DLG4_RAT - dbPTM
DLG4_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DLG4_RAT
UniProt AC P31016
Protein Name Disks large homolog 4
Gene Name Dlg4
Organism Rattus norvegicus (Rat).
Sequence Length 724
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cell junction, synapse . Cytoplasm . Cell projection, axon . High levels in postsynaptic density of neurons in the forebrain.
Protein Description Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B. Also regulates AMPA-type glutamate receptor (AMPAR) immobilization at postsynaptic density keeping the channels in an activated state in the presence of glutamate and preventing synaptic depression (By similarity)..
Protein Sequence MDCLCIVTTKKYRYQDEDTPPLEHSPAHLPNQANSPPVIVNTDTLEAPGYELQVNGTEGEMEYEEITLERGNSGLGFSIAGGTDNPHIGDDPSIFITKIIPGGAAAQDGRLRVNDSILFVNEVDVREVTHSAAVEALKEAGSIVRLYVMRRKPPAEKVMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKILAVNSVGLEDVMHEDAVAALKNTYDVVYLKVAKPSNAYLSDSYAPPDITTSYSQHLDNEISHSSYLGTDYPTAMTPTSPRRYSPVAKDLLGEEDIPREPRRIVIHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDQILSVNGVDLRNASHEQAAIALKNAGQTVTIIAQYKPEEYSRFEAKIHDLREQLMNSSLGSGTASLRSNPKRGFYIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDAGDEEWWQARRVHSDSETDDIGFIPSKRRVERREWSRLKAKDWGSSSGSQGREDSVLSYETVTQMEVHYARPIIILGPTKDRANDDLLSEFPDKFGSCVPHTTRPKREYEIDGRDYHFVSSREKMEKDIQAHKFIEAGQYNSHLYGTSVQSVREVAEQGKHCILDVSANAVRRLQAAHLHPIAIFIRPRSLENVLEINKRITEEQARKAFDRATKLEQEFTECFSAIVEGDSFEEIYHKVKRVIEDLSGPYIWVPARERL
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
3S-palmitoylation-----MDCLCIVTTK
-----CCEEEEEECC		3.0127307232
5S-palmitoylation---MDCLCIVTTKKY
---CCEEEEEECCCE		2.7127307232
19PhosphorylationYRYQDEDTPPLEHSP
EECCCCCCCCCCCCC		25.43-
73PhosphorylationITLERGNSGLGFSIA
EEEECCCCCCCEEEC		37.9125403869
131PhosphorylationDVREVTHSAAVEALK
EHHHHCHHHHHHHHH		14.4625403869
138AcetylationSAAVEALKEAGSIVR
HHHHHHHHHHCCEEE		53.1922902405
138UbiquitinationSAAVEALKEAGSIVR
HHHHHHHHHHCCEEE		53.19-
142PhosphorylationEALKEAGSIVRLYVM
HHHHHHCCEEEEEEE		25.5929779826
157UbiquitinationRRKPPAEKVMEIKLI
ECCCCHHHEEEEEEE		49.33-
162AcetylationAEKVMEIKLIKGPKG
HHHEEEEEEEECCCC		30.7422902405
162UbiquitinationAEKVMEIKLIKGPKG
HHHEEEEEEEECCCC		30.74-
190PhosphorylationIPGDNSIYVTKIIEG
CCCCCCEEEEEEEEC		11.24-
192PhosphorylationGDNSIYVTKIIEGGA
CCCCEEEEEEEECCC		10.27-
202UbiquitinationIEGGAAHKDGRLQIG
EECCCCCCCCCCCCC		58.09-
236PhosphorylationVAALKNTYDVVYLKV
HHHHHCCEEEEEEEE		19.01-
240PhosphorylationKNTYDVVYLKVAKPS
HCCEEEEEEEEECCC		10.7227097102
255PhosphorylationNAYLSDSYAPPDITT
CCCCCCCCCCCCCCC		28.28-
264PhosphorylationPPDITTSYSQHLDNE
CCCCCCCHHHHHCCC		15.40-
276PhosphorylationDNEISHSSYLGTDYP
CCCCCCCCCCCCCCC		20.96-
282PhosphorylationSSYLGTDYPTAMTPT
CCCCCCCCCCCCCCC		11.43-
284PhosphorylationYLGTDYPTAMTPTSP
CCCCCCCCCCCCCCC		23.88-
287PhosphorylationTDYPTAMTPTSPRRY
CCCCCCCCCCCCCCC		22.4314741046
290PhosphorylationPTAMTPTSPRRYSPV
CCCCCCCCCCCCCHH		20.0130240740
294PhosphorylationTPTSPRRYSPVAKDL
CCCCCCCCCHHHHHH		20.7128551015
295PhosphorylationPTSPRRYSPVAKDLL
CCCCCCCCHHHHHHC		15.8715358237
397PhosphorylationAQYKPEEYSRFEAKI
EEECHHHHHHHHHHH		11.9521965656
398PhosphorylationQYKPEEYSRFEAKIH
EECHHHHHHHHHHHH		33.50-
414PhosphorylationLREQLMNSSLGSGTA
HHHHHHHCCCCCCCC		16.9927097102
415PhosphorylationREQLMNSSLGSGTAS
HHHHHHCCCCCCCCH		31.5727097102
418PhosphorylationLMNSSLGSGTASLRS
HHHCCCCCCCCHHCC		37.9627097102
420PhosphorylationNSSLGSGTASLRSNP
HCCCCCCCCHHCCCC		18.1227097102
422PhosphorylationSLGSGTASLRSNPKR
CCCCCCCHHCCCCCC		24.9327097102
425PhosphorylationSGTASLRSNPKRGFY
CCCCHHCCCCCCCEE		63.8825403869
432PhosphorylationSNPKRGFYIRALFDY
CCCCCCEEEEEEECC		7.72-
439PhosphorylationYIRALFDYDKTKDCG
EEEEEECCCCCCCCC		16.41-
441UbiquitinationRALFDYDKTKDCGFL
EEEECCCCCCCCCHH		51.77-
441AcetylationRALFDYDKTKDCGFL
EEEECCCCCCCCCHH		51.77-
442PhosphorylationALFDYDKTKDCGFLS
EEECCCCCCCCCHHH		29.26-
443UbiquitinationLFDYDKTKDCGFLSQ
EECCCCCCCCCHHHH		57.68-
449PhosphorylationTKDCGFLSQALSFRF
CCCCCHHHHHHHHCC		15.9025403869
478PhosphorylationWQARRVHSDSETDDI
HHCEECCCCCCCCCC		39.7230240740
480PhosphorylationARRVHSDSETDDIGF
CEECCCCCCCCCCCC		45.4730240740
482PhosphorylationRVHSDSETDDIGFIP
ECCCCCCCCCCCCCC		42.8122673903
509PhosphorylationLKAKDWGSSSGSQGR
HCCHHCCCCCCCCCC		19.6527097102
510PhosphorylationKAKDWGSSSGSQGRE
CCHHCCCCCCCCCCC		34.4827097102
511PhosphorylationAKDWGSSSGSQGRED
CHHCCCCCCCCCCCC		44.1327097102
513PhosphorylationDWGSSSGSQGREDSV
HCCCCCCCCCCCCCC		31.2627097102
523PhosphorylationREDSVLSYETVTQME
CCCCCCEEEEEEEEE		16.0918721130
533PhosphorylationVTQMEVHYARPIIIL
EEEEEEEECCCEEEE		14.9620220006
544AcetylationIIILGPTKDRANDDL
EEEECCCCCCCCCHH		48.64133523
558UbiquitinationLLSEFPDKFGSCVPH
HHHHCCCCCCCCCCC		52.44-
561PhosphorylationEFPDKFGSCVPHTTR
HCCCCCCCCCCCCCC		18.31-
573PhosphorylationTTRPKREYEIDGRDY
CCCCCCEEEECCCCE		23.40-
580PhosphorylationYEIDGRDYHFVSSRE
EEECCCCEEEECCHH		8.87-
584PhosphorylationGRDYHFVSSREKMEK
CCCEEEECCHHHHHH		23.80-
585PhosphorylationRDYHFVSSREKMEKD
CCEEEECCHHHHHHH		38.87-
591UbiquitinationSSREKMEKDIQAHKF
CCHHHHHHHHHHHHH		57.54-
597UbiquitinationEKDIQAHKFIEAGQY
HHHHHHHHHHHHCCC		51.56-
597AcetylationEKDIQAHKFIEAGQY
HHHHHHHHHHHHCCC		51.5622902405
604PhosphorylationKFIEAGQYNSHLYGT
HHHHHCCCCCCCCCC		20.09-
606PhosphorylationIEAGQYNSHLYGTSV
HHHCCCCCCCCCCCH		15.22-
609PhosphorylationGQYNSHLYGTSVQSV
CCCCCCCCCCCHHHH		16.97-
654PhosphorylationAIFIRPRSLENVLEI
EEEECCCCHHHHHHH		42.5925403869
663AcetylationENVLEINKRITEEQA
HHHHHHHHHCCHHHH		51.3322902405
663UbiquitinationENVLEINKRITEEQA
HHHHHHHHHCCHHHH		51.33-
715PhosphorylationIEDLSGPYIWVPARE
HHHHCCCEEEEECHH		15.79-
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
19TPhosphorylationKinaseGSK3BP49841
PSP
19TPhosphorylationKinaseGSK3BP18266
PSP
73SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
73SPhosphorylationKinaseCAMK2AP11275
PSP
287TPhosphorylationKinaseMAPK1P28482
GPS
287TPhosphorylationKinaseMAPK12P53778
GPS
287TPhosphorylationKinaseMAPK13O15264
GPS
290SPhosphorylationKinaseMAPK1P28482
GPS
290SPhosphorylationKinaseMAPK12P53778
GPS
295SPhosphorylationKinaseMAPK8P45983
GPS
295SPhosphorylationKinaseJNK1P49185
PSP
533YPhosphorylationKinaseABL1P00519
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DLG4_RAT !!
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 DLG4_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKAP5_HUMANAKAP5physical
10939335
UBC_RATUbcphysical
14642282
PZRN3_HUMANPDZRN3physical
17118964
GRASP_RATGraspphysical
12586822
ACTG_RATActg1physical
12063253
KLH17_RATKlhl17physical
12063253
M3K11_RATMap3k11physical
19449206
GRIK2_RATGrik2physical
19449206
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DLG4_RAT

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting,postsynaptic targeting, and ion channel clustering.";
El-Husseini A.E., Craven S.E., Chetkovich D.M., Firestein B.L.,Schnell E., Aoki C., Bredt D.S.;
J. Cell Biol. 148:159-172(2000).
Cited for: MUTAGENESIS OF CYS-3 AND CYS-5, AND PALMITOYLATION AT CYS-3 AND CYS-5.

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