GLYC_HUMAN
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 03-AUG-2022, entry version 217.
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 PDBsum; 1BJ4; -.
DR PDBsum; 6FL5; -.
DR PDBsum; 6M5W; -.
DR AlphaFoldDB; P34896; -.
DR SMR; P34896; -.
DR BioGRID; 112366; 70.
DR CORUM; P34896; -.
DR IntAct; P34896; 22.
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; P34896; -.
DR PeptideAtlas; P34896; -.
DR PRIDE; P34896; -.
DR ProteomicsDB; 4797; -.
DR ProteomicsDB; 54945; -. [P34896-1]
DR ProteomicsDB; 54946; -. [P34896-2]
DR ProteomicsDB; 54947; -. [P34896-3]
DR Antibodypedia; 13529; 282 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 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; ANASVMH; -.
DR OrthoDB; 372408at2759; -.
DR PhylomeDB; P34896; -.
DR TreeFam; TF314667; -.
DR BioCyc; MetaCyc:HS11114-MON; -.
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; 14 hits in 1085 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 100 other tissues.
DR ExpressionAtlas; P34896; baseline and differential.
DR Genevisible; P34896; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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:0006730; P:one-carbon metabolic process; IBA:GO_Central.
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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00096; SHMT; 1.
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 13..21
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 31..46
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 87..103
FT /evidence="ECO:0007829|PDB:1BJ4"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:1BJ4"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:1BJ4"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:1BJ4"
FT TURN 297..300
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 306..318
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 322..344
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 370..379
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 406..410
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 415..438
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 445..452
FT /evidence="ECO:0007829|PDB:1BJ4"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:1BJ4"
FT HELIX 458..472
FT /evidence="ECO:0007829|PDB:1BJ4"
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
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