ID   GLYC_HUMAN              Reviewed;         483 AA.
AC   P34896; B4DPM9; D3DXD0; Q96HY0; Q9UMD1; Q9UMD2;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 226.
DE   RecName: Full=Serine hydroxymethyltransferase, cytosolic;
DE            Short=SHMT;
DE            EC=2.1.2.1 {ECO:0000269|PubMed:24698160, ECO:0000269|PubMed:8505317};
DE   AltName: Full=Glycine hydroxymethyltransferase;
DE   AltName: Full=Serine methylase;
GN   Name=SHMT1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8505317; DOI=10.1016/s0021-9258(19)50286-1;
RA   Garrow T.A., Brenner A.A., Whitehead M.V., Chen X.-N., Duncan R.G.,
RA   Korenberg J.R., Shane B.;
RT   "Cloning of human cDNAs encoding mitochondrial and cytosolic serine
RT   hydroxymethyltransferases and chromosomal localization.";
RL   J. Biol. Chem. 268:11910-11916(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Xu L., Mangum J.H., Robertson D.L.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=9056951; DOI=10.1042/bst025053s;
RA   Chave K.J., Snell K., Sanders P.G.;
RT   "Isolation and characterisation of human genomic sequences encoding
RT   cytosolic serine hydroxymethyltransferase.";
RL   Biochem. Soc. Trans. 25:53-53(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Liver;
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-474.
RA   Mural R.J., Istrail S., Sutton G.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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   PHE-474.
RC   TISSUE=Bone marrow, Lymph, and Testis;
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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-271 (ISOFORM 2), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   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   [9]
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., Buerckstuemmer T.,
RA   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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BRISC COMPLEX,
RP   AND INTERACTION WITH ABRAXAS2.
RX   PubMed=24075985; DOI=10.1016/j.celrep.2013.08.025;
RA   Zheng H., Gupta V., Patterson-Fortin J., Bhattacharya S., Katlinski K.,
RA   Wu J., Varghese B., Carbone C.J., Aressy B., Fuchs S.Y., Greenberg R.A.;
RT   "A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon
RT   responses.";
RL   Cell Rep. 5:180-193(2013).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, SUBUNIT, AND COFACTOR.
RX   PubMed=24698160; DOI=10.1111/febs.12803;
RA   Pinthong C., Maenpuen S., Amornwatcharapong W., Yuthavong Y.,
RA   Leartsakulpanich U., Chaiyen P.;
RT   "Distinct biochemical properties of human serine hydroxymethyltransferase
RT   compared with the Plasmodium enzyme: implications for selective
RT   inhibition.";
RL   FEBS J. 281:2570-2583(2014).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [13]
RP   SUBUNIT, AND COFACTOR.
RX   PubMed=25619277; DOI=10.1111/febs.13211;
RA   Giardina G., Brunotti P., Fiascarelli A., Cicalini A., Costa M.G.,
RA   Buckle A.M., di Salvo M.L., Giorgi A., Marani M., Paone A., Rinaldo S.,
RA   Paiardini A., Contestabile R., Cutruzzola F.;
RT   "How pyridoxal 5'-phosphate differentially regulates human cytosolic and
RT   mitochondrial serine hydroxymethyltransferase oligomeric state.";
RL   FEBS J. 282:1225-1241(2015).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 11-480, COFACTOR, AND SUBUNIT.
RX   PubMed=9753690; DOI=10.1016/s0969-2126(98)00112-9;
RA   Renwick S.B., Snell K., Baumann U.;
RT   "The crystal structure of human cytosolic serine hydroxymethyltransferase:
RT   a target for cancer chemotherapy.";
RL   Structure 6:1105-1116(1998).
CC   -!- FUNCTION: Interconversion of serine and glycine (PubMed:8505317,
CC       PubMed:24698160). {ECO:0000269|PubMed:24698160,
CC       ECO:0000269|PubMed:8505317}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC         (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC         Evidence={ECO:0000269|PubMed:24698160, ECO:0000269|PubMed:8505317};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:24698160, ECO:0000269|PubMed:25619277,
CC         ECO:0000269|PubMed:9753690};
CC   -!- ACTIVITY REGULATION: Inhibited by tetrahydrofolate concentrations above
CC       40 uM. {ECO:0000269|PubMed:24698160}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.18 mM for L-serine {ECO:0000269|PubMed:24698160};
CC         KM=5.2 uM for tetrahydrofolate {ECO:0000269|PubMed:24698160};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000305|PubMed:24698160}.
