dbPTM

DLG1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DLG1_RAT
UniProt AC	Q62696
Protein Name	Disks large homolog 1
Gene Name	Dlg1
Organism	Rattus norvegicus (Rat).
Sequence Length	911
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 (By similarity). 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. 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	MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVISIFQSNLFQALIDIQEFYEVTLLDNPKCVDHSKQCEPVQPGNPWESGSLSSAAVTSESLPGGLSPPVEKYRYQDEEVLPSERISPQVPNEVLGPELVHVSEKSLSEIENVHGFVSHSHISPIKPTEAVPPSSPIVPVTPALPVPAESPVVLPSTPQANPPPVLVNTDSLETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRLRVNDCILRVNEADVRDVTHSKAVEALKEAGSIVRLYVKRRKAFRKNHEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAVNSVCLEEVTHEEAVTALKNTSDFVYLKAAKPTSMYINDGYAPPDITNSSSQSVDNHVSPSSYLGQTPASPARYSPISKAVLGDDEITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVTIVAQYRPEEYSRFEAKIHDLRETMMNSSVSSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVTPDGESDEVGVIPSKRRVEKKERARLKTVKFNSKTRGDKGEIPDDMGSKGLKHVTSNASDSESSYHEYGCSKGGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRVNDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVRAVAEKGKHCILDVSGNAIKRLQIAQLYPISIFIKPKSMENIMEMNKRLTDEQARKTFERAVRLEQEFTEHFTAIVQGDTLEDIYNQVKQIIEEQSGPYIWVPAKEKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
39	Phosphorylation	SSIERVISIFQSNLF HHHHHHHHHHHHCHH	17.94	17156128
108	Phosphorylation	LSPPVEKYRYQDEEV CCCCCHHCCCCCCCC	10.88	28689409
110	Phosphorylation	PPVEKYRYQDEEVLP CCCHHCCCCCCCCCC	19.75	25575281
118	Phosphorylation	QDEEVLPSERISPQV CCCCCCCCCCCCCCC	35.03	25575281
122	Phosphorylation	VLPSERISPQVPNEV CCCCCCCCCCCCCCC	18.59	27097102
138	Phosphorylation	GPELVHVSEKSLSEI CHHEEECCHHCHHHH	25.16	29779826
141	Phosphorylation	LVHVSEKSLSEIENV EEECCHHCHHHHHCC	32.83	23984901
143	Phosphorylation	HVSEKSLSEIENVHG ECCHHCHHHHHCCCC	43.55	28432305
153	Phosphorylation	ENVHGFVSHSHISPI HCCCCCCCCCCCCCC	19.60	28432305
155	Phosphorylation	VHGFVSHSHISPIKP CCCCCCCCCCCCCCC	18.27	28432305
158	Phosphorylation	FVSHSHISPIKPTEA CCCCCCCCCCCCCCC	18.36	27097102
209	Phosphorylation	VNTDSLETPTYVNGT ECCCCCCCCCEECCC	26.65	-
232	Phosphorylation	ITLERGNSGLGFSIA EEEECCCCCCCEEEC	37.91	22108457
297	Ubiquitination	SKAVEALKEAGSIVR HHHHHHHHHCCHHHH	53.19	-
301	Phosphorylation	EALKEAGSIVRLYVK HHHHHCCHHHHHHHH	25.59	29779826
348	Phosphorylation	IPGDNSIYVTKIIEG CCCCCCEEEEEEEEC	11.24	-
350	Phosphorylation	GDNSIYVTKIIEGGA CCCCEEEEEEEECCC	10.27	-
375	Phosphorylation	DKLLAVNSVCLEEVT CEEEEEEEEEEEECC	13.96	22108457
