ALF_DROME - dbPTM
ALF_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALF_DROME
UniProt AC P07764
Protein Name Fructose-bisphosphate aldolase
Gene Name Ald
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 361
Subcellular Localization
Protein Description May take part in developmental stage-specific or tissue -specific sugar-phosphate metabolisms. Protein acts on two substrates fructose 1,6-bisphosphate and fructose 1-phosphate (like other class I aldolases)..
Protein Sequence MTTYFNYPSKELQDELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTDPKLAENISGVILFHETLYQKADDGTPFAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLARYASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQSAKKNTPEEIALATVQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAKANGDAAQGKYVAGSAGAGSGSLFVANHAY
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
2Acetylation------MTTYFNYPS
------CCCCCCCCC		30.151959612
36PhosphorylationGILAADESGPTMGKR
CEEEECCCCCCCCHH		51.0927794539
39PhosphorylationAADESGPTMGKRLQD
EECCCCCCCCHHHHH		41.9227794539
42AcetylationESGPTMGKRLQDIGV
CCCCCCCHHHHHHCC		38.8321791702
119PhosphorylationGVVPLFGSEDEVTTQ
CCEECCCCCCCHHCC		34.2427794539
161PhosphorylationIGKNTPSYQSILENA
ECCCCCCHHHHHHHH		13.9021082442
163PhosphorylationKNTPSYQSILENANV
CCCCCHHHHHHHHHH		22.4021082442
230AcetylationYLEGTLLKPNMVTAG
EEECEEECCCCCCCC		37.1421791702
346PhosphorylationQGKYVAGSAGAGSGS
CCCEEECCCCCCCCC		17.5021082442
351PhosphorylationAGSAGAGSGSLFVAN
ECCCCCCCCCEEEEC		25.3622668510
353PhosphorylationSAGAGSGSLFVANHA
CCCCCCCCEEEECCC		21.9721082442
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 ALF_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALF_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 ALF_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ALF_DROMEAldphysical
14605208
GPDA_DROMEGpdhphysical
22036573
INO1_DROMEInosphysical
22036573
MLR_DROMEMlc2physical
22036573
TPM2_DROMETm2physical
22036573
KARG_DROMEArgkphysical
22036573
MYSA_DROMEMhcphysical
22036573
ENO_DROMEEnophysical
22036573
MLC1_DROMEMlc1physical
22036573
SH3BG_DROMESh3betaphysical
22036573
TNNT_DROMEupphysical
22036573
FTN_DROMEflnphysical
22036573
LSP2_DROMELsp2physical
22036573
NLP_DROMENlpphysical
22036573
TNNI_DROMEwupAphysical
22036573
MYSP1_DROMEPrmphysical
22036573
MYSP2_DROMEPrmphysical
22036573
APLP_DROMERfabgphysical
22036573
YC17_DROMECG16817physical
22036573
GSTS1_DROMEGstS1physical
22036573
VIT3_DROMEYp3physical
22036573
NDKA_DROMEawdphysical
22036573
PGK_DROMEPgkphysical
22036573
ACTN_DROMEActnphysical
22036573
6PGD_DROMEPgdphysical
22036573
ANX10_DROMEAnxB10physical
22036573
CALR_DROMECrcphysical
22036573
TNNC1_DROMETpnC41Cphysical
22036573
NACA_DROMENacalphaphysical
22036573
PYG_DROMEGlyPphysical
22036573
UCHL_DROMEUchphysical
22036573
FKB12_DROMEFK506-bp2physical
22036573
G3P2_DROMEGapdh2physical
22036573
PCNA_DROMEPCNAphysical
22036573
TERA_DROMETER94physical
22036573
HCD2_DROMEscuphysical
22036573
VIT2_DROMEYp2physical
22036573
PICO_DROMEPicotphysical
22036573
ATP5J_DROMEATPsyn-Cf6physical
22036573
SODM_DROMESod2physical
22036573
ITPA_DROMECG8891physical
22036573
CISY_DROMEkdnphysical
22036573
ALF_DROMEAldphysical
12756285
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALF_DROME

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"The crystal structure of fructose-1,6-bisphosphate aldolase fromDrosophila melanogaster at 2.5-A resolution.";
Hester G., Brenner-Holzach O., Rossi F.A., Struck-Donatz M.,Winterhalter K.H., Smit J.D.G., Piontek K.;
FEBS Lett. 292:237-242(1991).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND ACETYLATION AT THR-2.
"Amino acid sequence of an invertebrate FBP aldolase (from Drosophilamelanogaster).";
Malek A.A., Suter F.X., Frank G., Brenner-Holzach O.;
Biochem. Biophys. Res. Commun. 126:199-205(1985).
Cited for: PROTEIN SEQUENCE OF 2-361 (ISOFORM GAMMA), AND ACETYLATION AT THR-2.

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