DLGP2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DLGP2_RAT
• UniProt AC: P97837
• Protein Name: Disks large-associated protein 2 {ECO:0000250|UniProtKB:Q9P1A6}
• Gene Name: Dlgap2 {ECO:0000312|RGD:620224}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 1059
• Subcellular Localization: Cell membrane ; Peripheral membrane protein . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cell junction, synapse . Postsynaptic density of neuronal cells.
• Protein Description: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane..
• Protein Sequence: MGTAQVLPGILQKHCCILPDRNTESQCTLCGEPEEEEGGDLAQPGLSFPGPAEEDIDQQYSWSPTQHFSEERYSPAPRNMKGLTGSRNQPQLCVGHTCGLSPTDECEHPHDHVRHGPDVRQPYLLSPAESCPMDHHRCSPRSSVHSECMMMPVMLGDHVSSSTFPRMHYSSHYDTRDDCATSHASTKVNRIPANLLDQFEKQLPLHRDGFHTLQYHRASAATEQRNESPGRIRHLVHSVQKLFTKSHSLEGSSKSNINGTKSEGRMDDHHQSHLSKHSKRSKSKERKPESKHKSGMSSWWSSDDNLDSDSTYRTPSVAHRHHMDHIPHCYPEALQSPFGDLSLKTSKSNSDVKCSACEGLALTPDTRYMKRSSWSTLTVSQAKEAYRKSSLNLDKPLVHPEIKPSLQPCHYLQVPQDDWGAYPTGGKEEEIPCRRMRSGSYIKAMGDEESGESDSSPKTSPTVALRPEPLLKSIIQRPLGDHQTQSYLQAATEVPVGHSLDPSVNYNSPKFRSRNQSYMRAVSTLSQASCVSQMSEAEVNGQFESVCESVFSEVESQAMDALDLPGCFRTRSHSYLRAIQAGYSQDDECIPVMTPSNMTSTIRSTAAVSYTNYKKTPPPVPPRTTSKPLISVTAQSSTESTQDAYQDSRAQRMSPWPQDSRGGLYNSMDSLDSNKAMNLALESAAAQRHAADTQSSSTRSIDKAVLVSKAEELLKSRCSSIGVQDSEFPDHQPYPRSDVETATDSDTESRGLREYHSVGVQVEDEKRHGRFKRSNSVTAAVQADLELEGFPGHVSMEDKGLQFGSSFQRHSEPSTPTQYGALRTVRTQGLFSYREDYRTQVDTSTLPPPDPWLEPSLDTVETGRMSPCRRDGSWFLKLLHTETKKMEGWCKEMEREAEENDLSEEILGKIRSAVGSAQLLMSQKFQQFYWLCQQNMDPSAMPRPTSQDLAGYWDMLQLSVEDVSMKFDELHQLKLNDWKIMESPERKEERKIPPPIPKKPPKGKFPITREKSLDLPDRQRQEARRRLMAAKRAASFRQNSATERADSIEIYIPEAQTRL

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
123	Phosphorylation	GPDVRQPYLLSPAES CCCCCCCEECCHHHH	16.37	-
126	Phosphorylation	VRQPYLLSPAESCPM CCCCEECCHHHHCCC	21.33	-
139	Phosphorylation	PMDHHRCSPRSSVHS CCCCCCCCCCHHHHH	24.25	-
160	Phosphorylation	VMLGDHVSSSTFPRM HHCCCCCCCCCCCCC	18.36	-
169	Phosphorylation	STFPRMHYSSHYDTR CCCCCCCCCCCCCCC	11.52	-
170	Phosphorylation	TFPRMHYSSHYDTRD CCCCCCCCCCCCCCC	8.92	-
171	Phosphorylation	FPRMHYSSHYDTRDD CCCCCCCCCCCCCCC	20.92	-
173	Phosphorylation	RMHYSSHYDTRDDCA CCCCCCCCCCCCCHH	22.43	-
175	Phosphorylation	HYSSHYDTRDDCATS CCCCCCCCCCCHHHC	28.91	-
182	Phosphorylation	TRDDCATSHASTKVN CCCCHHHCCHHHHHH	9.87	-
187	Ubiquitination	ATSHASTKVNRIPAN HHCCHHHHHHCCCHH	34.71	-
201	Ubiquitination	NLLDQFEKQLPLHRD HHHHHHHHHCCCCCC	59.43	-
248	Phosphorylation	KLFTKSHSLEGSSKS HHHHCCCCCCCCCCC	34.90	25403869
