DLG1_HUMAN - dbPTM
DLG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DLG1_HUMAN
UniProt AC Q12959
Protein Name Disks large homolog 1 {ECO:0000305}
Gene Name DLG1 {ECO:0000312|HGNC:HGNC:2900}
Organism Homo sapiens (Human).
Sequence Length 904
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 . Apical cell membrane . Ce
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. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel..
Protein Sequence MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQPVNTWEISSLPSSTVTSETLPSSLSPSVEKYRYQDEDTPPQEHISPQITNEVIGPELVHVSEKNLSEIENVHGFVSHSHISPIKPTEAVLPSPPTVPVIPVLPVPAENTVILPTIPQANPPPVLVNTDSLETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRLRVNDCILRVNEVDVRDVTHSKAVEALKEAGSIVRLYVKRRKPVSEKIMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAVNNVCLEEVTHEEAVTALKNTSDFVYLKVAKPTSMYMNDGYAPPDITNSSSQPVDNHVSPSSFLGQTPASPARYSPVSKAVLGDDEITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVTIVAQYRPEEYSRFEAKIHDLREQMMNSSISSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVTPDGESDEVGVIPSKRRVEKKERARLKTVKFNSKTRDKGEIPDDMGSKGLKHVTSNASDSESSYRGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCILDVSGNAIKRLQIAQLYPISIFIKPKSMENIMEMNKRLTEEQARKTFERAMKLEQEFTEHFTAIVQGDTLEDIYNQVKQIIEEQSGSYIWVPAKEKL
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
3 (in isoform 8)Phosphorylation-13.2629438985
3 (in isoform 9)Phosphorylation-13.2629438985
9 (in isoform 8)Phosphorylation-36.6220068231
9 (in isoform 9)Phosphorylation-36.6220068231
12 (in isoform 8)Phosphorylation-2.9724719451
12 (in isoform 9)Phosphorylation-2.9724719451
13 (in isoform 8)Phosphorylation-27.6420068231
13 (in isoform 9)Phosphorylation-27.6420068231
16 (in isoform 8)Phosphorylation-60.3825954137
16 (in isoform 9)Phosphorylation-60.3825954137
18PhosphorylationALHLLEEYRSKLSQT
HHHHHHHHHHHCCHH
15.71-
21 (in isoform 8)Phosphorylation-43.0625954137
21 (in isoform 9)Phosphorylation-43.0625954137
22 (in isoform 8)Phosphorylation-4.9025954137
22 (in isoform 9)Phosphorylation-4.9025954137
23PhosphorylationEEYRSKLSQTEDRQL
HHHHHHCCHHHHHHH
38.5020068231
25PhosphorylationYRSKLSQTEDRQLRS
HHHHCCHHHHHHHHH
36.1620068231
32PhosphorylationTEDRQLRSSIERVIN
HHHHHHHHHHHHHHH
44.2328102081
33PhosphorylationEDRQLRSSIERVINI
HHHHHHHHHHHHHHH
23.2628102081
40 (in isoform 8)Phosphorylation-1.9825332170
40 (in isoform 9)Phosphorylation-1.9825332170
41 (in isoform 8)Phosphorylation-5.8725332170
41 (in isoform 9)Phosphorylation-5.8725332170
56PhosphorylationLIDIQEFYEVTLLDN
HHHHHHHHEEEECCC
14.5624275569
70PhosphorylationNPKCIDRSKPSEPIQ
CCCCCCCCCCCCCCC
