Full text data of DGKG
DGKG
(DAGK3)
[Confidence: low (only semi-automatic identification from reviews)]
Diacylglycerol kinase gamma; DAG kinase gamma; 2.7.1.107 (Diglyceride kinase gamma; DGK-gamma)
Diacylglycerol kinase gamma; DAG kinase gamma; 2.7.1.107 (Diglyceride kinase gamma; DGK-gamma)
UniProt
P49619
ID DGKG_HUMAN Reviewed; 791 AA.
AC P49619; B2RAH4; Q2M1H4; Q5FWG1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-NOV-2010, sequence version 3.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Diacylglycerol kinase gamma;
DE Short=DAG kinase gamma;
DE EC=2.7.1.107;
DE AltName: Full=Diglyceride kinase gamma;
DE Short=DGK-gamma;
GN Name=DGKG; Synonyms=DAGK3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-316.
RC TISSUE=Liver;
RX PubMed=8034597;
RA Kai M., Sakane F., Imai S., Wada I., Kanoh H.;
RT "Molecular cloning of a diacylglycerol kinase isozyme predominantly
RT expressed in human retina with a truncated and inactive enzyme
RT expression in most other human cells.";
RL J. Biol. Chem. 269:18492-18498(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-316.
RX PubMed=10071200; DOI=10.1007/s004390050917;
RA Stoehr H., Klein J., Gehrig A., Koehler M.R., Jurklies B., Kellner U.,
RA Leo-Kottler B., Schmid M., Weber B.H.F.;
RT "Mapping and genomic characterization of the gene encoding
RT diacylglycerol kinase gamma (DAGK3): assessment of its role in
RT dominant optic atrophy (OPA1).";
RL Hum. Genet. 104:99-105(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP SER-142 AND LYS-316.
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP VARIANTS SER-142 AND LYS-316.
RC TISSUE=Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-706.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Reverses the normal flow of glycerolipid biosynthesis by
CC phosphorylating diacylglycerol back to phosphatidic acid.
CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-
CC sn-glycerol 3-phosphate.
CC -!- ENZYME REGULATION: Requires phosphatidylserine for maximal
CC activity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Can be loosely
CC bound to the membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=P49619-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P49619-2; Sequence=VSP_001267;
CC Note=May be inactive;
CC Name=3;
CC IsoId=P49619-3; Sequence=VSP_039922;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in retina and in a
CC much lesser extent in the brain. Other tissues contain extremely
CC low levels of DGK-gamma.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC family.
CC -!- SIMILARITY: Contains 1 DAGKc domain.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
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DR EMBL; D26135; BAA05132.1; -; mRNA.
DR EMBL; AF020945; AAC04686.1; -; Genomic_DNA.
DR EMBL; AF020922; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020923; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020924; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020925; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020926; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020927; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020928; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020929; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020930; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020931; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020932; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020933; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020934; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020935; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020936; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020937; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020938; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020939; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020940; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020941; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020942; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020943; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020944; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AK314192; BAG36871.1; -; mRNA.
DR EMBL; AC007917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089411; AAH89411.1; -; mRNA.
DR EMBL; BC112363; AAI12364.1; -; mRNA.
DR PIR; A53691; A53691.
DR RefSeq; NP_001074213.1; NM_001080744.1.
DR RefSeq; NP_001074214.1; NM_001080745.1.
DR RefSeq; NP_001337.2; NM_001346.2.
DR UniGene; Hs.683449; -.
DR ProteinModelPortal; P49619; -.
DR SMR; P49619; 1-79, 138-248, 265-323.
DR IntAct; P49619; 2.
DR STRING; 9606.ENSP00000265022; -.
DR ChEMBL; CHEMBL1075157; -.
DR DrugBank; DB00144; Phosphatidylserine.
DR PhosphoSite; P49619; -.
DR DMDM; 311033457; -.
DR PaxDb; P49619; -.
DR PRIDE; P49619; -.
DR DNASU; 1608; -.
DR Ensembl; ENST00000265022; ENSP00000265022; ENSG00000058866.
DR Ensembl; ENST00000344484; ENSP00000339777; ENSG00000058866.
DR Ensembl; ENST00000382164; ENSP00000371599; ENSG00000058866.
DR GeneID; 1608; -.
