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Database: UniProt
Entry: A5D7R8
LinkDB: A5D7R8
Original site: A5D7R8 
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   13-FEB-2019, entry version 74.
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:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+);
CC         Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216;
CC         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
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};
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   SMR; 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   VGNC; VGNC:35884; TK1.
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; CAGLDQD; -.
DR   OrthoDB; 1413914at2759; -.
DR   TreeFam; TF314839; -.
DR   Reactome; R-BTA-73614; Pyrimidine salvage.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000007121; Expressed in 10 organ(s), highest expression level in colon.
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: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   PIRSF; PIRSF035805; TK_cell; 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
//
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