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P36897

- TGFR1_HUMAN

UniProt

P36897 - TGFR1_HUMAN

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Protein

TGF-beta receptor type-1

Gene

TGFBR1

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 II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation.7 Publications

Catalytic activityi

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

Cofactori

Magnesium or manganese.By similarity

Enzyme regulationi

Kept in an inactive conformation by FKBP1A preventing receptor activation in absence of ligand. CD109 is another inhibitor of the receptor.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei232 – 2321ATPPROSITE-ProRule annotation
Active sitei333 – 3331Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi211 – 2199ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. activation of MAPKK activity Source: BHF-UCL
  2. angiogenesis Source: Ensembl
  3. anterior/posterior pattern specification Source: BHF-UCL
  4. apoptotic process Source: UniProtKB-KW
  5. artery morphogenesis Source: BHF-UCL
  6. blastocyst development Source: Ensembl
  7. cell cycle arrest Source: UniProtKB
  8. cell motility Source: BHF-UCL
  9. cellular response to transforming growth factor beta stimulus Source: BHF-UCL
  10. collagen fibril organization Source: BHF-UCL
  11. embryonic cranial skeleton morphogenesis Source: BHF-UCL
  12. endothelial cell migration Source: Ensembl
  13. epithelial to mesenchymal transition Source: UniProtKB
  14. extracellular structure organization Source: UniProtKB
  15. germ cell migration Source: BHF-UCL
  16. heart development Source: BHF-UCL
  17. in utero embryonic development Source: BHF-UCL
  18. kidney development Source: BHF-UCL
  19. lens development in camera-type eye Source: Ensembl
  20. mesenchymal cell differentiation Source: UniProtKB
  21. negative regulation of apoptotic process Source: Ensembl
  22. negative regulation of chondrocyte differentiation Source: BHF-UCL
  23. negative regulation of endothelial cell proliferation Source: Ensembl
  24. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  25. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
  26. neuron fate commitment Source: BHF-UCL
  27. palate development Source: BHF-UCL
  28. parathyroid gland development Source: BHF-UCL
  29. pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  30. peptidyl-serine phosphorylation Source: UniProtKB
  31. peptidyl-threonine phosphorylation Source: BHF-UCL
  32. pharyngeal system development Source: BHF-UCL
  33. positive regulation of apoptotic signaling pathway Source: UniProtKB
  34. positive regulation of cell growth Source: BHF-UCL
  35. positive regulation of cell proliferation Source: HGNC
  36. positive regulation of cellular component movement Source: BHF-UCL
  37. positive regulation of filopodium assembly Source: Ensembl
  38. positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  39. positive regulation of protein kinase B signaling Source: BHF-UCL
  40. positive regulation of SMAD protein import into nucleus Source: BHF-UCL
  41. positive regulation of transcription, DNA-templated Source: BHF-UCL
  42. post-embryonic development Source: Ensembl
  43. protein phosphorylation Source: BHF-UCL
  44. regulation of protein binding Source: Ensembl
  45. regulation of protein ubiquitination Source: UniProtKB
  46. regulation of transcription, DNA-templated Source: HGNC
  47. response to cholesterol Source: BHF-UCL
  48. signal transduction Source: HGNC
  49. skeletal system development Source: BHF-UCL
  50. skeletal system morphogenesis Source: BHF-UCL
  51. thymus development Source: BHF-UCL
  52. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  53. wound healing Source: UniProtKB
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.
SignaLinkiP36897.

Names & Taxonomyi

Protein namesi
Recommended name:
TGF-beta receptor type-1 (EC:2.7.11.30)
Short name:
TGFR-1
Alternative name(s):
Activin A receptor type II-like protein kinase of 53kD
Activin receptor-like kinase 5
Short name:
ALK-5
Short name:
ALK5
Serine/threonine-protein kinase receptor R4
Short name:
SKR4
TGF-beta type I receptor
Transforming growth factor-beta receptor type I
Short name:
TGF-beta receptor type I
Short name:
TbetaR-I
Gene namesi
Name:TGFBR1
Synonyms:ALK5, SKR4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:11772. TGFBR1.

