Full text data of DTYMK
DTYMK
(CDC8, TMPK, TYMK)
[Confidence: low (only semi-automatic identification from reviews)]
Thymidylate kinase; 2.7.4.9 (dTMP kinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Thymidylate kinase; 2.7.4.9 (dTMP kinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P23919
ID KTHY_HUMAN Reviewed; 212 AA.
AC P23919; Q6FGX1; Q9BUX4;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-DEC-2004, sequence version 4.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Thymidylate kinase;
DE EC=2.7.4.9;
DE AltName: Full=dTMP kinase;
GN Name=DTYMK; Synonyms=CDC8, TMPK, TYMK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2017365; DOI=10.1093/nar/19.4.823;
RA Su J.Y., Sclafani R.A.;
RT "Molecular cloning and expression of the human deoxythymidylate kinase
RT gene in yeast.";
RL Nucleic Acids Res. 19:823-827(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8024690; DOI=10.1089/dna.1994.13.461;
RA Huang S.H., Tang A., Drisco B., Zhang S.Q., Seeger R., Li C., Jong A.;
RT "Human dTMP kinase: gene expression and enzymatic activity coinciding
RT with cell cycle progression and cell growth.";
RL DNA Cell Biol. 13:461-471(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=12614151; DOI=10.1021/bi027302t;
RA Ostermann N., Segura-Pena D., Meier C., Veit T., Monnerjahn C.,
RA Konrad M., Lavie A.;
RT "Structures of human thymidylate kinase in complex with prodrugs:
RT implications for the structure-based design of novel compounds.";
RL Biochemistry 42:2568-2577(2003).
CC -!- FUNCTION: Catalyzes the conversion of dTMP to dTDP.
CC -!- CATALYTIC ACTIVITY: ATP + dTMP = ADP + dTDP.
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X54729; CAA38528.1; -; mRNA.
DR EMBL; L16991; AAA21719.1; -; mRNA.
DR EMBL; CR541986; CAG46783.1; -; mRNA.
DR EMBL; BC001827; AAH01827.1; -; mRNA.
DR PIR; S26845; S26845.
DR RefSeq; NP_036277.2; NM_012145.3.
DR UniGene; Hs.471873; -.
DR PDB; 1E2D; X-ray; 1.65 A; A=1-212.
DR PDB; 1E2E; X-ray; 2.00 A; A=1-212.
DR PDB; 1E2F; X-ray; 1.60 A; A=1-212.
DR PDB; 1E2G; X-ray; 1.70 A; A=1-212.
DR PDB; 1E2Q; X-ray; 1.70 A; A=1-212.
DR PDB; 1E98; X-ray; 1.90 A; A=1-212.
DR PDB; 1E99; X-ray; 1.80 A; A=1-212.
DR PDB; 1E9A; X-ray; 1.60 A; A=1-212.
DR PDB; 1E9B; X-ray; 1.70 A; A=1-212.
DR PDB; 1E9C; X-ray; 1.60 A; A=1-212.
DR PDB; 1E9D; X-ray; 1.70 A; A=1-212.
DR PDB; 1E9E; X-ray; 1.60 A; A=1-212.
DR PDB; 1E9F; X-ray; 1.90 A; A=1-212.
DR PDB; 1NMX; X-ray; 1.70 A; A=1-212.
DR PDB; 1NMY; X-ray; 1.60 A; A=4-212.
DR PDB; 1NMZ; X-ray; 1.75 A; A=1-212.
DR PDB; 1NN0; X-ray; 1.60 A; A=1-212.
DR PDB; 1NN1; X-ray; 1.90 A; A=1-212.
DR PDB; 1NN3; X-ray; 1.55 A; A=1-212.
DR PDB; 1NN5; X-ray; 1.50 A; A=1-212.
DR PDB; 2XX3; X-ray; 2.00 A; A=1-212.
DR PDBsum; 1E2D; -.
DR PDBsum; 1E2E; -.
DR PDBsum; 1E2F; -.
DR PDBsum; 1E2G; -.
DR PDBsum; 1E2Q; -.
DR PDBsum; 1E98; -.
DR PDBsum; 1E99; -.