45.2127080861
73PhosphorylationCIDRSKPSEPIQPVN
CCCCCCCCCCCCCCC
60.7927080861
81PhosphorylationEPIQPVNTWEISSLP
CCCCCCCEEEEECCC
25.3927080861
85PhosphorylationPVNTWEISSLPSSTV
CCCEEEEECCCCCCC
17.8229514088
86PhosphorylationVNTWEISSLPSSTVT
CCEEEEECCCCCCCC
50.3826657352
89PhosphorylationWEISSLPSSTVTSET
EEEECCCCCCCCCCC
43.8929514088
90PhosphorylationEISSLPSSTVTSETL
EEECCCCCCCCCCCC
25.5929514088
91PhosphorylationISSLPSSTVTSETLP
EECCCCCCCCCCCCC
31.9429514088
93PhosphorylationSLPSSTVTSETLPSS
CCCCCCCCCCCCCCC
22.4228450419
94PhosphorylationLPSSTVTSETLPSSL
CCCCCCCCCCCCCCC
25.0128450419
96PhosphorylationSSTVTSETLPSSLSP
CCCCCCCCCCCCCCC
43.6828450419
99PhosphorylationVTSETLPSSLSPSVE
CCCCCCCCCCCCCCE
47.2028450419
100PhosphorylationTSETLPSSLSPSVEK
CCCCCCCCCCCCCEE
30.8128450419
102PhosphorylationETLPSSLSPSVEKYR
CCCCCCCCCCCEEEC
19.6525159151
104PhosphorylationLPSSLSPSVEKYRYQ
CCCCCCCCCEEECCC
39.2628387310
107UbiquitinationSLSPSVEKYRYQDED
CCCCCCEEECCCCCC
32.6421906983
107 (in isoform 1)Ubiquitination-32.6421890473
107 (in isoform 2)Ubiquitination-32.6421890473
107 (in isoform 3)Ubiquitination-32.6421890473
107 (in isoform 4)Ubiquitination-32.6421890473
107 (in isoform 5)Ubiquitination-32.6421890473
107 (in isoform 6)Ubiquitination-32.6421890473
107 (in isoform 7)Ubiquitination-32.6421890473
108PhosphorylationLSPSVEKYRYQDEDT
CCCCCEEECCCCCCC
10.8830576142
110PhosphorylationPSVEKYRYQDEDTPP
CCCEEECCCCCCCCC
19.7530266825
115PhosphorylationYRYQDEDTPPQEHIS
ECCCCCCCCCHHCCC
34.5230266825
122PhosphorylationTPPQEHISPQITNEV
CCCHHCCCHHHHCCC
16.8030266825
126PhosphorylationEHISPQITNEVIGPE
HCCCHHHHCCCCCHH
21.7830266825
138PhosphorylationGPELVHVSEKNLSEI
CHHHEECCCCCHHHH
28.1625159151
140UbiquitinationELVHVSEKNLSEIEN
HHEECCCCCHHHHCC
56.53-
143PhosphorylationHVSEKNLSEIENVHG
ECCCCCHHHHCCCCC
46.0228176443
153PhosphorylationENVHGFVSHSHISPI
CCCCCCCCCCCCCCC
19.6030266825
155PhosphorylationVHGFVSHSHISPIKP
CCCCCCCCCCCCCCC
18.2730266825
158PhosphorylationFVSHSHISPIKPTEA
CCCCCCCCCCCCCCC
18.3630266825
158 (in isoform 3)Phosphorylation-18.3625849741
158 (in isoform 4)Phosphorylation-18.3625849741
158 (in isoform 5)Phosphorylation-18.3625849741
204PhosphorylationPPPVLVNTDSLETPT
CCCEEEECCCCCCCC
21.3428348404
206PhosphorylationPVLVNTDSLETPTYV
CEEEECCCCCCCCEE
26.5128348404
209PhosphorylationVNTDSLETPTYVNGT
EECCCCCCCCEECCC
26.6528348404
211PhosphorylationTDSLETPTYVNGTDA
CCCCCCCCEECCCCC
47.7428348404
212PhosphorylationDSLETPTYVNGTDAD
CCCCCCCEECCCCCC
7.9728348404
216PhosphorylationTPTYVNGTDADYEYE
CCCEECCCCCCCEEE
23.8628348404
220PhosphorylationVNGTDADYEYEEITL
ECCCCCCCEEEEEEE
23.3328102081
222PhosphorylationGTDADYEYEEITLER
CCCCCCEEEEEEEEC
16.7828102081
232PhosphorylationITLERGNSGLGFSIA
EEEECCCCCCCEEEC
37.9119060867
285UbiquitinationRVNEVDVRDVTHSKA
EECEEEHHHCCHHHH
28.3721890473
291UbiquitinationVRDVTHSKAVEALKE
HHHCCHHHHHHHHHH
49.17-
301PhosphorylationEALKEAGSIVRLYVK
HHHHHHCCEEEEEEE
25.5928857561
321UbiquitinationSEKIMEIKLIKGPKG
CHHHHEEEEEECCCC
30.74-
321 (in isoform 2)Ubiquitination-30.74-
347PhosphorylationQHIPGDNSIYVTKII
CCCCCCCCEEEEEEE
21.7519690332
350 (in isoform 5)Ubiquitination-4.1321890473
351PhosphorylationGDNSIYVTKIIEGGA
CCCCEEEEEEEECCC
10.2719690332
361UbiquitinationIEGGAAHKDGKLQIG
EECCCCCCCCCCCCC
64.55-
368 (in isoform 3)Ubiquitination-17.0321890473
368 (in isoform 4)Ubiquitination-17.0321890473
370UbiquitinationGKLQIGDKLLAVNNV
CCCCCCCEEEEEECE
39.94-
395PhosphorylationVTALKNTSDFVYLKV
HHHHHCCCCEEEEEE
38.1428442448
399PhosphorylationKNTSDFVYLKVAKPT
HCCCCEEEEEEECCC
10.7828152594
401UbiquitinationTSDFVYLKVAKPTSM
CCCEEEEEEECCCCC
23.5921890473
401UbiquitinationTSDFVYLKVAKPTSM
CCCEEEEEEECCCCC
23.5921890473
401 (in isoform 1)Ubiquitination-23.5921890473
401 (in isoform 2)Ubiquitination-23.5921890473
401 (in isoform 6)Ubiquitination-23.5921890473
401 (in isoform 7)Ubiquitination-23.5921890473
406PhosphorylationYLKVAKPTSMYMNDG
EEEEECCCCCCCCCC
25.9725002506
407PhosphorylationLKVAKPTSMYMNDGY
EEEECCCCCCCCCCC
19.2225002506
409PhosphorylationVAKPTSMYMNDGYAP
EECCCCCCCCCCCCC
7.7919901323
414PhosphorylationSMYMNDGYAPPDITN
CCCCCCCCCCCCCCC
20.8527259358
420PhosphorylationGYAPPDITNSSSQPV
CCCCCCCCCCCCCCC
36.1125002506
422PhosphorylationAPPDITNSSSQPVDN
CCCCCCCCCCCCCCC
23.7925002506
423PhosphorylationPPDITNSSSQPVDNH
CCCCCCCCCCCCCCC
34.7525002506
424PhosphorylationPDITNSSSQPVDNHV
CCCCCCCCCCCCCCC
38.0230576142
432PhosphorylationQPVDNHVSPSSFLGQ
CCCCCCCCHHHHCCC
16.1225002506
434PhosphorylationVDNHVSPSSFLGQTP
CCCCCCHHHHCCCCC
26.6425002506
435PhosphorylationDNHVSPSSFLGQTPA
CCCCCHHHHCCCCCC
28.0726074081
440PhosphorylationPSSFLGQTPASPARY
HHHHCCCCCCCCCCC
21.0126074081
443PhosphorylationFLGQTPASPARYSPV
HCCCCCCCCCCCCCC
21.9428188228
447PhosphorylationTPASPARYSPVSKAV
CCCCCCCCCCCCHHH
21.3126074081
448PhosphorylationPASPARYSPVSKAVL
CCCCCCCCCCCHHHH
17.1730576142
451PhosphorylationPARYSPVSKAVLGDD
CCCCCCCCHHHHCCC
20.4826074081
452UbiquitinationARYSPVSKAVLGDDE
CCCCCCCHHHHCCCC
42.63-
503PhosphorylationAGGPADLSGELRKGD
ECCCCCCCCCCCCCC
30.6722210691
514PhosphorylationRKGDRIISVNSVDLR
CCCCEEEEECCEECH
16.9330266825
517PhosphorylationDRIISVNSVDLRAAS
CEEEEECCEECHHCC
18.1730266825
533 (in isoform 2)Malonylation-39.7730639696