Subcellular locationi

GO - Cellular componenti

  1. endosome Source: Ensembl
  2. plasma membrane Source: BHF-UCL
  3. receptor complex Source: BHF-UCL
  4. tight junction Source: UniProtKB
  5. transforming growth factor beta receptor homodimeric complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

Pathology & Biotechi

Involvement in diseasei

Loeys-Dietz syndrome 1 (LDS1) [MIM:609192]: 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.6 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry. TGFBR1 mutation Gln-487 has been reported to be associated with thoracic aortic aneurysms and dissection (TAAD) (PubMed:16791849). This phenotype, also known as thoracic aortic aneurysms type 5 (AAT5), is distinguised from LDS1 by having aneurysms restricted to thoracic aorta. It is unclear, however, if this condition is fulfilled in individuals bearing Gln-487 mutation, that is why they are considered as LDS1 by the OMIM resource.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti200 – 2001T → I in LDS1. 1 Publication
VAR_022344
Natural varianti232 – 2321K → E in LDS1. 1 Publication
VAR_029481
Natural varianti241 – 2411S → L in LDS1. 2 Publications
VAR_029482
Natural varianti266 – 2661D → Y in LDS1. 1 Publication
VAR_066720
Natural varianti318 – 3181M → R in LDS1. 1 Publication
VAR_022345
Natural varianti351 – 3511D → G in LDS1. 1 Publication
VAR_066721
Natural varianti375 – 3751T → I in LDS1. 1 Publication
VAR_066722
Natural varianti400 – 4001D → G in LDS1. 1 Publication
VAR_022346
Natural varianti487 – 4871R → P in LDS1. 2 Publications
VAR_022347
Natural varianti487 – 4871R → Q in LDS1. 3 Publications
VAR_029484
Natural varianti487 – 4871R → W in LDS1. 1 Publication
VAR_029485
Multiple self-healing squamous epithelioma (MSSE) [MIM:132800]: A disorder characterized by multiple skin tumors that undergo spontaneous regression. Tumors appear most often on sun-exposed regions, are locally invasive, and undergo spontaneous resolution over a period of months leaving pitted scars.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411C → Y in MSSE; hypomorphic mutation. 1 Publication
VAR_065826
Natural varianti45 – 451N → S in MSSE; hypomorphic mutation. 1 Publication
VAR_065827
Natural varianti52 – 521G → R in MSSE; hypomorphic mutation. 1 Publication
VAR_065828
Natural varianti83 – 831P → L in MSSE; hypomorphic mutation. 1 Publication
VAR_065829

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi185 – 1862TT → VV: Loss of phosphorylation on threonine residues. Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with A-187; A-189 and A-191. 1 Publication
Mutagenesisi187 – 1871S → 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. 1 Publication
Mutagenesisi189 – 1891S → 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. 1 Publication
Mutagenesisi191 – 1911S → 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. 1 Publication
Mutagenesisi193 – 1931L → G: Loss of interaction with FKBP1A. 1 Publication
Mutagenesisi194 – 1941P → K: Loss of interaction with FKBP1A. 1 Publication
Mutagenesisi200 – 2001T → D: Loss of response to TGF-beta. 1 Publication
Mutagenesisi200 – 2001T → V: Loss of phosphorylation. Loss of response to TGF-beta. 1 Publication
Mutagenesisi204 – 2041T → D: Constitutive activation. 1 Publication
Mutagenesisi204 – 2041T → V: Reduced phosphorylation. Reduced response to TGF-beta. 1 Publication

Keywords - Diseasei

Aortic aneurysm, Craniosynostosis, Disease mutation

Organism-specific databases

MIMi132800. phenotype.
609192. phenotype.
Orphaneti91387. Familial thoracic aortic aneurysm and aortic dissection.
60030. Loeys-Dietz syndrome.
65748. Multiple keratoacanthoma, Ferguson-Smith type.
PharmGKBiPA36485.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33331 PublicationAdd
BLAST
Chaini34 – 503470TGF-beta receptor type-1PRO_0000024423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 54
Disulfide bondi38 ↔ 41
Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi48 ↔ 71
Disulfide bondi86 ↔ 100
Disulfide bondi101 ↔ 106
Modified residuei165 – 1651Phosphoserine1 Publication
Modified residuei185 – 1851Phosphothreonine; by TGFBR21 Publication
Modified residuei186 – 1861Phosphothreonine; by TGFBR21 Publication
Modified residuei187 – 1871Phosphoserine; by TGFBR21 Publication
Modified residuei189 – 1891Phosphoserine; by TGFBR21 Publication
Modified residuei191 – 1911Phosphoserine; by TGFBR21 Publication
Cross-linki391 – 391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Phosphorylated at basal levels in the absence of ligand. Activated upon phosphorylation by TGFBR2, mainly in the GS domain. Phosphorylation in the GS domain abrogates FKBP1A-binding.3 Publications
N-Glycosylated.1 Publication
Ubiquitinated; undergoes ubiquitination catalyzed by several E3 ubiquitin ligases including SMURF1, SMURF2 and NEDD4L2. Results in the proteasomal and/or lysosomal degradation of the receptor thereby negatively regulating its activity. Deubiquitinated by USP15, leading to stabilization of the protein and enhanced TGF-beta signal.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP36897.
PaxDbiP36897.
PRIDEiP36897.

