dbPTM

DLG4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DLG4_HUMAN
UniProt AC	P78352
Protein Name	Disks large homolog 4
Gene Name	DLG4
Organism	Homo sapiens (Human).
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..
Protein Sequence	MDCLCIVTTKKYRYQDEDTPPLEHSPAHLPNQANSPPVIVNTDTLEAPGYELQVNGTEGEMEYEEITLERGNSGLGFSIAGGTDNPHIGDDPSIFITKIIPGGAAAQDGRLRVNDSILFVNEVDVREVTHSAAVEALKEAGSIVRLYVMRRKPPAEKVMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKILAVNSVGLEDVMHEDAVAALKNTYDVVYLKVAKPSNAYLSDSYAPPDITTSYSQHLDNEISHSSYLGTDYPTAMTPTSPRRYSPVAKDLLGEEDIPREPRRIVIHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDQILSVNGVDLRNASHEQAAIALKNAGQTVTIIAQYKPEEYSRFEAKIHDLREQLMNSSLGSGTASLRSNPKRGFYIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDASDEEWWQARRVHSDSETDDIGFIPSKRRVERREWSRLKAKDWGSSSGSQGREDSVLSYETVTQMEVHYARPIIILGPTKDRANDDLLSEFPDKFGSCVPHTTRPKREYEIDGRDYHFVSSREKMEKDIQAHKFIEAGQYNSHLYGTSVQSVREVAEQGKHCILDVSANAVRRLQAAHLHPIAIFIRPRSLENVLEINKRITEEQARKAFDRATKLEQEFTECFSAIVEGDSFEEIYHKVKRVIEDLSGPYIWVPARERL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	S-palmitoylation	-----MDCLCIVTTK -----CCEEEEEECC	3.01	10629226
5	S-palmitoylation	---MDCLCIVTTKKY ---CCEEEEEECCCE	2.71	10629226
8	Phosphorylation	MDCLCIVTTKKYRYQ CCEEEEEECCCEECC	17.00	-
19	Phosphorylation	YRYQDEDTPPLEHSP EECCCCCCCCCCCCC	25.43	-
62	Phosphorylation	NGTEGEMEYEEITLE CCCCCEEEEEEEEEE	45.55	-
68	Phosphorylation	MEYEEITLERGNSGL EEEEEEEEECCCCCC	5.33	-
73	Phosphorylation	ITLERGNSGLGFSIA EEEECCCCCCCEEEC	37.91	12933808
83	Phosphorylation	GFSIAGGTDNPHIGD CEEECCCCCCCCCCC	31.52	25332170
116	Phosphorylation	GRLRVNDSILFVNEV CCCEECCEEEEEEEE	18.91	-
129	Phosphorylation	EVDVREVTHSAAVEA EEEHHHHCHHHHHHH	12.83	25003641
142	Phosphorylation	EALKEAGSIVRLYVM HHHHHHCCEEEEEEE	25.59	28857561
147	Phosphorylation	AGSIVRLYVMRRKPP HCCEEEEEEEECCCC	5.01	-
185	Phosphorylation	VGNQHIPGDNSIYVT CCCCCCCCCCCEEEE	46.24	-
188	Phosphorylation	QHIPGDNSIYVTKII CCCCCCCCEEEEEEE	21.75	19690332
192	Phosphorylation	GDNSIYVTKIIEGGA CCCCEEEEEEEECCC	10.27	19690332
217	Phosphorylation	DKILAVNSVGLEDVM CEEEEEECCCHHHHC	15.80	24076635
236	Phosphorylation	VAALKNTYDVVYLKV HHHHHCCEEEEEEEE	19.01	-
240	Phosphorylation	KNTYDVVYLKVAKPS HCCEEEEEEEEECCC	10.72	24927040
279	Phosphorylation	ISHSSYLGTDYPTAM CCCCCCCCCCCCCCC	14.33	-
283	Phosphorylation	SYLGTDYPTAMTPTS CCCCCCCCCCCCCCC	19.25	-
294	Phosphorylation	TPTSPRRYSPVAKDL CCCCCCCCCHHHHHH	20.71	26699800
295	Phosphorylation	PTSPRRYSPVAKDLL CCCCCCCCHHHHHHC	15.87	26699800
338	Phosphorylation	EDGEGIFISFILAGG CCCCEEEEEEEEECC	2.88	24719451
397	Phosphorylation	AQYKPEEYSRFEAKI EEECHHHHHHHHHHH	11.95	-
414	Phosphorylation	LREQLMNSSLGSGTA HHHHHHHCCCCCCCC	16.99	24076635
415	Phosphorylation	REQLMNSSLGSGTAS HHHHHHCCCCCCCCH	31.57	19060867
418	Phosphorylation	LMNSSLGSGTASLRS HHHCCCCCCCCHHCC	37.96	19060867
420	Phosphorylation	NSSLGSGTASLRSNP HCCCCCCCCHHCCCC	18.12	24076635
422	Phosphorylation	SLGSGTASLRSNPKR CCCCCCCHHCCCCCC	24.93	24076635
425	Phosphorylation	SGTASLRSNPKRGFY CCCCHHCCCCCCCEE	63.88	23911959
440	Phosphorylation	IRALFDYDKTKDCGF EEEEECCCCCCCCCH	54.73	-
442	Phosphorylation	ALFDYDKTKDCGFLS EEECCCCCCCCCHHH	29.26	24076635
446	Ubiquitination	YDKTKDCGFLSQALS CCCCCCCCHHHHHHH	36.34	-
449	Phosphorylation	TKDCGFLSQALSFRF CCCCCHHHHHHHHCC	15.90	24076635
453	Phosphorylation	GFLSQALSFRFGDVL CHHHHHHHHCCCCEE	19.86	24076635
468	Phosphorylation	HVIDASDEEWWQARR EEEECCHHHHHHHHC	53.69	-
478	Phosphorylation	WQARRVHSDSETDDI HHHHCCCCCCCCCCC	39.72	25307156
480	Phosphorylation	ARRVHSDSETDDIGF HHCCCCCCCCCCCCC	45.47	25332170
482	Phosphorylation	RVHSDSETDDIGFIP CCCCCCCCCCCCCCC	42.81	25332170
490	Phosphorylation	DDIGFIPSKRRVERR CCCCCCCCCHHHCHH	33.70	24719451
511	Phosphorylation	AKDWGSSSGSQGRED CHHCCCCCCCCCCCC	44.13	25307156
523	Phosphorylation	REDSVLSYETVTQME CCCCCCEEEEEEEEE	16.09	18721130
561	Phosphorylation	EFPDKFGSCVPHTTR HCCCCCCCCCCCCCC	18.31	29116813
566	Phosphorylation	FGSCVPHTTRPKREY CCCCCCCCCCCCCEE	20.59	-
573	Phosphorylation	TTRPKREYEIDGRDY CCCCCCEEEECCCCE	23.40	-
580	Phosphorylation	YEIDGRDYHFVSSRE EEECCCCEEEECCHH	8.87	28796482
604	Phosphorylation	KFIEAGQYNSHLYGT HHHHHCCCCCCCCCC	20.09	21082442
606	Phosphorylation	IEAGQYNSHLYGTSV HHHCCCCCCCCCCCH	15.22	-
623	Phosphorylation	VREVAEQGKHCILDV HHHHHHCCCEEEEEC	17.12	27642862
654	Phosphorylation	AIFIRPRSLENVLEI EEEECCCCHHHHHHH	42.59	25332170
666	Phosphorylation	LEINKRITEEQARKA HHHHHHCCHHHHHHH	37.19	22210691
701	Phosphorylation	GDSFEEIYHKVKRVI CCCHHHHHHHHHHHH	10.00	17053785
715	Phosphorylation	IEDLSGPYIWVPARE HHHHCCCEEEEECHH	15.79	21082442
744	Phosphorylation	--------------------------- ---------------------------		-

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
73	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
523	Y	Phosphorylation	Kinase	FYN	P06241	PSP
523	Y	Phosphorylation	Kinase	SRC	P12931	PSP
561	S	Phosphorylation	Kinase	MARK2	Q7KZI7	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:14642282
-	K	Ubiquitination	E3 ubiquitin ligase	UBE3A	Q05086	PMID:17121805

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DLG4_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KCNJ4_HUMAN	KCNJ4	physical	10627592
