ID CTDS1_HUMAN Reviewed; 261 AA. AC Q9GZU7; C9IYG0; Q7Z5Q3; Q7Z5Q4; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 185. DE RecName: Full=Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1; DE EC=3.1.3.16 {ECO:0000269|PubMed:12721286, ECO:0000269|PubMed:17157258}; DE AltName: Full=Nuclear LIM interactor-interacting factor 3; DE Short=NLI-IF; DE Short=NLI-interacting factor 3; DE AltName: Full=Small C-terminal domain phosphatase 1; DE Short=SCP1; DE Short=Small CTD phosphatase 1; GN Name=CTDSP1; Synonyms=NIF3, NLIIF, SCP1; 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 [GENOMIC DNA / MRNA] (ISOFORM 1). RX PubMed=10967134; DOI=10.1007/s003350010151; RA Marquet S., Lepage P., Hudson T.J., Musser J.M., Schurr E.; RT "Complete nucleotide sequence and genomic structure of the human NRAMP1 RT gene region on chromosome region 2q35."; RL Mamm. Genome 11:755-762(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF RP 50-260 (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GTF2F1, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-96 AND ASP-98. RX PubMed=12721286; DOI=10.1074/jbc.m301791200; RA Yeo M., Lin P.S., Dahmus M.E., Gill G.N.; RT "A novel RNA polymerase II C-terminal domain phosphatase that RT preferentially dephosphorylates serine 5."; RL J. Biol. Chem. 278:26078-26085(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Placenta; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph; 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, TISSUE SPECIFICITY, AND INTERACTION WITH REST. RX PubMed=15681389; DOI=10.1126/science.1100801; RA Yeo M., Lee S.-K., Lee B., Ruiz E.C., Pfaff S.L., Gill G.N.; RT "Small CTD phosphatases function in silencing neuronal gene expression."; RL Science 307:596-600(2005). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 77-261 IN COMPLEX WITH MAGNESIUM RP AND INHIBITOR, AND ACTIVE SITE. RX PubMed=15304220; DOI=10.1016/j.molcel.2004.06.035; RA Kamenski T., Heilmeier S., Meinhart A., Cramer P.; RT "Structure and mechanism of RNA polymerase II CTD phosphatases."; RL Mol. Cell 15:399-407(2004). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 77-256 OF MUTANT ASN-96 IN COMPLEX RP WITH SUBSTRATE PEPTIDES AND MAGNESIUM, CATALYTIC ACTIVITY, SUBSTRATE RP SPECIFICITY, AND ACTIVE SITE. RX PubMed=17157258; DOI=10.1016/j.molcel.2006.10.027; RA Zhang Y., Kim Y., Genoud N., Gao J., Kelly J.W., Pfaff S.L., Gill G.N., RA Dixon J.E., Noel J.P.; RT "Determinants for dephosphorylation of the RNA polymerase II C-terminal RT domain by Scp1."; RL Mol. Cell 24:759-770(2006). CC -!- FUNCTION: Preferentially catalyzes the dephosphorylation of 'Ser-5' CC within the tandem 7 residue repeats in the C-terminal domain (CTD) of CC the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA CC polymerase II transcription, possibly by controlling the transition CC from initiation/capping to processive transcript elongation. Recruited CC by REST to neuronal genes that contain RE-1 elements, leading to CC neuronal gene silencing in non-neuronal cells. CC {ECO:0000269|PubMed:12721286, ECO:0000269|PubMed:15681389}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000269|PubMed:12721286, ECO:0000269|PubMed:17157258}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000269|PubMed:12721286, ECO:0000269|PubMed:17157258}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:12721286}; CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000269|PubMed:15304220, CC ECO:0000269|PubMed:17157258}; CC -!