PTM databases

PhosphoSiteiP36897.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP36897.
CleanExiHS_TGFBR1.
ExpressionAtlasiP36897. baseline and differential.
GenevestigatoriP36897.

Organism-specific databases

HPAiCAB002441.
CAB031481.

Interactioni

Subunit structurei

Homodimer; in the endoplasmic reticulum but also at the cell membrane. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands assemble a functional receptor composed of two TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The respective affinity of TGBRB1 and TGFBR2 for the ligands may modulate the kinetics of assembly of the receptor and may explain the different biological activities of TGFB1, TGFB2 and TGFB3. Interacts with CD109; inhibits TGF-beta receptor activation in keratinocytes. Interacts with RBPMS. Interacts (unphosphorylated) with FKBP1A; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation. Interacts with SMAD2, SMAD3 and ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta receptor. Interacts with TRAF6 and MAP3K7; induces MAP3K7 activation by TRAF6. Interacts with PARD6A; involved in TGF-beta induced epithelial to mesenchymal transition. Interacts with SMAD7, NEDD4L, SMURF1 and SMURF2; SMAD7 recruits NEDD4L, SMURF1 and SMURF2 to the TGF-beta receptor. Interacts with USP15 and VPS39.20 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB85EBI-1027557,EBI-6858501From a different organism.
FKBP1AP629422EBI-1027557,EBI-1027571
TGFB1P011372EBI-1027557,EBI-779636
YWHAZP631044EBI-1027557,EBI-347088

Protein-protein interaction databases

BioGridi112904. 172 interactions.
DIPiDIP-5935N.
IntActiP36897. 11 interactions.
MINTiMINT-152959.
STRINGi9606.ENSP00000364133.

Structurei

Secondary structure

1
503
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 373
Turni42 – 465
Beta strandi51 – 577
Beta strandi61 – 633
Beta strandi69 – 724
Turni74 – 763
Beta strandi77 – 826
Turni84 – 863
Helixi89 – 924
Beta strandi94 – 1018
Beta strandi102 – 1054
Helixi107 – 1093
Helixi177 – 1837
Beta strandi187 – 1904
Beta strandi191 – 1933
Helixi202 – 2043
Beta strandi205 – 2139
Beta strandi215 – 22410
Beta strandi227 – 2348
Helixi236 – 2383
Helixi239 – 24911
Beta strandi251 – 2533
Beta strandi262 – 2698
Beta strandi271 – 28111
Helixi288 – 2947
Helixi299 – 31719
Beta strandi322 – 3243
Beta strandi328 – 3303
Beta strandi338 – 3414
Beta strandi347 – 3493
Helixi352 – 3543
Beta strandi356 – 3594
Turni360 – 3634
Beta strandi364 – 3663
Helixi376 – 3783
Helixi381 – 3844
Helixi393 – 41321
Beta strandi417 – 4193
Turni427 – 4315
Helixi438 – 4458
Helixi456 – 4594
Helixi462 – 47211
Helixi479 – 4813
Helixi485 – 49713

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B6CX-ray2.60B/D/F/H162-503[»]
1IASX-ray2.90A/B/C/D/E162-503[»]
1PY5X-ray2.30A175-500[»]
1RW8X-ray2.40A200-500[»]
1TBImodel-A34-114[»]
1VJYX-ray2.00A201-503[»]
2L5SNMR-A31-115[»]
2PJYX-ray3.00C33-111[»]
2WOTX-ray1.85A200-503[»]
2WOUX-ray2.30A200-503[»]
2X7OX-ray3.70A/B/C/D/E162-503[»]
3FAAX-ray3.35A/B/C/D/E162-503[»]
3GXLX-ray1.80A201-503[»]
3HMMX-ray1.70A201-503[»]
3KCFX-ray2.80A/B/C/D/E162-503[»]
3KFDX-ray3.00I/J/K/L31-115[»]
3TZMX-ray1.70A200-503[»]
ProteinModelPortaliP36897.
SMRiP36897. Positions 31-115, 175-500.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36897.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 12693ExtracellularSequence AnalysisAdd
BLAST
Topological domaini148 – 503356CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei127 – 14721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini175 – 20430GSPROSITE-ProRule annotationAdd
BLAST
Domaini205 – 495291Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi193 – 1942FKBP1A-binding

Sequence similaritiesi

Contains 1 GS domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000230587.
HOVERGENiHBG054502.
InParanoidiP36897.
KOiK04674.
OMAiLYICHNR.
PhylomeDBiP36897.
TreeFamiTF314724.

