FOG_DROME - dbPTM
FOG_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOG_DROME
UniProt AC P40795
Protein Name Protein folded gastrulation
Gene Name fog
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 730
Subcellular Localization Secreted, extracellular space, extracellular matrix .
Protein Description Coordinates cell shape changes during formation of the ventral furrow and invagination of the posterior midgut primordium, by inducing apical constriction of cells in spatially and temporally defined manners. Could function as a secreted signal to initiate apical constriction by acting as a ligand for an unidentified G protein-coupled receptor, which in turn activates the G protein alpha subunit encoded by concertina, in neighboring cells. Such an intracellular pathway would ultimately induce contraction of the apical actin-myosin network. In the ventral furrow, fog appears to ensure that all the cells initiate constriction within several minutes of each other. In the posterior midgut invagination, fog appears to direct the ordered progression of constriction initiations out from a central region and also to delimit the peripheral extent of this spreading..
Protein Sequence MSPPNCLLAVLALTVFIGANNALPITSRPIEGNVQRMVWEDWVNLDPEQRNLTKEKKITAKSIFTLPFRHCPQGHTLFNQLCIPQSNIDPTDLVKQELILAGGSNGSPPPPPIGDYDYGDDEESEEIVYDLSVIPTAMQDGLPPSVGTGDQALPSEDAPLKFNIFEKKFPTGTGEHEEMPLPPDMAAATYAKNISTTPETSTSITPTSTTTFAVPSVPSGEASNRIPGGVDLLAAPSDAFSTSTTLSMPTSNTTTTSNKDIGQVESIVLPADQEHDGLVHLVTSSLSDNDSDDSSTTLNGFNAEADLAQLLKVDAFWPVYDGSIELLPPLFSHRKVAPPLSADQDVKTKHAVDAAEKVGAELEEEVGEEEVTATDILPSEEDEYTTETATTTGDTTVAEASMDTSTATSTSGQSSPHPPEEPEIDERENRLVLIKSKVQPVQLTTTTSATATTAADVANSSSSTDRFHYQHFVEDESSTTTATPEPSSSTPGDPIEQSDMPASDNDNLMTNTIGGRGDDDDDGGHKATSEIHVQQELRLINELVKGKQRQQHQPQKQQLEPTSTEITSALTSTSTEDATTTTTTTTAYTNWSKVMPQLGQSTSETAATTETVATSGQVNEISLTATSASTEVKHFSITNRSYRNSKIIREDRLTVEPEGIVESAASTESAGTAATTPNSSSNPDGYTPLWWLPSIGWRLDRHLDGNGEDQSLLLRFFSTFRGSNTAATTR
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
51N-linked_GlycosylationNLDPEQRNLTKEKKI
CCCHHHCCCCCCCCC
52.32-
193N-linked_GlycosylationAAATYAKNISTTPET
HHHHHEECCCCCCCC
25.85-
252N-linked_GlycosylationTLSMPTSNTTTTSNK
EEECCCCCCCCCCCC
43.87-
289N-linked_GlycosylationVTSSLSDNDSDDSST
EECCCCCCCCCCCCC
47.51-
459N-linked_GlycosylationTTAADVANSSSSTDR
CCHHHHHCCCCCCCC
42.12-
590N-linked_GlycosylationTTTTAYTNWSKVMPQ
EEEEEECCHHHHCHH
28.48-
639N-linked_GlycosylationVKHFSITNRSYRNSK
EEEEEEECCCHHCCE
29.27-
678N-linked_GlycosylationGTAATTPNSSSNPDG
CCCCCCCCCCCCCCC
53.05-

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 FOG_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOG_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 FOG_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MARF_DROMEMarfgenetic
24101729
MTH1_DROMEmthl1genetic
24222713
GNAL_DROMEctagenetic
24101729

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

loading...

Related Literatures of Post-Translational Modification

TOP