MYC_DROME - dbPTM
MYC_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYC_DROME
UniProt AC Q9W4S7
Protein Name Myc protein {ECO:0000312|FlyBase:FBgn0262656}
Gene Name Myc {ECO:0000303|PubMed:8929412, ECO:0000312|FlyBase:FBgn0262656}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 717
Subcellular Localization Nucleus . Cytoplasm . Transolcation from the cytoplasm to the nucleus may be promoted by the TORC2 complex (Lst8 and rictor).
Protein Description Participates in the regulation of gene transcription. [PubMed: 8929412]
Protein Sequence MALYRSDPYSIMDDQLFSNISIFDMDNDLYDMDKLLSSSTIQSDLEKIEDMESVFQDYDLEEDMKPEIRNIDCMWPAMSSCLTSGNGNGIESGNSAASSYSETGAVSLAMVSGSTNLYSAYQRSQTTDNTQSNQQHVVNSAENMPVIIKKELADLDYTVCQKRLRLSGGDKKSQIQDEVHLIPPGGSLLRKRNNQDIIRKSGELSGSDSIKYQRPDTPHSLTDEVAASEFRHNVDLRACVMGSNNISLTGNDSDVNYIKQISRELQNTGKDPLPVRYIPPINDVLDVLNQHSNSTGGQQQLNQQQLDEQQQAIDIATGRNTVDSPPTTGSDSDSDDGEPLNFDLRHHRTSKSGSNASITTNNNNSNNKNNKLKNNSNGMLHMMHITDHSYTRCNDMVDDGPNLETPSDSDEEIDVVSYTDKKLPTNPSCHLMGALQFQMAHKISIDHMKQKPRYNNFNLPYTPASSSPVKSVANSRYPSPSSTPYQNCSSASPSYSPLSVDSSNVSSSSSSSSSQSSFTTSSSNKGRKRSSLKDPGLLISSSSVYLPGVNNKVTHSSMMSKKSRGKKVVGTSSGNTSPISSGQDVDAMDRNWQRRSGGIATSTSSNSSVHRKDFVLGFDEADTIEKRNQHNDMERQRRIGLKNLFEALKKQIPTIRDKERAPKVNILREAAKLCIQLTQEEKELSMQRQLLSLQLKQRQDTLASYQMELNESRSVSG
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
217PhosphorylationIKYQRPDTPHSLTDE
CCCCCCCCCCCCCHH
26.1118327897
220PhosphorylationQRPDTPHSLTDEVAA
CCCCCCCCCCHHHHH
33.8818327897
461PhosphorylationYNNFNLPYTPASSSP
CCCCCCCCCCCCCCC
28.6425749252
560PhosphorylationVTHSSMMSKKSRGKK
CCHHHHHCCCCCCCC
28.4322817900
571PhosphorylationRGKKVVGTSSGNTSP
CCCCEECCCCCCCCC
14.2219429919
572PhosphorylationGKKVVGTSSGNTSPI
CCCEECCCCCCCCCC
30.2519429919
573PhosphorylationKKVVGTSSGNTSPIS
CCEECCCCCCCCCCC
35.5819429919
576PhosphorylationVGTSSGNTSPISSGQ
ECCCCCCCCCCCCCC
39.1319429919
577PhosphorylationGTSSGNTSPISSGQD
CCCCCCCCCCCCCCC
25.0019429919
580PhosphorylationSGNTSPISSGQDVDA
CCCCCCCCCCCCCCC
31.6219429919
581PhosphorylationGNTSPISSGQDVDAM
CCCCCCCCCCCCCCC
40.9919429919

