ID GRK4_HUMAN Reviewed; 578 AA. AC P32298; O00641; O00642; Q13293; Q13294; Q13295; Q14453; Q14725; AC Q15313; Q15314; Q15315; Q15316; Q17RH6; Q53EQ8; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 3. DT 09-DEC-2015, entry version 158. DE RecName: Full=G protein-coupled receptor kinase 4; DE EC=2.7.11.16; DE AltName: Full=G protein-coupled receptor kinase GRK4; DE AltName: Full=ITI1; GN Name=GRK4; Synonyms=GPRK2L, GPRK4; 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 [GENOMIC DNA] (ISOFORM 3), AND VARIANT ALA-486. RX PubMed=1338872; DOI=10.1093/hmg/1.9.697; RA Ambrose C., James M., Barnes G., Lin C., Bates G., Altherr M., RA Duyao M., Groot N., Church D., Wasmuth J.J., Lehrach H., Housman D., RA Buckler A.J., Gusella J.F., McDonald M.E.; RT "A novel G protein-coupled receptor kinase gene cloned from 4p16.3."; RL Hum. Mol. Genet. 1:697-703(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND VARIANT RP ALA-486. RC TISSUE=Testis; RX PubMed=9092566; DOI=10.1074/jbc.272.15.10188; RA Sallese M., Mariggio S., Collodel G., Moretti E., Piomboni P., RA Baccetti B., de Blasi A.; RT "G protein-coupled receptor kinase GRK4. Molecular analysis of the RT four isoforms and ultrastructural localization in spermatozoa and RT germinal cells."; RL J. Biol. Chem. 272:10188-10195(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PALMITOYLATION, RP AND VARIANT ALA-486. RC TISSUE=Testis; RX PubMed=8626439; DOI=10.1074/jbc.271.11.6403; RA Premont R.T., Macrae A.D., Stoffel R.H., Chung N., Pitcher J.A., RA Ambrose C., Inglese J., MacDonald M.E., Lefkowitz R.J.; RT "Characterization of the G protein-coupled receptor kinase GRK4. RT Identification of four splice variants."; RL J. Biol. Chem. 271:6403-6410(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ALA-486. RC TISSUE=Brain; RX PubMed=8135832; DOI=10.1006/bbrc.1994.1306; RA Sallese M., Lombardi M.S., de Blasi A.; RT "Two isoforms of G protein-coupled receptor kinase 4 identified by RT molecular cloning."; RL Biochem. Biophys. Res. Commun. 199:848-854(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Kidney; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP ALA-486. 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 [8] RP TISSUE SPECIFICITY. RX PubMed=16636192; DOI=10.1161/01.HYP.0000222004.74872.17; RA Sanada H., Yatabe J., Midorikawa S., Katoh T., Hashimoto S., RA Watanabe T., Xu J., Luo Y., Wang X., Zeng C., Armando I., Felder R.A., RA Jose P.A.; RT "Amelioration of genetic hypertension by suppression of renal G RT protein-coupled receptor kinase type 4 expression."; RL Hypertension 47:1131-1139(2006). RN [9] RP FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, AND INTERACTION RP WITH DRD3. RX PubMed=19520868; DOI=10.1074/jbc.M109.003665; RA Villar V.A.M., Jones J.E., Armando I., Palmes-Saloma C., Yu P., RA Pascua A.M., Keever L., Arnaldo F.B., Wang Z., Luo Y., Felder R.A., RA Jose P.A.; RT "G protein-coupled receptor kinase 4 (GRK4) regulates the RT phosphorylation and function of the dopamine D3 receptor."; RL J. Biol. Chem. 284:21425-21434(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [11] RP VARIANTS [LARGE SCALE ANALYSIS] LEU-65; THR-116; VAL-142; ILE-247; RP GLN-383; PRO-425; ILE-473; ALA-486 AND THR-495. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Specifically phosphorylates the activated forms of G CC protein-coupled receptors. GRK4-alpha can phosphorylate rhodopsin CC and its activity is inhibited by calmodulin; the other three CC isoforms do not phosphorylate rhodopsin and do not interact with CC calmodulin. GRK4-alpha and GRK4-gamma phosphorylate DRD3. CC Phosphorylates ADRB2. {ECO:0000269|PubMed:19520868, CC ECO:0000269|PubMed:8626439}. CC -!