BMP2_MOUSE
ID BMP2_MOUSE Reviewed; 394 AA.
AC P21274; Q497W8;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Bone morphogenetic protein 2;
DE Short=BMP-2;
DE AltName: Full=Bone morphogenetic protein 2A;
DE Short=BMP-2A;
DE Flags: Precursor;
GN Name=Bmp2; Synonyms=Bmp-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8018727; DOI=10.1016/0167-4781(94)90017-5;
RA Feng J.Q., Harris M.A., Ghosh-Choudhury N., Feng M., Mundy G.R.,
RA Harris S.E.;
RT "Structure and sequence of mouse bone morphogenetic protein-2 gene (BMP-2):
RT comparison of the structures and promoter regions of BMP-2 and BMP-4
RT genes.";
RL Biochim. Biophys. Acta 1218:221-224(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thyroid;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-351.
RX PubMed=1970330; DOI=10.1016/0888-7543(90)90480-i;
RA Dickinson M.E., Kobrin M.S., Silan C.M., Kingsley D.M., Justice M.J.,
RA Miller D.A., Ceci J.D., Lock L.F., Lee A., Buchberg A.M., Siracusa L.D.,
RA Lyons K.M., Derynck R., Hogan B.L.M., Copeland N.G., Jenkins N.A.;
RT "Chromosomal localization of seven members of the murine TGF-beta
RT superfamily suggests close linkage to several morphogenetic mutant loci.";
RL Genomics 6:505-520(1990).
RN [7]
RP INTERACTION WITH SOSTDC1.
RX PubMed=14623234; DOI=10.1016/j.ydbio.2003.08.011;
RA Laurikkala J., Kassai Y., Pakkasjaervi L., Thesleff I., Itoh N.;
RT "Identification of a secreted BMP antagonist, ectodin, integrating BMP,
RT FGF, and SHH signals from the tooth enamel knot.";
RL Dev. Biol. 264:91-105(2003).
RN [8]
RP INTERACTION WITH GREM2.
RX PubMed=15039429; DOI=10.1074/jbc.m402376200;
RA Sudo S., Avsian-Kretchmer O., Wang L.S., Hsueh A.J.;
RT "Protein related to DAN and cerberus is a bone morphogenetic protein
RT antagonist that participates in ovarian paracrine regulation.";
RL J. Biol. Chem. 279:23134-23141(2004).
RN [9]
RP INTERACTION WITH RGMB.
RX PubMed=15671031; DOI=10.1074/jbc.m410034200;
RA Samad T.A., Rebbapragada A., Bell E., Zhang Y., Sidis Y., Jeong S.-J.,
RA Campagna J.A., Perusini S., Fabrizio D.A., Schneyer A.L., Lin H.Y.,
RA Brivanlou A.H., Attisano L., Woolf C.J.;
RT "DRAGON, a bone morphogenetic protein co-receptor.";
RL J. Biol. Chem. 280:14122-14129(2005).
RN [10]
RP INTERACTION WITH RGMA.
RX PubMed=15975920; DOI=10.1074/jbc.m503511200;
RA Babitt J.L., Zhang Y., Samad T.A., Xia Y., Tang J., Campagna J.A.,
RA Schneyer A.L., Woolf C.J., Lin H.Y.;
RT "Repulsive guidance molecule (RGMa), a DRAGON homologue, is a bone
RT morphogenetic protein co-receptor.";
RL J. Biol. Chem. 280:29820-29827(2005).
RN [11]
RP INTERACTION WITH RGMC.
RX PubMed=16604073; DOI=10.1038/ng1777;
RA Babitt J.L., Huang F.W., Wrighting D.M., Xia Y., Sidis Y., Samad T.A.,
RA Campagna J.A., Chung R.T., Schneyer A.L., Woolf C.J., Andrews N.C.,
RA Lin H.Y.;
RT "Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin
RT expression.";
RL Nat. Genet. 38:531-539(2006).
RN [12]
RP INTERACTION WITH RGMA.
RX PubMed=17472960; DOI=10.1074/jbc.m701679200;
RA Xia Y., Yu P.B., Sidis Y., Beppu H., Bloch K.D., Schneyer A.L., Lin H.Y.;
RT "Repulsive guidance molecule RGMa alters utilization of bone morphogenetic
RT protein (BMP) type II receptors by BMP2 and BMP4.";
RL J. Biol. Chem. 282:18129-18140(2007).
RN [13]
RP INTERACTION WITH ASPN.
RX PubMed=17522060; DOI=10.1074/jbc.m611181200;
RA Yamada S., Tomoeda M., Ozawa Y., Yoneda S., Terashima Y., Ikezawa K.,
RA Ikegawa S., Saito M., Toyosawa S., Murakami S.;
RT "PLAP-1/asporin, a novel negative regulator of periodontal ligament
RT mineralization.";
RL J. Biol. Chem. 282:23070-23080(2007).
RN [14]
RP INTERACTION WITH MFAP5.
RX PubMed=23963447; DOI=10.1074/jbc.m113.497727;
RA Combs M.D., Knutsen R.H., Broekelmann T.J., Toennies H.M., Brett T.J.,
RA Miller C.A., Kober D.L., Craft C.S., Atkinson J.J., Shipley J.M.,
RA Trask B.C., Mecham R.P.;
RT "Microfibril-associated glycoprotein 2 (MAGP2) loss of function has
RT pleiotropic effects in vivo.";
RL J. Biol. Chem. 288:28869-28880(2013).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=29198724; DOI=10.1016/j.ajhg.2017.10.006;
RA Tan T.Y., Gonzaga-Jauregui C., Bhoj E.J., Strauss K.A., Brigatti K.,
RA Puffenberger E., Li D., Xie L., Das N., Skubas I., Deckelbaum R.A.,
RA Hughes V., Brydges S., Hatsell S., Siao C.J., Dominguez M.G.,
RA Economides A., Overton J.D., Mayne V., Simm P.J., Jones B.O., Eggers S.,
RA Le Guyader G., Pelluard F., Haack T.B., Sturm M., Riess A., Waldmueller S.,
RA Hofbeck M., Steindl K., Joset P., Rauch A., Hakonarson H., Baker N.L.,
RA Farlie P.G.;
RT "Monoallelic BMP2 variants predicted to result in haploinsufficiency cause
RT craniofacial, skeletal, and cardiac features overlapping those of 20p12
RT deletions.";
RL Am. J. Hum. Genet. 101:985-994(2017).
CC -!- FUNCTION: Growth factor of the TGF-beta superfamily that plays
CC essential roles in many developmental processes, including
CC cardiogenesis, neurogenesis, and osteogenesis. Induces cartilage and
CC bone formation. Initiates the canonical BMP signaling cascade by
CC associating with type I receptor BMPR1A and type II receptor BMPR2.
CC Once all three components are bound together in a complex at the cell
CC surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A
CC propagates signal by phosphorylating SMAD1/5/8 that travel to the
CC nucleus and act as activators and repressors of transcription of target
CC genes. Can also signal through non-canonical pathways such as ERK/MAP
CC kinase signaling cascade that regulates osteoblast differentiation.
CC Stimulates also the differentiation of myoblasts into osteoblasts via
CC the EIF2AK3-EIF2A-ATF4 pathway by stimulating EIF2A phosphorylation
CC which leads to increased expression of ATF4 which plays a central role
CC in osteoblast differentiation. {ECO:0000250|UniProtKB:P12643}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with SOSTDC1 (By
CC similarity). Interacts with GREM2, RGMA, RGMB and RGMC. Interacts with
CC ASPN (By similarity). Interacts with MAFP5 (By similarity). Interacts
CC with FBN1 (via N-terminal domain) and FBN2. Interacts with type I
CC receptor BMPR1A. Interacts with type II receptor BMPR2 (By similarity).
