ID SERB_HUMAN Reviewed; 225 AA. AC P78330; B2RCR5; Q7Z3S5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 2. DT 24-JAN-2024, entry version 203. DE RecName: Full=Phosphoserine phosphatase {ECO:0000305|PubMed:12213811}; DE Short=PSP {ECO:0000305|PubMed:12213811}; DE Short=PSPase; DE EC=3.1.3.3 {ECO:0000269|PubMed:12213811, ECO:0000269|PubMed:14673469, ECO:0000269|PubMed:15291819, ECO:0000269|PubMed:1965857, ECO:0000269|PubMed:25080166, ECO:0000269|PubMed:9222972}; DE AltName: Full=L-3-phosphoserine phosphatase {ECO:0000303|PubMed:9188776}; DE AltName: Full=O-phosphoserine phosphohydrolase; GN Name=PSPH {ECO:0000312|HGNC:HGNC:9577}; 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]. RX PubMed=9188776; DOI=10.1016/s0014-5793(97)00438-9; RA Collet J.-F., Gerin I., Rider M.H., Veiga-Da-Cunha M., Van Schaftingen E.; RT "Human L-3-phosphoserine phosphatase: sequence, expression and evidence for RT a phosphoenzyme intermediate."; RL FEBS Lett. 408:281-284(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Endometrial tumor; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [6] RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY. RX PubMed=1965857; DOI=10.1007/bf01208581; RA Shetty V., Shetty K.T.; RT "Phosphoserine phosphatase of human brain: partial purification, RT characterization, regional distribution, and effect of certain modulators RT including psychoactive drugs."; RL Neurochem. Res. 15:1203-1210(1990). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND SUBUNIT. RX PubMed=15291819; DOI=10.1111/j.0014-2956.2004.04277.x; RA Peeraer Y., Rabijns A., Collet J.F., Van Schaftingen E., De Ranter C.; RT "How calcium inhibits the magnesium-dependent enzyme human phosphoserine RT phosphatase."; RL Eur. J. Biochem. 271:3421-3427(2004). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(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] {ECO:0007744|PDB:1L8L, ECO:0007744|PDB:1L8O} RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 3-225 IN COMPLEXES WITH INHIBITOR RP 2-AMINO-3-PHOSPHONOPROPIONIC ACID, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, RP AND MUTAGENESIS OF SER-23; GLU-29; ARG-65; ASN-133; THR-182 AND ARG-202. RX PubMed=12213811; DOI=10.1074/jbc.m204866200; RA Kim H.Y., Heo Y.S., Kim J.H., Park M.H., Moon J., Kim E., Kwon D., Yoon J., RA Shin D., Jeong E.J., Park S.Y., Lee T.G., Jeon Y.H., Ro S., Cho J.M., RA Hwang K.Y.; RT "Molecular basis for the local conformational rearrangement of human RT phosphoserine phosphatase."; RL J. Biol. Chem. 277:46651-46658(2002). RN [11] {ECO:0007744|PDB:1NNL} RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 3-225 IN COMPLEX WITH CALCIUM RP IONS, AND SUBUNIT. RX PubMed=12777757; DOI=10.1107/s0907444903005407; RA Peeraer Y., Rabijns A., Verboven C., Collet J.F., Van Schaftingen E., RA De Ranter C.; RT "High-resolution structure of human phosphoserine phosphatase in open RT conformation."; RL Acta Crystallogr. D 59:971-977(2003). RN [12] {ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J} RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 5-225 IN COMPLEX WITH RP O-PHOSPHO-L-SERINE PHOSPHATE L-SERINE; SERINE AND PHOSPHATE, COFACTOR, RP SUBUNIT, AND ACTIVE SITE. RX PubMed=31205021; DOI=10.1107/s2059798319006867; RA Haufroid M., Mirgaux M., Leherte L., Wouters J.; RT "Crystal structures and snapshots along the reaction pathway of human RT phosphoserine phosphatase."; RL Acta Crystallogr. D 75:592-604(2019). RN [13] RP INVOLVEMENT IN PSPHD, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=9222972; DOI=10.1136/jmg.34.7.594; RA Jaeken J., Detheux M., Fryns J.P., Collet J.F., Alliet P., RA Van Schaftingen E.; RT "Phosphoserine phosphatase deficiency in a patient with Williams RT syndrome."; RL J. Med. Genet. 