SCR_DROME - dbPTM
SCR_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCR_DROME
UniProt AC P09077
Protein Name Homeotic protein Sex combs reduced
Gene Name Scr
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 417
Subcellular Localization Nucleus.
Protein Description Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Controls the segmental transformation of the first to the second thoracic segment (prothorax to mesothorax) and of the labial palps into maxillary palps. In embryo, required for fusion of labial lobes and development of the T1 denticle belt. In adult, expression in the head is necessary for proper development of the labium. In the first thoracic segment of the adult, required for proper development of the sex comb and to suppress improper prothoracic wing development..
Protein Sequence MDPDCFAMSSYQFVNSLASCYPQQMNPQQNHPGAGNSSAGGSGGGAGGSGGVVPSGGTNGGQGSAGAATPGANDYFPAAAAYTPNLYPNTPQAHYANQAAYGGQGNPDMVDYTQLQPQRLLLQQQQQQQQQQHAHAAAAVAAQQQQQLAQQQHPQQQQQQQQANISCKYANDPVTPGGSGGGGVSGSNNNNNSANSNNNNSQSLASPQDLSTRDISPKLSPSSVVESVARSLNKGVLGGSLAAAAAAAGLNNNHSGSGVSGGPGNVNVPMHSPGGGDSDSESDSGNEAGSSQNSGNGKKNPPQIYPWMKRVHLGTSTVNANGETKRQRTSYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKEHKMASMNIVPYHMGPYGHPYHQFDIHPSQFAHLSA
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
216PhosphorylationDLSTRDISPKLSPSS
HCCCCCCCCCCCHHH
21.9222817900

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 SCR_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCR_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 SCR_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCL_DROMEPclgenetic
6813190
HMPB_DROMEpbgenetic
10322642
HMPB_DROMEpbgenetic
16094438
HTH_DROMEhthgenetic
10395787
MED13_DROMEskdgenetic
11090137
HMG2_DROMEDsp1genetic
11139505
EXD_DROMEexdphysical
17981120
EXD_DROMEexdphysical
10398683
EXD_DROMEexdphysical
20634319
SLP2_DROMEslp2physical
25869471
EYA_DROMEeyaphysical
25869471
TF2B_DROMETfIIBphysical
25869471
SALM_DROMEsalmphysical
25869471
SUH_DROMESu(H)physical
25869471
TSH_DROMEtshphysical
25869471
APTE_DROMEapphysical
25869471
MEF2_DROMEMef2physical
25869471
EVE_DROMEevephysical
25869471
MAM_DROMEmamphysical
25869471
TWIST_DROMEtwiphysical
25869471
DLL_DROMEDllphysical
25869471
MED19_DROMEMED19physical
24786462
KNIR_DROMEkniphysical
25869471
SCR_DROMEScrphysical
22564794
SCR_DROMEScrphysical
26428533
POXM_DROMEPoxmphysical
25869471
HTH_DROMEhthphysical
20634319
EMS_DROMEemsphysical
25869471
SRP_DROMEsrpphysical
25869471
TIN_DROMEtinphysical
25869471
BAGP_DROMEbapphysical
25869471
SLOU_DROMEslouphysical
25869471
PNT1_DROMEpntphysical
25869471
PNT2_DROMEpntphysical
25869471
MYOD_DROMEnauphysical
25869471
ZFH1_DROMEzfh1physical
25869471
PNR_DROMEpnrphysical
25869471
COLL_DROMEknphysical
25869471

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SCR_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-216, AND MASSSPECTROMETRY.

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