BMR1B_HUMAN
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 03-AUG-2022, entry version 219.
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 {ECO:0000250|UniProtKB:P36898};
DE AltName: CD_antigen=CDw293;
DE Flags: Precursor;
GN Name=BMPR1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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-IB) and
RT its expression in prostate cancer in comparison with other 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., Miyazono K.,
RA ten Dijke P., Stenman G.;
RT "Chromosomal localization of three human genes encoding bone morphogenetic
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Nickel J.,
RA Ploger F., Raspopovic J., Sharpe J., Dathe K., Hecht J.T., Mundlos S.,
RA 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 INTERACTION WITH SCUBE3.
RX PubMed=33308444; DOI=10.1016/j.ajhg.2020.11.015;
RG Genomics England Research Consortium;
RA Lin Y.C., Niceta M., Muto V., Vona B., Pagnamenta A.T., Maroofian R.,
RA Beetz C., van Duyvenvoorde H., Dentici M.L., Lauffer P., Vallian S.,
RA Ciolfi A., Pizzi S., Bauer P., Gruening N.M., Bellacchio E.,
RA Del Fattore A., Petrini S., Shaheen R., Tiosano D., Halloun R.,
RA Pode-Shakked B., Albayrak H.M., Isik E., Wit J.M., Dittrich M.,
RA Freire B.L., Bertola D.R., Jorge A.A.L., Barel O., Sabir A.H.,
RA Al Tenaiji A.M.J., Taji S.M., Al-Sannaa N., Al-Abdulwahed H., Digilio M.C.,
RA Irving M., Anikster Y., Bhavani G.S.L., Girisha K.M., Haaf T., Taylor J.C.,
RA Dallapiccola B., Alkuraya F.S., Yang R.B., Tartaglia M.;
RT "SCUBE3 loss-of-function causes a recognizable recessive developmental
RT disorder due to defective bone morphogenetic protein signaling.";
RL Am. J. Hum. Genet. 108:115-133(2021).
RN [9]
RP VARIANTS BDA2 LYS-200 AND TRP-486, AND CHARACTERIZATION OF VARIANTS BDA2
RP 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 brachydactyly
RT type A2.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12277-12282(2003).
RN [10]
RP INVOLVEMENT IN AMD3.
RX PubMed=15805157; DOI=10.1136/jmg.2004.023564;
RA Demirhan O., Tuerkmen S., Schwabe G.C., Soyupak S., Akguel E., Tastemir D.,
RA 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 [11]
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 type
RT C/symphalangism-like phenotype or brachydactyly type A2.";
RL Eur. J. Hum. Genet. 14:1248-1254(2006).
RN [12]
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., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [13]
RP VARIANT AMD3 ARG-53, AND CHARACTERIZATION OF VARIANT AMD3 ARG-53.
RX PubMed=24129431; DOI=10.1038/ejhg.2013.222;
RA Graul-Neumann L.M., Deichsel A., Wille U., Kakar N., Koll R., Bassir C.,
RA Ahmad J., Cormier-Daire V., Mundlos S., Kubisch C., Borck G., Klopocki E.,
RA Mueller T.D., Doelken S.C., Seemann P.;
RT "Homozygous missense and nonsense mutations in BMPR1B cause acromesomelic
RT chondrodysplasia-type Grebe.";
RL Eur. J. Hum. Genet. 22:726-733(2014).
RN [14]
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 [15]
RP VARIANT AMD3 CYS-31, AND CHARACTERIZATION OF VARIANT AMD3 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 dysplasia.";
RL Orphanet J. Rare Dis. 10:84-84(2015).
CC -!- FUNCTION: On ligand binding, forms a receptor complex consisting of two
CC type II and two type I transmembrane serine/threonine kinases. Type II
CC receptors phosphorylate and activate type I receptors which
CC autophosphorylate, then bind and activate SMAD transcriptional
CC regulators. Receptor for BMP7/OP-1 and GDF5. Positively regulates
CC chondrocyte differentiation through GDF5 interaction.
CC {ECO:0000250|UniProtKB:P36898}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC Evidence={ECO:0000250|UniProtKB:P36898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44881;
CC Evidence={ECO:0000250|UniProtKB:P36898};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30; Evidence={ECO:0000250|UniProtKB:P36898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18674;
CC Evidence={ECO:0000250|UniProtKB:P36898};
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 regulates
CC chondrocyte differentiation. Interacts with SCUBE3 (PubMed:33308444).
CC {ECO:0000269|PubMed:24098149, ECO:0000269|PubMed:33308444}.
CC -!- INTERACTION:
CC O00238; P12643: BMP2; NbExp=3; IntAct=EBI-7527193, EBI-1029262;
CC O00238; P43026: GDF5; NbExp=7; IntAct=EBI-7527193, EBI-8571476;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36898};
CC Single-pass type I membrane protein {ECO:0000255}.
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 -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P36898}.
CC -!- DISEASE: Acromesomelic dysplasia 3 (AMD3) [MIM:609441]: A form of
CC acromesomelic dysplasia, a skeletal disorder characterized by short
CC stature, very short limbs and hand/foot malformations. The severity of
CC limb abnormalities increases from proximal to distal with profoundly
CC affected hands and feet showing brachydactyly and/or rudimentary
CC fingers (knob-like fingers). AMD3 is an autosomal recessive form
CC characterized by bilateral aplasia of the fibula, severe brachydactyly,
CC and fusion of carpal and tarsal bones. {ECO:0000269|PubMed:15805157,
CC ECO:0000269|PubMed:24129431, ECO:0000269|PubMed:26105076}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Brachydactyly A2 (BDA2) [MIM:112600]: A form of brachydactyly.
CC Brachydactyly defines a group of inherited malformations characterized
CC by shortening of the digits due to abnormal development of the
CC phalanges and/or the metacarpals. In brachydactyly type A2 shortening
CC of the middle phalanges is confined to the index finger and the second
CC toe, all other digits being more or less normal. Because of a rhomboid
CC or triangular shape of the affected middle phalanx, the end of the
CC second finger usually deviates radially. {ECO:0000269|PubMed:14523231,
CC ECO:0000269|PubMed:16957682}. Note=The disease is caused by variants
CC 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 abnormal
CC development of the phalanges and/or the metacarpals. Brachydactyly type
CC A1 is characterized by middle phalanges of all the digits rudimentary
CC or fused with the terminal phalanges. The proximal phalanges of the
CC thumbs and big toes are short. BDA1D inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:25758993}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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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 PDB; 3MDY; X-ray; 2.05 A; A/C=168-502.
DR PDBsum; 3MDY; -.
DR AlphaFoldDB; O00238; -.
DR SMR; O00238; -.
DR BioGRID; 107126; 79.
DR IntAct; O00238; 7.
DR MINT; O00238; -.
DR STRING; 9606.ENSP00000401907; -.
DR BindingDB; O00238; -.
DR ChEMBL; CHEMBL5476; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; O00238; -.
DR GuidetoPHARMACOLOGY; 1789; -.
DR iPTMnet; O00238; -.
DR PhosphoSitePlus; O00238; -.
DR BioMuta; BMPR1B; -.
DR jPOST; O00238; -.
DR MassIVE; O00238; -.
DR MaxQB; O00238; -.
DR PaxDb; O00238; -.
DR PeptideAtlas; O00238; -.
DR PRIDE; O00238; -.
DR ProteomicsDB; 47802; -. [O00238-1]
DR Antibodypedia; 4045; 659 antibodies from 36 providers.
DR DNASU; 658; -.
DR Ensembl; ENST00000264568.8; ENSP00000264568.4; ENSG00000138696.11. [O00238-1]
DR Ensembl; ENST00000394931.1; ENSP00000378389.1; ENSG00000138696.11. [O00238-1]
DR Ensembl; ENST00000440890.7; ENSP00000401907.2; ENSG00000138696.11. [O00238-2]
DR Ensembl; ENST00000509540.6; ENSP00000421671.1; ENSG00000138696.11. [O00238-1]
DR Ensembl; ENST00000512312.5; ENSP00000425444.1; ENSG00000138696.11. [O00238-1]
DR Ensembl; ENST00000515059.6; ENSP00000426617.1; ENSG00000138696.11. [O00238-1]
DR Ensembl; ENST00000672698.1; ENSP00000500035.1; ENSG00000138696.11. [O00238-1]
DR GeneID; 658; -.
DR KEGG; hsa:658; -.
DR MANE-Select; ENST00000515059.6; ENSP00000426617.1; NM_001203.3; NP_001194.1.
DR UCSC; uc003htm.5; human. [O00238-1]
DR CTD; 658; -.
DR DisGeNET; 658; -.
DR GeneCards; BMPR1B; -.
DR GeneReviews; BMPR1B; -.
DR HGNC; HGNC:1077; BMPR1B.
DR HPA; ENSG00000138696; Tissue enhanced (brain, cervix, prostate).
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 VEuPathDB; HostDB:ENSG00000138696; -.
DR eggNOG; KOG2052; Eukaryota.
DR GeneTree; ENSGT00940000155919; -.
DR HOGENOM; CLU_000288_8_1_1; -.
DR InParanoid; O00238; -.
DR OMA; SWNNERE; -.
DR OrthoDB; 776697at2759; -.
DR PhylomeDB; O00238; -.
DR TreeFam; TF314724; -.
DR BRENDA; 2.7.10.2; 2681.
DR PathwayCommons; O00238; -.
DR Reactome; R-HSA-201451; Signaling by BMP.
DR SignaLink; O00238; -.
DR SIGNOR; O00238; -.
DR BioGRID-ORCS; 658; 15 hits in 1101 CRISPR screens.
DR ChiTaRS; BMPR1B; human.
DR EvolutionaryTrace; O00238; -.
DR GeneWiki; BMPR1B; -.
DR GenomeRNAi; 658; -.
DR Pharos; O00238; Tchem.
DR PRO; PR:O00238; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O00238; protein.
DR Bgee; ENSG00000138696; Expressed in calcaneal tendon and 158 other tissues.
