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Database: UniProt
Entry: P04183
LinkDB: P04183
Original site: P04183 
ID   KITH_HUMAN              Reviewed;         234 AA.
AC   P04183; B2RC58; Q969V0; Q9UMG9;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   13-FEB-2019, entry version 196.
DE   RecName: Full=Thymidine kinase, cytosolic;
DE            EC=2.7.1.21;
GN   Name=TK1;
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=6549046; DOI=10.1128/MCB.4.11.2316;
RA   Bradshaw H.D. Jr., Deininger P.L.;
RT   "Human thymidine kinase gene: molecular cloning and nucleotide
RT   sequence of a cDNA expressible in mammalian cells.";
RL   Mol. Cell. Biol. 4:2316-2320(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3301530; DOI=10.1016/0378-1119(87)90053-9;
RA   Flemington E., Bradshaw H.D. Jr., Traina-Dorge V., Slagel V.,
RA   Deininger P.L.;
RT   "Sequence, structure and promoter characterization of the human
RT   thymidine kinase gene.";
RL   Gene 52:267-277(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymph, Skin, and Uterus;
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX   PubMed=3785218; DOI=10.1128/MCB.6.8.2903;
RA   Kreidberg J.A., Kelly T.J.;
RT   "Genetic analysis of the human thymidine kinase gene promoter.";
RL   Mol. Cell. Biol. 6:2903-2909(1986).
RN   [7]
RP   PHOSPHORYLATION AT SER-13.
RX   PubMed=9575153; DOI=10.1074/jbc.273.20.12095;
RA   Chang Z.F., Huang D.Y., Chi L.M.;
RT   "Serine 13 is the site of mitotic phosphorylation of human thymidine
RT   kinase.";
RL   J. Biol. Chem. 273:12095-12100(1998).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-231, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP   SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
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   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-13, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-193 IN COMPLEX WITH ZINC
RP   IONS AND TTP, AND SUBUNIT.
RX   PubMed=15611477; DOI=10.1073/pnas.0406332102;
RA   Welin M., Kosinska U., Mikkelsen N.E., Carnrot C., Zhu C., Wang L.,
RA   Eriksson S., Munch-Petersen B., Eklund H.;
RT   "Structures of thymidine kinase 1 of human and mycoplasmic origin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:17970-17975(2004).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 15-194 IN COMPLEX WITH ZINC
RP   IONS AND TTP.
RX   PubMed=15733844; DOI=10.1016/j.febslet.2005.01.034;
RA   Birringer M.S., Claus M.T., Folkers G., Kloer D.P., Schulz G.E.,
RA   Scapozza L.;
RT   "Structure of a type II thymidine kinase with bound dTTP.";
RL   FEBS Lett. 579:1376-1382(2005).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ZINC IONS;
RP   SUBSTRATE AND ATP ANALOG, AND SUBUNIT.
RX   PubMed=17407781; DOI=10.1016/j.jmb.2007.02.104;
RA   Segura-Pena D., Lutz S., Monnerjahn C., Konrad M., Lavie A.;
RT   "Binding of ATP to TK1-like enzymes is associated with a
RT   conformational change in the quaternary structure.";
RL   J. Mol. Biol. 369:129-141(2007).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-193 OF MUTANT SER-163,
RP   ZINC-BINDING SITES, AND MUTAGENESIS OF THR-163.
RX   PubMed=22385435; DOI=10.1111/j.1742-4658.2012.08554.x;
RA   Skovgaard T., Uhlin U., Munch-Petersen B.;
RT   "Comparative active-site mutation study of human and Caenorhabditis
RT   elegans thymidine kinase 1.";
RL   FEBS J. 279:1777-1787(2012).
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:0000269|PubMed:15611477,
CC       ECO:0000269|PubMed:15733844, ECO:0000269|PubMed:17407781}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-712550, EBI-712550;
CC       Q1RN33:MAGEA4; NbExp=3; IntAct=EBI-712550, EBI-10194128;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Phosphorylated on Ser-13 in mitosis.
CC       {ECO:0000269|PubMed:9575153}.