- CATALYTIC ACTIVITY: ATP + [G-protein-coupled receptor] = ADP + [G- CC protein-coupled receptor] phosphate. CC -!- ENZYME REGULATION: Inhibited by heparin. CC {ECO:0000269|PubMed:19520868}. CC -!- SUBUNIT: Interacts with DRD3. {ECO:0000269|PubMed:19520868}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cell cortex. Note=Both CC at the cell surface and dispersed in the cytoplasm under basal CC conditions. Receptor stimulation results in the internalization of CC GRK4 to the perinuclear area, where colocalization with DRD3 is CC observed strongly at 5 and 15 minutes. DRD3 and GRK4 colocalize in CC lipid rafts of renal proximal tubule cells. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=GRK4-alpha, GRK4D; CC IsoId=P32298-1; Sequence=Displayed; CC Name=2; Synonyms=GRK4-beta, GRK4C; CC IsoId=P32298-2; Sequence=VSP_004936; CC Name=3; Synonyms=GRK4-delta, GRK4A; CC IsoId=P32298-3; Sequence=VSP_004936, VSP_004937; CC Name=4; Synonyms=GRK4-gamma, GRK4B; CC IsoId=P32298-4; Sequence=VSP_004937; CC -!- TISSUE SPECIFICITY: Isoform 1, isoform 2, isoform 3, and isoform 4 CC are expressed in testis. Isoform 4 is expressed in myometrium. CC {ECO:0000269|PubMed:16636192, ECO:0000269|PubMed:8626439}. CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:8626439}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. GPRK subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SIMILARITY: Contains 1 RGS domain. {ECO:0000255|PROSITE- CC ProRule:PRU00171}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L03718; AAB04045.1; -; Genomic_DNA. DR EMBL; X97879; CAA66468.1; -; mRNA. DR EMBL; X97880; CAA66469.1; -; mRNA. DR EMBL; X97881; CAA66470.1; -; mRNA. DR EMBL; U33054; AAC50406.1; -; mRNA. DR EMBL; U33055; AAC50407.1; -; mRNA. DR EMBL; U33056; AAC50408.1; -; mRNA. DR EMBL; U33168; AAC50409.1; -; Genomic_DNA. DR EMBL; U33153; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33155; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33156; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33157; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33158; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33159; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33160; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33161; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33162; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33163; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33164; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33165; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33166; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33167; AAC50409.1; JOINED; Genomic_DNA. DR EMBL; U33168; AAC50410.1; -; Genomic_DNA. DR EMBL; U33153; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33154; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33155; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33156; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33157; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33158; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33159; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33160; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33161; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33162; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33163; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33164; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33165; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33166; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33167; AAC50410.1; JOINED; Genomic_DNA. DR