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P37173

- TGFR2_HUMAN

UniProt

P37173 - TGFR2_HUMAN

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Protein

TGF-beta receptor type-2

Gene
TGFBR2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Magnesium or manganese By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei277 – 2771ATP By similarity
Active sitei379 – 3791Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi250 – 2589ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. activation of protein kinase activity Source: BHF-UCL
  2. aging Source: Ensembl
  3. apoptotic process Source: UniProtKB
  4. blood vessel development Source: BHF-UCL
  5. brain development Source: BHF-UCL
  6. bronchus morphogenesis Source: Ensembl
  7. cartilage development Source: Ensembl
  8. common-partner SMAD protein phosphorylation Source: Ensembl
  9. digestive tract development Source: Ensembl
  10. embryo implantation Source: Ensembl
  11. embryonic cranial skeleton morphogenesis Source: BHF-UCL
  12. embryonic hemopoiesis Source: BHF-UCL
  13. gastrulation Source: Ensembl
  14. heart development Source: BHF-UCL
  15. in utero embryonic development Source: Ensembl
  16. lens development in camera-type eye Source: Ensembl
  17. lens fiber cell apoptotic process Source: Ensembl
  18. lung lobe morphogenesis Source: Ensembl
  19. mammary gland morphogenesis Source: Ensembl
  20. myeloid dendritic cell differentiation Source: BHF-UCL
  21. negative regulation of cardiac muscle cell proliferation Source: Ensembl
  22. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
  23. organ regeneration Source: Ensembl
  24. palate development Source: BHF-UCL
  25. pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  26. patterning of blood vessels Source: BHF-UCL
  27. peptidyl-serine phosphorylation Source: BHF-UCL
  28. peptidyl-threonine phosphorylation Source: BHF-UCL
  29. positive regulation of B cell tolerance induction Source: BHF-UCL
  30. positive regulation of cell proliferation Source: ProtInc
  31. positive regulation of epithelial cell migration Source: Ensembl
  32. positive regulation of mesenchymal cell proliferation Source: BHF-UCL
  33. positive regulation of NK T cell differentiation Source: BHF-UCL
  34. positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
  35. positive regulation of skeletal muscle tissue regeneration Source: Ensembl
  36. positive regulation of smooth muscle cell proliferation Source: Ensembl
  37. positive regulation of T cell tolerance induction Source: BHF-UCL
  38. positive regulation of tolerance induction to self antigen Source: BHF-UCL
  39. protein phosphorylation Source: BHF-UCL
  40. receptor-mediated endocytosis Source: Ensembl
  41. regulation of cell proliferation Source: BHF-UCL
  42. response to cholesterol Source: BHF-UCL
  43. response to drug Source: BHF-UCL
  44. response to estrogen Source: Ensembl
  45. response to glucose Source: Ensembl
  46. response to mechanical stimulus Source: Ensembl
  47. response to nutrient Source: Ensembl
  48. smoothened signaling pathway Source: Ensembl
  49. trachea formation Source: Ensembl
  50. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  51. vasculogenesis Source: BHF-UCL
  52. wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Apoptosis, Differentiation, Growth regulation

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_120850. TGF-beta receptor signaling activates SMADs.
REACT_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_169165. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_169263. TGFBR1 KD Mutants in Cancer.
REACT_169440. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_169445. TGFBR1 LBD Mutants in Cancer.
SignaLinkiP37173.