Family and domain databases

InterProiIPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR003605. TGF_beta_rcpt_GS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTiSM00467. GS. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P36897-1) [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

        10         20         30         40         50
MEAAVAAPRP RLLLLVLAAA AAAAAALLPG ATALQCFCHL CTKDNFTCVT
60 70 80 90 100
DGLCFVSVTE TTDKVIHNSM CIAEIDLIPR DRPFVCAPSS KTGSVTTTYC
110 120 130 140 150
CNQDHCNKIE LPTTVKSSPG LGPVELAAVI AGPVCFVCIS LMLMVYICHN
160 170 180 190 200
RTVIHHRVPN EEDPSLDRPF ISEGTTLKDL IYDMTTSGSG SGLPLLVQRT
210 220 230 240 250
IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER SWFREAEIYQ
260 270 280 290 300
TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE
310 320 330 340 350
GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA
360 370 380 390 400
DLGLAVRHDS ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD
410 420 430 440 450
IYAMGLVFWE IARRCSIGGI HEDYQLPYYD LVPSDPSVEE MRKVVCEQKL
460 470 480 490 500
RPNIPNRWQS CEALRVMAKI MRECWYANGA ARLTALRIKK TLSQLSQQEG

IKM
Length:503
Mass (Da):55,960
Last modified:June 1, 1994 - v1
Checksum:i179F11404725DDCB
GO
Isoform 2 (identifier: P36897-2) [UniParc]FASTAAdd to Basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     114-114: T → TGPFS

Show »
Length:507
Mass (Da):56,348
Checksum:i9EFAF4435F30E4C2
GO
Isoform 3 (identifier: P36897-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:426
Mass (Da):47,690
Checksum:i97EA2F587AFA08F6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 263Missing in allele TGFBR1*6A; could be a tumor susceptibility allele.
VAR_022342
Natural varianti26 – 261A → AA in allele TGFBR1*10A; rare polymorphism. 1 Publication
VAR_022343
Natural varianti41 – 411C → Y in MSSE; hypomorphic mutation. 1 Publication
VAR_065826
Natural varianti45 – 451N → S in MSSE; hypomorphic mutation. 1 Publication
VAR_065827
Natural varianti52 – 521G → R in MSSE; hypomorphic mutation. 1 Publication
VAR_065828
Natural varianti83 – 831P → L in MSSE; hypomorphic mutation. 1 Publication
VAR_065829
Natural varianti139 – 1391I → V.1 Publication
VAR_054160
Natural varianti153 – 1531V → I.1 Publication
Corresponds to variant rs56014374 [ dbSNP | Ensembl ].
VAR_041412
Natural varianti200 – 2001T → I in LDS1. 1 Publication
VAR_022344
Natural varianti232 – 2321K → E in LDS1. 1 Publication
VAR_029481
Natural varianti241 – 2411S → L in LDS1. 2 Publications
VAR_029482
Natural varianti266 – 2661D → Y in LDS1. 1 Publication
VAR_066720
Natural varianti267 – 2671N → H in a patient with Marfan syndrome. 1 Publication
VAR_029483
Natural varianti291 – 2911Y → C.1 Publication
Corresponds to variant rs35974499 [ dbSNP | Ensembl ].
VAR_041413
Natural varianti318 – 3181M → R in LDS1. 1 Publication
VAR_022345
Natural varianti351 – 3511D → G in LDS1. 1 Publication
VAR_066721
Natural varianti375 – 3751T → I in LDS1. 1 Publication
VAR_066722
Natural varianti400 – 4001D → G in LDS1. 1 Publication
VAR_022346
Natural varianti487 – 4871R → P in LDS1. 2 Publications
VAR_022347
Natural varianti487 – 4871R → Q in LDS1. 3 Publications
VAR_029484
Natural varianti487 – 4871R → W in LDS1. 1 Publication
VAR_029485