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 MYC_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYC_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 MYC_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THOC7_DROMEthoc7physical
14605208
OCTB2_DROMEOctbeta2Rphysical
14605208
ELG_DROMEEts97Dphysical
14605208
MAX_DROMEMaxphysical
14605208
GROU_DROMEgrophysical
17898168
UBE2S_DROMECG8188physical
19364825
KDM5_DROMElidphysical
17311883
ASH2_DROMEash2physical
17311883
BRM_DROMEbrmphysical
17311883
AST4_DROMEscgenetic
21220321
SQH_DROMEsqhgenetic
26287461
SISA_DROMEsisAgenetic
21220321
HEP_DROMEhepgenetic
15066286
RUNT_DROMErungenetic
21220321
RPA2_DROMERpI135genetic
15723055
DECA_DROMEdppgenetic
15066287
KDM5_DROMElidgenetic
17311883
KDM5_DROMElidgenetic
21124823
REF2P_DROMEref(2)Pgenetic
23950728
DIA_DROMEdiagenetic
26287461
LTV1_DROMECG7686genetic
25858587
SUZ2_DROMESu(z)2genetic
17311883
TFDP_DROMEDpgenetic
15084262
ASX_DROMEAsxgenetic
17311883
CADE_DROMEshggenetic
26287461
YAP1_DROMEykigenetic
22069188
PUF68_DROMEpUf68genetic
14993190
FBXW7_DROMEagogenetic
17311883
FBXW7_DROMEagogenetic
24173801
FBXW7_DROMEagogenetic
15182669
ERCC3_DROMEhaygenetic
26074141
FLOWR_DROMEfwegenetic
20627080
BRM_DROMEbrmgenetic
17311883
DIAP1_DROMEthgenetic
26287461
RUVB2_DROMEreptgenetic
16087886
MAX_DROMEMaxgenetic
19165923
E2AK3_DROMEPEKgenetic
23950728
CNC_DROMEcncgenetic
23950728
ASH2_DROMEash2genetic
17311883
ASH2_DROMEash2genetic
20937797
ELG_DROMEEts97Dgenetic
19742324
HCF_DROMEHcfgenetic
20937797
RL8_DROMERpL8genetic
18957936
RUVB1_DROMEpontgenetic
16087886
INSL5_DROMEIlp5genetic
23608455
LSG1_DROMENs3physical
27626673
RSSA_DROMEstaphysical
27626673
LVA_DROMElvaphysical
27626673
MLC2_DROMEMlc-cphysical
27626673
RL7A_DROMERpL7Aphysical
27626673
RL17_DROMERpL17physical
27626673
RS6_DROMERpS6physical
27626673
HSP7C_DROMEHsc70-3physical
27626673
HANG_DROMEhangphysical
27626673
FLII_DROMEfliIphysical
27626673
RLA1_DROMERpLP1physical
27626673
KDM5_DROMElidphysical
21124823
RS23_DROMERpS23physical
27626673
RLA2_DROMERpLP2physical
27626673
RL18A_DROMERpL18Aphysical
27626673
ACT3_DROMEAct57Bphysical
27626673
RS16_DROMERpS16physical
27626673
RL19_DROMERpL19physical
27626673
SPTCA_DROMEalpha-Specphysical
27626673
RL28_DROMERpL28physical
27626673
SARM1_DROMEEct4physical
27626673
RS17_DROMERpS17physical
27626673
RS9_DROMERpS9physical
27626673
R10AB_DROMERpL10Abphysical
27626673
MAX_DROMEMaxphysical
27626673
MAX_DROMEMaxphysical
19165923
VATE_DROMEVha26physical
27626673
RL13A_DROMERpL13Aphysical
27626673
HYD_DROMEhydphysical
27626673
TCPA_DROMET-cp1physical
27626673
RL4_DROMERpL4physical
27626673
RS7_DROMERpS7physical
27626673
HCF_DROMEHcfphysical
20937797
GAWKY_DROMEgwphysical
27626673
KCC2A_DROMECaMKIIphysical
27626673
CSK2A_DROMECkIIalphaphysical
27626673
ANKHM_DROMEmaskphysical
27626673
LARP_DROMElarpphysical
27626673
CAPR1_DROMECaprphysical
27626673

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYC_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 THR-217 AND SER-220, ANDMASS SPECTROMETRY.

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