DLG2_MOUSE - dbPTM
DLG2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DLG2_MOUSE
UniProt AC Q91XM9
Protein Name Disks large homolog 2
Gene Name Dlg2
Organism Mus musculus (Mouse).
Sequence Length 852
Subcellular Localization Cell membrane
Lipid-anchor . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cell junction, synapse. Membrane . Cell projection, axon . Concentrated in soma and postsynaptic density of a subset of neurons.
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..
Protein Sequence MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPELVHVSEKNLSQIENVHGYVLQSHISPLKASPAPIIVNTDTLDTIPYVNGTEIEYEFEEITLERGNSGLGFSIAGGTDNPHIGDDPGIFITKIIPGGAAAEDGRLRVNDCILRVNEVDVSEVSHSKAVEALKEAGSIVRLYVRRRRPILETVVEIKLFKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIDGGAAQKDGRLQVGDRLLMVNNYSLEEVTHEEAVAILKNTSDVVYLKVGKPTTIYMTDPYGPPDITHSYSPPMENHLLSGNNGTLEYKTSLPPISPGRYSPIPKHMLGEDDYTRPPEPVYSTVNKLCDKPASPRHYSPVECDKSFLLSTPYPHYHLGLLPDSDMTSHSQHSTATRQPSVTLQRAISLEGEPRKVVLHKGSTGLGFNIVGGEDGEGIFVSFILAGGPADLSGELQRGDQILSVNGIDLRGASHEQAAAALKGAGQTVTIIAQYQPEDYARFEAKIHDLREQMMNHSMSSGSGSLRTNQKRSLYVRAMFDYDKSKDSGLPSQGLSFKYGDILHVINASDDEWWQARRVTLDGDSEEMGVIPSKRRVERKERARLKTVKFNAKPGVIDSKGDIPGLGDDGYGTKTLRGQEDLILSYEPVTRQEINYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVISREQMEKDIQEHKFIEAGQYNDNLYGTSVQSVRFVAERGKHCILDVSGNAIKRLQVAQLYPIAIFIKPKSLEPLMEMNKRLTEEQAKKTYDRAIKLEQEFGEYFTAIVQGDTLEDIYNQCKLVIEEQSGPFIWIPSKEKL
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
5S-palmitoylation---MFFACYCALRTN
---CCCHHHHHHHHC		2.12-
7S-palmitoylation-MFFACYCALRTNVK
-CCCHHHHHHHHCCE		2.64-
28PhosphorylationEDGPHDHSLPRLTHE
CCCCCCCCCCCCCCC		46.2425521595
33PhosphorylationDHSLPRLTHEVRGPE
CCCCCCCCCCCCCCE		19.7829899451
45PhosphorylationGPELVHVSEKNLSQI
CCEEEEECCCCHHHH		28.1625521595
50PhosphorylationHVSEKNLSQIENVHG
EECCCCHHHHCCHHH		38.2122324799
58PhosphorylationQIENVHGYVLQSHIS
HHCCHHHHEEECCCC		5.3229899451
62PhosphorylationVHGYVLQSHISPLKA
HHHHEEECCCCCCCC		20.7325521595
65PhosphorylationYVLQSHISPLKASPA
HEEECCCCCCCCCCC		20.8225521595
106PhosphorylationITLERGNSGLGFSIA
EEECCCCCCCCEEEC		37.9129899451
111PhosphorylationGNSGLGFSIAGGTDN
CCCCCCEEECCCCCC		15.10-
122 (in isoform 7)Phosphorylation-31.2729899451
131UbiquitinationDPGIFITKIIPGGAA
CCCEEEEEECCCCHH		33.55-
165UbiquitinationVSEVSHSKAVEALKE
HHHCCCHHHHHHHHH		51.53-
171UbiquitinationSKAVEALKEAGSIVR
HHHHHHHHHHCCCHH		53.19-
175PhosphorylationEALKEAGSIVRLYVR
HHHHHHCCCHHEEHH		25.5918056256
201UbiquitinationIKLFKGPKGLGFSIA
EEECCCCCCCCEEEC		75.36-
235UbiquitinationIDGGAAQKDGRLQVG
