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                                                                Synonyms: GDF-9B | growth/differentiation factor 9B
                                 
                                                         
                            Compound class: 
                                                            Endogenous peptide in human, mouse or rat
                                 
                                
                                    
                                        Comment: The BMP-15 gene is X-linked and expressed in oocytes. BMP-15 protein appears to be involved in early ovarian folliculogenesis [1-3], acting in synergy with growth/differentiation factor-9 [4]. BMP-15 is a selective modulator of FSH action [3]. The active peptide is a disulphide bond-linked homodimer.
                                    
                                 
                            
                                
                                    Species: Human
                                 
                            
                            
                          
                                
                                    
                                
                          
                                   
                                   
                                  
                                    
                                    
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Peptide Sequence ![]()  | 
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                                                                            QADGISAEVTASSSKHSGPENNQCSLHPFQISFRQLGWDHWIIAPPFYTPNYCKGTCLRVLRDGLNSPNHAIIQNLINQL VDQSVPRPSCVPYKYVPISVLMIEANGSILYKEYEGMIAESCTCR  | 
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| Post-translational Modification | |
| The active peptide is a homodimer, which in contrast to other bone-morphogentic proteins is not disulphide linked. C-terminal glutamine residue is pyrrolidone carboxylic acid; serine residue at position 6 is phosphoserine; threonine resdiue at position 10 is O-linked glycosylated; asparagine resdiue at position 106 is predicted to be N-linked glycosylated; predicted disulphide bond formation between cysteine residues at positions 24 and 90, 53 and 122, and 57 and 124 | |