LOLA1_DROME - dbPTM
LOLA1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LOLA1_DROME
UniProt AC P42283
Protein Name Longitudinals lacking protein, isoform G
Gene Name lola {ECO:0000312|FlyBase:FBgn0283521}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 891
Subcellular Localization Nucleus .
Protein Description Putative transcription factor required for axon growth and guidance in the central and peripheral nervous systems. Repels CNS axons away from the midline by promoting the expression of the midline repellent sli and its receptor robo..
Protein Sequence MDDDQQFCLRWNNHQSTLISVFDTLLENETLVDCTLAAEGKFLKAHKVVLSACSPYFATLLQEQYDKHPIFILKDVKYQELRAMMDYMYRGEVNISQDQLAALLKAAESLQIKGLSDNRTGGGVAPKPESSGHHRGGKLSGAYTLEQTKRARLATGGAMDTSGDVSGSREGSSSPSRRRRKVRRRSMENDAHDNSNSSVLQAAASNQSILQQTGAGLAVSALVTTQLSSGPAAGTSSQASSTQQQQPLTSTNVTKKTESAKLTSSTAAPASGASASAAVQQAHLHQQQAQTTSDAINTENVQAQSQGGAQGVQGDDEDIDEGSAVGGPNSATGPNPASASASAVHAGVVVKQLASVVDKSSSNHKHKIKDNSVSSVGSEMVIEPKAEYDDDAHDENVEDLTLDEEDMTMEELDQTAGTSQGGEGSSQTYATWQHDRSQDELGLMAQDAQQRDPQDLSRKENTAPDVASTAEIQRSFQRSILNGKQRDEQKIQLPGSRRKRLSVTEVSDMLFEFYKTKSAKVPKAEQPHRQVSPTSGEILDPSTISAIAVYGTASETASKNLNADEVMRVQNATATRVVGAAAGAAASFHPRPKYTLKTAASSTEHTTAIPTSVLVANSAAALTPKPQAAVIAEALMRNGLHNFQQQLRAQEILRQQTPHRRIKEENDVEIAGGDITPTKILENLLRKQQERDLRHSECENEPGYSTEDDEEGRYHAFDDIHLMEQSGGKFGNNSGMGMFNANAHGGSASSILDAHQAFRNLEFTLSDYGGSSSNGSTTSPNGIGLDGEPVYECRHCGKKYRWKSTLRRHENVECGGKEPSHQCPYCPYKSKQRGNLGVHVRKHHTDLPQLPSKRRSKYSMNRENGMSGSMSDDSQGKLIIDFNGKGELETK
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
138AcetylationSGHHRGGKLSGAYTL
CCCCCCCCCCCCEEH
42.1621791702
140PhosphorylationHHRGGKLSGAYTLEQ
CCCCCCCCCCEEHHH
25.5118327897
161PhosphorylationATGGAMDTSGDVSGS
HCCCCCCCCCCCCCC
22.8618327897
162PhosphorylationTGGAMDTSGDVSGSR
CCCCCCCCCCCCCCC
28.8218327897
168PhosphorylationTSGDVSGSREGSSSP
CCCCCCCCCCCCCCH
21.4718327897
372PhosphorylationKHKIKDNSVSSVGSE
CCCCCCCCCCCCCCE
33.2518327897
375PhosphorylationIKDNSVSSVGSEMVI
CCCCCCCCCCCEEEE
28.4818327897
378PhosphorylationNSVSSVGSEMVIEPK
CCCCCCCCEEEECCC
21.9918327897
696PhosphorylationQERDLRHSECENEPG
HHHHHCCHHCCCCCC
37.1918327897
699PhosphorylationDLRHSECENEPGYST
HHCCHHCCCCCCCCC
61.6518327897
705PhosphorylationCENEPGYSTEDDEEG
CCCCCCCCCCCCCCC
31.1018327897
706PhosphorylationENEPGYSTEDDEEGR
CCCCCCCCCCCCCCC
34.6418327897
708PhosphorylationEPGYSTEDDEEGRYH
CCCCCCCCCCCCCEE
69.5718327897
709PhosphorylationPGYSTEDDEEGRYHA
CCCCCCCCCCCCEEE
50.0018327897
749PhosphorylationNAHGGSASSILDAHQ
CCCCCCHHHHHHHHH
21.4318327897
750PhosphorylationAHGGSASSILDAHQA
CCCCCHHHHHHHHHH
27.2118327897
752PhosphorylationGGSASSILDAHQAFR
CCCHHHHHHHHHHHH
5.2718327897
753PhosphorylationGSASSILDAHQAFRN
CCHHHHHHHHHHHHC
40.0918327897
874PhosphorylationSGSMSDDSQGKLIID
CCCCCCCCCCCEEEE
45.9111880341
877PhosphorylationMSDDSQGKLIIDFNG
CCCCCCCCEEEEECC
28.9518327897

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 LOLA1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LOLA1_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 LOLA1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LOLA1_DROMElolaphysical
14605208
LOLA2_DROMElolaphysical
14605208
LOLA3_DROMElolaphysical
14605208
LOLA4_DROMElolaphysical
14605208
LOLA6_DROMElolaphysical
14605208
LOLA5_DROMElolaphysical
14605208
MILT_DROMEmiltphysical
14605208
Y2199_DROMECG2199physical
14605208
MED9_DROMEMED9physical
14605208
GIANT_DROMEgtphysical
14605208
SLIT_DROMEsligenetic
11880341
KGP25_DROMEforgenetic
27098704
KGP24_DROMEforgenetic
27098704
JIL1_DROMEJIL-1physical
12538650
LOLA1_DROMElolaphysical
12538650
LOLA2_DROMElolaphysical
12538650
LOLA3_DROMElolaphysical
12538650
LOLA4_DROMElolaphysical
12538650
LOLA6_DROMElolaphysical
12538650
LOLA5_DROMElolaphysical
12538650
LOLA1_DROMElolaphysical
23847101
LOLA2_DROMElolaphysical
23847101
LOLA3_DROMElolaphysical
23847101
LOLA4_DROMElolaphysical
23847101
LOLA6_DROMElolaphysical
23847101
LOLA5_DROMElolaphysical
23847101
LOLA1_DROMElolaphysical
27898696
LOLA2_DROMElolaphysical
27898696
LOLA3_DROMElolaphysical
27898696
LOLA4_DROMElolaphysical
27898696
LOLA6_DROMElolaphysical
27898696
LOLA5_DROMElolaphysical
27898696
KGP25_DROMEforphysical
27098704
KGP24_DROMEforphysical
27098704

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LOLA1_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-140; THR-161; SER-162;SER-168; SER-372; SER-375; SER-378; SER-696; SER-705; THR-706;SER-749; SER-750 AND SER-874, AND MASS SPECTROMETRY.

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