EECCCCCCCCCCEEC		58.38-
236UbiquitinationDGGAAQKDGRLQVGD
ECCCCCCCCCCEECC		35.05-
268PhosphorylationAVAILKNTSDVVYLK
HHHHHHCCCCEEEEE		25.3929899451
269PhosphorylationVAILKNTSDVVYLKV
HHHHHCCCCEEEEEE		37.4929899451
288PhosphorylationTIYMTDPYGPPDITH
EEEEECCCCCCCCCC		45.1129899451
296PhosphorylationGPPDITHSYSPPMEN
CCCCCCCCCCCCCCC		20.7529899451
297PhosphorylationPPDITHSYSPPMENH
CCCCCCCCCCCCCCC		20.0029899451
298PhosphorylationPDITHSYSPPMENHL
CCCCCCCCCCCCCCE		27.6729899451
307PhosphorylationPMENHLLSGNNGTLE
CCCCCEECCCCCCEE		45.9222817900
312PhosphorylationLLSGNNGTLEYKTSL
EECCCCCCEEEECCC		20.6622817900
317PhosphorylationNGTLEYKTSLPPISP
CCCEEEECCCCCCCC		34.3026804993
318PhosphorylationGTLEYKTSLPPISPG
CCEEEECCCCCCCCC		34.4221183079
323PhosphorylationKTSLPPISPGRYSPI
ECCCCCCCCCCCCCC		30.9425521595
327PhosphorylationPPISPGRYSPIPKHM
CCCCCCCCCCCCHHH		25.3922817900
328PhosphorylationPISPGRYSPIPKHML
CCCCCCCCCCCHHHC		18.2625521595
332UbiquitinationGRYSPIPKHMLGEDD
CCCCCCCHHHCCCCC		42.22-
340PhosphorylationHMLGEDDYTRPPEPV
HHCCCCCCCCCCCCC		19.5718034455
341O-linked_GlycosylationMLGEDDYTRPPEPVY
HCCCCCCCCCCCCCC		43.638505205
341PhosphorylationMLGEDDYTRPPEPVY
HCCCCCCCCCCCCCC		43.6325177544
342PhosphorylationLGEDDYTRPPEPVYS
CCCCCCCCCCCCCCH		38.25-
347PhosphorylationYTRPPEPVYSTVNKL
CCCCCCCCCHHHHHH		5.86-
348PhosphorylationTRPPEPVYSTVNKLC
CCCCCCCCHHHHHHC		14.8925177544
349PhosphorylationRPPEPVYSTVNKLCD
CCCCCCCHHHHHHCC		26.55-
350PhosphorylationPPEPVYSTVNKLCDK
CCCCCCHHHHHHCCC		15.4829899451
353PhosphorylationPVYSTVNKLCDKPAS
CCCHHHHHHCCCCCC		46.27-
357UbiquitinationTVNKLCDKPASPRHY
HHHHHCCCCCCCCCC		41.30-
358PhosphorylationVNKLCDKPASPRHYS
HHHHCCCCCCCCCCC		25.39-
360PhosphorylationKLCDKPASPRHYSPV
HHCCCCCCCCCCCCC		30.8725521595
362PhosphorylationCDKPASPRHYSPVEC
CCCCCCCCCCCCCCC		38.59-
363PhosphorylationDKPASPRHYSPVECD
CCCCCCCCCCCCCCC		30.70-
364PhosphorylationKPASPRHYSPVECDK
CCCCCCCCCCCCCCC		18.8921183079
365PhosphorylationPASPRHYSPVECDKS
CCCCCCCCCCCCCCC		19.1525521595
393PhosphorylationLLPDSDMTSHSQHST
CCCCCCCCCCCCCCC		28.4222807455
400PhosphorylationTSHSQHSTATRQPSV
CCCCCCCCCCCCCCE		29.8922807455
406PhosphorylationSTATRQPSVTLQRAI
CCCCCCCCEEEEEEH		21.2822324799
408PhosphorylationATRQPSVTLQRAISL
CCCCCCEEEEEEHHC		22.8522324799
414PhosphorylationVTLQRAISLEGEPRK
EEEEEEHHCCCCCCE		21.2725521595
500PhosphorylationTVTIIAQYQPEDYAR
EEEEEEEECHHHHHH		19.6018034455
505PhosphorylationAQYQPEDYARFEAKI
EEECHHHHHHHHHHH		9.6718034455
511UbiquitinationDYARFEAKIHDLREQ
HHHHHHHHHHHHHHH		33.12-
525PhosphorylationQMMNHSMSSGSGSLR
