ID BMR1B_HUMAN Reviewed; 502 AA. AC O00238; B2R953; B4DSV1; P78366; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 13-FEB-2019, entry version 198. DE RecName: Full=Bone morphogenetic protein receptor type-1B; DE Short=BMP type-1B receptor; DE Short=BMPR-1B; DE EC=2.7.11.30; DE AltName: CD_antigen=CDw293; DE Flags: Precursor; GN Name=BMPR1B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Prostate; RX PubMed=9178898; DOI=10.1038/sj.onc.1200964; RA Ide H., Katoh M., Sasaki H., Yoshida T., Aoki K., Nawa Y., Osada Y., RA Sugimura T., Terada M.; RT "Cloning of human bone morphogenetic protein type IB receptor (BMPR- RT IB) and its expression in prostate cancer in comparison with other RT BMPRs."; RL Oncogene 14:1377-1382(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Ovary; RX PubMed=10051328; DOI=10.1007/s003359900990; RA Astroem A.-K., Jin D.F., Imamura T., Roijer E., Rosenzweig B., RA Miyazono K., ten Dijke P., Stenman G.; RT "Chromosomal localization of three human genes encoding bone RT morphogenetic protein receptors."; RL Mamm. Genome 10:299-302(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=PNS; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INTERACTION WITH GDF5. RX PubMed=24098149; DOI=10.1371/journal.pgen.1003846; RA Degenkolbe E., Konig J., Zimmer J., Walther M., Reissner C., RA Nickel J., Ploger F., Raspopovic J., Sharpe J., Dathe K., Hecht J.T., RA Mundlos S., Doelken S.C., Seemann P.; RT "A GDF5 point mutation strikes twice--causing BDA1 and SYNS2."; RL PLoS Genet. 9:E1003846-E1003846(2013). RN [8] RP VARIANTS BDA2 LYS-200 AND TRP-486. RX PubMed=14523231; DOI=10.1073/pnas.2133476100; RA Lehmann K., Seemann P., Stricker S., Sammar M., Meyer B., Suering K., RA Majewski F., Tinschert S., Grzeschik K.-H., Mueller D., Knaus P., RA Nuernberg P., Mundlos S.; RT "Mutations in bone morphogenetic protein receptor 1B cause RT brachydactyly type A2."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12277-12282(2003). RN [9] RP INVOLVEMENT IN AMDD. RX PubMed=15805157; DOI=10.1136/jmg.2004.023564; RA Demirhan O., Tuerkmen S., Schwabe G.C., Soyupak S., Akguel E., RA Tastemir D., Karahan D., Mundlos S., Lehmann K.; RT "A homozygous BMPR1B mutation causes a new subtype of acromesomelic RT chondrodysplasia with genital anomalies."; RL J. Med. Genet. 42:314-317(2005). RN [10] RP VARIANT BRACHYDACTYLY TYPE C/BDA2 GLN-486. RX PubMed=16957682; DOI=10.1038/sj.ejhg.5201708; RA Lehmann K., Seemann P., Boergermann J., Morin G., Reif S., Knaus P., RA Mundlos S.; RT "A novel R486Q mutation in BMPR1B resulting in either a brachydactyly RT type C/symphalangism-like phenotype or brachydactyly type A2."; RL Eur. J. Hum. Genet. 14:1248-1254(2006). RN [11] RP VARIANTS [LARGE SCALE ANALYSIS] HIS-31; TRP-149; HIS-224; ASN-297 AND RP GLN-371. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). RN [12] RP VARIANT AMDD ARG-53, AND CHARACTERIZATION OF VARIANT AMDD ARG-53. RX PubMed=24129431; DOI=10.1038/ejhg.2013.222; RA Graul-Neumann L.M., Deichsel A., Wille U., Kakar N., Koll R., RA Bassir C., Ahmad J., Cormier-Daire V., Mundlos S., Kubisch C., RA Borck G., Klopocki E., Mueller T.D., Doelken S.C., Seemann P.; RT "Homozygous missense and nonsense mutations in BMPR1B cause RT acromesomelic chondrodysplasia-type Grebe."; RL Eur. J. Hum. Genet. 22:726-733(2014). RN [13] RP INVOLVEMENT IN BDA1D, VARIANT BDA1D ASN-325, AND CHARACTERIZATION OF RP VARIANT BDA1D ASN-325. RX PubMed=25758993; DOI=10.1038/ejhg.2015.38; RA Racacho L., Byrnes A.M., MacDonald H., Dranse H.J., Nikkel S.M., RA Allanson J., Rosser E., Underhill T.M., Bulman D.E.; RT "Two novel disease-causing variants in BMPR1B are associated with RT brachydactyly type A1."; RL Eur. J. Hum. Genet. 