394	Phosphorylation	VTALKNTSDFVYLKA HHHHHCCCCEEEEEE	38.14	30181290
398	Phosphorylation	KNTSDFVYLKAAKPT HCCCCEEEEEECCCC	11.50	28689409
431	Phosphorylation	QSVDNHVSPSSYLGQ CCCCCCCCHHHHCCC	16.12	-
439	Phosphorylation	PSSYLGQTPASPARY HHHHCCCCCCCCCCC	21.01	27097102
442	Phosphorylation	YLGQTPASPARYSPI HCCCCCCCCCCCCCC	21.94	27097102
446	Phosphorylation	TPASPARYSPISKAV CCCCCCCCCCCCHHH	22.39	30181290
447	Phosphorylation	PASPARYSPISKAVL CCCCCCCCCCCHHHH	15.37	18779572
450	Phosphorylation	PARYSPISKAVLGDD CCCCCCCCHHHHCCC	20.25	30181290
516	Phosphorylation	DRIISVNSVDLRAAS CEEEEECCEECHHCC	18.17	28432305
567	Phosphorylation	RETMMNSSVSSGSGS HHHHHHCCCCCCCCC	22.48	-
569	Phosphorylation	TMMNSSVSSGSGSLR HHHHCCCCCCCCCCC	30.81	28689409
570	Phosphorylation	MMNSSVSSGSGSLRT HHHCCCCCCCCCCCC	34.52	28689409
572	Phosphorylation	NSSVSSGSGSLRTSQ HCCCCCCCCCCCCCC	27.44	28689409
574	Phosphorylation	SVSSGSGSLRTSQKR CCCCCCCCCCCCCCC	19.17	28689409
577	Phosphorylation	SGSGSLRTSQKRSLY CCCCCCCCCCCCEEE	40.58	23984901
578	Phosphorylation	GSGSLRTSQKRSLYV CCCCCCCCCCCEEEE	27.54	-
591	Phosphorylation	YVRALFDYDKTKDSG EEEHHCCCCCCCCCC	16.41	-
593	Acetylation	RALFDYDKTKDSGLP EHHCCCCCCCCCCCC	51.77	22902405
594	Phosphorylation	ALFDYDKTKDSGLPS HHCCCCCCCCCCCCC	36.87	28432305
597	Phosphorylation	DYDKTKDSGLPSQGL CCCCCCCCCCCCCCC	43.73	25403869
601	Phosphorylation	TKDSGLPSQGLNFKF CCCCCCCCCCCCEEC	41.75	25575281
618	Phosphorylation	ILHVINASDDEWWQA EEEEEECCCCHHHHC	40.90	22673903
629	Phosphorylation	WWQARQVTPDGESDE HHHCEEECCCCCCCC	13.81	28689409
634	Phosphorylation	QVTPDGESDEVGVIP EECCCCCCCCCCCCC	44.60	30181290
642	Phosphorylation	DEVGVIPSKRRVEKK CCCCCCCCCCCCCHH	27.89	30181290
643	Ubiquitination	EVGVIPSKRRVEKKE CCCCCCCCCCCCHHH	38.58	-
676	Phosphorylation	EIPDDMGSKGLKHVT CCCCCCCCCCCCEEC	19.53	22673903
684	Phosphorylation	KGLKHVTSNASDSES CCCCEECCCCCCCCC	29.34	-
687	Phosphorylation	KHVTSNASDSESSYH CEECCCCCCCCCCCC	46.01	21630457
691	Phosphorylation	SNASDSESSYHEYGC CCCCCCCCCCCCCCC	39.90	-
693	Phosphorylation	ASDSESSYHEYGCSK CCCCCCCCCCCCCCC	14.14	-
748	Phosphorylation	EFPDKFGSCVPHTTR HCCCCCCCCCCCCCC	18.31	-
760	Phosphorylation	TTRPKRDYEVDGRDY CCCCCCCEEECCCEE	23.14	-
767	Phosphorylation	YEVDGRDYHFVTSRE EEECCCEEEEECCHH	8.87	-
791	Phosphorylation	KFIEAGQYNNHLYGT CEEECCCCCCCCCCC	19.60	26022182
798	Phosphorylation	YNNHLYGTSVQSVRA CCCCCCCCCHHHHHH	16.50	26022182
802	Phosphorylation	LYGTSVQSVRAVAEK CCCCCHHHHHHHHHC	16.06	26022182
841	Phosphorylation	SIFIKPKSMENIMEM EEEECHHHHHHHHHH	39.60	12933808

