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Protein

Bone morphogenetic protein receptor type-2

Gene

BMPR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei230 – 2301ATP
Active sitei333 – 3331Proton acceptorPROSITE-ProRule annotation
Binding sitei351 – 3511ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi209 – 2179ATP
Nucleotide bindingi280 – 2823ATP
Nucleotide bindingi337 – 3382ATP

GO - Molecular functioni

  1. activin receptor activity, type II Source: Reactome
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. receptor signaling protein serine/threonine kinase activity Source: InterPro
  5. transforming growth factor beta-activated receptor activity Source: InterPro

GO - Biological processi

  1. activin receptor signaling pathway Source: GOC
  2. anterior/posterior pattern specification Source: BHF-UCL
  3. artery development Source: BHF-UCL
  4. blood vessel remodeling Source: BHF-UCL
  5. BMP signaling pathway Source: BHF-UCL
  6. brain development Source: Ensembl
  7. cellular response to starvation Source: BHF-UCL
  8. chondrocyte development Source: AgBase
  9. endochondral bone morphogenesis Source: AgBase
  10. limb development Source: Ensembl
  11. lung alveolus development Source: BHF-UCL
  12. lymphangiogenesis Source: BHF-UCL
  13. lymphatic endothelial cell differentiation Source: BHF-UCL
  14. mesoderm formation Source: BHF-UCL
  15. negative regulation of cell growth Source: UniProtKB
  16. negative regulation of chondrocyte proliferation Source: AgBase
  17. negative regulation of DNA biosynthetic process Source: BHF-UCL
  18. negative regulation of systemic arterial blood pressure Source: BHF-UCL
  19. negative regulation of vasoconstriction Source: BHF-UCL
  20. positive regulation of axon extension involved in axon guidance Source: Ensembl
  21. positive regulation of BMP signaling pathway Source: UniProtKB
  22. positive regulation of bone mineralization Source: BHF-UCL
  23. positive regulation of cartilage development Source: AgBase
  24. positive regulation of endothelial cell migration Source: UniProtKB
  25. positive regulation of endothelial cell proliferation Source: UniProtKB
  26. positive regulation of epithelial cell migration Source: UniProtKB
  27. positive regulation of osteoblast differentiation Source: BHF-UCL
  28. positive regulation of pathway-restricted SMAD protein phosphorylation Source: UniProtKB
  29. proteoglycan biosynthetic process Source: AgBase
  30. regulation of cell proliferation Source: HGNC
  31. regulation of lung blood pressure Source: BHF-UCL
  32. retina vasculature development in camera-type eye Source: BHF-UCL
  33. transcription from RNA polymerase II promoter Source: BHF-UCL
  34. transmembrane receptor protein serine/threonine kinase signaling pathway Source: BHF-UCL
  35. vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  36. venous blood vessel development Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_12034. Signaling by BMP.
SignaLinkiQ13873.

Names & Taxonomyi

Protein namesi
Recommended name:
Bone morphogenetic protein receptor type-2 (EC:2.7.11.30)
Short name:
BMP type-2 receptor
Short name:
BMPR-2
Alternative name(s):
Bone morphogenetic protein receptor type II
Short name:
BMP type II receptor
Short name:
BMPR-II
Gene namesi
Name:BMPR2
Synonyms:PPH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:1078. BMPR2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 150124ExtracellularSequence AnalysisAdd
BLAST
Transmembranei151 – 17121HelicalSequence AnalysisAdd
BLAST
Topological domaini172 – 1038867CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. basal plasma membrane Source: Ensembl
  3. caveola Source: Ensembl
  4. cell surface Source: Ensembl
  5. cytoplasm Source: Ensembl
  6. dendrite Source: Ensembl
  7. extracellular space Source: UniProtKB
  8. integral component of plasma membrane Source: BHF-UCL
  9. neuronal cell body Source: Ensembl
  10. plasma membrane Source: BHF-UCL
  11. spanning component of plasma membrane Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Pulmonary hypertension, primary, 1 (PPH1)6 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare disorder characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure, and death. The disease can occur from infancy throughout life and it has a mean age at onset of 36 years. Penetrance is reduced. Although familial pulmonary hypertension is rare, cases secondary to known etiologies are more common and include those associated with the appetite-suppressant drugs.