23:1640-1645(2015). RN [14] RP VARIANT AMDD CYS-31, AND CHARACTERIZATION OF VARIANT AMDD CYS-31. RX PubMed=26105076; DOI=10.1186/s13023-015-0299-5; RA Stange K., Desir J., Kakar N., Mueller T.D., Budde B.S., Gordon C.T., RA Horn D., Seemann P., Borck G.; RT "A hypomorphic BMPR1B mutation causes du Pan acromesomelic RT dysplasia."; RL Orphanet J. Rare Dis. 10:84-84(2015). CC -!- FUNCTION: On ligand binding, forms a receptor complex consisting CC of two type II and two type I transmembrane serine/threonine CC kinases. Type II receptors phosphorylate and activate type I CC receptors which autophosphorylate, then bind and activate SMAD CC transcriptional regulators. Receptor for BMP7/OP-1 and GDF5. CC Positively regulates chondrocyte differentiation through GDF5 CC interaction. {ECO:0000250|UniProtKB:P36898}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[receptor-protein]-L-threonine + ATP = [receptor- CC protein]-O-phospho-L-threonine + ADP + H(+); CC Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA- CC COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.30; CC -!- CATALYTIC ACTIVITY: CC Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O- CC phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA- CC COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, CC ChEBI:CHEBI:456216; EC=2.7.11.30; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- SUBUNIT: Interacts with high affinity with GDF5; positively CC regulates chondrocyte differentiation. CC {ECO:0000269|PubMed:24098149}. CC -!- INTERACTION: CC P12643:BMP2; NbExp=3; IntAct=EBI-7527193, EBI-1029262; CC P43026:GDF5; NbExp=7; IntAct=EBI-7527193, EBI-8571476; CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000250|UniProtKB:P36898}. Membrane; Single-pass type I CC membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O00238-1; Sequence=Displayed; CC Name=2; CC IsoId=O00238-2; Sequence=VSP_045100; CC -!- DISEASE: Acromesomelic dysplasia, Demirhan type (AMDD) CC [MIM:609441]: A form of chondrodysplasia. Acromesomelic CC chondrodysplasias are rare hereditary skeletal disorders CC characterized by short stature, very short limbs and hand/foot CC malformations. The severity of limb abnormalities increases from CC proximal to distal with profoundly affected hands and feet showing CC brachydactyly and/or rudimentary fingers (knob-like fingers). AMDD CC inheritance is autosomal recessive. {ECO:0000269|PubMed:15805157, CC ECO:0000269|PubMed:24129431, ECO:0000269|PubMed:26105076}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: Brachydactyly A2 (BDA2) [MIM:112600]: A form of CC brachydactyly. Brachydactyly defines a group of inherited CC malformations characterized by shortening of the digits due to CC abnormal development of the phalanges and/or the metacarpals. In CC brachydactyly type A2 shortening of the middle phalanges is CC confined to the index finger and the second toe, all other digits CC being more or less normal. Because of a rhomboid or triangular CC shape of the affected middle phalanx, the end of the second finger CC usually deviates radially. {ECO:0000269|PubMed:14523231, CC ECO:0000269|PubMed:16957682}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Brachydactyly A1, D (BDA1D) [MIM:616849]: A form of CC brachydactyly type A1. Brachydactyly defines a group of inherited CC malformations characterized by shortening of the digits due to CC abnormal development of the phalanges and/or the metacarpals. CC Brachydactyly type A1 is characterized by middle phalanges of all CC the digits rudimentary or fused with the terminal phalanges. The CC