301	Phosphorylation	SGMSSWWSSDDNLDS CCCCCCCCCCCCCCC	20.03	22673903
302	Phosphorylation	GMSSWWSSDDNLDSD CCCCCCCCCCCCCCC	34.95	22673903
308	Phosphorylation	SSDDNLDSDSTYRTP CCCCCCCCCCCCCCC	36.31	22673903
310	Phosphorylation	DDNLDSDSTYRTPSV CCCCCCCCCCCCCCH	31.15	22673903
311	Phosphorylation	DNLDSDSTYRTPSVA CCCCCCCCCCCCCHH	23.24	-
312	Phosphorylation	NLDSDSTYRTPSVAH CCCCCCCCCCCCHHH	19.21	-
314	Phosphorylation	DSDSTYRTPSVAHRH CCCCCCCCCCHHHHH	14.97	-
316	Phosphorylation	DSTYRTPSVAHRHHM CCCCCCCCHHHHHCH	31.18	-
353	Ubiquitination	SKSNSDVKCSACEGL CCCCCCCCCCCCCCE	27.71	-
363	Phosphorylation	ACEGLALTPDTRYMK CCCCEECCCCCCCCC	17.32	-
389	Phosphorylation	AKEAYRKSSLNLDKP HHHHHHHHCCCCCCC	30.93	22673903
390	Phosphorylation	KEAYRKSSLNLDKPL HHHHHHHCCCCCCCC	25.06	22673903
411	Phosphorylation	PSLQPCHYLQVPQDD CCCCCCEEEECCCCC	12.92	-
438	Phosphorylation	IPCRRMRSGSYIKAM CCCCHHCCCCCEEEC	23.81	22673903
440	Phosphorylation	CRRMRSGSYIKAMGD CCHHCCCCCEEECCC	25.57	16452087
441	Phosphorylation	RRMRSGSYIKAMGDE CHHCCCCCEEECCCC	15.23	22673903
450	Phosphorylation	KAMGDEESGESDSSP EECCCCCCCCCCCCC	45.90	22673903
453	Phosphorylation	GDEESGESDSSPKTS CCCCCCCCCCCCCCC	46.44	22673903
455	Phosphorylation	EESGESDSSPKTSPT CCCCCCCCCCCCCCC	58.79	22673903
456	Phosphorylation	ESGESDSSPKTSPTV CCCCCCCCCCCCCCE	35.09	22673903
459	Phosphorylation	ESDSSPKTSPTVALR CCCCCCCCCCCEECC	43.24	22673903
460	Phosphorylation	SDSSPKTSPTVALRP CCCCCCCCCCEECCC	25.38	22673903
462	Phosphorylation	SSPKTSPTVALRPEP CCCCCCCCEECCCHH	20.41	22673903
506	Phosphorylation	SLDPSVNYNSPKFRS CCCCCCCCCCHHHHH	18.18	-
508	Phosphorylation	DPSVNYNSPKFRSRN CCCCCCCCHHHHHCC	21.07	-
574	Phosphorylation	CFRTRSHSYLRAIQA CCCCCCHHHHHHHHC	27.40	30411139
575	Phosphorylation	FRTRSHSYLRAIQAG CCCCCHHHHHHHHCC	8.52	28551015
583	Phosphorylation	LRAIQAGYSQDDECI HHHHHCCCCCCCCCE	13.23	-
584	Phosphorylation	RAIQAGYSQDDECIP HHHHCCCCCCCCCEE	26.64	-
610	Phosphorylation	RSTAAVSYTNYKKTP HCCEEECCCCCCCCC	7.75	-
611	Phosphorylation	STAAVSYTNYKKTPP CCEEECCCCCCCCCC	25.27	-
613	Phosphorylation	AAVSYTNYKKTPPPV EEECCCCCCCCCCCC	13.18	-
616	Phosphorylation	SYTNYKKTPPPVPPR CCCCCCCCCCCCCCC	36.55	25403869
633	Phosphorylation	SKPLISVTAQSSTES CCCEEEEEECCCCCC	16.52	22673903
636	Phosphorylation	LISVTAQSSTESTQD EEEEEECCCCCCHHH	36.44	22673903
637	Phosphorylation	ISVTAQSSTESTQDA EEEEECCCCCCHHHH	24.90	22673903
638	Phosphorylation	SVTAQSSTESTQDAY EEEECCCCCCHHHHH	38.92	22673903
640	Phosphorylation	TAQSSTESTQDAYQD EECCCCCCHHHHHHH	31.30	22673903
641	Phosphorylation	AQSSTESTQDAYQDS ECCCCCCHHHHHHHH	25.00	22673903
645	Phosphorylation	TESTQDAYQDSRAQR CCCHHHHHHHHHHHH	22.57	-
665	Phosphorylation	QDSRGGLYNSMDSLD CCCCCCCCCCHHHCC	14.41	25403869
667	Phosphorylation	SRGGLYNSMDSLDSN CCCCCCCCHHHCCHH	15.48	25403869
670	Phosphorylation	GLYNSMDSLDSNKAM CCCCCHHHCCHHHHH	25.99	25403869
673	Phosphorylation	NSMDSLDSNKAMNLA CCHHHCCHHHHHHHH	45.59	25403869
700	Phosphorylation	TQSSSTRSIDKAVLV CCCCCCCCCCHHHHH	34.92	25403869
703	Ubiquitination	SSTRSIDKAVLVSKA CCCCCCCHHHHHHHH	38.43	-
709	Ubiquitination	DKAVLVSKAEELLKS CHHHHHHHHHHHHHH	52.95	-
719	Phosphorylation	ELLKSRCSSIGVQDS HHHHHHHHHCCCCCC	24.71	25403869
720	Phosphorylation	LLKSRCSSIGVQDSE HHHHHHHHCCCCCCC	27.30	25403869
741	Phosphorylation	YPRSDVETATDSDTE CCHHHCCCCCCCCCH	34.40	28551015
743	Phosphorylation	RSDVETATDSDTESR HHHCCCCCCCCCHHC	43.38	25403869
745	Phosphorylation	DVETATDSDTESRGL HCCCCCCCCCHHCCC	41.92	30411139
747	Phosphorylation	ETATDSDTESRGLRE CCCCCCCCHHCCCHH	39.55	28551015
749	Phosphorylation	ATDSDTESRGLREYH CCCCCCHHCCCHHHH	33.47	28551015
755	Phosphorylation	ESRGLREYHSVGVQV HHCCCHHHHCCEEEE	7.92	-
757	Phosphorylation	RGLREYHSVGVQVED CCCHHHHCCEEEEEC	21.47	-
776	Phosphorylation	GRFKRSNSVTAAVQA CCCCCCCCCCCEEEC	23.30	-
805	Phosphorylation	DKGLQFGSSFQRHSE HCCCCCCCCHHCCCC	29.30	25403869
806	Phosphorylation	KGLQFGSSFQRHSEP CCCCCCCCHHCCCCC	26.27	25403869
811	Phosphorylation	GSSFQRHSEPSTPTQ CCCHHCCCCCCCCCH	54.08	25403869
814	Phosphorylation	FQRHSEPSTPTQYGA HHCCCCCCCCCHHCC	42.86	-
815	Phosphorylation	QRHSEPSTPTQYGAL HCCCCCCCCCHHCCC	40.86	-
817	Phosphorylation	HSEPSTPTQYGALRT CCCCCCCCHHCCCHH	34.21	-
819	Phosphorylation	EPSTPTQYGALRTVR CCCCCCHHCCCHHHH	13.57	-
903	Phosphorylation	EAEENDLSEEILGKI HHHHCCCCHHHHHHH	35.73	-
983	Phosphorylation	NDWKIMESPERKEER CCCCCCCCCCHHHHC	18.06	22673903
1012	Phosphorylation	FPITREKSLDLPDRQ CCCCCCCCCCCCHHH	23.51	25403869
1040	Phosphorylation	AASFRQNSATERADS HHHHHHCCHHCCCCE	28.38	16452087
1047	Phosphorylation	SATERADSIEIYIPE CHHCCCCEEEEECCH	22.57	25403869
1051	Phosphorylation	RADSIEIYIPEAQTR CCCEEEEECCHHHHC	9.53	-

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
1012	S	Phosphorylation	Kinase	CAMK2A	P11275	PSP
1012	S	Phosphorylation	Kinase	CAMK2B	P08413	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DLGP2_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DLGP2_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAP1A_RAT	Map1a	physical	9786987

Drug and Disease Associations

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