KTHY_MOUSE
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 03-AUG-2022, entry version 159.
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 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; 2.
DR STRING; 10090.ENSMUSP00000027503; -.
DR iPTMnet; P97930; -.
DR PhosphoSitePlus; P97930; -.
DR EPD; P97930; -.
DR MaxQB; P97930; -.
DR PaxDb; P97930; -.
DR PeptideAtlas; P97930; -.
DR PRIDE; P97930; -.
DR ProteomicsDB; 289992; -. [P97930-1]
DR ProteomicsDB; 289993; -. [P97930-2]
DR Antibodypedia; 34572; 467 antibodies from 30 providers.
DR DNASU; 21915; -.
DR Ensembl; ENSMUST00000027503; ENSMUSP00000027503; ENSMUSG00000026281. [P97930-1]
DR Ensembl; ENSMUST00000112890; ENSMUSP00000108511; ENSMUSG00000026281. [P97930-2]
DR GeneID; 21915; -.
DR KEGG; mmu:21915; -.
DR UCSC; uc007cek.2; mouse. [P97930-1]
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; CYAPERG; -.
DR OrthoDB; 1259751at2759; -.
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 74 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 275 other tissues.
DR ExpressionAtlas; P97930; baseline and differential.
DR Genevisible; P97930; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
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:0009041; F:uridylate kinase activity; IBA:GO_Central.
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 Gene3D; 3.40.50.300; -; 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 Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
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