EMBL; U33168; AAC50411.1; -; Genomic_DNA. DR EMBL; U33153; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33154; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33155; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33156; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33157; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33158; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33159; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33160; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33161; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33162; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33163; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33164; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33165; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33166; AAC50411.1; JOINED; Genomic_DNA. DR EMBL; U33168; AAC50412.1; -; Genomic_DNA. DR EMBL; U33153; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33155; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33156; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33157; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33158; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33159; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33160; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33161; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33162; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33163; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33164; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33165; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; U33166; AAC50412.1; JOINED; Genomic_DNA. DR EMBL; AK223581; BAD97301.1; -; mRNA. DR EMBL; X98118; CAA66802.1; -; mRNA. DR EMBL; X75897; CAA53506.1; -; mRNA. DR EMBL; Z68192; CAA92341.1; -; Genomic_DNA. DR EMBL; BC117320; AAI17321.1; -; mRNA. DR CCDS; CCDS33946.1; -. [P32298-1] DR CCDS; CCDS33947.1; -. [P32298-4] DR CCDS; CCDS47002.1; -. [P32298-2] DR CCDS; CCDS68656.1; -. [P32298-3] DR PIR; I54326; I54326. DR PIR; JC2127; JC2127. DR RefSeq; NP_001004056.1; NM_001004056.1. [P32298-2] DR RefSeq; NP_001004057.1; NM_001004057.1. [P32298-4] DR RefSeq; NP_005298.2; NM_005307.2. [P32298-3] DR RefSeq; NP_892027.2; NM_182982.2. [P32298-1] DR UniGene; Hs.32959; -. DR PDB; 4YHJ; X-ray; 2.60 A; A/B=1-578. DR PDBsum; 4YHJ; -. DR ProteinModelPortal; P32298; -. DR SMR; P32298; 2-558. DR BioGrid; 109126; 5. DR IntAct; P32298; 2. DR STRING; 9606.ENSP00000381129; -. DR BindingDB; P32298; -. DR ChEMBL; CHEMBL5861; -. DR GuidetoPHARMACOLOGY; 1468; -. DR PhosphoSite; P32298; -. DR BioMuta; GRK4; -. DR DMDM; 143811400; -. DR MaxQB; P32298; -. DR PaxDb; P32298; -. DR PRIDE; P32298; -. DR DNASU; 2868; -. DR Ensembl; ENST00000345167; ENSP00000264764; ENSG00000125388. [P32298-2] DR Ensembl; ENST00000398051; ENSP00000381128; ENSG00000125388. [P32298-3] DR Ensembl; ENST00000398052; ENSP00000381129; ENSG00000125388. [P32298-1] DR Ensembl; ENST00000504933; ENSP00000427445; ENSG00000125388. [P32298-4] DR GeneID; 2868; -. DR KEGG; hsa:2868; -. DR UCSC; uc003ggn.1; human. [P32298-1] DR UCSC; uc003ggo.1; human. [P32298-4] DR UCSC; uc003ggp.1; human. [P32298-2] DR