P37173 (TGFR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
TGF-beta receptor type-2
Short name=TGFR-2
EC=2.7.11.30

Alternative name(s):
TGF-beta type II receptor
Transforming growth factor-beta receptor type II
Short name=TGF-beta receptor type II
Short name=TbetaR-II

Gene names

Name:

TGFBR2

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	567 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 I serine/threonine kinase receptor, TGFBR1, 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 TGFRB1 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. Ref.11
Catalytic activity	ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
Cofactor	Magnesium or manganese By similarity.
Subunit structure	Homodimer. 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 TGFRB1 and TGFRB2 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 DAXX. Interacts with TCTEX1D4. Interacts with ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta receptor. Interacts with and is activated by SCUBE3; this interaction does not affect TGFB1-binding to TGFBR2. Interacts with VPS39; this interaction is independent of the receptor kinase activity and of the presence of TGF-beta. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19
Subcellular location	Cell membrane; Single-pass type I membrane protein Ref.1.
Post-translational modification	Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.
Involvement in disease	Hereditary non-polyposis colorectal cancer 6 (HNPCC6) [MIM:614331]: An autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra-colonic tumors of the gastrointestinal, urological and female reproductive tracts. HNPCC is reported to be the most common form of inherited colorectal cancer in the Western world. Clinically, HNPCC is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical HNPCC is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term 'suspected HNPCC' or 'incomplete HNPCC' can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25 Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage. Note: The disease is caused by mutations affecting the gene represented in this entry. Loeys-Dietz syndrome 1B (LDS1B) [MIM:610168]: 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.31 Ref.32 Ref.36 Ref.37 Ref.38 Ref.39 Loeys-Dietz syndrome 2B (LDS2B) [MIM:610380]: 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. TGFBR2 mutations Cys-460 and His-460 have been reported to be associated with thoracic aortic aneurysms and dissection (TAAD). This phenotype, also known as thoracic aortic aneurysms type 3 (AAT3), is distinguised from LDS2B by having aneurysms restricted to thoracic aorta. As individuals carrying these mutations also exhibit descending aortic disease and aneurysms of other arteries (Ref.30), they have been considered as LDS2B by the OMIM resource. Ref.29 Ref.30 Ref.35
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Apoptosis Differentiation Growth regulation
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Aortic aneurysm Disease mutation Hereditary nonpolyposis colorectal cancer
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 Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of protein kinase activity Inferred from sequence or structural similarity. Source: BHF-UCL aging Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW brain development Inferred from sequence or structural similarity. Source: BHF-UCL bronchus morphogenesis Inferred from electronic annotation. Source: Compara cartilage development Inferred from electronic annotation. Source: Compara common-partner SMAD protein phosphorylation Inferred from electronic annotation. Source: Compara digestive tract development Inferred from electronic annotation. Source: Compara embryo implantation Inferred from electronic annotation. Source: Compara embryonic cranial skeleton morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL embryonic hemopoiesis Inferred from sequence or structural similarity. Source: BHF-UCL gastrulation Inferred from electronic annotation. Source: Compara heart development Inferred from sequence or structural similarity. Source: BHF-UCL in utero embryonic development Inferred from electronic annotation. Source: Compara lens development in camera-type eye Inferred from electronic annotation. Source: Compara lung lobe morphogenesis Inferred from electronic annotation. Source: Compara mammary gland morphogenesis Inferred from electronic annotation. Source: Compara myeloid dendritic cell differentiation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of cardiac muscle cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome organ regeneration Inferred from electronic annotation. Source: Compara palate development Inferred from sequence or structural similarity. Source: BHF-UCL pathway-restricted SMAD protein phosphorylation Inferred from direct assay PubMed 18453574PubMed 11157754. Source: BHF-UCL patterning of blood vessels Inferred from sequence or structural similarity. Source: BHF-UCL peptidyl-serine phosphorylation Inferred from direct assay PubMed 12015308. Source: BHF-UCL peptidyl-threonine phosphorylation Inferred from direct assay PubMed 12015308. Source: BHF-UCL positive regulation of B cell tolerance induction Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of NK T cell differentiation Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of T cell tolerance induction Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of epithelial cell migration Inferred from electronic annotation. Source: Compara positive regulation of mesenchymal cell proliferation Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of reactive oxygen species metabolic process Inferred from mutant phenotype PubMed 20160708. Source: BHF-UCL positive regulation of skeletal muscle tissue regeneration Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of tolerance induction to self antigen Inferred from sequence or structural similarity. Source: BHF-UCL receptor-mediated endocytosis Inferred from electronic annotation. Source: Compara response to cholesterol Inferred from direct assay PubMed 17878231. Source: BHF-UCL response to drug Inferred from direct assay PubMed 17878231. Source: BHF-UCL response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC smoothened signaling pathway Inferred from electronic annotation. Source: Compara trachea formation Inferred from electronic annotation. Source: Compara transforming growth factor beta receptor signaling pathway Inferred from direct assay PubMed 18453574. Source: BHF-UCL vasculogenesis Inferred from sequence or structural similarity. Source: BHF-UCL wound healing Inferred from electronic annotation. Source: Compara
Cellular_component	caveola Inferred from direct assay PubMed 17878231. Source: BHF-UCL cytosol Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from direct assay PubMed 18453574. Source: BHF-UCL transforming growth factor beta receptor homodimeric complex Inferred by curator PubMed 1326540. Source: BHF-UCL
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW SMAD binding Inferred from direct assay PubMed 11157754PubMed 18453574PubMed 11157754. Source: BHF-UCL glycosaminoglycan binding Inferred from direct assay PubMed 7852346. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor signaling protein serine/threonine kinase activity Inferred from electronic annotation. Source: InterPro transforming growth factor beta binding Inferred from direct assay Ref.23PubMed 18453574PubMed 7852346PubMed 11157754. Source: BHF-UCL transforming growth factor beta receptor activity, type II Inferred from electronic annotation. Source: InterPro transforming growth factor beta-activated receptor activity Inferred from direct assay PubMed 18453574PubMed 7852346. Source: BHF-UCL type I transforming growth factor beta receptor binding Inferred from direct assay PubMed 11157754. Source: BHF-UCL type III 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
DAXX	Q9UER7	2	EBI-296151,EBI-77321
SCUBE3	Q8IX30	6	EBI-296151,EBI-4479975
TGFB1	P01137	4	EBI-296151,EBI-779636
TGFB1	P07200	2	EBI-296151,EBI-907660	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P37173-1)