Names & Taxonomyi

Protein namesi
Recommended name:
TGF-beta receptor type-2 (EC:2.7.11.30)
Short name:
TGFR-2
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 namesi
Name:TGFBR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:11773. TGFBR2.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 166144Extracellular Reviewed predictionAdd
BLAST
Transmembranei167 – 18721Helical; Reviewed predictionAdd
BLAST
Topological domaini188 – 567380Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. caveola Source: BHF-UCL
  2. cytosol Source: Reactome
  3. external side of plasma membrane Source: BHF-UCL
  4. integral component of membrane Source: BHF-UCL
  5. plasma membrane Source: Reactome
  6. receptor complex Source: BHF-UCL
  7. transforming growth factor beta receptor homodimeric complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti315 – 3151T → M in HNPCC6. 2 Publications
Corresponds to variant rs34833812 [ dbSNP | Ensembl ].
VAR_008156
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 2 (LDS2) [MIM:610168]: An aortic aneurysm syndrome with widespread systemic involvement, characterized by arterial tortuosity and aneurysms, hypertelorism, and bifid uvula or cleft palate. Physical findings include prominent joint laxity, easy bruising, wide and atrophic scars, velvety and translucent skin with easily visible veins, spontaneous rupture of the spleen or bowel, and catastrophic complications of pregnancy, including rupture of the gravid uterus and the arteries, either during pregnancy or in the immediate postpartum period. Some patients have craniosynostosis, exotropy, micrognathia and retrognathia, structural brain abnormalities, and intellectual deficit.
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 LDS2 by having aneurysms restricted to thoracic aorta. As individuals carrying these mutations also exhibit descending aortic disease and aneurysms of other arteries (1 Publication), they have been considered as LDS2 by the OMIM resource.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti306 – 3061Q → HE in LDS2.
VAR_066723
Natural varianti308 – 3081L → P in LDS2; has a negative effect on TGF-beta signaling.
Corresponds to variant rs28934568 [ dbSNP | Ensembl ].
VAR_022351
Natural varianti336 – 3361Y → N in LDS2.
VAR_022352
Natural varianti355 – 3551A → P in LDS2.
VAR_022353
Natural varianti357 – 3571G → W in LDS2.
VAR_022354
Natural varianti377 – 3771H → R in LDS2.
VAR_066724
Natural varianti446 – 4461D → N in LDS2.
VAR_066725
Natural varianti449 – 4491S → F in LDS2; has a negative effect on TGF-beta signaling.
VAR_022358
Natural varianti457 – 4571M → K in LDS2.
VAR_066726
Natural varianti460 – 4601R → C in LDS2.
VAR_029760
Natural varianti460 – 4601R → H in LDS2.
VAR_029761
Natural varianti509 – 5091G → V in LDS2.
VAR_066727
Natural varianti510 – 5101I → F in LDS2.
VAR_066728
Natural varianti510 – 5101I → S in LDS2.
VAR_066729
Natural varianti514 – 5141C → R in LDS2.
VAR_066730
Natural varianti521 – 5211W → R in LDS2.
VAR_066731
Natural varianti528 – 5281R → C in LDS2.
VAR_022360
Natural varianti528 – 5281R → H in LDS2.
VAR_022361
Natural varianti537 – 5371R → C in LDS2; has a negative effect on TGF-beta signaling.
Corresponds to variant rs28934869 [ dbSNP | Ensembl ].
VAR_022362

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi277 – 2771K → R: Abolishes kinase activity, TGF-beta signaling and interaction with DAXX. 1 Publication

Keywords - Diseasei

Aortic aneurysm, Disease mutation, Hereditary nonpolyposis colorectal cancer

Organism-specific databases

MIMi133239. phenotype.
610168. phenotype.
614331. phenotype.
Orphaneti91387. Familial thoracic aortic aneurysm and aortic dissection.
144. Hereditary nonpolyposis colon cancer.
60030. Loeys-Dietz syndrome.
284973. Marfan syndrome type 2.
PharmGKBiPA36486.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 567545TGF-beta receptor type-2PRO_0000024426Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 842 Publications
Disulfide bondi54 ↔ 712 Publications
Disulfide bondi61 ↔ 672 Publications
Glycosylationi70 – 701N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi77 ↔ 1012 Publications
Glycosylationi94 – 941N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi121 ↔ 1362 Publications
Disulfide bondi138 ↔ 1432 Publications
Glycosylationi154 – 1541N-linked (GlcNAc...) Reviewed prediction
Modified residuei548 – 5481Phosphoserine1 Publication
Modified residuei553 – 5531Phosphoserine By similarity

Post-translational modificationi

Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP37173.
PaxDbiP37173.
PRIDEiP37173.

PTM databases

PhosphoSiteiP37173.