- ACTIVITY REGULATION: Stimulated by GTF2F1. Inhibited by beryllofluoride CC anions. {ECO:0000269|PubMed:12721286}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5. {ECO:0000269|PubMed:12721286}; CC -!- SUBUNIT: Monomer (By similarity). Interacts with GTF2F1. Interacts with CC REST. {ECO:0000250, ECO:0000269|PubMed:12721286, CC ECO:0000269|PubMed:15304220, ECO:0000269|PubMed:15681389, CC ECO:0000269|PubMed:17157258}. CC -!- INTERACTION: CC Q9GZU7; Q08043: ACTN3; NbExp=3; IntAct=EBI-751587, EBI-2880652; CC Q9GZU7; O95817: BAG3; NbExp=3; IntAct=EBI-751587, EBI-747185; CC Q9GZU7; Q99618: CDCA3; NbExp=10; IntAct=EBI-751587, EBI-739534; CC Q9GZU7; P42773: CDKN2C; NbExp=3; IntAct=EBI-751587, EBI-711290; CC Q9GZU7; P53672: CRYBA2; NbExp=3; IntAct=EBI-751587, EBI-750444; CC Q9GZU7; Q9H0L4: CSTF2T; NbExp=3; IntAct=EBI-751587, EBI-747012; CC Q9GZU7; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-751587, EBI-12013806; CC Q9GZU7; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-751587, EBI-1752811; CC Q9GZU7; Q9NW38: FANCL; NbExp=3; IntAct=EBI-751587, EBI-2339898; CC Q9GZU7; P27987: ITPKB; NbExp=5; IntAct=EBI-751587, EBI-751388; CC Q9GZU7; P06239-3: LCK; NbExp=3; IntAct=EBI-751587, EBI-13287659; CC Q9GZU7; O60336: MAPKBP1; NbExp=3; IntAct=EBI-751587, EBI-947402; CC Q9GZU7; P02686: MBP; NbExp=4; IntAct=EBI-751587, EBI-947410; CC Q9GZU7; P02686-2: MBP; NbExp=4; IntAct=EBI-751587, EBI-12159027; CC Q9GZU7; Q6PF18: MORN3; NbExp=3; IntAct=EBI-751587, EBI-9675802; CC Q9GZU7; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-751587, EBI-12025760; CC Q9GZU7; Q17RL8: PDZD4; NbExp=3; IntAct=EBI-751587, EBI-10239064; CC Q9GZU7; Q8ND90: PNMA1; NbExp=2; IntAct=EBI-751587, EBI-302345; CC Q9GZU7; Q8TBN0: RAB3IL1; NbExp=3; IntAct=EBI-751587, EBI-743796; CC Q9GZU7; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-751587, EBI-12000762; CC Q9GZU7; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-751587, EBI-748391; CC Q9GZU7; O00560: SDCBP; NbExp=3; IntAct=EBI-751587, EBI-727004; CC Q9GZU7; Q15797: SMAD1; NbExp=2; IntAct=EBI-751587, EBI-1567153; CC Q9GZU7; Q7Z7C7: STRA8; NbExp=3; IntAct=EBI-751587, EBI-12036261; CC Q9GZU7; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-751587, EBI-750487; CC Q9GZU7; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-751587, EBI-8451480; CC Q9GZU7; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-751587, EBI-12040603; CC Q9GZU7; P62699: YPEL5; NbExp=3; IntAct=EBI-751587, EBI-11721624; CC Q9GZU7; Q05516: ZBTB16; NbExp=3; IntAct=EBI-751587, EBI-711925; CC Q9GZU7; P58466: Ctdsp1; Xeno; NbExp=2; IntAct=EBI-751587, EBI-7091612; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12721286}. CC Note=Colocalizes with RNA polymerase II. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9GZU7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9GZU7-2; Sequence=VSP_045866; CC Name=3; CC IsoId=Q9GZU7-3; Sequence=VSP_045865, VSP_045866; CC -!- TISSUE SPECIFICITY: Expression is restricted to non-neuronal tissues. CC Highest expression in skeletal muscle, spleen, lung and placenta. CC {ECO:0000269|PubMed:15681389}. CC -!- SEQUENCE CAUTION: CC Sequence=AAP34398.1; Type=Frameshift; Evidence={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; AF229163; AAG15404.1; -; Genomic_DNA. DR EMBL; AF229162; AAG15402.1; -; mRNA. DR EMBL; AY279529; AAP34397.1; -; mRNA. DR EMBL; AY279530; AAP34398.1; ALT_FRAME; mRNA. DR EMBL; BX446444; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC021016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC012977; AAH12977.1; -; mRNA. DR CCDS; CCDS2416.1; -. [Q9GZU7-1] DR CCDS; CCDS56166.1; -. [Q9GZU7-3] DR RefSeq; NP_001193807.1; NM_001206878.1. [Q9GZU7-3] DR RefSeq; NP_067021.1; NM_021198.2. [Q9GZU7-1] DR RefSeq; NP_872580.1; NM_182642.2. [Q9GZU7-2] DR PDB; 1T9Z; X-ray; 2.30 A; A=77-261. DR PDB; 1TA0; X-ray; 2.10 A; A=77-261. DR PDB; 2GHQ; X-ray; 2.05 A; A/B=77-256. DR PDB; 2GHT; X-ray; 1.80 A; A/B=77-256. DR PDB; 3L0B; X-ray; 2.35 A; A/B=77-256. DR PDB; 3L0C; X-ray; 2.45 A; A/B=77-256. DR PDB; 3L0Y; X-ray; 2.30 A; A/B=77-256. DR PDB; 3PGL; X-ray; 2.35 A; A/B=77-256. DR PDB; 4YGY; X-ray; 2.36 A; A/B=77-261. DR PDB; 4YH1; X-ray; 2.20 A; A/B=77-255. DR PDB; 6DU3; X-ray; 2.58 A; A/B=77-256. DR PDBsum; 1T9Z; -. DR PDBsum; 1TA0; -. DR PDBsum; 2GHQ; -. DR PDBsum; 2GHT; -. DR PDBsum; 3L0B; -. DR PDBsum; 3L0C; -. DR PDBsum; 3L0Y; -. DR PDBsum; 3PGL; -. DR PDBsum; 4YGY; -. DR PDBsum; 4YH1; -. DR PDBsum; 6DU3; -. DR AlphaFoldDB; Q9GZU7; -. DR SMR; Q9GZU7; -. DR BioGRID; 121804; 114. DR DIP; DIP-61246N; -. DR IntAct; Q9GZU7; 51. DR MINT; Q9GZU7; -. DR STRING; 9606.ENSP00000273062; -. DR BindingDB; Q9GZU7; -. DR ChEMBL; CHEMBL1795098; -. DR DrugBank; DB04156; Aspartate beryllium trifluoride. DR DrugBank; DB04272; Citric acid. DR DEPOD; CTDSP1; -. DR GlyCosmos; Q9GZU7; 1 site, 1 glycan. DR GlyGen; Q9GZU7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9GZU7; -. DR PhosphoSitePlus; Q9GZU7; -. DR SwissPalm; Q9GZU7; -. DR BioMuta; CTDSP1; -. DR DMDM; 17865510; -. DR EPD; Q9GZU7; -. DR jPOST; Q9GZU7; -. DR MassIVE; Q9GZU7; -. DR MaxQB; Q9GZU7; -. DR PaxDb; 9606-ENSP00000273062; -. DR PeptideAtlas; Q9GZU7; -. DR ProteomicsDB; 7655; -. DR ProteomicsDB; 80150; -. [Q9GZU7-1] DR ProteomicsDB; 80151; -. [Q9GZU7-2] DR Pumba; Q9GZU7; -. DR Antibodypedia; 34272; 490 antibodies from 33 providers. DR DNASU; 58190; -. DR Ensembl; ENST00000273062.7; ENSP00000273062.2; ENSG00000144579.9. [Q9GZU7-1] DR Ensembl; ENST00000710837.1; ENSP00000518515.1; ENSG00000144579.9. [Q9GZU7-2] DR GeneID; 58190; -. DR KEGG; hsa:58190; -. DR MANE-Select; ENST00000273062.7; ENSP00000273062.2; NM_021198.3; NP_067021.1. DR UCSC; uc002vhy.3; human. [Q9GZU7-1] DR AGR; HGNC:21614; -. DR CTD; 58190; -. DR DisGeNET; 58190; -. DR GeneCards; CTDSP1; -. DR HGNC; HGNC:21614; CTDSP1. DR HPA; ENSG00000144579; Low tissue specificity. DR MIM; 605323; gene. DR neXtProt; NX_Q9GZU7; -. DR OpenTargets; ENSG00000144579; -. DR PharmGKB; PA134938848; -. DR VEuPathDB; HostDB:ENSG00000144579; -. DR eggNOG; KOG1605; Eukaryota. DR GeneTree; ENSGT01040000240451; -. DR InParanoid; Q9GZU7; -. DR OMA; LFCCWRN; -. DR OrthoDB; 5473812at2759; -. DR PhylomeDB; Q9GZU7; -. DR TreeFam; TF313556; -. DR PathwayCommons; Q9GZU7; -. DR SignaLink; Q9GZU7; -. DR SIGNOR; Q9GZU7; -. DR