ID DGKI_HUMAN Reviewed; 1065 AA. AC O75912; A4D1Q9; Q9NZ49; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 25-JAN-2012, entry version 106. DE RecName: Full=Diacylglycerol kinase iota; DE Short=DAG kinase iota; DE EC=2.7.1.107; DE AltName: Full=Diglyceride kinase iota; DE Short=DGK-iota; GN Name=DGKI; 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]. RC TISSUE=Retina; RX MEDLINE=99047655; PubMed=9830018; DOI=10.1074/jbc.273.49.32746; RA Ding L., Traer E., McIntyre T.M., Zimmerman G.A., Prescott S.M.; RT "The cloning and characterization of a novel human diacylglycerol RT kinase, DGK-iota."; RL J. Biol. Chem. 273:32746-32752(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22616434; 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., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA 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., RA Mural R.J., Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-1065, AND VARIANT PHE-153. RX MEDLINE=20173854; PubMed=10706894; RA Bowne S.J., Sullivan L.S., Ding L., Traer E., Prescott S.M., RA Birch D.G., Kennan A., Humphries P., Daiger S.P.; RT "Evaluation of human diacylglycerol kinase iota, DGKI, a homolog of RT Drosophila rdgA, in inherited retinopathy mapping to 7q."; RL Mol. Vis. 6:6-9(2000). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1049 AND TYR-1053, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18187866; DOI=10.2116/analsci.24.161; RA Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; RT "Automated phosphoproteome analysis for cultured cancer cells by two- RT dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; RL Anal. Sci. 24:161-166(2008). CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl- CC sn-glycerol 3-phosphate. CC -!- INTERACTION: CC P40337-3:VHL; NbExp=3; IntAct=EBI-1765520, EBI-301270; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase CC family. CC -!- SIMILARITY: Contains 2 ANK repeats. CC -!- SIMILARITY: Contains 1 DAGKc domain. CC -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF061936; AAC62010.1; -; mRNA. DR EMBL; CH236950; EAL24051.1; -; Genomic_DNA. DR EMBL; AF219939; AAF43006.1; -; Genomic_DNA. DR EMBL; AF219907; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219908; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219909; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219910; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219911; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219912; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219913; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219914; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219915; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219916; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219917; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219918; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219919; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219920; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219921; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219922; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219923; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219924; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219925; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219926; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219927; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219928; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219929; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219930; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219931; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219932; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219933; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219934; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219935; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219936; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219937; AAF43006.1; JOINED; Genomic_DNA. DR