Bone morphogenetic protein receptor type-1B precursor

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Reviewed, UniProtKB/Swiss-Prot O00238 (BMR1B_HUMAN)

Last modified July 22, 2008. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Bone morphogenetic protein receptor type-1B
    EC=2.7.11.30
Alternative name(s):
    CD_antigen=CDw293

Gene names

Name:

BMPR1B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	502 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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. 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.
Involvement in 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). 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.
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily. Contains 1 GS domain. Contains 1 protein kinase domain.

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Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal Transmembrane
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
Gene Ontology (GO)
Biological process	BMP signaling pathway Ref.2 Non-traceable author statement. Source: UniProtKB cartilage condensation Ref.4 Non-traceable author statement. Source: UniProtKB eye development Inferred from sequence or structural similarity. Source: UniProtKB limb morphogenesis Ref.4 Inferred from mutant phenotype. Source: UniProtKB ovarian cumulus expansion Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of bone mineralization Inferred from mutant phenotype. Source: UniProtKB positive regulation of osteoblast differentiation Inferred from mutant phenotype. Source: UniProtKB protein amino acid phosphorylation Inferred from direct assay. Source: HGNC
Cellular component	integral to plasma membrane Ref.4 Inferred by curator. Source: UniProtKB receptor complex Ref.4 Traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from direct assay. Source: HGNC SMAD binding Inferred from direct assay. Source: HGNC transmembrane receptor protein serine/threonine kinase activity Ref.2 Ref.4 Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 13

Potential

Chain

14 – 502

489

Bone morphogenetic protein receptor type-1B

Regions

Topological domain

14 – 126

113

Extracellular Potential

Transmembrane

127 – 148

Potential

Topological domain

149 – 502

354

Cytoplasmic Potential

Domain

174 – 203

Domain

204 – 494

291

Protein kinase

Nucleotide binding

210 – 218

ATP By similarity

Sites

Active site

332

Proton acceptor By similarity

Binding site

231

ATP By similarity

Natural variations

Natural variant

R → H in a gastric adenocarcinoma sample; somatic mutation.

Natural variant

149

R → W

Natural variant

200

I → K in BDA2.

Natural variant

224

R → H

Natural variant

297

D → N in a metastatic melanoma sample; somatic mutation.

Natural variant

371

R → Q

Natural variant

486

R → Q in brachydactyly type C and BDA2; with also additional features of symphalangism-1.

Natural variant

486

R → W in BDA2.

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Sequences

Sequence

Length

Mass (Da)

Tools

O00238-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: B283D9BF45535C79
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FASTA

502

56,930

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human bone morphogenetic protein type IB receptor (BMPR-IB) and its expression in prostate cancer in comparison with other BMPRs." Ide H., Katoh M., Sasaki H., Yoshida T., Aoki K., Nawa Y., Osada Y., Sugimura T., Terada M. Oncogene 14:1377-1382(1997) [PubMed: 9178898] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Prostate.
[2]	"Chromosomal localization of three human genes encoding bone morphogenetic protein receptors." Astroem A.-K., Jin D.F., Imamura T., Roijer E., Rosenzweig B., Miyazono K., ten Dijke P., Stenman G. Mamm. Genome 10:299-302(1999) [PubMed: 10051328] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: PNS.
[4]	"Mutations in bone morphogenetic protein receptor 1B cause brachydactyly type A2." 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. Proc. Natl. Acad. Sci. U.S.A. 100:12277-12282(2003) [PubMed: 14523231] [Abstract] Cited for: VARIANTS BDA2 LYS-200 AND TRP-486.
[5]	"A homozygous BMPR1B mutation causes a new subtype of acromesomelic chondrodysplasia with genital anomalies." Demirhan O., Tuerkmen S., Schwabe G.C., Soyupak S., Akguel E., Tastemir D., Karahan D., Mundlos S., Lehmann K. J. Med. Genet. 42:314-317(2005) [PubMed: 15805157] [Abstract] Cited for: INVOLVEMENT IN ACROMESOMELIC CHONDRODYSPLASIA WITH GENITAL ANOMALIES.
[6]	"A novel R486Q mutation in BMPR1B resulting in either a brachydactyly type C/symphalangism-like phenotype or brachydactyly type A2." Lehmann K., Seemann P., Boergermann J., Morin G., Reif S., Knaus P., Mundlos S. Eur. J. Hum. Genet. 14:1248-1254(2006) [PubMed: 16957682] [Abstract] Cited for: VARIANT BRACHYDACTYLY TYPE C/BDA2 GLN-486.
[7]	"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. Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-31; TRP-149; HIS-224; ASN-297 AND GLN-371.

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Web resources

GeneReviews

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Cross-references

Sequence databases
	D89675 mRNA. Translation: BAA19765.1. U89326 mRNA. Translation: AAC28131.1. BC047773 mRNA. Translation: AAH47773.1. BC069796 mRNA. Translation: AAH69796.1. BC069803 mRNA. Translation: AAH69803.1.
RefSeq	NP_001194.1.
UniGene	Hs.661426
3D structure databases
HSSP	HSSP built from PDB template 1IAS based on UniProtKB P36897.
ModBase	Search...
Genome annotation databases
Ensembl	ENSG00000138696. Homo sapiens. [Contig view]
GeneID	658.
KEGG	hsa:658.
Organism-specific databases
H-InvDB	HIX0024604.
HGNC	HGNC:1077. BMPR1B.
HPA	CAB009634.
MIM	112600. phenotype. 603248. gene. 609441. phenotype.
Orphanet	69028. Brachydactyly.
PharmGKB	PA25387.
GenAtlas	Search...
GeneCards	Search...
GeneLynx	Search...
Phylogenomic databases
HOGENOM	O00238.
HOVERGEN	O00238.
Gene expression databases
ArrayExpress	O00238.
CleanEx	HS_BMPR1B.
GermOnline	ENSG00000138696. Homo sapiens.
Family and domain databases
InterPro	IPR000333. Activin_II_recpt. IPR000472. Activin_rcpt. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR003605. TGF_beta_rcpt_GS. [Graphical view]
Pfam	PF01064. Activin_recp. 1 hit. PF00069. Pkinase. 1 hit. PF08515. TGF_beta_GS. 1 hit. [Graphical view]
PRINTS	PR00653. ACTIVIN2R.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00467. GS. 1 hit. [Graphical view]
PROSITE	PS51256. GS. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
BLOCKS	Search...
Other Resources
LinkHub	O00238.
SOURCE	Search...
ProtoNet	Search...

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Entry information

Entry name

BMR1B_HUMAN

Accession

Primary (citable) accession number: O00238
Secondary accession number(s): P78366

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 1, 1997
Last modified:	July 22, 2008
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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