AKT1_DROME - dbPTM
AKT1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AKT1_DROME
UniProt AC Q8INB9
Protein Name RAC serine/threonine-protein kinase
Gene Name Akt1 {ECO:0000312|FlyBase:FBgn0010379}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 611
Subcellular Localization Cytoplasm, cytosol. Cell membrane. Recruited to plasma membrane upon activation.
Protein Description Serine/threonine kinase involved in various developmental processes. [PubMed: 10587646]
Protein Sequence MNYLPFVLQRRSTVVASAPAPGSASRIPESPTTTGSNIINIIYSQSTHPNSSPTSGSAEKFSWQQSWPSRTSAAPTHDSGTMSINTTFDLSSPSVTSGHALTEQTQVVKEGWLMKRGEHIKNWRQRYFVLHSDGRLMGYRSKPADSASTPSDFLLNNFTVRGCQIMTVDRPKPFTFIIRGLQWTTVIERTFAVESELERQQWTEAIRNVSSRLIDVGEVAMTPSEQTDMTDVDMATIAEDELSEQFSVQGTTCNSSGVKKVTLENFEFLKVLGKGTFGKVILCREKATAKLYAIKILKKEVIIQKDEVAHTLTESRVLKSTNHPFLISLKYSFQTNDRLCFVMQYVNGGELFWHLSHERIFTEDRTRFYGAEIISALGYLHSQGIIYRDLKLENLLLDKDGHIKVADFGLCKEDITYGRTTKTFCGTPEYLAPEVLDDNDYGQAVDWWGTGVVMYEMICGRLPFYNRDHDVLFTLILVEEVKFPRNITDEAKNLLAGLLAKDPKKRLGGGKDDVKEIQAHPFFASINWTDLVLKKIPPPFKPQVTSDTDTRYFDKEFTGESVELTPPDPTGPLGSIAEEPLFPQFSYQGDMASTLGTSSHISTSTSLASMQ
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
12PhosphorylationPFVLQRRSTVVASAP
HHHEEECCEEEEECC		27.9519429919
13PhosphorylationFVLQRRSTVVASAPA
HHEEECCEEEEECCC		19.7219429919
30PhosphorylationSASRIPESPTTTGSN
CHHCCCCCCCCCCCC		23.3822817900
36PhosphorylationESPTTTGSNIINIIY
CCCCCCCCCEEEEEE		23.8221082442
44PhosphorylationNIINIIYSQSTHPNS
CEEEEEEECCCCCCC		13.7721082442
46PhosphorylationINIIYSQSTHPNSSP
EEEEEECCCCCCCCC		23.8121082442
47PhosphorylationNIIYSQSTHPNSSPT
EEEEECCCCCCCCCC		33.4421082442
51PhosphorylationSQSTHPNSSPTSGSA
ECCCCCCCCCCCCCC		41.9921082442
52PhosphorylationQSTHPNSSPTSGSAE
CCCCCCCCCCCCCCC		38.5522668510
54PhosphorylationTHPNSSPTSGSAEKF
CCCCCCCCCCCCCCC		47.9021082442
66PhosphorylationEKFSWQQSWPSRTSA
CCCCCCCCCCCCCCC		26.3422817900
148PhosphorylationSKPADSASTPSDFLL
CCCCCCCCCCCHHHH		44.8121082442
149PhosphorylationKPADSASTPSDFLLN
CCCCCCCCCCHHHHC		26.9121082442
151PhosphorylationADSASTPSDFLLNNF
CCCCCCCCHHHHCCC		40.8721082442
184PhosphorylationIIRGLQWTTVIERTF
EEECCEEEEEEEEEE		9.7519429919
185PhosphorylationIRGLQWTTVIERTFA
EECCEEEEEEEEEEE		19.2719429919
586PhosphorylationEPLFPQFSYQGDMAS
CCCCCCCCCCCCHHH		15.9915718470
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 AKT1_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AKT1_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 AKT1_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VTU2_DROMEVm26Abphysical
15575970
CCNC_DROMECycCphysical
15575970
GUS_DROMEgusphysical
15575970
PGAM5_DROMEPgam5physical
15575970
FRY_DROMEfryphysical
15575970
RAD51_DROMEspn-Aphysical
15575970
CEG1A_DROMECenG1Aphysical
15575970
ENA_DROMEenaphysical
15575970
MED15_DROMEMED15physical
15575970
MSIR6_DROMERbp6physical
15575970
ECR_DROMEEcRphysical
15575970
GSB_DROMEgsbphysical
15575970
FOXO_DROMEfoxophysical
12893776
SESN_DROMESesngenetic
20203043
PDPK1_DROMEPdk1genetic
11344272
PTP61_DROMEPtp61Fgenetic
24752400
FOXO_DROMEfoxogenetic
25889856
