O00238 (BMR1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bone morphogenetic protein receptor type-1B
Short name=BMP type-1B receptor
Short name=BMPR-1B
EC=2.7.11.30

Alternative name(s):
CD_antigen=CDw293

Gene names

Name:

BMPR1B

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	502 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. Receptor for BMP7/OP-1 and GDF5.
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	Acromesomelic chondrodysplasia, with genital anomalies (AMDGA) [MIM:609441]: A form of chondrodysplasia. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbsand 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). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Brachydactyly A2 (BDA2) [MIM:112600]: A form of brachydactyly. Brachydactyly defines a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. In brachydactyly type A2 shortening of the middle phalanges is confined to the index finger and the second toe, all other digits being more or less normal. Because of a rhomboid or triangular shape of the affected middle phalanx, the end of the second finger usually deviates radially. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7
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.

Ontologies

Keywords
Biological process	Chondrogenesis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Dwarfism
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
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Non-traceable author statement Ref.2. Source: UniProtKB cartilage condensation Non-traceable author statement Ref.7. Source: UniProtKB dorsal/ventral pattern formation Inferred from electronic annotation. Source: Compara eye development Inferred from sequence or structural similarity. Source: UniProtKB inflammatory response Inferred from electronic annotation. Source: Compara limb morphogenesis Inferred from mutant phenotype Ref.7. Source: UniProtKB ovarian cumulus expansion Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of bone mineralization Inferred from mutant phenotype PubMed 18436533. Source: BHF-UCL positive regulation of osteoblast differentiation Inferred from mutant phenotype PubMed 18436533. Source: BHF-UCL retina development in camera-type eye Inferred from electronic annotation. Source: Compara retinal ganglion cell axon guidance Inferred from electronic annotation. Source: Compara signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	integral to plasma membrane Inferred by curator Ref.7. Source: UniProtKB receptor complex Traceable author statement Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay PubMed 12065756. Source: HGNC SMAD binding Inferred from direct assay PubMed 12065756. Source: HGNC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor signaling protein serine/threonine kinase activity Inferred from electronic annotation. Source: InterPro transforming growth factor beta receptor activity, type I Inferred from electronic annotation. Source: Compara transmembrane receptor protein serine/threonine kinase activity Inferred from mutant phenotype Ref.7. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O00238-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O00238-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGWLEELNWQLHIFLLILLSMHTRANFLDNM

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 13

13

Potential

Chain

14 – 502

489

Bone morphogenetic protein receptor type-1B

PRO_0000024412

Regions

Topological domain

14 – 126

113

Extracellular Potential

Transmembrane

127 – 148

22

Helical; Potential

Topological domain

149 – 502

354

Cytoplasmic Potential

Domain

174 – 203

30

GS

Domain

204 – 494

291

Protein kinase

Nucleotide binding

210 – 218

9

ATP By similarity

Sites

Active site

332

1

Proton acceptor By similarity

Binding site

231

1

ATP By similarity

Amino acid modifications

Disulfide bond

32 ↔ 53

By similarity

Disulfide bond

34 ↔ 38

By similarity

Disulfide bond

47 ↔ 71

By similarity

Disulfide bond

81 ↔ 95

By similarity

Disulfide bond

96 ↔ 102

By similarity

Natural variations

Alternative sequence

1

1

M → MGWLEELNWQLHIFLLILLS MHTRANFLDNM in isoform 2.

VSP_045100

Natural variant

31

1

R → H in a gastric adenocarcinoma sample; somatic mutation. Ref.10

VAR_041401

Natural variant

149

1

R → W. Ref.10
Corresponds to variant rs34231464 [ dbSNP | Ensembl ].

VAR_041402

Natural variant

200

1

I → K in BDA2. Ref.7
Corresponds to variant rs28939703 [ dbSNP | Ensembl ].

VAR_023819

Natural variant

224

1

R → H. Ref.10
Corresponds to variant rs35973133 [ dbSNP | Ensembl ].

VAR_041403

Natural variant

297

1

D → N in a metastatic melanoma sample; somatic mutation. Ref.10

VAR_041404

Natural variant

371

1

R → Q. Ref.10
Corresponds to variant rs34970181 [ dbSNP | Ensembl ].

VAR_041405

Natural variant

486

1

R → Q in brachydactyly type C and BDA2; with also additional features of symphalangism-1. Ref.9

VAR_037967

Natural variant

486

1

R → W in BDA2. Ref.7
Corresponds to variant rs28939704 [ dbSNP | Ensembl ].

VAR_023820

Secondary structure

1

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502

Helix Strand Turn

Details...