DR KEGG; hsa:1608; -.
DR UCSC; uc003fqa.3; human.
DR CTD; 1608; -.
DR GeneCards; GC03M185823; -.
DR HGNC; HGNC:2853; DGKG.
DR HPA; HPA036577; -.
DR MIM; 601854; gene.
DR neXtProt; NX_P49619; -.
DR PharmGKB; PA27314; -.
DR eggNOG; NOG47311; -.
DR HOGENOM; HOG000252931; -.
DR HOVERGEN; HBG051345; -.
DR InParanoid; P49619; -.
DR KO; K00901; -.
DR OMA; CYQSVTA; -.
DR OrthoDB; EOG75XGK8; -.
DR PhylomeDB; P49619; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_604; Hemostasis.
DR SABIO-RK; P49619; -.
DR GeneWiki; DGKG; -.
DR GenomeRNAi; 1608; -.
DR NextBio; 6606; -.
DR PRO; PR:P49619; -.
DR ArrayExpress; P49619; -.
DR Bgee; P49619; -.
DR CleanEx; HS_DGKG; -.
DR Genevestigator; P49619; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; TAS:ProtInc.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
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 GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR016064; ATP-NAD_kinase_PpnK-typ.
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; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR Pfam; PF00130; C1_1; 1.
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 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Calcium; Complete proteome;
KW Cytoplasm; Kinase; Membrane; Metal-binding; Nucleotide-binding;
KW Polymorphism; Reference proteome; Repeat; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1 791 Diacylglycerol kinase gamma.
FT /FTId=PRO_0000218459.
FT DOMAIN 175 210 EF-hand 1.
FT DOMAIN 220 255 EF-hand 2.
FT DOMAIN 430 564 DAGKc.
FT CA_BIND 188 199 1 (Potential).
FT CA_BIND 233 244 2 (Potential).
FT ZN_FING 271 321 Phorbol-ester/DAG-type 1.
FT ZN_FING 336 385 Phorbol-ester/DAG-type 2.
FT COMPBIAS 151 156 Poly-Ser.
FT VAR_SEQ 334 372 Missing (in isoform 3).
FT /FTId=VSP_039922.
FT VAR_SEQ 451 475 Missing (in isoform 2).
FT /FTId=VSP_001267.
FT VARIANT 142 142 T -> S (in dbSNP:rs1004588).
FT /FTId=VAR_020259.
FT VARIANT 316 316 R -> K (in dbSNP:rs2193587).
FT /FTId=VAR_024430.
FT VARIANT 370 370 R -> W (in dbSNP:rs3213770).
FT /FTId=VAR_020260.
FT VARIANT 706 706 E -> K (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036119.
FT CONFLICT 271 271 R -> G (in Ref. 1; BAA05132 and 2;
FT AAC04686).
SQ SEQUENCE 791 AA; 89124 MW; A1382CF1B2CD7362 CRC64;
MGEERWVSLT PEEFDQLQKY SEYSSKKIKD ALTEFNEGGS LKQYDPHEPI SYDVFKLFMR
AYLEVDLPQP LSTHLFLAFS QKPRHETSDH PTEGASNSEA NSADTNIQNA DNATKADEAC
APDTESNMAE KQAPAEDQVA ATPLEPPVPR SSSSESPVVY LKDVVCYLSL LETGRPQDKL
EFMFRLYDSD ENGLLDQAEM DCIVNQMLHI AQYLEWDPTE LRPILKEMLQ GMDYDRDGFV
SLQEWVHGGM TTIPLLVLLG MDDSGSKGDG RHAWTMKHFK KPTYCNFCHI MLMGVRKQGL
CCTYCKYTVH ERCVSRNIPG CVKTYSKAKR SGEVMQHAWV EGNSSVKCDR CHKSIKCYQS
VTARHCVWCR MTFHRKCELS TLCDGGELRD HILLPTSICP ITRDRPGEKS DGCVSAKGEL
VMQYKIIPTP GTHPLLVLVN PKSGGRQGER ILRKFHYLLN PKQVFNLDNG GPTPGLNFFR
DTPDFRVLAC GGDGTVGWIL DCIDKANFAK HPPVAVLPLG TGNDLARCLR WGGGYEGGSL
TKILKDIEQS PLVMLDRWHL EVIPREEVEN GDQVPYSIMN NYFSIGVDAS IAHRFHVMRE
KHPEKFNSRM KNKLWYFEFG TSETFAATCK KLHDHIELEC DGVGVDLSNI FLEGIAILNI
PSMYGGTNLW GENKKNRAVI RESRKGVTDP KELKFCVQDL SDQLLEVVGL EGAMEMGQIY
TGLKSAGRRL AQCASVTIRT NKLLPMQVDG EPWMQPCCTI KITHKNQAPM MMGPPQKSSF
FSLRRKSRSK D
//
ID DGKG_HUMAN Reviewed; 791 AA.
