[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Prostate; DOI=10.1038/sj.onc.1200964; PubMed=9178898 [NCBI, ExPASy, EBI, Israel, Japan] Ide H., Katoh M., Sasaki H., Yoshida T., Aoki K., Nawa Y., Osada Y., Sugimura T., Terada M.; "Cloning of human bone morphogenetic protein type IB receptor (BMPR-IB) and its expression in prostate cancer in comparison with other BMPRs."; Oncogene 14:1377-1382(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Ovary; DOI=10.1007/s003359900990; PubMed=10051328 [NCBI, ExPASy, EBI, Israel, Japan] Astroem A.-K., Jin D.F., Imamura T., Roijer E., Rosenzweig B., Miyazono K., ten Dijke P., Stenman G.; "Chromosomal localization of three human genes encoding bone morphogenetic protein receptors."; Mamm. Genome 10:299-302(1999).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=PNS; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[4]	VARIANTS BDA2 LYS-200 AND TRP-486. DOI=10.1073/pnas.2133476100; PubMed=14523231 [NCBI, ExPASy, EBI, Israel, Japan] Lehmann K., Seemann P., Stricker S., Sammar M., Meyer B., Suering K., Majewski F., Tinschert S., Grzeschik K.-H., Mueller D., Knaus P., Nuernberg P., Mundlos S.; "Mutations in bone morphogenetic protein receptor 1B cause brachydactyly type A2."; Proc. Natl. Acad. Sci. U.S.A. 100:12277-12282(2003).
[5]	INVOLVEMENT IN ACROMESOMELIC CHONDRODYSPLASIA WITH GENITAL ANOMALIES. DOI=10.1136/jmg.2004.023564; PubMed=15805157 [NCBI, ExPASy, EBI, Israel, Japan] Demirhan O., Tuerkmen S., Schwabe G.C., Soyupak S., Akguel E., Tastemir D., Karahan D., Mundlos S., Lehmann K.; "A homozygous BMPR1B mutation causes a new subtype of acromesomelic chondrodysplasia with genital anomalies."; J. Med. Genet. 42:314-317(2005).
[6]	VARIANT BRACHYDACTYLY TYPE C/BDA2 GLN-486. DOI=10.1038/sj.ejhg.5201708; PubMed=16957682 [NCBI, ExPASy, EBI, Israel, Japan] Lehmann K., Seemann P., Boergermann J., Morin G., Reif S., Knaus P., Mundlos S.; "A novel R486Q mutation in BMPR1B resulting in either a brachydactyly type C/symphalangism-like phenotype or brachydactyly type A2."; Eur. J. Hum. Genet. 14:1248-1254(2006).
[7]	VARIANTS [LARGE SCALE ANALYSIS] HIS-31; TRP-149; HIS-224; ASN-297 AND GLN-371. DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan] 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).

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. Receptor for BMPS/OP-1.
CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
COFACTOR: Magnesium or manganese (By similarity).
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
DISEASE: Defects in BMPR1B are the cause of acromesomelic chondrodysplasia with genital anomalies [MIM:609441]. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs, and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers).
DISEASE: Defects in BMPR1B are a cause of brachydactyly type A2 (BDA2) [MIM:112600]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits. BDA2 was described first in a large Norwegian kindred. BDA2 is caused by mutations in BMPR1B gene and studies demonstrate that these mutations function as dominant negatives in vitro and in vivo.
SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.
SIMILARITY: Contains 1 GS domain.
SIMILARITY: Contains 1 protein kinase domain.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=BMPR1B";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D89675; BAA19765.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89326; AAC28131.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC047773; AAH47773.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069796; AAH69796.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069803; AAH69803.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001194.1; -.

UniGene

Hs.661426

3D structure databases

HSSP

P36897; 1IAS. [HSSP ENTRY / PDB]

ModBase

O00238.

Organism-specific databases

H-InvDB

HIX0024604; -.

HGNC

HGNC:1077; BMPR1B.

GeneLynx

BMPR1B; Homo sapiens.

GenAtlas

BMPR1B.

MIM

112600; phenotype. [NCBI / EBI]
603248; gene. [NCBI / EBI]
609441; phenotype. [NCBI / EBI]

Orphanet

69028; Brachydactyly.

PharmGKB

PA25387; -.

GeneCards

O00238.

Gene expression databases

ArrayExpress

O00238; -.

CleanEx

HS_BMPR1B; -.

GermOnline

ENSG00000138696; Homo sapiens.

