BMPR2_HUMAN - dbPTM
BMPR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BMPR2_HUMAN
UniProt AC Q13873
Protein Name Bone morphogenetic protein receptor type-2
Gene Name BMPR2
Organism Homo sapiens (Human).
Sequence Length 1038
Subcellular Localization Cell 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. Binds to BMP7, BMP2 and, less efficiently, BMP4. Binding is weak but enhanced by the presence of type I receptors for BMPs. Mediates induction of adipogenesis by GDF6..
Protein Sequence MTSSLQRPWRVPWLPWTILLVSTAAASQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTTPLSPPHSFNRDETIIIALASVSVLAVLIVALCFGYRMLTGDRKQGLHSMNMMEAAASEPSLDLDNLKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYRVPLMEHDNIARFIVGDERVTADGRMEYLLVMEYYPNGSLCKYLSLHTSDWVSSCRLAHSVTRGLAYLHTELPRGDHYKPAISHRDLNSRNVLVKNDGTCVISDFGLSMRLTGNRLVRPGEEDNAAISEVGTIRYMAPEVLEGAVNLRDCESALKQVDMYALGLIYWEIFMRCTDLFPGESVPEYQMAFQTEVGNHPTFEDMQVLVSREKQRPKFPEAWKENSLAVRSLKETIEDCWDQDAEARLTAQCAEERMAELMMIWERNKSVSPTVNPMSTAMQNERNLSHNRRVPKIGPYPDYSSSSYIEDSIHHTDSIVKNISSEHSMSSTPLTIGEKNRNSINYERQQAQARIPSPETSVTSLSTNTTTTNTTGLTPSTGMTTISEMPYPDETNLHTTNVAQSIGPTPVCLQLTEEDLETNKLDPKEVDKNLKESSDENLMEHSLKQFSGPDPLSSTSSSLLYPLIKLAVEATGQQDFTQTANGQACLIPDVLPTQIYPLPKQQNLPKRPTSLPLNTKNSTKEPRLKFGSKHKSNLKQVETGVAKMNTINAAEPHVVTVTMNGVAGRNHSVNSHAATTQYANGTVLSGQTTNIVTHRAQEMLQNQFIGEDTRLNINSSPDEHEPLLRREQQAGHDEGVLDRLVDRRERPLEGGRTNSNNNNSNPCSEQDVLAQGVPSTAADPGPSKPRRAQRPNSLDLSATNVLDGSSIQIGESTQDGKSGSGEKIKKRVKTPYSLKRWRPSTWVISTESLDCEVNNNGSNRAVHSKSSTAVYLAEGGTATTMVSKDIGMNCL
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
55N-linked_GlycosylationESRISHENGTILCSK
CCEEECCCCEEEECC		47.70UniProtKB CARBOHYD
110N-linked_GlycosylationTTPPSIQNGTYRFCC
CCCCCCCCCCEEEEE		43.00UniProtKB CARBOHYD
126N-linked_GlycosylationSTDLCNVNFTENFPP
CCCCCCCCCCCCCCC		24.91UniProtKB CARBOHYD
137O-linked_GlycosylationNFPPPDTTPLSPPHS
CCCCCCCCCCCCCCC		29.61OGP
219AcetylationGRYGAVYKGSLDERP
CCCEEEECCCCCCCC		35.1123749302
219AcetylationGRYGAVYKGSLDERP
CCCEEEECCCCCCCC		35.11-
247PhosphorylationFINEKNIYRVPLMEH
CCCCCCCEEEECCCC		18.2325884760
314PhosphorylationSVTRGLAYLHTELPR
HHHHHHHHHCCCCCC		12.2125884760
336PhosphorylationISHRDLNSRNVLVKN
CCCCCCCCCCEEEEC		32.3124719451
355PhosphorylationVISDFGLSMRLTGNR
EECCCCCEEEEECCC		11.3924719451
359PhosphorylationFGLSMRLTGNRLVRP
CCCEEEEECCCCCCC		23.2624719451
375PhosphorylationEEDNAAISEVGTIRY
CCCCCCCCCCCCCEE		22.8529255136
379PhosphorylationAAISEVGTIRYMAPE
CCCCCCCCCEECCHH		13.8829255136
413PhosphorylationMYALGLIYWEIFMRC
HHHHHHHHHHHHHHH		11.3027732954
470PhosphorylationPEAWKENSLAVRSLK
CHHHHHCCHHHHHHH		20.8523532336
513PhosphorylationMIWERNKSVSPTVNP
HHHHCCCCCCCCCCH		31.2328102081
515PhosphorylationWERNKSVSPTVNPMS
HHCCCCCCCCCCHHH		23.1928102081
517PhosphorylationRNKSVSPTVNPMSTA
CCCCCCCCCCHHHHH		25.9630108239
539UbiquitinationSHNRRVPKIGPYPDY
CCCCCCCCCCCCCCC		58.3929967540
546PhosphorylationKIGPYPDYSSSSYIE
CCCCCCCCCCCCHHH		13.1225884760
547PhosphorylationIGPYPDYSSSSYIED
CCCCCCCCCCCHHHH		30.9927642862
549PhosphorylationPYPDYSSSSYIEDSI
CCCCCCCCCHHHHHH		22.6327642862
550PhosphorylationYPDYSSSSYIEDSIH
CCCCCCCCHHHHHHC		31.8825884760
551PhosphorylationPDYSSSSYIEDSIHH
CCCCCCCHHHHHHCC		15.4125884760
555PhosphorylationSSSYIEDSIHHTDSI
CCCHHHHHHCCCHHH		15.8428348404
559PhosphorylationIEDSIHHTDSIVKNI
HHHHHCCCHHHHHHC		19.7828348404
561PhosphorylationDSIHHTDSIVKNISS
HHHCCCHHHHHHCCC		30.3627642862
564UbiquitinationHHTDSIVKNISSEHS
CCCHHHHHHCCCCCC		47.0629967540
567PhosphorylationDSIVKNISSEHSMSS
HHHHHHCCCCCCCCC		38.7823312004
568PhosphorylationSIVKNISSEHSMSST
HHHHHCCCCCCCCCC		35.2223312004
571PhosphorylationKNISSEHSMSSTPLT
HHCCCCCCCCCCCEE		19.1327050516
573PhosphorylationISSEHSMSSTPLTIG
CCCCCCCCCCCEECC		33.7923312004
574PhosphorylationSSEHSMSSTPLTIGE
CCCCCCCCCCEECCC		25.9623312004
575PhosphorylationSEHSMSSTPLTIGEK
CCCCCCCCCEECCCC		18.2723312004
578PhosphorylationSMSSTPLTIGEKNRN
CCCCCCEECCCCCCC		28.3023312004
586PhosphorylationIGEKNRNSINYERQQ
CCCCCCCCCCHHHHH		14.6921955146
589PhosphorylationKNRNSINYERQQAQA
CCCCCCCHHHHHHHH		15.7225884760
680PhosphorylationVDKNLKESSDENLME
HHHHHHHCCCHHHHH		41.3129255136
681PhosphorylationDKNLKESSDENLMEH
HHHHHHCCCHHHHHH		50.4629255136
689PhosphorylationDENLMEHSLKQFSGP
CHHHHHHHHHHHCCC		24.7723403867
694PhosphorylationEHSLKQFSGPDPLSS
HHHHHHHCCCCCCCC		47.0928348404
700PhosphorylationFSGPDPLSSTSSSLL
HCCCCCCCCCCHHHH		36.6428348404
701PhosphorylationSGPDPLSSTSSSLLY
CCCCCCCCCCHHHHH		39.7428348404
702PhosphorylationGPDPLSSTSSSLLYP
CCCCCCCCCHHHHHH		29.2928348404
703PhosphorylationPDPLSSTSSSLLYPL
CCCCCCCCHHHHHHH		21.6328348404
704PhosphorylationDPLSSTSSSLLYPLI
CCCCCCCHHHHHHHH		25.7028348404
705PhosphorylationPLSSTSSSLLYPLIK
CCCCCCHHHHHHHHH		23.3528348404
708PhosphorylationSTSSSLLYPLIKLAV
CCCHHHHHHHHHHHH		10.9825884760
756PhosphorylationQNLPKRPTSLPLNTK
CCCCCCCCCCCCCCC		47.1030266825
757PhosphorylationNLPKRPTSLPLNTKN
CCCCCCCCCCCCCCC		30.5830266825
762PhosphorylationPTSLPLNTKNSTKEP
CCCCCCCCCCCCCCC		39.0127251275
763UbiquitinationTSLPLNTKNSTKEPR
CCCCCCCCCCCCCCC		48.0723000965
765PhosphorylationLPLNTKNSTKEPRLK
CCCCCCCCCCCCCCC		42.2724719451
766PhosphorylationPLNTKNSTKEPRLKF
CCCCCCCCCCCCCCC		49.1428348404
767UbiquitinationLNTKNSTKEPRLKFG
CCCCCCCCCCCCCCC		66.5923000965
782UbiquitinationSKHKSNLKQVETGVA
HHHHHHHHHHHHHHH		57.4533845483
803PhosphorylationAAEPHVVTVTMNGVA
CCCCCEEEEEECCEE		14.79-
805O-linked_GlycosylationEPHVVTVTMNGVAGR
CCCEEEEEECCEECC		8.7828657654
805PhosphorylationEPHVVTVTMNGVAGR
CCCEEEEEECCEECC		8.78-
818PhosphorylationGRNHSVNSHAATTQY
CCCCCCCCCCCEEEC		16.6126425664
825PhosphorylationSHAATTQYANGTVLS
CCCCEEECCCCEEEC		10.43-
862PhosphorylationDTRLNINSSPDEHEP
CCCCCCCCCCCCCCH		39.1830266825
863PhosphorylationTRLNINSSPDEHEPL
CCCCCCCCCCCCCHH		31.7030266825
940PhosphorylationRRAQRPNSLDLSATN
CCCCCCCCCCCCCCE		26.4129978859
944PhosphorylationRPNSLDLSATNVLDG
CCCCCCCCCCEECCC		32.4928102081
946PhosphorylationNSLDLSATNVLDGSS
CCCCCCCCEECCCCC		23.6022617229
952PhosphorylationATNVLDGSSIQIGES
CCEECCCCCEEECCC		24.7629978859
953PhosphorylationTNVLDGSSIQIGEST
CEECCCCCEEECCCC		24.8430576142
959PhosphorylationSSIQIGESTQDGKSG
CCEEECCCCCCCCCC		26.5929978859
