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Q62312

- TGFR2_MOUSE

UniProt

Q62312 - TGFR2_MOUSE

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Protein

TGF-beta receptor type-2

Gene

Tgfbr2

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei302 – 3021ATPPROSITE-ProRule annotation
Active sitei404 – 4041Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi275 – 2839ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. activation of protein kinase activity Source: MGI
  2. aging Source: Ensembl
  3. brain development Source: BHF-UCL
  4. bronchus development Source: MGI
  5. bronchus morphogenesis Source: MGI
  6. cartilage development Source: UniProtKB
  7. common-partner SMAD protein phosphorylation Source: Ensembl
  8. digestive tract development Source: Ensembl
  9. embryo implantation Source: Ensembl
  10. embryonic cranial skeleton morphogenesis Source: BHF-UCL
  11. embryonic hemopoiesis Source: BHF-UCL
  12. gastrulation Source: MGI
  13. heart development Source: MGI
  14. in utero embryonic development Source: MGI
  15. lens development in camera-type eye Source: MGI
  16. lens fiber cell apoptotic process Source: MGI
  17. lung development Source: MGI
  18. lung lobe morphogenesis Source: MGI
  19. lung morphogenesis Source: MGI
  20. mammary gland morphogenesis Source: MGI
  21. myeloid dendritic cell differentiation Source: MGI
  22. negative regulation of cardiac muscle cell proliferation Source: Ensembl
  23. organ regeneration Source: Ensembl
  24. palate development Source: BHF-UCL
  25. pathway-restricted SMAD protein phosphorylation Source: Ensembl
  26. patterning of blood vessels Source: MGI
  27. peptidyl-serine phosphorylation Source: Ensembl
  28. peptidyl-threonine phosphorylation Source: Ensembl
  29. positive regulation of angiogenesis Source: MGI
  30. positive regulation of B cell tolerance induction Source: MGI
  31. positive regulation of epithelial cell migration Source: MGI
  32. positive regulation of mesenchymal cell proliferation Source: BHF-UCL
  33. positive regulation of NK T cell differentiation Source: MGI
  34. positive regulation of reactive oxygen species metabolic process Source: Ensembl
  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: MGI
  38. positive regulation of tolerance induction to self antigen Source: MGI
  39. protein phosphorylation Source: MGI
  40. receptor-mediated endocytosis Source: Ensembl
  41. regulation of cell proliferation Source: MGI
  42. response to cholesterol Source: BHF-UCL
  43. response to drug Source: Ensembl
  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: MGI
  49. trachea formation Source: MGI
  50. trachea morphogenesis Source: MGI
  51. transforming growth factor beta receptor signaling pathway Source: Ensembl
  52. vasculogenesis Source: BHF-UCL
  53. 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. 3474.
ReactomeiREACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_203510. TGF-beta receptor signaling activates SMADs.
REACT_209370. TGFBR2 MSI Frameshift Mutants in Cancer.
REACT_215733. Downregulation of TGF-beta receptor signaling.
REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_217958. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_224217. TGFBR1 LBD Mutants in Cancer.
REACT_224787. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_224802. TGFBR1 KD Mutants in Cancer.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:98729. Tgfbr2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 184161ExtracellularSequence AnalysisAdd
BLAST
Transmembranei185 – 21430HelicalSequence AnalysisAdd
BLAST
Topological domaini215 – 592378CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. caveola Source: MGI
  2. cytosol Source: Ensembl
  3. external side of plasma membrane Source: MGI
  4. integral component of plasma membrane Source: Ensembl
  5. membrane raft Source: MGI
  6. receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 592569TGF-beta receptor type-2PRO_0000024427Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi76 ↔ 109By similarity
Disulfide bondi79 ↔ 96By similarity
Disulfide bondi86 ↔ 92By similarity
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi102 ↔ 126By similarity
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi146 ↔ 161By similarity
Disulfide bondi163 ↔ 168By similarity
Modified residuei573 – 5731PhosphoserineBy similarity
Modified residuei578 – 5781Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ62312.
PaxDbiQ62312.
PRIDEiQ62312.

