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Bone morphogenetic protein receptor type-2 (BMP type-2 receptor) (BMPR-2) (EC 2.7.11.30) (Bone morphogenetic protein receptor type II) (BMP type II receptor) (BMPR-II)

 BMPR2_HUMAN             Reviewed;        1038 AA.
Q13873; Q13161; Q16569; Q4ZG08; Q53SA5; Q585T8;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
17-JUN-2020, entry version 218.
RecName: Full=Bone morphogenetic protein receptor type-2;
Short=BMP type-2 receptor;
Short=BMPR-2;
EC=2.7.11.30;
AltName: Full=Bone morphogenetic protein receptor type II;
Short=BMP type II receptor;
Short=BMPR-II;
Flags: Precursor;
Name=BMPR2; Synonyms=PPH1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
TISSUE=Kidney;
PubMed=7791754; DOI=10.1128/mcb.15.7.3479;
Liu F., Ventura F., Doody J., Massague J.;
"Human type II receptor for bone morphogenic proteins (BMPs): extension of
the two-kinase receptor model to the BMPs.";
Mol. Cell. Biol. 15:3479-3486(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Substantia nigra;
PubMed=7644468; DOI=10.1073/pnas.92.17.7632;
Rosenzweig B.L., Imamura T., Okadome T., Cox G.N., Yamashita H.,
ten Dijke P., Heldin C., Miyazono K.;
"Cloning and characterization of a human type II receptor for bone
morphogenetic proteins.";
Proc. Natl. Acad. Sci. U.S.A. 92:7632-7636(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Skin fibroblast;
PubMed=7673243; DOI=10.1074/jbc.270.38.22522;
Nohno T., Ishikawa T., Saito T., Hosokawa K., Noji S., Wosing D.H.,
Rosenbaum J.S.;
"Identification of a human type II receptor for bone morphogenetic protein-
4 that forms differential heteromeric complexes with bone morphogenetic
protein type I receptors.";
J. Biol. Chem. 270:22522-22526(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7890683; DOI=10.1074/jbc.270.10.5625;
Kawabata M., Chytil A., Moses H.L.;
"Cloning of a novel type II serine/threonine kinase receptor through
interaction with the type I transforming growth factor-beta receptor.";
J. Biol. Chem. 270:5625-5630(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-379, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[10]
INTERACTION WITH GDF5.
PubMed=21976273; DOI=10.1002/jbmr.532;
Schwaerzer G.K., Hiepen C., Schrewe H., Nickel J., Ploeger F., Sebald W.,
Mueller T., Knaus P.;
"New insights into the molecular mechanism of multiple synostoses syndrome
(SYNS): mutation within the GDF5 knuckle epitope causes noggin-
resistance.";
J. Bone Miner. Res. 27:429-442(2012).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 33-131, AND DISULFIDE BONDS.
PubMed=17094948; DOI=10.1016/j.bbrc.2006.10.109;
Mace P.D., Cutfield J.F., Cutfield S.M.;
"High resolution structures of the bone morphogenetic protein type II
receptor in two crystal forms: implications for ligand binding.";
Biochem. Biophys. Res. Commun. 351:831-838(2006).
[13]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 189-517 IN COMPLEX WITH ADP.
Structural genomics consortium (SGC);
"Crystal structure of the BMPR2 kinase domain.";
Submitted (FEB-2009) to the PDB data bank.
[14]
VARIANTS PPH1 GLN-491 AND TRP-491.
PubMed=10903931; DOI=10.1086/303059;
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.;
"Familial primary pulmonary hypertension (gene PPH1) is caused by mutations
in the bone morphogenetic protein receptor-II gene.";
Am. J. Hum. Genet. 67:737-744(2000).
[15]
VARIANTS PPH1 TYR-60; TYR-117 AND ARG-483.
PubMed=11015450; DOI=10.1136/jmg.37.10.741;
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.;
"Sporadic primary pulmonary hypertension is associated with germline
mutations of the gene encoding BMPR-II, a receptor member of the TGF-beta
family.";
J. Med. Genet. 37:741-745(2000).
[16]
VARIANTS PPH1 TRP-118; TYR-347 AND GLY-485.
PubMed=10973254; DOI=10.1038/79226;
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.;
"Heterozygous germline mutations in BMPR2, encoding a TGF-beta receptor,
cause familial primary pulmonary hypertension.";
Nat. Genet. 26:81-84(2000).
[17]
VARIANTS PPH1 ARG-123; SER-123; ARG-420 AND THR-512, VARIANT ASP-224, AND
CHARACTERIZATION OF VARIANT PPH1 GLY-485.
PubMed=11115378; DOI=10.1086/316947;
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.;
"BMPR2 haploinsufficiency as the inherited molecular mechanism for primary
pulmonary hypertension.";
Am. J. Hum. Genet. 68:92-102(2001).
[18]
VARIANTS PPH1 HIS-82; ASP-182 AND ARG-483.
PubMed=12358323; DOI=10.1183/09031936.02.01762002;
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.;
"BMPR2 germline mutations in pulmonary hypertension associated with
fenfluramine derivatives.";
Eur. Respir. J. 20:518-523(2002).
[19]
INVOLVEMENT IN PVOD1.
PubMed=12446270; DOI=10.1164/rccm.200208-861oc;
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;
"Pulmonary veno-occlusive disease caused by an inherited mutation in bone
morphogenetic protein receptor II.";
Am. J. Respir. Crit. Care Med. 167:889-894(2003).
[20]
VARIANT PPH1 PRO-899, AND CHARACTERIZATION OF VARIANT PPH1 PRO-899.
PubMed=15965979; DOI=10.1002/humu.20200;
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.;
"BMPR2 mutations have short lifetime expectancy in primary pulmonary
hypertension.";
Hum. Mutat. 26:119-124(2005).
[21]
INVOLVEMENT IN PVOD1.
PubMed=16429395; DOI=10.1002/humu.20285;
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.;
"Mutations of the TGF-beta type II receptor BMPR2 in pulmonary arterial
hypertension.";
Hum. Mutat. 27:121-132(2006).
[22]
VARIANT [LARGE SCALE ANALYSIS] ASN-775.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[23]
VARIANTS PPH1 LEU-77; PHE-84; TYR-87; LEU-92; PRO-162; ASN-264 AND MET-341,
AND VARIANT ASN-775.
PubMed=24936649; DOI=10.1371/journal.pone.0100261;
Pousada G., Baloira A., Vilarino C., Cifrian J.M., Valverde D.;
"Novel mutations in BMPR2, ACVRL1 and KCNA5 genes and hemodynamic
parameters in patients with pulmonary arterial hypertension.";
PLoS ONE 9:E100261-E100261(2014).
[24]
VARIANTS PPH1 CYS-67 AND ASN-863, CHARACTERIZATION OF VARIANTS PPH1 CYS-67
AND ASN-863, AND SUBCELLULAR LOCATION.
PubMed=25187962; DOI=10.1371/journal.pone.0106703;
Wang H., Ji R., Meng J., Cui Q., Zou W., Li L., Wang G., Sun L., Li Z.,
Huo L., Fan Y., Penny D.J.;
"Functional changes in pulmonary arterial endothelial cells associated with
BMPR2 mutations.";
PLoS ONE 9:E106703-E106703(2014).
[25]
VARIANTS PPH1 ARG-64; PHE-84; HIS-109; ALA-138; 218-TYR--LEU-1038 DEL;
GLY-248; 298-TRP--LEU-1038 DEL AND ARG-467, CHARACTERIZATION OF VARIANTS
PPH1 ARG-64; LEU-77; TYR-87; LEU-92; HIS-109; ALA-138; PRO-162;
218-TYR--LEU-1038 DEL; GLY-248; ASN-264; 298-TRP--LEU-1038 DEL; MET-341 AND
ARG-467, AND CHARACTERIZATION OF VARIANT ASN-775.
PubMed=28507310; DOI=10.1038/s41598-017-02074-8;
Pousada G., Lupo V., Castro-Sanchez S., Alvarez-Satta M.,
Sanchez-Monteagudo A., Baloira A., Espinos C., Valverde D.;
"Molecular and functional characterization of the BMPR2 gene in Pulmonary
Arterial Hypertension.";
Sci. Rep. 7:1923-1923(2017).
-!- 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 BMP7, BMP2 and, less efficiently, BMP4. Binding is
weak but enhanced by the presence of type I receptors for BMPs.
Mediates induction of adipogenesis by GDF6.
{ECO:0000250|UniProtKB:O35607}.
-!- CATALYTIC ACTIVITY:
Reaction=[receptor-protein]-L-threonine + ATP = [receptor-protein]-O-
phospho-L-threonine + ADP + H(+); Xref=Rhea:RHEA:44880, Rhea:RHEA-
COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
ChEBI:CHEBI:456216; EC=2.7.11.30;
-!- CATALYTIC ACTIVITY:
Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
ChEBI:CHEBI:456216; EC=2.7.11.30;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with GDF5. {ECO:0000269|PubMed:21976273}.
-!- INTERACTION:
Q13873; P43026: GDF5; NbExp=4; IntAct=EBI-527196, EBI-8571476;
Q13873; Q13976: PRKG1; NbExp=2; IntAct=EBI-527196, EBI-3952014;
Q13873; P08607: C4bpa; Xeno; NbExp=3; IntAct=EBI-527196, EBI-527325;
Q13873; P68404: Prkcb; Xeno; NbExp=4; IntAct=EBI-527196, EBI-397048;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25187962};
Single-pass type I membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13873-1; Sequence=Displayed;
Name=2;
IsoId=Q13873-2; Sequence=VSP_054441, VSP_054442;
-!- TISSUE SPECIFICITY: Highly expressed in heart and liver.
-!- 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. {ECO:0000269|PubMed:10903931, ECO:0000269|PubMed:10973254,
ECO:0000269|PubMed:11015450, ECO:0000269|PubMed:11115378,
ECO:0000269|PubMed:12358323, ECO:0000269|PubMed:15965979,
ECO:0000269|PubMed:24936649, ECO:0000269|PubMed:25187962,
ECO:0000269|PubMed:28507310}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: 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. {ECO:0000269|PubMed:12446270,
ECO:0000269|PubMed:16429395}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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EMBL; U25110; AAA86519.1; -; mRNA.
EMBL; Z48923; CAA88759.1; -; mRNA.
EMBL; D50516; BAA09094.1; -; mRNA.
EMBL; U20165; AAC50105.1; -; mRNA.
EMBL; AC009960; AAX76517.1; -; Genomic_DNA.
EMBL; AC073410; AAX88941.1; -; Genomic_DNA.
EMBL; AC064836; AAY24146.1; -; Genomic_DNA.
EMBL; CH471063; EAW70309.1; -; Genomic_DNA.
EMBL; BC052985; AAH52985.1; -; mRNA.
CCDS; CCDS33361.1; -. [Q13873-1]
PIR; I38935; I38935.
RefSeq; NP_001195.2; NM_001204.6. [Q13873-1]
PDB; 2HLQ; X-ray; 1.45 A; A=33-131.
PDB; 3G2F; X-ray; 2.35 A; A/B=189-517.
PDBsum; 2HLQ; -.
PDBsum; 3G2F; -.
SMR; Q13873; -.
BioGRID; 107127; 68.
DIP; DIP-5794N; -.
ELM; Q13873; -.
IntAct; Q13873; 44.
MINT; Q13873; -.
STRING; 9606.ENSP00000363708; -.
BindingDB; Q13873; -.
ChEMBL; CHEMBL5467; -.
DrugBank; DB11639; Dibotermin alfa.
DrugBank; DB12010; Fostamatinib.
DrugCentral; Q13873; -.
GuidetoPHARMACOLOGY; 1794; -.
GlyConnect; 1046; -.
iPTMnet; Q13873; -.
PhosphoSitePlus; Q13873; -.
BioMuta; BMPR2; -.
DMDM; 12643724; -.
CPTAC; CPTAC-2209; -.
EPD; Q13873; -.
jPOST; Q13873; -.
MassIVE; Q13873; -.
MaxQB; Q13873; -.
PaxDb; Q13873; -.
PeptideAtlas; Q13873; -.
PRIDE; Q13873; -.
ProteomicsDB; 59705; -. [Q13873-1]
Antibodypedia; 19946; 505 antibodies.
DNASU; 659; -.
Ensembl; ENST00000374574; ENSP00000363702; ENSG00000204217. [Q13873-2]
Ensembl; ENST00000374580; ENSP00000363708; ENSG00000204217. [Q13873-1]
GeneID; 659; -.
KEGG; hsa:659; -.
UCSC; uc002uzf.5; human. [Q13873-1]
CTD; 659; -.
DisGeNET; 659; -.
EuPathDB; HostDB:ENSG00000204217.12; -.
GeneCards; BMPR2; -.
GeneReviews; BMPR2; -.
HGNC; HGNC:1078; BMPR2.
HPA; ENSG00000204217; Low tissue specificity.
MalaCards; BMPR2; -.
MIM; 178600; phenotype.
MIM; 265450; phenotype.
MIM; 600799; gene.
neXtProt; NX_Q13873; -.
OpenTargets; ENSG00000204217; -.
Orphanet; 275786; Drug- or toxin-induced pulmonary arterial hypertension.
Orphanet; 275777; Heritable pulmonary arterial hypertension.
Orphanet; 31837; Pulmonary venoocclusive disease.
PharmGKB; PA25388; -.
eggNOG; KOG3653; Eukaryota.
eggNOG; ENOG410XS2Z; LUCA.
GeneTree; ENSGT00940000156449; -.
HOGENOM; CLU_013015_0_0_1; -.
InParanoid; Q13873; -.
KO; K04671; -.
OMA; IPLMEHD; -.
OrthoDB; 390511at2759; -.
PhylomeDB; Q13873; -.
TreeFam; TF314724; -.
Reactome; R-HSA-201451; Signaling by BMP.
SignaLink; Q13873; -.
SIGNOR; Q13873; -.
BioGRID-ORCS; 659; 8 hits in 817 CRISPR screens.
ChiTaRS; BMPR2; human.
EvolutionaryTrace; Q13873; -.
GeneWiki; BMPR2; -.
GenomeRNAi; 659; -.
Pharos; Q13873; Tchem.
PRO; PR:Q13873; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; Q13873; protein.
Bgee; ENSG00000204217; Expressed in upper lobe of lung and 219 other tissues.
ExpressionAtlas; Q13873; baseline and differential.
Genevisible; Q13873; HS.
GO; GO:0005912; C:adherens junction; IDA:BHF-UCL.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0044214; C:spanning component of plasma membrane; TAS:AgBase.
GO; GO:0016362; F:activin receptor activity, type II; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0036122; F:BMP binding; IPI:UniProtKB.
GO; GO:0098821; F:BMP receptor activity; ISS:UniProtKB.
GO; GO:0045296; F:cadherin binding; IPI:ARUK-UCL.
GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL.
GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IBA:GO_Central.
GO; GO:0009952; P:anterior/posterior pattern specification; ISS:BHF-UCL.
GO; GO:0003176; P:aortic valve development; ISS:BHF-UCL.
GO; GO:0060840; P:artery development; ISS:BHF-UCL.
GO; GO:0060413; P:atrial septum morphogenesis; ISS:BHF-UCL.