DR PDBsum; 1E9A; -.
DR PDBsum; 1E9B; -.
DR PDBsum; 1E9C; -.
DR PDBsum; 1E9D; -.
DR PDBsum; 1E9E; -.
DR PDBsum; 1E9F; -.
DR PDBsum; 1NMX; -.
DR PDBsum; 1NMY; -.
DR PDBsum; 1NMZ; -.
DR PDBsum; 1NN0; -.
DR PDBsum; 1NN1; -.
DR PDBsum; 1NN3; -.
DR PDBsum; 1NN5; -.
DR PDBsum; 2XX3; -.
DR ProteinModelPortal; P23919; -.
DR SMR; P23919; 4-212.
DR IntAct; P23919; 2.
DR MINT; MINT-3010142; -.
DR STRING; 9606.ENSP00000304802; -.
DR BindingDB; P23919; -.
DR ChEMBL; CHEMBL4388; -.
DR PhosphoSite; P23919; -.
DR DMDM; 56405325; -.
DR PaxDb; P23919; -.
DR PRIDE; P23919; -.
DR DNASU; 1841; -.
DR Ensembl; ENST00000305784; ENSP00000304802; ENSG00000168393.
DR GeneID; 1841; -.
DR KEGG; hsa:1841; -.
DR UCSC; uc002wbz.2; human.
DR CTD; 1841; -.
DR GeneCards; GC02M242634; -.
DR H-InvDB; HIX0161852; -.
DR HGNC; HGNC:3061; DTYMK.
DR HPA; HPA042593; -.
DR HPA; HPA042719; -.
DR MIM; 188345; gene.
DR neXtProt; NX_P23919; -.
DR PharmGKB; PA150; -.
DR eggNOG; COG0125; -.
DR HOGENOM; HOG000229079; -.
DR HOVERGEN; HBG051418; -.
DR InParanoid; P23919; -.
DR KO; K00943; -.
DR OMA; GKMIDSY; -.
DR OrthoDB; EOG7WQ7T8; -.
DR PhylomeDB; P23919; -.
DR BioCyc; MetaCyc:HS11384-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P23919; -.
DR UniPathway; UPA00575; -.
DR EvolutionaryTrace; P23919; -.
DR GeneWiki; DTYMK; -.
DR GenomeRNAi; 1841; -.
DR NextBio; 7537; -.
DR PRO; PR:P23919; -.
DR ArrayExpress; P23919; -.
DR Bgee; P23919; -.
DR CleanEx; HS_DTYMK; -.
DR Genevestigator; P23919; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050145; F:nucleoside phosphate kinase activity; EXP:Reactome.
DR GO; GO:0004798; F:thymidylate kinase activity; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; TAS:ProtInc.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:Ensembl.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen stimulus; IEA:Ensembl.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR018095; Thymidylate_kin_CS.
DR InterPro; IPR018094; Thymidylate_kinase.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Complete proteome; Kinase;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 212 Thymidylate kinase.
FT /FTId=PRO_0000155210.
FT NP_BIND 13 20 ATP (Probable).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 169 169 N6-acetyllysine.
FT CONFLICT 3 3 A -> P (in Ref. 3; CAG46783).
FT CONFLICT 31 37 CAAGHRA -> SRGPPP (in Ref. 1; CAA38528).
FT CONFLICT 58 58 Q -> K (in Ref. 2; AAA21719).
FT CONFLICT 68 68 V -> A (in Ref. 3; CAG46783).
FT CONFLICT 183 184 SI -> RL (in Ref. 1; CAA38528).
FT CONFLICT 190 191 DI -> EL (in Ref. 1 and 2).
FT STRAND 8 14
FT HELIX 19 32
FT STRAND 37 43
FT HELIX 48 57
FT HELIX 65 77
FT HELIX 80 88
FT STRAND 92 97
FT HELIX 99 107
FT HELIX 114 118
FT HELIX 119 121
FT STRAND 124 126
FT STRAND 128 134
FT HELIX 137 142
FT HELIX 149 151
FT HELIX 154 167
FT STRAND 171 173
FT STRAND 175 179
FT HELIX 184 201
FT HELIX 202 204
SQ SEQUENCE 212 AA; 23819 MW; A52876625B3621B1 CRC64;
MAARRGALIV LEGVDRAGKS TQSRKLVEAL CAAGHRAELL RFPERSTEIG KLLSSYLQKK
SDVEDHSVHL LFSANRWEQV PLIKEKLSQG VTLVVDRYAF SGVAFTGAKE NFSLDWCKQP
DVGLPKPDLV LFLQLQLADA AKRGAFGHER YENGAFQERA LRCFHQLMKD TTLNWKMVDA
SKSIEAVHED IRVLSEDAIR TATEKPLGEL WK
//
ID KTHY_HUMAN Reviewed; 212 AA.
AC P23919; Q6FGX1; Q9BUX4;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-DEC-2004, sequence version 4.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Thymidylate kinase;
DE EC=2.7.4.9;
DE AltName: Full=dTMP kinase;
GN Name=DTYMK; Synonyms=CDC8, TMPK, TYMK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2017365; DOI=10.1093/nar/19.4.823;
RA Su J.Y., Sclafani R.A.;
RT "Molecular cloning and expression of the human deoxythymidylate kinase
RT gene in yeast.";
RL Nucleic Acids Res. 19:823-827(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8024690; DOI=10.1089/dna.1994.13.461;
RA Huang S.H., Tang A., Drisco B., Zhang S.Q., Seeger R., Li C., Jong A.;
RT "Human dTMP kinase: gene expression and enzymatic activity coinciding
RT with cell cycle progression and cell growth.";
RL DNA Cell Biol. 13:461-471(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=12614151; DOI=10.1021/bi027302t;
RA Ostermann N., Segura-Pena D., Meier C., Veit T., Monnerjahn C.,
RA Konrad M., Lavie A.;
RT "Structures of human thymidylate kinase in complex with prodrugs:
RT implications for the structure-based design of novel compounds.";
RL Biochemistry 42:2568-2577(2003).
CC -!- FUNCTION: Catalyzes the conversion of dTMP to dTDP.
CC -!- CATALYTIC ACTIVITY: ATP + dTMP = ADP + dTDP.
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X54729; CAA38528.1; -; mRNA.
DR EMBL; L16991; AAA21719.1; -; mRNA.
DR EMBL; CR541986; CAG46783.1; -; mRNA.
DR EMBL; BC001827; AAH01827.1; -; mRNA.
DR PIR; S26845; S26845.
DR RefSeq; NP_036277.2; NM_012145.3.
DR UniGene; Hs.471873; -.
DR PDB; 1E2D; X-ray; 1.65 A; A=1-212.
DR PDB; 1E2E; X-ray; 2.00 A; A=1-212.
DR PDB; 1E2F; X-ray; 1.60 A; A=1-212.
DR PDB; 1E2G; X-ray; 1.70 A; A=1-212.
DR PDB; 1E2Q; X-ray; 1.70 A; A=1-212.
DR PDB; 1E98; X-ray; 1.90 A; A=1-212.
DR PDB; 1E99; X-ray; 1.80 A; A=1-212.
DR PDB; 1E9A; X-ray; 1.60 A; A=1-212.
DR PDB; 1E9B; X-ray; 1.70 A; A=1-212.
DR PDB; 1E9C; X-ray; 1.60 A; A=1-212.
DR PDB; 1E9D; X-ray; 1.70 A; A=1-212.
DR PDB; 1E9E; X-ray; 1.60 A; A=1-212.
DR PDB; 1E9F; X-ray; 1.90 A; A=1-212.
DR PDB; 1NMX; X-ray; 1.70 A; A=1-212.
DR PDB; 1NMY; X-ray; 1.60 A; A=4-212.
DR PDB; 1NMZ; X-ray; 1.75 A; A=1-212.
DR PDB; 1NN0; X-ray; 1.60 A; A=1-212.
DR PDB; 1NN1; X-ray; 1.90 A; A=1-212.
DR PDB; 1NN3; X-ray; 1.55 A; A=1-212.
DR PDB; 1NN5; X-ray; 1.50 A; A=1-212.
DR PDB; 2XX3; X-ray; 2.00 A; A=1-212.
DR PDBsum; 1E2D; -.
DR PDBsum; 1E2E; -.
DR PDBsum; 1E2F; -.
DR PDBsum; 1E2G; -.
DR PDBsum; 1E2Q; -.
DR PDBsum; 1E98; -.
DR PDBsum; 1E99; -.
DR PDBsum; 1E9A; -.
DR PDBsum; 1E9B; -.
DR PDBsum; 1E9C; -.
DR PDBsum; 1E9D; -.
DR PDBsum; 1E9E; -.
DR PDBsum; 1E9F; -.
DR PDBsum; 1NMX; -.
DR PDBsum; 1NMY; -.
DR PDBsum; 1NMZ; -.
DR PDBsum; 1NN0; -.
DR PDBsum; 1NN1; -.
DR PDBsum; 1NN3; -.
DR PDBsum; 1NN5; -.
DR PDBsum; 2XX3; -.
DR ProteinModelPortal; P23919; -.
DR SMR; P23919; 4-212.
DR IntAct; P23919; 2.
DR MINT; MINT-3010142; -.
DR STRING; 9606.ENSP00000304802; -.
DR BindingDB; P23919; -.
DR ChEMBL; CHEMBL4388; -.
DR PhosphoSite; P23919; -.
DR DMDM; 56405325; -.
DR PaxDb; P23919; -.
DR PRIDE; P23919; -.
DR DNASU; 1841; -.
DR Ensembl; ENST00000305784; ENSP00000304802; ENSG00000168393.
DR GeneID; 1841; -.
DR KEGG; hsa:1841; -.
DR UCSC; uc002wbz.2; human.
DR CTD; 1841; -.
DR GeneCards; GC02M242634; -.
DR H-InvDB; HIX0161852; -.
DR HGNC; HGNC:3061; DTYMK.
DR HPA; HPA042593; -.
DR HPA; HPA042719; -.
DR MIM; 188345; gene.
DR neXtProt; NX_P23919; -.
DR PharmGKB; PA150; -.
DR eggNOG; COG0125; -.
DR HOGENOM; HOG000229079; -.
DR HOVERGEN; HBG051418; -.
DR InParanoid; P23919; -.
DR KO; K00943; -.
DR OMA; GKMIDSY; -.
DR OrthoDB; EOG7WQ7T8; -.
DR PhylomeDB; P23919; -.
DR BioCyc; MetaCyc:HS11384-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P23919; -.
DR UniPathway; UPA00575; -.
DR EvolutionaryTrace; P23919; -.
DR GeneWiki; DTYMK; -.
DR GenomeRNAi; 1841; -.
DR NextBio; 7537; -.
DR PRO; PR:P23919; -.
DR ArrayExpress; P23919; -.
DR Bgee; P23919; -.
DR CleanEx; HS_DTYMK; -.
DR Genevestigator; P23919; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050145; F:nucleoside phosphate kinase activity; EXP:Reactome.
DR GO; GO:0004798; F:thymidylate kinase activity; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; TAS:ProtInc.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:Ensembl.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen stimulus; IEA:Ensembl.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR018095; Thymidylate_kin_CS.
DR InterPro; IPR018094; Thymidylate_kinase.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Complete proteome; Kinase;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 212 Thymidylate kinase.
FT /FTId=PRO_0000155210.
FT NP_BIND 13 20 ATP (Probable).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 169 169 N6-acetyllysine.
FT CONFLICT 3 3 A -> P (in Ref. 3; CAG46783).
FT CONFLICT 31 37 CAAGHRA -> SRGPPP (in Ref. 1; CAA38528).
FT CONFLICT 58 58 Q -> K (in Ref. 2; AAA21719).
FT CONFLICT 68 68 V -> A (in Ref. 3; CAG46783).
FT CONFLICT 183 184 SI -> RL (in Ref. 1; CAA38528).
FT CONFLICT 190 191 DI -> EL (in Ref. 1 and 2).