Helix

176 – 186

11

Beta strand

190 – 192

3

Helix

194 – 197

4

Helix

200 – 203

4

Beta strand

205 – 213

9

Beta strand

216 – 223

8

Beta strand

226 – 234

9

Helix

235 – 237

3

Helix

238 – 248

11

Beta strand

261 – 268

8

Helix

270 – 272

3

Beta strand

274 – 279

6

Helix

287 – 293

7

Helix

298 – 316

19

Beta strand

337 – 340

4

Beta strand

346 – 348

3

Helix

375 – 377

3

Helix

380 – 383

4

Helix

393 – 411

19

Turn

426 – 430

5

Helix

437 – 444

8

Helix

455 – 459

5

Helix

461 – 473

13

Helix

478 – 480

3

Helix

484 – 496

13

Turn

497 – 499

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: B283D9BF45535C79	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
	Isoform 2 [UniParc]. Checksum: 5DF28FF01C96D541	FASTA	532	60,582
	10 20 30 40 50 60 MGWLEELNWQ LHIFLLILLS MHTRANFLDN MLLRSAGKLN VGTKKEDGES TAPTPRPKVL 70 80 90 100 110 120 RCKCHHHCPE DSVNNICSTD GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR 130 140 150 160 170 180 RSIECCTERN ECNKDLHPTL PPLKNRDFVD GPIHHRALLI SVTVCSLLLV LIILFCYFRY 190 200 210 220 230 240 KRQETRPRYS IGLEQDETYI PPGESLRDLI EQSQSSGSGS GLPLLVQRTI AKQIQMVKQI 250 260 270 280 290 300 GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS WFRETEIYQT VLMRHENILG FIAADIKGTG 310 320 330 340 350 360 SWTQLYLITD YHENGSLYDY LKSTTLDAKS MLKLAYSSVS GLCHLHTEIF STQGKPAIAH 370 380 390 400 410 420 RDLKSKNILV KKNGTCCIAD LGLAVKFISD TNEVDIPPNT RVGTKRYMPP EVLDESLNRN 430 440 450 460 470 480 HFQSYIMADM YSFGLILWEV ARRCVSGGIV EEYQLPYHDL VPSDPSYEDM REIVCIKKLR 490 500 510 520 530 PSFPNRWSSD ECLRQMGKLM TECWAHNPAS RLTALRVKKT LAKMSESQDI KL

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Ovary.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain and Uterus.
[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]	Mural R.J., Istrail S., Sutton G.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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORM 1). Tissue: PNS.
[7]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS BDA2 LYS-200 AND TRP-486.
[8]	"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] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN AMDGA.
[9]	"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] [Europe PMC] [Abstract] Cited for: VARIANT BRACHYDACTYLY TYPE C/BDA2 GLN-486.
[10]	"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: VARIANTS [LARGE SCALE ANALYSIS] HIS-31; TRP-149; HIS-224; ASN-297 AND GLN-371.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D89675 mRNA. Translation: BAA19765.1.
U89326 mRNA. Translation: AAC28131.1.
AK299930 mRNA. Translation: BAG61763.1.
AK313642 mRNA. Translation: BAG36400.1.
AC004061 Genomic DNA. No translation available.
AC092609 Genomic DNA. No translation available.
AC093634 Genomic DNA. No translation available.
AC105395 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06060.1.
BC047773 mRNA. Translation: AAH47773.1.
BC069796 mRNA. Translation: AAH69796.1.
BC069803 mRNA. Translation: AAH69803.1.

IPI

IPI00939250.

RefSeq

NP_001194.1. NM_001203.2.
NP_001243721.1. NM_001256792.1.
NP_001243722.1. NM_001256793.1.
NP_001243723.1. NM_001256794.1.

UniGene

Hs.598475.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MDY	X-ray	2.05	A/C	168-502	[»]

ProteinModelPortal

O00238.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1340235.

STRING

9606.ENSP00000264568.

PTM databases

PhosphoSite

O00238.

Proteomic databases

PaxDb

O00238.

PRIDE

O00238.

Protocols and materials databases

DNASU

658.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264568; ENSP00000264568; ENSG00000138696.
ENST00000394931; ENSP00000378389; ENSG00000138696.
ENST00000440890; ENSP00000401907; ENSG00000138696.
ENST00000509540; ENSP00000421671; ENSG00000138696.
ENST00000512312; ENSP00000425444; ENSG00000138696.
ENST00000515059; ENSP00000426617; ENSG00000138696.

GeneID

658.

KEGG

hsa:658.

UCSC

uc003htm.4. human.

Organism-specific databases

CTD

658.

GeneCards

GC04P095679.

HGNC

HGNC:1077. BMPR1B.

HPA

CAB009634.

MIM

112600. phenotype.
603248. gene.
609441. phenotype.

neXtProt

NX_O00238.

Orphanet

93396. Brachydactyly type A2.
93384. Brachydactyly type C.

PharmGKB

PA25387.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000230587.

HOVERGEN

HBG054502.

InParanoid

O00238.

KO

K13578.

OMA

DGPIHHK.

PhylomeDB

O00238.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

bmppathway. BMP receptor signaling.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

O00238.

Bgee

O00238.

CleanEx

HS_BMPR1B.

Genevestigator

O00238.

GermOnline

ENSG00000138696. Homo sapiens.

Family and domain databases

InterPro

IPR000333. Activin_II/TGFBeta-II_recpt.
IPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_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.

SMART

SM00467. GS. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

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]

ProtoNet

Search...

Other

BindingDB

O00238.

ChEMBL

CHEMBL5476.

ChiTaRS

BMPR1B. human.

EvolutionaryTrace

O00238.

GenomeRNAi

658.

NextBio

2676.

SOURCE

Search...

Entry information

Entry name

BMR1B_HUMAN

Accession

Primary (citable) accession number: O00238
Secondary accession number(s): B2R953, B4DSV1, P78366

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 141 of the entry and version 1 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.