GO; GO:0001568; P:blood vessel development; IBA:GO_Central.
GO; GO:0001974; P:blood vessel remodeling; ISS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL.
GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
GO; GO:0009267; P:cellular response to starvation; IEP:BHF-UCL.
GO; GO:0002063; P:chondrocyte development; IMP:AgBase.
GO; GO:0003197; P:endocardial cushion development; ISS:BHF-UCL.
GO; GO:0060350; P:endochondral bone morphogenesis; ISS:AgBase.
GO; GO:0072577; P:endothelial cell apoptotic process; IMP:UniProtKB.
GO; GO:0001935; P:endothelial cell proliferation; IMP:UniProtKB.
GO; GO:0060173; P:limb development; IEA:Ensembl.
GO; GO:0048286; P:lung alveolus development; ISS:BHF-UCL.
GO; GO:0001946; P:lymphangiogenesis; ISS:BHF-UCL.
GO; GO:0060836; P:lymphatic endothelial cell differentiation; ISS:BHF-UCL.
GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
GO; GO:0001707; P:mesoderm formation; ISS:BHF-UCL.
GO; GO:0003183; P:mitral valve morphogenesis; ISS:BHF-UCL.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0003252; P:negative regulation of cell proliferation involved in heart valve morphogenesis; ISS:BHF-UCL.
GO; GO:1902731; P:negative regulation of chondrocyte proliferation; IMP:AgBase.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:BHF-UCL.
GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:BHF-UCL.
GO; GO:0045906; P:negative regulation of vasoconstriction; ISS:BHF-UCL.
GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL.
GO; GO:0061626; P:pharyngeal arch artery morphogenesis; ISS:BHF-UCL.
GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IEA:Ensembl.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:UniProtKB.
GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
GO; GO:0061036; P:positive regulation of cartilage development; ISS:AgBase.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IDA:UniProtKB.
GO; GO:0045778; P:positive regulation of ossification; ISS:BHF-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:AgBase.
GO; GO:0003177; P:pulmonary valve development; ISS:BHF-UCL.
GO; GO:0042127; P:regulation of cell population proliferation; IMP:HGNC-UCL.
GO; GO:0014916; P:regulation of lung blood pressure; IMP:BHF-UCL.
GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:BHF-UCL.
GO; GO:1905314; P:semi-lunar valve development; ISS:BHF-UCL.
GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IDA:BHF-UCL.
GO; GO:0003186; P:tricuspid valve morphogenesis; ISS:BHF-UCL.
GO; GO:0001944; P:vasculature development; IBA:GO_Central.
GO; GO:0060841; P:venous blood vessel development; ISS:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
InterPro; IPR000472; Activin_recp.
InterPro; IPR015770; BMPR2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
PANTHER; PTHR23255:SF63; PTHR23255:SF63; 1.
Pfam; PF01064; Activin_recp; 1.
Pfam; PF00069; Pkinase; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Disease mutation; Disulfide bond; Glycoprotein; Kinase; Magnesium;
Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Polymorphism; Receptor; Reference proteome;
Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
Transmembrane helix.
SIGNAL 1..26
/evidence="ECO:0000255"
CHAIN 27..1038
/note="Bone morphogenetic protein receptor type-2"
/id="PRO_0000024415"
TOPO_DOM 27..150
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 151..171
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 172..1038
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 203..504
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 209..217
/note="ATP"
/evidence="ECO:0000305|Ref.13"
NP_BIND 280..282
/note="ATP"
/evidence="ECO:0000305|Ref.13"
NP_BIND 337..338
/note="ATP"
/evidence="ECO:0000305|Ref.13"
COMPBIAS 547..550
/note="Poly-Ser"
COMPBIAS 610..618
/note="Poly-Thr"
COMPBIAS 901..908
/note="Poly-Asn"
ACT_SITE 333
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 230
/note="ATP"
/evidence="ECO:0000305|Ref.13"
BINDING 351
/note="ATP"
/evidence="ECO:0000305|Ref.13"
MOD_RES 379
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:19369195"