DR ExpressionAtlas; O00238; baseline and differential.
DR Genevisible; O00238; HS.
DR GO; GO:1990712; C:HFE-transferrin receptor complex; IC:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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-UCL.
DR GO; GO:0036122; F:BMP binding; IEA:Ensembl.
DR GO; GO:0098821; F:BMP receptor activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019211; F:phosphatase activator activity; IEA:Ensembl.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC-UCL.
DR GO; GO:0046332; F:SMAD binding; IDA:HGNC-UCL.
DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IBA:GO_Central.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; NAS:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IEA:Ensembl.
DR GO; GO:0002063; P:chondrocyte development; ISS:AgBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
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:1902731; P:negative regulation of chondrocyte proliferation; ISS:AgBase.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0001550; P:ovarian cumulus expansion; ISS:UniProtKB.
DR GO; GO:0042698; P:ovulation cycle; ISS:UniProtKB.
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: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-UCL.
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 Gene3D; 2.10.60.10; -; 1.
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; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 SUPFAM; SSF57302; SSF57302; 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; Disease variant; Disulfide bond; Dwarfism; Kinase;
KW Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..13
FT /evidence="ECO:0000255"
FT CHAIN 14..502
FT /note="Bone morphogenetic protein receptor type-1B"
FT /id="PRO_0000024412"
FT TOPO_DOM 14..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 174..203
FT /note="GS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
FT DOMAIN 204..494
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 210..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DISULFID 32..53
FT /evidence="ECO:0000250|UniProtKB:P36898"
FT DISULFID 34..38
FT /evidence="ECO:0000250|UniProtKB:P36898"
FT DISULFID 47..71
FT /evidence="ECO:0000250|UniProtKB:P36898"
FT DISULFID 81..95
FT /evidence="ECO:0000250|UniProtKB:P36898"
FT DISULFID 96..102
FT /evidence="ECO:0000250|UniProtKB:P36898"
FT VAR_SEQ 1
FT /note="M -> MGWLEELNWQLHIFLLILLSMHTRANFLDNM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045100"
FT VARIANT 31
FT /note="R -> C (in AMD3; unknown pathological significance;
FT mouse BMPR1B construct containing this mutation shows
FT reduced GDF5-dependent receptor activation, mouse BMPR1B
FT construct containing this mutation shows no loss of cell
FT membrane localization; dbSNP:rs745854387)"
FT /evidence="ECO:0000269|PubMed:26105076"
FT /id="VAR_075520"
FT VARIANT 31
FT /note="R -> H (in a gastric adenocarcinoma sample; somatic
FT mutation; dbSNP:rs200035802)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041401"
FT VARIANT 53
FT /note="C -> R (in AMD3; mouse BMPR1B construct containing
FT this mutation shows loss of GDF5-dependent receptor
FT activation, chicken BMPR1B construct containing this
FT mutation does not show reduced chondrocyte differentiation,
FT mouse BMPR1B construct containing this mutation shows no
FT loss of cell membrane localization; dbSNP:rs863225041)"
FT /evidence="ECO:0000269|PubMed:24129431"
FT /id="VAR_075521"
FT VARIANT 149
FT /note="R -> W (in dbSNP:rs34231464)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041402"
FT VARIANT 200
FT /note="I -> K (in BDA2; in animal models loss of kinase
FT activity and loss of positive regulation of chondrocyte
FT differentiation; dbSNP:rs121434417)"
FT /evidence="ECO:0000269|PubMed:14523231"
FT /id="VAR_023819"
FT VARIANT 224
FT /note="R -> H (in dbSNP:rs35973133)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041403"
FT VARIANT 297
FT /note="D -> N (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041404"
FT VARIANT 325
FT /note="K -> N (in BDA1D; acts in a dominant-negative
FT manner; dbSNP:rs869025614)"
FT /evidence="ECO:0000269|PubMed:25758993"
FT /id="VAR_076406"
FT VARIANT 371
FT /note="R -> Q (in dbSNP:rs34970181)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041405"
FT VARIANT 486
FT /note="R -> Q (in brachydactyly type C and BDA2; with also
FT additional features of symphalangism-1; dbSNP:rs121434419)"
FT /evidence="ECO:0000269|PubMed:16957682"
FT /id="VAR_037967"
FT VARIANT 486
FT /note="R -> W (in BDA2; in animal models no effect on
FT kinase activity but strongly decreased positive regulation
FT of chondrocyte differentiation; dbSNP:rs121434418)"
FT /evidence="ECO:0000269|PubMed:14523231"
FT /id="VAR_023820"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:3MDY"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:3MDY"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:3MDY"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:3MDY"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:3MDY"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3MDY"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 298..316
FT /evidence="ECO:0007829|PDB:3MDY"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:3MDY"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 393..411
FT /evidence="ECO:0007829|PDB:3MDY"
FT TURN 426..430
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 437..444
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 455..459
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 461..473
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:3MDY"
FT HELIX 484..496
FT /evidence="ECO:0007829|PDB:3MDY"
FT TURN 497..499
FT /evidence="ECO:0007829|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
