CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014473
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Disks large homolog 3 
Protein Synonyms/Alias
 PSD-95/SAP90-related protein 1; Synapse-associated protein 102; SAP-102; SAP102 
Gene Name
 Dlg3 
Gene Synonyms/Alias
 Dlgh3 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
286IEGGAAQKDGRLQIGubiquitination[1]
683LISEFPHKFGSCVPHacetylation[2]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Required for learning most likely through its role in synaptic plasticity following NMDA receptor signaling (By similarity). 
Sequence Annotation
 DOMAIN 149 235 PDZ 1.
 DOMAIN 244 330 PDZ 2.
 DOMAIN 404 484 PDZ 3.
 DOMAIN 519 589 SH3.
 DOMAIN 659 834 Guanylate kinase-like.
 MOD_RES 705 705 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Phosphoprotein; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 849 AA 
Protein Sequence
MHKHQHCCKC PECYEVTRLA ALRRLEPPGY GDWQVPDPYG PSGGNGASSG YGGYSSQTLP 60
SQAGATPTPR TKAKLIPTGR DVGPVPPKPV PGKNTPKLNG SGPSWWPECT CTNRDWYEQA 120
SPAPLLVNPE ALEPSLSVNG SDGMFKYEEI VLERGNSGLG FSIAGGIDNP HVPDDPGIFI 180
TKIIPGGAAA MDGRLGVNDC VLRVNEVDVS EVVHSRAVEA LKEAGPVVRL VVRRRQPPPE 240
TIMEVNLLKG PKGLGFSIAG GIGNQHIPGD NSIYITKIIE GGAAQKDGRL QIGDRLLAVN 300
NTNLQDVRHE EAVASLKNTS DMVYLKVAKP GSLHLNDMYA PPDYASTFTA LADNHISHNS 360
SLGYLGAVES KVTYPAPPQV PPTRYSPIPR HMLAEEDFTR EPRKIILHKG STGLGFNIVG 420
GEDGEGIFVS FILAGGPADL SGELRRGDRI LSVNGVNLRN ATHEQAAAAL KRAGQSVTIV 480
AQYRPEEYSR FESKIHDLRE QMMNSSMSSG SGSLRTSEKR SLYVRALFDY DRTRDSCLPS 540
QGLSFSYGDI LHVINASDDE WWQARLVTPH GESEQIGVIP SKKRVEKKER ARLKTVKFHA 600
RTGMIESNRD FPGLSDDYYG AKNLKGVTSN TSDSESSSKG QEDAILSYEP VTRQEIHYAR 660
PVIILGPMKD RVNDDLISEF PHKFGSCVPH TTRPRRDNEV DGQDYHFVVS REQMEKDIQD 720
NKFIEAGQFN DNLYGTSIQS VRAVAERGKH CILDVSGNAI KRLQQAQLYP IAIFIKPKSI 780
EALMEMNRRQ TYEQANKIFD KAMKLEQEFG EYFTAIVQGD SLEEIYNKIK QIIEDQSGHY 840
IWVPSPEKL 849 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0043198; C:dendritic shaft; IDA:UniProtKB.
 GO:0030426; C:growth cone; IDA:UniProtKB.
 GO:0043025; C:neuronal cell body; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0014069; C:postsynaptic density; IDA:UniProtKB.
 GO:0005923; C:tight junction; IEA:Compara.
 GO:0019902; F:phosphatase binding; ISS:UniProtKB.
 GO:0019904; F:protein domain specific binding; IDA:RGD.
 GO:0001736; P:establishment of planar polarity; IEA:Compara.
 GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IEA:Compara.
 GO:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB. 
Interpro
 IPR008144; Guanylate_kin.
 IPR008145; Guanylate_kin/L-typ_Ca_channel.
 IPR020590; Guanylate_kinase_CS.
 IPR016313; M-assoc_guanylate_kinase.
 IPR019590; MAGUK_PEST_N.
 IPR027417; P-loop_NTPase.
 IPR001478; PDZ.
 IPR019583; PDZ_assoc.
 IPR001452; SH3_domain. 
Pfam
 PF00625; Guanylate_kin
 PF10608; MAGUK_N_PEST
 PF00595; PDZ
 PF10600; PDZ_assoc
 PF00018; SH3_1 
SMART
 SM00072; GuKc
 SM00228; PDZ
 SM00326; SH3 
PROSITE
 PS00856; GUANYLATE_KINASE_1
 PS50052; GUANYLATE_KINASE_2
 PS50106; PDZ
 PS50002; SH3 
PRINTS