MOD_RES 586
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18691976"
MOD_RES 680
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O35607"
MOD_RES 681
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O35607"
CARBOHYD 55
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 110
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 126
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 34..66
/evidence="ECO:0000244|PDB:2HLQ,
ECO:0000269|PubMed:17094948"
DISULFID 60..84
/evidence="ECO:0000244|PDB:2HLQ,
ECO:0000269|PubMed:17094948"
DISULFID 94..117
/evidence="ECO:0000244|PDB:2HLQ,
ECO:0000269|PubMed:17094948"
DISULFID 99..116
/evidence="ECO:0000244|PDB:2HLQ,
ECO:0000269|PubMed:17094948"
DISULFID 118..123
/evidence="ECO:0000244|PDB:2HLQ,
ECO:0000269|PubMed:17094948"
VAR_SEQ 530
/note="N -> R (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7791754"
/id="VSP_054441"
VAR_SEQ 531..1038
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7791754"
/id="VSP_054442"
VARIANT 60
/note="C -> Y (in PPH1; dbSNP:rs1085307172)"
/evidence="ECO:0000269|PubMed:11015450"
/id="VAR_013670"
VARIANT 64
/note="S -> R (in PPH1; unknown pathological significance;
unchanged subcellular localization)"
/evidence="ECO:0000269|PubMed:28507310"
/id="VAR_079588"
VARIANT 67
/note="Y -> C (in PPH1; significant decrease in nitric
oxide synthesis by endothelial cells; dbSNP:rs1085307177)"
/evidence="ECO:0000269|PubMed:25187962"
/id="VAR_073041"
VARIANT 77
/note="I -> L (in PPH1; unknown pathological significance;
unchanged subcellular localization)"
/evidence="ECO:0000269|PubMed:24936649,
ECO:0000269|PubMed:28507310"
/id="VAR_079589"
VARIANT 82
/note="Q -> H (in PPH1; dbSNP:rs1085307185)"
/evidence="ECO:0000269|PubMed:12358323"
/id="VAR_033109"
VARIANT 84
/note="C -> F (in PPH1; alters alternative splicing of
BMPR2; dbSNP:rs1085307197)"
/evidence="ECO:0000269|PubMed:24936649,
ECO:0000269|PubMed:28507310"
/id="VAR_079590"
VARIANT 87
/note="H -> Y (in PPH1; unknown pathological significance;
unchanged subcellular localization)"
/evidence="ECO:0000269|PubMed:24936649,
ECO:0000269|PubMed:28507310"
/id="VAR_079591"
VARIANT 92
/note="Q -> L (in PPH1; unknown pathological significance;
unchanged subcellular localization)"
/evidence="ECO:0000269|PubMed:24936649,
ECO:0000269|PubMed:28507310"
/id="VAR_079592"
VARIANT 109
/note="Q -> H (in PPH1; unknown pathological significance;
unchanged subcellular localization)"
/evidence="ECO:0000269|PubMed:28507310"
/id="VAR_079593"
VARIANT 117
/note="C -> Y (in PPH1; dbSNP:rs1085307215)"
/evidence="ECO:0000269|PubMed:11015450"
/id="VAR_013671"
VARIANT 118
/note="C -> W (in PPH1; dbSNP:rs137852743)"
/evidence="ECO:0000269|PubMed:10973254"
/id="VAR_013672"
VARIANT 123
/note="C -> R (in PPH1; dbSNP:rs137852750)"
/evidence="ECO:0000269|PubMed:11115378"
/id="VAR_013673"
VARIANT 123
/note="C -> S (in PPH1; dbSNP:rs137852750)"
/evidence="ECO:0000269|PubMed:11115378"
/id="VAR_013674"
VARIANT 138
/note="P -> A (in PPH1; unknown pathological significance;
unchanged subcellular localization)"
/evidence="ECO:0000269|PubMed:28507310"
/id="VAR_079594"
VARIANT 162
/note="A -> P (in PPH1; unknown pathological significance;
unchanged subcellular localization)"
/evidence="ECO:0000269|PubMed:24936649,
ECO:0000269|PubMed:28507310"
/id="VAR_079595"
VARIANT 182
/note="G -> D (in PPH1; dbSNP:rs137852754)"
/evidence="ECO:0000269|PubMed:12358323"
/id="VAR_033110"
VARIANT 218..1038
/note="Missing (in PPH1; changed localization to the plasma
membrane)"
/evidence="ECO:0000269|PubMed:28507310"
/id="VAR_079596"
VARIANT 224
/note="E -> D (in dbSNP:rs754343081)"
/evidence="ECO:0000269|PubMed:11115378"
/id="VAR_013675"
VARIANT 248
/note="R -> G (in PPH1; unknown pathological significance;
unchanged subcellular localization)"
/evidence="ECO:0000269|PubMed:28507310"
/id="VAR_079597"
VARIANT 264
/note="D -> N (in PPH1; unknown pathological significance;
unchanged subcellular localization)"
/evidence="ECO:0000269|PubMed:24936649,
ECO:0000269|PubMed:28507310"