FOXO_DROMEfoxogenetic
12908874
2AAA_DROMEPp2A-29Bphysical
27626673
RL17_DROMERpL17physical
27626673
OST48_DROMEOst48physical
27626673
CH60_DROMEHsp60physical
27626673
HSP7C_DROMEHsc70-3physical
27626673
UBE2N_DROMEbenphysical
27626673
CLH_DROMEChcphysical
27626673
IF2A_DROMEeIF-2alphaphysical
27626673
PRS8_DROMERpt6physical
27626673
RLA1_DROMERpLP1physical
27626673
CAPZB_DROMEcpbphysical
27626673
DX39B_DROMEHel25Ephysical
27626673
IF4A_DROMEeIF-4aphysical
27626673
GBLP_DROMERack1physical
27626673
RL9_DROMERpL9physical
27626673
NFS1_DROMECG12264physical
27626673
MET13_DROMECG2614physical
27626673
EF2_DROMEEF2physical
27626673
RL31_DROMERpL31physical
27626673
TERA_DROMETER94physical
27626673
EF1A1_DROMEEf1alpha48Dphysical
27626673
ADRM1_DROMERpn13physical
27626673
HSP7E_DROMEHsc70-5physical
27626673
CLU_DROMEcluphysical
27626673
HTS_DROMEhtsphysical
27626673
PCNA_DROMEPCNAphysical
27626673
ACT3_DROMEAct57Bphysical
27626673
CAPZA_DROMEcpaphysical
27626673
TUD_DROMEtudphysical
27626673
RS16_DROMERpS16physical
27626673
ATPA_DROMEblwphysical
27626673
RL23_DROMERpL23physical
27626673
TBB3_DROMEbetaTub60Dphysical
27626673
ROP_DROMERopphysical
27626673
ACADM_DROMECG12262physical
27626673
RS17_DROMERpS17physical
27626673
RS9_DROMERpS9physical
27626673
FAXC_DROMEfaxphysical
27626673
LONM_DROMELonphysical
27626673
PSMD4_DROMERpn10physical
27626673
ARF1_DROMEArf79Fphysical
27626673
GMPPB_DROMECG1129physical
27626673
TCTP_DROMETctpphysical
27626673
DDB1_DROMEpicphysical
27626673
SQD_DROMEsqdphysical
27626673
IF2G_DROMEeIF-2gammaphysical
27626673
UMPS_DROMEr-lphysical
27626673
KPYK_DROMEPyKphysical
27626673
TCPA_DROMET-cp1physical
27626673
PRS4_DROMERpt2physical
27626673
ATPG_DROMEATPsyn-gammaphysical
27626673
DRICE_DROMEIcephysical
27626673
RS7_DROMERpS7physical
27626673
ATPB_DROMEATPsyn-betaphysical
27626673
RS15A_DROMERpS15Aaphysical
27626673
VATA2_DROMEVha68-2physical
27626673
LDH_DROMEImpL3physical
27626673
SGPL_DROMESplyphysical
27626673
METK_DROMESam-Sphysical
27626673
TID_DROMEl(2)tidphysical
27626673
ATNA_DROMEAtpalphaphysical
27626673
ATC1_DROMECa-P60Aphysical
27626673
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AKT1_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-30, AND MASSSPECTROMETRY.
"Phosphorylation and regulation of Akt/PKB by the rictor-mTORcomplex.";
Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.;
Science 307:1098-1101(2005).
Cited for: PHOSPHORYLATION AT SER-586.
"PHLPP: a phosphatase that directly dephosphorylates Akt, promotesapoptosis, and suppresses tumor growth.";
Gao T., Furnari F., Newton A.C.;
Mol. Cell 18:13-24(2005).
Cited for: DEPHOSPHORYLATION AT SER-586.
"The conserved PI3'K/PTEN/Akt signaling pathway regulates both cellsize and survival in Drosophila.";
Scanga S.E., Ruel L., Binari R.C., Snow B., Stambolic V., Bouchard D.,Peters M., Calvieri B., Mak T.W., Woodgett J.R., Manoukian A.S.;
Oncogene 19:3971-3977(2000).
Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-586.

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