Expressioni

Gene expression databases

ArrayExpressiP37173.
BgeeiP37173.
CleanExiHS_TGFBR2.
GenevestigatoriP37173.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DAXXQ9UER72EBI-296151,EBI-77321
MED12Q930743EBI-296151,EBI-394357
Med12A2AGH63EBI-296151,EBI-5744969From a different organism.
SCUBE3Q8IX306EBI-296151,EBI-4479975
TGFB1P011376EBI-296151,EBI-779636
TGFB1P072002EBI-296151,EBI-907660From a different organism.
TGFB3P106008EBI-296151,EBI-1033020

Protein-protein interaction databases

BioGridi112906. 45 interactions.
DIPiDIP-5939N.
IntActiP37173. 17 interactions.
MINTiMINT-206666.
STRINGi9606.ENSP00000351905.

Structurei

Secondary structure

1
567
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 456
Beta strandi50 – 523
Beta strandi55 – 584
Beta strandi65 – 684
Beta strandi74 – 763
Beta strandi78 – 814
Beta strandi83 – 908
Beta strandi95 – 1028
Beta strandi106 – 1105
Turni114 – 1174
Beta strandi119 – 1224
Beta strandi124 – 1263
Beta strandi131 – 1388
Beta strandi140 – 1423
Helixi143 – 1453
Beta strandi146 – 1483
Beta strandi149 – 1546

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KTZX-ray2.15B38-159[»]
1M9ZX-ray1.05A49-159[»]
1PLONMR-A38-159[»]
2PJYX-ray3.00B42-149[»]
3KFDX-ray3.00E/F/G/H38-153[»]
ProteinModelPortaliP37173.
SMRiP37173. Positions 48-153, 244-539.

Miscellaneous databases

EvolutionaryTraceiP37173.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini244 – 544301Protein kinaseAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000231495.
HOVERGENiHBG104975.
KOiK04388.
OMAiWETSKPR.
OrthoDBiEOG7JHM5B.
PhylomeDBiP37173.
TreeFamiTF314724.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR000333. TGFB_receptor.
IPR017194. Transform_growth_fac-b_typ-2.
IPR015013. Transforming_GF_b_rcpt_2_ecto.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF08917. ecTbetaR2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF037393. TGFRII. 1 hit.
PRINTSiPR00653. ACTIVIN2R.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P37173-1) [UniParc]FASTAAdd to Basket

