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Database: UniProt/SWISS-PROT
Entry: KITH_RAT
LinkDB: KITH_RAT
Original site: KITH_RAT 
ID   KITH_RAT                Reviewed;         121 AA.
AC   P27158; Q6LAG4;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   23-MAY-2018, entry version 111.
DE   RecName: Full=Thymidine kinase, cytosolic;
DE            EC=2.7.1.21;
DE   Flags: Fragment;
GN   Name=Tk1; Synonyms=Tk-1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3479791; DOI=10.1073/pnas.84.23.8277;
RA   Murphy A.J.M., Efstratiadis A.;
RT   "Cloning vectors for expression of cDNA libraries in mammalian
RT   cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:8277-8281(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RC   STRAIN=Sprague-Dawley;
RA   Sauer M.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RC   TISSUE=Liver;
RX   PubMed=1777676; DOI=10.3109/10425179109039682;
RA   Arcot S., Traina-Dorge V.L., Deininger P.L.;
RT   "The rat thymidine kinase gene 5' region: evolution of a promoter.";
RL   DNA Seq. 2:129-131(1991).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC       phosphate.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-8306437, EBI-8306437;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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}.
DR   EMBL; M22642; AAA75560.1; -; mRNA.
DR   EMBL; Y17296; CAA76733.1; -; Genomic_DNA.
DR   EMBL; X54173; CAA38106.1; -; Genomic_DNA.
DR   PIR; A39968; A39968.
DR   RefSeq; NP_434687.1; NM_052800.1.
DR   UniGene; Rn.147549; -.
DR   UniGene; Rn.195325; -.
DR   UniGene; Rn.233805; -.
DR   ProteinModelPortal; P27158; -.
DR   SMR; P27158; -.
DR   MINT; P27158; -.
DR   STRING; 10116.ENSRNOP00000067459; -.
DR   BindingDB; P27158; -.
DR   ChEMBL; CHEMBL4022; -.
DR   PaxDb; P27158; -.
DR   PRIDE; P27158; -.
DR   GeneID; 24834; -.
DR   KEGG; rno:24834; -.
DR   CTD; 7083; -.
DR   RGD; 621014; Tk1.
DR   eggNOG; KOG3125; Eukaryota.
DR   eggNOG; COG1435; LUCA.
DR   HOVERGEN; HBG006215; -.
DR   InParanoid; P27158; -.
DR   KO; K00857; -.
DR   PhylomeDB; P27158; -.
DR   BRENDA; 2.7.1.21; 5301.
DR   SABIO-RK; P27158; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004797; F:thymidine kinase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0048565; P:digestive tract development; IEP:RGD.
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:0060138; P:fetal process involved in parturition; IEP:RGD.
DR   GO; GO:0001889; P:liver development; IEP:RGD.
DR   GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR   GO; GO:0051414; P:response to cortisol; IEP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR   GO; GO:0014856; P:skeletal muscle cell proliferation; IEP:RGD.
DR   GO; GO:0046104; P:thymidine metabolic process; IDA:RGD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
DR   PANTHER; PTHR11441; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm; DNA synthesis;
KW   Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P04183}.
FT   CHAIN         2   >121       Thymidine kinase, cytosolic.
FT                                /FTId=PRO_0000174950.
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   ACT_SITE     98     98       Proton acceptor. {ECO:0000255}.
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   NON_TER     121    121
SQ   SEQUENCE   121 AA;  13511 MW;  8330BDFD9CDA9EB0 CRC64;
     MSYINLPTVL PISPSKTRGQ IQVILGPMFS GKSTELMRRV RRFQIAQYKC LVIKYAKDTR
     YSNSFSTHDR NTMDALPACM LKDVAQEALG VAVIGIDEGQ FFPDIVDFCE TMANTGKTVI
     V
//
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