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei114 – 1141T → TGPFS in isoform 2. 1 PublicationVSP_041326
Alternative sequencei115 – 19177Missing in isoform 3. 1 PublicationVSP_041327Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11695 mRNA. Translation: AAA16073.1.
AF054598
, AF054590, AF054591, AF054592, AF054593, AF054594, AF054595, AF054596, AF054597 Genomic DNA. Translation: AAC08998.1.
AF035670
, AF035662, AF035663, AF035664, AF035665, AF035666, AF035667, AF035668, AF035669 Genomic DNA. Translation: AAD02042.1.
AY497473 Genomic DNA. Translation: AAR32097.1.
AL162427 Genomic DNA. No translation available.
BC071181 mRNA. Translation: AAH71181.1.
AJ619019 mRNA. Translation: CAF02096.2.
AJ619020 mRNA. Translation: CAF02097.1.
CCDSiCCDS47998.1. [P36897-3]
CCDS6738.1. [P36897-1]
PIRiA49432.
RefSeqiNP_001124388.1. NM_001130916.1. [P36897-3]
NP_004603.1. NM_004612.2. [P36897-1]
XP_005252207.1. XM_005252150.1. [P36897-2]
UniGeneiHs.494622.

Genome annotation databases

EnsembliENST00000374990; ENSP00000364129; ENSG00000106799. [P36897-3]
ENST00000374994; ENSP00000364133; ENSG00000106799. [P36897-1]
ENST00000552516; ENSP00000447297; ENSG00000106799. [P36897-2]
GeneIDi7046.
KEGGihsa:7046.
UCSCiuc004azc.3. human. [P36897-1]
uc004azd.3. human. [P36897-3]
uc004aze.3. human. [P36897-2]

Polymorphism databases

DMDMi547777.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11695 mRNA. Translation: AAA16073.1 .
AF054598
, AF054590 , AF054591 , AF054592 , AF054593 , AF054594 , AF054595 , AF054596 , AF054597 Genomic DNA. Translation: AAC08998.1 .
AF035670
, AF035662 , AF035663 , AF035664 , AF035665 , AF035666 , AF035667 , AF035668 , AF035669 Genomic DNA. Translation: AAD02042.1 .
AY497473 Genomic DNA. Translation: AAR32097.1 .
AL162427 Genomic DNA. No translation available.
BC071181 mRNA. Translation: AAH71181.1 .
AJ619019 mRNA. Translation: CAF02096.2 .
AJ619020 mRNA. Translation: CAF02097.1 .
CCDSi CCDS47998.1. [P36897-3 ]
CCDS6738.1. [P36897-1 ]
PIRi A49432.
RefSeqi NP_001124388.1. NM_001130916.1. [P36897-3 ]
NP_004603.1. NM_004612.2. [P36897-1 ]
XP_005252207.1. XM_005252150.1. [P36897-2 ]
UniGenei Hs.494622.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B6C X-ray 2.60 B/D/F/H 162-503 [» ]
1IAS X-ray 2.90 A/B/C/D/E 162-503 [» ]
1PY5 X-ray 2.30 A 175-500 [» ]
1RW8 X-ray 2.40 A 200-500 [» ]
1TBI model - A 34-114 [» ]
1VJY X-ray 2.00 A 201-503 [» ]
2L5S NMR - A 31-115 [» ]
2PJY X-ray 3.00 C 33-111 [» ]
2WOT X-ray 1.85 A 200-503 [» ]
2WOU X-ray 2.30 A 200-503 [» ]
2X7O X-ray 3.70 A/B/C/D/E 162-503 [» ]
3FAA X-ray 3.35 A/B/C/D/E 162-503 [» ]
3GXL X-ray 1.80 A 201-503 [» ]
3HMM X-ray 1.70 A 201-503 [» ]
3KCF X-ray 2.80 A/B/C/D/E 162-503 [» ]
3KFD X-ray 3.00 I/J/K/L 31-115 [» ]
3TZM X-ray 1.70 A 200-503 [» ]
ProteinModelPortali P36897.
SMRi P36897. Positions 31-115, 175-500.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112904. 172 interactions.
DIPi DIP-5935N.
IntActi P36897. 11 interactions.
MINTi MINT-152959.
STRINGi 9606.ENSP00000364133.

Chemistry

BindingDBi P36897.
ChEMBLi CHEMBL4439.
GuidetoPHARMACOLOGYi 1788.

PTM databases

PhosphoSitei P36897.

Polymorphism databases

DMDMi 547777.

Proteomic databases

MaxQBi P36897.
PaxDbi P36897.
PRIDEi P36897.

Protocols and materials databases

DNASUi 7046.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374990 ; ENSP00000364129 ; ENSG00000106799 . [P36897-3 ]
ENST00000374994 ; ENSP00000364133 ; ENSG00000106799 . [P36897-1 ]
ENST00000552516 ; ENSP00000447297 ; ENSG00000106799 . [P36897-2 ]
GeneIDi 7046.
KEGGi hsa:7046.
UCSCi uc004azc.3. human. [P36897-1 ]
uc004azd.3. human. [P36897-3 ]
uc004aze.3. human. [P36897-2 ]

Organism-specific databases

CTDi 7046.
GeneCardsi GC09P101867.
GeneReviewsi TGFBR1.
HGNCi HGNC:11772. TGFBR1.
HPAi CAB002441.
CAB031481.
MIMi 132800. phenotype.
190181. gene.
609192. phenotype.
neXtProti NX_P36897.
Orphaneti 91387. Familial thoracic aortic aneurysm and aortic dissection.
60030. Loeys-Dietz syndrome.
65748. Multiple keratoacanthoma, Ferguson-Smith type.
PharmGKBi PA36485.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118876.
HOGENOMi HOG000230587.
HOVERGENi HBG054502.
InParanoidi P36897.
KOi K04674.
OMAi LYICHNR.
PhylomeDBi P36897.
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 P36897.

Miscellaneous databases

ChiTaRSi TGFBR1. human.
EvolutionaryTracei P36897.
GeneWikii TGF_beta_receptor_1.
GenomeRNAii 7046.
NextBioi 27533.
PROi P36897.
SOURCEi Search...

Gene expression databases

Bgeei P36897.
CleanExi HS_TGFBR1.
ExpressionAtlasi P36897. baseline and differential.
Genevestigatori P36897.