proximal phalanges of the thumbs and big toes are short. BDA1D CC inheritance is autosomal dominant. {ECO:0000269|PubMed:25758993}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; D89675; BAA19765.1; -; mRNA. DR EMBL; U89326; AAC28131.1; -; mRNA. DR EMBL; AK299930; BAG61763.1; -; mRNA. DR EMBL; AK313642; BAG36400.1; -; mRNA. DR EMBL; AC004061; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092609; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093634; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105395; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471057; EAX06060.1; -; Genomic_DNA. DR EMBL; BC047773; AAH47773.1; -; mRNA. DR EMBL; BC069796; AAH69796.1; -; mRNA. DR EMBL; BC069803; AAH69803.1; -; mRNA. DR CCDS; CCDS3642.1; -. [O00238-1] DR CCDS; CCDS58919.1; -. [O00238-2] DR RefSeq; NP_001194.1; NM_001203.2. [O00238-1] DR RefSeq; NP_001243721.1; NM_001256792.1. [O00238-1] DR RefSeq; NP_001243722.1; NM_001256793.1. [O00238-2] DR RefSeq; NP_001243723.1; NM_001256794.1. [O00238-1] DR RefSeq; XP_011530503.1; XM_011532201.2. [O00238-1] DR RefSeq; XP_016864047.1; XM_017008558.1. [O00238-1] DR RefSeq; XP_016864048.1; XM_017008559.1. [O00238-1] DR RefSeq; XP_016864049.1; XM_017008560.1. [O00238-1] DR RefSeq; XP_016864050.1; XM_017008561.1. [O00238-1] DR UniGene; Hs.598475; -. DR PDB; 3MDY; X-ray; 2.05 A; A/C=168-502. DR PDBsum; 3MDY; -. DR ProteinModelPortal; O00238; -. DR SMR; O00238; -. DR BioGrid; 107126; 72. DR IntAct; O00238; 3. DR MINT; O00238; -. DR STRING; 9606.ENSP00000264568; -. DR BindingDB; O00238; -. DR ChEMBL; CHEMBL5476; -. DR GuidetoPHARMACOLOGY; 1789; -. DR iPTMnet; O00238; -. DR PhosphoSitePlus; O00238; -. DR BioMuta; BMPR1B; -. DR EPD; O00238; -. DR jPOST; O00238; -. DR MaxQB; O00238; -. DR PaxDb; O00238; -. DR PeptideAtlas; O00238; -. DR PRIDE; O00238; -. DR ProteomicsDB; 47802; -. DR DNASU; 658; -. DR Ensembl; ENST00000264568; ENSP00000264568; ENSG00000138696. [O00238-1] DR Ensembl; ENST00000394931; ENSP00000378389; ENSG00000138696. [O00238-1] DR Ensembl; ENST00000440890; ENSP00000401907; ENSG00000138696. [O00238-2] DR Ensembl; ENST00000509540; ENSP00000421671; ENSG00000138696. [O00238-1] DR Ensembl; ENST00000512312; ENSP00000425444; ENSG00000138696. [O00238-1] DR Ensembl; ENST00000515059; ENSP00000426617; ENSG00000138696. [O00238-1] DR GeneID; 658; -. DR KEGG; hsa:658; -. DR UCSC; uc003htm.5; human. [O00238-1] DR CTD; 658; -. DR DisGeNET; 658; -. DR EuPathDB; HostDB:ENSG00000138696.10; -. DR GeneCards; BMPR1B; -. DR GeneReviews; BMPR1B; -. DR HGNC; HGNC:1077; BMPR1B. DR MalaCards; BMPR1B; -. DR MIM; 112600; phenotype. DR MIM; 603248; gene. DR MIM; 609441; phenotype. DR MIM; 616849; phenotype. DR neXtProt; NX_O00238; -. DR OpenTargets; ENSG00000138696; -. DR Orphanet; 2098; Acromesomelic dysplasia, Grebe type. DR Orphanet; 93388; Brachydactyly type A1. DR Orphanet; 93396; Brachydactyly type A2. DR Orphanet; 93384; Brachydactyly type C. DR Orphanet; 2639; Fibular aplasia-complex brachydactyly syndrome. DR PharmGKB; PA25387; -. DR eggNOG; KOG2052; Eukaryota. DR eggNOG; ENOG410XQT0; LUCA. DR GeneTree; ENSGT00940000155919; -. DR HOGENOM; HOG000230587; -. DR HOVERGEN; HBG054502; -. DR InParanoid; O00238; -. DR KO; K13578; -. DR OMA; LMMECWA; -. DR OrthoDB; 776697at2759; -. DR PhylomeDB; O00238; -. DR TreeFam; TF314724; -. DR BRENDA; 2.7.10.2; 2681. DR Reactome; R-HSA-201451; Signaling by BMP. DR SignaLink; O00238; -. DR SIGNOR; O00238; -. DR ChiTaRS; BMPR1B; human. DR EvolutionaryTrace; O00238; -. DR GeneWiki; BMPR1B; -. DR GenomeRNAi; 658; -. DR PRO; PR:O00238; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000138696; Expressed in 175 organ(s), highest expression level in metanephros. DR ExpressionAtlas; O00238; baseline and differential. DR Genevisible; O00238; HS. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:1990712; C:HFE-transferrin receptor complex; IC:BHF-UCL. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IDA:HGNC. DR GO; GO:0019838; F:growth factor binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC. DR GO; GO:0046332; F:SMAD binding; IDA:HGNC. DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IBA:GO_Central. DR GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IBA:GO_Central. DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IMP:UniProtKB. DR GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL. DR GO; GO:0001502; P:cartilage condensation; NAS:UniProtKB. DR GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL. DR GO; GO:0002063; P:chondrocyte development; ISS:AgBase. DR GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl. DR GO; GO:0060350; P:endochondral bone morphogenesis; ISS:AgBase. DR GO; GO:0001654; P:eye development; ISS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl. DR GO; GO:0035108; P:limb morphogenesis; IMP:UniProtKB. DR GO; GO:1902731; P:negative regulation of chondrocyte proliferation; ISS:AgBase. DR GO; GO:0001550; P:ovarian cumulus expansion; ISS:UniProtKB. DR GO; GO:0042698; P:ovulation cycle; ISS:UniProtKB. DR GO; GO:0007389; P:pattern specification process; IBA:GO_Central. DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL. DR GO; GO:0061036; P:positive regulation of cartilage development; ISS:AgBase. DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB. DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISS:UniProtKB. DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0006468; P:protein phosphorylation; IDA:HGNC. DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:AgBase. DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl. DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl. DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central. DR InterPro; IPR000472; Activin_recp. DR InterPro; IPR003605; GS_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR000333; TGFB_receptor. DR PANTHER; PTHR23255; PTHR23255; 1. DR Pfam; PF01064; Activin_recp; 1. DR Pfam; PF07714; Pkinase_Tyr; 1. DR Pfam; PF08515; TGF_beta_GS; 1. DR PRINTS; PR00653; ACTIVIN2R. DR SMART; SM00467; GS; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS51256; GS; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; KW Chondrogenesis; Complete proteome; Disease mutation; Disulfide bond; KW Dwarfism; Kinase; Magnesium; Manganese; Membrane; Metal-binding; KW Nucleotide-binding; Polymorphism; Receptor; Reference proteome; KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 13 {ECO:0000255}. FT CHAIN 14 502 Bone morphogenetic protein receptor type- FT 1B. FT /FTId=PRO_0000024412. FT TOPO_DOM 14 126 Extracellular. {ECO:0000255}. FT TRANSMEM 127 148 Helical. {ECO:0000255}. FT TOPO_DOM 149 502 Cytoplasmic. {ECO:0000255}. FT DOMAIN 174 203 GS. {ECO:0000255|PROSITE- FT ProRule:PRU00585}. FT DOMAIN 204 494 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 210 218 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 332 332 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 231 231 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT DISULFID 32 53 {ECO:0000250|UniProtKB:P36898}. FT DISULFID 34 38 {ECO:0000250|UniProtKB:P36898}. FT DISULFID 47 71 {ECO:0000250|UniProtKB:P36898}. FT DISULFID 81 95 {ECO:0000250|UniProtKB:P36898}. FT DISULFID 96 102 {ECO:0000250|UniProtKB:P36898}. FT VAR_SEQ 1 1 M -> MGWLEELNWQLHIFLLILLSMHTRANFLDNM (in FT isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_045100. FT VARIANT 31 31 R -> C (in AMDD; unknown pathological FT significance; mouse BMPR1B construct FT containing this mutation shows reduced FT GDF5-dependent receptor activation, mouse FT BMPR1B construct containing this mutation FT shows no loss of cell membrane FT localization; dbSNP:rs745854387). FT {ECO:0000269|PubMed:26105076}. FT /FTId=VAR_075520. FT VARIANT 31 31 R -> H (in a gastric adenocarcinoma FT sample; somatic mutation; FT dbSNP:rs200035802). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041401. FT VARIANT 53 53 C -> R (in AMDD; mouse BMPR1B construct FT containing this mutation shows loss of FT GDF5-dependent receptor activation, FT chicken BMPR1B construct containing this FT mutation does not show reduced FT chondrocyte differentiation, mouse BMPR1B FT construct containing this mutation shows FT no loss of cell membrane localization; FT dbSNP:rs863225041). FT {ECO:0000269|PubMed:24129431}. FT /FTId=VAR_075521. FT VARIANT 149 149 R -> W (in dbSNP:rs34231464). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041402. FT VARIANT 200 200 I -> K (in BDA2; dbSNP:rs121434417). FT {ECO:0000269|PubMed:14523231}. FT /FTId=VAR_023819. FT VARIANT 224 224 R -> H (in dbSNP:rs35973133). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041403. FT VARIANT 297 297 D -> N (in a metastatic melanoma sample; FT somatic mutation). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041404. FT VARIANT 325 325 K -> N (in BDA1D; acts in a dominant- FT negative manner; dbSNP:rs869025614). FT {ECO:0000269|PubMed:25758993}. FT /FTId=VAR_076406. FT VARIANT 371 371 R -> Q (in dbSNP:rs34970181). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041405. FT VARIANT 486 486 R -> Q (in brachydactyly type C and BDA2; FT with also additional features of FT symphalangism-1; dbSNP:rs121434419). FT {ECO:0000269|PubMed:16957682}. FT /FTId=VAR_037967. FT VARIANT 486 486 R -> W (in BDA2; dbSNP:rs121434418). FT {ECO:0000269|PubMed:14523231}. FT /FTId=VAR_023820. FT HELIX 176 186 {ECO:0000244|PDB:3MDY}. FT STRAND 190 192 {ECO:0000244|PDB:3MDY}. FT HELIX 194 197 {ECO:0000244|PDB:3MDY}. FT HELIX 200 203 {ECO:0000244|PDB:3MDY}. FT STRAND 205 213 {ECO:0000244|PDB:3MDY}. FT STRAND 216 223 {ECO:0000244|PDB:3MDY}. FT STRAND 226 234 {ECO:0000244|PDB:3MDY}. FT HELIX 235 237 {ECO:0000244|PDB:3MDY}. FT HELIX 238 248 {ECO:0000244|PDB:3MDY}. FT STRAND 261 268 {ECO:0000244|PDB:3MDY}. FT HELIX 270 272 {ECO:0000244|PDB:3MDY}. FT STRAND 274 279 {ECO:0000244|PDB:3MDY}. FT HELIX 287 293 {ECO:0000244|PDB:3MDY}. FT HELIX 298 316 {ECO:0000244|PDB:3MDY}. FT STRAND 337 340 {ECO:0000244|PDB:3MDY}. FT STRAND 346 348 {ECO:0000244|PDB:3MDY}. FT HELIX 375 377 {ECO:0000244|PDB:3MDY}. FT HELIX 380 383 {ECO:0000244|PDB:3MDY}. FT HELIX 393 411 {ECO:0000244|PDB:3MDY}. FT TURN 426 430 {ECO:0000244|PDB:3MDY}. FT HELIX 437 444 {ECO:0000244|PDB:3MDY}. FT HELIX 455 459 {ECO:0000244|PDB:3MDY}. FT HELIX 461 473 {ECO:0000244|PDB:3MDY}. FT HELIX 478 480 {ECO:0000244|PDB:3MDY}. FT HELIX 484 496 {ECO:0000244|PDB:3MDY}. FT TURN 497 499 {ECO:0000244|PDB:3MDY}. SQ SEQUENCE 502 AA; 56930 MW; B283D9BF45535C79 CRC64; MLLRSAGKLN VGTKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD GPIHHRALLI SVTVCSLLLV LIILFCYFRY KRQETRPRYS IGLEQDETYI PPGESLRDLI EQSQSSGSGS GLPLLVQRTI AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS WFRETEIYQT VLMRHENILG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDAKS MLKLAYSSVS GLCHLHTEIF STQGKPAIAH RDLKSKNILV KKNGTCCIAD LGLAVKFISD TNEVDIPPNT RVGTKRYMPP EVLDESLNRN HFQSYIMADM YSFGLILWEV ARRCVSGGIV EEYQLPYHDL VPSDPSYEDM REIVCIKKLR PSFPNRWSSD ECLRQMGKLM TECWAHNPAS RLTALRVKKT LAKMSESQDI KL //