dbPTM

DLG2_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DLG2_RAT
UniProt AC	Q63622
Protein Name	Disks large homolog 2
Gene Name	Dlg2
Organism	Rattus norvegicus (Rat).
Sequence Length	852
Subcellular Localization	Cell membrane Lipid-anchor . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cell junction, synapse. Cell projection, axon . Membrane . Concentrated in soma and postsynaptic density of a subset of neurons (PubMed:11095503
Protein Description	Required for perception of chronic pain through NMDA receptor signaling. Regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord. Interacts with the cytoplasmic tail of NMDA receptor subunits as well as inward rectifying potassium channels. Involved in regulation of synaptic stability at cholinergic synapses. Part of the postsynaptic protein scaffold of excitatory synapses (By similarity)..
Protein Sequence	MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPELVHVSEKNLSQIENVHGYVLQSHISPLKASPAPIIVNTDTLDTIPYVNGTEIEYEFEEITLERGNSGLGFSIAGGTDNPHIGDDPGIFITKIIPGGAAAEDGRLRVNDCILRVNEVDVSEVSHSKAVEALKEAGSIVRLYVRRRRPILETVVEIKLFKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIDGGAAQKDGRLQVGDRLLMVNNYSLEEVTHEEAVAILKNTSDVVYLKVGKPTTIYMTDPYGPPDITHSYSPPMENHLLSGNNGTLEYKTSLPPISPGRYSPIPKHMLVEDDYTRPPEPVYSTVNKLCDKPASPRHYSPVECDKSFLLSTPYPHYHLGLLPDSDMTSHSQHSTATRQPSVTLQRAISLEGEPRKVVLHKGSTGLGFNIVGGEDGEGIFVSFILAGGPADLSGELQRGDQILSVNGIDLRGASHEQAAAALKGAGQTVTIIAQYQPEDYARFEAKIHDLREQMMNHSMSSGSGSLRTNQKRSLYVRAMFDYDKSKDSGLPSQGLSFKYGDILHVINASDDEWWQARRVILDGDSEEMGVIPSKRRVERKERARLKTVKFNAKPGVIDSKGDIPGLGDDGYGTKTLRGQEDLILSYEPVTRQEINYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVISREQMEKDIQEHKFIEAGQYNDNLYGTSVQSVRFVAERGKHCILDVSGNAIKRLQVAQLYPIAIFIKPKSLEPLMEMNKRLTEEQAKKTYDRAIKLEQEFGEYFTAIVQGDTLEDIYNQCKLVIEEQSGPFIWIPSKEKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	S-palmitoylation	---MFFACYCALRTN ---CCCHHHHHHHHC	2.12	10779526
7	S-palmitoylation	-MFFACYCALRTNVK -CCCHHHHHHHHCCE	2.64	10779526
28	Phosphorylation	EDGPHDHSLPRLTHE CCCCCCCCCCCCCCC	46.24	30240740
45	Phosphorylation	GPELVHVSEKNLSQI CCEEEEECCCCHHHH	28.16	30240740
58	Phosphorylation	QIENVHGYVLQSHIS HHCCHHHHEEECCCC	5.32	-
65	Phosphorylation	YVLQSHISPLKASPA HEEECCCCCCCCCCC	20.82	30240740
106	Phosphorylation	ITLERGNSGLGFSIA EEECCCCCCCCEEEC	37.91	12933808
165	Ubiquitination	VSEVSHSKAVEALKE HHHCCCHHHHHHHHH	51.53	-
171	Ubiquitination	SKAVEALKEAGSIVR HHHHHHHHHHCCCHH	53.19	-
175	Phosphorylation	EALKEAGSIVRLYVR HHHHHHCCCHHEEHH	25.59	29779826
201	Ubiquitination	IKLFKGPKGLGFSIA EEECCCCCCCCEEEC	75.36	-
223	Phosphorylation	IPGDNSIYVTKIIDG CCCCCEEEEEEEEEC	11.24	-
225	Phosphorylation	GDNSIYVTKIIDGGA CCCEEEEEEEEECCC	10.27	-
235	Ubiquitination	IDGGAAQKDGRLQVG EECCCCCCCCCCEEC	58.38	-
307	Phosphorylation	PMENHLLSGNNGTLE CCCCCEECCCCCCEE	45.92	-
323	Phosphorylation	KTSLPPISPGRYSPI ECCCCCCCCCCCCCC	27.37	30240740
327	Phosphorylation	PPISPGRYSPIPKHM CCCCCCCCCCCCCHH	25.39	25403869
328	Phosphorylation	PISPGRYSPIPKHML CCCCCCCCCCCCHHC	18.26	30240740
340	Phosphorylation	HMLVEDDYTRPPEPV HHCCCCCCCCCCCCC	19.57	-
341	Phosphorylation	MLVEDDYTRPPEPVY HCCCCCCCCCCCCCC	43.63	-
