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 10-FEB-2009, entry version 16. 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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- PTM: Phosphorylated on Ser-13 in mitosis (By similarity). 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. 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 IPI; IPI00695261; -. DR RefSeq; NP_001091041.1; -. DR UniGene; Bt.964; -. DR Ensembl; ENSBTAG00000007121; Bos taurus. DR GeneID; 504652; -. DR KEGG; bta:504652; -. DR BRENDA; 2.7.1.21; 251. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004797; F:thymidine kinase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR InterPro; IPR001267; TK_cell. DR PANTHER; PTHR11441; TK_cell; 1. DR Pfam; PF00265; TK; 1. DR PIRSF; PIRSF035805; TK_cell; 1. DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1. PE 2: Evidence at transcript level; KW ATP-binding; Cytoplasm; DNA synthesis; Kinase; Nucleotide-binding; KW Phosphoprotein; Transferase. FT CHAIN 1 238 Thymidine kinase, cytosolic. FT /FTId=PRO_0000322129. FT NP_BIND 26 33 ATP (Probable). FT MOD_RES 13 13 Phosphoserine (By similarity). 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 //