BMR1A_HUMAN - dbPTM
BMR1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BMR1A_HUMAN
UniProt AC P36894
Protein Name Bone morphogenetic protein receptor type-1A
Gene Name BMPR1A
Organism Homo sapiens (Human).
Sequence Length 532
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP2, BMP4, GDF5 and GDF6. Positively regulates chondrocyte differentiation through GDF5 interaction. Mediates induction of adipogenesis by GDF6..
Protein Sequence MPQLYIYIRLLGAYLFIISRVQGQNLDSMLHGTGMKSDSDQKKSENGVTLAPEDTLPFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQPTLPPVVIGPFFDGSIRWLVLLISMAVCIIAMIIFSSCFCYKHYCKSISSRRRYNRDLEQDEAFIPVGESLKDLIDQSQSSGSGSGLPLLVQRTIAKQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVKRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVESQDVKI
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
5Phosphorylation---MPQLYIYIRLLG
---CCCHHHHHHHHH		6.0924043423
7Phosphorylation-MPQLYIYIRLLGAY
-CCCHHHHHHHHHHH		2.6624043423
49O-linked_GlycosylationKKSENGVTLAPEDTL
CCCCCCCEECCCCCC		20.71OGP
55O-linked_GlycosylationVTLAPEDTLPFLKCY
CEECCCCCCCCHHHH		34.37OGP
73N-linked_GlycosylationHCPDDAINNTCITNG
CCCCCHHCCCEEECC		39.21UniProtKB CARBOHYD
137O-linked_GlycosylationCNQYLQPTLPPVVIG
HHHHHCCCCCCEEEC		38.65OGP
205PhosphorylationAFIPVGESLKDLIDQ
CCCCCCHHHHHHHHH		34.4928348404
207UbiquitinationIPVGESLKDLIDQSQ
CCCCHHHHHHHHHHH		60.8223503661
213PhosphorylationLKDLIDQSQSSGSGS
HHHHHHHHHCCCCCC		28.4317081983
215PhosphorylationDLIDQSQSSGSGSGL
HHHHHHHCCCCCCCH		41.7419060867
216PhosphorylationLIDQSQSSGSGSGLP
HHHHHHCCCCCCCHH		29.3719060867
218PhosphorylationDQSQSSGSGSGLPLL
HHHHCCCCCCCHHHH		31.5619060867
220PhosphorylationSQSSGSGSGLPLLVQ
HHCCCCCCCHHHHHH		38.5619060867
232UbiquitinationLVQRTIAKQIQMVRQ
HHHHHHHHHHHHHHH		44.0523000965
391PhosphorylationAVKFNSDTNEVDVPL
EEEECCCCCCCCCCC		32.8524719451
407PhosphorylationTRVGTKRYMAPEVLD
CCCCCCEECCHHHHC		10.1325884760
416PhosphorylationAPEVLDESLNKNHFQ
CHHHHCHHHCCCCCC		36.5930622161
453PhosphorylationTGGIVEEYQLPYYNM
HCCHHEEEECCCCCC		11.2222210691
457PhosphorylationVEEYQLPYYNMVPSD
HEEEECCCCCCCCCC		18.9622210691
466PhosphorylationNMVPSDPSYEDMREV
CCCCCCCCHHHHHHH		46.2622210691
477UbiquitinationMREVVCVKRLRPIVS
HHHHEEEEECCCCCC		40.36-
513PhosphorylationHNPASRLTALRIKKT
CCHHHHHHHHHHHHH		23.6424719451
518UbiquitinationRLTALRIKKTLAKMV
HHHHHHHHHHHHHHH		33.0223503661
519UbiquitinationLTALRIKKTLAKMVE
HHHHHHHHHHHHHHH		46.5323503661
523UbiquitinationRIKKTLAKMVESQDV
HHHHHHHHHHHCCCC		46.7433845483
531UbiquitinationMVESQDVKI------
HHHCCCCCC------		51.4921906983
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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20558834
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BMR1A_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 BMR1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SF3B4_HUMANSF3B4physical
15351706
SMAD7_MOUSESmad7physical
9738003
BMP2_HUMANBMP2physical
11263668
BMPR2_HUMANBMPR2physical
7791754
FKB1B_HUMANFKBP1Bphysical
15351706
BMP6_HUMANBMP6physical
10504300
FKB1A_HUMANFKBP1Aphysical
9663660
ZMY11_HUMANZMYND11physical
9663660
BMR1B_HUMANBMPR1Bphysical
10712517
BMPR2_HUMANBMPR2physical
10712517
BMR1A_HUMANBMPR1Aphysical
10712517
T22D1_HUMANTSC22D1physical
21791611
IGSF1_HUMANIGSF1physical
11266516
SMUF1_HUMANSMURF1physical
12857866
BAMBI_HUMANBAMBIphysical
19758997
SMAD1_HUMANSMAD1physical
9136927
PEG10_HUMANPEG10physical
15611116
CAV1_HUMANCAV1physical
15657086
BMR1A_HUMANBMPR1Aphysical
18436533
ACVR1_HUMANACVR1physical
18436533
OTUB1_HUMANOTUB1physical
25872870
Drug and Disease Associations
Kegg Disease
H01023 Juvenile polyposis syndrome
H01024 Hereditary mixed polyposis syndrome
OMIM Disease
174900Juvenile polyposis syndrome (JPS)
610069Polyposis syndrome, mixed hereditary 2 (HMPS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BMR1A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-216; SER-218AND SER-220, AND MASS SPECTROMETRY.

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