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: P37173-2)

The sequence of this isoform differs from the canonical sequence as follows:
     31-32: SV → SDVEMEAQKDEIICPSCNRTAHPLRHI

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.10

Chain

23 – 567

545

TGF-beta receptor type-2

PRO_0000024426

Regions

Topological domain

23 – 166

144

Extracellular Potential

Transmembrane

167 – 187

21

Helical; Potential

Topological domain

188 – 567

380

Cytoplasmic Potential

Domain

244 – 544

301

Protein kinase

Nucleotide binding

250 – 258

9

ATP By similarity

Sites

Active site

379

1

Proton acceptor By similarity

Binding site

277

1

ATP By similarity

Amino acid modifications

Modified residue

548

1

Phosphoserine Ref.17

Glycosylation

70

1

N-linked (GlcNAc...) Potential

Glycosylation

94

1

N-linked (GlcNAc...) Potential

Glycosylation

154

1

N-linked (GlcNAc...) Potential

Disulfide bond

51 ↔ 84

Ref.23 Ref.24

Disulfide bond

54 ↔ 71

Ref.23 Ref.24

Disulfide bond

61 ↔ 67

Ref.23 Ref.24

Disulfide bond

77 ↔ 101

Ref.23 Ref.24

Disulfide bond

121 ↔ 136

Ref.23 Ref.24

Disulfide bond

138 ↔ 143

Ref.23 Ref.24

Natural variations

Alternative sequence

31 – 32

2

SV → SDVEMEAQKDEIICPSCNRT AHPLRHI in isoform 2.

VSP_012157

Natural variant

36

1

M → V. Ref.7
Corresponds to variant rs17025864 [ dbSNP | Ensembl ].

