Transforming growth factor, beta receptor I

mammalian protein found in Mus musculus

Protein protein Q14911575

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Transforming growth factor, beta receptor I

Summary

Transforming growth factor, beta receptor I is a protein^[1].

Key Facts

Transforming growth factor, beta receptor I's instance of is recorded as protein^[2].
Transforming growth factor, beta receptor I's UniProt protein ID is recorded as Hans Grodotzki^[3].
Transforming growth factor, beta receptor I's part of is recorded as Protein kinase-like domain superfamily^[4].
Transforming growth factor, beta receptor I's part of is recorded as TGFβ superfamily receptor^[5].
Transforming growth factor, beta receptor I's part of is recorded as membrane protein^[6].
Transforming growth factor, beta receptor I's part of is recorded as activin types I and II receptor domain, protein family^[7].
Transforming growth factor, beta receptor I's part of is recorded as GS domain, protein family^[8].
Transforming growth factor, beta receptor I's part of is recorded as Protein kinase domain, protein family^[9].
Transforming growth factor, beta receptor I's part of is recorded as Protein kinase, ATP binding site, protein family^[10].
Transforming growth factor, beta receptor I's part of is recorded as Serine/threonine-protein kinase, active site, protein family^[11].
Transforming growth factor, beta receptor I's has part is recorded as serine/threonine-protein kinase, active site^[12].
Transforming growth factor, beta receptor I's has part is recorded as activin types I and II receptor domain^[13].
Transforming growth factor, beta receptor I's has part is recorded as protein kinase, ATP binding site^[14].
Transforming growth factor, beta receptor I's has part is recorded as GS domain^[15].
Transforming growth factor, beta receptor I's has part is recorded as protein kinase domain^[16].
Transforming growth factor, beta receptor I's RefSeq protein ID is recorded as NP_001299797^[17].
Transforming growth factor, beta receptor I's RefSeq protein ID is recorded as NP_001299798^[18].
Transforming growth factor, beta receptor I's RefSeq protein ID is recorded as NP_033396^[19].
Transforming growth factor, beta receptor I's RefSeq protein ID is recorded as XP_030109257^[20].
Transforming growth factor, beta receptor I's RefSeq protein ID is recorded as XP_036019848^[21].
Transforming growth factor, beta receptor I's molecular function is recorded as SMAD binding^[22].
Transforming growth factor, beta receptor I's molecular function is recorded as growth factor binding^[23].
Transforming growth factor, beta receptor I's molecular function is recorded as metal ion binding^[24].
Transforming growth factor, beta receptor I's molecular function is recorded as transferase activity^[25].
Transforming growth factor, beta receptor I's molecular function is recorded as signaling receptor binding^[26].

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Quick Facts

Instance of protein

Part of Protein kinase-like domain superfamily, TGFβ superfamily receptor, membrane protein, activin types I and II receptor domain, protein family, GS domain, protein family, Protein kinase domain, protein family, Protein kinase, ATP binding site, protein family, Serine/threonine-protein kinase, active site, protein family

Properties

Biological process artery morphogenesis, positive regulation of pathway-restricted SMAD protein phosphorylation, cell motility, germ cell migration, development of the heart, activin receptor signaling pathway, regulation of gene expression, skeletal system morphogenesis, post-embryonic development, negative regulation of chondrocyte differentiation, phosphorylation, signal transduction, regulation of epithelial to mesenchymal transition, parathyroid gland development, transmembrane receptor protein serine/threonine kinase signaling pathway, thymus development, collagen fibril organization, peptidyl-threonine phosphorylation, regulation of transcription, DNA-templated, protein phosphorylation, cellular response to transforming growth factor beta stimulus, skeletal system development, apoptotic process, positive regulation of cell growth, roof of mouth development, negative regulation of apoptotic process, endothelial cell activation, pathway-restricted SMAD protein phosphorylation, positive regulation of apoptotic signaling pathway, anterior/posterior pattern specification, in utero embryonic development, epithelial to mesenchymal transition, intracellular signal transduction, positive regulation of cell population proliferation, kidney development, endothelial cell migration, negative regulation of extrinsic apoptotic signaling pathway, mesenchymal cell differentiation, positive regulation of filopodium assembly, male gonad development, regulation of growth, regulation of protein ubiquitination, lens development in camera-type eye, embryonic cranial skeleton morphogenesis, pharyngeal system development, positive regulation of endothelial cell proliferation, blastocyst development, positive regulation of transcription, DNA-templated, peptidyl-serine phosphorylation, angiogenesis, regulation of protein binding, negative regulation of endothelial cell proliferation, positive regulation of SMAD protein signal transduction, cardiac epithelial to mesenchymal transition, cell differentiation, response to cholesterol, positive regulation of cell migration, positive regulation of protein kinase B signaling, neuron fate commitment, proepicardium development, regulation of cardiac muscle cell proliferation, ventricular septum morphogenesis, positive regulation of stress fiber assembly, transforming growth factor beta receptor signaling pathway, coronary artery morphogenesis, ventricular compact myocardium morphogenesis, positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation, epicardium morphogenesis, positive regulation of tight junction disassembly, angiogenesis involved in coronary vascular morphogenesis, ventricular trabecula myocardium morphogenesis, positive regulation of epithelial to mesenchymal transition, positive regulation of apoptotic process, positive regulation of gene expression, response to estrogen, negative regulation of endothelial cell differentiation, protein autophosphorylation, negative regulation of pri-miRNA transcription by RNA polymerase II, positive regulation of pri-miRNA transcription by RNA polymerase II, transforming growth factor beta receptor signaling pathway, pattern specification process, activin receptor signaling pathway