See also OMIM:178600
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601C → Y in PPH1. 1 Publication
VAR_013670
Natural varianti82 – 821Q → H in PPH1. 1 Publication
VAR_033109
Natural varianti117 – 1171C → Y in PPH1. 1 Publication
VAR_013671
Natural varianti118 – 1181C → W in PPH1. 1 Publication
VAR_013672
Natural varianti123 – 1231C → R in PPH1. 1 Publication
VAR_013673
Natural varianti123 – 1231C → S in PPH1. 1 Publication
VAR_013674
Natural varianti182 – 1821G → D in PPH1. 1 Publication
VAR_033110
Natural varianti347 – 3471C → Y in PPH1. 1 Publication
VAR_013676
Natural varianti420 – 4201C → R in PPH1. 1 Publication
VAR_013677
Natural varianti483 – 4831C → R in PPH1; sporadic. 2 Publications
VAR_013678
Natural varianti485 – 4851D → G in PPH1; complete loss of function. 2 Publications
VAR_013679
Natural varianti491 – 4911R → Q in PPH1; sporadic. 1 Publication
VAR_013680
Natural varianti491 – 4911R → W in PPH1. 1 Publication
VAR_013681
Natural varianti512 – 5121K → T in PPH1. 1 Publication
VAR_013682
Natural varianti519 – 5191N → K in PPH1.
VAR_013683
Natural varianti899 – 8991R → P in PPH1; leads to constitutive activation of the MAPK14 pathway. 1 Publication
Corresponds to variant rs137852752 [ dbSNP | Ensembl ].
VAR_033111
Pulmonary venoocclusive disease 1, autosomal dominant (PVOD1)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disease characterized by widespread fibrous obstruction and intimal thickening of septal veins and preseptal venules, a low diffusing capacity for carbon monoxide, occult alveolar hemorrhage, and nodular ground-glass opacities, septal lines and lymph node enlargement showed by high-resolution computed tomography of the chest. It is frequently associated with pulmonary capillary dilatation and proliferation, and is a rare and devastating cause of pulmonary hypertension.

See also OMIM:265450

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi178600. phenotype.
265450. phenotype.
Orphaneti275777. Heritable pulmonary arterial hypertension.
275766. Idiopathic pulmonary arterial hypertension.
31837. Pulmonary venoocclusive disease.
PharmGKBiPA25388.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 10381012Bone morphogenetic protein receptor type-2PRO_0000024415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 66By similarity
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi94 ↔ 117By similarity
Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Modified residuei379 – 3791Phosphothreonine1 Publication
Modified residuei586 – 5861Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ13873.
PaxDbiQ13873.
PRIDEiQ13873.

PTM databases

PhosphoSiteiQ13873.

Expressioni

Tissue specificityi

Highly expressed in heart and liver.

Gene expression databases

BgeeiQ13873.
CleanExiHS_BMPR2.
GenevestigatoriQ13873.

Organism-specific databases

HPAiHPA017385.
HPA049014.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
C4bpaP086073EBI-527196,EBI-527325From a different organism.
GDF5P430264EBI-527196,EBI-8571476
PrkcbP684044EBI-527196,EBI-397048From a different organism.
PRKG1Q139762EBI-527196,EBI-3952014

Protein-protein interaction databases

BioGridi107127. 51 interactions.
DIPiDIP-5794N.
IntActiQ13873. 33 interactions.
MINTiMINT-124272.
STRINGi9606.ENSP00000363708.