/id="VAR_079598"
VARIANT 298..1038
/note="Missing (in PPH1; loss of localization to the plasma
membrane; localized to the cytoplasm)"
/evidence="ECO:0000269|PubMed:28507310"
/id="VAR_079599"
VARIANT 341
/note="V -> M (in PPH1; unknown pathological significance;
unchanged subcellular localization; dbSNP:rs767882551)"
/evidence="ECO:0000269|PubMed:24936649,
ECO:0000269|PubMed:28507310"
/id="VAR_079600"
VARIANT 347
/note="C -> Y (in PPH1; dbSNP:rs137852744)"
/evidence="ECO:0000269|PubMed:10973254"
/id="VAR_013676"
VARIANT 420
/note="C -> R (in PPH1; dbSNP:rs1085307324)"
/evidence="ECO:0000269|PubMed:11115378"
/id="VAR_013677"
VARIANT 467
/note="K -> R (in PPH1; unknown pathological significance;
unchanged subcellular localization)"
/evidence="ECO:0000269|PubMed:28507310"
/id="VAR_079601"
VARIANT 483
/note="C -> R (in PPH1; sporadic; dbSNP:rs1085307354)"
/evidence="ECO:0000269|PubMed:11015450,
ECO:0000269|PubMed:12358323"
/id="VAR_013678"
VARIANT 485
/note="D -> G (in PPH1; complete loss of function;
dbSNP:rs137852745)"
/evidence="ECO:0000269|PubMed:10973254,
ECO:0000269|PubMed:11115378"
/id="VAR_013679"
VARIANT 491
/note="R -> Q (in PPH1; sporadic; dbSNP:rs137852749)"
/evidence="ECO:0000269|PubMed:10903931"
/id="VAR_013680"
VARIANT 491
/note="R -> W (in PPH1; dbSNP:rs137852746)"
/evidence="ECO:0000269|PubMed:10903931"
/id="VAR_013681"
VARIANT 512
/note="K -> T (in PPH1; dbSNP:rs1085307364)"
/evidence="ECO:0000269|PubMed:11115378"
/id="VAR_013682"
VARIANT 519
/note="N -> K (in PPH1; dbSNP:rs1085307365)"
/id="VAR_013683"
VARIANT 775
/note="S -> N (polymorphism; unchanged subcellular
localization; dbSNP:rs2228545)"
/evidence="ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:24936649, ECO:0000269|PubMed:28507310"
/id="VAR_019996"
VARIANT 863
/note="S -> N (in PPH1; abnormal subcellular localization;
significant increase in apoptosis of endothelial cells;
significant decrease in proliferation of endothelial cells;
significant decrease in nitric oxide synthesis by
endothelial cells; significant increase in endothelin 1
synthesis by endothelial cells; dbSNP:rs1006246556)"
/evidence="ECO:0000269|PubMed:25187962"
/id="VAR_073042"
VARIANT 899
/note="R -> P (in PPH1; leads to constitutive activation of
the MAPK14 pathway; dbSNP:rs137852752)"
/evidence="ECO:0000269|PubMed:15965979"
/id="VAR_033111"
CONFLICT 828
/note="G -> R (in Ref. 2; CAA88759)"
/evidence="ECO:0000305"
STRAND 33..35
/evidence="ECO:0000244|PDB:2HLQ"
TURN 42..47
/evidence="ECO:0000244|PDB:2HLQ"
HELIX 48..50
/evidence="ECO:0000244|PDB:2HLQ"
TURN 53..56
/evidence="ECO:0000244|PDB:2HLQ"
STRAND 57..59
/evidence="ECO:0000244|PDB:2HLQ"
STRAND 66..73
/evidence="ECO:0000244|PDB:2HLQ"
STRAND 76..84
/evidence="ECO:0000244|PDB:2HLQ"
STRAND 90..92
/evidence="ECO:0000244|PDB:2HLQ"
TURN 105..109
/evidence="ECO:0000244|PDB:2HLQ"
STRAND 113..118
/evidence="ECO:0000244|PDB:2HLQ"
HELIX 123..125
/evidence="ECO:0000244|PDB:2HLQ"
STRAND 202..211
/evidence="ECO:0000244|PDB:3G2F"
STRAND 213..222
/evidence="ECO:0000244|PDB:3G2F"
STRAND 225..233
/evidence="ECO:0000244|PDB:3G2F"
HELIX 234..236
/evidence="ECO:0000244|PDB:3G2F"
HELIX 237..247
/evidence="ECO:0000244|PDB:3G2F"
STRAND 260..267
/evidence="ECO:0000244|PDB:3G2F"
STRAND 273..279
/evidence="ECO:0000244|PDB:3G2F"
HELIX 287..293
/evidence="ECO:0000244|PDB:3G2F"
HELIX 298..316
/evidence="ECO:0000244|PDB:3G2F"
HELIX 322..324
/evidence="ECO:0000244|PDB:3G2F"
STRAND 338..341
/evidence="ECO:0000244|PDB:3G2F"
STRAND 347..349
/evidence="ECO:0000244|PDB:3G2F"
STRAND 359..362
/evidence="ECO:0000244|PDB:3G2F"
HELIX 380..382
/evidence="ECO:0000244|PDB:3G2F"
HELIX 385..388
/evidence="ECO:0000244|PDB:3G2F"
HELIX 394..396
/evidence="ECO:0000244|PDB:3G2F"
HELIX 397..417
/evidence="ECO:0000244|PDB:3G2F"
HELIX 421..423
/evidence="ECO:0000244|PDB:3G2F"
HELIX 437..440
/evidence="ECO:0000244|PDB:3G2F"
HELIX 446..453
/evidence="ECO:0000244|PDB:3G2F"
HELIX 471..483
/evidence="ECO:0000244|PDB:3G2F"
HELIX 488..490
/evidence="ECO:0000244|PDB:3G2F"
HELIX 494..506
/evidence="ECO:0000244|PDB:3G2F"
