DLG3_HUMAN - dbPTM
DLG3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DLG3_HUMAN
UniProt AC Q92796
Protein Name Disks large homolog 3
Gene Name DLG3
Organism Homo sapiens (Human).
Sequence Length 817
Subcellular Localization
Protein Description Required for learning most likely through its role in synaptic plasticity following NMDA receptor signaling..
Protein Sequence MHKHQHCCKCPECYEVTRLAALRRLEPPGYGDWQVPDPYGPGGGNGASAGYGGYSSQTLPSQAGATPTPRTKAKLIPTGRDVGPVPPKPVPGKSTPKLNGSGPSWWPECTCTNRDWYEQVNGSDGMFKYEEIVLERGNSGLGFSIAGGIDNPHVPDDPGIFITKIIPGGAAAMDGRLGVNDCVLRVNEVDVSEVVHSRAVEALKEAGPVVRLVVRRRQPPPETIMEVNLLKGPKGLGFSIAGGIGNQHIPGDNSIYITKIIEGGAAQKDGRLQIGDRLLAVNNTNLQDVRHEEAVASLKNTSDMVYLKVAKPGSLHLNDMYAPPDYASTFTALADNHISHNSSLGYLGAVESKVSYPAPPQVPPTRYSPIPRHMLAEEDFTREPRKIILHKGSTGLGFNIVGGEDGEGIFVSFILAGGPADLSGELRRGDRILSVNGVNLRNATHEQAAAALKRAGQSVTIVAQYRPEEYSRFESKIHDLREQMMNSSMSSGSGSLRTSEKRSLYVRALFDYDRTRDSCLPSQGLSFSYGDILHVINASDDEWWQARLVTPHGESEQIGVIPSKKRVEKKERARLKTVKFHARTGMIESNRDFPGLSDDYYGAKNLKGQEDAILSYEPVTRQEIHYARPVIILGPMKDRVNDDLISEFPHKFGSCVPHTTRPRRDNEVDGQDYHFVVSREQMEKDIQDNKFIEAGQFNDNLYGTSIQSVRAVAERGKHCILDVSGNAIKRLQQAQLYPIAIFIKPKSIEALMEMNRRQTYEQANKIYDKAMKLEQEFGEYFTAIVQGDSLEEIYNKIKQIIEDQSGHYIWVPSPEKL
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
1 (in isoform 3)Acetylation-9.5422814378
2 (in isoform 3)Acetylation-35.9822814378
4 (in isoform 3)Phosphorylation-14.1325159151
5 (in isoform 3)Phosphorylation-35.8025159151
6Ubiquitination--MHKHQHCCKCPEC
--CCCCCCCCCCCCH		20.7521890473
6 (in isoform 2)Ubiquitination-20.75-
8 (in isoform 2)Phosphorylation-4.8222617229
14PhosphorylationCCKCPECYEVTRLAA
CCCCCCHHHHHHHHH		16.2727196784
37 (in isoform 2)Phosphorylation-50.6328348404
78PhosphorylationTKAKLIPTGRDVGPV
CCCEECCCCCCCCCC		37.5416674116
94 (in isoform 3)Phosphorylation-56.7224719451
106 (in isoform 3)Phosphorylation-5.3325849741
109 (in isoform 3)Phosphorylation-3.1225849741
112 (in isoform 3)Phosphorylation-18.3524719451
112PhosphorylationWWPECTCTNRDWYEQ
CCCCCEECCCHHHHH		18.3520058876
117 (in isoform 3)Phosphorylation-10.77-
117PhosphorylationTCTNRDWYEQVNGSD
EECCCHHHHHHCCCC		10.7720058876
121 (in isoform 3)Phosphorylation-43.90-
123PhosphorylationWYEQVNGSDGMFKYE
HHHHHCCCCCCEEEE		26.2820058876
129 (in isoform 3)Phosphorylation-13.9224719451
137 (in isoform 3)Phosphorylation-24.2321955146
138 (in isoform 3)Phosphorylation-38.8430108239
139PhosphorylationIVLERGNSGLGFSIA
EEEECCCCCCCCEEE		37.9124076635
145 (in isoform 3)Phosphorylation-3.7430108239
146 (in isoform 3)Phosphorylation-14.6823663014
148 (in isoform 3)Phosphorylation-18.3023663014
149 (in isoform 3)Phosphorylation-4.5325159151
151 (in isoform 3)Phosphorylation-27.0223663014
153 (in isoform 3)Phosphorylation-50.4230108239
154 (in isoform 3)Phosphorylation-6.1630108239
155 (in isoform 3)Phosphorylation-36.9330108239
163PhosphorylationDDPGIFITKIIPGGA
CCCCEEEEEECCCCH		12.87-
240 (in isoform 2)Phosphorylation-3.7424719451
252 (in isoform 2)Phosphorylation-40.1125849741
255 (in isoform 2)Phosphorylation-3.4625849741
258 (in isoform 2)Phosphorylation-10.1424719451
263 (in isoform 2)Phosphorylation-22.19-
267 (in isoform 2)Phosphorylation-43.78-
268UbiquitinationIEGGAAQKDGRLQIG
EECCCCCCCCCCEEC		58.38-
275 (in isoform 2)Phosphorylation-10.8724719451
276 (in isoform 2)Ubiquitination-39.4221890473
283 (in isoform 2)Phosphorylation-24.6021955146
284 (in isoform 2)Phosphorylation-31.9130108239
291 (in isoform 2)Phosphorylation-36.7830108239
292 (in isoform 2)Phosphorylation-36.7723663014
294 (in isoform 2)Phosphorylation-10.1323663014
295 (in isoform 2)Phosphorylation-4.1525159151
297 (in isoform 2)Phosphorylation-33.0223663014
299 (in isoform 2)Phosphorylation-56.5430108239
300 (in isoform 2)Phosphorylation-50.5430108239
301 (in isoform 2)Phosphorylation-25.2330108239
306PhosphorylationKNTSDMVYLKVAKPG
CCCCCCEEEEECCCC		8.3118083107
314AcetylationLKVAKPGSLHLNDMY
EEECCCCCCCCCCCC		22.5719608861
365PhosphorylationAPPQVPPTRYSPIPR
CCCCCCCCCCCCCCH		35.8527732954
367PhosphorylationPQVPPTRYSPIPRHM
CCCCCCCCCCCCHHH		22.6827732954
368PhosphorylationQVPPTRYSPIPRHML
CCCCCCCCCCCHHHC		17.0524719451
458PhosphorylationALKRAGQSVTIVAQY
HHHHCCCEEEEEEEE		21.95-
460AcetylationKRAGQSVTIVAQYRP
HHCCCEEEEEEEECH		18.2519608861
487PhosphorylationLREQMMNSSMSSGSG
HHHHHHHCCCCCCCC		14.9927732954
488PhosphorylationREQMMNSSMSSGSGS
HHHHHHCCCCCCCCC		20.0627732954
490PhosphorylationQMMNSSMSSGSGSLR
HHHHCCCCCCCCCCC		33.2327732954
491PhosphorylationMMNSSMSSGSGSLRT
HHHCCCCCCCCCCCC		28.4727732954
493PhosphorylationNSSMSSGSGSLRTSE
HCCCCCCCCCCCCHH		27.4427732954
495PhosphorylationSMSSGSGSLRTSEKR
CCCCCCCCCCCHHCC		19.1727732954
498PhosphorylationSGSGSLRTSEKRSLY
CCCCCCCCHHCCHHH		46.6730177828
499PhosphorylationGSGSLRTSEKRSLYV
CCCCCCCHHCCHHHH		34.3930177828
503PhosphorylationLRTSEKRSLYVRALF
CCCHHCCHHHHHHHC		34.8118083107
505PhosphorylationTSEKRSLYVRALFDY
CHHCCHHHHHHHCCC		6.8029083192
512PhosphorylationYVRALFDYDRTRDSC
HHHHHCCCCCCCCCC		10.4522210691
515PhosphorylationALFDYDRTRDSCLPS
HHCCCCCCCCCCCCC		35.6122210691
539PhosphorylationILHVINASDDEWWQA
EEEEEECCCCCCEEE		40.9018220336
550PhosphorylationWWQARLVTPHGESEQ
CEEEEEECCCCCHHH		17.7323312004
555PhosphorylationLVTPHGESEQIGVIP
EECCCCCHHHCCCCC		39.1223312004
563PhosphorylationEQIGVIPSKKRVEKK
HHCCCCCCCCCCCHH		39.4224719451
589PhosphorylationARTGMIESNRDFPGL
HHCCCCCCCCCCCCC		26.6624719451
600PhosphorylationFPGLSDDYYGAKNLK
CCCCCCCCCCCCCCC		14.5927196784
601PhosphorylationPGLSDDYYGAKNLKG
CCCCCCCCCCCCCCC		20.0127196784
615PhosphorylationGQEDAILSYEPVTRQ
CCCCEEEEECCCCHH		22.7228796482
616PhosphorylationQEDAILSYEPVTRQE
CCCEEEEECCCCHHH		22.3228796482
620PhosphorylationILSYEPVTRQEIHYA
