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 02-DEC-2020, entry version 81. 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; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC 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: CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21; 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 in CC cytosol and one in mitochondria. Activity of the cytosolic enzyme is CC high in proliferating cells and peaks during the S-phase of the cell CC 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 SMR; A5D7R8; -. DR STRING; 9913.ENSBTAP00000034599; -. DR PaxDb; A5D7R8; -. DR PRIDE; A5D7R8; -. DR GeneID; 504652; -. DR KEGG; bta:504652; -. DR CTD; 7083; -. DR eggNOG; KOG3125; Eukaryota. DR HOGENOM; CLU_064400_3_1_1; -. DR InParanoid; A5D7R8; -. DR OMA; GWLELIC; -. DR OrthoDB; 1413914at2759; -. DR TreeFam; TF314839; -. DR Reactome; R-BTA-73614; Pyrimidine salvage. DR Proteomes; UP000009136; Unplaced. DR Bgee; ENSBTAG00000007121; Expressed in conceptus and 19 other tissues. 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: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; Cytoplasm; DNA synthesis; Kinase; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P04183" FT CHAIN 2..238 FT /note="Thymidine kinase, cytosolic" FT /id="PRO_0000322129" FT NP_BIND 26..33 FT /note="ATP" FT /evidence="ECO:0000305" FT NP_BIND 58..60 FT /note="ATP" FT /evidence="ECO:0000250" FT NP_BIND 97..100 FT /note="ATP" FT /evidence="ECO:0000250" FT REGION 172..176 FT /note="Substrate binding" FT /evidence="ECO:0000250" FT ACT_SITE 98 FT /note="Proton acceptor" FT /evidence="ECO:0000255" FT METAL 153 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 156 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 185 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 188 FT /note="Zinc" FT /evidence="ECO:0000250" FT BINDING 128 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000250" FT BINDING 181 FT /note="Substrate" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P04183" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04183" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04183" FT MOD_RES 235 FT /note="Phosphoserine" FT /evidence="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 //