SEQUENCE 1038 AA; 115201 MW; 1389923CE574B913 CRC64;
MTSSLQRPWR VPWLPWTILL VSTAAASQNQ ERLCAFKDPY QQDLGIGESR ISHENGTILC
SKGSTCYGLW EKSKGDINLV KQGCWSHIGD PQECHYEECV VTTTPPSIQN GTYRFCCCST
DLCNVNFTEN FPPPDTTPLS PPHSFNRDET IIIALASVSV LAVLIVALCF GYRMLTGDRK
QGLHSMNMME AAASEPSLDL DNLKLLELIG RGRYGAVYKG SLDERPVAVK VFSFANRQNF
INEKNIYRVP LMEHDNIARF IVGDERVTAD GRMEYLLVME YYPNGSLCKY LSLHTSDWVS
SCRLAHSVTR GLAYLHTELP RGDHYKPAIS HRDLNSRNVL VKNDGTCVIS DFGLSMRLTG
NRLVRPGEED NAAISEVGTI RYMAPEVLEG AVNLRDCESA LKQVDMYALG LIYWEIFMRC
TDLFPGESVP EYQMAFQTEV GNHPTFEDMQ VLVSREKQRP KFPEAWKENS LAVRSLKETI
EDCWDQDAEA RLTAQCAEER MAELMMIWER NKSVSPTVNP MSTAMQNERN LSHNRRVPKI
GPYPDYSSSS YIEDSIHHTD SIVKNISSEH SMSSTPLTIG EKNRNSINYE RQQAQARIPS
PETSVTSLST NTTTTNTTGL TPSTGMTTIS EMPYPDETNL HTTNVAQSIG PTPVCLQLTE
EDLETNKLDP KEVDKNLKES SDENLMEHSL KQFSGPDPLS STSSSLLYPL IKLAVEATGQ
QDFTQTANGQ ACLIPDVLPT QIYPLPKQQN LPKRPTSLPL NTKNSTKEPR LKFGSKHKSN
LKQVETGVAK MNTINAAEPH VVTVTMNGVA GRNHSVNSHA ATTQYANGTV LSGQTTNIVT
HRAQEMLQNQ FIGEDTRLNI NSSPDEHEPL LRREQQAGHD EGVLDRLVDR RERPLEGGRT
NSNNNNSNPC SEQDVLAQGV PSTAADPGPS KPRRAQRPNS LDLSATNVLD GSSIQIGEST
QDGKSGSGEK IKKRVKTPYS LKRWRPSTWV ISTESLDCEV NNNGSNRAVH SKSSTAVYLA
EGGTATTMVS KDIGMNCL


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E0015m ELISA Activin receptor-like kinase 3,Acvrlk3,ALK-3,BMP type-1A receptor,BMP-2_BMP-4 receptor,Bmpr,Bmpr1a,BMPR-1A,Bone morphogenetic protein receptor type-1A,Mouse,Mus musculus,Serine_threonine-protein 96T
E0015r ELISA kit Activin receptor-like kinase 3,ALK-3,BMP type-1A receptor,Bmpr1a,BMPR-1A,Bone morphogenetic protein 4 receptor,Bone morphogenetic protein receptor type-1A,Rat,Rattus norvegicus 96T
U0015r CLIA Activin receptor-like kinase 3,ALK-3,BMP type-1A receptor,Bmpr1a,BMPR-1A,Bone morphogenetic protein 4 receptor,Bone morphogenetic protein receptor type-1A,Rat,Rattus norvegicus 96T
E0015r ELISA Activin receptor-like kinase 3,ALK-3,BMP type-1A receptor,Bmpr1a,BMPR-1A,Bone morphogenetic protein 4 receptor,Bone morphogenetic protein receptor type-1A,Rat,Rattus norvegicus 96T
E0015h ELISA kit Activin receptor-like kinase 3,ACVRLK3,ALK3,ALK-3,BMP type-1A receptor,BMPR1A,BMPR-1A,Bone morphogenetic protein receptor type-1A,Homo sapiens,Human,Serine_threonine-protein kinase receptor 96T
E0015h ELISA Activin receptor-like kinase 3,ACVRLK3,ALK3,ALK-3,BMP type-1A receptor,BMPR1A,BMPR-1A,Bone morphogenetic protein receptor type-1A,Homo sapiens,Human,Serine_threonine-protein kinase receptor R5,S 96T
U0015h CLIA Activin receptor-like kinase 3,ACVRLK3,ALK3,ALK-3,BMP type-1A receptor,BMPR1A,BMPR-1A,Bone morphogenetic protein receptor type-1A,Homo sapiens,Human,Serine_threonine-protein kinase receptor R5,SK 96T
C303 Bone Morphogenetic Protein Receptor Type II BMPR-II 500
C303 Bone Morphogenetic Protein Receptor Type II BMPR-II lmg
C303 Human Bone Morphogenetic Protein Receptor Type II BMPR-II l0
CD59 Human Bone Morphogenetic Protein Receptor Type II BMPR-II 50
CSB-E04517r Rat Bone morphogenetic protein receptor Ⅱ,BMPR-Ⅱ ELISA Kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL002748RA Rat Bone morphogenetic protein receptor 1A,BMPR-1A ELISA Kit, Species Rat, Sample Type serum, plasma 96T
18-272-195260 BMPR2 - Goat polyclonal to BMPR2; EC 2.7.11.30; Bone morphogenetic protein receptor type II; BMP type II receptor; BMPR-II Polyclonal 0.05 mg
CSB-EL002748MO Mouse Bone morphogenetic protein receptor 1A,BMPR-1A ELISA Kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL002748HU Human Bone morphogenetic protein receptor 1A,BMPR-1A ELISA Kit, Species Human, Sample Type serum, plasma 96T
CSB-EL002752HU Human Bone morphogenetic protein receptor Ⅱ,BMPR-Ⅱ ELISA Kit, Species Human, Sample Type serum, plasma 96T
Pathways :
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP1354: B Cell Receptor Signaling Pathway
WP23: B Cell Receptor Signaling Pathway
WP733: Serotonin Receptor 2 and STAT3 Signaling
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP362: TGF-beta Receptor Signaling Pathway
WP894: T Cell Receptor Signaling Pathway