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; K02581; AAA61187.1; -; mRNA.
DR   EMBL; M15205; AAA61191.1; -; Genomic_DNA.
DR   EMBL; AK314950; BAG37455.1; -; mRNA.
DR   EMBL; BT006941; AAP35587.1; -; mRNA.
DR   EMBL; BC006484; AAH06484.1; -; mRNA.
DR   EMBL; BC007872; AAH07872.1; -; mRNA.
DR   EMBL; BC007986; AAH07986.1; -; mRNA.
DR   EMBL; M13643; AAA61189.1; -; Genomic_DNA.
DR   CCDS; CCDS11754.1; -.
DR   PIR; A27318; KIHUT.
DR   RefSeq; NP_003249.3; NM_003258.4.
DR   UniGene; Hs.515122; -.
DR   PDB; 1W4R; X-ray; 1.83 A; A/B/C/D/E/F/G/H=15-194.
DR   PDB; 1XBT; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-193.
DR   PDB; 2ORV; X-ray; 2.30 A; A/B=1-234.
DR   PDB; 2WVJ; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-193.
DR   PDBsum; 1W4R; -.
DR   PDBsum; 1XBT; -.
DR   PDBsum; 2ORV; -.
DR   PDBsum; 2WVJ; -.
DR   ProteinModelPortal; P04183; -.
DR   SMR; P04183; -.
DR   BioGrid; 112938; 178.
DR   IntAct; P04183; 162.
DR   MINT; P04183; -.
DR   STRING; 9606.ENSP00000301634; -.
DR   BindingDB; P04183; -.
DR   ChEMBL; CHEMBL2883; -.
DR   DrugBank; DB01692; Dithioerythritol.
DR   DrugBank; DB02452; Thymidine-5'-Triphosphate.
DR   DrugBank; DB00432; Trifluridine.
DR   DrugBank; DB00495; Zidovudine.
DR   iPTMnet; P04183; -.
DR   PhosphoSitePlus; P04183; -.
DR   BioMuta; TK1; -.
DR   DMDM; 23503074; -.
DR   EPD; P04183; -.
DR   jPOST; P04183; -.
DR   MaxQB; P04183; -.
DR   PaxDb; P04183; -.
DR   PeptideAtlas; P04183; -.
DR   PRIDE; P04183; -.
DR   ProteomicsDB; 51674; -.
DR   DNASU; 7083; -.
DR   Ensembl; ENST00000301634; ENSP00000301634; ENSG00000167900.
DR   GeneID; 7083; -.
DR   KEGG; hsa:7083; -.
DR   UCSC; uc002juw.3; human.
DR   CTD; 7083; -.
DR   DisGeNET; 7083; -.
DR   EuPathDB; HostDB:ENSG00000167900.11; -.
DR   GeneCards; TK1; -.
DR   HGNC; HGNC:11830; TK1.
DR   HPA; CAB004683; -.
DR   MIM; 188300; gene.
DR   neXtProt; NX_P04183; -.
DR   OpenTargets; ENSG00000167900; -.
DR   PharmGKB; PA352; -.
DR   eggNOG; KOG3125; Eukaryota.
DR   eggNOG; COG1435; LUCA.
DR   GeneTree; ENSGT00390000011309; -.
DR   HOGENOM; HOG000076390; -.
DR   HOVERGEN; HBG006215; -.
DR   InParanoid; P04183; -.
DR   KO; K00857; -.
DR   OrthoDB; 1413914at2759; -.
DR   PhylomeDB; P04183; -.
DR   TreeFam; TF314839; -.
DR   BioCyc; MetaCyc:HS09657-MONOMER; -.
DR   BRENDA; 2.7.1.21; 2681.
DR   Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
DR   Reactome; R-HSA-73614; Pyrimidine salvage.
DR   SABIO-RK; P04183; -.
DR   SIGNOR; P04183; -.
DR   ChiTaRS; TK1; human.
DR   EvolutionaryTrace; P04183; -.
DR   GeneWiki; Thymidine_kinase_1; -.
DR   GenomeRNAi; 7083; -.
DR   PRO; PR:P04183; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000167900; Expressed in 146 organ(s), highest expression level in endometrium epithelium.
DR   ExpressionAtlas; P04183; baseline and differential.
DR   Genevisible; P04183; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019206; F:nucleoside kinase activity; EXP:Reactome.
DR   GO; GO:0004797; F:thymidine kinase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IDA: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:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR   GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
DR   GO; GO:0043097; P:pyrimidine nucleoside salvage; TAS:Reactome.
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   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW   DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:22223895,
FT                                ECO:0000244|PubMed:22814378}.
FT   CHAIN         2    234       Thymidine kinase, cytosolic.
FT                                /FTId=PRO_0000174948.
FT   NP_BIND      26     33       ATP. {ECO:0000244|PDB:1W4R,
FT                                ECO:0000244|PDB:1XBT,
FT                                ECO:0000244|PDB:2ORV,
FT                                ECO:0000244|PDB:2WVJ,
FT                                ECO:0000269|PubMed:15611477,
FT                                ECO:0000269|PubMed:15733844,
FT                                ECO:0000269|PubMed:17407781,
FT                                ECO:0000269|PubMed:22385435}.
FT   NP_BIND      58     60       ATP. {ECO:0000244|PDB:1W4R,
FT                                ECO:0000244|PDB:1XBT,
FT                                ECO:0000244|PDB:2WVJ,
FT                                ECO:0000269|PubMed:15611477,
FT                                ECO:0000269|PubMed:15733844,
FT                                ECO:0000269|PubMed:22385435}.
FT   NP_BIND      97    100       ATP. {ECO:0000244|PDB:1W4R,
FT                                ECO:0000244|PDB:2WVJ,
FT                                ECO:0000269|PubMed:15733844,
FT                                ECO:0000269|PubMed:22385435}.
FT   REGION      172    176       Substrate binding. {ECO:0000244|PDB:1W4R,
FT                                ECO:0000244|PDB:1XBT,
FT                                ECO:0000244|PDB:2WVJ,
FT                                ECO:0000269|PubMed:15611477,
FT                                ECO:0000269|PubMed:15733844,
FT                                ECO:0000269|PubMed:22385435}.
FT   ACT_SITE     98     98       Proton acceptor. {ECO:0000255}.
FT   METAL       153    153       Zinc. {ECO:0000244|PDB:1W4R,
FT                                ECO:0000244|PDB:1XBT,
FT                                ECO:0000244|PDB:2ORV,
FT                                ECO:0000244|PDB:2WVJ,
FT                                ECO:0000269|PubMed:15611477,
FT                                ECO:0000269|PubMed:15733844,
FT                                ECO:0000269|PubMed:17407781,
FT                                ECO:0000269|PubMed:22385435}.
FT   METAL       156    156       Zinc. {ECO:0000244|PDB:1W4R,
FT                                ECO:0000244|PDB:1XBT,
FT                                ECO:0000244|PDB:2ORV,
FT                                ECO:0000244|PDB:2WVJ,
FT                                ECO:0000269|PubMed:15611477,
FT                                ECO:0000269|PubMed:15733844,
FT                                ECO:0000269|PubMed:17407781,
FT                                ECO:0000269|PubMed:22385435}.
FT   METAL       185    185       Zinc. {ECO:0000244|PDB:1W4R,
FT                                ECO:0000244|PDB:1XBT,
FT                                ECO:0000244|PDB:2ORV,
FT                                ECO:0000244|PDB:2WVJ,
FT                                ECO:0000269|PubMed:15611477,
FT                                ECO:0000269|PubMed:15733844,
FT                                ECO:0000269|PubMed:17407781,
FT                                ECO:0000269|PubMed:22385435}.
FT   METAL       188    188       Zinc. {ECO:0000244|PDB:1W4R,
FT                                ECO:0000244|PDB:1XBT,
FT                                ECO:0000244|PDB:2ORV,
FT                                ECO:0000244|PDB:2WVJ,
FT                                ECO:0000269|PubMed:15611477,
FT                                ECO:0000269|PubMed:15733844,
FT                                ECO:0000269|PubMed:17407781,
FT                                ECO:0000269|PubMed:22385435}.