Structurei

Secondary structure

1
1038
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 353Combined sources
Turni42 – 476Combined sources
Helixi48 – 503Combined sources
Turni53 – 564Combined sources
Beta strandi57 – 593Combined sources
Beta strandi66 – 738Combined sources
Beta strandi76 – 849Combined sources
Beta strandi90 – 923Combined sources
Turni105 – 1095Combined sources
Beta strandi113 – 1186Combined sources
Helixi123 – 1253Combined sources
Beta strandi202 – 21110Combined sources
Beta strandi213 – 22210Combined sources
Beta strandi225 – 2339Combined sources
Helixi234 – 2363Combined sources
Helixi237 – 24711Combined sources
Beta strandi260 – 2678Combined sources
Beta strandi273 – 2797Combined sources
Helixi287 – 2937Combined sources
Helixi298 – 31619Combined sources
Helixi322 – 3243Combined sources
Beta strandi338 – 3414Combined sources
Beta strandi347 – 3493Combined sources
Beta strandi359 – 3624Combined sources
Helixi380 – 3823Combined sources
Helixi385 – 3884Combined sources
Helixi394 – 3963Combined sources
Helixi397 – 41721Combined sources
Helixi421 – 4233Combined sources
Helixi437 – 4404Combined sources
Helixi446 – 4538Combined sources
Helixi471 – 48313Combined sources
Helixi488 – 4903Combined sources
Helixi494 – 50613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HLQX-ray1.45A33-131[»]
3G2FX-ray2.35A/B189-517[»]
ProteinModelPortaliQ13873.
SMRiQ13873. Positions 33-131, 197-510.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13873.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini203 – 504302Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi547 – 5504Poly-Ser
Compositional biasi610 – 6189Poly-Thr
Compositional biasi901 – 9088Poly-Asn

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000043088.
HOVERGENiHBG050705.
InParanoidiQ13873.
KOiK04671.
OMAiDHYKPAI.
OrthoDBiEOG7JHM5B.
PhylomeDBiQ13873.
TreeFamiTF314724.

Family and domain databases

InterProiIPR015770. BMPR2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000472. TFB_recept_I/II_C.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PTHR23255:SF63. PTHR23255:SF63. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 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. AlignAdd to basket

Isoform 1 (identifier: Q13873-1) [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
MTSSLQRPWR VPWLPWTILL VSTAAASQNQ ERLCAFKDPY QQDLGIGESR
60 70 80 90 100
ISHENGTILC SKGSTCYGLW EKSKGDINLV KQGCWSHIGD PQECHYEECV
110 120 130 140 150
VTTTPPSIQN GTYRFCCCST DLCNVNFTEN FPPPDTTPLS PPHSFNRDET
160 170 180 190 200
IIIALASVSV LAVLIVALCF GYRMLTGDRK QGLHSMNMME AAASEPSLDL
210 220 230 240 250
DNLKLLELIG RGRYGAVYKG SLDERPVAVK VFSFANRQNF INEKNIYRVP
260 270 280 290 300
LMEHDNIARF IVGDERVTAD GRMEYLLVME YYPNGSLCKY LSLHTSDWVS
310 320 330 340 350
SCRLAHSVTR GLAYLHTELP RGDHYKPAIS HRDLNSRNVL VKNDGTCVIS
360 370 380 390 400
DFGLSMRLTG NRLVRPGEED NAAISEVGTI RYMAPEVLEG AVNLRDCESA
410 420 430 440 450
LKQVDMYALG LIYWEIFMRC TDLFPGESVP EYQMAFQTEV GNHPTFEDMQ
460 470 480 490 500
VLVSREKQRP KFPEAWKENS LAVRSLKETI EDCWDQDAEA RLTAQCAEER
510 520 530 540 550
MAELMMIWER NKSVSPTVNP MSTAMQNERN LSHNRRVPKI GPYPDYSSSS
560 570 580 590 600
YIEDSIHHTD SIVKNISSEH SMSSTPLTIG EKNRNSINYE RQQAQARIPS
610 620 630 640 650
PETSVTSLST NTTTTNTTGL TPSTGMTTIS EMPYPDETNL HTTNVAQSIG
660 670 680 690 700
PTPVCLQLTE EDLETNKLDP KEVDKNLKES SDENLMEHSL KQFSGPDPLS
710 720 730 740 750
STSSSLLYPL IKLAVEATGQ QDFTQTANGQ ACLIPDVLPT QIYPLPKQQN
760 770 780 790 800
LPKRPTSLPL NTKNSTKEPR LKFGSKHKSN LKQVETGVAK MNTINAAEPH
810 820 830 840 850
VVTVTMNGVA GRNHSVNSHA ATTQYANGTV LSGQTTNIVT HRAQEMLQNQ
860 870 880 890 900
FIGEDTRLNI NSSPDEHEPL LRREQQAGHD EGVLDRLVDR RERPLEGGRT
910 920 930 940 950
NSNNNNSNPC SEQDVLAQGV PSTAADPGPS KPRRAQRPNS LDLSATNVLD
960 970 980 990 1000
GSSIQIGEST QDGKSGSGEK IKKRVKTPYS LKRWRPSTWV ISTESLDCEV
1010 1020 1030
NNNGSNRAVH SKSSTAVYLA EGGTATTMVS KDIGMNCL
Length:1,038
Mass (Da):115,201
Last modified:December 1, 2000 - v2
Checksum:i1389923CE574B913
GO
Isoform 2 (identifier: Q13873-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     530-530: N → R
     531-1038: Missing.