VAR_020510

Natural variant

61

1

C → R in a gastric adenocarcinoma sample; somatic mutation. Ref.34

VAR_041414

Natural variant

73

1

I → V in a colorectal cancer sample; somatic mutation. Ref.33

VAR_036070

Natural variant

191

1

V → I. Ref.28 Ref.34
Corresponds to variant rs56105708 [ dbSNP | Ensembl ].

VAR_017606

Natural variant

306

1

Q → HE in LDS1B.

VAR_066723

Natural variant

308

1

L → P in LDS1B and LDS2B; has a negative effect on TGF-beta signaling. Ref.29 Ref.37
Corresponds to variant rs28934568 [ dbSNP | Ensembl ].

VAR_022351

Natural variant

315

1

T → M in HNPCC6. Ref.25 Ref.34
Corresponds to variant rs34833812 [ dbSNP | Ensembl ].

VAR_008156

Natural variant

328

1

H → Y in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.34

VAR_041415

Natural variant

336

1

Y → N in LDS1B. Ref.31

VAR_022352

Natural variant

355

1

A → P in LDS1B. Ref.31

VAR_022353

Natural variant

357

1

G → W in LDS1B. Ref.31

VAR_022354

Natural variant

373

1

M → I. Ref.34
Corresponds to variant rs35719192 [ dbSNP | Ensembl ].

VAR_041416

Natural variant

377

1

H → R in LDS1B. Ref.38

VAR_066724

Natural variant

387

1

V → M in a breast tumor. Ref.27 Ref.34
Corresponds to variant rs35766612 [ dbSNP | Ensembl ].

VAR_022355

Natural variant

435

1

N → S in a breast tumor; signaling of TGF-beta significantly inhibited. Ref.27

VAR_022356

Natural variant

439

1

V → A. Ref.1 Ref.4 Ref.5 Ref.6
Corresponds to variant rs1050833 [ dbSNP | Ensembl ].

VAR_028063

Natural variant

446

1

D → N in LDS1B. Ref.32

VAR_066725

Natural variant

447

1

V → A in a breast tumor; signaling of TGF-beta significantly inhibited. Ref.27

VAR_022357

Natural variant

449

1

S → F in LDS1B and LDS2B; has a negative effect on TGF-beta signaling. Ref.29 Ref.38

VAR_022358

Natural variant

452

1

L → M in a breast tumor; signaling of TGF-beta significantly inhibited. Ref.27

VAR_022359

Natural variant

457

1

M → K in LDS1B. Ref.36

VAR_066726

Natural variant

460

1

R → C in LDS2B. Ref.30

VAR_029760

Natural variant

460

1

R → H in LDS2B. Ref.30

VAR_029761

Natural variant

490

1

N → S in a gastric adenocarcinoma sample; somatic mutation. Ref.34

VAR_041417

Natural variant

509

1

G → V in LDS1B. Ref.39

VAR_066727

Natural variant

510

1

I → F in LDS1B. Ref.39

VAR_066728

Natural variant

510

1

I → S in LDS2B. Ref.35

VAR_066729

Natural variant

514

1

C → R in LDS1B. Ref.38

VAR_066730

Natural variant

521

1

W → R in LDS1B. Ref.37

VAR_066731

Natural variant

526

1

E → Q in esophageal cancer. Ref.26

VAR_015816

Natural variant

528

1

R → C in LDS1B. Ref.31

VAR_022360

Natural variant

528

1

R → H in LDS1B. Ref.31 Ref.33

VAR_022361

Natural variant

537

1

R → C in LDS2B; has a negative effect on TGF-beta signaling. Ref.29
Corresponds to variant rs28934869 [ dbSNP | Ensembl ].

VAR_022362

Experimental info

Mutagenesis

277

1

K → R: Abolishes kinase activity, TGF-beta signaling and interaction with DAXX. Ref.14

Sequence conflict

381

1

K → N in BAA09332. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

567

Helix Strand Turn

Details...

Beta strand

40 – 45

6

Beta strand

50 – 52

3

Beta strand

55 – 58

4

Beta strand

65 – 68

4

Beta strand

74 – 76

3

Beta strand

78 – 81

4

Beta strand

83 – 90

8

Beta strand

95 – 102

8

Beta strand

106 – 110

5

Turn

114 – 117

4

Beta strand

119 – 122

4

Beta strand

124 – 126

3

Beta strand

131 – 138

8

Beta strand

140 – 142

3

Helix

143 – 145

3

Beta strand

146 – 148

3

Beta strand

149 – 154

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: C541DA751FFBDBEB	FASTA	567	64,568
	10 20 30 40 50 60 MGRGLLRGLW PLHIVLWTRI ASTIPPHVQK SVNNDMIVTD NNGAVKFPQL CKFCDVRFST 70 80 90 100 110 120 CDNQKSCMSN CSITSICEKP QEVCVAVWRK NDENITLETV CHDPKLPYHD FILEDAASPK 130 140 150 160 170 180 CIMKEKKKPG ETFFMCSCSS DECNDNIIFS EEYNTSNPDL LLVIFQVTGI SLLPPLGVAI 190 200 210 220 230 240 SVIIIFYCYR VNRQQKLSST WETGKTRKLM EFSEHCAIIL EDDRSDISST CANNINHNTE 250 260 270 280 290 300 LLPIELDTLV GKGRFAEVYK AKLKQNTSEQ FETVAVKIFP YEEYASWKTE KDIFSDINLK 310 320 330 340 350 360 HENILQFLTA EERKTELGKQ YWLITAFHAK GNLQEYLTRH VISWEDLRKL GSSLARGIAH 370 380 390 400 410 420 LHSDHTPCGR PKMPIVHRDL KSSNILVKND LTCCLCDFGL SLRLDPTLSV DDLANSGQVG 430 440 450 460 470 480 TARYMAPEVL ESRMNLENVE SFKQTDVYSM ALVLWEMTSR CNAVGEVKDY EPPFGSKVRE 490 500 510 520 530 540 HPCVESMKDN VLRDRGRPEI PSFWLNHQGI QMVCETLTEC WDHDPEARLT AQCVAERFSE 550 560 LEHLDRLSGR SCSEEKIPED GSLNTTK
	Isoform 2 [UniParc]. Checksum: 8ADCBA70F95E1CBB	FASTA	592	67,457
	10 20 30 40 50 60 MGRGLLRGLW PLHIVLWTRI ASTIPPHVQK SDVEMEAQKD EIICPSCNRT AHPLRHINND 70 80 90 100 110 120 MIVTDNNGAV KFPQLCKFCD VRFSTCDNQK SCMSNCSITS ICEKPQEVCV AVWRKNDENI 130 140 150 160 170 180 TLETVCHDPK LPYHDFILED AASPKCIMKE KKKPGETFFM CSCSSDECND NIIFSEEYNT 190 200 210 220 230 240 SNPDLLLVIF QVTGISLLPP LGVAISVIII FYCYRVNRQQ KLSSTWETGK TRKLMEFSEH 250 260 270 280 290 300 CAIILEDDRS DISSTCANNI NHNTELLPIE LDTLVGKGRF AEVYKAKLKQ NTSEQFETVA 310 320 330 340 350 360 VKIFPYEEYA SWKTEKDIFS DINLKHENIL QFLTAEERKT ELGKQYWLIT AFHAKGNLQE 370 380 390 400 410 420 YLTRHVISWE DLRKLGSSLA RGIAHLHSDH TPCGRPKMPI VHRDLKSSNI LVKNDLTCCL 430 440 450 460 470 480 CDFGLSLRLD PTLSVDDLAN SGQVGTARYM APEVLESRMN LENVESFKQT DVYSMALVLW 490 500 510 520 530 540 EMTSRCNAVG EVKDYEPPFG SKVREHPCVE SMKDNVLRDR GRPEIPSFWL NHQGIQMVCE 550 560 570 580 590 TLTECWDHDP EARLTAQCVA ERFSELEHLD RLSGRSCSEE KIPEDGSLNT TK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression cloning of the TGF-beta type II receptor, a functional transmembrane serine/threonine kinase." Lin H.Y., Wang X.-F., Ng-Eaton E., Weinberg R.A., Lodish H.F. Cell 68:775-785(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-439, SUBCELLULAR LOCATION. Tissue: Liver.
[2]	Erratum Lin H.Y., Wang X.-F., Ng-Eaton E., Weinberg R.A., Lodish H.F. Cell 70:1069-1069(1992) [PubMed] [Europe PMC] [Abstract]
[3]	"A cDNA encoding the human transforming growth factor beta receptor suppresses the growth defect of a yeast mutant." Nikawa J. Gene 149:367-372(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Glial cell.
[4]	"The genomic structure of the gene encoding the human transforming growth factor beta type II receptor (TGF-beta RII)." Takenoshita S., Hagiwara K., Nagashima M., Gemma A., Bennett W.P., Harris C.C. Genomics 36:341-344(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT ALA-439.
[5]	"Genomic structure of the transforming growth factor beta type II receptor gene and its mutations in hereditary nonpolyposis colorectal cancers." Lu S.-L., Zhang W.C., Akiyama Y., Nomizu T., Yuasa Y. Cancer Res. 56:4595-4598(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT ALA-439.
