ID E5KR06_HUMAN Unreviewed; 629 AA. AC E5KR06; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAR-2024, entry version 91. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; 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 {ECO:0000313|EMBL:ADP91336.1}; RN [1] {ECO:0000313|EMBL:ADP91336.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=20843780; DOI=10.1093/nar/gkq750; RA Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., RA Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., RA Speed T.P., Scharfe C.; RT "Identification of rare DNA variants in mitochondrial disorders with RT improved array-based sequencing."; RL Nucleic Acids Res. 39:44-58(2011). 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=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00001433}; 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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}. 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; HQ205626; ADP91336.1; -; Genomic_DNA. DR EMBL; HQ205627; ADP91340.1; -; Genomic_DNA. DR EMBL; HQ205628; ADP91344.1; -; Genomic_DNA. DR EMBL; HQ205629; ADP91348.1; -; Genomic_DNA. DR EMBL; HQ205630; ADP91352.1; -; Genomic_DNA. DR EMBL; HQ205631; ADP91356.1; -; Genomic_DNA. DR EMBL; HQ205632; ADP91360.1; -; Genomic_DNA. DR EMBL; HQ205633; ADP91364.1; -; Genomic_DNA. DR EMBL; HQ205634; ADP91368.1; -; Genomic_DNA. DR EMBL; HQ205635; ADP91372.1; -; Genomic_DNA. DR EMBL; HQ205636; ADP91376.1; -; Genomic_DNA. DR EMBL; HQ205637; ADP91380.1; -; Genomic_DNA. DR EMBL; HQ205638; ADP91384.1; -; Genomic_DNA. DR EMBL; HQ205639; ADP91388.1; -; Genomic_DNA. DR EMBL; HQ205640; ADP91392.1; -; Genomic_DNA. DR EMBL; HQ205641; ADP91396.1; -; Genomic_DNA. DR EMBL; HQ205642; ADP91400.1; -; Genomic_DNA. DR EMBL; HQ205643; ADP91404.1; -; Genomic_DNA. DR EMBL; HQ205644; ADP91408.1; -; Genomic_DNA. DR EMBL; HQ205645; ADP91412.1; -; Genomic_DNA. DR EMBL; HQ205646; ADP91416.1; -; Genomic_DNA. DR EMBL; HQ205647; ADP91420.1; -; Genomic_DNA. DR EMBL; HQ205648; ADP91424.1; -; Genomic_DNA. DR EMBL; HQ205649; ADP91428.1; -; Genomic_DNA. DR EMBL; HQ205650; ADP91432.1; -; Genomic_DNA. DR EMBL; HQ205651; ADP91436.1; -; Genomic_DNA. DR EMBL; HQ205652; ADP91440.1; -; Genomic_DNA. DR EMBL; HQ205653; ADP91444.1; -; Genomic_DNA. DR EMBL; HQ205654; ADP91448.1; -; Genomic_DNA. DR EMBL; HQ205655; ADP91452.1; -; Genomic_DNA. DR EMBL; HQ205656; ADP91456.1; -; Genomic_DNA. DR EMBL; HQ205657; ADP91460.1; -; Genomic_DNA. DR EMBL; HQ205658; ADP91464.1; -; Genomic_DNA. DR EMBL; HQ205659; ADP91468.1; -; Genomic_DNA. DR EMBL; HQ205660; ADP91472.1; -; Genomic_DNA. DR EMBL; HQ205661; ADP91476.1; -; Genomic_DNA. DR EMBL; HQ205662; ADP91480.1; -; Genomic_DNA. DR EMBL; HQ205663; ADP91484.1; -; Genomic_DNA. DR EMBL; HQ205664; ADP91488.1; -; Genomic_DNA. DR EMBL; HQ205665; ADP91492.1; -; Genomic_DNA. DR RefSeq; NP_004400.4; NM_004409.4. DR AlphaFoldDB; E5KR06; -. DR SMR; E5KR06; -. DR Antibodypedia; 2044; 319 antibodies from 30 providers. DR DNASU; 1760; -. DR GeneID; 1760; -. DR KEGG; hsa:1760; -. DR CTD; 1760; -. DR VEuPathDB; HostDB:ENSG00000104936; -. DR OMA; YFEFPPG; -. DR OrthoDB; 988261at2759; -. DR BioGRID-ORCS; 1760; 17 hits in 1192 CRISPR screens. DR GenomeRNAi; 1760; -. DR ExpressionAtlas; E5KR06; baseline and differential. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:Ensembl. DR GO; GO:0006998; P:nuclear envelope organization; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0014853; P:regulation of excitatory postsynaptic membrane potential involved in skeletal muscle contraction; IEA:Ensembl. DR GO; GO:0008016; P:regulation of heart contraction; IEA:Ensembl. DR GO; GO:0010830; P:regulation of myotube differentiation; IEA:Ensembl. DR GO; GO:0014722; P:regulation of skeletal muscle contraction by calcium ion signaling; IEA:Ensembl. DR GO; GO:0002028; P:regulation of sodium ion transport; IEA:Ensembl. DR GO; GO:0051823; P:regulation of synapse structural plasticity; IEA:Ensembl. DR CDD; cd05597; STKc_DMPK_like; 1. DR Gene3D; 1.20.5.340; -; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR22988:SF72; LOW QUALITY PROTEIN: MYOTONIN-PROTEIN KINASE; 1. DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1. DR Pfam; PF08826; DMPK_coil; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADP91336.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 71..339 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 340..415 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51285" FT COILED 457..530 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 100 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 629 AA; 69385 MW; 46783ED4AE65B493 CRC64; MSAEVRLRRL QQLVLDPGFL GLEPLLDLLL GVHQELGASE LAQDKYVADF LQWAEPIVVR LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR GEVSCFREER DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE MARFYLAEIV MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV AVGTPDYLSP EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI VHYKEHLSLP LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS VPPFTPDFEG ATDTCNFDLV EDGLTAMVSG GGETLSDIRE GAPLGVHLPF VGYSYSCMAL RDSEVPGPTP MELEAEQLLE PHVQAPSLEP SVSPQDETAE VAVPAAVPAA EAEAEVTLRE LQEALEEEVL TRQSLSREME AIRTDNQNFA SQLREAEARN RDLEAHVRQL QERMELLQAE GATAVTGVPS PRATDPPSHL DGPPAVAVGQ CPLVGPGPMH RRHLLLPARV PRPGLSEALS LLLFAVVLSR AAALGCIGLV AHAGQLTAVW RRPGAARAP //