PTM databases

PhosphoSiteiQ62312.

Expressioni

Tissue specificityi

Widely expressed in adult. Expressed primarily in mesenchyme and epidermis of the midgestational fetus.

Gene expression databases

BgeeiQ62312.
CleanExiMM_TGFBR2.
ExpressionAtlasiQ62312. baseline and differential.
GenevestigatoriQ62312.

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 (By similarity). Interacts with and is activated by SCUBE3; this interaction does not affect TGFB1-binding to TGFBR2 (By similarity). Interacts with VPS39; this interaction is independent of the receptor kinase activity and of the presence of TGF-beta (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Cdh5P552844EBI-2899332,EBI-7087433
DLG5Q8TDM63EBI-2899332,EBI-715138From a different organism.
Shc1P98083-12EBI-2899332,EBI-7533258
Shc1P98083-23EBI-2899332,EBI-1019301

Protein-protein interaction databases

BioGridi204164. 2 interactions.
DIPiDIP-44605N.
IntActiQ62312. 8 interactions.
MINTiMINT-5181700.

Structurei

3D structure databases

ProteinModelPortaliQ62312.
SMRiQ62312. Positions 73-178, 269-564.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini269 – 569301Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000231495.
HOVERGENiHBG104975.
InParanoidiQ62312.
KOiK04388.
OMAiWETSKPR.
OrthoDBiEOG7JHM5B.
PhylomeDBiQ62312.
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 RII-2 (identifier: Q62312-1) [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
MGRGLLRGLW PLHIVLWTRI ASTIPPHVPK SDVEMEAQKD ASIHLSCNRT
60 70 80 90 100
IHPLKHFNSD VMASDNGGAV KLPQLCKFCD VRLSTCDNQK SCMSNCSITA
110 120 130 140 150
ICEKPHEVCV AVWRKNDKNI TLETVCHDPK LTYHGFTLED AASPKCVMKE
160 170 180 190 200
KKRAGETFFM CACNMEECND YIIFSEEYTT SSPDLLLVII QVTGVSLLPP
210 220 230 240 250
LGIAIAVIII FYCYRVHRQQ KLSPSWESSK PRKLMDFSDN CAIILEDDRS
260 270 280 290 300
DISSTCANNI NHNTELLPIE LDTLVGKGRF AEVYKAKLKQ NTSEQFETVA
310 320 330 340 350
VKIFPYEEYS SWKTEKDIFS DINLKHENIL QFLTAEERKT ELGKQYWLIT
360 370 380 390 400
AFHAKGNLQE YLTRHVISWE DLRKLGSSLA RGIAHLHSDH TPCGRPKMPI
410 420 430 440 450
VHRDLKSSNI LVKNDLTCCL CDFGLSLRLD PTLSVDDLAN SGQVGTARYM
460 470 480 490 500
APEVLESRMN LENVESFKQT DVYSMALVLW EMTSRCNAVG EVKDYEPPFG
510 520 530 540 550
SKVREHPCVE SMKDSVLRDR GRPEIPSFWL NHQGIQIVCE TLTECWDHDP
560 570 580 590
EARLTAQCVA ERFSELEHPE RLSGRSCSQE KIPEDGSLNT TK
Length:592
Mass (Da):67,122
Last modified:November 1, 1996 - v1
Checksum:i1A12D58550921F5E
GO
Isoform RII-1 (identifier: Q62312-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     32-56: Missing.
     57-57: F → V

Show »
Length:567
Mass (Da):64,219
Checksum:i4C66067ADA84F986
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81G → A in AAB30100. (PubMed:8119124)Curated
Sequence conflicti117 – 1171D → N in AAB30100. (PubMed:8119124)Curated
Sequence conflicti354 – 3541A → R in AAB30100. (PubMed:8119124)Curated
Sequence conflicti440 – 4434NSGQ → KQRE in AAB30100. (PubMed:8119124)Curated
Sequence conflicti486 – 4861C → W in AAB30100. (PubMed:8119124)Curated
Sequence conflicti506 – 5061H → P in AAB30100. (PubMed:8119124)Curated
Sequence conflicti569 – 5702PE → MD in AAB30100. (PubMed:8119124)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei32 – 5625Missing in isoform RII-1. CuratedVSP_004955Add
BLAST
Alternative sequencei57 – 571F → V in isoform RII-1. CuratedVSP_004956

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D32072 mRNA. Translation: BAA06840.1.
S69114 mRNA. Translation: AAB30100.2.
BC052629 mRNA. No translation available.
CCDSiCCDS23601.1. [Q62312-1]
CCDS23602.1. [Q62312-2]
PIRiS51371.
RefSeqiNP_033397.3. NM_009371.3. [Q62312-1]
UniGeneiMm.172346.

Genome annotation databases

EnsembliENSMUST00000035014; ENSMUSP00000035014; ENSMUSG00000032440. [Q62312-2]
ENSMUST00000061101; ENSMUSP00000062333; ENSMUSG00000032440. [Q62312-1]
GeneIDi21813.
KEGGimmu:21813.
UCSCiuc009rys.2. mouse. [Q62312-1]
uc009ryt.2. mouse. [Q62312-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D32072 mRNA. Translation: BAA06840.1 .
S69114 mRNA. Translation: AAB30100.2 .
BC052629 mRNA. No translation available.
CCDSi CCDS23601.1. [Q62312-1 ]
CCDS23602.1. [Q62312-2 ]
PIRi S51371.
RefSeqi NP_033397.3. NM_009371.3. [Q62312-1 ]
UniGenei Mm.172346.

3D structure databases

ProteinModelPortali Q62312.
SMRi Q62312. Positions 73-178, 269-564.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204164. 2 interactions.
DIPi DIP-44605N.
IntActi Q62312. 8 interactions.
MINTi MINT-5181700.

PTM databases

PhosphoSitei Q62312.

Proteomic databases

MaxQBi Q62312.
PaxDbi Q62312.
PRIDEi Q62312.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035014 ; ENSMUSP00000035014 ; ENSMUSG00000032440 . [Q62312-2 ]
ENSMUST00000061101 ; ENSMUSP00000062333 ; ENSMUSG00000032440 . [Q62312-1 ]
GeneIDi 21813.
KEGGi mmu:21813.
UCSCi uc009rys.2. mouse. [Q62312-1 ]
uc009ryt.2. mouse. [Q62312-2 ]

Organism-specific databases

CTDi 7048.
MGIi MGI:98729. Tgfbr2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118876.
HOGENOMi HOG000231495.
HOVERGENi HBG104975.
InParanoidi Q62312.
KOi K04388.
OMAi WETSKPR.
OrthoDBi EOG7JHM5B.
PhylomeDBi Q62312.
TreeFami TF314724.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_203510. TGF-beta receptor signaling activates SMADs.
REACT_209370. TGFBR2 MSI Frameshift Mutants in Cancer.
REACT_215733. Downregulation of TGF-beta receptor signaling.
REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_217958. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_224217. TGFBR1 LBD Mutants in Cancer.
REACT_224787. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_224802. TGFBR1 KD Mutants in Cancer.

Miscellaneous databases

ChiTaRSi Tgfbr2. mouse.
NextBioi 301206.
PROi Q62312.
SOURCEi Search...

Gene expression databases

Bgeei Q62312.
CleanExi MM_TGFBR2.
ExpressionAtlasi Q62312. baseline and differential.
Genevestigatori Q62312.

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. "Cloning of an isoform of mouse TGF-beta type II receptor gene."
    Suzuki A., Shioda N., Maeda T., Tada M., Ueno N.
    FEBS Lett. 355:19-22(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Tissue: Brain.
  2. "The murine type II TGF-beta receptor has a coincident embryonic expression and binding preference for TGF-beta 1."
    Lawler S., Candia A.F., Ebner R., Shum L., Lopez A.R., Moses H.L., Wright C.V., Derynck R.
    Development 120:165-175(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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 RII-2).
    Tissue: Olfactory epithelium.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTGFR2_MOUSE
AccessioniPrimary (citable) accession number: Q62312
Secondary accession number(s): Q63947
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3