[6]	"Cloning of a cDNA encoding the human transforming growth factor-beta type II receptor: heterogeneity of the mRNA." Ogasa H., Noma T., Murata H., Kawai S., Nakazawa A. Gene 181:185-190(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-439. Tissue: Liver.
[7]	NIEHS SNPs program Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-36.
[8]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Placenta.
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-37.
[11]	"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 IN PHOSPHORYLATION OF TGFBR1.
[12]	"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.
[13]	"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.
[14]	"TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation." Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., Weinberg R.A. Nat. Cell Biol. 3:708-714(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DAXX, MUTAGENESIS OF LYS-277.
[15]	"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.
[16]	"Identification of Tctex2beta, a novel dynein light chain family member that interacts with different transforming growth factor-beta receptors." Meng Q.-J., Lux A., Holloschi A., Li J., Hughes J.M.X., Foerg T., McCarthy J.E.G., Heagerty A.M., Kioschis P., Hafner M., Garland J.M. J. Biol. Chem. 281:37069-37080(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TCTEX1D4.
[17]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"SCUBE3 is an endogenous TGF-beta receptor ligand and regulates the epithelial-mesenchymal transition in lung cancer." Wu Y.Y., Peck K., Chang Y.L., Pan S.H., Cheng Y.F., Lin J.C., Yang R.B., Hong T.M., Yang P.C. Oncogene 30:3682-3693(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCUBE3.
[20]	"Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex." Hart P.J., Deep S., Taylor A.B., Shu Z., Hinck C.S., Hinck A.P. Nat. Struct. Biol. 9:203-208(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 38-159 IN COMPLEX WITH TGF-BETA3.
[21]	"The 1.1 A crystal structure of human TGF-beta type II receptor ligand binding domain." Boesen C.C., Radaev S., Motyka S.A., Patamawenu A., Sun P.D. Structure 10:913-919(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 49-159.
[22]	"Solution structure and backbone dynamics of the TGFbeta type II receptor extracellular domain." Deep S., Walker K.P. III, Shu Z., Hinck A.P. Biochemistry 42:10126-10139(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 38-159.
[23]	"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 43-149 IN COMPLEX WITH TGFBR1 AND TGFB3, DISULFIDE BONDS.
[24]	"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 38-153 IN COMPLEX WITH TGFBR1 AND TGFB1, RECEPTOR AFFINITY FOR LIGANDS, DISULFIDE BONDS.
[25]	"HNPCC associated with germline mutation in the TGF-beta type II receptor gene." Lu S.-L., Kawabata M., Imamura T., Akiyama Y., Nomizu T., Miyazono K., Yuasa Y. Nat. Genet. 19:17-18(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HNPCC6 MET-315.
[26]	"A dominant negative mutation of transforming growth factor-beta receptor type II gene in microsatellite stable oesophageal carcinoma." Tanaka S., Mori M., Mafune K., Ohno S., Sugimachi K. Br. J. Cancer 82:1557-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ESOPHAGEAL CANCER GLN-526.
[27]	"Inhibiting mutations in the transforming growth factor beta type 2 receptor in recurrent human breast cancer." Luecke C.D., Philpott A., Metcalfe J.C., Thompson A.M., Hughes-Davies L., Kemp P.R., Hesketh R. Cancer Res. 61:482-485(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BREAST TUMOR MET-387; SER-435; ALA-447 AND MET-452, CHARACTERIZATION OF VARIANTS BREAST TUMOR SER-435; ALA-447 AND MET-452.