Ontologies

GO:0005887;	Cellular component: integral to plasma membrane (inferred by curator from UniProtKB).
GO:0043235;	Cellular component: receptor complex (traceable author statement from UniProtKB).
GO:0005524;	Molecular function: ATP binding (inferred from direct assay from HGNC).
GO:0046332;	Molecular function: SMAD binding (inferred from direct assay from HGNC).
GO:0004675;	Molecular function: transmembrane receptor protein serine/threonine kinase activity (inferred from mutant phenotype from UniProtKB).
GO:0030509;	Biological process: BMP signaling pathway (non-traceable author statement from UniProtKB).
GO:0001502;	Biological process: cartilage condensation (non-traceable author statement from UniProtKB).
GO:0001654;	Biological process: eye development (inferred from sequence or structural similarity from UniProtKB).
GO:0035108;	Biological process: limb morphogenesis (inferred from mutant phenotype from UniProtKB).
GO:0001550;	Biological process: ovarian cumulus expansion (inferred from sequence or structural similarity from UniProtKB).
GO:0045597;	Biological process: positive regulation of cell differentiation (inferred from mutant phenotype from UniProtKB).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from direct assay from HGNC).
QuickGo view.

Family and domain databases

InterPro

IPR000333; Activin_II_recpt.
IPR000472; Activin_rcpt.
IPR000719; Prot_kinase_core.
IPR008271; Ser_thr_pkin_AS.
IPR003605; TGF_beta_rcpt_GS.
Graphical view of domain structure.

Pfam

PF01064; Activin_recp; 1.
PF08515; TGF_beta_GS; 1.
Pfam graphical view of domain structure.

PRINTS

PR00653; ACTIVIN2R.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00467; GS; 1.
SMART graphical view of domain structure.

PROSITE

PS51256; GS; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

O00238.

Genome annotation databases

Ensembl

ENSG00000138696; Homo sapiens. [Contig view]

GeneID

658; -.

KEGG

hsa:658; -.

Other

LinkHub

O00238; -.

SOURCE

BMPR1B; Homo sapiens.

ProtoNet

O00238.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Disease mutation; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Polymorphism; Receptor; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 13`	`13`	`Potential.`
`CHAIN`	`14 502`	`489`	`Bone morphogenetic protein receptor type-1B.`	`PRO_0000024412`
`TOPO_DOM`	`14 126`	`113`	`Extracellular (Potential).`
`TRANSMEM`	`127 148`	`22`	`Potential.`
`TOPO_DOM`	`149 502`	`354`	`Cytoplasmic (Potential).`
`DOMAIN`	`174 203`	`30`	`GS.`
`DOMAIN`	`204 494`	`291`	`Protein kinase.`
`NP_BIND`	`210 218`	`9`	`ATP (By similarity).`
`ACT_SITE`	`332 332`		`Proton acceptor (By similarity).`
`BINDING`	`231 231`		`ATP (By similarity).`
`VARIANT`	`31 31`	`1`	`R -> H (in a gastric adenocarcinoma sample; somatic mutation).`	`VAR_041401 [3D]`
`VARIANT`	`149 149`	`1`	`R -> W.`	`VAR_041402`
`VARIANT`	`200 200`	`1`	`I -> K (in BDA2).`	`VAR_023819`
`VARIANT`	`224 224`	`1`	`R -> H.`	`VAR_041403`
`VARIANT`	`297 297`	`1`	`D -> N (in a metastatic melanoma sample; somatic mutation).`	`VAR_041404`
`VARIANT`	`371 371`	`1`	`R -> Q.`	`VAR_041405`
`VARIANT`	`486 486`	`1`	`R -> Q (in brachydactyly type C and BDA2; with also additional features of symphalangism-1).`	`VAR_037967`
`VARIANT`	`486 486`	`1`	`R -> W (in BDA2).`	`VAR_023820`

Sequence information

Length: 502 AA [This is the length of the unprocessed precursor]

Molecular weight: 56930 Da [This is the MW of the unprocessed precursor]

CRC64: B283D9BF45535C79 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLLRSAGKLN VGTKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED 

        70         80         90        100        110        120 
DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD 

       130        140        150        160        170        180 
GPIHHRALLI SVTVCSLLLV LIILFCYFRY KRQETRPRYS IGLEQDETYI PPGESLRDLI 

       190        200        210        220        230        240 
EQSQSSGSGS GLPLLVQRTI AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS 

       250        260        270        280        290        300 
WFRETEIYQT VLMRHENILG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDAKS 

       310        320        330        340        350        360 
MLKLAYSSVS GLCHLHTEIF STQGKPAIAH RDLKSKNILV KKNGTCCIAD LGLAVKFISD 

       370        380        390        400        410        420 
TNEVDIPPNT RVGTKRYMPP EVLDESLNRN HFQSYIMADM YSFGLILWEV ARRCVSGGIV 

       430        440        450        460        470        480 
EEYQLPYHDL VPSDPSYEDM REIVCIKKLR PSFPNRWSSD ECLRQMGKLM TECWAHNPAS 

       490        500 
RLTALRVKKT LAKMSESQDI KL

O00238 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools