ID KITH_BOVIN Reviewed; 238 AA. AC A5D7R8; A7E3S3; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 05-OCT-2016, entry version 65. DE RecName: Full=Thymidine kinase, cytosolic; DE EC=2.7.1.21; GN Name=TK1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Fetal liver; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'- CC phosphate. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- PTM: Phosphorylated on Ser-13 in mitosis. {ECO:0000250}. CC -!- MISCELLANEOUS: Two forms have been identified in animal cells, one CC in cytosol and one in mitochondria. Activity of the cytosolic CC enzyme is high in proliferating cells and peaks during the S-phase CC of the cell cycle; it is very low in resting cells. CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ABS45010.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; BT030694; ABS45010.1; ALT_INIT; mRNA. DR EMBL; BC140658; AAI40659.1; -; mRNA. DR RefSeq; NP_001091041.1; NM_001097572.1. DR UniGene; Bt.964; -. DR ProteinModelPortal; A5D7R8; -. DR STRING; 9913.ENSBTAP00000034599; -. DR PaxDb; A5D7R8; -. DR PRIDE; A5D7R8; -. DR Ensembl; ENSBTAT00000034713; ENSBTAP00000034599; ENSBTAG00000007121. DR GeneID; 504652; -. DR KEGG; bta:504652; -. DR CTD; 7083; -. DR eggNOG; KOG3125; Eukaryota. DR eggNOG; COG1435; LUCA. DR GeneTree; ENSGT00390000011309; -. DR HOGENOM; HOG000076390; -. DR HOVERGEN; HBG006215; -. DR InParanoid; A5D7R8; -. DR KO; K00857; -. DR OMA; VITGPMY; -. DR OrthoDB; EOG091G0HZR; -. DR TreeFam; TF314839; -. DR Reactome; R-BTA-73614; Pyrimidine salvage reactions. DR Proteomes; UP000009136; Chromosome 19. DR Bgee; ENSBTAG00000007121; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004797; F:thymidine kinase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006259; P:DNA metabolic process; IBA:GO_Central. DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl. DR GO; GO:0046104; P:thymidine metabolic process; IBA:GO_Central. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001267; Thymidine_kinase. DR InterPro; IPR020633; Thymidine_kinase_CS. DR PANTHER; PTHR11441; PTHR11441; 1. DR Pfam; PF00265; TK; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1. PE 2: Evidence at transcript level; KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; DNA synthesis; KW Kinase; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase; Zinc. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P04183}. FT CHAIN 2 238 Thymidine kinase, cytosolic. FT /FTId=PRO_0000322129. FT NP_BIND 26 33 ATP. {ECO:0000305}. FT NP_BIND 58 60 ATP. {ECO:0000250}. FT NP_BIND 97 100 ATP. {ECO:0000250}. FT REGION 172 176 Substrate binding. {ECO:0000250}. FT ACT_SITE 98 98 Proton acceptor. {ECO:0000255}. FT METAL 153 153 Zinc. {ECO:0000250}. FT METAL 156 156 Zinc. {ECO:0000250}. FT METAL 185 185 Zinc. {ECO:0000250}. FT METAL 188 188 Zinc. {ECO:0000250}. FT BINDING 128 128 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 181 181 Substrate. {ECO:0000250}. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000250|UniProtKB:P04183}. FT MOD_RES 2 2 Phosphoserine. FT {ECO:0000250|UniProtKB:P04183}. FT MOD_RES 13 13 Phosphoserine. FT {ECO:0000250|UniProtKB:P04183}. FT MOD_RES 235 235 Phosphoserine. FT {ECO:0000250|UniProtKB:P04183}. SQ SEQUENCE 238 AA; 26377 MW; B9D720679A18C452 CRC64; MSCINLPNVL PGSPSKTRGQ IQVILGPMFS GKSTELMRRV RRFQVAQYKC LVIKYAKDTR YSSLFSTHDR NTMEALPACL LRDVIQDAQR VAVIGIDEGQ FFPDIVEFCE NMANSGKTVI VAALDGTFQR KAFGTILNLV PLAESVVKLT AVCMECFREA AYTKRLGVEK EVEVIGGADK YHSVCRLCYF KKASGQPAVL DSEENKENCP MTLGKPAEAP GVRKLFATHQ IWQCSQAN //