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

« Hide

MGRGLLRGLW PLHIVLWTRI ASTIPPHVQK SVNNDMIVTD NNGAVKFPQL    50
CKFCDVRFST CDNQKSCMSN CSITSICEKP QEVCVAVWRK NDENITLETV 100
CHDPKLPYHD FILEDAASPK CIMKEKKKPG ETFFMCSCSS DECNDNIIFS 150
EEYNTSNPDL LLVIFQVTGI SLLPPLGVAI SVIIIFYCYR VNRQQKLSST 200
WETGKTRKLM EFSEHCAIIL EDDRSDISST CANNINHNTE LLPIELDTLV 250
GKGRFAEVYK AKLKQNTSEQ FETVAVKIFP YEEYASWKTE KDIFSDINLK 300
HENILQFLTA EERKTELGKQ YWLITAFHAK GNLQEYLTRH VISWEDLRKL 350
GSSLARGIAH LHSDHTPCGR PKMPIVHRDL KSSNILVKND LTCCLCDFGL 400
SLRLDPTLSV DDLANSGQVG TARYMAPEVL ESRMNLENVE SFKQTDVYSM 450
ALVLWEMTSR CNAVGEVKDY EPPFGSKVRE HPCVESMKDN VLRDRGRPEI 500
PSFWLNHQGI QMVCETLTEC WDHDPEARLT AQCVAERFSE LEHLDRLSGR 550
SCSEEKIPED GSLNTTK 567
Length:567
Mass (Da):64,568
Last modified:October 17, 2006 - v2
Checksum:iC541DA751FFBDBEB
GO
Isoform 2 (identifier: P37173-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:592
Mass (Da):67,457
Checksum:i8ADCBA70F95E1CBB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361M → V.1 Publication
Corresponds to variant rs17025864 [ dbSNP | Ensembl ].
VAR_020510
Natural varianti61 – 611C → R in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041414
Natural varianti73 – 731I → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036070
Natural varianti191 – 1911V → I.2 Publications
Corresponds to variant rs56105708 [ dbSNP | Ensembl ].
VAR_017606
Natural varianti306 – 3061Q → HE in LDS2.
VAR_066723
Natural varianti308 – 3081L → P in LDS2; has a negative effect on TGF-beta signaling.
Corresponds to variant rs28934568 [ dbSNP | Ensembl ].
VAR_022351
Natural varianti315 – 3151T → M in HNPCC6. 2 Publications
Corresponds to variant rs34833812 [ dbSNP | Ensembl ].
VAR_008156
Natural varianti328 – 3281H → Y in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
VAR_041415
Natural varianti336 – 3361Y → N in LDS2.
VAR_022352
Natural varianti355 – 3551A → P in LDS2.
VAR_022353
Natural varianti357 – 3571G → W in LDS2.
VAR_022354
Natural varianti373 – 3731M → I.1 Publication
Corresponds to variant rs35719192 [ dbSNP | Ensembl ].
VAR_041416
Natural varianti377 – 3771H → R in LDS2.
VAR_066724
Natural varianti387 – 3871V → M in a breast tumor. 2 Publications
Corresponds to variant rs35766612 [ dbSNP | Ensembl ].
VAR_022355
Natural varianti435 – 4351N → S in a breast tumor; signaling of TGF-beta significantly inhibited. 1 Publication
VAR_022356
Natural varianti439 – 4391V → A.4 Publications
Corresponds to variant rs1050833 [ dbSNP | Ensembl ].
VAR_028063
Natural varianti446 – 4461D → N in LDS2.
VAR_066725
Natural varianti447 – 4471V → A in a breast tumor; signaling of TGF-beta significantly inhibited. 1 Publication
VAR_022357
Natural varianti449 – 4491S → F in LDS2; has a negative effect on TGF-beta signaling.
VAR_022358
Natural varianti452 – 4521L → M in a breast tumor; signaling of TGF-beta significantly inhibited. 1 Publication
VAR_022359
Natural varianti457 – 4571M → K in LDS2.
VAR_066726
Natural varianti460 – 4601R → C in LDS2.
VAR_029760
Natural varianti460 – 4601R → H in LDS2.
VAR_029761
Natural varianti490 – 4901N → S in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041417
Natural varianti509 – 5091G → V in LDS2.
VAR_066727
Natural varianti510 – 5101I → F in LDS2.
VAR_066728
Natural varianti510 – 5101I → S in LDS2.
VAR_066729
Natural varianti514 – 5141C → R in LDS2.
VAR_066730
Natural varianti521 – 5211W → R in LDS2.
VAR_066731
Natural varianti526 – 5261E → Q in esophageal cancer. 1 Publication
VAR_015816
Natural varianti528 – 5281R → C in LDS2.
VAR_022360
Natural varianti528 – 5281R → H in LDS2.
VAR_022361
Natural varianti537 – 5371R → C in LDS2; has a negative effect on TGF-beta signaling.
Corresponds to variant rs28934869 [ dbSNP | Ensembl ].
VAR_022362

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei31 – 322SV → SDVEMEAQKDEIICPSCNRT AHPLRHI in isoform 2. VSP_012157

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti381 – 3811K → N in BAA09332. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2648.1. [P37173-1]
CCDS33727.1. [P37173-2]
PIRiA42100.
RefSeqiNP_001020018.1. NM_001024847.2. [P37173-2]
NP_003233.4. NM_003242.5. [P37173-1]
UniGeneiHs.604277.
Hs.82028.

Genome annotation databases

EnsembliENST00000295754; ENSP00000295754; ENSG00000163513. [P37173-1]
ENST00000359013; ENSP00000351905; ENSG00000163513. [P37173-2]
GeneIDi7048.
KEGGihsa:7048.
UCSCiuc003ceo.3. human. [P37173-1]

Polymorphism databases

DMDMi116242818.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2648.1. [P37173-1 ]
CCDS33727.1. [P37173-2 ]
PIRi A42100.
RefSeqi NP_001020018.1. NM_001024847.2. [P37173-2 ]
NP_003233.4. NM_003242.5. [P37173-1 ]
UniGenei Hs.604277.
Hs.82028.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KTZ X-ray 2.15 B 38-159 [» ]
1M9Z X-ray 1.05 A 49-159 [» ]
1PLO NMR - A 38-159 [» ]
2PJY X-ray 3.00 B 42-149 [» ]
3KFD X-ray 3.00 E/F/G/H 38-153 [» ]
ProteinModelPortali P37173.
SMRi P37173. Positions 48-153, 244-539.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112906. 45 interactions.
DIPi DIP-5939N.
IntActi P37173. 17 interactions.
MINTi MINT-206666.
STRINGi 9606.ENSP00000351905.

Chemistry

BindingDBi P37173.
ChEMBLi CHEMBL4267.
GuidetoPHARMACOLOGYi 1795.

PTM databases

PhosphoSitei P37173.

Polymorphism databases

DMDMi 116242818.

Proteomic databases

MaxQBi P37173.
PaxDbi P37173.
PRIDEi P37173.

Protocols and materials databases

DNASUi 7048.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295754 ; ENSP00000295754 ; ENSG00000163513 . [P37173-1 ]
ENST00000359013 ; ENSP00000351905 ; ENSG00000163513 . [P37173-2 ]
GeneIDi 7048.
KEGGi hsa:7048.
UCSCi uc003ceo.3. human. [P37173-1 ]

Organism-specific databases

CTDi 7048.
GeneCardsi GC03P030623.
GeneReviewsi TGFBR2.
H-InvDB HIX0024332.
HGNCi HGNC:11773. TGFBR2.
MIMi 133239. phenotype.
190182. gene.
610168. phenotype.
614331. phenotype.
neXtProti NX_P37173.
Orphaneti 91387. Familial thoracic aortic aneurysm and aortic dissection.
144. Hereditary nonpolyposis colon cancer.
60030. Loeys-Dietz syndrome.
284973. Marfan syndrome type 2.
PharmGKBi PA36486.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000231495.
HOVERGENi HBG104975.
KOi K04388.
OMAi WETSKPR.
OrthoDBi EOG7JHM5B.
PhylomeDBi P37173.
TreeFami TF314724.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_120850. TGF-beta receptor signaling activates SMADs.
REACT_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_169165. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_169263. TGFBR1 KD Mutants in Cancer.
REACT_169440. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_169445. TGFBR1 LBD Mutants in Cancer.
SignaLinki P37173.

Miscellaneous databases

ChiTaRSi TGFBR2. human.
EvolutionaryTracei P37173.
GeneWikii TGF_beta_receptor_2.
GenomeRNAii 7048.
NextBioi 27541.
PROi P37173.
SOURCEi Search...

Gene expression databases

ArrayExpressi P37173.
Bgeei P37173.
CleanExi HS_TGFBR2.
Genevestigatori P37173.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR000333. TGFB_receptor.
IPR017194. Transform_growth_fac-b_typ-2.
IPR015013. Transforming_GF_b_rcpt_2_ecto.
[Graphical view ]
PANTHERi PTHR23255. PTHR23255. 1 hit.
Pfami PF08917. ecTbetaR2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF037393. TGFRII. 1 hit.
PRINTSi PR00653. ACTIVIN2R.
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "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.
  3. "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.
  4. "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.
  5. "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.
  6. NIEHS SNPs program
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-36.
  7. "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.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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.
  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 IN PHOSPHORYLATION OF TGFBR1.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. Cited for: VARIANTS LDS2 PRO-308; PHE-449 AND CYS-537, CHARACTERIZATION OF VARIANTS LDS2 PRO-308; PHE-449 AND CYS-537.
  29. "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 LDS2 CYS-460 AND HIS-460.
  30. Cited for: VARIANTS LDS2 ASN-336; PRO-355; TRP-357; HIS-528 AND CYS-528.
  31. Cited for: VARIANT LDS2 ASN-446.
  32. Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-73 AND HIS-528.
  33. "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.
  34. "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 LDS2 SER-510.
  35. Cited for: VARIANT LDS2 LYS-457.
  36. "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 LDS2 PRO-308 AND ARG-521.
  37. "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 LDS2 GLN-306 DELINS HIS-GLU; ARG-377; PHE-449 AND ARG-514.
  38. "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 LDS2 VAL-509 AND PHE-510.

Entry informationi

Entry nameiTGFR2_HUMAN
AccessioniPrimary (citable) accession number: P37173
Secondary accession number(s): B4DTV5
, Q15580, Q6DKT6, Q99474
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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