BMR1B_HUMAN - dbPTM
BMR1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BMR1B_HUMAN
UniProt AC O00238
Protein Name Bone morphogenetic protein receptor type-1B
Gene Name BMPR1B
Organism Homo sapiens (Human).
Sequence Length 502
Subcellular Localization Cell membrane . 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 BMP7/OP-1 and GDF5. Positively regulates chondrocyte differentiation through GDF5 interaction..
Protein Sequence MLLRSAGKLNVGTKKEDGESTAPTPRPKVLRCKCHHHCPEDSVNNICSTDGYCFTMIEEDDSGLPVVTSGCLGLEGSDFQCRDTPIPHQRRSIECCTERNECNKDLHPTLPPLKNRDFVDGPIHHRALLISVTVCSLLLVLIILFCYFRYKRQETRPRYSIGLEQDETYIPPGESLRDLIEQSQSSGSGSGLPLLVQRTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDYLKSTTLDAKSMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKFISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNHFQSYIMADMYSFGLILWEVARRCVSGGIVEEYQLPYHDLVPSDPSYEDMREIVCIKKLRPSFPNRWSSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQDIKL
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
92PhosphorylationPIPHQRRSIECCTER
CCCCCCCCEECCCCC
25.5728348404
97PhosphorylationRRSIECCTERNECNK
CCCEECCCCCCCCCC
50.03-
109O-linked_GlycosylationCNKDLHPTLPPLKNR
CCCCCCCCCCCCCCC
40.9455832527
122PhosphorylationNRDFVDGPIHHRALL
CCCCCCCCCHHHHHH
20.4827251275
155PhosphorylationFRYKRQETRPRYSIG
HHHHCCCCCCCCEEC
37.3223532336
159PhosphorylationRQETRPRYSIGLEQD
CCCCCCCCEECCCCC
13.8128348404
160PhosphorylationQETRPRYSIGLEQDE
CCCCCCCEECCCCCC
16.0924719451
175PhosphorylationTYIPPGESLRDLIEQ
CCCCCCHHHHHHHHH
34.3222210691
190PhosphorylationSQSSGSGSGLPLLVQ
HHHCCCCCCHHHHHH
38.5617081983
205PhosphorylationRTIAKQIQMVKQIGK
HHHHHHHHHHHHHCC
28.2927251275
290PhosphorylationENGSLYDYLKSTTLD
CCCCHHHHHHHCCCC
11.50-
293PhosphorylationSLYDYLKSTTLDAKS
CHHHHHHHCCCCHHH
24.8330622161
294PhosphorylationLYDYLKSTTLDAKSM
HHHHHHHCCCCHHHH
29.7730622161
295PhosphorylationYDYLKSTTLDAKSML
HHHHHHCCCCHHHHH
29.7230622161
300PhosphorylationSTTLDAKSMLKLAYS
HCCCCHHHHHHHHHH
30.9430622161
336UbiquitinationAHRDLKSKNILVKKN
ECCCCCCCCEEEEEC
46.55-
402PhosphorylationYIMADMYSFGLILWE
HHHHHHHHHHHHHHH
13.24-
483PhosphorylationHNPASRLTALRVKKT
CCHHHHHHHHHHHHH
23.6424719451
493UbiquitinationRVKKTLAKMSESQDI
HHHHHHHHHCCCCCC
46.18-

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 BMR1B_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 BMR1B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KBRS1_MOUSENkiras1physical
15761153
REBL1_MOUSERhebl1physical
15761153
RHOD_MOUSERhodphysical
15761153
RAB6B_MOUSERab6bphysical
15761153
RAB38_MOUSERab38physical
15761153
RHBT1_MOUSERhobtb1physical
15761153
RS27A_MOUSERps27aphysical
15761153
FBX3_MOUSEFbxo3physical
15761153
SQSTM_MOUSESqstm1physical
15761153
DCAF7_MOUSEDcaf7physical
15761153
MKNK2_MOUSEMknk2physical
15761153
MP2K3_MOUSEMap2k3physical
15761153
FANCL_MOUSEFanclphysical
15761153
TGFR1_MOUSETgfbr1physical
15761153
LZTR1_MOUSELztr1physical
15761153
PKHB1_MOUSEPlekhb1physical
15761153
FKB1B_MOUSEFkbp1bphysical
15761153
FKB1A_MOUSEFkbp1aphysical
15761153
IRF7_MOUSEIrf7physical
15761153
RHOJ_MOUSERhojphysical
15761153
RRAS2_MOUSERras2physical
15761153
FBX34_MOUSEFbxo34physical
15761153
STK35_MOUSEStk35physical
15761153
CDK14_MOUSECdk14physical
15761153
ILKAP_MOUSEIlkapphysical
15761153
PP2BC_MOUSEPpp3ccphysical
15761153
SRGP1_MOUSESrgap1physical
15761153
NAA20_MOUSENaa20physical
15761153
RHES_MOUSERasd2physical
15761153
BCR_MOUSEBcrphysical
15761153
CHIN_MOUSEChn1physical
15761153
UBP45_MOUSEUsp45physical
15761153
A16L1_MOUSEAtg16l1physical
15761153
FBXW5_MOUSEFbxw5physical
15761153
CDK4_MOUSECdk4physical
15761153
UHMK1_MOUSEUhmk1physical
15761153
BMPR2_MOUSEBmpr2physical
15761153
CHIP_MOUSEStub1physical
15761153
KLHL1_MOUSEKlhl1physical
15761153
ARHG6_MOUSEArhgef6physical
15761153
PP2AA_MOUSEPpp2caphysical
15761153
SH3K1_MOUSESh3kbp1physical
15761153
SMAD6_MOUSESmad6physical
15761153
SMAD7_MOUSESmad7physical
15761153
RAP2A_MOUSERap2aphysical
15761153
BMPR2_HUMANBMPR2physical
7791754
BMPR2_HUMANBMPR2physical
10712517
BMR1B_HUMANBMPR1Bphysical
10712517
TRAF6_HUMANTRAF6physical
18758450
XIAP_HUMANXIAPphysical
19782107
T22D1_HUMANTSC22D1physical
21791611
IGSF1_HUMANIGSF1physical
11266516
SMUF1_HUMANSMURF1physical
12857866
SMAD6_HUMANSMAD6physical
11483516
BAMBI_HUMANBAMBIphysical
19758997
A4_HUMANAPPphysical
21832049
PEG10_HUMANPEG10physical
15611116
OTUB1_HUMANOTUB1physical
25872870

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BMR1B_HUMAN

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Related Literatures of Post-Translational Modification

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