JRA_DROME - dbPTM
JRA_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JRA_DROME
UniProt AC P18289
Protein Name Transcription factor AP-1
Gene Name Jra
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 289
Subcellular Localization Nucleus .
Protein Description Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. [PubMed: 1696724]
Protein Sequence MKTPVSAAANLSIQNAGSSGATAIQIIPKTEPVGEEGPMSLDFQSPNLNTSTPNPNKRPGSLDLNSKSAKNKRIFAPLVINSPDLSSKTVNTPDLEKILLSNNLMQTPQPGKVFPTKAGPVTVEQLDFGRGFEEALHNLHTNSQAFPSANSAANSAANNTTAAAMTAVNNGISGGTFTYTNMTEGFSVIKDEPVNQASSPTVNPIDMEAQEKIKLERKRQRNRVAASKCRKRKLERISKLEDRVKVLKGENVDLASIVKNLKDHVAQLKQQVMEHIAAGCTVPPNSTDQ
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
61PhosphorylationNPNKRPGSLDLNSKS
CCCCCCCCCCCCCCC		22.7619429919
82PhosphorylationFAPLVINSPDLSSKT
EEEEEECCCCCCCCC		14.5219429919
86PhosphorylationVINSPDLSSKTVNTP
EECCCCCCCCCCCCC		36.8523607784
89PhosphorylationSPDLSSKTVNTPDLE
CCCCCCCCCCCCCHH		22.4219429919
92PhosphorylationLSSKTVNTPDLEKIL
CCCCCCCCCCHHHHH		17.5319429919
101PhosphorylationDLEKILLSNNLMQTP
CHHHHHHHCCCCCCC		21.8919429919
107PhosphorylationLSNNLMQTPQPGKVF
HHCCCCCCCCCCCCC		15.2119429919
112AcetylationMQTPQPGKVFPTKAG
CCCCCCCCCCCCCCC		47.5921791702
198PhosphorylationDEPVNQASSPTVNPI
CCCCCCCCCCCCCCC		27.3819429919
199PhosphorylationEPVNQASSPTVNPID
CCCCCCCCCCCCCCC		27.8319429919
201PhosphorylationVNQASSPTVNPIDME
CCCCCCCCCCCCCHH		34.5619429919
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 JRA_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JRA_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 JRA_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JRA_DROMEJraphysical
14605208
PEPT1_DROMEyinphysical
14605208
TPM1_DROMETm1physical
14605208
TPM4_DROMETm1physical
14605208
FOSLD_DROMEkayphysical
22036573
FOSLA_DROMEkayphysical
22036573
MOC2B_DROMEMocs2physical
20813260
NC2B_DROMENC2betaphysical
20813260
FOSLD_DROMEkayphysical
23661758
FOSLA_DROMEkayphysical
23661758
POK_DROMEaopgenetic
8521492
PHYL_DROMEphylgenetic
8521492
MBL_DROMEmblgenetic
9334280
PNT1_DROMEpntgenetic
18291359
PNT2_DROMEpntgenetic
18291359
PNT1_DROMEpntgenetic
8521492
PNT2_DROMEpntgenetic
8521492
PNT1_DROMEpntgenetic
10903185
PNT2_DROMEpntgenetic
10903185
FOSLD_DROMEkaygenetic
18832361
FOSLA_DROMEkaygenetic
18832361
HP1_DROMESu(var)205physical
25945750
FOSLD_DROMEkayphysical
2116361
FOSLA_DROMEkayphysical
2116361
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of JRA_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASSSPECTROMETRY.

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