CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011957
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Disks large homolog 1 
Protein Synonyms/Alias
 Synapse-associated protein 97; SAP-97; SAP97; hDlg 
Gene Name
 DLG1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
107SLSPSVEKYRYQDEDubiquitination[1]
321SEKIMEIKLIKGPKGubiquitination[2]
401TSDFVYLKVAKPTSMubiquitination[3]
690KFPFYKNKDQSEQETubiquitination[1, 4]
865ENIMEMNKRLTEEQAubiquitination[5]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
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. 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. 
Sequence Annotation
 DOMAIN 4 64 L27.
 DOMAIN 224 310 PDZ 1.
 DOMAIN 319 405 PDZ 2.
 DOMAIN 466 546 PDZ 3.
 DOMAIN 581 651 SH3.
 DOMAIN 714 889 Guanylate kinase-like.
 REGION 162 212 Interaction with SH3 domains.
 MOD_RES 115 115 Phosphothreonine.
 MOD_RES 122 122 Phosphoserine.
 MOD_RES 158 158 Phosphoserine.
 MOD_RES 232 232 Phosphoserine (By similarity).
 MOD_RES 301 301 Phosphoserine (By similarity).
 MOD_RES 399 399 Phosphotyrosine (By similarity).
 MOD_RES 568 568 Phosphoserine.
 MOD_RES 575 575 Phosphoserine.
 MOD_RES 619 619 Phosphoserine.
 MOD_RES 683 683 Phosphothreonine (By similarity).
 MOD_RES 684 684 Phosphoserine.
 MOD_RES 687 687 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell junction; Cell membrane; Complete proteome; Endoplasmic reticulum; Host-virus interaction; Membrane; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Reference proteome; Repeat; SH3 domain; Synapse. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 904 AA 
Protein Sequence
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 60
LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS LSPSVEKYRY QDEDTPPQEH 120
ISPQITNEVI GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVLPSP PTVPVIPVLP 180
VPAENTVILP TIPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG 240
GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EVDVRDVTHS KAVEALKEAG 300
SIVRLYVKRR KPVSEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV TKIIEGGAAH 360
KDGKLQIGDK LLAVNNVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYM NDGYAPPDIT 420
NSSSQPVDNH VSPSSFLGQT PASPARYSPV SKAVLGDDEI TREPRKVVLH RGSTGLGFNI 480
VGGEDGEGIF ISFILAGGPA DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT 540
IVAQYRPEEY SRFEAKIHDL REQMMNSSIS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL 600
PSQGLNFKFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK ERARLKTVKF 660
NSKTRDKGQS FNDKRKKNLF SRKFPFYKNK DQSEQETSDA DQHVTSNASD SESSYRGQEE 720
YVLSYEPVNQ QEVNYTRPVI ILGPMKDRIN DDLISEFPDK FGSCVPHTTR PKRDYEVDGR 780
DYHFVTSREQ MEKDIQEHKF IEAGQYNNHL YGTSVQSVRE VAEKGKHCIL DVSGNAIKRL 840
QIAQLYPISI FIKPKSMENI MEMNKRLTEE QARKTFERAM KLEQEFTEHF TAIVQGDTLE 900
DIYNQVKQII EEQSGSYIWV PAKEKL 926 
Gene Ontology
 GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
 GO:0031253; C:cell projection membrane; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0001772; C:immunological synapse; TAS:BHF-UCL.
 GO:0009898; C:internal side of plasma membrane; IDA:UniProtKB.
 GO:0043219; C:lateral loop; IEA:Compara.
 GO:0016328; C:lateral plasma membrane; IEA:Compara.
 GO:0045121; C:membrane raft; IEA:Compara.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0097025; C:MPP7-DLG1-LIN7 complex; IDA:BHF-UCL.
 GO:0035748; C:myelin sheath abaxonal region; IEA:Compara.
 GO:0031594; C:neuromuscular junction; IEA:Compara.
 GO:0033268; C:node of Ranvier; IEA:Compara.
 GO:0005634; C:nucleus; IDA:BHF-UCL.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
 GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
 GO:0005923; C:tight junction; IDA:BHF-UCL.
 GO:0008092; F:cytoskeletal protein binding; TAS:ProtInc.
 GO:0004385; F:guanylate kinase activity; TAS:ProtInc.
 GO:0004721; F:phosphoprotein phosphatase activity; TAS:UniProtKB.
 GO:0015459; F:potassium channel regulator activity; NAS:UniProtKB.
 GO:0007015; P:actin filament organization; IDA:UniProtKB.
 GO:0032147; P:activation of protein kinase activity; IEA:Compara.
 GO:0042982; P:amyloid precursor protein metabolic process; IEA:Compara.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Compara.
 GO:0016337; P:cell-cell adhesion; IDA:UniProtKB.
 GO:0030866; P:cortical actin cytoskeleton organization; IDA:UniProtKB.
 GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Compara.
 GO:0001935; P:endothelial cell proliferation; IDA:UniProtKB.
 GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB.
 GO:0060022; P:hard palate development; IEA:Compara.
 GO:0001771; P:immunological synapse formation; IEA:Compara.
 GO:0002088; P:lens development in camera-type eye; IEA:Compara.
 GO:0031579; P:membrane raft organization; IEA:Compara.
 GO:0007093; P:mitotic cell cycle checkpoint; NAS:UniProtKB.
 GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Compara.
 GO:0045930; P:negative regulation of mitotic cell cycle; IMP:UniProtKB.
 GO:0042130; P:negative regulation of T cell proliferation; IEA:Compara.
 GO:0030432; P:peristalsis; IEA:Compara.
 GO:0030838; P:positive regulation of actin filament polymerization; IEA:Compara.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IDA:BHF-UCL.
 GO:0043268; P:positive regulation of potassium ion transport; IDA:BHF-UCL.
 GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
 GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
 GO:0048608; P:reproductive structure development; IEA:Compara.
 GO:0048745; P:smooth muscle tissue development; IEA:Compara.
 GO:0007268; P:synaptic transmission; TAS:Reactome.
 GO:0042110; P:T cell activation; IEA:Compara.
 GO:0002369; P:T cell cytokine production; IEA:Compara.
 GO:0070830; P:tight junction assembly; IDA:BHF-UCL.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
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