556UbiquitinationEYSRFEAKIHDLREQ
HHHHHHHHHHHHHHH
33.12-
567PhosphorylationLREQMMNSSISSGSG
HHHHHHHCCCCCCCC
15.9130266825
568PhosphorylationREQMMNSSISSGSGS
HHHHHHCCCCCCCCC
22.8330266825
570PhosphorylationQMMNSSISSGSGSLR
HHHHCCCCCCCCCCC
30.5123401153
571PhosphorylationMMNSSISSGSGSLRT
HHHCCCCCCCCCCCC
35.0029255136
573PhosphorylationNSSISSGSGSLRTSQ
HCCCCCCCCCCCCCC
27.4429255136
575PhosphorylationSISSGSGSLRTSQKR
CCCCCCCCCCCCCCC
19.1729255136
578PhosphorylationSGSGSLRTSQKRSLY
CCCCCCCCCCCCEEE
40.5830576142
579PhosphorylationGSGSLRTSQKRSLYV
CCCCCCCCCCCEEEE
27.5423927012
583PhosphorylationLRTSQKRSLYVRALF
CCCCCCCEEEEEHHC
30.9622496350
585PhosphorylationTSQKRSLYVRALFDY
CCCCCEEEEEHHCCC
6.80-
592PhosphorylationYVRALFDYDKTKDSG
EEEHHCCCCCCCCCC
16.4123312004
593 (in isoform 5)Ubiquitination-54.7321890473
595PhosphorylationALFDYDKTKDSGLPS
HHCCCCCCCCCCCCC
36.8720873877
598PhosphorylationDYDKTKDSGLPSQGL
CCCCCCCCCCCCCCC
43.7325159151
602PhosphorylationTKDSGLPSQGLNFKF
CCCCCCCCCCCCEEC
41.7520873877
611 (in isoform 3)Ubiquitination-43.3321890473
611 (in isoform 4)Ubiquitination-43.3321890473
619PhosphorylationILHVINASDDEWWQA
EEEEEECCCCHHHHC
40.9022617229
619 (in isoform 2)Phosphorylation-40.9018220336
630PhosphorylationWWQARQVTPDGESDE
HHHCEEECCCCCCCC
13.8128985074
635PhosphorylationQVTPDGESDEVGVIP
EECCCCCCCCCCCCC
44.6024719451
636PhosphorylationVTPDGESDEVGVIPS
ECCCCCCCCCCCCCC
50.7424719451
637 (in isoform 4)Phosphorylation-50.9122167270
643PhosphorylationDEVGVIPSKRRVEKK
CCCCCCCCCCCCCHH
27.8924719451
644AcetylationEVGVIPSKRRVEKKE
CCCCCCCCCCCCHHH
38.5811921265
644UbiquitinationEVGVIPSKRRVEKKE
CCCCCCCCCCCCHHH
38.582190698
644 (in isoform 1)Ubiquitination-38.5821890473
644 (in isoform 2)Ubiquitination-38.5821890473
644 (in isoform 6)Ubiquitination-38.5821890473
644 (in isoform 7)Ubiquitination-38.5821890473
657PhosphorylationKERARLKTVKFNSKT
HHHHHCEEEECCCCC
33.2622027822
657 (in isoform 4)Ubiquitination-33.2621890473
659UbiquitinationRARLKTVKFNSKTRD
HHHCEEEECCCCCCC
44.02-
660 (in isoform 4)Phosphorylation-12.4028450419
662PhosphorylationLKTVKFNSKTRDKGE
CEEEECCCCCCCCCC
38.2423312004
664PhosphorylationTVKFNSKTRDKGEIP
EEECCCCCCCCCCCC
43.8724719451
664 (in isoform 4)Phosphorylation-43.8723663014
665 (in isoform 4)Phosphorylation-47.5925849741
670 (in isoform 2)Phosphorylation-6.5522167270
672 (in isoform 4)Phosphorylation-65.2823927012
673 (in isoform 4)Phosphorylation-37.6823927012
676 (in isoform 4)Phosphorylation-19.5326503892
677AcetylationIPDDMGSKGLKHVTS
CCCCCCCCCCCCHHC
63.637427837
678 (in isoform 4)Phosphorylation-41.4723663014
680 (in isoform 4)Phosphorylation-44.7023663014
681 (in isoform 4)Phosphorylation-32.8823663014
682 (in isoform 4)Phosphorylation-6.3328450419
683PhosphorylationSKGLKHVTSNASDSE
CCCCCCHHCCCCCCC
18.9129255136
684PhosphorylationKGLKHVTSNASDSES
CCCCCHHCCCCCCCC
29.3429255136
687PhosphorylationKHVTSNASDSESSYR
CCHHCCCCCCCCCCC
46.0129255136
689PhosphorylationVTSNASDSESSYRGQ
HHCCCCCCCCCCCCC
36.5629255136
690 (in isoform 2)Ubiquitination-49.0121890473
691PhosphorylationSNASDSESSYRGQEE
CCCCCCCCCCCCCEE
36.3029255136
692PhosphorylationNASDSESSYRGQEEY
CCCCCCCCCCCCEEE
18.1329255136
693PhosphorylationASDSESSYRGQEEYV
CCCCCCCCCCCEEEE
28.2123927012
693 (in isoform 2)Phosphorylation-28.2128450419
697 (in isoform 2)Phosphorylation-54.8723663014
698 (in isoform 2)Phosphorylation-32.8125849741
705 (in isoform 2)Phosphorylation-23.3323927012
706 (in isoform 2)Phosphorylation-7.2523927012
709 (in isoform 2)Phosphorylation-51.9426503892
711 (in isoform 2)Phosphorylation-6.0423663014
713 (in isoform 2)Phosphorylation-14.8623663014
714 (in isoform 2)Phosphorylation-24.2423663014
715 (in isoform 2)Phosphorylation-17.0928450419
724UbiquitinationVIILGPMKDRINDDL
EEEECCCCCCCCHHH
47.17-
741PhosphorylationEFPDKFGSCVPHTTR
HCCCCCCCCCCCCCC
18.31-
753PhosphorylationTTRPKRDYEVDGRDY
CCCCCCCEEECCCEE
23.1428152594
760PhosphorylationYEVDGRDYHFVTSRE
EEECCCEEEEECCHH
8.8730183078
764PhosphorylationGRDYHFVTSREQMEK
CCEEEEECCHHHHHH
22.5628152594
765PhosphorylationRDYHFVTSREQMEKD
CEEEEECCHHHHHHH
28.6328152594
782PhosphorylationEHKFIEAGQYNNHLY
HHCEEECCCCCCCCC
20.0917389395
784PhosphorylationKFIEAGQYNNHLYGT
CEEECCCCCCCCCCC
19.6028796482
789PhosphorylationGQYNNHLYGTSVQSV
CCCCCCCCCCCHHHH
15.7128796482
791PhosphorylationYNNHLYGTSVQSVRE
CCCCCCCCCHHHHHH
16.5028796482
792PhosphorylationNNHLYGTSVQSVREV
CCCCCCCCHHHHHHH
17.5028442448
795PhosphorylationLYGTSVQSVREVAEK
CCCCCHHHHHHHHHC
22.4628442448
824PhosphorylationRLQIAQLYPISIFIK
HHHHEEEEEEEEEEC
6.09-
834PhosphorylationSIFIKPKSMENIMEM
EEEECHHHHHHHHHH
39.6028270605
843UbiquitinationENIMEMNKRLTEEQA
HHHHHHHHHCCHHHH
47.69-
853PhosphorylationTEEQARKTFERAMKL
CHHHHHHHHHHHHHH
25.7724719451
865 (in isoform 2)Ubiquitination-28.00-
892PhosphorylationKQIIEEQSGSYIWVP
HHHHHHCCCCEEEEE
32.74-
895PhosphorylationIEEQSGSYIWVPAKE
HHHCCCCEEEEECCC
11.43-
901UbiquitinationSYIWVPAKEKL----
CEEEEECCCCC----
49.68-

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
122SPhosphorylationKinaseP38DQ9Z1B7
PSP
122SPhosphorylationKinaseP38GQ63538
PSP
158SPhosphorylationKinaseCDK1P06493
PSP
158SPhosphorylationKinaseP38DQ9Z1B7
PSP
158SPhosphorylationKinaseP38GQ63538
PSP