Cell component endosome, receptor complex, cell surface, plasma membrane, caveola, integral component of membrane, bicellular tight junction, membrane, membrane raft, cell junction, intracellular anatomical structure, intracellular membrane-bounded organelle, basolateral plasma membrane, apical plasma membrane, protein-containing complex, integral component of plasma membrane, receptor complex, activin receptor complex, nucleus, endosome, nucleus, endosome

Encoded by Tgfbr1

Found in taxon house mouse

Has part(s) serine/threonine-protein kinase, active site, activin types I and II receptor domain, protein kinase, ATP binding site, GS domain, protein kinase domain

Imported from wholeness_audit_2026-05-02

Molecular function SMAD binding, growth factor binding, metal ion binding, transferase activity, signaling receptor binding, type II transforming growth factor beta receptor binding, protein kinase activity, nucleotide binding, protein serine/threonine kinase activity, I-SMAD binding, transforming growth factor beta receptor activity, type I, transforming growth factor beta binding, transmembrane receptor protein serine/threonine kinase activity, ATP binding, transforming growth factor beta-activated receptor activity, protein binding, kinase activity, ubiquitin protein ligase binding, protein-containing complex binding, protein heterodimerization activity, transforming growth factor beta-activated receptor activity, transforming growth factor beta receptor activity, type I, growth factor binding, SMAD binding, activin binding, transforming growth factor beta binding

External References (3)

Ensembl protein id ENSMUSP00000007757, ENSMUSP00000048501, ENSMUSP00000103353, ENSMUSP00000123761

Refseq protein id NP_001299797, NP_001299798, NP_033396, XP_030109257, XP_036019848

Uniprot protein id Hans Grodotzki

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

[2] ↑ Transforming growth factor, beta receptor I — instance of (P31): protein. Q905695. Retrieved 2022-05-25. wikidata.org.
[3] ↑ Transforming growth factor, beta receptor I — UniProt protein ID (P352): Hans Grodotzki. Q905695. Retrieved 2022-05-25. wikidata.org.
[4] ↑ Transforming growth factor, beta receptor I — part of (P361): Protein kinase-like domain superfamily. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[5] ↑ Transforming growth factor, beta receptor I — part of (P361): TGFβ superfamily receptor. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[6] ↑ Transforming growth factor, beta receptor I — part of (P361): membrane protein. wikidata.org.
[7] ↑ Transforming growth factor, beta receptor I — part of (P361): activin types I and II receptor domain, protein family. wikidata.org.
[8] ↑ Transforming growth factor, beta receptor I — part of (P361): GS domain, protein family. wikidata.org.
[9] ↑ Transforming growth factor, beta receptor I — part of (P361): Protein kinase domain, protein family. wikidata.org.
[10] ↑ Transforming growth factor, beta receptor I — part of (P361): Protein kinase, ATP binding site, protein family. wikidata.org.
[11] ↑ Transforming growth factor, beta receptor I — part of (P361): Serine/threonine-protein kinase, active site, protein family. wikidata.org.
[12] ↑ Transforming growth factor, beta receptor I — has part(s) (P527): serine/threonine-protein kinase, active site. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[13] ↑ Transforming growth factor, beta receptor I — has part(s) (P527): activin types I and II receptor domain. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[14] ↑ Transforming growth factor, beta receptor I — has part(s) (P527): protein kinase, ATP binding site. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[15] ↑ Transforming growth factor, beta receptor I — has part(s) (P527): GS domain. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[16] ↑ Transforming growth factor, beta receptor I — has part(s) (P527): protein kinase domain. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[17] ↑ Transforming growth factor, beta receptor I — RefSeq protein ID (P637): NP_001299797. Q20641742. Retrieved 2022-03-20. wikidata.org.
[18] ↑ Transforming growth factor, beta receptor I — RefSeq protein ID (P637): NP_001299798. Q20641742. Retrieved 2022-03-20. wikidata.org.
[19] ↑ Transforming growth factor, beta receptor I — RefSeq protein ID (P637): NP_033396. Q20641742. Retrieved 2022-03-20. wikidata.org.
[20] ↑ Transforming growth factor, beta receptor I — RefSeq protein ID (P637): XP_030109257. Q20641742. Retrieved 2022-03-20. wikidata.org.
[21] ↑ Transforming growth factor, beta receptor I — RefSeq protein ID (P637): XP_036019848. Q20641742. Retrieved 2022-03-20. wikidata.org.
[22] ↑ Transforming growth factor, beta receptor I — molecular function (P680): SMAD binding. GOA. Retrieved 2018-04-24. ebi.ac.uk. Provenance: wikidata.org.
[23] ↑ Transforming growth factor, beta receptor I — molecular function (P680): growth factor binding. GOA. Retrieved 2018-04-24. ebi.ac.uk. Provenance: wikidata.org.
[24] ↑ Transforming growth factor, beta receptor I — molecular function (P680): metal ion binding. GOA. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[25] ↑ Transforming growth factor, beta receptor I — molecular function (P680): transferase activity. GOA. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[26] ↑ Transforming growth factor, beta receptor I — molecular function (P680): signaling receptor binding. Galectin-9-CD44 interaction enhances stability and function of adaptive regulatory T cells. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

[1] ↑ Transforming growth factor, beta receptor I is an instance of protein (Q8054) [P31, primary]. Wikidata. wikidata.org.

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APA

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MLA

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BibTeX

@misc{4ortxyz_transforming-growth-factor-beta-receptor-i_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Transforming growth factor, beta receptor I}}, year = {2026}, url = {https://4ort.xyz/entity/transforming-growth-factor-beta-receptor-i}, note = {Accessed: 2026-05-03}}

LLM prompt

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