CC   -!- SUBUNIT: Homotetramer (PubMed:24698160, PubMed:25619277,
CC       PubMed:9753690). Identified in complex with ABRAXAS2 and the other
CC       subunits of the BRISC complex, at least composed of ABRAXAS2,
CC       BRCC3/BRCC36, BABAM2 and BABAM1/NBA1 (PubMed:24075985).
CC       {ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:24698160,
CC       ECO:0000269|PubMed:25619277, ECO:0000269|PubMed:9753690}.
CC   -!- INTERACTION:
CC       P34896; P26196: DDX6; NbExp=3; IntAct=EBI-715117, EBI-351257;
CC       P34896; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-715117, EBI-739467;
CC       P34896; P50213: IDH3A; NbExp=6; IntAct=EBI-715117, EBI-355999;
CC       P34896; P45984: MAPK9; NbExp=7; IntAct=EBI-715117, EBI-713568;
CC       P34896; Q99750: MDFI; NbExp=3; IntAct=EBI-715117, EBI-724076;
CC       P34896; P34896: SHMT1; NbExp=4; IntAct=EBI-715117, EBI-715117;
CC       P34896; P0DMM9: SULT1A3; NbExp=3; IntAct=EBI-715117, EBI-10196922;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P34896-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P34896-2; Sequence=VSP_006095;
CC       Name=3;
CC         IsoId=P34896-3; Sequence=VSP_006096;
CC       Name=4;
CC         IsoId=P34896-4; Sequence=VSP_054610;
CC   -!- MISCELLANEOUS: In eukaryotes there are two forms of the enzymes: a
CC       cytosolic one and a mitochondrial one. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR   EMBL; L11931; AAA63257.1; -; mRNA.
DR   EMBL; L23928; AAA36020.1; -; mRNA.
DR   EMBL; L23928; AAA36019.1; -; mRNA.
DR   EMBL; L23928; AAA36018.1; -; mRNA.
DR   EMBL; Y14485; CAB54838.1; -; mRNA.
DR   EMBL; Y14486; CAB54839.1; -; mRNA.
DR   EMBL; Y14487; CAB54840.1; -; mRNA.
DR   EMBL; AK298415; BAG60641.1; -; mRNA.
DR   EMBL; AC127537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471196; EAW55637.1; -; Genomic_DNA.
DR   EMBL; CH471196; EAW55640.1; -; Genomic_DNA.
DR   EMBL; CH471196; EAW55641.1; -; Genomic_DNA.
DR   EMBL; BC007979; AAH07979.1; -; mRNA.
DR   EMBL; BC022874; AAH22874.1; -; mRNA.
DR   EMBL; BC038598; AAH38598.1; -; mRNA.
DR   CCDS; CCDS11196.1; -. [P34896-1]
DR   CCDS; CCDS11197.1; -. [P34896-2]
DR   CCDS; CCDS62112.1; -. [P34896-4]
DR   PIR; A46746; A46746.
DR   RefSeq; NP_001268715.1; NM_001281786.1. [P34896-4]
DR   RefSeq; NP_004160.3; NM_004169.4. [P34896-1]
DR   RefSeq; NP_683718.1; NM_148918.2. [P34896-2]
DR   RefSeq; XP_005256824.1; XM_005256767.3. [P34896-1]
DR   RefSeq; XP_011522294.1; XM_011523992.2. [P34896-3]
DR   RefSeq; XP_016880446.1; XM_017024957.1. [P34896-1]
DR   RefSeq; XP_016880447.1; XM_017024958.1. [P34896-2]
DR   PDB; 1BJ4; X-ray; 2.65 A; A=11-480.
DR   PDB; 6FL5; X-ray; 3.60 A; A/D/G/J=11-481.
DR   PDB; 6M5W; X-ray; 3.10 A; A=1-483.
DR   PDB; 7RJL; X-ray; 1.50 A; C/D=270-275.
DR   PDB; 7RJP; X-ray; 1.25 A; B=270-275.
DR   PDB; 8A11; EM; 3.52 A; A/B/C/D=1-483.
DR   PDBsum; 1BJ4; -.
DR   PDBsum; 6FL5; -.
DR   PDBsum; 6M5W; -.
DR   PDBsum; 7RJL; -.
DR   PDBsum; 7RJP; -.
DR   PDBsum; 8A11; -.
DR   AlphaFoldDB; P34896; -.
DR   SMR; P34896; -.
DR   BioGRID; 112366; 83.
DR   CORUM; P34896; -.
DR   IntAct; P34896; 23.
DR   MINT; P34896; -.
DR   STRING; 9606.ENSP00000318868; -.
DR   BindingDB; P34896; -.
DR   ChEMBL; CHEMBL1772927; -.
DR   DrugBank; DB02800; 5-hydroxymethyl-5,6-dihydrofolic acid.
DR   DrugBank; DB00145; Glycine.
DR   DrugBank; DB01055; Mimosine.
DR   DrugBank; DB02824; N-Pyridoxyl-Glycine-5-Monophosphate.
DR   DrugBank; DB00114; Pyridoxal phosphate.
DR   DrugBank; DB00116; Tetrahydrofolic acid.
DR   DrugBank; DB02067; Triglu-5-formyl-tetrahydrofolate.
DR   DrugCentral; P34896; -.
DR   MoonProt; P34896; -.
DR   iPTMnet; P34896; -.
DR   PhosphoSitePlus; P34896; -.
DR   SwissPalm; P34896; -.
DR   BioMuta; SHMT1; -.
DR   DMDM; 462184; -.
DR   EPD; P34896; -.
DR   jPOST; P34896; -.
DR   MassIVE; P34896; -.
DR   MaxQB; P34896; -.
DR   PaxDb; 9606-ENSP00000318868; -.
DR   PeptideAtlas; P34896; -.
DR   ProteomicsDB; 4797; -.
DR   ProteomicsDB; 54945; -. [P34896-1]
DR   ProteomicsDB; 54946; -. [P34896-2]
DR   ProteomicsDB; 54947; -. [P34896-3]
DR   Pumba; P34896; -.
DR   Antibodypedia; 13529; 318 antibodies from 34 providers.
DR   DNASU; 6470; -.
DR   Ensembl; ENST00000316694.8; ENSP00000318868.3; ENSG00000176974.21. [P34896-1]
DR   Ensembl; ENST00000352886.10; ENSP00000345881.7; ENSG00000176974.21. [P34896-4]
DR   Ensembl; ENST00000354098.7; ENSP00000318805.3; ENSG00000176974.21. [P34896-2]
DR   Ensembl; ENST00000640392.2; ENSP00000492715.2; ENSG00000284320.3. [P34896-1]
DR   Ensembl; ENST00000644141.2; ENSP00000495756.2; ENSG00000284320.3. [P34896-1]
DR   GeneID; 6470; -.
DR   KEGG; hsa:6470; -.
DR   MANE-Select; ENST00000316694.8; ENSP00000318868.3; NM_004169.5; NP_004160.3.
DR   UCSC; uc002gta.5; human. [P34896-1]
DR   AGR; HGNC:10850; -.
DR   CTD; 6470; -.
DR   DisGeNET; 6470; -.
DR   GeneCards; SHMT1; -.
DR   HGNC; HGNC:10850; SHMT1.
DR   HPA; ENSG00000176974; Tissue enhanced (kidney, liver).
DR   MIM; 182144; gene.
DR   neXtProt; NX_P34896; -.
DR   OpenTargets; ENSG00000176974; -.
DR   PharmGKB; PA35753; -.
DR   VEuPathDB; HostDB:ENSG00000176974; -.
DR   eggNOG; KOG2467; Eukaryota.
DR   GeneTree; ENSGT00390000002762; -.
DR   HOGENOM; CLU_022477_0_0_1; -.
DR   InParanoid; P34896; -.
DR   OMA; CATTHKV; -.
DR   OrthoDB; 5358603at2759; -.
DR   PhylomeDB; P34896; -.
DR   TreeFam; TF314667; -.
DR   BioCyc; MetaCyc:HS11114-MONOMER; -.
DR   BRENDA; 2.1.2.1; 2681.
DR   PathwayCommons; P34896; -.
DR   Reactome; R-HSA-196757; Metabolism of folate and pterines.
DR   Reactome; R-HSA-71262; Carnitine synthesis.
DR   SABIO-RK; P34896; -.
DR   SignaLink; P34896; -.
DR   SIGNOR; P34896; -.
DR   UniPathway; UPA00193; -.
DR   BioGRID-ORCS; 6470; 16 hits in 1172 CRISPR screens.