AC P49619; B2RAH4; Q2M1H4; Q5FWG1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-NOV-2010, sequence version 3.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Diacylglycerol kinase gamma;
DE Short=DAG kinase gamma;
DE EC=2.7.1.107;
DE AltName: Full=Diglyceride kinase gamma;
DE Short=DGK-gamma;
GN Name=DGKG; Synonyms=DAGK3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-316.
RC TISSUE=Liver;
RX PubMed=8034597;
RA Kai M., Sakane F., Imai S., Wada I., Kanoh H.;
RT "Molecular cloning of a diacylglycerol kinase isozyme predominantly
RT expressed in human retina with a truncated and inactive enzyme
RT expression in most other human cells.";
RL J. Biol. Chem. 269:18492-18498(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-316.
RX PubMed=10071200; DOI=10.1007/s004390050917;
RA Stoehr H., Klein J., Gehrig A., Koehler M.R., Jurklies B., Kellner U.,
RA Leo-Kottler B., Schmid M., Weber B.H.F.;
RT "Mapping and genomic characterization of the gene encoding
RT diacylglycerol kinase gamma (DAGK3): assessment of its role in
RT dominant optic atrophy (OPA1).";
RL Hum. Genet. 104:99-105(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP SER-142 AND LYS-316.
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP VARIANTS SER-142 AND LYS-316.
RC TISSUE=Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-706.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Reverses the normal flow of glycerolipid biosynthesis by
CC phosphorylating diacylglycerol back to phosphatidic acid.
CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-
CC sn-glycerol 3-phosphate.
CC -!- ENZYME REGULATION: Requires phosphatidylserine for maximal
CC activity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Can be loosely
CC bound to the membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=P49619-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P49619-2; Sequence=VSP_001267;
CC Note=May be inactive;
CC Name=3;
CC IsoId=P49619-3; Sequence=VSP_039922;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in retina and in a
CC much lesser extent in the brain. Other tissues contain extremely
CC low levels of DGK-gamma.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC family.
CC -!- SIMILARITY: Contains 1 DAGKc domain.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
CC -----------------------------------------------------------------------
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DR EMBL; D26135; BAA05132.1; -; mRNA.
DR EMBL; AF020945; AAC04686.1; -; Genomic_DNA.
DR EMBL; AF020922; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020923; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020924; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020925; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020926; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020927; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020928; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020929; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020930; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020931; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020932; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020933; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020934; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020935; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020936; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020937; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020938; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020939; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020940; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020941; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020942; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020943; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020944; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AK314192; BAG36871.1; -; mRNA.
DR EMBL; AC007917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089411; AAH89411.1; -; mRNA.
DR EMBL; BC112363; AAI12364.1; -; mRNA.
DR PIR; A53691; A53691.
DR RefSeq; NP_001074213.1; NM_001080744.1.
DR RefSeq; NP_001074214.1; NM_001080745.1.
DR RefSeq; NP_001337.2; NM_001346.2.
DR UniGene; Hs.683449; -.
DR ProteinModelPortal; P49619; -.
DR SMR; P49619; 1-79, 138-248, 265-323.
DR IntAct; P49619; 2.
DR STRING; 9606.ENSP00000265022; -.
DR ChEMBL; CHEMBL1075157; -.
DR DrugBank; DB00144; Phosphatidylserine.
DR PhosphoSite; P49619; -.
DR DMDM; 311033457; -.
DR PaxDb; P49619; -.
DR PRIDE; P49619; -.
DR DNASU; 1608; -.
DR Ensembl; ENST00000265022; ENSP00000265022; ENSG00000058866.
DR Ensembl; ENST00000344484; ENSP00000339777; ENSG00000058866.
DR Ensembl; ENST00000382164; ENSP00000371599; ENSG00000058866.
DR GeneID; 1608; -.
DR KEGG; hsa:1608; -.
DR UCSC; uc003fqa.3; human.
DR CTD; 1608; -.
DR GeneCards; GC03M185823; -.
DR HGNC; HGNC:2853; DGKG.
DR HPA; HPA036577; -.
DR MIM; 601854; gene.
DR neXtProt; NX_P49619; -.
DR PharmGKB; PA27314; -.
DR eggNOG; NOG47311; -.
DR HOGENOM; HOG000252931; -.
DR HOVERGEN; HBG051345; -.
DR InParanoid; P49619; -.
DR KO; K00901; -.
DR OMA; CYQSVTA; -.
DR OrthoDB; EOG75XGK8; -.
DR PhylomeDB; P49619; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_604; Hemostasis.
DR SABIO-RK; P49619; -.
DR GeneWiki; DGKG; -.
DR GenomeRNAi; 1608; -.
DR NextBio; 6606; -.
DR PRO; PR:P49619; -.
DR ArrayExpress; P49619; -.
DR Bgee; P49619; -.
DR CleanEx; HS_DGKG; -.
DR Genevestigator; P49619; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; TAS:ProtInc.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
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 GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR016064; ATP-NAD_kinase_PpnK-typ.
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; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR Pfam; PF00130; C1_1; 1.
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 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Calcium; Complete proteome;
KW Cytoplasm; Kinase; Membrane; Metal-binding; Nucleotide-binding;
KW Polymorphism; Reference proteome; Repeat; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1 791 Diacylglycerol kinase gamma.
FT /FTId=PRO_0000218459.
FT DOMAIN 175 210 EF-hand 1.
FT DOMAIN 220 255 EF-hand 2.
FT DOMAIN 430 564 DAGKc.
FT CA_BIND 188 199 1 (Potential).
FT CA_BIND 233 244 2 (Potential).
FT ZN_FING 271 321 Phorbol-ester/DAG-type 1.
FT ZN_FING 336 385 Phorbol-ester/DAG-type 2.
FT COMPBIAS 151 156 Poly-Ser.
FT VAR_SEQ 334 372 Missing (in isoform 3).
FT /FTId=VSP_039922.
FT VAR_SEQ 451 475 Missing (in isoform 2).
FT /FTId=VSP_001267.
FT VARIANT 142 142 T -> S (in dbSNP:rs1004588).
FT /FTId=VAR_020259.
FT VARIANT 316 316 R -> K (in dbSNP:rs2193587).
FT /FTId=VAR_024430.
FT VARIANT 370 370 R -> W (in dbSNP:rs3213770).
FT /FTId=VAR_020260.
FT VARIANT 706 706 E -> K (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036119.
FT CONFLICT 271 271 R -> G (in Ref. 1; BAA05132 and 2;
FT AAC04686).
SQ SEQUENCE 791 AA; 89124 MW; A1382CF1B2CD7362 CRC64;
MGEERWVSLT PEEFDQLQKY SEYSSKKIKD ALTEFNEGGS LKQYDPHEPI SYDVFKLFMR
AYLEVDLPQP LSTHLFLAFS QKPRHETSDH PTEGASNSEA NSADTNIQNA DNATKADEAC
APDTESNMAE KQAPAEDQVA ATPLEPPVPR SSSSESPVVY LKDVVCYLSL LETGRPQDKL
EFMFRLYDSD ENGLLDQAEM DCIVNQMLHI AQYLEWDPTE LRPILKEMLQ GMDYDRDGFV
SLQEWVHGGM TTIPLLVLLG MDDSGSKGDG RHAWTMKHFK KPTYCNFCHI MLMGVRKQGL
CCTYCKYTVH ERCVSRNIPG CVKTYSKAKR SGEVMQHAWV EGNSSVKCDR CHKSIKCYQS
VTARHCVWCR MTFHRKCELS TLCDGGELRD HILLPTSICP ITRDRPGEKS DGCVSAKGEL
VMQYKIIPTP GTHPLLVLVN PKSGGRQGER ILRKFHYLLN PKQVFNLDNG GPTPGLNFFR
DTPDFRVLAC GGDGTVGWIL DCIDKANFAK HPPVAVLPLG TGNDLARCLR WGGGYEGGSL
TKILKDIEQS PLVMLDRWHL EVIPREEVEN GDQVPYSIMN NYFSIGVDAS IAHRFHVMRE
KHPEKFNSRM KNKLWYFEFG TSETFAATCK KLHDHIELEC DGVGVDLSNI FLEGIAILNI
PSMYGGTNLW GENKKNRAVI RESRKGVTDP KELKFCVQDL SDQLLEVVGL EGAMEMGQIY
TGLKSAGRRL AQCASVTIRT NKLLPMQVDG EPWMQPCCTI KITHKNQAPM MMGPPQKSSF
FSLRRKSRSK D
//
MIM
601854
*RECORD*
*FIELD* NO
601854
*FIELD* TI
*601854 DIACYLGLYCEROL KINASE, GAMMA, 90-KD; DGKG
;;DIACYLGLYCEROL KINASE, GAMMA; DAGK3;;
read moreDAGK, 90-KD;;
DGK-GAMMA
*FIELD* TX
See 125855 for a general discussion of the diacylglycerol kinases.
