Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00380
Entry Name
UniProt Accession
Theoretical PI
5.84
Molecular Weight
94934.34
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Disks large homolog 2
Protein Synonyms/Alias
Channel-associated protein of synapse-110; Chapsyn-110; Postsynaptic density protein PSD-93;
Gene Name
Dlg2
Gene Synonyms/Alias
Dlgh2;
Created Date
01-NOV-1997
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
5
Canonical
***MFFACYCALRTN
[1]
S-Palmitoylation
7
Canonical
*MFFACYCALRTNVK
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] El-Husseini AE, Topinka JR, Lehrer-Graiwer JE, Firestein BL, Craven SE, AokiC, Bredt DS. Ion channel clustering by membrane-associated guanylate kinases.Differential regulation by N-terminal lipid and metal binding motifs. J BiolChem. 2000 Aug 4;275(31):23904-10.[PMID:10779526]
Functional 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).
Sequence Annotation
Domain: 98 184 PDZ 1.
Domain: 193 279 PDZ 2.
Domain: 421 501 PDZ 3.
Domain: 536 606 SH3.
Domain: 662 837 Guanylate kinase-like.
Modified residue: 28 28 Phosphoserine.
Modified residue: 58 58 Phosphotyrosine.
Modified residue: 65 65 Phosphoserine.
Modified residue: 414 414 Phosphoserine.
Modified residue: 505 505 Phosphotyrosine.
Modified residue: 732 732 Phosphotyrosine.
Modified residue: 737 737 Phosphotyrosine.
Protein Length
852 AA.
Protein Sequence
(Canonical)
MFFACYCALR TNVKKYRYQD EDGPHDHSLP RLTHEVRGPE LVHVSEKNLS QIENVHGYVL  60
QSHISPLKAS PAPIIVNTDT LDTIPYVNGT EIEYEFEEIT LERGNSGLGF SIAGGTDNPH  120
IGDDPGIFIT KIIPGGAAAE DGRLRVNDCI LRVNEVDVSE VSHSKAVEAL KEAGSIVRLY  180
VRRRRPILET VVEIKLFKGP KGLGFSIAGG VGNQHIPGDN SIYVTKIIDG GAAQKDGRLQ  240
VGDRLLMVNN YSLEEVTHEE AVAILKNTSD VVYLKVGKPT TIYMTDPYGP PDITHSYSPP  300
MENHLLSGNN GTLEYKTSLP PISPGRYSPI PKHMLVEDDY TRPPEPVYST VNKLCDKPAS  360
PRHYSPVECD KSFLLSTPYP HYHLGLLPDS DMTSHSQHST ATRQPSVTLQ RAISLEGEPR  420
KVVLHKGSTG LGFNIVGGED GEGIFVSFIL AGGPADLSGE LQRGDQILSV NGIDLRGASH  480
EQAAAALKGA GQTVTIIAQY QPEDYARFEA KIHDLREQMM NHSMSSGSGS LRTNQKRSLY  540
VRAMFDYDKS KDSGLPSQGL SFKYGDILHV INASDDEWWQ ARRVILDGDS EEMGVIPSKR  600
RVERKERARL KTVKFNAKPG VIDSKGDIPG LGDDGYGTKT LRGQEDLILS YEPVTRQEIN  660
YTRPVIILGP MKDRINDDLI SEFPDKFGSC VPHTTRPKRD YEVDGRDYHF VISREQMEKD  720
IQEHKFIEAG QYNDNLYGTS VQSVRFVAER GKHCILDVSG NAIKRLQVAQ LYPIAIFIKP  780
KSLEPLMEMN KRLTEEQAKK TYDRAIKLEQ EFGEYFTAIV QGDTLEDIYN QCKLVIEEQS  840
GPFIWIPSKE KL                                                      852
FASTA
(Canonical)
>LipidDB-10116-00380|Q63622
MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPELVHVSEKNLSQIENVHGYVL
QSHISPLKASPAPIIVNTDTLDTIPYVNGTEIEYEFEEITLERGNSGLGFSIAGGTDNPH
IGDDPGIFITKIIPGGAAAEDGRLRVNDCILRVNEVDVSEVSHSKAVEALKEAGSIVRLY
VRRRRPILETVVEIKLFKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIDGGAAQKDGRLQ
VGDRLLMVNNYSLEEVTHEEAVAILKNTSDVVYLKVGKPTTIYMTDPYGPPDITHSYSPP
MENHLLSGNNGTLEYKTSLPPISPGRYSPIPKHMLVEDDYTRPPEPVYSTVNKLCDKPAS
PRHYSPVECDKSFLLSTPYPHYHLGLLPDSDMTSHSQHSTATRQPSVTLQRAISLEGEPR
KVVLHKGSTGLGFNIVGGEDGEGIFVSFILAGGPADLSGELQRGDQILSVNGIDLRGASH
EQAAAALKGAGQTVTIIAQYQPEDYARFEAKIHDLREQMMNHSMSSGSGSLRTNQKRSLY
VRAMFDYDKSKDSGLPSQGLSFKYGDILHVINASDDEWWQARRVILDGDSEEMGVIPSKR
RVERKERARLKTVKFNAKPGVIDSKGDIPGLGDDGYGTKTLRGQEDLILSYEPVTRQEIN
YTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVISREQMEKD
IQEHKFIEAGQYNDNLYGTSVQSVRFVAERGKHCILDVSGNAIKRLQVAQLYPIAIFIKP
KSLEPLMEMNKRLTEEQAKKTYDRAIKLEQEFGEYFTAIVQGDTLEDIYNQCKLVIEEQS
GPFIWIPSKEKL
Gene Ontology
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0005737; C:cytoplasm; IDA:RGD
GO:0030425; C:dendrite; IDA:RGD
GO:0044224; C:juxtaparanode region of axon; IDA:MGI
GO:0016020; C:membrane; IDA:RGD
GO:0043025; C:neuronal cell body; IDA:RGD
GO:0014069; C:postsynaptic density; TAS:UniProtKB
GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW
GO:0030165; F:PDZ domain binding; IPI:RGD
GO:0008022; F:protein C-terminus binding; IPI:UniProtKB
GO:0046982; F:protein heterodimerization activity; IPI:RGD
GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL
GO:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB
GO:0045161; P:neuronal ion channel clustering; IMP:RGD
GO:0043113; P:receptor clustering; IMP:RGD
Interpro
InterPro; IPR016313; DLG1
InterPro; IPR008145; GK/Ca_channel_bsu
InterPro; IPR008144; Guanylate_kin-like
InterPro; IPR020590; Guanylate_kinase_CS
InterPro; IPR019590; MAGUK_PEST_N
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR001478; PDZ
InterPro; IPR019583; PDZ_assoc
InterPro; IPR011511; SH3_2
InterPro; IPR001452; SH3_domain
Pfam
Pfam; PF00625; Guanylate_kin;
Pfam; PF10608; MAGUK_N_PEST;
Pfam; PF00595; PDZ;
Pfam; PF10600; PDZ_assoc;
Pfam; PF07653; SH3_2;
SMART
SMART; SM00072; GuKc;
SMART; SM00228; PDZ;
SMART; SM00326; SH3;
PROSITE
PROSITE; PS00856; GUANYLATE_KINASE_1;
PROSITE; PS50052; GUANYLATE_KINASE_2;
PROSITE; PS50106; PDZ;
PROSITE; PS50002; SH3;
PRINTS