158SPhosphorylationKinaseMAPK12P53778
GPS
158SPhosphorylationKinaseMAPK7Q13164
GPS
158SPhosphorylationKinaseCDK2P24941
PSP
209TPhosphorylationKinaseMAPK12P53778
GPS
209TPhosphorylationKinaseP38GQ63538
PSP
209TPhosphorylationKinaseP38DQ9Z1B7
PSP
232SPhosphorylationKinaseCAMK2-FAMILY-GPS
232SPhosphorylationKinaseCAM-KII_GROUP-PhosphoELM
443SPhosphorylationKinaseMAPK12P53778
GPS
443SPhosphorylationKinaseCDK2P24941
PSP
443SPhosphorylationKinaseCDK1P06493
PSP
657TPhosphorylationKinasePRKCAP17252
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:12902344
-KUbiquitinationE3 ubiquitin ligaseUBE3AQ05086
PMID:16482544
-KUbiquitinationE3 ubiquitin ligaseMARCHF2Q9P0N8
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseE6P03126
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
232SPhosphorylation

-

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AGRA2_HUMANGPR124physical
15021905
CSKP_HUMANCASKphysical
14960569
LIN7A_HUMANLIN7Aphysical
14960569
LIN7C_HUMANLIN7Cphysical
14960569
APBA1_HUMANAPBA1physical
14960569
KCJ12_HUMANKCNJ12physical
14960569
NMDE1_HUMANGRIN2Aphysical
12933808
GRIA1_HUMANGRIA1physical
12933808
FBW1A_HUMANBTRCphysical
12902344
ACTN2_HUMANACTN2physical
12860415
ADA17_HUMANADAM17physical
12668732
41_HUMANEPB41physical
7937897
DLGP1_HUMANDLGAP1physical
9115257
KCNJ6_HUMANKCNJ6physical
10619846
DLGP1_HUMANDLGAP1physical
9286858
GRIK2_HUMANGRIK2physical
11279111
DLGP1_HUMANDLGAP1physical
11060025
DLGP1_HUMANDLGAP1physical
9024696
KI13B_HUMANKIF13Bphysical
10859302
KCNJ2_HUMANKCNJ2physical
11181181
KCJ12_HUMANKCNJ12physical
11181181
KCNJ4_HUMANKCNJ4physical
11181181
CSKP_HUMANCASKphysical
10993877
LCK_HUMANLCKphysical
9341123
KCNA3_HUMANKCNA3physical
9341123
MARH2_HUMANMARCH2physical
17980554
ARHG8_HUMANNET1physical
19586902
KCNA5_HUMANKCNA5physical
16466689
MAP1A_HUMANMAP1Aphysical
9786987
ARHG8_HUMANNET1physical
17938206
ADA17_HUMANADAM17physical
18930083
TGFA_HUMANTGFAphysical
18930083

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DLG1_HUMAN

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Related Literatures of Post-Translational Modification
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 SER-575, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115; SER-122; SER-575;SER-684 AND SER-687, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684 AND SER-687, ANDMASS SPECTROMETRY.
"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-760, 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-760, AND MASSSPECTROMETRY.

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