DLG1_DROME - dbPTM
DLG1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DLG1_DROME
UniProt AC P31007
Protein Name Disks large 1 tumor suppressor protein
Gene Name dlg1
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 970
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasm, cytoskeleton . Cell junction, septate junction . Cytoskeleton- and membrane-associated. Located at the cytoplasmic face of the membrane in the cellular blastoderm
Protein Description During embryonic development, some isoforms are essential for proper neuronal differentiation and organization. Required for cell polarity; maintenance of apicobasal polarity. Plays a critical role at septate junctions in cellular growth control during larval development. The presence of a guanylate kinase domain suggests involvement in cellular adhesion as well as signal transduction to control cellular proliferation..
Protein Sequence MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERVIRIFKSRLFQALLDIQEFYELTLLDDSKSIQQKTAETLQIATKWEKDGQAVKIADFIKSSNLNRNCAYEFNNDASSNQTNQSALNQNPIANNVSAQAQAEALSRTFKSELEEILNQRMRIESDTENAKEPTVEQQQKQQQAQQRSSRSPQQQNPQQQQGSKSRSGSQTVNGDDSWLYEDIQLERGNSGLGFSIAGGTDNPHIGTDTSIYITKLISGGAAAADGRLSINDIIVSVNDVSVVDVPHASAVDALKKAGNVVKLHVKRKRGTATTPAAGSAAGDARDSAASGPKVIEIDLVKGGKGLGFSIAGGIGNQHIPGDNGIYVTKLMDGGAAQVDGRLSIGDKLIAVRTNGSEKNLENVTHELAVATLKSITDKVTLIIGKTQHLTTSASGGGGGGLSSGQQLSQSQSQLATSQSQSQVHQQQHATPMVNSQSTEPGSRYASTNVLAAVPPGTPRAVSTEDITREPRTITIQKGPQGLGFNIVGGEDGQGIYVSFILAGGPADLGSELKRGDQLLSVNNVNLTHATHEEAAQALKTSGGVVTLLAQYRPEEYNRFEARIQELKQQAALGAGGSGTLLRTTQKRSLYVRALFDYDPNRDDGLPSRGLPFKHGDILHVTNASDDEWWQARRVLGDNEDEQIGIVPSKRRWERKMRARDRSVKFQGHAAANNNLDKQSTLDRKKKNFTFSRKFPFMKSRDEKNEDGSDQEPFMLCYTQDDANAEGASEENVLSYEAVQRLSINYTRPVIILGPLKDRINDDLISEYPDKFGSCVPHTTRPKREYEVDGRDYHFVSSREQMERDIQNHLFIEAGQYNDNLYGTSVASVREVAEKGKHCILDVSGNAIKRLQVAQLYPVAVFIKPKSVDSVMEMNRRMTEEQAKKTYERAIKMEQEFGEYFTGVVQGDTIEEIYSKVKSMIWSQSGPTIWVPSKESL
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
12 (in isoform 4)Phosphorylation-4.8627794539
13 (in isoform 5)Phosphorylation-50.7719429919
13 (in isoform 4)Phosphorylation-50.7727794539
13 (in isoform 3)Phosphorylation-50.7719429919
13 (in isoform 1)Phosphorylation-50.7719429919
22 (in isoform 4)Phosphorylation-7.6427794539
22 (in isoform 3)Phosphorylation-7.6419429919
23 (in isoform 3)Phosphorylation-41.5019429919
29 (in isoform 3)Phosphorylation-14.9619429919
144 (in isoform 8)Phosphorylation-42.2727794539
183PhosphorylationQQAQQRSSRSPQQQN
HHHHHHHCCCHHHCC		38.6827794539
185PhosphorylationAQQRSSRSPQQQNPQ
HHHHHCCCHHHCCCC		29.0727794539
307PhosphorylationKRKRGTATTPAAGSA
EECCCCCCCCCCCCH		32.9022817900
308PhosphorylationRKRGTATTPAAGSAA
ECCCCCCCCCCCCHH		14.4128490779
313PhosphorylationATTPAAGSAAGDARD
CCCCCCCCHHCCHHH		15.3728490779
321PhosphorylationAAGDARDSAASGPKV
HHCCHHHHHHCCCEE		21.8521082442
390PhosphorylationIAVRTNGSEKNLENV
EEEEECCCCCCHHHH		47.6827794539
446 (in isoform 5)Phosphorylation-32.2019429919
446 (in isoform 1)Phosphorylation-32.2019429919
448 (in isoform 5)Phosphorylation-7.3219429919
448 (in isoform 1)Phosphorylation-7.3219429919
454 (in isoform 3)Phosphorylation-30.1919429919
456 (in isoform 3)Phosphorylation-29.1319429919
478PhosphorylationSTEPGSRYASTNVLA
CCCCCCCCCCCCEEE		13.4528490779
480PhosphorylationEPGSRYASTNVLAAV
CCCCCCCCCCEEEEC		16.1619429919
481PhosphorylationPGSRYASTNVLAAVP
CCCCCCCCCEEEECC		22.6019429919
491PhosphorylationLAAVPPGTPRAVSTE
EEECCCCCCCCCCHH		18.5119429919
496PhosphorylationPGTPRAVSTEDITRE
CCCCCCCCHHHCCCC		25.7019429919
497PhosphorylationGTPRAVSTEDITREP
CCCCCCCHHHCCCCC		30.9528490779
501PhosphorylationAVSTEDITREPRTIT
CCCHHHCCCCCEEEE		41.1022817900
611PhosphorylationAALGAGGSGTLLRTT
HHHCCCCCCHHCCCC		27.9019060867
613PhosphorylationLGAGGSGTLLRTTQK
HCCCCCCHHCCCCCC		25.0722817900
713PhosphorylationNNNLDKQSTLDRKKK
CCCCCCCCHHCHHHH		36.3623607784
714PhosphorylationNNLDKQSTLDRKKKN
CCCCCCCHHCHHHHC		30.1325749252
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 DLG1_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DLG1_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 DLG1_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MIRO_DROMEMirophysical
14605208
KNRL_DROMEknrlphysical
14605208
KCNAS_DROMEShgenetic
9354326
DSH_DROMEdshphysical
25461409
DLG1_DROMEdlg1physical
16377571
DLG1_DROMEdlg1physical
19261607
KCNAS_DROMEShphysical
25813388
HTS_DROMEhtsphysical
21791202
HTS_DROMEhtsphysical
25416060
HTS_DROMEhtsphysical
25650626
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DLG1_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-496 AND THR-714, ANDMASS SPECTROMETRY.

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