ID   Q53Y97_HUMAN            Unreviewed;       313 AA.
AC   Q53Y97;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Thymidylate synthase {ECO:0000256|ARBA:ARBA00015931};
DE            EC=2.1.1.45 {ECO:0000256|ARBA:ARBA00011947};
GN   Name=TYMS {ECO:0000313|EMBL:EAX01721.1};
GN   ORFNames=hCG_1994842 {ECO:0000313|EMBL:EAX01721.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAP35457.1};
RN   [1] {ECO:0000313|EMBL:EAX01721.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:AAP35457.1}
RP   NUCLEOTIDE SEQUENCE.
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 vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAX01721.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:BAG36830.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lung {ECO:0000313|EMBL:BAG36830.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y.,
RA   Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R.,
RA   Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N.,
RA   Isogai T.;
RT   "NEDO functional analysis of protein and research application project.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004992}.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009972}.
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DR   EMBL; BT006811; AAP35457.1; -; mRNA.
DR   EMBL; AK314140; BAG36830.1; -; mRNA.
DR   EMBL; CH471113; EAX01721.1; -; Genomic_DNA.
DR   RefSeq; NP_001062.1; NM_001071.2.
DR   AlphaFoldDB; Q53Y97; -.
DR   SMR; Q53Y97; -.
DR   MaxQB; Q53Y97; -.
DR   Antibodypedia; 3461; 1366 antibodies from 41 providers.
DR   DNASU; 7298; -.
DR   GeneID; 7298; -.
DR   KEGG; hsa:7298; -.
DR   UCSC; uc010dka.2; human.
DR   CTD; 7298; -.
DR   PharmGKB; PA359; -.
DR   VEuPathDB; HostDB:ENSG00000176890; -.
DR   HOGENOM; CLU_021669_0_2_1; -.
DR   OMA; IVYELLW; -.
DR   OrthoDB; 1118873at2759; -.
DR   UniPathway; UPA00575; -.
DR   BioGRID-ORCS; 7298; 334 hits in 1189 CRISPR screens.
DR   ChiTaRS; TYMS; human.
DR   GenomeRNAi; 7298; -.
DR   ExpressionAtlas; Q53Y97; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005542; F:folic acid binding; IEA:Ensembl.
DR   GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR   GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0060574; P:intestinal epithelial cell maturation; IEA:Ensembl.
DR   GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:Ensembl.
DR   GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR   GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:Ensembl.
DR   GO; GO:0019860; P:uracil metabolic process; IEA:Ensembl.
DR   CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR   Gene3D; 3.30.572.10; Thymidylate synthase/dCMP hydroxymethylase domain; 1.
DR   HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR   InterPro; IPR045097; Thymidate_synth/dCMP_Mease.
DR   InterPro; IPR023451; Thymidate_synth/dCMP_Mease_dom.
DR   InterPro; IPR036926; Thymidate_synth/dCMP_Mease_sf.
DR   InterPro; IPR000398; Thymidylate_synthase.
DR   InterPro; IPR020940; Thymidylate_synthase_AS.
DR   NCBIfam; TIGR03284; thym_sym; 1.
DR   PANTHER; PTHR11548:SF2; THYMIDYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1.
DR   Pfam; PF00303; Thymidylat_synt; 1.
DR   PRINTS; PR00108; THYMDSNTHASE.
DR   SUPFAM; SSF55831; Thymidylate synthase/dCMP hydroxymethylase; 1.
DR   PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          32..313
FT                   /note="Thymidylate synthase/dCMP hydroxymethylase"
FT                   /evidence="ECO:0000259|Pfam:PF00303"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
SQ   SEQUENCE   313 AA;  35716 MW;  148D377F19915B6A CRC64;
     MPVAGSELPR RPLPPAAQER DAEPRPPHGE LQYLGQIQHI LRCGVRKDDR TGTGTLSVFG
     MQARYSLRDE FPLLTTKRVF WKGVLEELLW FIKGSTNAKE LSSKGVKIWD ANGSRDFLDS
     LGFSTREEGD LGPVYGFQWR HFGAEYRDME SDYSGQGVDQ LQRVIDTIKT NPDDRRIIMC
     AWNPRDLPLM ALPPCHALCQ FYVVNSELSC QLYQRSGDMG LGVPFNIASY ALLTYMIAHI
     TGLKPGDFIH TLGDAHIYLN HIEPLKIQLQ REPRPFPKLR ILRKVEKIDD FKAEDFQIEG
     YNPHPTIKME MAV
//