Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (ESK2) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)

 TGFR1_MOUSE             Reviewed;         503 AA.
Q64729; A2AJN0;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 180.
RecName: Full=TGF-beta receptor type-1;
Short=TGFR-1;
EC=2.7.11.30;
AltName: Full=ESK2;
AltName: Full=Transforming growth factor-beta receptor type I;
Short=TGF-beta receptor type I;
Short=TbetaR-I;
Flags: Precursor;
Name=Tgfbr1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain, and Testis;
PubMed=8117261; DOI=10.1006/bbrc.1994.1150;
Tomoda T., Kudoh T., Noma T., Nakazawa A., Muramatsu M.-A., Arai K.;
"Molecular cloning of a mouse counterpart for human TGF-beta type I
receptor.";
Biochem. Biophys. Res. Commun. 198:1054-1062(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=8117262; DOI=10.1006/bbrc.1994.1151;
Suzuki A., Shioda N., Maeda T., Tada M., Ueno N.;
"A mouse TGF-beta type I receptor that requires type II receptor for
ligand binding.";
Biochem. Biophys. Res. Commun. 198:1063-1069(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Transmembrane serine/threonine kinase forming with the
TGF-beta type II serine/threonine kinase receptor, TGFBR2, the
non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2
and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the
cell surface to the cytoplasm and is thus regulating a plethora of
physiological and pathological processes including cell cycle
arrest in epithelial and hematopoietic cells, control of
mesenchymal cell proliferation and differentiation, wound healing,
extracellular matrix production, immunosuppression and
carcinogenesis. The formation of the receptor complex composed of
2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the
cytokine dimer results in the phosphorylation and the activation
of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1
phosphorylates SMAD2 which dissociates from the receptor and
interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently
translocated to the nucleus where it modulates the transcription
of the TGF-beta-regulated genes. This constitutes the canonical
SMAD-dependent TGF-beta signaling cascade. Also involved in non-
canonical, SMAD-independent TGF-beta signaling pathways. For
instance, TGFBR1 induces TRAF6 autoubiquitination which in turn
results in MAP3K7 ubiquitination and activation to trigger
apoptosis. Also regulates epithelial to mesenchymal transition
through a SMAD-independent signaling pathway through PARD6A
phosphorylation and activation (By similarity).
{ECO:0000250|UniProtKB:P36897}.
-!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
protein] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Kept in an inactive conformation by FKBP1A
preventing receptor activation in absence of ligand. CD109 is
another inhibitor of the receptor (By similarity).
{ECO:0000250|UniProtKB:P36897}.
-!- SUBUNIT: 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 (By similarity). Interacts
with USP15 and VPS39. Interacts with SDCBP (via C-terminus).
Interacts with CAV1 and this interaction is impaired in the
presence of SDCBP (By similarity). {ECO:0000250|UniProtKB:P36897}.
-!- INTERACTION:
P63010:AP2B1 (xeno); NbExp=3; IntAct=EBI-2899393, EBI-432924;
Q9DBG3:Ap2b1; NbExp=2; IntAct=EBI-2899393, EBI-775229;
P49817:Cav1; NbExp=4; IntAct=EBI-2899393, EBI-1161338;
P15379:Cd44; NbExp=4; IntAct=EBI-2899393, EBI-7565891;
P55284:Cdh5; NbExp=2; IntAct=EBI-2899393, EBI-7087433;
Q8TDM6:DLG5 (xeno); NbExp=3; IntAct=EBI-2899393, EBI-715138;
P05533:Ly6a; NbExp=2; IntAct=EBI-2899393, EBI-11600492;
P98083-2:Shc1; NbExp=7; IntAct=EBI-2899393, EBI-1019301;
P84022:SMAD3 (xeno); NbExp=6; IntAct=EBI-2899393, EBI-347161;
Q62312:Tgfbr2; NbExp=3; IntAct=EBI-2899393, EBI-2899332;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P36897}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P36897}. Cell junction, tight
junction {ECO:0000250|UniProtKB:P36897}. Membrane raft
{ECO:0000250|UniProtKB:P36897}. Cell surface
{ECO:0000250|UniProtKB:P36897}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q64729-1; Sequence=Displayed;
Name=2;
IsoId=Q64729-2; Sequence=VSP_021593;
Note=May be due to a competing donor splice site.;
-!- PTM: 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 (By
similarity). {ECO:0000250|UniProtKB:P36897}.
-!- PTM: N-Glycosylated. {ECO:0000250|UniProtKB:P36897}.
-!- PTM: 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. Its ubiquitination and proteasome-mediated
degradation is negatively regulated by SDCBP (By similarity).