EMBL; AF219938; AAF43006.1; JOINED; Genomic_DNA. DR IPI; IPI00027380; -. DR RefSeq; NP_004708.1; NM_004717.2. DR UniGene; Hs.242947; -. DR ProteinModelPortal; O75912; -. DR SMR; O75912; 924-1051. DR IntAct; O75912; 2. DR STRING; O75912; -. DR PhosphoSite; O75912; -. DR PRIDE; O75912; -. DR Ensembl; ENST00000288490; ENSP00000288490; ENSG00000157680. DR GeneID; 9162; -. DR KEGG; hsa:9162; -. DR UCSC; uc003vtt.1; human. DR CTD; 9162; -. DR GeneCards; GC07M137073; -. DR H-InvDB; HIX0078758; -. DR H-InvDB; HIX0078873; -. DR HGNC; HGNC:2855; DGKI. DR HPA; HPA021924; -. DR MIM; 604072; gene. DR neXtProt; NX_O75912; -. DR PharmGKB; PA27316; -. DR eggNOG; prNOG18217; -. DR GeneTree; ENSGT00600000084185; -. DR HOVERGEN; HBG067303; -. DR InParanoid; O75912; -. DR PhylomeDB; O75912; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_604; Hemostasis. DR NextBio; 34367; -. DR ArrayExpress; O75912; -. DR Bgee; O75912; -. DR CleanEx; HS_DGKI; -. DR Genevestigator; O75912; -. DR GermOnline; ENSG00000157680; Homo sapiens. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004143; F:diacylglycerol kinase activity; TAS:ProtInc. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007205; P:activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway; IEA:InterPro. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0030168; P:platelet activation; TAS:Reactome. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR020683; Ankyrin_rpt-contain_dom. DR InterPro; IPR000756; Diacylglycerol_kin_accessory. DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom. DR InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd. DR Gene3D; G3DSA:1.25.40.20; ANK; 1. DR KO; K00901; -. DR Pfam; PF00023; Ank; 1. DR Pfam; PF00130; C1_1; 1. DR Pfam; PF00609; DAGK_acc; 1. DR Pfam; PF00781; DAGK_cat; 1. DR SMART; SM00248; ANK; 2. DR SMART; SM00109; C1; 2. DR SMART; SM00045; DAGKa; 1. DR SMART; SM00046; DAGKc; 1. DR SUPFAM; SSF48403; ANK; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 2. DR PROSITE; PS50146; DAGK; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; FALSE_NEG. DR PROSITE; PS50081; ZF_DAG_PE_2; FALSE_NEG. PE 1: Evidence at protein level; KW ANK repeat; ATP-binding; Complete proteome; Cytoplasm; Kinase; KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; Transferase; Zinc; KW Zinc-finger. FT CHAIN 1 1065 Diacylglycerol kinase iota. FT /FTId=PRO_0000218466. FT DOMAIN 372 507 DAGKc. FT REPEAT 958 990 ANK 1. FT REPEAT 997 1026 ANK 2. FT ZN_FING 178 232 Phorbol-ester/DAG-type 1. FT ZN_FING 251 309 Phorbol-ester/DAG-type 2. FT COMPBIAS 20 31 Poly-Ala. FT COMPBIAS 69 74 Poly-Ser. FT COMPBIAS 95 102 Poly-Ala. FT MOD_RES 1049 1049 Phosphoserine. FT MOD_RES 1053 1053 Phosphotyrosine. FT VARIANT 153 153 L -> F. FT /FTId=VAR_010190. FT CONFLICT 160 160 A -> P (in Ref. 3; AAF43006). SQ SEQUENCE 1065 AA; 116997 MW; B84971AA7630A799 CRC64; MDAAGRGCHL LPLPAARGPA RAPAAAAAAA ASPPGPCSGA ACAPSAAAGA GAMNPSSSAG EEKGATGGSS SSGSGAGSCC LGAEGGADPR GAGSAAAAGA AALDEPAAAG QKEKDEALEE KLRNLTFRKQ VSYRKAISRA GLQHLAPAHP LSLPVANGPA KEPRATLDWS ENAVNGEHLW LETNVSGDLC YLGEENCQVR FAKSALRRKC AVCKIVVHTA CIEQLEKINF RCKPTFREGG SRSPRENFVR HHWVHRRRQE GKCKQCGKGF QQKFSFHSKE IVAISCSWCK QAFHNKVTCF MLHHIEEPCS LGAHAAVIVP PTWIIKVKKP QNSLKASNRK KKRTSFKRKA SKRGMEQENK GRPFVIKPIS SPLMKPLLVF VNPKSGGNQG TKVLQMFMWY LNPRQVFDLS QEGPKDALEL YRKVPNLRIL ACGGDGTVGW ILSILDELQL SPQPPVGVLP LGTGNDLART LNWGGGYTDE PVSKILCQVE DGTVVQLDRW NLHVERNPDL PPEELEDGVC KLPLNVFNNY FSLGFDAHVT LEFHESREAN PEKFNSRFRN KMFYAGAAFS DFLQRSSRDL SKHVKVVCDG TDLTPKIQEL KFQCIVFLNI PRYCAGTMPW GNPGDHHDFE PQRHDDGYIE VIGFTMASLA ALQVGGHGER LHQCREVMLL TYKSIPMQVD GEPCRLAPAM IRISLRNQAN MVQKSKRRTS MPLLNDPQSV PDRLRIRVNK ISLQDYEGFH YDKEKLREAS ISDWLRTIAG ELVQSFGAIP LGILVVRGDC DLETCRMYID RLQEDLQSVS SGSQRVHYQD HETSFPRALS AQRLSPRWCF LDDRSQEHLH FVMEISQDEI FILDPDMVVS QPAGTPPGMP DLVVEQASGI SDWWNPALRK RMLSDSGLGM IAPYYEDSDL KDLSHSRVLQ SPVSSEDHAI LQAVIAGDLM KLIESYKNGG SLLIQGPDHC SLLHYAAKTG NGEIVKYILD HGPSELLDMA DSETGETALH KAACQRNRAV CQLLVDAGAS LRKTDSKGKT PQERAQQAGD PDLAAYLESR QNYKVIGHED LETAV //