Show »
Length:530
Mass (Da):59,963
Checksum:iA1F2BC5D95F42D7C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti828 – 8281G → R in CAA88759 (PubMed:7644468).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601C → Y in PPH1. 1 Publication
VAR_013670
Natural varianti82 – 821Q → H in PPH1. 1 Publication
VAR_033109
Natural varianti117 – 1171C → Y in PPH1. 1 Publication
VAR_013671
Natural varianti118 – 1181C → W in PPH1. 1 Publication
VAR_013672
Natural varianti123 – 1231C → R in PPH1. 1 Publication
VAR_013673
Natural varianti123 – 1231C → S in PPH1. 1 Publication
VAR_013674
Natural varianti182 – 1821G → D in PPH1. 1 Publication
VAR_033110
Natural varianti224 – 2241E → D.1 Publication
VAR_013675
Natural varianti347 – 3471C → Y in PPH1. 1 Publication
VAR_013676
Natural varianti420 – 4201C → R in PPH1. 1 Publication
VAR_013677
Natural varianti483 – 4831C → R in PPH1; sporadic. 2 Publications
VAR_013678
Natural varianti485 – 4851D → G in PPH1; complete loss of function. 2 Publications
VAR_013679
Natural varianti491 – 4911R → Q in PPH1; sporadic. 1 Publication
VAR_013680
Natural varianti491 – 4911R → W in PPH1. 1 Publication
VAR_013681
Natural varianti512 – 5121K → T in PPH1. 1 Publication
VAR_013682
Natural varianti519 – 5191N → K in PPH1.
VAR_013683
Natural varianti775 – 7751S → N.1 Publication
Corresponds to variant rs2228545 [ dbSNP | Ensembl ].
VAR_019996
Natural varianti899 – 8991R → P in PPH1; leads to constitutive activation of the MAPK14 pathway. 1 Publication
Corresponds to variant rs137852752 [ dbSNP | Ensembl ].
VAR_033111

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei530 – 5301N → R in isoform 2. 2 PublicationsVSP_054441
Alternative sequencei531 – 1038508Missing in isoform 2. 2 PublicationsVSP_054442Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25110 mRNA. Translation: AAA86519.1.
Z48923 mRNA. Translation: CAA88759.1.
D50516 mRNA. Translation: BAA09094.1.
U20165 mRNA. Translation: AAC50105.1.
AC009960 Genomic DNA. Translation: AAX76517.1.
AC073410 Genomic DNA. Translation: AAX88941.1.
AC064836 Genomic DNA. Translation: AAY24146.1.
CH471063 Genomic DNA. Translation: EAW70309.1.
BC052985 mRNA. Translation: AAH52985.1.
CCDSiCCDS33361.1. [Q13873-1]
PIRiI38935.
RefSeqiNP_001195.2. NM_001204.6. [Q13873-1]
UniGeneiHs.471119.

Genome annotation databases

EnsembliENST00000374574; ENSP00000363702; ENSG00000204217. [Q13873-2]
ENST00000374580; ENSP00000363708; ENSG00000204217. [Q13873-1]
GeneIDi659.
KEGGihsa:659.
UCSCiuc002uzf.4. human. [Q13873-1]
uc010ftr.3. human.

Polymorphism databases

DMDMi12643724.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25110 mRNA. Translation: AAA86519.1.
Z48923 mRNA. Translation: CAA88759.1.
D50516 mRNA. Translation: BAA09094.1.
U20165 mRNA. Translation: AAC50105.1.
AC009960 Genomic DNA. Translation: AAX76517.1.
AC073410 Genomic DNA. Translation: AAX88941.1.
AC064836 Genomic DNA. Translation: AAY24146.1.
CH471063 Genomic DNA. Translation: EAW70309.1.
BC052985 mRNA. Translation: AAH52985.1.
CCDSiCCDS33361.1. [Q13873-1]
PIRiI38935.
RefSeqiNP_001195.2. NM_001204.6. [Q13873-1]
UniGeneiHs.471119.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HLQX-ray1.45A33-131[»]
3G2FX-ray2.35A/B189-517[»]
ProteinModelPortaliQ13873.
SMRiQ13873. Positions 33-131, 197-510.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107127. 51 interactions.
DIPiDIP-5794N.
IntActiQ13873. 33 interactions.
MINTiMINT-124272.
STRINGi9606.ENSP00000363708.

Chemistry

BindingDBiQ13873.
ChEMBLiCHEMBL5467.
GuidetoPHARMACOLOGYi1794.

PTM databases

PhosphoSiteiQ13873.

Polymorphism databases

DMDMi12643724.

Proteomic databases

MaxQBiQ13873.
PaxDbiQ13873.
PRIDEiQ13873.

Protocols and materials databases

DNASUi659.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374574; ENSP00000363702; ENSG00000204217. [Q13873-2]
ENST00000374580; ENSP00000363708; ENSG00000204217. [Q13873-1]
GeneIDi659.
KEGGihsa:659.
UCSCiuc002uzf.4. human. [Q13873-1]
uc010ftr.3. human.

Organism-specific databases

CTDi659.
GeneCardsiGC02P203205.
GeneReviewsiBMPR2.
HGNCiHGNC:1078. BMPR2.
HPAiHPA017385.
HPA049014.
MIMi178600. phenotype.
265450. phenotype.
600799. gene.
neXtProtiNX_Q13873.
Orphaneti275777. Heritable pulmonary arterial hypertension.
275766. Idiopathic pulmonary arterial hypertension.
31837. Pulmonary venoocclusive disease.
PharmGKBiPA25388.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000043088.
HOVERGENiHBG050705.
InParanoidiQ13873.
KOiK04671.
OMAiDHYKPAI.
OrthoDBiEOG7JHM5B.
PhylomeDBiQ13873.
TreeFamiTF314724.

Enzyme and pathway databases

ReactomeiREACT_12034. Signaling by BMP.
SignaLinkiQ13873.

Miscellaneous databases

ChiTaRSiBMPR2. human.
EvolutionaryTraceiQ13873.
GeneWikiiBMPR2.
GenomeRNAii659.
NextBioi2680.
PROiQ13873.
SOURCEiSearch...

Gene expression databases

BgeeiQ13873.
CleanExiHS_BMPR2.
GenevestigatoriQ13873.