960PhosphorylationSIQIGESTQDGKSGS
CEEECCCCCCCCCCC		26.7830576142
965PhosphorylationESTQDGKSGSGEKIK
CCCCCCCCCCCHHHH		43.6629978859
967PhosphorylationTQDGKSGSGEKIKKR
CCCCCCCCCHHHHHH		51.3629978859
977PhosphorylationKIKKRVKTPYSLKRW
HHHHHCCCCCCCCCC		25.3022322096
979PhosphorylationKKRVKTPYSLKRWRP
HHHCCCCCCCCCCCC		31.6922322096
980PhosphorylationKRVKTPYSLKRWRPS
HHCCCCCCCCCCCCC		28.7224719451
1011PhosphorylationGSNRAVHSKSSTAVY
CCCCEEEECCCCEEE		27.8630576142
1013PhosphorylationNRAVHSKSSTAVYLA
CCEEEECCCCEEEEC		35.6222210691
1014PhosphorylationRAVHSKSSTAVYLAE
CEEEECCCCEEEECC		24.9122210691
1015PhosphorylationAVHSKSSTAVYLAEG
EEEECCCCEEEECCC		27.5122210691
1018PhosphorylationSKSSTAVYLAEGGTA
ECCCCEEEECCCCCE		9.5730576142
1024PhosphorylationVYLAEGGTATTMVSK
EEECCCCCEEEEEEC		31.5222210691
1026PhosphorylationLAEGGTATTMVSKDI
ECCCCCEEEEEECCC		18.4322210691
1027PhosphorylationAEGGTATTMVSKDIG
CCCCCEEEEEECCCC		17.0822210691
1030PhosphorylationGTATTMVSKDIGMNC
CCEEEEEECCCCCCC		17.4930576142
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 BMPR2_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 BMPR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EST3_HUMANCES3physical
15188402
GLR_HUMANGCGRphysical
15188402
ARP8_MOUSEActr8physical
15188402
ASNA_MOUSEAsna1physical
15188402
CRYAB_HUMANCRYABphysical
15188402
CTBP1_MOUSECtbp1physical
15188402
FRS3_HUMANFRS3physical
15188402
OC90_MOUSEOc90physical
15188402
KPCB_MOUSEPrkcbphysical
15188402
SPA3K_MOUSESerpina3kphysical
15188402
TBB5_MOUSETubb5physical
15188402
FOXL1_MOUSEFoxl1physical
15188402
LMX1A_MOUSELmx1aphysical
15188402
LSP1_MOUSELsp1physical
15188402
PZRN3_MOUSEPdzrn3physical
15188402
MPPA_MOUSEPmpcaphysical
15188402
TWF1_MOUSETwf1physical
15188402
PGTA_MOUSERabggtaphysical
15188402
TRPC1_MOUSETrpc1physical
15188402
TGFR1_HUMANTGFBR1physical
7791754
ACV1B_HUMANACVR1Bphysical
7791754
TSR1_HUMANTSR1physical
7791754
ACVR1_HUMANACVR1physical
7791754
BMR1A_HUMANBMPR1Aphysical
7791754
BMR1B_HUMANBMPR1Bphysical
7791754
BMP4_HUMANBMP4physical
7644468
BMP6_HUMANBMP6physical
10504300
GDF9_HUMANGDF9physical
12135884
BMPR2_HUMANBMPR2physical
10712517
ACVR1_HUMANACVR1physical
7890683
TGFR1_HUMANTGFBR1physical
7890683
FHL2_HUMANFHL2physical
19265191
XIAP_HUMANXIAPphysical
19782107
TRIB3_HUMANTRIB3physical
17576816
BMP4_HUMANBMP4physical
12045205
CAV1_HUMANCAV1physical
15657086
GDF2_HUMANGDF2physical
22718755
BMP10_HUMANBMP10physical
22718755
BMP7_HUMANBMP7physical
7644468
Drug and Disease Associations
Kegg Disease
H01300 Primary pulmonary hypertension (PPH); Pulmonary venoocclusive disease
OMIM Disease
178600Pulmonary hypertension, primary, 1 (PPH1)
265450Pulmonary venoocclusive disease 1, autosomal dominant (PVOD1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BMPR2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; THR-379; SER-513;SER-515; SER-680; SER-757 AND SER-862, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586; SER-680; SER-681;SER-757 AND SER-863, AND MASS SPECTROMETRY.

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