| UniProt ID | BMP2_HUMAN | |
|---|---|---|
| UniProt AC | P12643 | |
| Protein Name | Bone morphogenetic protein 2 | |
| Gene Name | BMP2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 396 | |
| Subcellular Localization | Secreted. | |
| Protein Description | Induces cartilage and bone formation. [PubMed: 3201241 Stimulates the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A- ATF4 pathway. BMP2 activation of EIF2AK3 stimulates phosphorylation of EIF2A which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation. In addition stimulates TMEM119, which upregulates the expression of ATF4] | |
| Protein Sequence | MVAGTRCLLALLLPQVLLGGAAGLVPELGRRKFAAASSGRPSSQPSDEVLSEFELRLLSMFGLKQRPTPSRDAVVPPYMLDLYRRHSGQPGSPAPDHRLERAASRANTVRSFHHEESLEELPETSGKTTRRFFFNLSSIPTEEFITSAELQVFREQMQDALGNNSSFHHRINIYEIIKPATANSKFPVTRLLDTRLVNQNASRWESFDVTPAVMRWTAQGHANHGFVVEVAHLEEKQGVSKRHVRISRSLHQDEHSWSQIRPLLVTFGHDGKGHPLHKREKRQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 87 | Phosphorylation | LDLYRRHSGQPGSPA HHHHHHHCCCCCCCC | 36.99 | - | |
| 111 | Phosphorylation | SRANTVRSFHHEESL HHHHHHHHHCCHHHH | 25.29 | 23312004 | |
| 117 | Phosphorylation | RSFHHEESLEELPET HHHCCHHHHHHCCCC | 37.79 | 26657352 | |
| 135 | N-linked_Glycosylation | TTRRFFFNLSSIPTE CEEEEEEECCCCCHH | 33.58 | UniProtKB CARBOHYD | |
| 163 | N-linked_Glycosylation | QMQDALGNNSSFHHR HHHHHHCCCCCCCCC | 46.16 | UniProtKB CARBOHYD | |
| 164 | N-linked_Glycosylation | MQDALGNNSSFHHRI HHHHHCCCCCCCCCE | 36.91 | UniProtKB CARBOHYD | |
| 181 | Phosphorylation | YEIIKPATANSKFPV HHEECCCCCCCCCCC | 34.59 | - | |
| 184 | Phosphorylation | IKPATANSKFPVTRL ECCCCCCCCCCCCHH | 32.96 | - | |
| 200 | N-linked_Glycosylation | DTRLVNQNASRWESF CHHCCCCCCCCCCCC | 34.38 | UniProtKB CARBOHYD | |
| 200 | N-linked_Glycosylation | DTRLVNQNASRWESF CHHCCCCCCCCCCCC | 34.38 | 20068230 | |
| 278 | Ubiquitination | GKGHPLHKREKRQAK CCCCCCCHHHHHHHH | 70.68 | - | |
| 338 | N-linked_Glycosylation | FPLADHLNSTNHAIV CCCHHHHCCCCHHHH | 43.28 | 9265423 | |
| 383 | Ubiquitination | ENEKVVLKNYQDMVV CCCCEEEECHHHHEE | 41.84 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of BMP2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BMP2_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of BMP2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| BMPR2_HUMAN | BMPR2 | physical | 7791754 | |
| CO2A1_HUMAN | COL2A1 | physical | 10085302 | |
| BMR1A_HUMAN | BMPR1A | physical | 10692589 | |
| BMR1A_HUMAN | BMPR1A | physical | 10880444 | |
| BMPR2_HUMAN | BMPR2 | physical | 10880444 | |
| ARP2_HUMAN | ACTR2 | physical | 10880444 | |
| MGP_HUMAN | MGP | physical | 11741887 | |
| BMR1A_HUMAN | BMPR1A | physical | 10712517 | |
| BMR1B_HUMAN | BMPR1B | physical | 10712517 | |
| BMPR2_HUMAN | BMPR2 | physical | 10712517 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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