DGKZ
entrez
8525
canonical
uniprot
Q13574
canonical
ensembl
ENSG00000149091
resolver
ensp
ENSP00000320340
resolver
ensp
ENSP00000343065
resolver
ensp
ENSP00000391021
resolver
ensp
ENSP00000395684
resolver
ensp
ENSP00000412178
resolver
ensp
ENSP00000436273
resolver
ensp
ENSP00000436291
resolver
genesymbol
DGKZ
resolver
genesymbol_syn
DAGK6
resolver
hgnc
HGNC:2857
resolver
uniprot
B7Z2M9
resolver
uniprot
B7Z6M3
resolver
uniprot
E9PPW4
resolver
uniprot
F6UCU9
resolver
uniprot
G3V0F6
resolver
uniprot
J3KNJ6
resolver
uniprot
O00542
resolver
uniprot
Q6ZVG7
resolver
uniprot
Q8IVW9
resolver
uniprot_entry
DGKZ_HUMAN
resolver
uniprot_sec
B7Z2M9
resolver
uniprot_sec
B7Z6M3
resolver
uniprot_sec
E9PPW4
resolver
uniprot_sec
F6UCU9
resolver
uniprot_sec
G3V0F6
resolver
uniprot_sec
J3KNJ6
resolver
uniprot_sec
O00542
resolver
uniprot_sec
Q6ZVG7
resolver
uniprot_sec
Q8IVW9
resolver
activity_regulation
ACTIVITY REGULATION: Activated by 1,2-diacyl-sn-glycero-3-phosphate/phosphatidic acid irrespective of its acyl chain composition. {ECO:0000269|PubMed:19744926}.
uniprot
proteins
amino_acid_sequence
MEPRDGSPEARSSDSESASASSSGSERDAGPEPDKAPRRLNKRRFPGLRLFGHRKAITKSGLQHLAPPPPTPGAPCSESERQIRSTVDWSESATYGEHIWFETNVSGDFCYVGEQYCVARMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSPLMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILACGGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIPRYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTTSKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRVSMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKLSPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLPTSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
uniprot
proteins
ec_number
2.7.1.107
uniprot
proteins
ec_number
2.7.1.93
uniprot
proteins
function
FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:15544348, PubMed:18004883, PubMed:19744926, PubMed:22108654, PubMed:22627129, PubMed:23949095, PubMed:9159104). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (PubMed:15544348, PubMed:18004883, PubMed:19744926, PubMed:22108654, PubMed:22627129, PubMed:23949095, PubMed:9159104). Also plays an important role in the biosynthesis of complex lipids (Probable). Does not exhibit an acyl chain-dependent substrate specificity among diacylglycerol species (PubMed:19744926, PubMed:22108654, PubMed:9159104). Can also phosphorylate 1-alkyl-2-acylglycerol in vitro but less efficiently and with a preference for alkylacylglycerols containing an arachidonoyl group (PubMed:15544348, PubMed:19744926, PubMed:22627129). The biological processes it is involved in include T cell activation since it negatively regulates T-cell receptor signaling which is in part mediated by diacylglycerol (By similarity). By generating phosphatidic acid, stimulates PIP5KIA activity which regulates actin polymerization (PubMed:15157668). Through the same mechanism could also positively regulate insulin-induced translocation of SLC2A4 to the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q80UP3, ECO:0000269|PubMed:15157668, ECO:0000269|PubMed:15544348, ECO:0000269|PubMed:18004883, ECO:0000269|PubMed:19744926, ECO:0000269|PubMed:22108654, ECO:0000269|PubMed:22627129, ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:9159104, ECO:0000305|PubMed:8626588}.; FUNCTION: [Isoform 1]: Regulates RASGRP1 activity. {ECO:0000269|PubMed:11257115}.; FUNCTION: [Isoform 2]: Does not regulate RASGRP1 activity. {ECO:0000269|PubMed:11257115}.
uniprot
proteins
mass_dalton
103981
uniprot
proteins
mutagenesis
MUTAGEN 926..927; /note="TA->NS: Loss of interaction with SNTG1."; /evidence="ECO:0000269|PubMed:11352924
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000305|PubMed:8626588}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of the MARCKS homology domain by PKC reduces nuclear accumulation of DGK-zeta. {ECO:0000269|PubMed:9716136}.
uniprot
proteins
protein_family
Eukaryotic diacylglycerol kinase family
uniprot
proteins
pubmed
11257115
uniprot
proteins
pubmed
11352924
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15157668
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15544348
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17351151
uniprot
proteins
pubmed
18004883
uniprot
proteins
pubmed
19744926
uniprot
proteins
pubmed
22108654
uniprot
proteins
pubmed
22627129
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23949095
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
8626588
uniprot
proteins
pubmed
9159104
uniprot
proteins
pubmed
9716136
uniprot
proteins
sequence_length
928
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11257115, ECO:0000269|PubMed:15157668, ECO:0000269|PubMed:9159104, ECO:0000269|PubMed:9716136}. Cytoplasm, cytosol {ECO:0000269|PubMed:11257115, ECO:0000269|PubMed:22627129}. Cell membrane {ECO:0000269|PubMed:11257115}. Cell projection, lamellipodium {ECO:0000269|PubMed:15157668}.
uniprot
proteins