FT STRAND 8 14
FT HELIX 19 32
FT STRAND 37 43
FT HELIX 48 57
FT HELIX 65 77
FT HELIX 80 88
FT STRAND 92 97
FT HELIX 99 107
FT HELIX 114 118
FT HELIX 119 121
FT STRAND 124 126
FT STRAND 128 134
FT HELIX 137 142
FT HELIX 149 151
FT HELIX 154 167
FT STRAND 171 173
FT STRAND 175 179
FT HELIX 184 201
FT HELIX 202 204
SQ SEQUENCE 212 AA; 23819 MW; A52876625B3621B1 CRC64;
MAARRGALIV LEGVDRAGKS TQSRKLVEAL CAAGHRAELL RFPERSTEIG KLLSSYLQKK
SDVEDHSVHL LFSANRWEQV PLIKEKLSQG VTLVVDRYAF SGVAFTGAKE NFSLDWCKQP
DVGLPKPDLV LFLQLQLADA AKRGAFGHER YENGAFQERA LRCFHQLMKD TTLNWKMVDA
SKSIEAVHED IRVLSEDAIR TATEKPLGEL WK
//
MIM
188345
*RECORD*
*FIELD* NO
188345
*FIELD* TI
*188345 DEOXYTHYMIDYLATE KINASE; DTYMK
;;THYMIDYLATE KINASE; TYMK;;
CDC8
*FIELD* TX
read moreThymidylate kinase (EC 2.7.4.9; ATP:dTMP phosphotransferase) catalyzes
the phosphorylation of dTMP to form dTDP in the dTTP synthesis pathway
for DNA synthesis. Knowledge of the essential function of dTMP kinase in
eukaryotes comes from the study of a cell cycle mutant, cdc8, in
Saccharomyces cerevisiae. The product of the cdc8 gene is involved in
the elongation step of S phase in cell cycle progression. Huang et al.
(1994) cloned the human thymidylate kinase gene by complementation with
the cdc8 mutation. The cDNA sequence revealed an open reading frame that
encodes a protein with a molecular weight of 23,806. Structural and
functional analyses suggested that the cDNA codes for authentic human
dTMP kinase. The mRNA levels and enzyme activities corresponded to cell
cycle progression and cell growth stages.
*FIELD* RF
1. Huang, S.; Tang, A.; Drisco, B.; Zhang, S. Q.; Seeger, R.; Li,
C.; Jong, A.: Human dTMP kinase: gene expression and enzymatic activity
coinciding with cell cycle progression and cell growth. DNA Cell
Biol. 13: 461-471, 1994.
*FIELD* CD
Victor A. McKusick: 6/17/1994
*FIELD* ED
carol: 02/01/1999
carol: 9/14/1994
jason: 6/17/1994
*RECORD*
*FIELD* NO
188345
*FIELD* TI
*188345 DEOXYTHYMIDYLATE KINASE; DTYMK
;;THYMIDYLATE KINASE; TYMK;;
CDC8
*FIELD* TX
read moreThymidylate kinase (EC 2.7.4.9; ATP:dTMP phosphotransferase) catalyzes
the phosphorylation of dTMP to form dTDP in the dTTP synthesis pathway
for DNA synthesis. Knowledge of the essential function of dTMP kinase in
eukaryotes comes from the study of a cell cycle mutant, cdc8, in
Saccharomyces cerevisiae. The product of the cdc8 gene is involved in
the elongation step of S phase in cell cycle progression. Huang et al.
(1994) cloned the human thymidylate kinase gene by complementation with
the cdc8 mutation. The cDNA sequence revealed an open reading frame that
encodes a protein with a molecular weight of 23,806. Structural and
functional analyses suggested that the cDNA codes for authentic human
dTMP kinase. The mRNA levels and enzyme activities corresponded to cell
cycle progression and cell growth stages.
*FIELD* RF
1. Huang, S.; Tang, A.; Drisco, B.; Zhang, S. Q.; Seeger, R.; Li,
C.; Jong, A.: Human dTMP kinase: gene expression and enzymatic activity
coinciding with cell cycle progression and cell growth. DNA Cell
Biol. 13: 461-471, 1994.
*FIELD* CD
Victor A. McKusick: 6/17/1994
*FIELD* ED
carol: 02/01/1999
carol: 9/14/1994
jason: 6/17/1994