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Q13873 (BMPR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·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):
Bone morphogenetic protein receptor type II
Short name=BMP type II receptor
Short name=BMPR-II
Gene names
Name:BMPR2
Synonyms:PPH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

Tissue specificity

Highly expressed in heart and liver.

Involvement in disease

Pulmonary hypertension, primary, 1 (PPH1) [MIM:178600]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

Pulmonary venoocclusive disease 1, autosomal dominant (PVOD1) [MIM:265450]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.16

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
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   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 term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from direct assay PubMed 18436533. Source: BHF-UCL

activin receptor signaling pathway

Traceable author statement. Source: GOC

anterior/posterior pattern specification

Inferred from sequence or structural similarity. Source: BHF-UCL

artery development

Inferred from sequence or structural similarity. Source: BHF-UCL

blood vessel remodeling

Inferred from sequence or structural similarity. Source: BHF-UCL

brain development

Inferred from electronic annotation. Source: Ensembl

cellular response to starvation

Inferred from expression pattern PubMed 15657086. Source: BHF-UCL

lung alveolus development

Inferred from sequence or structural similarity. Source: BHF-UCL

lymphangiogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

lymphatic endothelial cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

mesoderm formation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of DNA biosynthetic process

Inferred from mutant phenotype PubMed 19366699. Source: BHF-UCL

negative regulation of cell growth

Inferred from direct assay PubMed 12819188. Source: UniProtKB

negative regulation of systemic arterial blood pressure

Inferred from mutant phenotype PubMed 18364108. Source: BHF-UCL

negative regulation of vasoconstriction

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of BMP signaling pathway

Inferred from mutant phenotype PubMed 17992660. Source: UniProtKB

positive regulation of bone mineralization

Inferred from mutant phenotype PubMed 18436533. Source: BHF-UCL

positive regulation of endothelial cell migration

Inferred from mutant phenotype PubMed 17992660. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 17992660. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from direct assay PubMed 12819188. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 18436533. Source: BHF-UCL

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from mutant phenotype PubMed 17992660. Source: UniProtKB

regulation of cell proliferation

Inferred from mutant phenotype PubMed 11502704. Source: HGNC

regulation of lung blood pressure

Inferred from mutant phenotype PubMed 18364108. Source: BHF-UCL

retina vasculature development in camera-type eye

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 12045205. Source: BHF-UCL

transmembrane receptor protein serine/threonine kinase signaling pathway

Inferred from direct assay PubMed 12045205. Source: BHF-UCL

vascular endothelial growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

venous blood vessel development

Inferred from sequence or structural similarity. 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 electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

integral component of plasma membrane

Inferred from direct assay PubMed 12045205. Source: BHF-UCL

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 15657086. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

activin receptor activity, type II

Traceable author statement. Source: Reactome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta-activated receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 10381012Bone morphogenetic protein receptor type-2
PRO_0000024415

Regions

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

Sites

Active site3331Proton acceptor By similarity
Binding site2301ATP
Binding site3511ATP

Amino acid modifications

Modified residue3791Phosphothreonine Ref.7
Modified residue5861Phosphoserine Ref.6
Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation1101N-linked (GlcNAc...) Potential
Glycosylation1261N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 66 By similarity
Disulfide bond94 ↔ 117 By similarity

Natural variations

Natural variant601C → Y in PPH1. Ref.10
VAR_013670
Natural variant821Q → H in PPH1. Ref.13
VAR_033109
Natural variant1171C → Y in PPH1. Ref.10
VAR_013671
Natural variant1181C → W in PPH1. Ref.11
VAR_013672
Natural variant1231C → R in PPH1. Ref.12
VAR_013673
Natural variant1231C → S in PPH1. Ref.12
VAR_013674
Natural variant1821G → D in PPH1. Ref.13
VAR_033110
Natural variant2241E → D. Ref.12
VAR_013675
Natural variant3471C → Y in PPH1. Ref.11
VAR_013676
Natural variant4201C → R in PPH1. Ref.12
VAR_013677
Natural variant4831C → R in PPH1; sporadic. Ref.10 Ref.13
VAR_013678
Natural variant4851D → G in PPH1; complete loss of function. Ref.11 Ref.12
VAR_013679
Natural variant4911R → Q in PPH1; sporadic. Ref.9
VAR_013680
Natural variant4911R → W in PPH1. Ref.9
VAR_013681
Natural variant5121K → T in PPH1. Ref.12
VAR_013682
Natural variant5191N → K in PPH1.
VAR_013683
Natural variant7751S → N. Ref.17
Corresponds to variant rs2228545 [ dbSNP | Ensembl ].
VAR_019996
Natural variant8991R → P in PPH1; leads to constitutive activation of the MAPK14 pathway. Ref.15
Corresponds to variant rs137852752 [ dbSNP | Ensembl ].
VAR_033111