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
39	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
39	S	Phosphorylation	Kinase	CAMK2A	P11275	PSP
39	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
39	S	Phosphorylation	Kinase	CAMK2B	P08413	GPS
122	S	Phosphorylation	Kinase	P38G	Q63538	PSP
122	S	Phosphorylation	Kinase	P38D	Q9Z1B7	PSP
158	S	Phosphorylation	Kinase	P38D	Q9Z1B7	PSP
158	S	Phosphorylation	Kinase	P38G	P53778	PSP
158	S	Phosphorylation	Kinase	P38G	Q63538	PSP
158	S	Phosphorylation	Kinase	P38D	O15264	PSP
209	T	Phosphorylation	Kinase	P38G	P53778	PSP
209	T	Phosphorylation	Kinase	P38G	Q63538	PSP
209	T	Phosphorylation	Kinase	P38D	Q9Z1B7	PSP
209	T	Phosphorylation	Kinase	P38D	O15264	PSP
232	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
232	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
232	S	Phosphorylation	Kinase	CAMK2B	P08413	GPS
232	S	Phosphorylation	Kinase	CAMK2A	P11275	PSP
232	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
431	S	Phosphorylation	Kinase	P38G	Q63538	PSP
431	S	Phosphorylation	Kinase	P38D	Q9Z1B7	PSP
442	S	Phosphorylation	Kinase	P38D	O15264	PSP
442	S	Phosphorylation	Kinase	P38G	Q63538	PSP
442	S	Phosphorylation	Kinase	P38D	Q9Z1B7	PSP
442	S	Phosphorylation	Kinase	P38G	P53778	PSP
447	S	Phosphorylation	Kinase	P38G	Q63538	PSP
447	S	Phosphorylation	Kinase	P38D	Q9Z1B7	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
39	S	Phosphorylation	15044483
Phosphorylation of Ser-39 modulates transport to the plasma membrane and phosphorylation of Ser-232 regulates association with GRIN2A.
232	S	Phosphorylation	12933808
Phosphorylation of Ser-39 modulates transport to the plasma membrane and phosphorylation of Ser-232 regulates association with GRIN2A.

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AKAP5_HUMAN	AKAP5	physical	10939335
MPP3_RAT	Mpp3	physical	12351654
CSKP_RAT	Cask	physical	12351654
DLG2_RAT	Dlg2	physical	12351654
GRIA1_RAT	Gria1	physical	12050163
CAV3_RAT	Cav3	physical	15277200
KCNA5_RAT	Kcna5	physical	15277200

Drug and Disease Associations

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

Regulatory Network of DLG1_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Calcium/calmodulin-dependent protein kinase II phosphorylation drivessynapse-associated protein 97 into spines."; Mauceri D., Cattabeni F., Di Luca M., Gardoni F.; J. Biol. Chem. 279:23813-23821(2004). Cited for: MUTAGENESIS OF SER-39, PHOSPHORYLATION AT SER-39, SUBCELLULARLOCATION, AND FUNCTION.	15044483 [Abstract]
"CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction."; Gardoni F., Mauceri D., Fiorentini C., Bellone C., Missale C.,Cattabeni F., Di Luca M.; J. Biol. Chem. 278:44745-44752(2003). Cited for: MUTAGENESIS OF SER-232, PHOSPHORYLATION AT SER-232, AND INTERACTIONWITH GRIN2A.	12933808 [Abstract]

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