ID E9PJI4_HUMAN Unreviewed; 170 AA. AC E9PJI4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; DE Flags: Fragment; GN Name=CHEK1 {ECO:0000313|Ensembl:ENSP00000431815.1}; 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|Ensembl:ENSP00000431815.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000431815.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000431815.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. NIM1 subfamily. {ECO:0000256|ARBA:ARBA00010791}. 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; AP001132; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455559; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; E9PJI4; -. DR SMR; E9PJI4; -. DR MassIVE; E9PJI4; -. DR MaxQB; E9PJI4; -. DR PeptideAtlas; E9PJI4; -. DR ProteomicsDB; 21150; -. DR Antibodypedia; 3671; 2113 antibodies from 48 providers. DR Ensembl; ENST00000526937.5; ENSP00000431815.1; ENSG00000149554.15. DR UCSC; uc058ivu.1; human. DR HGNC; HGNC:1925; CHEK1. DR VEuPathDB; HostDB:ENSG00000149554; -. DR GeneTree; ENSGT00940000159682; -. DR OMA; GYTCKVG; -. DR ChiTaRS; CHEK1; human. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000149554; Expressed in secondary oocyte and 130 other cell types or tissues. DR ExpressionAtlas; E9PJI4; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1. DR PANTHER; PTHR24346:SF73; SERINE_THREONINE-PROTEIN KINASE CHK1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Cell cycle {ECO:0000256|ARBA:ARBA00023306}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Proteomics identification {ECO:0007829|EPD:E9PJI4, KW ECO:0007829|MaxQB:E9PJI4}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 9..170 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT NON_TER 170 FT /evidence="ECO:0000313|Ensembl:ENSP00000431815.1" SQ SEQUENCE 170 AA; 19531 MW; 5E816AA77265F720 CRC64; MAVPFVEDWD LVQTLGEGAY GEVQLAVNRV TEEAVAVKIV DMKRAVDCPE NIKKEICINK MLNHENVVKF YGHRREGNIQ YLFLEYCSGG ELFDRIEPDI GMPEPDAQRF FHQLMAGVVY LHGIGITHRD IKPENLLLDE RDNLKISDFG LATVFRYNNR ERLLNKMCGT //