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O35607 (BMPR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bone morphogenetic protein receptor type-2

Short name=BMP type-2 receptor
Short name=BMPR-2
EC=2.7.11.30
Alternative name(s):
BRK-3
Bone morphogenetic protein receptor type II
Short name=BMP type II receptor
Short name=BMPR-II
Gene names
Name:Bmpr2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1038 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. 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.

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from mutant phenotype PubMed 17472960. Source: MGI

anterior/posterior pattern specification

Inferred from mutant phenotype PubMed 10772805. Source: MGI

artery development

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

blood vessel remodeling

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

brain development

Inferred from electronic annotation. Source: Ensembl

cellular response to starvation

Inferred from electronic annotation. Source: Ensembl

limb development

Inferred from genetic interaction PubMed 23610558. Source: MGI

lung alveolus development

Inferred from mutant phenotype PubMed 18552156. Source: BHF-UCL

lymphangiogenesis

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

lymphatic endothelial cell differentiation

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

mesoderm formation

Inferred from mutant phenotype PubMed 10772805. Source: MGI

negative regulation of DNA biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

negative regulation of vasoconstriction

Inferred from mutant phenotype PubMed 18552156. Source: BHF-UCL

positive regulation of BMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of axon extension involved in axon guidance

Inferred from mutant phenotype PubMed 24052814. Source: UniProt

positive regulation of bone mineralization

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of lung blood pressure

Inferred from mutant phenotype PubMed 18552156. Source: BHF-UCL

retina vasculature development in camera-type eye

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

vascular endothelial growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 18552156. Source: BHF-UCL

venous blood vessel development

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basal plasma membrane

Inferred from electronic annotation. Source: Ensembl

caveola

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 12117821. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 19424179. Source: IntAct

transforming growth factor beta-activated receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Prkg1P0C6054EBI-527224,EBI-6991999

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 10381012Bone morphogenetic protein receptor type-2
PRO_0000024416

Regions

Topological domain27 – 150124Extracellular Potential
Transmembrane151 – 17121Helical; Potential
Topological domain172 – 1038867Cytoplasmic Potential
Domain203 – 504302Protein kinase
Nucleotide binding209 – 2179ATP By similarity
Nucleotide binding280 – 2823ATP By similarity
Nucleotide binding337 – 3382ATP By similarity
Compositional bias191 – 1944Poly-Ala
Compositional bias547 – 5504Poly-Ser
Compositional bias610 – 6189Poly-Thr
Compositional bias901 – 9088Poly-Asn

Sites

Active site3331Proton acceptor By similarity
Binding site2301ATP By similarity
Binding site3511ATP By similarity

Amino acid modifications

Modified residue3791Phosphothreonine By similarity
Modified residue5861Phosphoserine By similarity
Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation1101N-linked (GlcNAc...) Potential
Glycosylation1261N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 66 By similarity
Disulfide bond94 ↔ 117 By similarity

Sequences

Sequence LengthMass (Da)Tools
O35607 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 4106945DC63250E1

FASTA1,038115,020
        10         20         30         40         50         60 
MTSSLHRPFR VPWLLWAVLL VSTTAASQNQ ERLCAFKDPY QQDLGIGESR ISHENGTILC 

        70         80         90        100        110        120 
SKGSTCYGLW EKSKGDINLV KQGCWSHIGD PQECHYEECV VTTTPPSIQN GTYRFCCCST 

       130        140        150        160        170        180 
DLCNVNFTEN FPPPDTTPLS PPHSFNRDET IIIALASVSV LAVLIVALCF GYRMLTGDRK 

       190        200        210        220        230        240 
QGLHSMNMME AAAAEPSLDL DNLKLLELIG RGRYGAVYKG SLDERPVAVK VFSFANRQNF 

       250        260        270        280        290        300 
INEKNIYRVP LMEHDNIARF IVGDERLTAD GRMEYLLVME YYPNGSLCKY LSLHTSDWVS 

       310        320        330        340        350        360 
SCRLAHSVTR GLAYLHTELP RGDHYKPAIS HRDLNSRNVL VKNDGACVIS DFGLSMRLTG 