Family and domain databases

InterProiIPR015770. BMPR2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000472. TFB_recept_I/II_C.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PTHR23255:SF63. PTHR23255:SF63. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs."
    Liu F., Ventura F., Doody J., Massague J.
    Mol. Cell. Biol. 15:3479-3486(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    Tissue: Kidney.
  2. "Cloning and characterization of a human type II receptor for bone morphogenetic proteins."
    Rosenzweig B.L., Imamura T., Okadome T., Cox G.N., Yamashita H., ten Dijke P., Heldin C., Miyazono K.
    Proc. Natl. Acad. Sci. U.S.A. 92:7632-7636(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Substantia nigra.
  3. "Identification of a human type II receptor for bone morphogenetic protein-4 that forms differential heteromeric complexes with bone morphogenetic protein type I receptors."
    Nohno T., Ishikawa T., Saito T., Hosokawa K., Noji S., Wosing D.H., Rosenbaum J.S.
    J. Biol. Chem. 270:22522-22526(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Skin fibroblast.
  4. "Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor."
    Kawabata M., Chytil A., Moses H.L.
    J. Biol. Chem. 270:5625-5630(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Skin.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Crystal structure of the BMPR2 kinase domain."
    Structural genomics consortium (SGC)
    Submitted (JAN-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 189-517 IN COMPLEX WITH ADP.
  12. "Familial primary pulmonary hypertension (gene PPH1) is caused by mutations in the bone morphogenetic protein receptor-II gene."
    Deng Z., Morse J.H., Slager S.L., Cuervo N., Moore K.J., Venetos G., Kalachikov S., Cayanis E., Fischer S.G., Barst R.J., Hodge S.E., Knowles J.A.
    Am. J. Hum. Genet. 67:737-744(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PPH1 GLN-491 AND TRP-491.
  13. "Sporadic primary pulmonary hypertension is associated with germline mutations of the gene encoding BMPR-II, a receptor member of the TGF-beta family."
    Thomson J.R., Machado R.D., Pauciulo M.W., Morgan N.V., Humbert M., Elliott G.C., Ward K., Yacoub M., Mikhail G., Rogers P., Newman J.H., Wheeler L., Higenbottam T., Gibbs J.S.R., Egan J., Crozier A., Peacock A., Allcock R.
    , Corris P., Loyd J.E., Trembath R.C., Nichols W.C.
    J. Med. Genet. 37:741-745(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PPH1 TYR-60; TYR-117 AND ARG-483.
  14. Cited for: VARIANTS PPH1 TRP-118; TYR-347 AND GLY-485.
  15. Cited for: VARIANTS PPH1 ARG-123; SER-123; ARG-420 AND THR-512, VARIANT ASP-224, CHARACTERIZATION OF VARIANT PPH1 GLY-485.
  16. "BMPR2 germline mutations in pulmonary hypertension associated with fenfluramine derivatives."
    Humbert M., Deng Z., Simonneau G., Barst R.J., Sitbon O., Wolf M., Cuervo N., Moore K.J., Hodge S.E., Knowles J.A., Morse J.H.
    Eur. Respir. J. 20:518-523(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PPH1 HIS-82; ASP-182 AND ARG-483.
  17. "Pulmonary veno-occlusive disease caused by an inherited mutation in bone morphogenetic protein receptor II."
    Runo J.R., Vnencak-Jones C.L., Prince M., Loyd J.E., Wheeler L., Robbins I.M., Lane K.B., Newman J.H., Johnson J., Nichols W.C., Phillips J.A. III
    Am. J. Respir. Crit. Care Med. 167:889-894(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PVOD1.
  18. Cited for: VARIANT PPH1 PRO-899, CHARACTERIZATION OF VARIANT PPH1 PRO-899.
  19. Cited for: INVOLVEMENT IN PVOD1.
  20. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-775.

Entry informationi

Entry nameiBMPR2_HUMAN
AccessioniPrimary (citable) accession number: Q13873
Secondary accession number(s): Q13161
, Q16569, Q4ZG08, Q53SA5, Q585T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: April 1, 2015
This is version 171 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.