UCSC; uc003ggq.1; human. [P32298-3] DR CTD; 2868; -. DR GeneCards; GRK4; -. DR HGNC; HGNC:4543; GRK4. DR HPA; HPA028737; -. DR HPA; HPA057023; -. DR MIM; 137026; gene. DR neXtProt; NX_P32298; -. DR PharmGKB; PA28941; -. DR eggNOG; KOG0986; Eukaryota. DR eggNOG; ENOG410YRQZ; LUCA. DR GeneTree; ENSGT00770000120493; -. DR HOVERGEN; HBG004532; -. DR InParanoid; P32298; -. DR KO; K08291; -. DR OMA; HSIEKDY; -. DR OrthoDB; EOG7V1FQK; -. DR PhylomeDB; P32298; -. DR TreeFam; TF313940; -. DR BRENDA; 2.7.11.16; 2681. DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade. DR SignaLink; P32298; -. DR ChiTaRS; GRK4; human. DR GeneWiki; GRK4; -. DR GenomeRNAi; 2868; -. DR NextBio; 11309; -. DR PRO; PR:P32298; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; P32298; -. DR ExpressionAtlas; P32298; baseline and differential. DR Genevisible; P32298; HS. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004703; F:G-protein coupled receptor kinase activity; IEA:UniProtKB-EC. DR GO; GO:0050254; F:rhodopsin kinase activity; IEA:Ensembl. DR GO; GO:0002031; P:G-protein coupled receptor internalization; IEA:Ensembl. DR GO; GO:0007603; P:phototransduction, visible light; TAS:Reactome. DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB. DR GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; TAS:ProtInc. DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome. DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:Reactome. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR000239; GPCR_kinase. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR016137; RGS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00615; RGS; 1. DR PRINTS; PR00717; GPCRKINASE. DR SMART; SM00315; RGS; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF48097; SSF48097; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50132; RGS; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Complete proteome; Cytoplasm; Kinase; Lipoprotein; Nucleotide-binding; KW Palmitate; Phosphoprotein; Polymorphism; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 578 G protein-coupled receptor kinase 4. FT /FTId=PRO_0000085967. FT DOMAIN 52 172 RGS. {ECO:0000255|PROSITE- FT ProRule:PRU00171}. FT DOMAIN 187 449 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT DOMAIN 450 515 AGC-kinase C-terminal. FT NP_BIND 193 201 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT REGION 1 154 N-terminal. FT ACT_SITE 312 312 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 216 216 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:22223895}. FT MOD_RES 485 485 Phosphoserine. FT {ECO:0000250|UniProtKB:P70507}. FT VAR_SEQ 18 49 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:8135832, FT ECO:0000303|PubMed:9092566, FT ECO:0000303|Ref.5}. FT /FTId=VSP_004936. FT VAR_SEQ 516 561 Missing (in isoform 3 and isoform 4). FT {ECO:0000303|PubMed:9092566, FT ECO:0000303|Ref.5}. FT /FTId=VSP_004937. FT VARIANT 65 65 R -> L (in dbSNP:rs2960306). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_024573. FT VARIANT 95 95 D -> H (in dbSNP:rs13305979). FT /FTId=VAR_051621. FT VARIANT 116 116 A -> T (in dbSNP:rs34857805). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_046043. FT VARIANT 142 142 A -> V (in dbSNP:rs1024323). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_024574. FT VARIANT 183 183 T -> R (in dbSNP:rs45538934). FT /FTId=VAR_051622. FT VARIANT 247 247 V -> I (in dbSNP:rs35605687). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_007806. FT VARIANT 383 383 H -> Q (in dbSNP:rs55852353). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_046044. FT VARIANT 425 425 L -> P. {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_040516. FT VARIANT 440 440 A -> V (in dbSNP:rs1801058). FT /FTId=VAR_051623. FT VARIANT 473 473 V -> I (in dbSNP:rs35024854). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_046045. FT VARIANT 486 486 V -> A (in dbSNP:rs1801058). FT {ECO:0000269|PubMed:1338872, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:8135832, FT ECO:0000269|PubMed:8626439, FT ECO:0000269|PubMed:9092566}. FT /FTId=VAR_024575. FT VARIANT 495 495 A -> T (in dbSNP:rs35463176). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_046046. FT CONFLICT 562 562 G -> D (in Ref. 1; CAA66468/CAA66802). FT {ECO:0000305}. FT HELIX 30 33 {ECO:0000244|PDB:4YHJ}. FT TURN 39 42 {ECO:0000244|PDB:4YHJ}. FT HELIX 43 48 {ECO:0000244|PDB:4YHJ}. FT HELIX 53 57 {ECO:0000244|PDB:4YHJ}. FT HELIX 61 71 {ECO:0000244|PDB:4YHJ}. FT HELIX 75 91 {ECO:0000244|PDB:4YHJ}. FT TURN 95 97 {ECO:0000244|PDB:4YHJ}. FT HELIX 98 109 {ECO:0000244|PDB:4YHJ}. FT STRAND 113 115 {ECO:0000244|PDB:4YHJ}. FT HELIX 123 132 {ECO:0000244|PDB:4YHJ}. FT STRAND 135 137 {ECO:0000244|PDB:4YHJ}. FT TURN 140 143 {ECO:0000244|PDB:4YHJ}. FT HELIX 144 154 {ECO:0000244|PDB:4YHJ}. FT HELIX 157 162 {ECO:0000244|PDB:4YHJ}. FT HELIX 166 178 {ECO:0000244|PDB:4YHJ}. FT HELIX 184 186 {ECO:0000244|PDB:4YHJ}. FT STRAND 187 195 {ECO:0000244|PDB:4YHJ}. FT STRAND 197 206 {ECO:0000244|PDB:4YHJ}. FT TURN 207 209 {ECO:0000244|PDB:4YHJ}. FT STRAND 212 219 {ECO:0000244|PDB:4YHJ}. FT HELIX 220 226 {ECO:0000244|PDB:4YHJ}. FT HELIX 229 241 {ECO:0000244|PDB:4YHJ}. FT STRAND 250 255 {ECO:0000244|PDB:4YHJ}. FT STRAND 257 264 {ECO:0000244|PDB:4YHJ}. FT HELIX 272 276 {ECO:0000244|PDB:4YHJ}. FT TURN 277 279 {ECO:0000244|PDB:4YHJ}. FT STRAND 280 283 {ECO:0000244|PDB:4YHJ}. FT HELIX 286 304 {ECO:0000244|PDB:4YHJ}. FT TURN 305 307 {ECO:0000244|PDB:4YHJ}. FT HELIX 315 317 {ECO:0000244|PDB:4YHJ}. FT STRAND 318 320 {ECO:0000244|PDB:4YHJ}. FT STRAND 326 328 {ECO:0000244|PDB:4YHJ}. FT STRAND 341 343 {ECO:0000244|PDB:4YHJ}. FT TURN 350 352 {ECO:0000244|PDB:4YHJ}. FT HELIX 355 358 {ECO:0000244|PDB:4YHJ}. FT STRAND 363 365 {ECO:0000244|PDB:4YHJ}. FT HELIX 366 381 {ECO:0000244|PDB:4YHJ}. FT STRAND 382 384 {ECO:0000244|PDB:4YHJ}. FT HELIX 395 403 {ECO:0000244|PDB:4YHJ}. FT HELIX 415 424 {ECO:0000244|PDB:4YHJ}. FT HELIX 429 431 {ECO:0000244|PDB:4YHJ}. FT TURN 433 438 {ECO:0000244|PDB:4YHJ}. FT HELIX 439 444 {ECO:0000244|PDB:4YHJ}. FT HELIX 447 449 {ECO:0000244|PDB:4YHJ}. FT HELIX 454 458 {ECO:0000244|PDB:4YHJ}. FT HELIX 494 500 {ECO:0000244|PDB:4YHJ}. FT STRAND 505 507 {ECO:0000244|PDB:4YHJ}. FT HELIX 509 518 {ECO:0000244|PDB:4YHJ}. FT TURN 519 524 {ECO:0000244|PDB:4YHJ}. SQ SEQUENCE 578 AA; 66583 MW; 72FCF94ED551F2D0 CRC64; MELENIVANS LLLKARQGGY GKKSGRSKKW KEILTLPPVS QCSELRHSIE KDYSSLCDKQ PIGRRLFRQF CDTKPTLKRH IEFLDAVAEY EVADDEDRSD CGLSILDRFF NDKLAAPLPE IPPDVVTECR LGLKEENPSK KAFEECTRVA HNYLRGEPFE EYQESSYFSQ FLQWKWLERQ PVTKNTFRHY RVLGKGGFGE VCACQVRATG KMYACKKLQK KRIKKRKGEA MALNEKRILE KVQSRFVVSL AYAYETKDAL CLVLTIMNGG DLKFHIYNLG NPGFDEQRAV FYAAELCCGL EDLQRERIVY RDLKPENILL DDRGHIRISD LGLATEIPEG QRVRGRVGTV GYMAPEVVNN EKYTFSPDWW GLGCLIYEMI QGHSPFKKYK EKVKWEEVDQ RIKNDTEEYS EKFSEDAKSI CRMLLTKNPS KRLGCRGEGA AGVKQHPVFK DINFRRLEAN MLEPPFCPDP HAVYCKDVLD IEQFSVVKGI YLDTADEDFY ARFATGCVSI PWQNEMIESG CFKDINKSES EEALPLDLDK NIHTPVSRPN RGFFYRLFRR GGCLTMVPSE KEVEPKQC //