34:594-596(1997). RN [14] RP VARIANTS PSPHD ASN-32 AND THR-52, CHARACTERIZATION OF VARIANTS PSPHD ASN-32 RP AND THR-52, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=14673469; DOI=10.1038/sj.ejhg.5201083; RA Veiga-da-Cunha M., Collet J.F., Prieur B., Jaeken J., Peeraer Y., RA Rabbijns A., Van Schaftingen E.; RT "Mutations responsible for 3-phosphoserine phosphatase deficiency."; RL Eur. J. Hum. Genet. 12:163-166(2004). RN [15] RP VARIANT PSPHD THR-35, CHARACTERIZATION OF VARIANT PSPHD THR-35, FUNCTION, RP CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=25080166; DOI=10.1111/cge.12445; RA Vincent J.B., Jamil T., Rafiq M.A., Anwar Z., Ayaz M., Hameed A., Nasr T., RA Naeem F., Khattak N.A., Carter M., Ahmed I., John P., Wiame E., RA Andrade D.M., Schaftingen E.V., Mir A., Ayub M.; RT "Phosphoserine phosphatase (PSPH) gene mutation in an intellectual RT disability family from Pakistan."; RL Clin. Genet. 87:296-298(2015). CC -!- FUNCTION: Catalyzes the last irreversible step in the biosynthesis of CC L-serine from carbohydrates, the dephosphorylation of O-phospho-L- CC serine to L-serine (PubMed:12213811, PubMed:15291819, PubMed:9222972, CC PubMed:14673469, PubMed:25080166). L-serine can then be used in protein CC synthesis, to produce other amino acids, in nucleotide metabolism or in CC glutathione synthesis, or can be racemized to D-serine, a CC neuromodulator (PubMed:14673469). May also act on O-phospho-D-serine CC (Probable). {ECO:0000269|PubMed:12213811, ECO:0000269|PubMed:14673469, CC ECO:0000269|PubMed:15291819, ECO:0000269|PubMed:25080166, CC ECO:0000269|PubMed:9222972, ECO:0000303|PubMed:14673469, CC ECO:0000305|PubMed:1965857}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate; CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3; CC Evidence={ECO:0000269|PubMed:12213811, ECO:0000269|PubMed:14673469, CC ECO:0000269|PubMed:15291819, ECO:0000269|PubMed:25080166, CC ECO:0000269|PubMed:9222972}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21209; CC Evidence={ECO:0000269|PubMed:14673469, ECO:0000269|PubMed:25080166, CC ECO:0000269|PubMed:9222972}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate; CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3; CC Evidence={ECO:0000305|PubMed:1965857}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24874; CC Evidence={ECO:0000305|PubMed:1965857}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:15291819, ECO:0000269|PubMed:31205021}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:15291819, CC ECO:0000269|PubMed:31205021}; CC -!- ACTIVITY REGULATION: Inhibited by calcium ions. CC {ECO:0000269|PubMed:15291819}. CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from CC 3-phospho-D-glycerate: step 3/3. {ECO:0000269|PubMed:14673469, CC ECO:0000269|PubMed:25080166, ECO:0000269|PubMed:9222972}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12213811, CC ECO:0000269|PubMed:12777757, ECO:0000269|PubMed:15291819, CC ECO:0000269|PubMed:31205021}. CC -!- INTERACTION: CC P78330; P78330: PSPH; NbExp=3; IntAct=EBI-1042956, EBI-1042956; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:1965857}. CC -!