Kai et al. (1994) used degenerate PCR to clone a novel DGK, termed
DGK-gamma, from HepG2 human hepatoma mRNA. They subsequently cloned a
full-length cDNA from a HepG2 cDNA library. Sequence analysis revealed
that DGK-gamma encodes a polypeptide of 791 amino acids which is 52%
similar to that of DGK-alpha (DAGK1; 125855) and 62% similar to that of
DGK-beta (604070). All 3 DGK isozymes contain 2 conserved EF-hand
calcium-binding motifs and 2 zinc finger domains. They also noted that
some cDNAs contained a 25-amino acid truncation, which the authors
presumed to be an alternate splicing variant. Both the full-length and
truncated transcripts are present in a range of human tissues, with
greatest expression observed in retina. When expressed in COS-7 cells,
Kai et al. (1994) observed that full-length, but not truncated,
DGK-gamma gave DGK activity. This activity was
phosphatidylserine-dependent and had no apparent specificity with regard
to the acyl group.
Kai et al. (1994) showed that DAGK3 is expressed predominantly in the
human retina. Mutations in the gene encoding an eye-specific
diacylglycerol kinase (DGK2) are known to cause retinal degeneration A
(rdgA) in Drosophila melanogaster (Masai et al., 1993). Based on these
findings, Stohr et al. (1999) reasoned that DAGK3 might be an excellent
candidate gene for a human eye disease. They found that the human DAGK3
gene spans over 30 kb of genomic DNA interrupted by 23 introns. By FISH,
they mapped the DAGK3 locus to 3q27-q28, overlapping the chromosomal
region known to contain the gene (OPA1; 605290) underlying dominant
optic atrophy (165500), the most common form of hereditary atrophy of
the optic nerve. Mutational analysis of the entire coding region of
DAGK3 in 19 unrelated German optic atrophy-1 patients did not reveal any
disease-causing mutations, thus excluding DAGK3 as a major cause
underlying optic atrophy-1.
*FIELD* RF
1. Kai, M.; Sakane, F.; Imai, S.; Wada, I.; Kanoh, H.: Molecular
cloning of a diacylglycerol kinase isozyme predominantly expressed
in human retina with a truncated and inactive enzyme expression in
most other human cells. J. Biol. Chem. 269: 18492-18498, 1994.
2. Masai, I.; Okazaki, A.; Hosoya, T.; Hotta, Y.: Drosophila retinal
degeneration A gene encodes an eye-specific diacylglycerol kinase
with cysteine-rich zinc-finger motifs and ankyrin repeats. Proc.
Nat. Acad. Sci. 90: 11157-11161, 1993.
3. Stohr, H.; Klein, J.; Gehrig, A.; Koehler, M. R.; Jurklies, B.;
Kellner, U.; Leo-Kottler, B.; Schmid, M.; Weber, B. H. F.: Mapping
and genomic characterization of the gene encoding diacylglycerol kinase
gamma (DAGK3): assessment of its role in dominant optic atrophy (OPA1). Hum.
Genet. 104: 99-105, 1999.
