ID   KTHY_MOUSE              Reviewed;         212 AA.
AC   P97930; Q8C2L0; Q8K2S2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=Thymidylate kinase;
DE            EC=2.7.4.9 {ECO:0000305|PubMed:8845311};
DE   AltName: Full=dTMP kinase;
GN   Name=Dtymk; Synonyms=Tmk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP   ACTIVITY, AND PATHWAY.
RC   STRAIN=BALB/cJ;
RX   PubMed=8845311;
RA   Liang P., Averboukh L., Zhu W., Haley T., Pardee A.B.;
RT   "Molecular characterization of the murine thymidylate kinase gene.";
RL   Cell Growth Differ. 6:1333-1338(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the phosphorylation of thymidine monophosphate
CC       (dTMP) to thymidine diphosphate (dTDP), the immediate precursor for the
CC       DNA building block dTTP, with ATP as the preferred phosphoryl donor in
CC       the presence of Mg(2+). {ECO:0000305|PubMed:8845311}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC         ChEBI:CHEBI:456216; EC=2.7.4.9;
CC         Evidence={ECO:0000305|PubMed:8845311};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P23919};
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC       {ECO:0000305|PubMed:8845311}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P23919}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=P97930-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P97930-2; Sequence=VSP_003029;
CC   -!- DEVELOPMENTAL STAGE: Very low mRNA levels in the quiescent cells. As
CC       cells exit from G0 to G1 phase, the expression levels gradually
CC       increase. {ECO:0000269|PubMed:8845311}.
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR   EMBL; S82852; AAB46837.1; -; mRNA.
DR   EMBL; S82853; AAB46838.1; -; mRNA.
DR   EMBL; AK088416; BAC40343.1; -; mRNA.
DR   EMBL; BC030178; AAH30178.1; -; mRNA.
DR   CCDS; CCDS35672.1; -. [P97930-2]
DR   CCDS; CCDS48329.1; -. [P97930-1]
DR   RefSeq; NP_001099137.1; NM_001105667.1. [P97930-1]
DR   AlphaFoldDB; P97930; -.
DR   SMR; P97930; -.
DR   BioGRID; 204232; 3.
DR   STRING; 10090.ENSMUSP00000027503; -.
DR   iPTMnet; P97930; -.
DR   PhosphoSitePlus; P97930; -.
DR   SwissPalm; P97930; -.
DR   EPD; P97930; -.
DR   MaxQB; P97930; -.
DR   PaxDb; 10090-ENSMUSP00000027503; -.
DR   PeptideAtlas; P97930; -.
DR   ProteomicsDB; 289992; -. [P97930-1]
DR   ProteomicsDB; 289993; -. [P97930-2]
DR   Pumba; P97930; -.
DR   Antibodypedia; 34572; 537 antibodies from 30 providers.
DR   DNASU; 21915; -.
DR   Ensembl; ENSMUST00000027503.14; ENSMUSP00000027503.8; ENSMUSG00000026281.16. [P97930-1]
DR   Ensembl; ENSMUST00000112890.3; ENSMUSP00000108511.3; ENSMUSG00000026281.16. [P97930-2]
DR   GeneID; 21915; -.
DR   KEGG; mmu:21915; -.
DR   UCSC; uc007cek.2; mouse. [P97930-1]
DR   AGR; MGI:108396; -.
DR   CTD; 1841; -.
DR   MGI; MGI:108396; Dtymk.
DR   VEuPathDB; HostDB:ENSMUSG00000026281; -.
DR   eggNOG; KOG3327; Eukaryota.
DR   GeneTree; ENSGT00940000154030; -.
DR   HOGENOM; CLU_049131_3_3_1; -.
DR   InParanoid; P97930; -.
DR   OMA; YWHQFDA; -.
DR   OrthoDB; 5473102at2759; -.
DR   PhylomeDB; P97930; -.
DR   TreeFam; TF324638; -.
DR   Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR   SABIO-RK; P97930; -.
DR   UniPathway; UPA00575; -.
DR   BioGRID-ORCS; 21915; 29 hits in 78 CRISPR screens.
DR   ChiTaRS; Dtymk; mouse.
DR   PRO; PR:P97930; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P97930; Protein.
DR   Bgee; ENSMUSG00000026281; Expressed in urogenital fold and 278 other cell types or tissues.
DR   ExpressionAtlas; P97930; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0004798; F:thymidylate kinase activity; IDA:MGI.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IDA:MGI.
DR   GO; GO:0006235; P:dTTP biosynthetic process; ISO:MGI.
DR   GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IDA:MGI.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0046105; P:thymidine biosynthetic process; ISO:MGI.
DR   CDD; cd01672; TMPK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   NCBIfam; TIGR00041; DTMP_kinase; 1.
DR   PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR   PANTHER; PTHR10344:SF1; THYMIDYLATE KINASE; 1.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
DR   Genevisible; P97930; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Kinase;
KW   Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P23919"
FT   CHAIN           2..212
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_0000155211"
FT   REGION          133..157
FT                   /note="LID"
FT                   /evidence="ECO:0000250|UniProtKB:P23919"
FT   BINDING         16..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P23919"
FT   BINDING         97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P23919"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P23919"
FT   BINDING         192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P23919"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P23919"
FT   VAR_SEQ         81..212
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8845311"
FT                   /id="VSP_003029"
FT   CONFLICT        151
FT                   /note="Y -> N (in Ref. 2; BAC40343)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183..212
FT                   /note="SIEEVHKEIRAHSEDAIRNAAQRPLGELWK -> RTPSETLHRGHWGSYGNK
FT                   SASIANTIFWFCKRLVEGSHLYTISRS (in Ref. 1; AAB46838)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   212 AA;  23915 MW;  2F9BC1770DE5902B CRC64;
     MASRRGALIV LEGVDRAGKT TQGLKLVTAL CASGHRAELL RFPERSTEIG KLLNSYLEKK
     TELEDHSVHL LFSANRWEQV PLIKAKLNQG VTLVLDRYAF SGVAFTGAKE NFSLDWCKQP
     DVGLPKPDLI LFLQLQLLDA AARGEFGLER YETGTFQKQV LLCFQQLMEE KNLNWKVVDA
     SKSIEEVHKE IRAHSEDAIR NAAQRPLGEL WK
//