{ECO:0000250|UniProtKB:P36897}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; D28526; BAA05878.1; -; mRNA.
EMBL; D25540; BAA05023.1; -; mRNA.
EMBL; AL772232; CAM13897.1; -; Genomic_DNA.
EMBL; AL772150; CAM13897.1; JOINED; Genomic_DNA.
EMBL; AL772150; CAM24923.1; -; Genomic_DNA.
EMBL; AL772232; CAM24923.1; JOINED; Genomic_DNA.
EMBL; BC063260; AAH63260.1; -; mRNA.
CCDS; CCDS18160.1; -. [Q64729-1]
CCDS; CCDS84728.1; -. [Q64729-2]
PIR; JC2061; JC2061.
PIR; JC2062; JC2062.
RefSeq; NP_001299797.1; NM_001312868.1. [Q64729-2]
RefSeq; NP_001299798.1; NM_001312869.1.
RefSeq; NP_033396.1; NM_009370.3. [Q64729-1]
UniGene; Mm.197552; -.
ProteinModelPortal; Q64729; -.
SMR; Q64729; -.
BioGrid; 204163; 25.
ComplexPortal; CPX-823; TGF-beta-1-TGFR complex.
ComplexPortal; CPX-826; TGF-beta-3-TGFR complex.
ComplexPortal; CPX-836; TGF-beta-2-TGFR complex.
CORUM; Q64729; -.
DIP; DIP-42262N; -.
IntAct; Q64729; 33.
MINT; Q64729; -.
STRING; 10090.ENSMUSP00000007757; -.
BindingDB; Q64729; -.
ChEMBL; CHEMBL2021750; -.
iPTMnet; Q64729; -.
PhosphoSitePlus; Q64729; -.
PaxDb; Q64729; -.
PRIDE; Q64729; -.
Ensembl; ENSMUST00000007757; ENSMUSP00000007757; ENSMUSG00000007613. [Q64729-1]
Ensembl; ENSMUST00000044234; ENSMUSP00000048501; ENSMUSG00000007613. [Q64729-2]
GeneID; 21812; -.
KEGG; mmu:21812; -.
UCSC; uc008sun.1; mouse. [Q64729-1]
UCSC; uc008suo.1; mouse. [Q64729-2]
CTD; 7046; -.
MGI; MGI:98728; Tgfbr1.
eggNOG; KOG2052; Eukaryota.
eggNOG; ENOG410XQT0; LUCA.
GeneTree; ENSGT00760000118876; -.
HOGENOM; HOG000230587; -.
HOVERGEN; HBG054502; -.
InParanoid; Q64729; -.
KO; K04674; -.
OMA; GATALQC; -.
OrthoDB; EOG091G0BIU; -.
PhylomeDB; Q64729; -.
TreeFam; TF314724; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-MMU-5689880; Ub-specific processing proteases.
ChiTaRS; Tgfbr1; mouse.
PRO; PR:Q64729; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000007613; -.
CleanEx; MM_TGFBR1; -.
ExpressionAtlas; Q64729; baseline and differential.
Genevisible; Q64729; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
GO; GO:0005901; C:caveola; ISO:MGI.
GO; GO:0005623; C:cell; ISS:AgBase.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016020; C:membrane; ISS:AgBase.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0070411; F:I-SMAD binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0046332; F:SMAD binding; IDA:BHF-UCL.
GO; GO:0050431; F:transforming growth factor beta binding; IPI:MGI.
GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; ISS:AgBase.
GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IDA:UniProtKB.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0000186; P:activation of MAPKK activity; ISO:MGI.
GO; GO:0032924; P:activin receptor signaling pathway; ISS:AgBase.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; IMP:BHF-UCL.
GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
GO; GO:0001824; P:blastocyst development; IDA:MGI.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0048870; P:cell motility; ISO:MGI.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL.
GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
GO; GO:0060982; P:coronary artery morphogenesis; IMP:BHF-UCL.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
GO; GO:0042118; P:endothelial cell activation; ISS:AgBase.
GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
GO; GO:1905223; P:epicardium morphogenesis; IMP:BHF-UCL.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0008354; P:germ cell migration; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; ISS:AgBase.
GO; GO:0001822; P:kidney development; IGI:MGI.
GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
GO; GO:0008584; P:male gonad development; IMP:MGI.
GO; GO:0048762; P:mesenchymal cell differentiation; ISS:AgBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:BHF-UCL.
GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:MGI.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IGI:MGI.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription by RNA polymerase II; ISO:MGI.
GO; GO:0048663; P:neuron fate commitment; IMP:MGI.
GO; GO:0060017; P:parathyroid gland development; IMP:MGI.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0060037; P:pharyngeal system development; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:BHF-UCL.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:MGI.
GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0051272; P:positive regulation of cellular component movement; ISO:MGI.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:AgBase.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IGI:BHF-UCL.
GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
GO; GO:1905075; P:positive regulation of occluding junction disassembly; IGI:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:MGI.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IGI:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:AgBase.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0060043; P:regulation of cardiac muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0043393; P:regulation of protein binding; IMP:MGI.
GO; GO:0031396; P:regulation of protein ubiquitination; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0070723; P:response to cholesterol; IDA:BHF-UCL.
GO; GO:0043627; P:response to estrogen; ISO:MGI.
GO; GO:0060021; P:roof of mouth development; IMP:MGI.
GO; GO:0007165; P:signal transduction; ISO:MGI.
GO; GO:0001501; P:skeletal system development; IGI:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IGI:MGI.
GO; GO:0048538; P:thymus development; IMP:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
GO; GO:0003223; P:ventricular compact myocardium morphogenesis; IMP:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
InterPro; IPR000472; Activin_recp.
InterPro; IPR003605; GS_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF01064; Activin_recp; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF08515; TGF_beta_GS; 1.
SMART; SM00467; GS; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51256; GS; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; ATP-binding; Cell junction;
Cell membrane; Complete proteome; Differentiation; Disulfide bond;
Glycoprotein; Growth regulation; Isopeptide bond; Kinase; Magnesium;
Manganese; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Receptor; Reference proteome;
Serine/threonine-protein kinase; Signal; Tight junction; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 29 {ECO:0000250}.
CHAIN 30 503 TGF-beta receptor type-1.
/FTId=PRO_0000024424.
TOPO_DOM 30 126 Extracellular. {ECO:0000255}.
TRANSMEM 127 147 Helical. {ECO:0000255}.
TOPO_DOM 148 503 Cytoplasmic. {ECO:0000255}.
DOMAIN 175 204 GS. {ECO:0000255|PROSITE-
ProRule:PRU00585}.
DOMAIN 205 495 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 211 219 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 193 194 FKBP1A-binding.
ACT_SITE 333 333 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 232 232 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000250|UniProtKB:P36897}.
MOD_RES 185 185 Phosphothreonine; by TGFBR2.
{ECO:0000250|UniProtKB:P36897}.
MOD_RES 186 186 Phosphothreonine; by TGFBR2.
{ECO:0000250|UniProtKB:P36897}.
MOD_RES 187 187 Phosphoserine; by TGFBR2.
{ECO:0000250|UniProtKB:P36897}.
MOD_RES 189 189 Phosphoserine; by TGFBR2.
{ECO:0000250|UniProtKB:P36897}.
MOD_RES 191 191 Phosphoserine; by TGFBR2.
{ECO:0000250|UniProtKB:P36897}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 32 50 {ECO:0000250|UniProtKB:P36897}.
DISULFID 34 37 {ECO:0000250|UniProtKB:P36897}.
DISULFID 44 67 {ECO:0000250|UniProtKB:P36897}.
DISULFID 82 96 {ECO:0000250|UniProtKB:P36897}.
DISULFID 97 102 {ECO:0000250|UniProtKB:P36897}.
CROSSLNK 391 391 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 111 114 Missing (in isoform 2).
{ECO:0000303|PubMed:8117262}.
/FTId=VSP_021593.
