CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005217
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Diacylglycerol kinase alpha 
Protein Synonyms/Alias
 DAG kinase alpha; 80 kDa diacylglycerol kinase; Diglyceride kinase alpha; DGK-alpha 
Gene Name
 DGKA 
Gene Synonyms/Alias
 DAGK; DAGK1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
18SDFAQLQKYMEYSTKubiquitination[1]
25KYMEYSTKKVSDVLKubiquitination[1]
26YMEYSTKKVSDVLKLubiquitination[1]
32KKVSDVLKLFEDGEMubiquitination[1]
41FEDGEMAKYVQGDAIubiquitination[2]
211GQHMWRPKRFPRPVYubiquitination[1]
239GLSCNLCKYTVHDQCubiquitination[1]
249VHDQCAMKALPCEVSubiquitination[1, 3]
260CEVSTYAKSRKDIGVubiquitination[1]
263STYAKSRKDIGVQSHubiquitination[1]
353KNSKTSQKTMDDLNLubiquitination[1, 2]
384LLVFVNPKSGGKQGQubiquitination[1]
388VNPKSGGKQGQRVLWubiquitination[1]
411RQVFNLLKDGPEIGLubiquitination[1, 2]
422EIGLRLFKDVPDSRIubiquitination[1, 3]
484YEGQNLAKILKDLEMacetylation[4]
484YEGQNLAKILKDLEMubiquitination[1]
487QNLAKILKDLEMSKVubiquitination[1, 2]
493LKDLEMSKVVHMDRWubiquitination[1, 2]
543RFHIMREKYPEKFNSubiquitination[1]
547MREKYPEKFNSRMKNubiquitination[1]
634QALGATAKVITDPDIubiquitination[1, 2]
643ITDPDILKTCVPDLSubiquitination[1, 5]
652CVPDLSDKRLEVVGLubiquitination[1, 5]
673GQIYTKLKNAGRRLAubiquitination[1]
681NAGRRLAKCSEITFHubiquitination[1]
691EITFHTTKTLPMQIDubiquitination[1]
714CTIKITHKNQMPMLMubiquitination[1]
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] 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]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. 
Sequence Annotation
 DOMAIN 110 145 EF-hand 1.
 DOMAIN 155 190 EF-hand 2.
 DOMAIN 372 506 DAGKc.
 ZN_FING 205 253 Phorbol-ester/DAG-type 1.
 ZN_FING 269 319 Phorbol-ester/DAG-type 2.
 MOD_RES 484 484 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Calcium; Complete proteome; Kinase; Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome; Repeat; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 735 AA 
Protein Sequence
MAKERGLISP SDFAQLQKYM EYSTKKVSDV LKLFEDGEMA KYVQGDAIGY EGFQQFLKIY 60
LEVDNVPRHL SLALFQSFET GHCLNETNVT KDVVCLNDVS CYFSLLEGGR PEDKLEFTFK 120
LYDTDRNGIL DSSEVDKIIL QMMRVAEYLD WDVSELRPIL QEMMKEIDYD GSGSVSQAEW 180
VRAGATTVPL LVLLGLEMTL KDDGQHMWRP KRFPRPVYCN LCESSIGLGK QGLSCNLCKY 240
TVHDQCAMKA LPCEVSTYAK SRKDIGVQSH VWVRGGCESG RCDRCQKKIR IYHSLTGLHC 300
VWCHLEIHDD CLQAVGHECD CGLLRDHILP PSSIYPSVLA SGPDRKNSKT SQKTMDDLNL 360
STSEALRIDP VPNTHPLLVF VNPKSGGKQG QRVLWKFQYI LNPRQVFNLL KDGPEIGLRL 420
FKDVPDSRIL VCGGDGTVGW ILETIDKANL PVLPPVAVLP LGTGNDLARC LRWGGGYEGQ 480
NLAKILKDLE MSKVVHMDRW SVEVIPQQTE EKSDPVPFQI INNYFSIGVD ASIAHRFHIM 540
REKYPEKFNS RMKNKLWYFE FATSESIFST CKKLEESLTV EICGKPLDLS NLSLEGIAVL 600
NIPSMHGGSN LWGDTRRPHG DIYGINQALG ATAKVITDPD ILKTCVPDLS DKRLEVVGLE 660
GAIEMGQIYT KLKNAGRRLA KCSEITFHTT KTLPMQIDGE PWMQTPCTIK ITHKNQMPML 720
MGPPPRSTNF FGFLS 735 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0004143; F:diacylglycerol kinase activity; TAS:ProtInc.
 GO:0005543; F:phospholipid binding; IEA:Compara.
 GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; IEA:InterPro. 
Interpro
 IPR000756; Diacylglycerol_kin_accessory.
 IPR001206; Diacylglycerol_kinase_cat_dom.
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR002219; Prot_Kinase_C-like_PE/DAG-bd. 
Pfam
 PF00130; C1_1
 PF00609; DAGK_acc
 PF00781; DAGK_cat
 PF13405; EF_hand_4 
SMART
 SM00109; C1
 SM00045; DAGKa
 SM00046; DAGKc
 SM00054; EFh 
PROSITE
 PS50146; DAGK
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS00479; ZF_DAG_PE_1
 PS50081; ZF_DAG_PE_2 
PRINTS