BMP2_HUMAN - dbPTM
BMP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
87PhosphorylationLDLYRRHSGQPGSPA
HHHHHHHCCCCCCCC
36.99-
111PhosphorylationSRANTVRSFHHEESL
HHHHHHHHHCCHHHH
25.2923312004
117PhosphorylationRSFHHEESLEELPET
HHHCCHHHHHHCCCC
37.7926657352
135N-linked_GlycosylationTTRRFFFNLSSIPTE
CEEEEEEECCCCCHH
33.58UniProtKB CARBOHYD
163N-linked_GlycosylationQMQDALGNNSSFHHR
HHHHHHCCCCCCCCC
46.16UniProtKB CARBOHYD
164N-linked_GlycosylationMQDALGNNSSFHHRI
HHHHHCCCCCCCCCE
36.91UniProtKB CARBOHYD
181PhosphorylationYEIIKPATANSKFPV
HHEECCCCCCCCCCC
34.59-
184PhosphorylationIKPATANSKFPVTRL
ECCCCCCCCCCCCHH
32.96-
200N-linked_GlycosylationDTRLVNQNASRWESF
CHHCCCCCCCCCCCC
34.38UniProtKB CARBOHYD
200N-linked_GlycosylationDTRLVNQNASRWESF
CHHCCCCCCCCCCCC
34.3820068230
278UbiquitinationGKGHPLHKREKRQAK
CCCCCCCHHHHHHHH
70.68-
338N-linked_GlycosylationFPLADHLNSTNHAIV
CCCHHHHCCCCHHHH
43.289265423
383UbiquitinationENEKVVLKNYQDMVV
CCCCEEEECHHHHEE
41.84-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BMP2_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BMPR2_HUMANBMPR2physical
7791754
CO2A1_HUMANCOL2A1physical
10085302
BMR1A_HUMANBMPR1Aphysical
10692589
BMR1A_HUMANBMPR1Aphysical
10880444
BMPR2_HUMANBMPR2physical
10880444
ARP2_HUMANACTR2physical
10880444
MGP_HUMANMGPphysical
11741887
BMR1A_HUMANBMPR1Aphysical
10712517
BMR1B_HUMANBMPR1Bphysical
10712517
BMPR2_HUMANBMPR2physical
10712517

Drug and Disease Associations
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.
Regulatory Network of BMP2_HUMAN

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Related Literatures of Post-Translational Modification

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