SEQUENCE 503 AA; 56179 MW; BB8BB6D2261793AF CRC64;
MEAAAAAPRR PQLLIVLVAA ATLLPGAKAL QCFCHLCTKD NFTCETDGLC FVSVTETTDK
VIHNSMCIAE IDLIPRDRPF VCAPSSKTGA VTTTYCCNQD HCNKIELPTT GPFSEKQSAG
LGPVELAAVI AGPVCFVCIA LMLMVYICHN RTVIHHRVPN EEDPSLDRPF ISEGTTLKDL
IYDMTTSGSG SGLPLLVQRT IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER
SWFREAEIYQ TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE
GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA DLGLAVRHDS
ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD IYAMGLVFWE IARRCSIGGI
HEDYQLPYYD LVPSDPSVEE MRKVVCEQKL RPNIPNRWQS CEALRVMAKI MRECWYANGA
ARLTALRIKK TLSQLSQQEG IKM


Related products :

Catalog number Product name Quantity
EIAAB42159 ESK2,Mouse,Mus musculus,TbetaR-I,TGF-beta receptor type I,TGF-beta receptor type-1,Tgfbr1,TGFR-1,Transforming growth factor-beta receptor type I
EIAAB42158 Rat,Rattus norvegicus,Serine_threonine-protein kinase receptor R4,SKR4,TbetaR-I,TGF-beta receptor type I,TGF-beta receptor type-1,TGF-beta type I receptor,Tgfbr1,TGFR-1,Transforming growth factor-beta
EIAAB42165 Homo sapiens,Human,TbetaR-II,TGF-beta receptor type II,TGF-beta receptor type-2,TGF-beta type II receptor,TGFBR2,TGFR-2,Transforming growth factor-beta receptor type II
EIAAB42157 Bos taurus,Bovine,TbetaR-I,TGF-beta receptor type I,TGF-beta receptor type-1,TGF-beta type I receptor,TGFBR1,TGFR-1,Transforming growth factor-beta receptor type I
EIAAB42163 Rat,Rattus norvegicus,TbetaR-II,TGF-beta receptor type II,TGF-beta receptor type-2,TGF-beta type II receptor,Tgfbr2,TGFR-2,Transforming growth factor-beta receptor type II
EIAAB42164 Mouse,Mus musculus,TbetaR-II,TGF-beta receptor type II,TGF-beta receptor type-2,TGF-beta type II receptor,Tgfbr2,TGFR-2,Transforming growth factor-beta receptor type II
EIAAB42156 Pig,Sus scrofa,TbetaR-I,TGF-beta receptor type I,TGF-beta receptor type-1,TGF-beta type I receptor,TGFBR1,TGFR-1,Transforming growth factor-beta receptor type I
EIAAB42162 Pig,Sus scrofa,TbetaR-II,TGF-beta receptor type II,TGF-beta receptor type-2,TGF-beta type II receptor,TGFBR2,TGFR-2,Transforming growth factor-beta receptor type II
101-M96 TGFR-1 (ALK-5) Anti-Human Host: Mouse transforming growth factor, beta receptor 1; AAT5; ALK5; MSSE; SKR4; ALK-5; LDS1A; LDS2A; TGFR-1; ACVRLK4;TGF-beta receptor type-1 tbetaR-I; TGF-beta receptor typ 100
EIAAB42161 Chicken,Gallus gallus,TbetaR-II,TGF-beta receptor type II,TGF-beta receptor type-2,TGF-beta type II receptor,TGFBR2,TGFR-2,Transforming growth factor-beta receptor type II
18-272-195253 TGFBR2 - Goat polyclonal to TGFBR2; EC 2.7.11.30; TGF-beta receptor type II; TGFR-2; TGF-beta type II receptor; Transforming growth factor-beta receptor type II; TbetaR-II Polyclonal 0.05 mg
EIAAB42139 Betaglycan,Homo sapiens,Human,TGF-beta receptor type 3,TGF-beta receptor type III,TGFBR3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
EIAAB42137 Betaglycan,Mouse,Mus musculus,TGF-beta receptor type 3,TGF-beta receptor type III,Tgfbr3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
EIAAB42140 Betaglycan,Rat,Rattus norvegicus,TGF-beta receptor type 3,TGF-beta receptor type III,Tgfbr3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
EIAAB42138 Betaglycan,Pig,Sus scrofa,TGF-beta receptor type 3,TGF-beta receptor type III,TGFBR3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
101-M96 TGFR-1 (ALK-5), Host: Mouse, Species: Anti-Human, Synonyms: transforming growth factor, beta receptor 1; AAT5; ALK5; SKR4; LDS1A; LDS2A; TGFR-1; TGF-beta receptor type-1 100 ug
H7659 Transforming growth factor beta receptor type 3 (TGFBR3), Rat, ELISA Kit 96T
CSB-EL023453RA Rat Transforming growth factor beta receptor type 3(TGFBR3) ELISA kit 96T
H7658 Transforming growth factor beta receptor type 3 (TGFBR3), Pig, ELISA Kit 96T
CSB-EL023453PI Pig Transforming growth factor beta receptor type 3(TGFBR3) ELISA kit SpeciesPig 96T
CSB-EL023453HU Human Transforming growth factor beta receptor type 3(TGFBR3) ELISA kit 96T
CSB-EL023453RA Rat Transforming growth factor beta receptor type 3(TGFBR3) ELISA kit SpeciesRat 96T
H7657 Transforming growth factor beta receptor type 3 (TGFBR3), Mouse, ELISA Kit 96T
CSB-EL023453MO Mouse Transforming growth factor beta receptor type 3(TGFBR3) ELISA kit 96T
H7656 Transforming growth factor beta receptor type 3 (TGFBR3), Human, ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur