SERB_HUMAN
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 03-AUG-2022, entry version 195.
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; 22.
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 EPD; P78330; -.
DR jPOST; P78330; -.
DR MassIVE; P78330; -.
DR MaxQB; P78330; -.
DR PaxDb; P78330; -.
DR PeptideAtlas; P78330; -.
DR PRIDE; P78330; -.
DR ProteomicsDB; 57569; -.
DR Antibodypedia; 13863; 347 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 CTD; 5723; -.
DR DisGeNET; 5723; -.
DR GeneCards; 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; 1009123at2759; -.
DR PhylomeDB; P78330; -.
DR TreeFam; TF315024; -.
DR BioCyc; MetaCyc:HS07370-MON; -.
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 1088 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 184 other tissues.
DR ExpressionAtlas; P78330; baseline and differential.
DR Genevisible; P78330; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
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 DisProt; DP02639; -.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004469; PSP.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00338; serB; 1.
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