CC Interacts with SCUBE3 (By similarity). Interacts with TNFAIP6
CC (primarily via Link domain); this interaction is inhibited by
CC hyaluronan. {ECO:0000250|UniProtKB:P12643, ECO:0000269|PubMed:14623234,
CC ECO:0000269|PubMed:15039429, ECO:0000269|PubMed:15671031,
CC ECO:0000269|PubMed:15975920, ECO:0000269|PubMed:16604073,
CC ECO:0000269|PubMed:17472960, ECO:0000269|PubMed:17522060,
CC ECO:0000269|PubMed:23963447}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DISRUPTION PHENOTYPE: Heterozygous BMP2-knockout mice show abnormal
CC numbers of rib pairs, a reduction in overall body length, and less bone
CC mineral content and volume than wild-type mice. Homozygous BMP2-
CC knockout mice die before embryonic day 12.5.
CC {ECO:0000269|PubMed:29198724}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; L25602; AAB05665.1; -; Genomic_DNA.
DR EMBL; AK133923; BAE21928.1; -; mRNA.
DR EMBL; AK161862; BAE36612.1; -; mRNA.
DR EMBL; AL831753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28371.1; -; Genomic_DNA.
DR EMBL; BC100344; AAI00345.1; -; mRNA.
DR CCDS; CCDS16782.1; -.
DR PIR; A34201; A34201.
DR PIR; S45355; S45355.
DR RefSeq; NP_031579.2; NM_007553.3.
DR AlphaFoldDB; P21274; -.
DR SMR; P21274; -.
DR BioGRID; 198363; 1.
DR STRING; 10090.ENSMUSP00000028836; -.
DR GlyGen; P21274; 4 sites.
DR PhosphoSitePlus; P21274; -.
DR MaxQB; P21274; -.
DR PaxDb; P21274; -.
DR PRIDE; P21274; -.
DR ProteomicsDB; 265312; -.
DR Antibodypedia; 8441; 995 antibodies from 42 providers.
DR DNASU; 12156; -.
DR Ensembl; ENSMUST00000028836; ENSMUSP00000028836; ENSMUSG00000027358.
DR GeneID; 12156; -.
DR KEGG; mmu:12156; -.
DR UCSC; uc008mnr.2; mouse.
DR CTD; 650; -.
DR MGI; MGI:88177; Bmp2.
DR VEuPathDB; HostDB:ENSMUSG00000027358; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000155666; -.
DR HOGENOM; CLU_020515_4_2_1; -.
DR InParanoid; P21274; -.
DR OMA; KFPMTRL; -.
DR OrthoDB; 962484at2759; -.
DR PhylomeDB; P21274; -.
DR TreeFam; TF351789; -.
DR Reactome; R-MMU-201451; Signaling by BMP.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 12156; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Bmp2; mouse.
DR PRO; PR:P21274; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P21274; protein.
DR Bgee; ENSMUSG00000027358; Expressed in gastrula and 310 other tissues.
DR Genevisible; P21274; MM.
DR GO; GO:0070724; C:BMP receptor complex; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0070700; F:BMP receptor binding; ISO:MGI.
DR GO; GO:0039706; F:co-receptor binding; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; IMP:BHF-UCL.
DR GO; GO:0008083; F:growth factor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019211; F:phosphatase activator activity; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:MGI.
DR GO; GO:0048018; F:receptor ligand activity; IDA:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0036305; P:ameloblast differentiation; IDA:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0003176; P:aortic valve development; IMP:BHF-UCL.
DR GO; GO:0048708; P:astrocyte differentiation; IDA:MGI.
DR GO; GO:1905222; P:atrioventricular canal morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
DR GO; GO:0061312; P:BMP signaling pathway involved in heart development; IMP:BHF-UCL.
DR GO; GO:0003130; P:BMP signaling pathway involved in heart induction; ISO:MGI.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0030282; P:bone mineralization; IDA:MGI.
DR GO; GO:0035630; P:bone mineralization involved in bone maturation; ISO:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:MGI.
DR GO; GO:0003210; P:cardiac atrium formation; IMP:BHF-UCL.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:1905072; P:cardiac jelly development; IMP:BHF-UCL.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IGI:BHF-UCL.
DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:MGI.
DR GO; GO:0035051; P:cardiocyte differentiation; ISO:MGI.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; ISO:MGI.
