DGKB_HUMAN
ID DGKB_HUMAN Reviewed; 804 AA.
AC Q9Y6T7; A4D116; A4D117; A8MXU2; O75241; Q2M377; Q75MF9; Q75MU7; Q86UI5;
AC Q86UM9; Q9UQ29;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Diacylglycerol kinase beta;
DE Short=DAG kinase beta;
DE EC=2.7.1.107 {ECO:0000269|PubMed:11719522};
DE AltName: Full=90 kDa diacylglycerol kinase;
DE AltName: Full=Diglyceride kinase beta;
DE Short=DGK-beta;
GN Name=DGKB; Synonyms=DAGK2, KIAA0718;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Caricasole A., Caldara F., Sala C.F.;
RT "Novel proteins.";
RL Patent number WO0047723, 17-AUG-2000.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, FUNCTION
RP (ISOFORM 2), CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY,
RP TISSUE SPECIFICITY (ISOFORMS 1 AND 2), AND REGION.
RX PubMed=11719522; DOI=10.1074/jbc.m110249200;
RA Caricasole A., Bettini E., Sala C., Roncarati R., Kobayashi N., Caldara F.,
RA Goto K., Terstappen G.C.;
RT "Molecular cloning and characterization of the human diacylglycerol kinase
RT beta (DGKbeta) gene: alternative splicing generates DGKbeta isotypes with
RT different properties.";
RL J. Biol. Chem. 277:4790-4796(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-804 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
CC -!- FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into
CC phosphatidic acid/phosphatidate/PA and regulates the respective levels
CC of these two bioactive lipids (PubMed:11719522). Thereby, acts as a
CC central switch between the signaling pathways activated by these second
CC messengers with different cellular targets and opposite effects in
CC numerous biological processes (Probable). Has a higher activity with
CC long-chain diacylglycerols like 1,2-di-(9Z-octadecenoyl)-sn-glycerol
CC compared to 1,2-didecanoyl-sn-glycerol (By similarity). Specifically
CC expressed in brain, it regulates neuron-specific morphological changes
CC including neurite branching and neurite spine formation (By
CC similarity). {ECO:0000250|UniProtKB:P49621,
CC ECO:0000250|UniProtKB:Q6NS52, ECO:0000269|PubMed:11719522,
CC ECO:0000305}.
CC -!- FUNCTION: [Isoform 2]: Does not associate with membranes but has a
CC diacylglycerol kinase activity. {ECO:0000269|PubMed:11719522}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:456216; EC=2.7.1.107;
CC Evidence={ECO:0000269|PubMed:11719522};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:11719522};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + ATP =
CC 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:40339, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:11719522};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340;
CC Evidence={ECO:0000305|PubMed:11719522};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + ATP =
CC 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:40339, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:11719522};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340;
CC Evidence={ECO:0000305|PubMed:11719522};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P49621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000250|UniProtKB:P49621};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P49621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000250|UniProtKB:P49621};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43428, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18155, ChEBI:CHEBI:30616, ChEBI:CHEBI:78227,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P49621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000250|UniProtKB:P49621};
CC -!- ACTIVITY REGULATION: Activated by calcium.
CC {ECO:0000250|UniProtKB:P49621}.
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:11719522}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q6NS52}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q6NS52}. Cell membrane
CC {ECO:0000269|PubMed:11719522}; Peripheral membrane protein
CC {ECO:0000305|PubMed:11719522}. Cytoplasm {ECO:0000269|PubMed:11719522}.
CC Note=Translocation to the plasma membrane is induced by phorbol esters.
CC {ECO:0000269|PubMed:11719522}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:11719522}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=STD {ECO:0000303|PubMed:11719522};
CC IsoId=Q9Y6T7-1; Sequence=Displayed;
CC Name=2; Synonyms=SV3' {ECO:0000303|PubMed:11719522};
CC IsoId=Q9Y6T7-2; Sequence=VSP_021898, VSP_021899;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Specifically expressed in brain but
CC also detected in uterus (PubMed:11719522). In adult brain, expressed in
CC the amygdala, caudate nucleus, and hippocampus (PubMed:11719522).
CC {ECO:0000269|PubMed:11719522}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: More ubiquitously expressed but at
CC lower level compared to isoform 1. {ECO:0000269|PubMed:11719522}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS07533.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AX032742; CAC09945.1; -; mRNA.
DR EMBL; AC005039; AAS07495.1; -; Genomic_DNA.
DR EMBL; AC005248; AAC25525.1; -; Genomic_DNA.
DR EMBL; AC006150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011229; AAP21868.1; -; Genomic_DNA.
DR EMBL; AC073258; AAS07533.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC105459; AAP22362.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24292.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24293.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93663.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93664.1; -; Genomic_DNA.
DR EMBL; BC105005; AAI05006.1; -; mRNA.
DR EMBL; AB018261; BAA34438.1; -; mRNA.
DR CCDS; CCDS47547.1; -. [Q9Y6T7-1]
DR CCDS; CCDS47548.1; -. [Q9Y6T7-2]
DR RefSeq; NP_004071.1; NM_004080.2.
DR RefSeq; NP_663733.1; NM_145695.2. [Q9Y6T7-2]
DR RefSeq; XP_005249685.1; XM_005249628.2.
DR RefSeq; XP_011513455.1; XM_011515153.2.
DR RefSeq; XP_011513456.1; XM_011515154.2. [Q9Y6T7-1]
DR AlphaFoldDB; Q9Y6T7; -.
DR BioGRID; 107977; 3.
DR STRING; 9606.ENSP00000385780; -.
DR BindingDB; Q9Y6T7; -.
DR ChEMBL; CHEMBL4105755; -.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR SwissLipids; SLP:000000915; -. [Q9Y6T7-1]
DR SwissLipids; SLP:000000916; -. [Q9Y6T7-2]
DR iPTMnet; Q9Y6T7; -.
DR PhosphoSitePlus; Q9Y6T7; -.
DR BioMuta; DGKB; -.
DR DMDM; 12643960; -.
DR jPOST; Q9Y6T7; -.
DR MassIVE; Q9Y6T7; -.
DR MaxQB; Q9Y6T7; -.
DR PaxDb; Q9Y6T7; -.
DR PeptideAtlas; Q9Y6T7; -.
DR PRIDE; Q9Y6T7; -.
DR ProteomicsDB; 86787; -. [Q9Y6T7-1]
DR ProteomicsDB; 86788; -. [Q9Y6T7-2]
DR Antibodypedia; 25192; 224 antibodies from 31 providers.
DR DNASU; 1607; -.
DR Ensembl; ENST00000399322.7; ENSP00000382260.3; ENSG00000136267.14. [Q9Y6T7-1]
DR Ensembl; ENST00000403951.6; ENSP00000385780.2; ENSG00000136267.14. [Q9Y6T7-1]
DR Ensembl; ENST00000406247.7; ENSP00000386066.3; ENSG00000136267.14. [Q9Y6T7-2]
DR GeneID; 1607; -.
DR KEGG; hsa:1607; -.
DR UCSC; uc003ssz.3; human. [Q9Y6T7-1]
DR CTD; 1607; -.
DR DisGeNET; 1607; -.
DR GeneCards; DGKB; -.
DR HGNC; HGNC:2850; DGKB.
DR HPA; ENSG00000136267; Tissue enriched (brain).
DR MIM; 604070; gene.
DR neXtProt; NX_Q9Y6T7; -.
DR OpenTargets; ENSG00000136267; -.
DR PharmGKB; PA27311; -.
DR VEuPathDB; HostDB:ENSG00000136267; -.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000159770; -.
DR InParanoid; Q9Y6T7; -.
DR OrthoDB; 633642at2759; -.
DR PhylomeDB; Q9Y6T7; -.
DR TreeFam; TF313104; -.
DR BRENDA; 2.7.1.107; 2681.
DR PathwayCommons; Q9Y6T7; -.
DR Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR SABIO-RK; Q9Y6T7; -.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 1607; 5 hits in 1070 CRISPR screens.
DR ChiTaRS; DGKB; human.
DR GeneWiki; DGKB; -.
DR GenomeRNAi; 1607; -.
DR Pharos; Q9Y6T7; Tbio.
DR PRO; PR:Q9Y6T7; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y6T7; protein.
DR Bgee; ENSG00000136267; Expressed in buccal mucosa cell and 126 other tissues.
DR ExpressionAtlas; Q9Y6T7; baseline and differential.
DR Genevisible; Q9Y6T7; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:BHF-UCL.
DR GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0046486; P:glycerolipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IDA:BHF-UCL.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00029; C1; 2.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.110; -; 2.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR029477; DAG_kinase_typeI_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR038199; DGK_typeI_N_sf.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; PTHR11255; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF14513; DAG_kinase_N; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calcium; Cell membrane; Cytoplasm;
KW Kinase; Lipid metabolism; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Synapse; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..804
FT /note="Diacylglycerol kinase beta"
FT /id="PRO_0000218457"
FT DOMAIN 149..184
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 194..229
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 434..568
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 244..294
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 309..358
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 385..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..804
FT /note="Required for association with membranes and function
FT in neurite spine formation"
FT /evidence="ECO:0000305|PubMed:11719522"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NS52"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NS52"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NS52"
FT VAR_SEQ 770..773
FT /note="IKIT -> VSTE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021898"
FT VAR_SEQ 774..804
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021899"
FT VARIANT 789
FT /note="G -> S (in dbSNP:rs34616903)"
FT /id="VAR_048858"
SQ SEQUENCE 804 AA; 90595 MW; CBCABD2339BFE176 CRC64;
MTNQEKWAHL SPSEFSQLQK YAEYSTKKLK DVLEEFHGNG VLAKYNPEGK QDILNQTIDF
EGFKLFMKTF LEAELPDDFT AHLFMSFSNK FPHSSPMVKS KPALLSGGLR MNKGAITPPR
TTSPANTCSP EVIHLKDIVC YLSLLERGRP EDKLEFMFRL YDTDGNGFLD SSELENIISQ
MMHVAEYLEW DVTELNPILH EMMEEIDYDH DGTVSLEEWI QGGMTTIPLL VLLGLENNVK
DDGQHVWRLK HFNKPAYCNL CLNMLIGVGK QGLCCSFCKY TVHERCVARA PPSCIKTYVK
SKRNTDVMHH YWVEGNCPTK CDKCHKTVKC YQGLTGLHCV WCQITLHNKC ASHLKPECDC
GPLKDHILPP TTICPVVLQT LPTSGVSVPE ERQSTVKKEK SGSQQPNKVI DKNKMQRANS
VTVDGQGLQV TPVPGTHPLL VFVNPKSGGK QGERIYRKFQ YLLNPRQVYS LSGNGPMPGL
NFFRDVPDFR VLACGGDGTV GWVLDCIEKA NVGKHPPVAI LPLGTGNDLA RCLRWGGGYE
GENLMKILKD IENSTEIMLD RWKFEVIPND KDEKGDPVPY SIINNYFSIG VDASIAHRFH
IMREKHPEKF NSRMKNKFWY FEFGTSETFS ATCKKLHESV EIECDGVQID LINISLEGIA
ILNIPSMHGG SNLWGESKKR RSHRRIEKKG SDKRTTVTDA KELKFASQDL SDQLLEVVGL
EGAMEMGQIY TGLKSAGRRL AQCSCVVIRT SKSLPMQIDG EPWMQTPCTI KITHKNQAPM
LMGPPPKTGL FCSLVKRTRN RSKE