[28]	"A catalog of 106 single-nucleotide polymorphisms (SNPs) and 11 other types of variations in genes for transforming growth factor-beta1 (TGF-beta1) and its signaling pathway." Watanabe Y., Kinoshita A., Yamada T., Ohta T., Kishino T., Matsumoto N., Ishikawa M., Niikawa N., Yoshiura K. J. Hum. Genet. 47:478-483(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ILE-191.
[29]	"Heterozygous TGFBR2 mutations in Marfan syndrome." Mizuguchi T., Collod-Beroud G., Akiyama T., Abifadel M., Harada N., Morisaki T., Allard D., Varret M., Claustres M., Morisaki H., Ihara M., Kinoshita A., Yoshiura K., Junien C., Kajii T., Jondeau G., Ohta T., Kishino T. , Furukawa Y., Nakamura Y., Niikawa N., Boileau C., Matsumoto N. Nat. Genet. 36:855-860(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LDS2B PRO-308; PHE-449 AND CYS-537, CHARACTERIZATION OF VARIANTS LDS2B PRO-308; PHE-449 AND CYS-537.
[30]	"Mutations in transforming growth factor-beta receptor type II cause familial thoracic aortic aneurysms and dissections." Pannu H., Fadulu V.T., Chang J., Lafont A., Hasham S.N., Sparks E., Giampietro P.F., Zaleski C., Estrera A.L., Safi H.J., Shete S., Willing M.C., Raman C.S., Milewicz D.M. Circulation 112:513-520(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LDS2B CYS-460 AND HIS-460.
[31]	"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 LDS1B ASN-336; PRO-355; TRP-357; HIS-528 AND CYS-528.
[32]	"Two novel and one known mutation of the TGFBR2 gene in Marfan syndrome not associated with FBN1 gene defects." Disabella E., Grasso M., Marziliano N., Ansaldi S., Lucchelli C., Porcu E., Tagliani M., Pilotto A., Diegoli M., Lanzarini L., Malattia C., Pelliccia A., Ficcadenti A., Gabrielli O., Arbustini E. Eur. J. Hum. Genet. 14:34-38(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LDS1B ASN-446.
[33]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-73 AND HIS-528.
[34]	"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] ARG-61; ILE-191; MET-315; TYR-328; ILE-373; MET-387 AND SER-490.
[35]	"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 LDS2B SER-510.
[36]	"Progressive aortic root and pulmonary artery aneurysms in a neonate with Loeys-Dietz syndrome type 1B." Muramatsu Y., Kosho T., Magota M., Yokotsuka T., Ito M., Yasuda A., Kito O., Suzuki C., Nagata Y., Kawai S., Ikoma M., Hatano T., Nakayama M., Kawamura R., Wakui K., Morisaki H., Morisaki T., Fukushima Y. Am. J. Med. Genet. A 152:417-421(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LDS1B LYS-457.
[37]	"Germline TGF-beta receptor mutations and skeletal fragility: a report on two patients with Loeys-Dietz syndrome." Kirmani S., Tebben P.J., Lteif A.N., Gordon D., Clarke B.L., Hefferan T.E., Yaszemski M.J., McGrann P.S., Lindor N.M., Ellison J.W. Am. J. Med. Genet. A 152:1016-1019(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LDS1B PRO-308 AND ARG-521.
[38]	"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 LDS1B GLN-306 DELINS HIS-GLU; ARG-377; PHE-449 AND ARG-514.
[39]	"A sporadic case of Loeys-Dietz syndrome type I with two novel mutations of the TGFBR2 gene." Ha J.S., Kim Y.H. Korean J. Pediatr. 54:272-275(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LDS1B VAL-509 AND PHE-510.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M85079 mRNA. Translation: AAA61164.1.
D28131 mRNA. Translation: BAA05673.1.
U52246 , U52240, U52241, U52242, U52244, U52245 Genomic DNA. Translation: AAB17553.1.
U69152 , U69146, U69147, U69148, U69149, U69150, U69151 Genomic DNA. Translation: AAB40916.1.
D50683 mRNA. Translation: BAA09332.1.
AY675319 Genomic DNA. Translation: AAT70724.1.
AK300383 mRNA. Translation: BAG62117.1.
CH471055 Genomic DNA. Translation: EAW64412.1.