       370        380        390        400        410        420 
NRLVRPGEED NAAISEVGTI RYMAPEVLEG AVNLRDCESA LKQVDMYALG LIYWEVFMRC 

       430        440        450        460        470        480 
TDLFPGESVP DYQMAFQTEV GNHPTFEDMQ VLVSREKQRP KFPEAWKENS LAVRSLKETI 

       490        500        510        520        530        540 
EDCWDQDAEA RLTAQCAEER MAELMMIWER NKSVSPTVNP MSTAMQNERN LSHNRRVPKI 

       550        560        570        580        590        600 
GPYPDYSSSS YIEDSIHHTD SIVKNISSEH SMSSTPLTIG EKNRNSINYE RQQAQARIPS 

       610        620        630        640        650        660 
PETSVTSLST NTTTTNTTGL TPSTGMTTIS EMPYPDETHL HATNVAQSIG PTPVCLQLTE 

       670        680        690        700        710        720 
EDLETNKLDP KEVDKNLKES SDENLMEHSL KQFSGPDPLS STSSSLLYPL IKLAVEVTGQ 

       730        740        750        760        770        780 
QDFTQAANGQ ACLIPDVPPA QIYPLPKQQN LPKRPTSLPL NTKNSTKEPR LKFGNKHKSN 

       790        800        810        820        830        840 
LKQVETGVAK MNTINAAEPH VVTVTMNGVA GRSHNVNSHA ATTQYANGAV PAGQAANIVA 

       850        860        870        880        890        900 
HRSQEMLQNQ FIGEDTRLNI NSSPDEHEPL LRREQQAGHD EGVLDRLVDR RERPLEGGRT 

       910        920        930        940        950        960 
NSNNNNSNPC SEQDILTQGV TSTAADPGPS KPRRAQRPNS LDLSATNILD GSSIQIGEST 

       970        980        990       1000       1010       1020 
QDGKSGSGEK IKRRVKTPYS LKRWRPSTWV ISTEPLDCEV NNNGSDRAVH SKSSTAVYLA 

      1030 
EGGTATTTVS KDIGMNCL 

« Hide

References

[1]"cDNA cloning and genomic organization of the mouse BMP type II receptor."
Beppu H., Minowa O., Miyazono K., Kawabata M.
Biochem. Biophys. Res. Commun. 235:499-504(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification of BMP receptor complexes with differential signaling properties and ligand binding profiles."
Whitaker G.B., Koenig B.B., Ting J., Tiesman J.P., Limberg A.L., Grant R.A., Begley K.B., Rosenbaum J.S.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF003942 mRNA. Translation: AAB63042.1.
U78048 mRNA. Translation: AAB87638.1.
CCDSCCDS35588.1.
PIRJC5527.
RefSeqNP_031587.1. NM_007561.4.
UniGeneMm.391654.
Mm.7106.

3D structure databases

ProteinModelPortalO35607.
SMRO35607. Positions 33-131, 197-555.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198373. 4 interactions.
IntActO35607. 4 interactions.
MINTMINT-1743993.

PTM databases

PhosphoSiteO35607.

Proteomic databases

PaxDbO35607.
PRIDEO35607.

Protocols and materials databases

DNASU12168.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000087435; ENSMUSP00000084701; ENSMUSG00000067336.
GeneID12168.
KEGGmmu:12168.
UCSCuc007bdz.1. mouse.

Organism-specific databases

CTD659.
MGIMGI:1095407. Bmpr2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00560000076906.
HOGENOMHOG000043088.
HOVERGENHBG050705.
InParanoidO35607.
KOK04671.
OMADHYKPAI.
OrthoDBEOG7JHM5B.
PhylomeDBO35607.
TreeFamTF314724.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.

Gene expression databases

ArrayExpressO35607.
BgeeO35607.
GenevestigatorO35607.

Family and domain databases

InterProIPR000472. Activin_rcpt.
IPR015770. BMPR2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERPTHR23255. PTHR23255. 1 hit.
PTHR23255:SF63. PTHR23255:SF63. 1 hit.
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBMPR2. mouse.
NextBio280539.
PROO35607.
SOURCESearch...

Entry information

Entry nameBMPR2_MOUSE
AccessionPrimary (citable) accession number: O35607
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot