L2GL_DROME - dbPTM
L2GL_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID L2GL_DROME
UniProt AC P08111
Protein Name Lethal(2) giant larvae protein
Gene Name l(2)gl
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1161
Subcellular Localization Cell membrane. Secreted, extracellular space, extracellular matrix. Intercellular matrix.
Protein Description Essential for the development of polarized epithelia, for cell polarity associated with asymmetric cell division of neuroblasts during development, and for oocyte polarity formation. Promotes the formation of actin-rich projections at the oocyte cortex and the posterior enrichment of par-1 which is required for oocyte polarization. Regulates the localization of axis-specifying morphogens such as stau and grk.; Isoform p78: Has an essential role in control of cell proliferation and differentiation during development and could act as a tumor suppressor.; Isoform p127: Has an accessory function in control of cell proliferation and differentiation during development..
Protein Sequence MLKFIRGKGQQPSADRHRLQKDLFAYRKTAQHGFPHKPSALAYDPVLKLMAIGTQTGALKVFGQPGVELYGQHTLLNNSASELNVQLLEWVYGTGRILSLTAANQLILWEPVGATLLPIKTLPFDGKLKKVSSLCCSLSKDLLWIGTEGGNIYQLDLHTFTIKEPVIYHDVVLEQVPPAYKLNPGAIESIRQLPNSPSKLLVAYNRGLCVLWDFESASVQRAYIAPGHGQSVGLTVNFEGSEFTWYHADGSYATWSIDNPEPPSNVNYVPYGPDPCKSINRLYKGKRRSNDVIVFSGGMPRSAYGDHNCVSVHASDGHKVCLDFTSKVIDFFVTFENNRDVAEVLVVLLEEELCAYDLTDPNICAIKAPYLHSVHASAVTCNYLASEVVQSVYESILRAGDEQDIDYSNISWPITGGTLPDNLEESVEEDATKLYEILLTGHEDGSVKFWDCTGVLLKPIYNFKTSSIFGSESDFRDDAAADMSAEQVDEGEPPFRKSGLFDPYSDDPRLAVKKIAFCPKTGQLIVGGTAGQIVIADFIDLPEKVSLKYISMNLVSDRDGFVWKGHDQLNVRSNLLDGEAIPTTERGVNISGVLQVLPPASITCMALEASWGLVSGGTAHGLVLFDFKNFVPVFHRCTLNPNDLTGAGEQLSRRKSFKKSLRESFRKLRKGRSTRTNQSNQVPTTLEARPVERQIEARCADDGLGSMVRCLLFAKTYVTNVNITSPTLWSATNASTVSVFLLHLPPAQTAATAVPSASGNAPPHMPRRISAQLAKEIQLKHRAPVVGISIFDQAGSPVDQLNAGENGSPPHRVLIASEEQFKVFSLPQLKPINKYKLTANEGARIRRIHFGSFSCRISPETLQSMHGCSPTKSTRSHGDGEADPNISGSLAVSRGDVYNETALICLTNMGDIMVLSVPELKRQLNAAAVRREDINGVSSLCFTNSGEALYMMSSSELQRIALATSRVVQPTGVVPVEPLENEESVLEENDAENNKETYACDEVVNTYEIKNPSGISICTRPAEENVGRNSVQQVNGVNISNSPNQANETISSSIGDITVDSVRDHLNMTTTTLCSINTEETIGRLSVLSTQTNKASTTVNMSEIPNINISNLEDLESKRNTTETSTSSVVIKSIITNISHEKTNGDNKIGTPKTAPEESQF
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
21AcetylationADRHRLQKDLFAYRK
HHHHHHHHHHHHHHH		62.0721791702
473PhosphorylationSSIFGSESDFRDDAA
CCCCCCHHHHCCCHH		43.6918327897
484PhosphorylationDDAAADMSAEQVDEG
CCHHHCCCHHHCCCC		29.2422817900
660PhosphorylationRRKSFKKSLRESFRK
HHHHHHHHHHHHHHH		33.0022668510
664PhosphorylationFKKSLRESFRKLRKG
HHHHHHHHHHHHHCC		24.7422668510
676PhosphorylationRKGRSTRTNQSNQVP
HCCCCCCCCCCCCCC		37.3819429919
679PhosphorylationRSTRTNQSNQVPTTL
CCCCCCCCCCCCCCE		31.1619429919
770PhosphorylationPHMPRRISAQLAKEI
CCCCHHHHHHHHHHH		14.2519429919
808PhosphorylationLNAGENGSPPHRVLI
CCCCCCCCCCCEEEE		47.0022817900
869PhosphorylationLQSMHGCSPTKSTRS
HHHHCCCCCCCCCCC		39.9522817900
871PhosphorylationSMHGCSPTKSTRSHG
HHCCCCCCCCCCCCC		22.7229892262
873PhosphorylationHGCSPTKSTRSHGDG
CCCCCCCCCCCCCCC		31.3722817900
876PhosphorylationSPTKSTRSHGDGEAD
CCCCCCCCCCCCCCC		31.7319429919
887PhosphorylationGEADPNISGSLAVSR
CCCCCCCCCCEEECC		29.0319429919
889PhosphorylationADPNISGSLAVSRGD
CCCCCCCCEEECCCC		13.3319429919
893PhosphorylationISGSLAVSRGDVYNE
CCCCEEECCCCCCCC		25.5719429919
984PhosphorylationEPLENEESVLEENDA
CCCCCCCHHCCCCCC		26.3119429919
1013PhosphorylationTYEIKNPSGISICTR
EEECCCCCCCEEECC		59.1423607784
1086PhosphorylationEETIGRLSVLSTQTN
HHHHHEEEEEECCCC		21.4619429919
1089PhosphorylationIGRLSVLSTQTNKAS
HHEEEEEECCCCCCC		19.1319429919
1090PhosphorylationGRLSVLSTQTNKAST
HEEEEEECCCCCCCC		34.9419429919
1121PhosphorylationDLESKRNTTETSTSS
HHHHHCCCCCCCHHH		30.0019429919
1122PhosphorylationLESKRNTTETSTSSV
HHHHCCCCCCCHHHH		40.5919429919
1139PhosphorylationKSIITNISHEKTNGD
EHHHHCCCCCCCCCC		27.8819429919
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 L2GL_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of L2GL_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 L2GL_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYC_DROMEdmgenetic
20374622
NUMB_DROMEnumbgenetic
11117747
NUMB_DROMEnumbgenetic
18854163
NUMB_DROMEnumbgenetic
22394487
SRC42_DROMESrc42Agenetic
24136228
DCAF1_DROMEmahjgenetic
20644714
PNT1_DROMEpntgenetic
14500904
PNT2_DROMEpntgenetic
14500904
PP2A_DROMEmtsgenetic
19690050
APKC_DROMEaPKCgenetic
14657233
APKC_DROMEaPKCgenetic
16357871
APKC_DROMEaPKCgenetic
19375318
APKC_DROMEaPKCgenetic
22394487
SRC64_DROMESrc64Bgenetic
24136228
RHEB_DROMERhebgenetic
20038815
L2GL_DROMEl(2)glphysical
15694314
DCAF1_DROMEmahjphysical
20644714
MYSN_DROMEzipphysical
15694314
APKC_DROMEaPKCphysical
22036573
APKC_DROMEaPKCphysical
12629552
APKC_DROMEaPKCphysical
18854163
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of L2GL_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-473; SER-484; SER-679;SER-808; SER-869; SER-876; SER-887; SER-889; SER-893 AND SER-1013, ANDMASS SPECTROMETRY.

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