IPI

IPI00020431.
IPI00164934.

PIR

A42100.

RefSeq

NP_001020018.1. NM_001024847.2.
NP_003233.4. NM_003242.5.

UniGene

Hs.604277.
Hs.82028.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KTZ	X-ray	2.15	B	38-159	[»]
1M9Z	X-ray	1.05	A	50-159	[»]
1PLO	NMR	-	A	38-159	[»]
2PJY	X-ray	3.00	B	43-149	[»]
3KFD	X-ray	3.00	E/F/G/H	38-153	[»]

ProteinModelPortal

P37173.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5939N.

IntAct

P37173. 12 interactions.

STRING

9606.ENSP00000351905.

PTM databases

PhosphoSite

P37173.

Polymorphism databases

DMDM

116242818.

Proteomic databases

PaxDb

P37173.

PRIDE

P37173.

Protocols and materials databases

DNASU

7048.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295754; ENSP00000295754; ENSG00000163513.
ENST00000359013; ENSP00000351905; ENSG00000163513.

GeneID

7048.

KEGG

hsa:7048.

UCSC

uc003ceo.3. human.

Organism-specific databases

CTD

7048.

GeneCards

GC03P030623.

H-InvDB

HIX0024332.

HGNC

HGNC:11773. TGFBR2.

MIM

133239. phenotype.
190182. gene.
610168. phenotype.
610380. phenotype.
614331. phenotype.

neXtProt

NX_P37173.

Orphanet

88636. Aortic dilatation - joint hypermobility - arterial tortuosity.
91387. Familial thoracic aortic aneurysm.
144. Hereditary nonpolyposis colon cancer.
60030. Loeys-Dietz syndrome type 1.
284973. Marfan syndrome type 2.

PharmGKB

PA36486.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000231495.

HOVERGEN

HBG104975.

KO

K04388.

OMA

MMVTDNN.

OrthoDB

EOG4FTW0J.

PhylomeDB

P37173.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

glypican_1pathway. Glypican 1 network.
avb3_integrin_pathway. Integrins in angiogenesis.
tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P37173.

Bgee

P37173.

CleanEx

HS_TGFBR2.

Genevestigator

P37173.

GermOnline

ENSG00000163513. Homo sapiens.

Family and domain databases

InterPro

IPR000333. Activin_II/TGFBeta-II_recpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR017194. Transform_growth_fac-b_typ-2.
IPR015013. Transforming_GF_b_rcpt_2_ecto.
[Graphical view]

PANTHER

PTHR23255:SF11. PTHR23255:SF11. 1 hit.

Pfam

PF08917. ecTbetaR2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

PIRSF

PIRSF037393. TGFRII. 1 hit.

PRINTS

PR00653. ACTIVIN2R.

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

BindingDB

P37173.

ChEMBL

CHEMBL4267.

ChiTaRS

TGFBR2. human.

EvolutionaryTrace

P37173.

GenomeRNAi

7048.

NextBio

27541.

SOURCE

Search...

Entry information

Entry name

TGFR2_HUMAN

Accession

Primary (citable) accession number: P37173
Secondary accession number(s): B4DTV5 , Q15580, Q6DKT6, Q99474

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 161 of the entry and version 2 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.