HHHHCCCCCCCCCCC		34.2622807455
526PhosphorylationMMNHSMSSGSGSLRT
HHHCCCCCCCCCCCC		28.4722807455
528PhosphorylationNHSMSSGSGSLRTNQ
HCCCCCCCCCCCCCC		27.4419060867
530PhosphorylationSMSSGSGSLRTNQKR
CCCCCCCCCCCCCCC		19.1719060867
540PhosphorylationTNQKRSLYVRAMFDY
CCCCCEEEEEEEEEC		6.8025521595
550PhosphorylationAMFDYDKSKDSGLPS
EEEECCCCCCCCCCC		38.5021183079
553PhosphorylationDYDKSKDSGLPSQGL
ECCCCCCCCCCCCCE		46.0625521595
557PhosphorylationSKDSGLPSQGLSFKY
CCCCCCCCCCEEEEC		41.7525521595
561PhosphorylationGLPSQGLSFKYGDIL
CCCCCCEEEECCCEE		26.9020415495
574PhosphorylationILHVINASDDEWWQA
EEEEEECCCCCCEEE		40.9021183079
585PhosphorylationWWQARRVTLDGDSEE
CEEEEEEEECCCCCC		2.4824719451
590PhosphorylationRVTLDGDSEEMGVIP
EEEECCCCCCCCCCC		40.7729550500
598PhosphorylationEEMGVIPSKRRVERK
CCCCCCCCCCCCCHH		27.8929550500
618UbiquitinationKTVKFNAKPGVIDSK
EEEEECCCCCCCCCC		43.33-
624PhosphorylationAKPGVIDSKGDIPGL
CCCCCCCCCCCCCCC		27.6720415495
625UbiquitinationKPGVIDSKGDIPGLG
CCCCCCCCCCCCCCC		57.78-
636PhosphorylationPGLGDDGYGTKTLRG
CCCCCCCCCCCCCCC		28.7229899451
638PhosphorylationLGDDGYGTKTLRGQE
CCCCCCCCCCCCCCC		16.6329899451
639UbiquitinationGDDGYGTKTLRGQED
CCCCCCCCCCCCCCE		40.99-
640PhosphorylationDDGYGTKTLRGQEDL
CCCCCCCCCCCCCEE		22.8629899451
689PhosphorylationEFPDKFGSCVPHTTR
HCCCCCCCCCCCCCC		18.31-
694PhosphorylationFGSCVPHTTRPKRDY
CCCCCCCCCCCCCCE		20.59-
701PhosphorylationTTRPKRDYEVDGRDY
CCCCCCCEEECCCEE		23.1423684622
708PhosphorylationYEVDGRDYHFVISRE
EEECCCEEEEEEEHH		8.8729899451
732PhosphorylationKFIEAGQYNDNLYGT
CEEECCCCCCCCCCC		24.4618034455
737PhosphorylationGQYNDNLYGTSVQSV
CCCCCCCCCCCHHEE		25.3116141072
764UbiquitinationDVSGNAIKRLQVAQL
ECCCHHHHHHHHHHE		44.65-
791UbiquitinationEPLMEMNKRLTEEQA
HHHHHHHHHCCHHHH		47.69-
849UbiquitinationPFIWIPSKEKL----
CEEEECCCCCC----		54.21-
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
348YPhosphorylationKinaseFYNP39688
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DLG2_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DLG2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DLG2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-414, ANDMASS SPECTROMETRY.
"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-58; SER-62; TYR-340;TYR-348; TYR-500; TYR-505; TYR-732 AND TYR-737, AND MASS SPECTROMETRY.
"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-28; SER-175; SER-365 ANDSER-414, AND MASS SPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND MASSSPECTROMETRY.

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