FOXO_DROME - dbPTM
FOXO_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOXO_DROME
UniProt AC Q95V55
Protein Name Forkhead box protein O {ECO:0000303|PubMed:12893776}
Gene Name foxo {ECO:0000312|EMBL:AAS65148.1}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 613
Subcellular Localization Cytoplasm . Nucleus . When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation.
Protein Description Transcription factor involved in the regulation of the insulin signaling pathway. Consistently activates both the downstream target Thor\d4EBP and the feedback control target InR. Involved in negative regulation of the cell cycle, modulating cell growth and proliferation. In response to cellular stresses, such as nutrient deprivation or increased levels of reactive oxygen species, foxo is activated and inhibits growth through the action of target genes such as Thor. Foxo activated in the adult fat body can regulate lifespan in adults; an insulin peptide itself may function as one secondary messenger of insulin-regulated aging. Also regulates Lip4, homolog of human acid lipases, thereby acting as a key modulator of lipid metabolism by insulin signaling and integrates insulin responses to glucose and lipid homeostasis..
Protein Sequence MMDGYAQEWPRLTHTDNGLAMDQLGGDLPLDVGFEPQTRARSNTWPCPRPENFVEPTDELDSTKASNQQLAPGDSQQAIQNANAAKKNSSRRNAWGNLSYADLITHAIGSATDKRLTLSQIYEWMVQNVPYFKDKGDSNSSAGWKNSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRGRAKKRVEALRQAGVVGLNDATPSPSSSVSEGLDHFPESPLHSGGGFQLSPDFRQRASSNASSCGRLSPIRAQDLEPDWGFPVDYQNTTMTQAHAQALEELTGTMADELTLCNQQQQGFSAASGLPSQPPPPPYQPPQHQQAQQQQQQQSPYALNGPASGYNTLQPQSQCLLHRSLNCSCMHNARDGLSPNSVTTTMSPAYPNSEPSSDSLNTYSNVVLDGPADTAALMVQQQQQQQQQQQLSASLEGQCLEVLNNEAQPIDEFNLENFPVGNLECNVEELLQQEMSYGGLLDINIPLATVNTNLVNSSSGPLSISNISNLSNISSNSGSSLSLNQLQAQLQQQQQQQQAQQQQQAQQQQQQHQQHQQQLLLNNNNNSSSSLELATQTATTNLNARVQYSQPSVVTSPPSWVH
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
44PhosphorylationQTRARSNTWPCPRPE
CCCCCCCCCCCCCCH		31.8412893776
66PhosphorylationELDSTKASNQQLAPG
CCCCCCCCCCCCCCC		36.4127794539
75PhosphorylationQQLAPGDSQQAIQNA
CCCCCCCHHHHHHHH		30.0618327897
190PhosphorylationSVRRRAASMETSRYE
HHHHHHHHHHCHHHH		19.0325749252
259PhosphorylationDFRQRASSNASSCGR
HHHHHHHCCCCCCCC		35.1222817900
262PhosphorylationQRASSNASSCGRLSP
HHHHCCCCCCCCCCC		30.3422817900
263PhosphorylationRASSNASSCGRLSPI
HHHCCCCCCCCCCCC		20.4122817900
268PhosphorylationASSCGRLSPIRAQDL
CCCCCCCCCCCHHCC		19.5419429919
268 (in isoform 2)Phosphorylation-19.5418327897
268 (in isoform 4)Phosphorylation-19.5418327897
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
44TPhosphorylationKinaseAKT1Q8INB9
Uniprot
190SPhosphorylationKinaseAKT1Q8INB9
Uniprot
259SPhosphorylationKinaseAKT1Q8INB9
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOXO_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 FOXO_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
USP_DROMEuspgenetic
25421296
HEP_DROMEhepgenetic
15820683
NOS_DROMENosgenetic
22393355
RAS2_DROMERas64Bgenetic
12844367
AKT1_DROMEAkt1genetic
25889856
AKT1_DROMEAkt1genetic
12844367
AKT1_DROMEAkt1genetic
12893776
AKT1_DROMEAkt1genetic
15843412
AKT1_DROMEAkt1genetic
18827008
AKT1_DROMEAkt1genetic
20624856
1433E_DROME14-3-3epsilongenetic
18665908
GCYH_DROMEGycalpha99Bgenetic
22393355
JNK_DROMEbskgenetic
15820683
KGP25_DROMEforgenetic
22393355
KGP24_DROMEforgenetic
22393355
