Q13873 (BMPR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1038 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Primary pulmonary hypertension (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 PPH1 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 (PVOD) [MIM:265450]: Rare form of pulmonary hypertension in which the vascular changes originate in the small pulmonary veins and venules. The pathogenesis is unknown and any link with PPH1 has been speculative. The finding of PVOD associated with a BMPR2 mutation reveals a possible pathogenetic connection with PPH1. 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 component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Inferred from direct assay PubMed 18436533. Source: BHF-UCL 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 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 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 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_component	cell surface Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from direct assay PubMed 12045205. Source: BHF-UCL
Molecular_function	ATP 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
C4bpa	P08607	3	EBI-527196,EBI-527325	From a different organism.
Prkcb	P68404	4	EBI-527196,EBI-397048	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 1038

1012

Bone morphogenetic protein receptor type-2

PRO_0000024415

Regions

Topological domain

27 – 150

124

Extracellular Potential

Transmembrane

151 – 171

21

Helical; Potential

Topological domain

172 – 1038

867

Cytoplasmic Potential

Domain

203 – 504

302

Protein kinase

Nucleotide binding

209 – 217

9

ATP

Nucleotide binding

280 – 282

3

ATP

Nucleotide binding

337 – 338

2

ATP

Compositional bias

547 – 550

4

Poly-Ser

Compositional bias

610 – 618

9

Poly-Thr

Compositional bias

901 – 908

8

Poly-Asn

Sites

Active site

333

1

Proton acceptor By similarity

Binding site

230

1

ATP

Binding site

351

1

ATP

Amino acid modifications

Modified residue

379

1

Phosphothreonine Ref.7

Modified residue

586

1

Phosphoserine Ref.6

Glycosylation

55

1

N-linked (GlcNAc...) Potential

Glycosylation

110

1

N-linked (GlcNAc...) Potential

Glycosylation

126

1

N-linked (GlcNAc...) Potential

Disulfide bond

34 ↔ 66

By similarity

Disulfide bond

94 ↔ 117

By similarity

Natural variations

Natural variant

60

1

C → Y in PPH1. Ref.10

VAR_013670

Natural variant

82

1

Q → H in PPH1. Ref.13

VAR_033109

Natural variant

117

1

C → Y in PPH1. Ref.10

VAR_013671

Natural variant

118

1

C → W in PPH1. Ref.11

VAR_013672

Natural variant

123

1

C → R in PPH1. Ref.12

VAR_013673

Natural variant

123

1

C → S in PPH1. Ref.12

VAR_013674

Natural variant

182

1

G → D in PPH1. Ref.13

VAR_033110

Natural variant

224

1

E → D. Ref.12

VAR_013675

Natural variant

347

1

C → Y in PPH1. Ref.11

VAR_013676

Natural variant

420

1

C → R in PPH1. Ref.12

VAR_013677

Natural variant

483

1

C → R in PPH1; sporadic. Ref.10 Ref.13

VAR_013678

Natural variant

485

1

D → G in PPH1; complete loss of function. Ref.11 Ref.12

VAR_013679

Natural variant

491

1

R → Q in PPH1; sporadic. Ref.9

VAR_013680

Natural variant

491

1

R → W in PPH1. Ref.9

VAR_013681

Natural variant

512

1

K → T in PPH1. Ref.12

VAR_013682

Natural variant

519

1

N → K in PPH1.

VAR_013683

Natural variant

775

1

S → N. Ref.17
Corresponds to variant rs2228545 [ dbSNP | Ensembl ].

VAR_019996

Natural variant

899

1

R → P in PPH1; leads to constitutive activation of the MAPK14 pathway. Ref.15

VAR_033111

Experimental info

Sequence conflict

828

1

G → R in CAA88759. Ref.1

Secondary structure

1

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1038

Helix Strand Turn

Details...

Beta strand

33 – 35

3

Turn

42 – 47

6

Helix

48 – 50

3

Turn

53 – 56

4

Beta strand

57 – 59

3

Beta strand

66 – 73

8

Beta strand

76 – 84

9

Beta strand

90 – 92

3

Turn

105 – 109

5

Beta strand

113 – 118

6

Helix

123 – 125

3

Beta strand

202 – 211

10

Beta strand

213 – 222

10

Beta strand

225 – 233

9

Helix

234 – 236

3

Helix

237 – 247

11

Beta strand

260 – 267

8

Beta strand

273 – 279

7

Helix

287 – 293

7

Helix

298 – 316

19

Helix

322 – 324

3

Beta strand

338 – 341

4

Beta strand

347 – 349

3

Beta strand

359 – 362

4

Helix

380 – 382

3

Helix

385 – 388

4

Helix

394 – 396

3

Helix

397 – 417

21

Helix

421 – 423

3

Helix

437 – 440

4

Helix

446 – 453

8

Helix

471 – 483

13

Helix

488 – 490

3

Helix

494 – 506

13

Sequences

	Sequence		Length	Mass (Da)
	Q13873 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 1389923CE574B913	FASTA	1,038	115,201
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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. , 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. , 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. , 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 PVOD.
[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. , 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 PVOD.
[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. , 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

GeneReviews

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.

IPI

IPI00783156.

PIR

I38935.

RefSeq

NP_001195.2. NM_001204.6.

UniGene

Hs.471119.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HLQ	X-ray	1.45	A	33-131	[»]
3G2F	X-ray	2.35	A/B	189-517	[»]

ProteinModelPortal

Q13873.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5794N.
DIP-5941N.
DIP-5942N.

IntAct

Q13873. 30 interactions.

STRING

9606.ENSP00000363708.

PTM databases

PhosphoSite

Q13873.

Polymorphism databases

DMDM

12643724.

Proteomic databases

PaxDb

Q13873.

PRIDE

Q13873.

Protocols and materials databases

DNASU

659.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374580; ENSP00000363708; ENSG00000204217.

GeneID

659.

KEGG

hsa:659.

UCSC

uc002uzf.4. human.

Organism-specific databases

CTD

659.

GeneCards

GC02P203205.

HGNC

HGNC:1078. BMPR2.

HPA

HPA017385.

MIM

178600. phenotype.
265450. phenotype.
600799. gene.

neXtProt

NX_Q13873.

Orphanet

275777. Heritable pulmonary arterial hypertension.
275766. Idiopathic pulmonary arterial hypertension.
31837. Pulmonary venoocclusive disease.

PharmGKB

PA25388.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000043088.

HOVERGEN

HBG050705.

InParanoid

Q13873.

KO

K04671.

OMA

LPRGDHY.

OrthoDB

EOG470TGJ.

Enzyme and pathway databases

Pathway_Interaction_DB

bmppathway. BMP receptor signaling.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q13873.

Bgee

Q13873.

CleanEx

HS_BMPR2.

Genevestigator

Q13873.

GermOnline

ENSG00000204217. Homo sapiens.

Family and domain databases

InterPro

IPR000472. Activin_rcpt.
IPR015770. BMPRII.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]

PANTHER

PTHR23255:SF12. PTHR23255:SF12. 1 hit.

Pfam

PF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q13873.

ChEMBL

CHEMBL5467.

ChiTaRS

BMPR2. human.

EvolutionaryTrace

Q13873.

GenomeRNAi

659.

NextBio

2680.

SOURCE

Search...

Entry information

Entry name

BMPR2_HUMAN

Accession

Primary (citable) accession number: Q13873
Secondary accession number(s): Q16569 , Q4ZG08, Q53SA5, Q585T8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.