*FIELD* CN
Rebekah S. Rasooly - updated: 7/28/1999
Victor A. McKusick - updated: 3/16/1999
*FIELD* CD
Jennifer P. Macke: 3/14/1997
*FIELD* ED
alopez: 09/26/2000
mgross: 7/28/1999
terry: 3/16/1999
alopez: 10/16/1998
terry: 7/30/1998
alopez: 6/24/1997
alopez: 6/10/1997
*RECORD*
*FIELD* NO
601854
*FIELD* TI
*601854 DIACYLGLYCEROL KINASE, GAMMA, 90-KD; DGKG
;;DIACYLGLYCEROL KINASE, GAMMA; DAGK3;;
read moreDAGK, 90-KD;;
DGK-GAMMA
*FIELD* TX
See 125855 for a general discussion of the diacylglycerol kinases.
Kai et al. (1994) used degenerate PCR to clone a novel DGK, termed
DGK-gamma, from HepG2 human hepatoma mRNA. They subsequently cloned a
full-length cDNA from a HepG2 cDNA library. Sequence analysis revealed
that DGK-gamma encodes a polypeptide of 791 amino acids which is 52%
similar to that of DGK-alpha (DAGK1; 125855) and 62% similar to that of
DGK-beta (604070). All 3 DGK isozymes contain 2 conserved EF-hand
calcium-binding motifs and 2 zinc finger domains. They also noted that
some cDNAs contained a 25-amino acid truncation, which the authors
presumed to be an alternate splicing variant. Both the full-length and
truncated transcripts are present in a range of human tissues, with
greatest expression observed in retina. When expressed in COS-7 cells,
Kai et al. (1994) observed that full-length, but not truncated,
DGK-gamma gave DGK activity. This activity was
phosphatidylserine-dependent and had no apparent specificity with regard
to the acyl group.
Kai et al. (1994) showed that DAGK3 is expressed predominantly in the
human retina. Mutations in the gene encoding an eye-specific
diacylglycerol kinase (DGK2) are known to cause retinal degeneration A
(rdgA) in Drosophila melanogaster (Masai et al., 1993). Based on these
findings, Stohr et al. (1999) reasoned that DAGK3 might be an excellent
candidate gene for a human eye disease. They found that the human DAGK3
gene spans over 30 kb of genomic DNA interrupted by 23 introns. By FISH,
they mapped the DAGK3 locus to 3q27-q28, overlapping the chromosomal
region known to contain the gene (OPA1; 605290) underlying dominant
optic atrophy (165500), the most common form of hereditary atrophy of
the optic nerve. Mutational analysis of the entire coding region of
DAGK3 in 19 unrelated German optic atrophy-1 patients did not reveal any
disease-causing mutations, thus excluding DAGK3 as a major cause
underlying optic atrophy-1.
*FIELD* RF
1. Kai, M.; Sakane, F.; Imai, S.; Wada, I.; Kanoh, H.: Molecular
cloning of a diacylglycerol kinase isozyme predominantly expressed
in human retina with a truncated and inactive enzyme expression in
most other human cells. J. Biol. Chem. 269: 18492-18498, 1994.
2. Masai, I.; Okazaki, A.; Hosoya, T.; Hotta, Y.: Drosophila retinal
degeneration A gene encodes an eye-specific diacylglycerol kinase
with cysteine-rich zinc-finger motifs and ankyrin repeats. Proc.
Nat. Acad. Sci. 90: 11157-11161, 1993.
3. Stohr, H.; Klein, J.; Gehrig, A.; Koehler, M. R.; Jurklies, B.;
Kellner, U.; Leo-Kottler, B.; Schmid, M.; Weber, B. H. F.: Mapping
and genomic characterization of the gene encoding diacylglycerol kinase
gamma (DAGK3): assessment of its role in dominant optic atrophy (OPA1). Hum.
Genet. 104: 99-105, 1999.
*FIELD* CN
Rebekah S. Rasooly - updated: 7/28/1999
Victor A. McKusick - updated: 3/16/1999
*FIELD* CD
Jennifer P. Macke: 3/14/1997
*FIELD* ED
alopez: 09/26/2000
mgross: 7/28/1999
terry: 3/16/1999
alopez: 10/16/1998
terry: 7/30/1998
alopez: 6/24/1997
alopez: 6/10/1997