DR GO; GO:0060128; P:corticotropin hormone secreting cell differentiation; IDA:MGI.
DR GO; GO:0035054; P:embryonic heart tube anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0003272; P:endocardial cushion formation; IMP:BHF-UCL.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IEP:UniProtKB.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0048762; P:mesenchymal cell differentiation; ISS:UniProtKB.
DR GO; GO:0072138; P:mesenchymal cell proliferation involved in ureteric bud development; IMP:UniProtKB.
DR GO; GO:0060485; P:mesenchyme development; ISS:BHF-UCL.
DR GO; GO:0032348; P:negative regulation of aldosterone biosynthetic process; ISO:MGI.
DR GO; GO:0051042; P:negative regulation of calcium-independent cell-cell adhesion; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; ISO:MGI.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:2000065; P:negative regulation of cortisol biosynthetic process; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:MGI.
DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0051148; P:negative regulation of muscle cell differentiation; IDA:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IGI:BHF-UCL.
DR GO; GO:0010894; P:negative regulation of steroid biosynthetic process; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0003308; P:negative regulation of Wnt signaling pathway involved in heart development; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IDA:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:MGI.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0060039; P:pericardium development; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; IDA:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:BHF-UCL.
DR GO; GO:0061036; P:positive regulation of cartilage development; IDA:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IDA:MGI.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; IMP:BHF-UCL.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IGI:BHF-UCL.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:MGI.
DR GO; GO:0042482; P:positive regulation of odontogenesis; IDA:MGI.
DR GO; GO:0045778; P:positive regulation of ossification; IDA:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:BHF-UCL.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; ISO:MGI.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:MGI.
DR GO; GO:0060804; P:positive regulation of Wnt signaling pathway by BMP signaling pathway; IDA:MGI.
DR GO; GO:0031648; P:protein destabilization; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0006029; P:proteoglycan metabolic process; IGI:MGI.
DR GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IGI:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR GO; GO:0021537; P:telencephalon development; ISO:MGI.
DR GO; GO:0021978; P:telencephalon regionalization; IGI:MGI.
DR GO; GO:0060129; P:thyroid-stimulating hormone-secreting cell differentiation; IDA:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Chondrogenesis; Cleavage on pair of basic residues; Cytokine;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Growth factor; Osteogenesis; Phosphoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..280
FT /note="Cleaved by PCSK5"
FT /evidence="ECO:0000305"
FT /id="PRO_0000033826"
FT CHAIN 281..394
FT /note="Bone morphogenetic protein 2"
FT /id="PRO_0000033827"
FT REGION 269..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..291
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12644"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 294..359
FT /evidence="ECO:0000250"
FT DISULFID 323..391
FT /evidence="ECO:0000250"
FT DISULFID 327..393
FT /evidence="ECO:0000250"
FT DISULFID 358
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 110
FT /note="S -> T (in Ref. 1; AAB05665)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..114
FT /note="HE -> QL (in Ref. 1; AAB05665)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="G -> R (in Ref. 6; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 44525 MW; D0C03B63B1D5C4E2 CRC64;
MVAGTRCLLV LLLPQVLLGG AAGLIPELGR KKFAAASSRP LSRPSEDVLS EFELRLLSMF
GLKQRPTPSK DVVVPPYMLD LYRRHSGQPG APAPDHRLER AASRANTVRS FHHEEAVEEL
PEMSGKTARR FFFNLSSVPS DEFLTSAELQ IFREQIQEAL GNSSFQHRIN IYEIIKPAAA
NLKFPVTRLL DTRLVNQNTS QWESFDVTPA VMRWTTQGHT NHGFVVEVAH LEENPGVSKR
HVRISRSLHQ DEHSWSQIRP LLVTFGHDGK GHPLHKREKR QAKHKQRKRL KSSCKRHPLY
VDFSDVGWND WIVAPPGYHA FYCHGECPFP LADHLNSTNH AIVQTLVNSV NSKIPKACCV
PTELSAISML YLDENEKVVL KNYQDMVVEG CGCR