348	Phosphorylation	TRPPEPVYSTVNKLC CCCCCCCCHHHHHHC	14.89	13129934
349	Phosphorylation	RPPEPVYSTVNKLCD CCCCCCCHHHHHHCC	26.55	-
350	Phosphorylation	PPEPVYSTVNKLCDK CCCCCCHHHHHHCCC	15.48	-
357	Ubiquitination	TVNKLCDKPASPRHY HHHHHCCCCCCCCCC	41.30	-
360	Phosphorylation	KLCDKPASPRHYSPV HHCCCCCCCCCCCCC	30.87	30411139
364	Phosphorylation	KPASPRHYSPVECDK CCCCCCCCCCCCCCC	18.89	25403869
365	Phosphorylation	PASPRHYSPVECDKS CCCCCCCCCCCCCCC	19.15	30411139
379	Phosphorylation	SFLLSTPYPHYHLGL CEEECCCCCCCCCCC	11.61	-
382	Phosphorylation	LSTPYPHYHLGLLPD ECCCCCCCCCCCCCC	8.34	-
393	Phosphorylation	LLPDSDMTSHSQHST CCCCCCCCCCCCCCC	28.42	-
406	Phosphorylation	STATRQPSVTLQRAI CCCCCCCCEEEEEEH	21.28	25403869
414	Phosphorylation	VTLQRAISLEGEPRK EEEEEEHHCCCCCCE	21.27	27097102
505	Phosphorylation	AQYQPEDYARFEAKI EEECHHHHHHHHHHH	9.67	-
511	Ubiquitination	DYARFEAKIHDLREQ HHHHHHHHHHHHHHH	33.12	-
523	Phosphorylation	REQMMNHSMSSGSGS HHHHHHCCCCCCCCC	18.50	25403869
525	Phosphorylation	QMMNHSMSSGSGSLR HHHHCCCCCCCCCCC	34.26	25403869
526	Phosphorylation	MMNHSMSSGSGSLRT HHHCCCCCCCCCCCC	28.47	22673903
528	Phosphorylation	NHSMSSGSGSLRTNQ HCCCCCCCCCCCCCC	27.44	25403869
530	Phosphorylation	SMSSGSGSLRTNQKR CCCCCCCCCCCCCCC	19.17	25403869
547	Phosphorylation	YVRAMFDYDKSKDSG EEEEEEECCCCCCCC	17.63	-
553	Phosphorylation	DYDKSKDSGLPSQGL ECCCCCCCCCCCCCE	46.06	25403869
574	Phosphorylation	ILHVINASDDEWWQA EEEEEECCCCHHHHE	40.90	22673903
618	Ubiquitination	KTVKFNAKPGVIDSK EEEEECCCCCCCCCC	43.33	-
625	Ubiquitination	KPGVIDSKGDIPGLG CCCCCCCCCCCCCCC	57.78	-
635 (in isoform 7)	Phosphorylation	-	27.75	22673903
636	Phosphorylation	PGLGDDGYGTKTLRG CCCCCCCCCCCCCCC	28.72	-
639	Ubiquitination	GDDGYGTKTLRGQED CCCCCCCCCCCCCCE	40.99	-
689	Phosphorylation	EFPDKFGSCVPHTTR HCCCCCCCCCCCCCC	18.31	-
701	Phosphorylation	TTRPKRDYEVDGRDY CCCCCCCEEECCCEE	23.14	-
708	Phosphorylation	YEVDGRDYHFVISRE EEECCCEEEEEEEHH	8.87	-
732	Phosphorylation	KFIEAGQYNDNLYGT CEEECCCCCCCCCCC	24.46	-
737	Phosphorylation	GQYNDNLYGTSVQSV CCCCCCCCCCCHHEE	25.31	-
764	Ubiquitination	DVSGNAIKRLQVAQL ECCCHHHHHHHHHHE	44.65	-
791	Ubiquitination	EPLMEMNKRLTEEQA HHHHHHHHHCCHHHH	47.69	-

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
323	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
323	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
348	Y	Phosphorylation	Kinase	FYN	Q62844	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DLG2_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 DLG2_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DLG2_RAT !!

Drug and Disease Associations

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

Regulatory Network of DLG2_RAT

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"Ion channel clustering by membrane-associated guanylate kinases.Differential regulation by N-terminal lipid and metal bindingmotifs."; El-Husseini A.E., Topinka J.R., Lehrer-Graiwer J.E., Firestein B.L.,Craven S.E., Aoki C., Bredt D.S.; J. Biol. Chem. 275:23904-23910(2000). Cited for: MUTAGENESIS OF CYS-5 AND CYS-7, AND PALMITOYLATION AT CYS-5 AND CYS-7.	10779526 [Abstract]