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Protein Page:
BMPR2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
BMPR2 a serine/threonine-protein kinase receptor for bone morphogenetic protein (BMP). Binds to BMP-7, BMP-2 and, less efficiently, BMP-4. Binding is weak but enhanced by the presence of type I receptors for BMPs. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Defects in BMPR2 are the cause of primary pulmonary hypertension (PPH1), a weakly penetrant dominant disorder, associated with lesions in pulmonary arterioles, elevated pulmonary arterial pressure, and right ventricular failure. Note: This description may include information from UniProtKB.
Protein type: EC 2.7.11.30; Protein kinase, TKL; Membrane protein, integral; Kinase, protein; Protein kinase, Ser/Thr (receptor); Cell cycle regulation; TKL group; STKR family; Type2 subfamily
Chromosomal Location of Human Ortholog: 2q33-q34
Cellular Component: caveola; extracellular space; integral to plasma membrane; plasma membrane
Molecular Function: activin receptor activity, type II; protein binding
Biological Process: alveolus development; anterior/posterior pattern formation; blood vessel remodeling; BMP signaling pathway; cellular response to starvation; chondrocyte development; endothelial cell proliferation; lymphangiogenesis; mesoderm formation; negative regulation of cell growth; negative regulation of systemic arterial blood pressure; negative regulation of vasoconstriction; positive regulation of BMP signaling pathway; positive regulation of bone mineralization; positive regulation of endothelial cell proliferation; positive regulation of osteoblast differentiation; positive regulation of transcription from RNA polymerase II promoter; proteoglycan biosynthetic process; regulation of cell proliferation; regulation of lung blood pressure; transcription from RNA polymerase II promoter; transmembrane receptor protein serine/threonine kinase signaling pathway; vascular endothelial growth factor receptor signaling pathway
Disease: Pulmonary Hypertension, Primary, 1; Pulmonary Venoocclusive Disease 1, Autosomal Dominant
Reference #:  Q13873 (UniProtKB)
Alt. Names/Synonyms: BMP type II receptor; BMP type-2 receptor; BMPR-2; BMPR-II; BMPR2; BMPR3; BMPRII; BMR2; Bone morphogenetic protein receptor type II; Bone morphogenetic protein receptor type-2; bone morphogenetic protein receptor, type II (serine/threonine kinase); BRK-3; FLJ41585; FLJ76945; PPH1; T-ALK; type II activin receptor-like kinase; type II receptor for bone morphogenetic protein-4
Gene Symbols: BMPR2
Molecular weight: 115,201 Da
Basal Isoelectric point: 5.82  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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BMPR2

Protein Structure Not Found.
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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T128 DLCNVNFTENFPPPD
0 1 K180 RMLTGDRKQGLHSMN
0 1 K219‑ac GRYGAVYkGSLDERP
0 2 Y247‑p FINEKNIyRVPLMEH
0 1 Y314‑p SVTRGLAyLHTELPR
0 4 S375‑p EEDNAAIsEVGtIRY
0 2 T379‑p AAIsEVGtIRYMAPE
0 1 K512 MMIWERNKsVsPTVN
0 3 S513‑p MIWERNKsVsPTVNP
0 4 S515‑p WERNKsVsPTVNPMS
0 3 T517 RNKsVsPTVNPMSTA
0 3 Y546‑p KIGPYPDysSSsyIE
0 1 S547‑p IGPYPDysSSsyIED
0 1 S548 GPYPDysSSsyIEDS
0 2 S550‑p YPDysSSsyIEDSIH
0 5 Y551‑p PDysSSsyIEDSIHH
0 1 S561 DSIHHTDSIVKNISS
0 1 S574‑p SSEHSMSstPLTIGE
0 3 T575‑p SEHSMSstPLTIGEK
0 6 S586‑p IGEKNRNsINyERQQ
0 3 Y589‑p KNRNsINyERQQAQA
0 7 S680‑p VDKNLKEssDENLME
0 7 S681‑p DKNLKEssDENLMEH
0 23 Y708‑p STSSSLLyPLIKLAV
1 5 S757‑p NLPKRPTsLPLNTKN
0 1 K782 SKHKSNLKQVETGVA
0 1 T803‑p AAEPHVVtVtMNGVA
0 1 T805‑p EPHVVtVtMNGVAGR
0 2 Y825‑p SHAATTQyANGTVLS
0 1 A843 TNIVTHRAQEMLQNQ
0 6 S862‑p DTRLNINssPDEHEP
0 14 S863‑p TRLNINssPDEHEPL
0 1 T977‑p KIKKRVKtPySLKRW
0 1 Y979‑p KKRVKtPySLKRWRP
  mouse