Experimental info

Sequence conflict8281G → R in CAA88759. Ref.1

Secondary structure

................................................................ 1038
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13873 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 1389923CE574B913

FASTA1,038115,201
        10         20         30         40         50         60 
MTSSLQRPWR VPWLPWTILL VSTAAASQNQ 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 AAASEPSLDL DNLKLLELIG RGRYGAVYKG SLDERPVAVK VFSFANRQNF 

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

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

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

       430        440        450        460        470        480 
TDLFPGESVP EYQMAFQTEV 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 EMPYPDETNL HTTNVAQSIG PTPVCLQLTE 

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

       730        740        750        760        770        780 
QDFTQTANGQ ACLIPDVLPT QIYPLPKQQN LPKRPTSLPL NTKNSTKEPR LKFGSKHKSN 

       790        800        810        820        830        840 
LKQVETGVAK MNTINAAEPH VVTVTMNGVA GRNHSVNSHA ATTQYANGTV LSGQTTNIVT 

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

       910        920        930        940        950        960 
NSNNNNSNPC SEQDVLAQGV PSTAADPGPS KPRRAQRPNS LDLSATNVLD GSSIQIGEST 

       970        980        990       1000       1010       1020 
QDGKSGSGEK IKKRVKTPYS LKRWRPSTWV ISTESLDCEV NNNGSNRAVH SKSSTAVYLA 