Family and domain databases

InterProi IPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR003605. TGF_beta_rcpt_GS.
IPR000333. TGFB_receptor.
[Graphical view ]
PANTHERi PTHR23255. PTHR23255. 1 hit.
Pfami PF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view ]
SMARTi SM00467. GS. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51256. GS. 1 hit.
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. "Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor."
    Franzen P., ten Dijke P., Ichijo H., Yamashita H., Schulz P., Heldin C.-H., Miyazono K.
    Cell 75:681-692(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning and genomic organization of the human transforming growth factor-beta type I receptor gene."
    Vellucci V.F., Reiss M.
    Genomics 46:278-283(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The genomic structure of the gene encoding the human transforming growth factor beta type I receptor."
    Lynch M.A., Song H., DeGroff V.L., Alam K.Y., Adams E.M., Weghorst C.M.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. NIEHS SNPs program
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Placenta.
  7. "Type I transforming growth factor beta receptor maps to 9q22 and exhibits a polymorphism and a rare variant within a polyalanine tract."
    Pasche B., Luo Y., Rao P.H., Nimer S.D., Dmitrovsky E., Caron P., Luzzatto L., Offit K., Cordon-Cardo C., Renault B., Satagopan J.M., Murty V.V., Massague J.
    Cancer Res. 58:2727-2732(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-40, SIGNAL SEQUENCE CLEAVAGE SITE, GLYCOSYLATION, CHARACTERIZATION OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL, VARIANT TGFBR1*10A ALA-26 INS.
  8. "Alternative splicing of TGF-betas and their high-affinity receptors T beta RI, T beta RII and T beta RIII (betaglycan) reveal new variants in human prostatic cells."
    Konrad L., Scheiber J.A., Volck-Badouin E., Keilani M.M., Laible L., Brandt H., Schmidt A., Aumuller G., Hofmann R.
    BMC Genomics 8:318-318(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 61-155 (ISOFORM 1), ALTERNATIVE SPLICING.
    Tissue: Prostate.
  9. Konrad L.
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION (ISOFORM 1).
  10. "GS domain mutations that constitutively activate T beta R-I, the downstream signaling component in the TGF-beta receptor complex."
    Wieser R., Wrana J.L., Massague J.
    EMBO J. 14:2199-2208(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-185; THR-186; SER-187; SER-189 AND SER-191 BY TGFBR2, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF 185-THR-THR-186; SER-187; SER-189; SER-191; THR-200 AND THR-204.
  11. "MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma."
    Eppert K., Scherer S.W., Ozcelik H., Pirone R., Hoodless P., Kim H., Tsui L.-C., Bapat B., Gallinger S., Andrulis I.L., Thomsen G.H., Wrana J.L., Attisano L.
    Cell 86:543-552(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SMAD2.
  12. "MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling."
    Macias-Silva M., Abdollah S., Hoodless P.A., Pirone R., Attisano L., Wrana J.L.
    Cell 87:1215-1224(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMAD2, FUNCTION IN PHOSPHORYLATION OF SMAD2, FUNCTION IN TRANSCRIPTION REGULATION.
  13. "Mechanism of TGFbeta receptor inhibition by FKBP12."
    Chen Y.G., Liu F., Massague J.
    EMBO J. 16:3866-3876(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FKBP1A, ENZYME REGULATION, MUTAGENESIS OF LEU-193 AND PRO-194.
  14. Cited for: INTERACTION WITH SMAD3.
  15. "TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling."
    Abdollah S., Macias-Silva M., Tsukazaki T., Hayashi H., Attisano L., Wrana J.L.
    J. Biol. Chem. 272:27678-27685(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMAD2, FUNCTION IN PHOSPHORYLATION OF SMAD2, FUNCTION IN TRANSCRIPTION REGULATION.
  16. "SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor."
    Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.
    Cell 95:779-791(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZFYVE9.
  17. "Oligomeric structure of type I and type II transforming growth factor beta receptors: homodimers form in the ER and persist at the plasma membrane."
    Gilboa L., Wells R.G., Lodish H.F., Henis Y.I.
    J. Cell Biol. 140:767-777(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, SUBCELLULAR LOCATION.
  18. "Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF-beta receptor for degradation."
    Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H., Wrana J.L.
    Mol. Cell 6:1365-1375(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMAD7 AND SMURF2, PROTEASOMAL AND LYSOSOMAL DEGRADATION.
  19. "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
    Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
    J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMAD7 AND SMURF1, PROTEASOMAL DEGRADATION.
  20. "TLP, a novel modulator of TGF-beta signaling, has opposite effects on Smad2- and Smad3-dependent signaling."
    Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S., McNally J.G., Roberts A.B.
    EMBO J. 22:4465-4477(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VPS39.
  21. "NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-beta (transforming growth factor-beta) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta type I receptor."
    Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K., Miyazono K., Imamura T.
    Biochem. J. 386:461-470(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEDD4L, UBIQUITINATION.
  22. "Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity."
    Ozdamar B., Bose R., Barrios-Rodiles M., Wang H.R., Zhang Y., Wrana J.L.
    Science 307:1603-1609(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EPITHELIAL TO MESENCHYMAL TRANSITION, SUBCELLULAR LOCATION, INTERACTION WITH PARD6A, FUNCTION IN PHOSPHORYLATION OF PARD6A.
  23. "Identification of CD109 as part of the TGF-beta receptor system in human keratinocytes."
    Finnson K.W., Tam B.Y.Y., Liu K., Marcoux A., Lepage P., Roy S., Bizet A.A., Philip A.
    FASEB J. 20:1525-1527(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELLULAR GROWTH INHIBITION, INTERACTION WITH CD109.
  24. "Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS."
    Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H., Ye Q.
    Nucleic Acids Res. 34:6314-6326(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBPMS.
  25. "The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner."
    Sorrentino A., Thakur N., Grimsby S., Marcusson A., von Bulow V., Schuster N., Zhang S., Heldin C.H., Landstrom M.
    Nat. Cell Biol. 10:1199-1207(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH TRAF6 AND MAP3K7.
  26. Cited for: REVIEW ON PROCESSES REGULATED BY THE TGF-BETA CYTOKINES.
  27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "USP15 stabilizes TGF-beta receptor I and promotes oncogenesis through the activation of TGF-beta signaling in glioblastoma."
    Eichhorn P.J., Rodon L., Gonzalez-Junca A., Dirac A., Gili M., Martinez-Saez E., Aura C., Barba I., Peg V., Prat A., Cuartas I., Jimenez J., Garcia-Dorado D., Sahuquillo J., Bernards R., Baselga J., Seoane J.
    Nat. Med. 18:429-435(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP15.
  29. "Extracellular domain of type I receptor for transforming growth factor-beta: molecular modelling using protectin (CD59) as a template."
    Jokiranta T.S., Tissari J., Teleman O., Meri S.
    FEBS Lett. 376:31-36(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 34-114.
  30. "Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12."
    Huse M., Chen Y.-G., Massague J., Kuriyan J.
    Cell 96:425-436(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 162-503 IN COMPLEX WITH FKBP1A.
  31. "The TGF beta receptor activation process: an inhibitor- to substrate-binding switch."
    Huse M., Muir T.W., Xu L., Chen Y.-G., Kuriyan J., Massague J.
    Mol. Cell 8:671-682(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 162-503, PHOSPHORYLATION, INTERACTION WITH SMAD2 AND FKBP1A.
  32. "Synthesis and activity of new aryl- and heteroaryl-substituted 5,6-dihydro-4H-pyrrolo[1,2-b]pyrazole inhibitors of the transforming growth factor-beta type I receptor kinase domain."
    Sawyer J.S., Beight D.W., Britt K.S., Anderson B.D., Campbell R.M., Goodson T. Jr., Herron D.K., Li H.-Y., McMillen W.T., Mort N., Parsons S., Smith E.C.R., Wagner J.R., Yan L., Zhang F., Yingling J.M.
    Bioorg. Med. Chem. Lett. 14:3581-3584(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 175-500 IN COMPLEX WITH SYNTHETIC INHIBITOR.
  33. "Identification of 1,5-naphthyridine derivatives as a novel series of potent and selective TGF-beta type I receptor inhibitors."
    Gellibert F., Woolven J., Fouchet M.-H., Mathews N., Goodland H., Lovegrove V., Laroze A., Nguyen V.-L., Sautet S., Wang R., Janson C., Smith W., Krysa G., Boullay V., De Gouville A.-C., Huet S., Hartley D.
    J. Med. Chem. 47:4494-4506(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 201-503 IN COMPLEX WITH SYNTHETIC INHIBITOR.
  34. "Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding."
    Groppe J., Hinck C.S., Samavarchi-Tehrani P., Zubieta C., Schuermann J.P., Taylor A.B., Schwarz P.M., Wrana J.L., Hinck A.P.
    Mol. Cell 29:157-168(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 33-111 IN COMPLEX WITH TGFBR2 AND TGFB3, DISULFIDE BONDS.
  35. "Ternary complex of transforming growth factor-beta1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily."
    Radaev S., Zou Z., Huang T., Lafer E.M., Hinck A.P., Sun P.D.
    J. Biol. Chem. 285:14806-14814(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 31-115 IN COMPLEX WITH TGFBR2 AND TGFB1, RECEPTOR AFFINITY FOR LIGANDS, DISULFIDE BONDS.
  36. "TGFBR1*6A and cancer risk: a meta-analysis of seven case-control studies."
    Kaklamani V.G., Hou N., Bian Y., Reich J., Offit K., Michel L.S., Rubinstein W.S., Rademaker A., Pasche B.
    J. Clin. Oncol. 21:3236-3243(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN CANCER RISK.
  37. Cited for: ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN PROSTATE CANCER.
  38. Cited for: VARIANTS LDS1 ILE-200; ARG-318; GLY-400 AND PRO-487.
  39. "TGFBR1(*)6A is not associated with prostate cancer in men of European ancestry."
    Suarez B.K., Pal P., Jin C.H., Kaushal R., Sun G., Jin L., Pasche B., Deka R., Catalona W.J.
    Prostate Cancer Prostatic Dis. 8:50-53(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN PROSTATE CANCER.
  40. "FBN1, TGFBR1, and the Marfan-craniosynostosis/mental retardation disorders revisited."
    Ades L.C., Sullivan K., Biggin A., Haan E.A., Brett M., Holman K.J., Dixon J., Robertson S., Holmes A.D., Rogers J., Bennetts B.
    Am. J. Med. Genet. A 140:1047-1058(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LDS1 LEU-241.
  41. "Identification and in silico analyses of novel TGFBR1 and TGFBR2 mutations in Marfan syndrome-related disorders."
    Matyas G., Arnold E., Carrel T., Baumgartner D., Boileau C., Berger W., Steinmann B.
    Hum. Mutat. 27:760-769(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LDS1 LEU-241 AND GLN-487, VARIANT HIS-267.
  42. Cited for: VARIANTS LDS1 GLU-232; TRP-487; PRO-487 AND GLN-487.
  43. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-153 AND CYS-291.
  44. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-139.
  45. "Loeys-Dietz syndrome type I and type II: clinical findings and novel mutations in two Italian patients."
    Drera B., Ritelli M., Zoppi N., Wischmeijer A., Gnoli M., Fattori R., Calzavara-Pinton P.G., Barlati S., Colombi M.
    Orphanet J. Rare Dis. 4:24-24(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LDS1 GLY-351.
  46. "Clinical features and genetic analysis of Korean patients with Loeys-Dietz syndrome."
    Yang J.H., Ki C.S., Han H., Song B.G., Jang S.Y., Chung T.Y., Sung K., Lee H.J., Kim D.K.
    J. Hum. Genet. 57:52-56(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LDS1 TYR-266; ILE-375 AND GLN-487.
  47. Cited for: VARIANTS MSSE TYR-41; SER-45; ARG-52 AND LEU-83.

Entry informationi

Entry nameiTGFR1_HUMAN
AccessioniPrimary (citable) accession number: P36897
Secondary accession number(s): Q6IR47, Q706C0, Q706C1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 175 of the entry and version 1 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 9
    Human chromosome 9: 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