FT   BINDING     128    128       Substrate; via amide nitrogen.
FT                                {ECO:0000244|PDB:1W4R,
FT                                ECO:0000244|PDB:1XBT,
FT                                ECO:0000244|PDB:2ORV,
FT                                ECO:0000244|PDB:2WVJ,
FT                                ECO:0000269|PubMed:15611477,
FT                                ECO:0000269|PubMed:15733844,
FT                                ECO:0000269|PubMed:17407781,
FT                                ECO:0000269|PubMed:22385435}.
FT   BINDING     181    181       Substrate. {ECO:0000244|PDB:1W4R,
FT                                ECO:0000244|PDB:1XBT,
FT                                ECO:0000244|PDB:2ORV,
FT                                ECO:0000269|PubMed:15611477,
FT                                ECO:0000269|PubMed:15733844,
FT                                ECO:0000269|PubMed:17407781,
FT                                ECO:0000269|PubMed:22385435}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:22223895,
FT                                ECO:0000244|PubMed:22814378}.
FT   MOD_RES       2      2       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163,
FT                                ECO:0000269|PubMed:9575153}.
FT   MOD_RES     231    231       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:20068231}.
FT   MUTAGEN     163    163       T->S: 140-fold lower K(m) for AZT.
FT                                {ECO:0000269|PubMed:22385435}.
FT   CONFLICT    106    106       V -> M (in Ref. 1; AAA61187 and 2;
FT                                AAA61191). {ECO:0000305}.
FT   STRAND       20     26       {ECO:0000244|PDB:1W4R}.
FT   HELIX        32     45       {ECO:0000244|PDB:1W4R}.
FT   STRAND       50     55       {ECO:0000244|PDB:1W4R}.
FT   HELIX        61     63       {ECO:0000244|PDB:1W4R}.
FT   HELIX        67     72       {ECO:0000244|PDB:1W4R}.
FT   STRAND       73     80       {ECO:0000244|PDB:1W4R}.
FT   HELIX        81     84       {ECO:0000244|PDB:1W4R}.
FT   HELIX        85     89       {ECO:0000244|PDB:1W4R}.
FT   STRAND       92     98       {ECO:0000244|PDB:1W4R}.
FT   HELIX        99    101       {ECO:0000244|PDB:1W4R}.
FT   HELIX       105    114       {ECO:0000244|PDB:1W4R}.
FT   STRAND      118    126       {ECO:0000244|PDB:1W4R}.
FT   STRAND      130    132       {ECO:0000244|PDB:1W4R}.
FT   HELIX       136    142       {ECO:0000244|PDB:1W4R}.
FT   STRAND      144    148       {ECO:0000244|PDB:1W4R}.
FT   TURN        154    156       {ECO:0000244|PDB:1W4R}.
FT   STRAND      158    160       {ECO:0000244|PDB:1W4R}.
FT   STRAND      162    167       {ECO:0000244|PDB:1W4R}.
FT   TURN        178    180       {ECO:0000244|PDB:1W4R}.
FT   STRAND      181    184       {ECO:0000244|PDB:1W4R}.
FT   HELIX       186    189       {ECO:0000244|PDB:1W4R}.
SQ   SEQUENCE   234 AA;  25469 MW;  76901415C631EF21 CRC64;
     MSCINLPTVL PGSPSKTRGQ IQVILGPMFS GKSTELMRRV RRFQIAQYKC LVIKYAKDTR
     YSSSFCTHDR NTMEALPACL LRDVAQEALG VAVIGIDEGQ FFPDIVEFCE AMANAGKTVI
     VAALDGTFQR KPFGAILNLV PLAESVVKLT AVCMECFREA AYTKRLGTEK EVEVIGGADK
     YHSVCRLCYF KKASGQPAGP DNKENCPVPG KPGEAVAARK LFAPQQILQC SPAN
//
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