KPCD3_HUMAN
ID KPCD3_HUMAN Reviewed; 890 AA.
AC O94806; D6W587; Q53TR7; Q8NEL8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Serine/threonine-protein kinase D3;
DE EC=2.7.11.13;
DE AltName: Full=Protein kinase C nu type;
DE AltName: Full=Protein kinase EPK2;
DE AltName: Full=nPKC-nu;
GN Name=PRKD3; Synonyms=EPK2, PRKCN;
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).
RC TISSUE=Embryo;
RX PubMed=10231560; DOI=10.1016/s0167-4889(99)00040-3;
RA Hayashi A., Seki N., Hattori A., Kozuma S., Saito T.;
RT "PKCnu, a new member of the protein kinase C family, composes a fourth
RT subfamily with PKCmu.";
RL Biochim. Biophys. Acta 1450:99-106(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 MRNA] (ISOFORM 2), AND VARIANTS THR-128
RP AND ARG-546.
RC TISSUE=Testis;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, PHORBOL-ESTER BINDING, AND
RP MUTAGENESIS OF THR-156; TYR-158; PRO-165; THR-166; TYR-170; PRO-282 AND
RP LYS-293.
RX PubMed=18076381; DOI=10.1042/bj20071334;
RA Chen J., Deng F., Li J., Wang Q.J.;
RT "Selective binding of phorbol esters and diacylglycerol by individual C1
RT domains of the PKD family.";
RL Biochem. J. 411:333-342(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-27; SER-37; SER-41;
RP SER-213; SER-216; SER-364 AND THR-535, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-44 AND
RP SER-364, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-213; SER-216;
RP SER-364 AND THR-535, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41 AND SER-44, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-44 AND SER-364, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP STRUCTURE BY NMR OF 414-532.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PH domain of protein kinase C, nu type from
RT human.";
RL Submitted (JAN-2007) to the PDB data bank.
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] MET-716.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Converts transient diacylglycerol (DAG) signals into
CC prolonged physiological effects, downstream of PKC. Involved in
CC resistance to oxidative stress (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by DAG and phorbol esters. Phorbol-
CC ester/DAG-type domains 1 and 2 bind both DAG and phorbol ester with
CC high affinity and mediate translocation to the cell membrane.
CC Autophosphorylation of Ser-735 and phosphorylation of Ser-731 by PKC
CC relieves auto-inhibition by the PH domain.
CC {ECO:0000269|PubMed:18076381}.
CC -!- INTERACTION:
CC O94806; P63027: VAMP2; NbExp=7; IntAct=EBI-1255366, EBI-520113;
CC O94806-2; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-13337369, EBI-10320765;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18076381}. Membrane
CC {ECO:0000269|PubMed:18076381}. Note=Translocation to the cell membrane
CC is required for kinase activation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94806-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94806-2; Sequence=VSP_029405, VSP_029406;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000305}.
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DR EMBL; AB015982; BAA36514.1; -; mRNA.
DR EMBL; AC007390; AAY14817.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00398.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00399.1; -; Genomic_DNA.
DR EMBL; BC030706; AAH30706.1; -; mRNA.
DR CCDS; CCDS1789.1; -. [O94806-1]
DR RefSeq; NP_005804.1; NM_005813.4. [O94806-1]
DR RefSeq; XP_005264294.1; XM_005264237.3. [O94806-1]
DR PDB; 2D9Z; NMR; -; A=417-532.
DR PDBsum; 2D9Z; -.
DR AlphaFoldDB; O94806; -.
DR BMRB; O94806; -.
DR SMR; O94806; -.
DR BioGRID; 117199; 26.
DR IntAct; O94806; 26.
DR MINT; O94806; -.
DR STRING; 9606.ENSP00000368356; -.
DR BindingDB; O94806; -.
DR ChEMBL; CHEMBL2595; -.
DR DrugCentral; O94806; -.
DR GuidetoPHARMACOLOGY; 2174; -.
DR iPTMnet; O94806; -.
DR PhosphoSitePlus; O94806; -.
DR SwissPalm; O94806; -.
DR BioMuta; PRKD3; -.
DR EPD; O94806; -.
DR jPOST; O94806; -.
DR MassIVE; O94806; -.
DR MaxQB; O94806; -.
DR PaxDb; O94806; -.
DR PeptideAtlas; O94806; -.
DR PRIDE; O94806; -.
DR ProteomicsDB; 50446; -. [O94806-1]
DR ProteomicsDB; 50447; -. [O94806-2]
DR Antibodypedia; 14569; 428 antibodies from 37 providers.
DR DNASU; 23683; -.
DR Ensembl; ENST00000234179.8; ENSP00000234179.2; ENSG00000115825.11. [O94806-1]
DR Ensembl; ENST00000379066.5; ENSP00000368356.1; ENSG00000115825.11. [O94806-1]
DR GeneID; 23683; -.
DR KEGG; hsa:23683; -.
DR MANE-Select; ENST00000234179.8; ENSP00000234179.2; NM_005813.6; NP_005804.1.
DR UCSC; uc002rqd.4; human. [O94806-1]
DR CTD; 23683; -.
DR DisGeNET; 23683; -.
DR GeneCards; PRKD3; -.
DR HGNC; HGNC:9408; PRKD3.
DR HPA; ENSG00000115825; Low tissue specificity.
DR MIM; 607077; gene.
DR neXtProt; NX_O94806; -.
DR OpenTargets; ENSG00000115825; -.
DR PharmGKB; PA33772; -.
DR VEuPathDB; HostDB:ENSG00000115825; -.
DR eggNOG; KOG4236; Eukaryota.
DR GeneTree; ENSGT00950000183024; -.
DR HOGENOM; CLU_009772_1_0_1; -.
DR InParanoid; O94806; -.
DR OMA; VCSVVYQ; -.
DR OrthoDB; 367841at2759; -.
DR PhylomeDB; O94806; -.
DR TreeFam; TF314320; -.
DR BRENDA; 2.7.11.13; 2681.
DR PathwayCommons; O94806; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR SignaLink; O94806; -.
DR SIGNOR; O94806; -.
DR BioGRID-ORCS; 23683; 14 hits in 1113 CRISPR screens.
DR ChiTaRS; PRKD3; human.
DR EvolutionaryTrace; O94806; -.
DR GeneWiki; PRKD3; -.
DR GenomeRNAi; 23683; -.
DR Pharos; O94806; Tchem.
DR PRO; PR:O94806; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O94806; protein.
DR Bgee; ENSG00000115825; Expressed in calcaneal tendon and 196 other tissues.
DR ExpressionAtlas; O94806; baseline and differential.
DR Genevisible; O94806; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IDA:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004697; F:protein kinase C activity; TAS:Reactome.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0089700; P:protein kinase D signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
DR CDD; cd00029; C1; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015727; Protein_Kinase_C_mu-related.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22968; PTHR22968; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000552; PKC_mu_nu_D2; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..890
FT /note="Serine/threonine-protein kinase D3"
FT /id="PRO_0000055717"
FT DOMAIN 416..532
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 576..832
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 154..204
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 271..321
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 332..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 699
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 582..590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 426
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 457
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL6"
FT MOD_RES 535
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1Y2"
FT MOD_RES 731
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 735
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 742
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL6"
FT VAR_SEQ 595..611
FT /note="HRKTGRDVAIKVIDKMR -> QLQPFAYCTHYFKNWKM (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029405"
FT VAR_SEQ 612..890
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029406"
FT VARIANT 42
FT /note="N -> D (in dbSNP:rs11896614)"
FT /id="VAR_037147"
FT VARIANT 128
FT /note="A -> T (in dbSNP:rs17852819)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037148"
FT VARIANT 225
FT /note="P -> S (in dbSNP:rs34280934)"
FT /id="VAR_050561"
FT VARIANT 445
FT /note="L -> I (in dbSNP:rs55912911)"
FT /id="VAR_061532"
FT VARIANT 546
FT /note="Q -> R (in dbSNP:rs17856887)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037149"
FT VARIANT 716
FT /note="V -> M (in a glioblastoma multiforme sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042336"
FT MUTAGEN 156
FT /note="T->A: Slight loss in ability to bind DAG and
FT phorbol-ester; when associated with F-158."
FT /evidence="ECO:0000269|PubMed:18076381"
FT MUTAGEN 158
FT /note="Y->F: Slight loss in ability to bind DAG and
FT phorbol-ester; when associated with A-156."
FT /evidence="ECO:0000269|PubMed:18076381"
FT MUTAGEN 165
FT /note="P->G: No effect on ability to bind phorbol ester,
FT loss of ability to bind DAG, reduced DAG-induced membrane
FT translocation."
FT /evidence="ECO:0000269|PubMed:18076381"
FT MUTAGEN 166
FT /note="T->A: Slight loss in ability to bind DAG and
FT phorbol-ester."
FT /evidence="ECO:0000269|PubMed:18076381"
FT MUTAGEN 170
FT /note="Y->F: Slight loss in ability to bind DAG and
FT phorbol-ester."
FT /evidence="ECO:0000269|PubMed:18076381"
FT MUTAGEN 282
FT /note="P->G: No effect on ability to bind phorbol ester,
FT increase in ability to bind DAG."
FT /evidence="ECO:0000269|PubMed:18076381"
FT MUTAGEN 284
FT /note="I->V: Slight increase in ability to bind DAG, no
FT effect on phorbol-ester binding."
FT MUTAGEN 293
FT /note="K->W: Increased ability to bind DAG, no effect on
FT phorbol-ester binding."
FT /evidence="ECO:0000269|PubMed:18076381"
FT STRAND 417..429
FT /evidence="ECO:0007829|PDB:2D9Z"
FT STRAND 434..443
FT /evidence="ECO:0007829|PDB:2D9Z"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:2D9Z"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:2D9Z"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:2D9Z"
FT STRAND 485..489
FT /evidence="ECO:0007829|PDB:2D9Z"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:2D9Z"
FT TURN 508..514
FT /evidence="ECO:0007829|PDB:2D9Z"
FT HELIX 517..532
FT /evidence="ECO:0007829|PDB:2D9Z"
SQ SEQUENCE 890 AA; 100471 MW; 66D5E7E7235064F5 CRC64;
MSANNSPPSA QKSVLPTAIP AVLPAASPCS SPKTGLSARL SNGSFSAPSL TNSRGSVHTV
SFLLQIGLTR ESVTIEAQEL SLSAVKDLVC SIVYQKFPEC GFFGMYDKIL LFRHDMNSEN
ILQLITSADE IHEGDLVEVV LSALATVEDF QIRPHTLYVH SYKAPTFCDY CGEMLWGLVR
QGLKCEGCGL NYHKRCAFKI PNNCSGVRKR RLSNVSLPGP GLSVPRPLQP EYVALPSEES
HVHQEPSKRI PSWSGRPIWM EKMVMCRVKV PHTFAVHSYT RPTICQYCKR LLKGLFRQGM
QCKDCKFNCH KRCASKVPRD CLGEVTFNGE PSSLGTDTDI PMDIDNNDIN SDSSRGLDDT
EEPSPPEDKM FFLDPSDLDV ERDEEAVKTI SPSTSNNIPL MRVVQSIKHT KRKSSTMVKE
GWMVHYTSRD NLRKRHYWRL DSKCLTLFQN ESGSKYYKEI PLSEILRISS PRDFTNISQG
SNPHCFEIIT DTMVYFVGEN NGDSSHNPVL AATGVGLDVA QSWEKAIRQA LMPVTPQASV
CTSPGQGKDH KDLSTSISVS NCQIQENVDI STVYQIFADE VLGSGQFGIV YGGKHRKTGR
DVAIKVIDKM RFPTKQESQL RNEVAILQNL HHPGIVNLEC MFETPERVFV VMEKLHGDML
EMILSSEKSR LPERITKFMV TQILVALRNL HFKNIVHCDL KPENVLLASA EPFPQVKLCD
FGFARIIGEK SFRRSVVGTP AYLAPEVLRS KGYNRSLDMW SVGVIIYVSL SGTFPFNEDE
DINDQIQNAA FMYPPNPWRE ISGEAIDLIN NLLQVKMRKR YSVDKSLSHP WLQDYQTWLD
LREFETRIGE RYITHESDDA RWEIHAYTHN LVYPKHFIMA PNPDDMEEDP
