ID E9PPA5_HUMAN Unreviewed; 192 AA. AC E9PPA5; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 2. DT 27-MAR-2024, entry version 73. 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:ENSP00000434646.2}; 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:ENSP00000434646.2, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000434646.2, 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:ENSP00000434646.2} 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 --------------------------------------------------------------------------- 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; E9PPA5; -. DR SMR; E9PPA5; -. DR MassIVE; E9PPA5; -. DR PeptideAtlas; E9PPA5; -. DR ProteomicsDB; 22661; -. DR Antibodypedia; 3671; 2113 antibodies from 48 providers. DR Ensembl; ENST00000532669.5; ENSP00000434646.2; ENSG00000149554.15. DR UCSC; uc058ivs.1; human. DR HGNC; HGNC:1925; CHEK1. DR VEuPathDB; HostDB:ENSG00000149554; -. DR GeneTree; ENSGT00940000159682; -. 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; E9PPA5; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. 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; 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; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Proteomics identification {ECO:0007829|EPD:E9PPA5, KW ECO:0007829|MaxQB:E9PPA5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 1..186 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT NON_TER 192 FT /evidence="ECO:0000313|Ensembl:ENSP00000434646.2" SQ SEQUENCE 192 AA; 22228 MW; AF03415DCD11B2E9 CRC64; MAVPFVEDWD LVQTLGEEPD IGMPEPDAQR FFHQLMAGVV YLHGIGITHR DIKPENLLLD ERDNLKISDF GLATVFRYNN RERLLNKMCG TLPYVAPELL KRREFHAEPV DVWSCGIVLT AMLAGELPWD QPSDSCQEYS DWKEKKTYLN PWKKIDSAPL ALLHKILVEN PSARITIPDI KKDRWYNKPL KK //