PP2A_DROMEmtsgenetic
18827008
RHEB_DROMERhebgenetic
15843412
FUTSC_DROMEfutschgenetic
22312004
RHEB_DROMERhebphysical
27626673
ARM_DROMEarmphysical
26936649
USP_DROMEuspphysical
25421296
ACT1_DROMEAct5Cphysical
27626673
RL7A_DROMERpL7Aphysical
27626673
RL17_DROMERpL17physical
27626673
RS6_DROMERpS6physical
27626673
NOP53_DROMECG1785physical
27626673
NAT10_DROMEl(1)G0020physical
27626673
HSP7C_DROMEHsc70-3physical
27626673
RRP12_DROMECG2691physical
27626673
CLH_DROMEChcphysical
27626673
NONA_DROMEnonAphysical
27626673
CLSPN_DROMEClaspinphysical
27626673
RS5A_DROMERpS5aphysical
27626673
RPA2_DROMERpI135physical
27626673
RLA1_DROMERpLP1physical
27626673
RL15_DROMERpL15physical
27626673
EIF3I_DROMETrip1physical
27626673
Y3096_DROMECG13096physical
27626673
PESC_DROMECG4364physical
27626673
RL9_DROMERpL9physical
27626673
RS26_DROMERpS26physical
27626673
MLE_DROMEmlephysical
27626673
1433Z_DROME14-3-3zetaphysical
22068330
1433Z_DROME14-3-3zetaphysical
27626673
RS11_DROMERpS11physical
27626673
ISWI_DROMEIswiphysical
27626673
RS23_DROMERpS23physical
27626673
RPA1_DROMERpI1physical
27626673
RLA2_DROMERpLP2physical
27626673
EIF3B_DROMEeIF3-S9physical
27626673
RL18A_DROMERpL18Aphysical
27626673
EIF3C_DROMEeIF3-S8physical
27626673
41_DROMEcoraphysical
27626673
EIF3K_DROMECG10306physical
27626673
HMGD_DROMEHmgDphysical
27626673
RL23_DROMERpL23physical
27626673
FBRL_DROMEFibphysical
27626673
DKC1_DROMENop60Bphysical
27626673
RL19_DROMERpL19physical
27626673
SPTCA_DROMEalpha-Specphysical
27626673
RL18_DROMERpL18physical
27626673
SARM1_DROMEEct4physical
27626673
RL14_DROMERpL14physical
27626673
RS17_DROMERpS17physical
27626673
RS9_DROMERpS9physical
27626673
AGO2_DROMEAGO2physical
27626673
BRM_DROMEbrmphysical
27626673
EIF3E_DROMEInt6physical
27626673
CHDM_DROMEMi-2physical
27626673
EIF3A_DROMEeIF3-S10physical
27626673
EI3F1_DROMECG9769physical
27626673
RL13A_DROMERpL13Aphysical
27626673
DDX17_DROMERm62physical
27626673
SLE_DROMEslephysical
27626673
T2FB_DROMETfIIFbetaphysical
27626673
Y6693_DROMECG6693physical
27626673
DDB1_DROMEpicphysical
27626673
SQD_DROMEsqdphysical
27626673
RRP15_DROMECG3817physical
27626673
CAF1_DROMECaf1physical
27626673
1433E_DROME14-3-3epsilonphysical
22068330
1433E_DROME14-3-3epsilonphysical
27626673
DDX18_DROMEpitphysical
27626673
TCPA_DROMET-cp1physical
27626673
PRS4_DROMERpt2physical
27626673
RS19B_DROMERpS19bphysical
27626673
KPEL_DROMEpllphysical
26474173
ROA1_DROMEHrb98DEphysical
27626673
RS7_DROMERpS7physical
27626673
PANG1_DROMEpanphysical
26936649
PANG2_DROMEpanphysical
26936649
PAX6_DROMEeyphysical
26555050
RL10_DROMERpL10physical
27626673
EIF3H_DROMEeIF-3p40physical
27626673
COPB2_DROMEbetaCOPphysical
27626673
TTF2_DROMEldsphysical
27626673
METK_DROMESam-Sphysical
27626673
LARP_DROMElarpphysical
27626673
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FOXO_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-75; SER-262; SER-263 ANDSER-268, AND MASS SPECTROMETRY.
"Control of cell number by Drosophila FOXO: downstream and feedbackregulation of the insulin receptor pathway.";
Puig O., Marr M.T., Ruhf M.L., Tjian R.;
Genes Dev. 17:2006-2020(2003).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULARLOCATION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT THR-44; SER-190 ANDSER-259, AND MUTAGENESIS OF THR-44; SER-190 AND SER-259.

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