 
T128‑p DLCNVNFtENFPPPD
K180‑ub RMLTGDRkQGLHSMN
K219 GRYGAVYKGSLDERP
Y247 FINEKNIYRVPLMEH
Y314 SVTRGLAYLHTELPR
S375‑p EEDNAAIsEVGTIRY
T379 AAIsEVGTIRYMAPE
K512‑ub MMIWERNksVsPtVN
S513‑p MIWERNksVsPtVNP
S515‑p WERNksVsPtVNPMS
T517‑p RNksVsPtVNPMSTA
Y546 KIGPYPDYSsSSYIE
S547 IGPYPDYSsSSYIED
S548‑p GPYPDYSsSSYIEDS
S550 YPDYSsSSYIEDSIH
Y551 PDYSsSSYIEDSIHH
S561‑p DSIHHTDsIVKNISS
S574 SSEHSMSStPLTIGE
T575‑p SEHSMSStPLTIGEK
S586‑p IGEKNRNsINYERQQ
Y589 KNRNsINYERQQAQA
S680‑p VDKNLKEssDENLME
S681‑p DKNLKEssDENLMEH
Y708 STSSSLLYPLIKLAV
S757‑p NLPKRPTsLPLNTKN
K782‑ub NKHKSNLkQVETGVA
T803 AAEPHVVTVTMNGVA
T805 EPHVVTVTMNGVAGR
Y825 SHAATTQYANGAVPA
S843‑p ANIVAHRsQEMLQNQ
S862‑p DTRLNINssPDEHEP
S863‑p TRLNINssPDEHEPL
T977 KIKRRVKTPYSLKRW
Y979 KRRVKTPYSLKRWRP
  rat

 
T128 DLCNVNFTENFPPPD
K180 RMLTGDRKQGLHSVS
K219 GRYGAVYKGSLDERP
Y247 FINEKNIYRVPLMEH
Y314 SVTRGLAYLHTELPR
S375 EEDNAAISEVGTIRY
T379 AAISEVGTIRYMAPE
K512 MMIWERNKSVSPTVN
S513 MIWERNKSVSPTVNP
S515 WERNKSVSPTVNPMS
T517 RNKSVSPTVNPMSTA
Y546 KIGPYPDYSSSSyIE
S547 IGPYPDYSSSSyIED
S548 GPYPDYSSSSyIEDS
S550 YPDYSSSSyIEDSIH
Y551‑p PDYSSSSyIEDSIHH
S561 DSIHHTDSIVKNISS
S574 SSEHSMSSTPLTIGE
T575 SEHSMSSTPLTIGEK
S586 IGEKNRNSINYERQQ
Y589 KNRNSINYERQQAQA
S680‑p VDKNLKEssDENLME
S681‑p DKNLKEssDENLMEH
Y708‑p STSSSLLyPLIKLAV
S757 NLPKRPTSLPLNTKN
K782 NKHKSNLKQVETGVA
T803 AAEPHVVTVTMNGVA
T805 EPHVVTVTMNGVAGR
Y825 SHAATTQYANGVVPS
A843 ANIVAHRAQEMLQNQ
S862‑p DTRLNINssPDEHEP
S863‑p TRLNINssPDEHEPL
T977 KIKRRVKTPYSLKRW
Y979 KRRVKTPYSLKRWRP
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