DR   ChiTaRS; SHMT1; human.
DR   EvolutionaryTrace; P34896; -.
DR   GenomeRNAi; 6470; -.
DR   Pharos; P34896; Tbio.
DR   PRO; PR:P34896; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P34896; Protein.
DR   Bgee; ENSG00000176974; Expressed in right lobe of liver and 102 other cell types or tissues.
DR   ExpressionAtlas; P34896; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA.
DR   GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IDA:CAFA.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR   GO; GO:0070905; F:serine binding; IDA:BHF-UCL.
DR   GO; GO:0036094; F:small molecule binding; IPI:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IBA:GO_Central.
DR   GO; GO:1904482; P:cellular response to tetrahydrofolate; IDA:BHF-UCL.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:Ensembl.
DR   GO; GO:0046655; P:folic acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IBA:GO_Central.
DR   GO; GO:0006544; P:glycine metabolic process; IDA:UniProtKB.
DR   GO; GO:0006565; P:L-serine catabolic process; IDA:UniProtKB.
DR   GO; GO:0006563; P:L-serine metabolic process; IDA:UniProtKB.
DR   GO; GO:0017148; P:negative regulation of translation; IDA:CAFA.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IDA:BHF-UCL.
DR   GO; GO:0046653; P:tetrahydrofolate metabolic process; IDA:UniProtKB.
DR   CDD; cd00378; SHMT; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00051; SHMT; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR   InterPro; IPR039429; SHMT-like_dom.
DR   PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11680:SF35; SERINE HYDROXYMETHYLTRANSFERASE, CYTOSOLIC; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00096; SHMT; 1.
DR   Genevisible; P34896; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   One-carbon metabolism; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..483
FT                   /note="Serine hydroxymethyltransferase, cytosolic"
FT                   /id="PRO_0000113504"
FT   MOD_RES         257
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:9753690,
FT                   ECO:0007744|PDB:1BJ4"
FT   VAR_SEQ         1..138
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054610"
FT   VAR_SEQ         273..352
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006096"
FT   VAR_SEQ         274..312
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_006095"
FT   VARIANT         340
FT                   /note="E -> Q (in dbSNP:rs7215148)"
FT                   /id="VAR_059795"
FT   VARIANT         474
FT                   /note="L -> F (in dbSNP:rs1979277)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6"
FT                   /id="VAR_022010"
FT   HELIX           15..23
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           26..29
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           31..45
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           59..65
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           68..70
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   TURN            84..87
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           88..103
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   TURN            108..110
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           120..131
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   TURN            143..146
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           162..166
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   TURN            176..178
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           183..193
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          196..201
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           211..221
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          224..228
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           229..231
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           233..238
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          249..256
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          265..270
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   TURN            278..280
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           288..296
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   TURN            297..300
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           306..319
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           322..344
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          355..362
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           363..365
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           370..379
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          385..387
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   STRAND          400..405
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           406..409
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   TURN            410..412
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           415..439
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           445..453
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   HELIX           455..472
FT                   /evidence="ECO:0007829|PDB:6M5W"
FT   MOD_RES         P34896-2:271
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
SQ   SEQUENCE   483 AA;  53083 MW;  6CDD6CA06D017C19 CRC64;
     MTMPVNGAHK DADLWSSHDK MLAQPLKDSD VEVYNIIKKE SNRQRVGLEL IASENFASRA
     VLEALGSCLN NKYSEGYPGQ RYYGGTEFID ELETLCQKRA LQAYKLDPQC WGVNVQPYSG
     SPANFAVYTA LVEPHGRIMG LDLPDGGHLT HGFMTDKKKI SATSIFFESM PYKVNPDTGY
     INYDQLEENA RLFHPKLIIA GTSCYSRNLE YARLRKIADE NGAYLMADMA HISGLVAAGV
     VPSPFEHCHV VTTTTHKTLR GCRAGMIFYR KGVKSVDPKT GKEILYNLES LINSAVFPGL
     QGGPHNHAIA GVAVALKQAM TLEFKVYQHQ VVANCRALSE ALTELGYKIV TGGSDNHLIL
     VDLRSKGTDG GRAEKVLEAC SIACNKNTCP GDRSALRPSG LRLGTPALTS RGLLEKDFQK
     VAHFIHRGIE LTLQIQSDTG VRATLKEFKE RLAGDKYQAA VQALREEVES FASLFPLPGL
     PDF
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