      1030 
EGGTATTMVS KDIGMNCL 

« Hide

References

« Hide 'large scale' references
[1]"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(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Substantia nigra.
[2]"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(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skin fibroblast.
[3]"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(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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. expand/collapse author list , 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(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Skin.
[6]"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(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Crystal structure of the BMPR2 kinase domain."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 189-517 IN COMPLEX WITH ADP.
[9]"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(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PPH1 GLN-491 AND TRP-491.
[10]"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. expand/collapse author list , Corris P., Loyd J.E., Trembath R.C., Nichols W.C.
J. Med. Genet. 37:741-745(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PPH1 TYR-60; TYR-117 AND ARG-483.
[11]"Heterozygous germline mutations in BMPR2, encoding a TGF-beta receptor, cause familial primary pulmonary hypertension."
Lane K.B., Machado R.D., Pauciulo M.W., Thomson J.R., Phillips J.A. III, Loyd J.E., Nichols W.C., Trembath R.C., Aldred M., Brannon C.A., Conneally P.M., Foroud T., Fretwell N., Gaddipati R., Koller D., Loyd E.J., Morgan N.V., Newman J.H. expand/collapse author list , Prince M.A., Vilarino Gueell C., Wheeler L.
Nat. Genet. 26:81-84(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PPH1 TRP-118; TYR-347 AND GLY-485.
[12]"BMPR2 haploinsufficiency as the inherited molecular mechanism for primary pulmonary hypertension."
Machado R.D., Pauciulo M.W., Thomson J.R., Lane K.B., Morgan N.V., Wheeler L., Phillips J.A. III, Newman J.H., Williams D., Galie N., Manes A., McNeil K., Yacoub M., Mikhail G., Rogers P., Corris P., Humbert M., Donnai D. expand/collapse author list , Martensson G., Tranebjaerg L., Loyd J.E., Trembath R.C., Nichols W.C.
Am. J. Hum. Genet. 68:92-102(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PPH1 ARG-123; SER-123; ARG-420 AND THR-512, VARIANT ASP-224, CHARACTERIZATION OF VARIANT PPH1 GLY-485.
[13]"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(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PPH1 HIS-82; ASP-182 AND ARG-483.
[14]"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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PVOD1.
[15]"BMPR2 mutations have short lifetime expectancy in primary pulmonary hypertension."
Sankelo M., Flanagan J.A., Machado R., Harrison R., Rudarakanchana N., Morrell N., Dixon M., Halme M., Puolijoki H., Kere J., Elomaa O., Kupari M., Raeisaenen-Sokolowski A., Trembath R.C., Laitinen T.
Hum. Mutat. 26:119-124(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PPH1 PRO-899, CHARACTERIZATION OF VARIANT PPH1 PRO-899.
[16]"Mutations of the TGF-beta type II receptor BMPR2 in pulmonary arterial hypertension."
Machado R.D., Aldred M.A., James V., Harrison R.E., Patel B., Schwalbe E.C., Gruenig E., Janssen B., Koehler R., Seeger W., Eickelberg O., Olschewski H., Elliott C.G., Glissmeyer E., Carlquist J., Kim M., Torbicki A., Fijalkowska A. expand/collapse author list , Szewczyk G., Parma J., Abramowicz M.J., Galie N., Morisaki H., Kyotani S., Nakanishi N., Morisaki T., Humbert M., Simonneau G., Sitbon O., Soubrier F., Coulet F., Morrell N.W., Trembath R.C.
Hum. Mutat. 27:121-132(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PVOD1.
[17]"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. expand/collapse author list , 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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-775.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
BC052985 mRNA. Translation: AAH52985.1.
PIRI38935.
RefSeqNP_001195.2. NM_001204.6.
UniGeneHs.471119.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HLQX-ray1.45A33-131[»]
3G2FX-ray2.35A/B189-517[»]
ProteinModelPortalQ13873.
SMRQ13873. Positions 33-131, 197-510.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107127. 50 interactions.
DIPDIP-5794N.
IntActQ13873. 33 interactions.
MINTMINT-124272.
STRING9606.ENSP00000363708.

Chemistry

BindingDBQ13873.
ChEMBLCHEMBL5467.
GuidetoPHARMACOLOGY1794.

PTM databases

PhosphoSiteQ13873.

Polymorphism databases

DMDM12643724.

Proteomic databases

PaxDbQ13873.
PRIDEQ13873.

Protocols and materials databases

DNASU659.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374580; ENSP00000363708; ENSG00000204217.
GeneID659.
KEGGhsa:659.
UCSCuc002uzf.4. human.

Organism-specific databases

CTD659.
GeneCardsGC02P203205.
HGNCHGNC:1078. BMPR2.
HPAHPA017385.
MIM178600. phenotype.
265450. phenotype.
600799. gene.
neXtProtNX_Q13873.
Orphanet275777. Heritable pulmonary arterial hypertension.
275766. Idiopathic pulmonary arterial hypertension.
31837. Pulmonary venoocclusive disease.
PharmGKBPA25388.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000043088.
HOVERGENHBG050705.
InParanoidQ13873.
KOK04671.
OMADHYKPAI.
OrthoDBEOG7JHM5B.
PhylomeDBQ13873.
TreeFamTF314724.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ13873.

Gene expression databases

ArrayExpressQ13873.
BgeeQ13873.
CleanExHS_BMPR2.
GenevestigatorQ13873.

Family and domain databases

InterProIPR000472. Activin_rcpt.
IPR015770. BMPRII.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PANTHERPTHR23255:SF12. PTHR23255:SF12. 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. human.
EvolutionaryTraceQ13873.
GeneWikiBMPR2.
GenomeRNAi659.
NextBio2680.
PROQ13873.
SOURCESearch...

Entry information

Entry nameBMPR2_HUMAN
AccessionPrimary (citable) accession number: Q13873
Secondary accession number(s): Q16569 expand/collapse secondary AC list , Q4ZG08, Q53SA5, Q585T8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM