dbPTM

DLG1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DLG1_MOUSE
UniProt AC	Q811D0
Protein Name	Disks large homolog 1
Gene Name	Dlg1
Organism	Mus musculus (Mouse).
Sequence Length	905
Subcellular Localization	Membrane Peripheral membrane protein . Basolateral cell membrane . Endoplasmic reticulum membrane . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cell junction, synapse . Cell membrane, sarcolemma . Cell junction . Cytoplasm
Protein Description	Essential multidomain scaffolding protein required for normal development. Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels (By similarity). Functional regulator of Kv1.5 channel (By similarity). May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation..
Protein Sequence	MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCVDHSKQCEPVQPVTTWEIASLPSTAVTSETLPGSLSPPVEKYRYQDEEVLPPEHISPQVTNEVLGPELVHVSEKNLSEIENVHGFVSHSHISPIKPTEAVPPSSPIVPVTPALPVPAESTVVLPSAPQANPPPVLVNTDSLETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRLRVNDCILRVNEADVRDVTHSKAVEALKEAGSIVRLYVKRRKPASEKIMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAVNSVCLEEVTHEEAVTALKNTSDFVYLKVAKPTSMYINDGYAPPDITNSSSQSVDNHVSPSSCLGQTPTSPARYSPISKAVLGDDEITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVTIVAQYRPEEYSRFEAKIHDLREQMMNSSVSSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFRFGDILHVINASDDEWWQARQVTPDGESDEVGVIPSKRRVEKKERARLKTVKFNSKTRGDKGEIPDDMGSKGLKHVTSNASDSESSYRGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRVNDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVRAVAEKGKHCILDVSGNAIKRLQIAQLYPISIFIKPKSMENIMEMNKRLTEEQARKTFERAMKLEQEFTEHFTAIVQGDTLEDIYNQVKQIIEEQSGPYIWVPAKEKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
86	Phosphorylation	VTTWEIASLPSTAVT CEEEEEECCCCCCCC	46.61	26643407
89	Phosphorylation	WEIASLPSTAVTSET EEEECCCCCCCCCCC	34.00	26643407
90	Phosphorylation	EIASLPSTAVTSETL EEECCCCCCCCCCCC	24.17	26643407
93	Phosphorylation	SLPSTAVTSETLPGS CCCCCCCCCCCCCCC	20.55	26643407
94	Phosphorylation	LPSTAVTSETLPGSL CCCCCCCCCCCCCCC	23.22	26643407
96	Phosphorylation	STAVTSETLPGSLSP CCCCCCCCCCCCCCC	37.71	26643407
100	Phosphorylation	TSETLPGSLSPPVEK CCCCCCCCCCCCCHH	24.59	26745281
102	Phosphorylation	ETLPGSLSPPVEKYR CCCCCCCCCCCHHCC	28.93	26745281
108	Phosphorylation	LSPPVEKYRYQDEEV CCCCCHHCCCCCCCC	10.88	26643407
110	Phosphorylation	PPVEKYRYQDEEVLP CCCHHCCCCCCCCCC	19.75	26643407
122	Phosphorylation	VLPPEHISPQVTNEV CCCHHHCCCCCCCCC	15.93	26643407
126	Phosphorylation	EHISPQVTNEVLGPE HHCCCCCCCCCCCCE	22.03	26643407
138	Phosphorylation	GPELVHVSEKNLSEI CCEEEEECCCCHHHH	28.16	21082442
143	Phosphorylation	HVSEKNLSEIENVHG EECCCCHHHHCCCCC	46.02	29899451
153	Phosphorylation	ENVHGFVSHSHISPI CCCCCCCCCCCCCCC	19.60	26745281
155	Phosphorylation	VHGFVSHSHISPIKP CCCCCCCCCCCCCCC	18.27	26745281
155 (in isoform 2)	Phosphorylation	-	18.27	25521595
158	Phosphorylation	FVSHSHISPIKPTEA CCCCCCCCCCCCCCC	18.36	26824392
158 (in isoform 2)	Phosphorylation	-	18.36	25521595
206	Phosphorylation	PVLVNTDSLETPTYV CEEEECCCCCCCCEE	26.51	29899451
209	Phosphorylation	VNTDSLETPTYVNGT EECCCCCCCCEECCC	26.65	25338131
222	Phosphorylation	GTDADYEYEEITLER CCCCCCEEEEEEEEC	16.78	-
232	Phosphorylation	ITLERGNSGLGFSIA EEEECCCCCCCEEEC	37.91	19060867
237	Phosphorylation	GNSGLGFSIAGGTDN CCCCCCEEECCCCCC	15.10	-
291	Ubiquitination	VRDVTHSKAVEALKE HHCCCHHHHHHHHHH	49.17	-
297	Ubiquitination	SKAVEALKEAGSIVR HHHHHHHHHHCCEEE	53.19	-
301	Phosphorylation	EALKEAGSIVRLYVK HHHHHHCCEEEEEEC	25.59	22324799
306	Phosphorylation	AGSIVRLYVKRRKPA HCCEEEEEECCCCCC	8.05	22324799
321	Acetylation	SEKIMEIKLIKGPKG CHHHEEEEEEECCCC	30.74	22902405
321	Ubiquitination	SEKIMEIKLIKGPKG CHHHEEEEEEECCCC	30.74	-
327	Ubiquitination	IKLIKGPKGLGFSIA EEEEECCCCCCCEEC	75.36	-
376	Phosphorylation	DKLLAVNSVCLEEVT CEEEEEEEEEEEECC	13.96	29514104
378	S-palmitoylation	LLAVNSVCLEEVTHE EEEEEEEEEEECCHH	3.87	28680068
383	Phosphorylation	SVCLEEVTHEEAVTA EEEEEECCHHHHHHH	27.18	23984901
389	Phosphorylation	VTHEEAVTALKNTSD CCHHHHHHHHHCCCC	33.06	23984901
399	Phosphorylation	KNTSDFVYLKVAKPT HCCCCEEEEEECCCC	10.78	25195567
414	Phosphorylation	SMYINDGYAPPDITN CEECCCCCCCCCCCC	20.85	29514104
432	Phosphorylation	QSVDNHVSPSSCLGQ CCCCCCCCHHHHCCC	16.12	-
434	Phosphorylation	VDNHVSPSSCLGQTP CCCCCCHHHHCCCCC	26.61	-
435	Phosphorylation	DNHVSPSSCLGQTPT CCCCCHHHHCCCCCC	19.42	-
440	Phosphorylation	PSSCLGQTPTSPARY HHHHCCCCCCCCCCC	27.08	-
442	Phosphorylation	SCLGQTPTSPARYSP HHCCCCCCCCCCCCC	51.21	25338131
443	Phosphorylation	CLGQTPTSPARYSPI HCCCCCCCCCCCCCC	20.12	29514104
447	Phosphorylation	TPTSPARYSPISKAV CCCCCCCCCCCCHHH	22.39	21743459
448	Phosphorylation	PTSPARYSPISKAVL CCCCCCCCCCCHHHH	15.37	18779572
451	Phosphorylation	PARYSPISKAVLGDD CCCCCCCCHHHHCCC	20.25	-
452	Ubiquitination	ARYSPISKAVLGDDE CCCCCCCHHHHCCCC	43.14	-
517	Phosphorylation	DRIISVNSVDLRAAS CEEEEECCEECHHCC	18.17	26239621
556	Ubiquitination	EYSRFEAKIHDLREQ HHHHHHHHHHHHHHH	33.12	-
567	Phosphorylation	LREQMMNSSVSSGSG HHHHHHHCCCCCCCC	17.77	25619855
568	Phosphorylation	REQMMNSSVSSGSGS HHHHHHCCCCCCCCC	22.48	25521595
570	Phosphorylation	QMMNSSVSSGSGSLR HHHHCCCCCCCCCCC	30.81	27742792
571	Phosphorylation	MMNSSVSSGSGSLRT HHHCCCCCCCCCCCC	34.52	25521595
573	Phosphorylation	NSSVSSGSGSLRTSQ HCCCCCCCCCCCCCC	27.44	25521595
575	Phosphorylation	SVSSGSGSLRTSQKR CCCCCCCCCCCCCCC	19.17	25521595
578	Phosphorylation	SGSGSLRTSQKRSLY CCCCCCCCCCCCEEE	40.58	25266776
579	Phosphorylation	GSGSLRTSQKRSLYV CCCCCCCCCCCEEEE	27.54	25266776
585	Phosphorylation	TSQKRSLYVRALFDY CCCCCEEEEEHHCCC	6.80	25521595
592	Phosphorylation	YVRALFDYDKTKDSG EEEHHCCCCCCCCCC	16.41	29899451
594	Ubiquitination	RALFDYDKTKDSGLP EHHCCCCCCCCCCCC	51.77	-
595	Phosphorylation	ALFDYDKTKDSGLPS HHCCCCCCCCCCCCC	36.87	29472430
598	Phosphorylation	DYDKTKDSGLPSQGL CCCCCCCCCCCCCCC	43.73	21082442
602	Phosphorylation	TKDSGLPSQGLNFRF CCCCCCCCCCCCEEC	41.75	25521595
619	Phosphorylation	ILHVINASDDEWWQA EEEEEECCCCHHHHC	40.90	21082442
624 (in isoform 2)	Phosphorylation	-	4.66	29514104
630	Phosphorylation	WWQARQVTPDGESDE HHHCEEECCCCCCCC	13.81	25521595
631 (in isoform 2)	Phosphorylation	-	49.07	29472430
635	Phosphorylation	QVTPDGESDEVGVIP EECCCCCCCCCCCCC	44.60	29899451
637 (in isoform 2)	Phosphorylation	-	50.91	30352176
643	Phosphorylation	DEVGVIPSKRRVEKK CCCCCCCCCCCCCHH	27.89	22324799
644	Ubiquitination	EVGVIPSKRRVEKKE CCCCCCCCCCCCHHH	38.58	-
657	Phosphorylation	KERARLKTVKFNSKT HHHHCCEEEEECCCC	33.26	29514104
657 (in isoform 3)	Phosphorylation	-	33.26	29514104
660 (in isoform 2)	Phosphorylation	-	12.40	26160508
664 (in isoform 2)	Phosphorylation	-	39.44	26160508
665 (in isoform 2)	Phosphorylation	-	55.86	26160508
671 (in isoform 3)	Phosphorylation	-	6.55	26824392
672 (in isoform 2)	Phosphorylation	-	27.52	23737553
673 (in isoform 2)	Phosphorylation	-	65.28	21149613
676 (in isoform 2)	Phosphorylation	-	32.95	25521595
677	Phosphorylation	EIPDDMGSKGLKHVT CCCCCCCCCCCCHHH	19.53	25521595
678 (in isoform 2)	Phosphorylation	-	63.63	21149613
680 (in isoform 2)	Phosphorylation	-	3.89	21149613
681 (in isoform 2)	Phosphorylation	-	44.70	26160508
682 (in isoform 2)	Phosphorylation	-	32.88	30635358
684	Phosphorylation	SKGLKHVTSNASDSE CCCCCHHHCCCCCCC	18.91	17242355
685	Phosphorylation	KGLKHVTSNASDSES CCCCHHHCCCCCCCC	29.34	29472430
688	Phosphorylation	KHVTSNASDSESSYR CHHHCCCCCCCCCCC	46.01	25521595
690	Phosphorylation	VTSNASDSESSYRGQ HHCCCCCCCCCCCCC	36.56	23684622
692	Phosphorylation	SNASDSESSYRGQEE CCCCCCCCCCCCCEE	36.30	28066266
693	Phosphorylation	NASDSESSYRGQEEY CCCCCCCCCCCCEEE	18.13	28066266
694 (in isoform 3)	Phosphorylation	-	28.21	26160508
698 (in isoform 3)	Phosphorylation	-	54.87	26160508
699 (in isoform 3)	Phosphorylation	-	32.81	26160508
706 (in isoform 3)	Phosphorylation	-	23.33	23737553
707 (in isoform 3)	Phosphorylation	-	7.25	21149613
710 (in isoform 3)	Phosphorylation	-	51.94	25521595
712 (in isoform 3)	Phosphorylation	-	6.04	21149613
714 (in isoform 3)	Phosphorylation	-	14.86	21149613
715 (in isoform 3)	Phosphorylation	-	24.24	26160508
716 (in isoform 3)	Phosphorylation	-	17.09	30635358
725	Ubiquitination	VIILGPMKDRVNDDL EEEEECCCCCCCHHH	45.58	22790023
739	Acetylation	LISEFPDKFGSCVPH HHHHCCCCCCCCCCC	52.44	22826441
739	Ubiquitination	LISEFPDKFGSCVPH HHHHCCCCCCCCCCC	52.44	-
742	Phosphorylation	EFPDKFGSCVPHTTR HCCCCCCCCCCCCCC	18.31	-
747	Phosphorylation	FGSCVPHTTRPKRDY CCCCCCCCCCCCCCE	20.59	-
754	Phosphorylation	TTRPKRDYEVDGRDY CCCCCCCEEECCCEE	23.14	23684622
761	Phosphorylation	YEVDGRDYHFVTSRE EEECCCEEEEECCHH	8.87	20116462
817	Ubiquitination	DVSGNAIKRLQIAQL ECCCHHHHHHHHEEE	44.65	-
835	Phosphorylation	SIFIKPKSMENIMEM EEEECHHHHHHHHHH	39.60	25521595
844	Ubiquitination	ENIMEMNKRLTEEQA HHHHHHHHHCCHHHH	47.69	-
854	Phosphorylation	TEEQARKTFERAMKL CHHHHHHHHHHHHHH	25.77	25338131

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
222	Y	Phosphorylation	Kinase	LCK	P06239	PSP
222	Y	Phosphorylation	Kinase	LCK	P06240	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Btrc	Q3ULA2	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
232	S	Phosphorylation		-
Phosphorylation of Ser-232 regulates association with GRIN2A (By similarity).

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LCK_MOUSE	Lck	physical	15699074
CBL_MOUSE	Cbl	physical	15699074
ZAP70_MOUSE	Zap70	physical	15699074
WASP_MOUSE	Was	physical	15699074
MK14_MOUSE	Mapk14	physical	17187070
ADA10_MOUSE	Adam10	physical	17301176
CSKP_MOUSE	Cask	physical	16105026

Drug and Disease Associations

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

Regulatory Network of DLG1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND MASSSPECTROMETRY.	16452087 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-684, PHOSPHORYLATION[LARGE SCALE ANALYSIS] AT SER-665 (ISOFORM 2), AND MASS SPECTROMETRY.	17242355 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-399, AND MASSSPECTROMETRY.	18034455 [Abstract]

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