WP1004: Kit Receptor Signaling Pathway
WP474: Endochondral Ossification
WP908: B Cell Receptor Signaling Pathway
WP1017: Type II interferon signaling (IFNG)
WP138: Androgen receptor signaling pathway
WP2328: Allograft rejection
WP768: EPO Receptor Signaling
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP252: Androgen Receptor Signaling Pathway
WP783: Androgen Receptor Signaling Pathway
WP1253: Type II interferon signaling (IFNG)
WP566: canonical wnt - zebrafish
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1449: Regulation of toll-like receptor signaling pathway
WP2140: MaxYvesSuperCombo
WP585: Interferon type I
WP996: EPO Receptor Signaling

Related Genes :
[BMPR2 PPH1] Bone morphogenetic protein receptor type-2 (BMP type-2 receptor) (BMPR-2) (EC 2.7.11.30) (Bone morphogenetic protein receptor type II) (BMP type II receptor) (BMPR-II)
[BMPR1A ACVRLK3 ALK3] Bone morphogenetic protein receptor type-1A (BMP type-1A receptor) (BMPR-1A) (EC 2.7.11.30) (Activin receptor-like kinase 3) (ALK-3) (Serine/threonine-protein kinase receptor R5) (SKR5) (CD antigen CD292)
[BMPR1B] Bone morphogenetic protein receptor type-1B (BMP type-1B receptor) (BMPR-1B) (EC 2.7.11.30) (CD antigen CDw293)
[BMP2 BMP2A] Bone morphogenetic protein 2 (BMP-2) (Bone morphogenetic protein 2A) (BMP-2A)
[BMP4 BMP2B DVR4] Bone morphogenetic protein 4 (BMP-4) (Bone morphogenetic protein 2B) (BMP-2B)
[GDF5 BMP14 CDMP1] Growth/differentiation factor 5 (GDF-5) (Bone morphogenetic protein 14) (BMP-14) (Cartilage-derived morphogenetic protein 1) (CDMP-1) (Lipopolysaccharide-associated protein 4) (LAP-4) (LPS-associated protein 4) (Radotermin)
[ACVR1 ACVRLK2] Activin receptor type-1 (EC 2.7.11.30) (Activin receptor type I) (ACTR-I) (Activin receptor-like kinase 2) (ALK-2) (Serine/threonine-protein kinase receptor R1) (SKR1) (TGF-B superfamily receptor type I) (TSR-I)
[GDF6 BMP13 GDF16] Growth/differentiation factor 6 (GDF-6) (Bone morphogenetic protein 13) (BMP-13) (Growth/differentiation factor 16)
[BMP7 OP1] Bone morphogenetic protein 7 (BMP-7) (Osteogenic protein 1) (OP-1) (Eptotermin alfa)
[botA atx bna bonT CLM_0897] Botulinum neurotoxin type A2 (BoNT/A) (Bontoxilysin-A) (BOTOX) [Cleaved into: Botulinum neurotoxin A2 light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin A2 heavy chain (HC)]
[Hjv Hfe2 Rgmc] Hemojuvelin (Hemochromatosis type 2 protein homolog) (Hemojuvelin BMP coreceptor) (RGM domain family member C)
[ACVR2B] Activin receptor type-2B (EC 2.7.11.30) (Activin receptor type IIB) (ACTR-IIB)
[Acvr2b Actriib] Activin receptor type-2B (EC 2.7.11.30) (Activin receptor type IIB) (ACTR-IIB)
[Acvr2b] Activin receptor type-2B (EC 2.7.11.30) (Activin receptor type IIB) (ACTR-IIB)
[Bmp8b] Bone morphogenetic protein 8B (BMP-8B)
[BMP15 GDF9B] Bone morphogenetic protein 15 (BMP-15) (Growth/differentiation factor 9B) (GDF-9B)
[ZMYND11 BRAM1 BS69] Zinc finger MYND domain-containing protein 11 (Adenovirus 5 E1A-binding protein) (Bone morphogenetic protein receptor-associated molecule 1) (Protein BS69)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[SORL1 C11orf32] Sortilin-related receptor (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (SorLA-1) (Sorting protein-related receptor containing LDLR class A repeats) (SorLA)
[Sorl1] Sortilin-related receptor (Gp250) (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (SorLA-1) (Sorting protein-related receptor containing LDLR class A repeats) (mSorLA)
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Sorl1] Sortilin-related receptor (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (Sorting protein-related receptor containing LDLR class A repeats) (SorLA)
[SORL1] Sortilin-related receptor (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (SorLA-1) (Sorting protein-related receptor containing LDLR class A repeats) (SorLA)
[TGFBR2] TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II)
[acr-2 K11G12.2] Acetylcholine receptor subunit beta-type acr-2
[Traf2] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

Bibliography :