UniProtKB pathway-restricted SMAD protein phosphorylation Inferred from direct assay. Source: UniProtKB peptidyl-serine phosphorylation Inferred from direct assay. Source: UniProtKB peptidyl-threonine phosphorylation Inferred from direct assay. Source: UniProtKB pharyngeal system development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of SMAD protein nuclear translocation Inferred from direct assay. Source: UniProtKB positive regulation of cell growth Inferred from direct assay. Source: UniProtKB positive regulation of cell motion Inferred from mutant phenotype. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype. Source: HGNC positive regulation of pathway-restricted SMAD protein phosphorylation Inferred from direct assay. Source: UniProtKB positive regulation of protein kinase B signaling cascade Inferred from direct assay. Source: UniProtKB positive regulation of survival gene product expression Inferred from mutant phenotype. Source: UniProtKB positive regulation of transcription Inferred from direct assay. Source: UniProtKB response to cholesterol Inferred from direct assay. Source: UniProtKB thymus development Inferred from sequence or structural similarity. Source: UniProtKB transforming growth factor beta receptor signaling pathway Inferred from direct assay. Source: UniProtKB
Cellular component	transforming growth factor beta receptor complex Inferred by curator. Source: UniProtKB
Molecular function	ATP binding Inferred from direct assay. Source: HGNC SMAD binding Inferred from direct assay. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein heterodimerization activity Inferred from direct assay. Source: UniProtKB transforming growth factor beta binding Inferred from direct assay. Source: UniProtKB transforming growth factor beta receptor activity, type I Inferred from direct assay. Source: UniProtKB type II transforming growth factor beta receptor binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STRAP	Q9Y3F4	1	EBI-1027557,EBI-727414

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Chain

25 – 503

479

TGF-beta receptor type-1

PRO_0000024423

Regions

Topological domain

25 – 125

101

Extracellular Potential

Transmembrane

126 – 147

22

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

Sites

Active site

333

1

Proton acceptor By similarity

Binding site

232

1

ATP By similarity

Amino acid modifications

Modified residue

185

1

Phosphothreonine Ref.5

Modified residue

186

1

Phosphothreonine Ref.5

Modified residue

187

1

Phosphoserine Ref.5

Modified residue

189

1

Phosphoserine Ref.5

Modified residue

191

1

Phosphoserine Ref.5

Glycosylation

45

1

N-linked (GlcNAc...) Potential

Disulfide bond

36 ↔ 54

Disulfide bond

38 ↔ 41

Disulfide bond

48 ↔ 71

Disulfide bond

86 ↔ 100

Disulfide bond

101 ↔ 106

Natural variations

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.12

VAR_022343

Natural variant

139

1

I → V

VAR_054160

Natural variant

153

1

V → I

VAR_041412

Natural variant

200

1

T → I in LDS1A. Ref.15

VAR_022344

Natural variant

232

1

K → E in LDS2A. Ref.19

VAR_029481

Natural variant

241

1

S → L in LDS1A. Ref.17 Ref.18

VAR_029482

Natural variant

267

1

N → H in a patient with Marfan syndrome. Ref.18

VAR_029483

Natural variant

291

1

Y → C

VAR_041413

Natural variant

318

1

M → R in LDS1A. Ref.15

VAR_022345

Natural variant

400

1

D → G in LDS1A. Ref.15

VAR_022346

Natural variant

487

1

R → P in LDS1A and LDS2A. Ref.15 Ref.19

VAR_022347

Natural variant

487

1

R → Q in LDS2A and AAT5. Ref.18 Ref.19

VAR_029484

Natural variant

487

1

R → W in LDS2A. Ref.19

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.5

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.5

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.5

Mutagenesis

200

1

T → D: Loss of response to TGF-beta. Ref.5

Mutagenesis

200

1

T → V: Loss of phosphorylation. Loss of response to TGF-beta. Ref.5

Mutagenesis

204

1

T → D: Constitutive activation. Ref.5

Mutagenesis

204

1

T → V: Reduced phosphorylation. Reduced response to TGF-beta. Ref.5

Secondary structure

1

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503

Helix Strand Turn

Details...

Helix

177 – 183

7

Beta strand

191 – 193

3

Helix

195 – 199

5

Helix

202 – 204

3

Beta strand

206 – 212

7

Beta strand

215 – 217

3

Beta strand

219 – 224

6

Beta strand

227 – 234

8

Helix

239 – 251

13

Beta strand

262 – 267

6

Beta strand

271 – 273

3

Beta strand

276 – 280

5

Helix

288 – 294

7

Helix

299 – 317

19

Beta strand

328 – 330

3

Helix

336 – 338

3

Beta strand

339 – 341

3

Beta strand

347 – 349

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

Turn

427 – 431

5

Helix

438 – 445

8

Helix

456 – 459

4

Helix

462 – 472

11

Helix

479 – 481

3

Helix

485 – 499

15

Sequences

	Sequence		Length	Mass (Da)
	P36897-1 [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

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: 8242743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 9417915] [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]	"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: 7774578] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT THR-185; THR-186; SER-187; SER-189 AND SER-191, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF 185-THR-THR-186; SER-187; SER-189; SER-191; THR-200 AND THR-204.
[6]	"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: 16754747] [Abstract] Cited for: INTERACTION WITH CD109.
[7]	"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: 8521960] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 34-114.
[8]	"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: 10025408] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 162-503 IN COMPLEX WITH FKBP1A.
[9]	"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: 11583628] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 162-503, PHOSPHORYLATION, INTERACTION WITH SMAD2 AND FKBP1A.
[10]	"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: 15177479] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 175-500 IN COMPLEX WITH SYNTHETIC INHIBITOR.
[11]	"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: 15317461] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 201-503 IN COMPLEX WITH SYNTHETIC INHIBITOR.
[12]	"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.V.S., Massague J. Cancer Res. 58:2727-2732(1998) [PubMed: 9661882] [Abstract] Cited for: VARIANT TGFBR1*6A ALA-24--26-ALA DEL, VARIANT TGFBR1*10A ALA-26 INS.
[13]	"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: 12947057] [Abstract] Cited for: ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN CANCER RISK.
[14]	"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: 15385056] [Abstract] Cited for: ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN PROSTATE CANCER.
[15]	"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: 15731757] [Abstract] Cited for: VARIANTS LDS1A ILE-200; ARG-318; GLY-400 AND PRO-487.
[16]	"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: 15505640] [Abstract] Cited for: ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN PROSTATE CANCER.
[17]	"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: 16596670] [Abstract] Cited for: VARIANT LDS1A LEU-241.
[18]	"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: 16791849] [Abstract] Cited for: VARIANT LDS1A LEU-241, VARIANT AAT5 GLN-487, VARIANT HIS-267.
[19]	"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: 16928994] [Abstract] Cited for: VARIANTS LDS2A GLU-232; TRP-487; PRO-487 AND GLN-487.
[20]	"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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-153 AND CYS-291.
[21]	"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: 18987736] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-139.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00005733.

PIR

A49432.

RefSeq

NP_004603.1.

UniGene

Hs.494622

3D structure databases

PDBPDBe

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	[»]
2PJY	X-ray	3.00	C	33-111	[»]
2WOT	X-ray	1.85	A	200-503	[»]
2WOU	X-ray	2.30	A	200-503	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5935N.

IntAct

P36897. 5 interactions.

STRING

P36897.

PTM databases

PhosphoSite

P36897.

Proteomic databases

PRIDE

P36897.

Genome annotation databases

Ensembl

ENST00000374990; ENSP00000364129; ENSG00000106799; Homo sapiens. [Genome view]
ENST00000374994; ENSP00000364133; ENSG00000106799; Homo sapiens. [Genome view]

GeneID

7046.

UCSC

uc004azc.1. human.

Organism-specific databases

CTD

7046.

GeneCards

GC09P100907.

H-InvDB

HIX0008228.

HGNC

HGNC:11772. TGFBR1.

MIM

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

Orphanet

60030. Aortic aneurysm syndrome, Loeys-Dietz type.
97295. Furlong syndrome.
91387. Thoracic aortic aneurysm, familial form.

PharmGKB

PA36485.

GenAtlas

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Phylogenomic databases

HOGENOM

P36897.

HOVERGEN

P36897.

OMA

KIELPTT.

Enzyme and pathway databases

BRENDA

2.7.10.2. 247.
2.7.11.30. 247.

Pathway_Interaction_DB

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

Reactome

REACT_6844. Signaling by TGF beta.

Gene expression databases

ArrayExpress

P36897.

Bgee

P36897.

CleanEx

HS_TGFBR1.

Genevestigator

P36897.

GermOnline

ENSG00000106799. Homo sapiens.

Family and domain databases

InterPro

IPR000472. Activin_rcpt.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_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]

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00467. GS. 1 hit.
[Graphical view]

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 Resources

NextBio

27533.

SOURCE

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Entry information

Entry name

TGFR1_HUMAN

Accession

Primary (citable) accession number: P36897

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 3, 2009
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.