- DISEASE: Phosphoserine phosphatase deficiency (PSPHD) [MIM:614023]: An CC autosomal recessive disorder that results in pre- and postnatal growth CC retardation, moderate psychomotor retardation and facial features CC suggestive of Williams syndrome. {ECO:0000269|PubMed:14673469, CC ECO:0000269|PubMed:25080166, ECO:0000269|PubMed:9222972}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y10275; CAA71318.1; -; mRNA. DR EMBL; AK315235; BAG37662.1; -; mRNA. DR EMBL; BX537439; CAD97681.1; -; mRNA. DR EMBL; CH471140; EAX07968.1; -; Genomic_DNA. DR EMBL; BC063614; AAH63614.1; -; mRNA. DR CCDS; CCDS5522.1; -. DR RefSeq; NP_004568.2; NM_004577.3. DR RefSeq; XP_005271830.1; XM_005271773.1. DR RefSeq; XP_005271831.1; XM_005271774.1. DR RefSeq; XP_005271832.1; XM_005271775.1. DR RefSeq; XP_005271833.1; XM_005271776.1. DR RefSeq; XP_006715823.1; XM_006715760.1. DR RefSeq; XP_011513763.1; XM_011515461.1. DR RefSeq; XP_016867955.1; XM_017012466.1. DR RefSeq; XP_016867956.1; XM_017012467.1. DR PDB; 1L8L; X-ray; 2.51 A; A/B=1-225. DR PDB; 1L8O; X-ray; 2.80 A; A/B=1-225. DR PDB; 1NNL; X-ray; 1.53 A; A/B=1-225. DR PDB; 6HYJ; X-ray; 1.93 A; A/B=3-224. DR PDB; 6HYY; X-ray; 1.57 A; A/B=5-225. DR PDB; 6Q6J; X-ray; 1.99 A; A/B=5-224. DR PDBsum; 1L8L; -. DR PDBsum; 1L8O; -. DR PDBsum; 1NNL; -. DR PDBsum; 6HYJ; -. DR PDBsum; 6HYY; -. DR PDBsum; 6Q6J; -. DR AlphaFoldDB; P78330; -. DR SMR; P78330; -. DR BioGRID; 111695; 25. DR IntAct; P78330; 5. DR MINT; P78330; -. DR STRING; 9606.ENSP00000378854; -. DR DrugBank; DB03292; 3-Phosphono-D-alanine. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR DEPOD; PSPH; -. DR GlyGen; P78330; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P78330; -. DR MetOSite; P78330; -. DR PhosphoSitePlus; P78330; -. DR BioMuta; PSPH; -. DR DMDM; 62906870; -. DR CPTAC; CPTAC-2765; -. DR CPTAC; CPTAC-2766; -. DR EPD; P78330; -. DR jPOST; P78330; -. DR MassIVE; P78330; -. DR MaxQB; P78330; -. DR PaxDb; 9606-ENSP00000378854; -. DR PeptideAtlas; P78330; -. DR ProteomicsDB; 57569; -. DR Pumba; P78330; -. DR Antibodypedia; 13863; 361 antibodies from 33 providers. DR DNASU; 5723; -. DR Ensembl; ENST00000275605.8; ENSP00000275605.3; ENSG00000146733.14. DR Ensembl; ENST00000395471.7; ENSP00000378854.3; ENSG00000146733.14. DR Ensembl; ENST00000437355.6; ENSP00000401639.2; ENSG00000146733.14. DR GeneID; 5723; -. DR KEGG; hsa:5723; -. DR MANE-Select; ENST00000275605.8; ENSP00000275605.3; NM_004577.4; NP_004568.2. DR UCSC; uc003trh.4; human. DR AGR; HGNC:9577; -. DR CTD; 5723; -. DR DisGeNET; 5723; -. DR GeneCards; PSPH; -. DR GeneReviews; PSPH; -. DR HGNC; HGNC:9577; PSPH. DR HPA; ENSG00000146733; Low tissue specificity. DR MalaCards; PSPH; -. DR MIM; 172480; gene. DR MIM; 614023; phenotype. DR neXtProt; NX_P78330; -. DR OpenTargets; ENSG00000146733; -. DR Orphanet; 79350; 3-phosphoserine phosphatase deficiency, infantile/juvenile form. DR PharmGKB; PA33928; -. DR VEuPathDB; HostDB:ENSG00000146733; -. DR eggNOG; KOG1615; Eukaryota. DR GeneTree; ENSGT00390000003115; -. DR HOGENOM; CLU_036368_2_1_1; -. DR InParanoid; P78330; -. DR OMA; RAQYYVT; -. DR OrthoDB; 275980at2759; -. DR PhylomeDB; P78330; -. DR TreeFam; TF315024; -. DR BioCyc; MetaCyc:HS07370-MONOMER; -. DR BRENDA; 3.1.3.3; 2681. DR PathwayCommons; P78330; -. DR Reactome; R-HSA-977347; Serine biosynthesis. DR SignaLink; P78330; -. DR SIGNOR; P78330; -. DR UniPathway; UPA00135; UER00198. DR BioGRID-ORCS; 5723; 14 hits in 1181 CRISPR screens. DR ChiTaRS; PSPH; human. DR EvolutionaryTrace; P78330; -. DR GeneWiki; PSPH; -. DR GenomeRNAi; 5723; -. DR Pharos; P78330; Tbio. DR PRO; PR:P78330; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P78330; Protein. DR Bgee; ENSG00000146733; Expressed in adrenal tissue and 186 other cell types or tissues. DR ExpressionAtlas; P78330; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0006564; P:L-serine biosynthetic process; IMP:UniProtKB. DR GO; GO:0006563; P:L-serine metabolic process; IDA:UniProtKB. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl. DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl. DR CDD; cd04309; HAD_PSP_eu; 1. DR DisProt; DP02639; -. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR004469; PSP. DR NCBIfam; TIGR01488; HAD-SF-IB; 1. DR NCBIfam; TIGR00338; serB; 1. DR PANTHER; PTHR43344; PHOSPHOSERINE PHOSPHATASE; 1. DR PANTHER; PTHR43344:SF2; PHOSPHOSERINE PHOSPHATASE; 1. DR Pfam; PF00702; Hydrolase; 1. DR SFLD; SFLDG01137; C1.6.1:_Phosphoserine_Phosphat; 1. DR SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR Genevisible; P78330; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Amino-acid biosynthesis; Cytoplasm; KW Disease variant; Hydrolase; Magnesium; Metal-binding; Reference proteome; KW Serine biosynthesis. FT CHAIN 1..225 FT /note="Phosphoserine phosphatase" FT /id="PRO_0000156879" FT ACT_SITE 20 FT /note="Nucleophile" FT /evidence="ECO:0000305|PubMed:31205021, FT ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, FT ECO:0007744|PDB:6Q6J" FT ACT_SITE 22 FT /note="Proton donor" FT /evidence="ECO:0000305|PubMed:31205021, FT ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, FT ECO:0007744|PDB:6Q6J" FT BINDING 20..22 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, FT ECO:0007744|PDB:6Q6J" FT BINDING 20 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYY" FT BINDING 22 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYY" FT BINDING 52 FT /ligand="O-phospho-L-serine" FT /ligand_id="ChEBI:CHEBI:57524" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, FT ECO:0007744|PDB:6Q6J" FT BINDING 53 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, FT ECO:0007744|PDB:6Q6J" FT BINDING 109..111 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, FT ECO:0007744|PDB:6Q6J" FT BINDING 109..111 FT /ligand="O-phospho-L-serine" FT /ligand_id="ChEBI:CHEBI:57524" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, FT ECO:0007744|PDB:6Q6J" FT BINDING 158 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, FT ECO:0007744|PDB:6Q6J" FT BINDING 158 FT /ligand="O-phospho-L-serine" FT /ligand_id="ChEBI:CHEBI:57524" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, FT ECO:0007744|PDB:6Q6J" FT BINDING 179 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYY" FT BINDING 182 FT /ligand="O-phospho-L-serine" FT /ligand_id="ChEBI:CHEBI:57524" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, FT ECO:0007744|PDB:6Q6J" FT BINDING 182 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000269|PubMed:31205021, FT ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, FT ECO:0007744|PDB:6Q6J" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT VARIANT 32 FT /note="D -> N (in PSPHD; decreased L-phosphoserine FT phosphatase activity; dbSNP:rs104894035)" FT /evidence="ECO:0000269|PubMed:14673469" FT /id="VAR_022378" FT VARIANT 35 FT /note="A -> T (in PSPHD; decreased L-phosphoserine FT phosphatase activity)" FT /evidence="ECO:0000269|PubMed:25080166" FT /id="VAR_084508" FT VARIANT 52 FT /note="M -> T (in PSPHD; decreased L-phosphoserine FT phosphatase activity; dbSNP:rs104894036)" FT /evidence="ECO:0000269|PubMed:14673469" FT /id="VAR_022379" FT MUTAGEN 23 FT /note="S->A: Reduces L-phosphoserine phosphatase activity FT by about 50%." FT /evidence="ECO:0000269|PubMed:12213811" FT MUTAGEN 23 FT /note="S->T: Reduces L-phosphoserine phosphatase activity FT by about 80%." FT /evidence="ECO:0000269|PubMed:12213811" FT MUTAGEN 29 FT /note="E->D: Reduces L-phosphoserine phosphatase activity FT by about 95%." FT /evidence="ECO:0000269|PubMed:12213811" FT MUTAGEN 29 FT /note="E->Q: Loss of L-phosphoserine phosphatase activity." FT /evidence="ECO:0000269|PubMed:12213811" FT MUTAGEN 65 FT /note="R->A,K: Loss of L-phosphoserine phosphatase FT activity." FT /evidence="ECO:0000269|PubMed:12213811" FT MUTAGEN 133 FT /note="N->A: Reduces L-phosphoserine phosphatase activity FT by about 75%." FT /evidence="ECO:0000269|PubMed:12213811" FT MUTAGEN 182 FT /note="T->S: Reduces L-phosphoserine phosphatase activity FT by about 99%." FT /evidence="ECO:0000269|PubMed:12213811" FT MUTAGEN 182 FT /note="T->V: Reduces L-phosphoserine phosphatase activity FT by about 25%." FT /evidence="ECO:0000269|PubMed:12213811" FT MUTAGEN 202 FT /note="R->A: Reduces L-phosphoserine phosphatase activity FT by about 99%." FT /evidence="ECO:0000269|PubMed:12213811" FT MUTAGEN 202 FT /note="R->K: Reduces L-phosphoserine phosphatase activity FT by about 95%." FT /evidence="ECO:0000269|PubMed:12213811" FT CONFLICT 2 FT /note="V -> I (in Ref. 1; CAA71318)" FT /evidence="ECO:0000305" FT HELIX 6..13 FT /evidence="ECO:0007829|PDB:1NNL" FT STRAND 15..20 FT /evidence="ECO:0007829|PDB:1NNL" FT TURN 23..25 FT /evidence="ECO:0007829|PDB:1NNL" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:1NNL" FT HELIX 30..37 FT /evidence="ECO:0007829|PDB:1NNL" FT TURN 41..43 FT /evidence="ECO:0007829|PDB:1NNL" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:1L8L" FT TURN 52..55 FT /evidence="ECO:0007829|PDB:6HYJ" FT HELIX 58..69 FT /evidence="ECO:0007829|PDB:1NNL" FT HELIX 73..82 FT /evidence="ECO:0007829|PDB:1NNL" FT HELIX 91..100 FT /evidence="ECO:0007829|PDB:1NNL" FT STRAND 104..112 FT /evidence="ECO:0007829|PDB:1NNL" FT HELIX 113..122 FT /evidence="ECO:0007829|PDB:1NNL" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:1NNL" FT STRAND 130..133 FT /evidence="ECO:0007829|PDB:1NNL" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:1NNL" FT STRAND 143..146 FT /evidence="ECO:0007829|PDB:1NNL" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:1L8L" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:1NNL" FT HELIX 157..169 FT /evidence="ECO:0007829|PDB:1NNL" FT STRAND 174..180 FT /evidence="ECO:0007829|PDB:1NNL" FT HELIX 181..184 FT /evidence="ECO:0007829|PDB:1NNL" FT TURN 185..189 FT /evidence="ECO:0007829|PDB:1NNL" FT STRAND 190..196 FT /evidence="ECO:0007829|PDB:1NNL" FT HELIX 203..208 FT /evidence="ECO:0007829|PDB:1NNL" FT STRAND 210..214 FT /evidence="ECO:0007829|PDB:1NNL" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:1NNL" FT HELIX 221..224 FT /evidence="ECO:0007829|PDB:1L8L" SQ SEQUENCE 225 AA; 25008 MW; BD5D72697747FA30 CRC64; MVSHSELRKL FYSADAVCFD VDSTVIREEG IDELAKICGV EDAVSEMTRR AMGGAVPFKA ALTERLALIQ PSREQVQRLI AEQPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA SKLNIPATNV FANRLKFYFN GEYAGFDETQ PTAESGGKGK VIKLLKEKFH FKKIIMIGDG ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE //