CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014451
UniProt Accession
Genbank Protein ID
 U14950 
Genbank Nucleotide ID
Protein Name
 Disks large homolog 1 
Protein Synonyms/Alias
 Synapse-associated protein 97; SAP-97; SAP97 
Gene Name
 Dlg1 
Gene Synonyms/Alias
 Dlgh1 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
643EVGVIPSKRRVEKKEubiquitination[1]
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] 
Functional 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. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel (By similarity). May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. 
Sequence Annotation
 DOMAIN 4 64 L27.
 DOMAIN 224 310 PDZ 1.
 DOMAIN 318 404 PDZ 2.
 DOMAIN 465 545 PDZ 3.
 DOMAIN 580 650 SH3.
 DOMAIN 721 896 Guanylate kinase-like.
 REGION 162 212 Interaction with SH3 domains (By
 MOD_RES 39 39 Phosphoserine; by CaMK2.
 MOD_RES 122 122 Phosphoserine (By similarity).
 MOD_RES 158 158 Phosphoserine (By similarity).
 MOD_RES 232 232 Phosphoserine; by CaMK2.
 MOD_RES 301 301 Phosphoserine (By similarity).
 MOD_RES 398 398 Phosphotyrosine (By similarity).
 MOD_RES 567 567 Phosphoserine (By similarity).
 MOD_RES 574 574 Phosphoserine (By similarity).
 MOD_RES 618 618 Phosphoserine (By similarity).
 MOD_RES 683 683 Phosphothreonine (By similarity).
 MOD_RES 684 684 Phosphoserine (By similarity).
 MOD_RES 687 687 Phosphoserine (By similarity).  
Keyword
 3D-structure; Cell junction; Cell membrane; Complete proteome; Endoplasmic reticulum; Membrane; Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat; SH3 domain; Synapse. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 911 AA 
Protein Sequence
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVISI FQSNLFQALI DIQEFYEVTL 60
LDNPKCVDHS KQCEPVQPGN PWESGSLSSA AVTSESLPGG LSPPVEKYRY QDEEVLPSER 120
ISPQVPNEVL GPELVHVSEK SLSEIENVHG FVSHSHISPI KPTEAVPPSS PIVPVTPALP 180
VPAESPVVLP STPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG 240
GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EADVRDVTHS KAVEALKEAG 300
SIVRLYVKRR KAFRKNHEIK LIKGPKGLGF SIAGGVGNQH IPGDNSIYVT KIIEGGAAHK 360
DGKLQIGDKL LAVNSVCLEE VTHEEAVTAL KNTSDFVYLK AAKPTSMYIN DGYAPPDITN 420
SSSQSVDNHV SPSSYLGQTP ASPARYSPIS KAVLGDDEIT REPRKVVLHR GSTGLGFNIV 480
GGEDGEGIFI SFILAGGPAD LSGELRKGDR IISVNSVDLR AASHEQAAAA LKNAGQAVTI 540
VAQYRPEEYS RFEAKIHDLR ETMMNSSVSS GSGSLRTSQK RSLYVRALFD YDKTKDSGLP 600
SQGLNFKFGD ILHVINASDD EWWQARQVTP DGESDEVGVI PSKRRVEKKE RARLKTVKFN 660
SKTRGDKGEI PDDMGSKGLK HVTSNASDSE SSYHEYGCSK GGQEEYVLSY EPVNQQEVNY 720
TRPVIILGPM KDRVNDDLIS EFPDKFGSCV PHTTRPKRDY EVDGRDYHFV TSREQMEKDI 780
QEHKFIEAGQ YNNHLYGTSV QSVRAVAEKG KHCILDVSGN AIKRLQIAQL YPISIFIKPK 840
SMENIMEMNK RLTDEQARKT FERAVRLEQE FTEHFTAIVQ GDTLEDIYNQ VKQIIEEQSG 900
PYIWVPAKEK L 911 
Gene Ontology
 GO:0009925; C:basal plasma membrane; IDA:RGD.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0014069; C:postsynaptic density; TAS:UniProtKB.
 GO:0045211; C:postsynaptic membrane; TAS:RGD.
 GO:0042734; C:presynaptic membrane; IDA:RGD.
 GO:0030315; C:T-tubule; IDA:RGD.
 GO:0019902; F:phosphatase binding; ISS:UniProtKB.
 GO:0019901; F:protein kinase binding; ISS:UniProtKB.
 GO:0007015; P:actin filament organization; ISS:UniProtKB.
 GO:0016337; P:cell-cell adhesion; ISS:UniProtKB.
 GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
 GO:0001935; P:endothelial cell proliferation; ISS:UniProtKB.
 GO:0045930; P:negative regulation of mitotic cell cycle; ISS:UniProtKB.
 GO:0043268; P:positive regulation of potassium ion transport; IMP:RGD.
 GO:0032880; P:regulation of protein localization; IMP:RGD. 
Interpro
 IPR008144; Guanylate_kin.
 IPR008145; Guanylate_kin/L-typ_Ca_channel.
 IPR020590; Guanylate_kinase_CS.
 IPR004172; L27.
 IPR015143; L27_1.
 IPR016313; M-assoc_guanylate_kinase.
 IPR019590; MAGUK_PEST_N.
 IPR027417; P-loop_NTPase.
 IPR001478; PDZ.
 IPR019583; PDZ_assoc.
 IPR011511; SH3_2.
 IPR001452; SH3_domain. 
Pfam
 PF00625; Guanylate_kin
 PF09058; L27_1
 PF10608; MAGUK_N_PEST
 PF00595; PDZ
 PF10600; PDZ_assoc
 PF07653; SH3_2 
SMART
 SM00072; GuKc
 SM00569; L27
 SM00228; PDZ
 SM00326; SH3 
PROSITE
 PS00856; GUANYLATE_KINASE_1
 PS50052; GUANYLATE_KINASE_2
 PS51022; L27
 PS50106; PDZ
 PS50002; SH3 
PRINTS