KCNJ2_HUMAN	KCNJ2	physical	10627592
LRP2_HUMAN	LRP2	physical	12713445
EXOC4_HUMAN	EXOC4	physical	12675619
ADA22_HUMAN	ADAM22	physical	16990550
LGI1_HUMAN	LGI1	physical	16990550
GRIA2_HUMAN	GRIA2	physical	16990550
GRIA3_HUMAN	GRIA3	physical	16990550
FAK2_HUMAN	PTK2B	physical	12576483
LRP2_HUMAN	LRP2	physical	10827173
LRP1_HUMAN	LRP1	physical	10827173
HGS_HUMAN	HGS	physical	12151521
CSKP_HUMAN	CASK	physical	12151521
DLG3_HUMAN	DLG3	physical	10026200
ERBB2_HUMAN	ERBB2	physical	10839362
ERBB4_HUMAN	ERBB4	physical	10839362
DLG4_HUMAN	DLG4	physical	9182804
ERBB4_HUMAN	ERBB4	physical	10725395
DLGP1_HUMAN	DLGAP1	physical	9115257
DLGP2_HUMAN	DLGAP2	physical	9115257
DLGP3_HUMAN	DLGAP3	physical	9115257
DLGP4_HUMAN	DLGAP4	physical	9115257
FYN_HUMAN	FYN	physical	12419528
NMDE1_HUMAN	GRIN2A	physical	12419528
NLGN1_HUMAN	NLGN1	physical	9278515
NMDE1_HUMAN	GRIN2A	physical	9278515
DLGP1_HUMAN	DLGAP1	physical	9286858
NMDE1_HUMAN	GRIN2A	physical	9286858
CRIPT_RAT	Cript	physical	9581762
KCNA4_RAT	Kcna4	physical	9581762
NMDE2_RAT	Grin2b	physical	9581762
GRIK2_HUMAN	GRIK2	physical	11279111
ADRB1_HUMAN	ADRB1	physical	10995758
PTPRG_HUMAN	PTPRG	physical	10521598
CCG2_HUMAN	CACNG2	physical	11805122
MAP1A_HUMAN	MAP1A	physical	9786987
NOS1_HUMAN	NOS1	physical	8625413
FZD1_HUMAN	FZD1	physical	12067714
FZD2_HUMAN	FZD2	physical	12067714
FZD4_HUMAN	FZD4	physical	12067714
FZD7_HUMAN	FZD7	physical	12067714
M3K10_HUMAN	MAP3K10	physical	11152698
M3K11_HUMAN	MAP3K11	physical	11152698
DLGP1_HUMAN	DLGAP1	physical	9024696
KCND2_HUMAN	KCND2	physical	12435606
KCNA1_HUMAN	KCNA1	physical	12435606
KCNA5_HUMAN	KCNA5	physical	12435606
KCNA4_HUMAN	KCNA4	physical	12435606
KCNA2_HUMAN	KCNA2	physical	12435606
ACTN2_HUMAN	ACTN2	physical	12435606
KI13B_HUMAN	KIF13B	physical	10859302
AGRB1_HUMAN	BAI1	physical	11937501
KPCA_HUMAN	PRKCA	physical	11937501
NMDE1_HUMAN	GRIN2A	physical	11937501
NMDE3_HUMAN	GRIN2C	physical	11937501
NMDE2_HUMAN	GRIN2B	physical	11937501
LIN7A_HUMAN	LIN7A	physical	10341223
KCNA5_HUMAN	KCNA5	physical	16466689
ADRB1_HUMAN	ADRB1	physical	11526121
KCNA4_HUMAN	KCNA4	physical	11744724
GRIK2_HUMAN	GRIK2	physical	11744724
NMDE2_HUMAN	GRIN2B	physical	11723117
KCNA4_HUMAN	KCNA4	physical	11723117
PCD10_HUMAN	PCDH10	physical	23260144
MDM2_HUMAN	MDM2	physical	23260144
SPR2A_HUMAN	SPRR2A	physical	18155796
PTN5_HUMAN	PTPN5	physical	27457929

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DLG4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-701, AND MASSSPECTROMETRY.	17053785 [Abstract]