CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018034
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Disks large homolog 5 
Protein Synonyms/Alias
 Discs large protein P-dlg; Placenta and prostate DLG 
Gene Name
 DLG5 
Gene Synonyms/Alias
 KIAA0583; PDLG 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
63LLKLLLAKERDHFQDubiquitination[1]
816ENIKDSDKMLSFRAHubiquitination[2, 3]
1587YRPEEFTKAKGLPGDubiquitination[4]
1589PEEFTKAKGLPGDSFubiquitination[4]
1784QAIERGVKDCLFVDYubiquitination[4]
Reference
 [1] 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]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [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] 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
Functional Description
 May play a role at the plasma membrane in the maintenance of the structure of epithelial cells and in the transmission of extracellular signals to the membrane and cytoskeleton. 
Sequence Annotation
 DOMAIN 620 710 PDZ 1.
 DOMAIN 705 796 PDZ 2.
 DOMAIN 1350 1429 PDZ 3.
 DOMAIN 1501 1582 PDZ 4.
 DOMAIN 1593 1661 SH3.
 DOMAIN 1722 1905 Guanylate kinase-like.
 MOD_RES 295 295 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell junction; Cell membrane; Coiled coil; Complete proteome; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1919 AA 
Protein Sequence
MEPQRRELLA QCQQSLAQAM TEVEAVLGLL EAAGALSPGE RRQLDEEAGG AKAELLLKLL 60
LAKERDHFQD LRAALEKTQP HLLPILYLNG VVGPPQPAEG AGSTYSVLST MPSDSESSSS 120
LSSVGTTGKA PSPPPLLTDQ QVNEKVENLS IQLRLMTRER NELRKRLAFA THGTAFDKRP 180
YHRLNPDYER LKIQCVRAMS DLQSLQNQHT NALKRCEEVA KETDFYHTLH SRLLSDQTRL 240
KDDVDMLRRE NGQLLRERNL LQQSWEDMKR LHEEDQKEIG DLRAQQQQVL KHNGSSEILN 300
KLYDTAMDKL EVVKKDYDAL RKRYSEKVAI HNADLSRLEQ LGEENQRLLK QTEMLTQQRD 360
TAIQLQHQCA LSLRRFEAIH HELNKATAQN KDLQWEMELL QSELTELRTT QVKTAKESEK 420
YREERDAVYS EYKLIMSERD QVISELDKLQ TEVELAESKL KSSTSEKKAA NEEMEALRQI 480
KDTVTMDAGR ANKEVEILRK QCKALCQELK EALQEADVAK CRRDWAFQER DKIVAERDSI 540
RTLCDNLRRE RDRAVSELAE ALRSLDDTRK QKNDVSRELK ELKEQMESQL EKEARFRQLM 600
AHSSHDSAID TDSMEWETEV VEFERETEDI DLKALGFDMA EGVNEPCFPG DCGIFVTKVD 660
KGSIADGRLR VNDWLLRIND VDLINKDKKQ AIKALLNGEG AINMVVRRRK SLGGKVVTPL 720
HINLSGQKDS GISLENGVYA AAVLPGSPAA KEGSLAVGDR IVAINGIALD NKSLNECESL 780
LRSCQDSLTL SLLKVFPQSS SWSGQNIFEN IKDSDKMLSF RAHGPEVQAH NKRNLIQHNN 840
STQTDIFYTD RLEDRKEPGP PGGSSSFLHK PFPGGPLQVC PQACPSASER SLSSFRSDAS 900
GDRGFGLVDV RGRRPLLPFE TEVGPCGVGE ASLDKADSEG SNSGGTWPKA MLSSTAVPEK 960
LSVYKKPKQR KSIFDPNTFK RPQTPPKIDY LLPGPGPAHS PQPSKRAGPL TPPKPPRRSD 1020
SIKFQHRLET SSESEATLVG SSPSTSPPSA LPPDVDPGEP MHASPPRKAR VRIASSYYPE 1080
GDGDSSHLPA KKSCDEDLTS QKVDELGQKR RRPKSAPSFR PKLAPVVIPA QFLEEQKCVP 1140
ASGELSPELQ EWAPYSPGHS SRHSNPPLYP SRPSVGTVPR SLTPSTTVSS ILRNPIYTVR 1200
SHRVGPCSSP PAARDAGPQG LHPSVQHQGR LSLDLSHRTC SDYSEMRATH GSNSLPSSAR 1260
LGSSSNLQFK AERIKIPSTP RYPRSVVGSE RGSVSHSECS TPPQSPLNID TLSSCSQSQT 1320
SASTLPRIAV NPASLGERRK DRPYVEEPRH VKVQKGSEPL GISIVSGEKG GIYVSKVTVG 1380
SIAHQAGLEY GDQLLEFNGI NLRSATEQQA RLIIGQQCDT ITILAQYNPH VHQLSSHSRS 1440
SSHLDPAGTH STLQGSGTTT PEHPSVIDPL MEQDEGPSTP PAKQSSSRIA GDANKKTLEP 1500
RVVFIKKSQL ELGVHLCGGN LHGVFVAEVE DDSPAKGPDG LVPGDLILEY GSLDVRNKTV 1560
EEVYVEMLKP RDGVRLKVQY RPEEFTKAKG LPGDSFYIRA LYDRLADVEQ ELSFKKDDIL 1620
YVDDTLPQGT FGSWMAWQLD ENAQKIQRGQ IPSKYVMDQE FSRRLSMSEV KDDNSATKTL 1680
SAAARRSFFR RKHKHKRSGS KDGKDLLALD AFSSDSIPLF EDSVSLAYQR VQKVDCTALR 1740
PVLILGPLLD VVKEMLVNEA PGKFCRCPLE VMKASQQAIE RGVKDCLFVD YKRRSGHFDV 1800
TTVASIKEIT EKNRHCLLDI APHAIERLHH MHIYPIVIFI HYKSAKHIKE QRDPIYLRDK 1860
VTQRHSKEQF EAAQKLEQEY SRYFTGVIQG GALSSICTQI LAMVNQEQNK VLWIPACPL 1919 
Gene Ontology
 GO:0005913; C:cell-cell adherens junction; IEA:Compara.
 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0005886; C:plasma membrane; NAS:UniProtKB.
 GO:0008013; F:beta-catenin binding; IDA:MGI.
 GO:0008092; F:cytoskeletal protein binding; IDA:MGI.
 GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
 GO:0016337; P:cell-cell adhesion; NAS:UniProtKB.
 GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
 GO:0042981; P:regulation of apoptotic process; IEA:InterPro. 
Interpro
 IPR001315; CARD.
 IPR011029; DEATH-like_dom.
 IPR006907; DUF622.
 IPR008144; Guanylate_kin.
 IPR008145; Guanylate_kin/L-typ_Ca_channel.
 IPR027417; P-loop_NTPase.
 IPR001478; PDZ.
 IPR001452; SH3_domain. 
Pfam
 PF00625; Guanylate_kin
 PF00595; PDZ
 PF04822; Takusan 
SMART
 SM00072; GuKc
 SM00228; PDZ
 SM00326; SH3 
PROSITE
 PS50209; CARD
 PS00856; GUANYLATE_KINASE_1
 PS50052; GUANYLATE_KINASE_2
 PS50106; PDZ
 PS50002; SH3 
PRINTS