MAD_DROME - dbPTM
MAD_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAD_DROME
UniProt AC P42003
Protein Name Protein mothers against dpp
Gene Name Mad
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 455
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Required for the function of decapentaplegic. May play an important role in mediating Dpp signaling. Involved in the BMP signaling pathway..
Protein Sequence MDTDDVESNTSSAMSTLGSLFSFTSPAVKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKGAIEELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLELCQYPFSAKQKEVCINPYHYKRVESPVLPPVLVPRHSEFAPGHSMLQFNHVAEPSMPHNVSYSNSGFNSHSLSTSNTSVGSPSSVNSNPNSPYDSLAGTPPPAYSPSEDGNSNNPNDGGQLLDAQMGDVAQVSYSEPAFWASIAYYELNCRVGEVFHCNNNSVIVDGFTNPSNNSDRCCLGQLSNVNRNSTIENTRRHIGKGVHLYYVTGEVYAECLSDSAIFVQSRNCNYHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNNGFEAVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNAISSVS
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
25PhosphorylationGSLFSFTSPAVKKLL
HHHHHCCCHHHHHHH
14.6217507407
453PhosphorylationSPHNAISSVS-----
CCCHHHCCCC-----
21.9218327897
455PhosphorylationHNAISSVS-------
CHHHCCCC-------
36.1318327897

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 MAD_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 MAD_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUMB_DROMEnumbphysical
14605208
CPN_DROMECpnphysical
14605208
UBCD2_DROMEUbcD2physical
14605208
BCD_DROMEbcdphysical
15575970
2ABA_DROMEtwsphysical
15575970
NPL4_DROMENpl4physical
15575970
DAN_DROMEdanphysical
15575970
COG5_DROMEfwsphysical
15575970
BOWEL_DROMEbowlphysical
15575970
MED15_DROMEMED15physical
15575970
PANG1_DROMEpanphysical
15575970
PANG2_DROMEpanphysical
15575970
TAMO_DROMEtamophysical
15575970
SUDX_DROMESu(dx)physical
15575970
VPS18_DROMEdorphysical
15575970
SMUF1_DROMElackphysical
15575970
Y3427_DROMECG43427physical
15575970
YAP1_DROMEykiphysical
19914168
EYA_DROMEeyagenetic
10683184
WNTG_DROMEwggenetic
21990430
YAP1_DROMEykigenetic
21238929
INHB_DROMEActbetagenetic
18820452
ERKA_DROMErlgenetic
17507407
ARM_DROMEarmphysical
21990430
CNEP1_DROMEDdphysical
27578171
MAD_DROMEMadphysical
9693372
MAD_DROMEMadphysical
19557331
FOXF_DROMEbinphysical
23935523
PANG1_DROMEpanphysical
21990430
PANG2_DROMEpanphysical
21990430

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453 AND SER-455, ANDMASS SPECTROMETRY.
"Drosophila Nemo antagonizes BMP signaling by phosphorylation of Madand inhibition of its nuclear accumulation.";
Zeng Y.A., Rahnama M., Wang S., Sosu-Sedzorme W., Verheyen E.M.;
Development 134:2061-2071(2007).
Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-25.
"DSmurf selectively degrades decapentaplegic-activated MAD, and itsoverexpression disrupts imaginal disc development.";
Liang Y.-Y., Lin X., Liang M., Brunicardi F.C., ten Dijke P., Chen Z.,Choi K.-W., Feng X.-H.;
J. Biol. Chem. 278:26307-26310(2003).
Cited for: INTERACTION WITH LACK, PHOSPHORYLATION AT SER-453 AND SER-455,MUTAGENESIS OF SER-453 AND SER-455, AND UBIQUITINATION.

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