EEEECCCCHHHHEEC		37.0328796482
626PhosphorylationVTRQEIHYARPVIIL
CCHHHHEECCCEEEE		15.23-
637UbiquitinationVIILGPMKDRVNDDL
EEEECCCCCCCCCHH		45.58-
660PhosphorylationGSCVPHTTRPRRDNE
CCCCCCCCCCCCCCC		35.32-
672PhosphorylationDNEVDGQDYHFVVSR
CCCCCCCEEEEEEEH		44.3917016520
673PhosphorylationNEVDGQDYHFVVSRE
CCCCCCEEEEEEEHH		6.8321945579
678PhosphorylationQDYHFVVSREQMEKD
CEEEEEEEHHHHHHH		25.4621945579
759PhosphorylationMEMNRRQTYEQANKI
HHHHHHHHHHHHHHH		27.4920736484
760PhosphorylationEMNRRQTYEQANKIY
HHHHHHHHHHHHHHH		9.56-
765AcetylationQTYEQANKIYDKAMK
HHHHHHHHHHHHHHH		45.7319608861
808PhosphorylationIEDQSGHYIWVPSPE
HHCCCCCEEEECCCC		10.4519060867
813PhosphorylationGHYIWVPSPEKL---
CCEEEECCCCCC---		35.7524719451
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
295SPhosphorylationKinaseCSNK2A1P68400
GPS
295SPhosphorylationKinaseCK2BP67870
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DLG3_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 DLG3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCC2A_HUMANCAMK2Aphysical
17353931
K1H1_HUMANKRT31physical
17353931
KRT35_HUMANKRT35physical
17353931
KRT85_HUMANKRT85physical
17353931
KRT34_HUMANKRT34physical
17353931
ANXA1_HUMANANXA1physical
17353931
CUL2_HUMANCUL2physical
17353931
KRT82_HUMANKRT82physical
17353931
KLDC3_HUMANKLHDC3physical
17353931
S10A3_HUMANS100A3physical
17353931
APC_HUMANAPCphysical
9188857
EXOC4_HUMANEXOC4physical
12738960
EXOC3_HUMANEXOC3physical
12738960
NMDE2_HUMANGRIN2Bphysical
12738960
FAK2_HUMANPTK2Bphysical
12576483
SYGP1_HUMANSYNGAP1physical
9581761
DLG4_HUMANDLG4physical
10026200
DLGP1_HUMANDLGAP1physical
9115257
GUAD_HUMANGDAphysical
10542258
NMDE2_HUMANGRIN2Bphysical
11937501
CRIPT_HUMANCRIPTphysical
11937501
NMDE1_HUMANGRIN2Aphysical
11937501
NMDE3_HUMANGRIN2Cphysical
11937501
ARFG1_HUMANARFGAP1physical
26344197
KS6A4_HUMANRPS6KA4physical
26344197
DLG1_HUMANDLG1physical
26496610
AP3B1_HUMANAP3B1physical
26496610
RBCC1_HUMANRB1CC1physical
26496610
COBL1_HUMANCOBLL1physical
26496610
KCTD2_HUMANKCTD2physical
26496610
ACAD8_HUMANACAD8physical
26496610
WDR91_HUMANWDR91physical
26496610
RM18_HUMANMRPL18physical
26496610
RM22_HUMANMRPL22physical
26496610
S18L2_HUMANSS18L2physical
26496610
RT26_HUMANMRPS26physical
26496610
ZFP91_HUMANZFP91physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300850Mental retardation, X-linked 90 (MRX90)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DLG3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-765, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-673, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-673, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-673, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-673 AND TYR-808, ANDMASS SPECTROMETRY.

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