BioGRID-ORCS; 58190; 32 hits in 1176 CRISPR screens. DR ChiTaRS; CTDSP1; human. DR EvolutionaryTrace; Q9GZU7; -. DR GeneWiki; CTDSP1; -. DR GenomeRNAi; 58190; -. DR Pharos; Q9GZU7; Tchem. DR PRO; PR:Q9GZU7; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9GZU7; Protein. DR Bgee; ENSG00000144579; Expressed in granulocyte and 187 other cell types or tissues. DR ExpressionAtlas; Q9GZU7; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IDA:UniProtKB. DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR CDD; cd07521; HAD_FCP1-like; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR IDEAL; IID00394; -. DR InterPro; IPR011948; Dullard_phosphatase. DR InterPro; IPR004274; FCP1_dom. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR040078; RNA_Pol_CTD_Phosphatase. DR NCBIfam; TIGR02251; HIF-SF_euk; 1. DR PANTHER; PTHR12210:SF139; CARBOXY-TERMINAL DOMAIN RNA POLYMERASE II POLYPEPTIDE A SMALL PHOSPHATASE 1; 1. DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1. DR Pfam; PF03031; NIF; 1. DR SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SMART; SM00577; CPDc; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR PROSITE; PS50969; FCP1; 1. DR Genevisible; Q9GZU7; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Hydrolase; Magnesium; KW Metal-binding; Nucleus; Protein phosphatase; Reference proteome. FT CHAIN 1..261 FT /note="Carboxy-terminal domain RNA polymerase II FT polypeptide A small phosphatase 1" FT /id="PRO_0000212572" FT DOMAIN 86..244 FT /note="FCP1 homology" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 96 FT /note="4-aspartylphosphate intermediate" FT /evidence="ECO:0000269|PubMed:15304220, FT ECO:0000269|PubMed:17157258" FT ACT_SITE 98 FT /note="Proton donor" FT /evidence="ECO:0000305|PubMed:15304220" FT BINDING 96 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15304220" FT BINDING 98 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15304220" FT BINDING 207 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15304220" FT SITE 152 FT /note="Transition state stabilizer" FT /evidence="ECO:0000305|PubMed:15304220" FT SITE 190 FT /note="Transition state stabilizer" FT /evidence="ECO:0000305|PubMed:15304220" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT VAR_SEQ 1..22 FT /note="MDSSAVITQISKEEARGPLRGK -> MVAAPWATQEQEEGRGIQPGDR (in FT isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_045865" FT VAR_SEQ 73 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:12721286, ECO:0000303|Ref.3" FT /id="VSP_045866" FT VARIANT 56 FT /note="A -> T (in dbSNP:rs2227249)" FT /id="VAR_049054" FT MUTAGEN 96 FT /note="D->E: No effect. Completely abolishes phosphatase FT activity; when associated with N-98." FT /evidence="ECO:0000269|PubMed:12721286" FT MUTAGEN 98 FT /note="D->N: Completely abolishes phosphatase activity; FT when associated with E-96." FT /evidence="ECO:0000269|PubMed:12721286" FT CONFLICT 180 FT /note="S -> F (in Ref. 3; BX446444)" FT /evidence="ECO:0000305" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:2GHT" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:2GHT" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:2GHT" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:2GHT" FT STRAND 113..120 FT /evidence="ECO:0007829|PDB:2GHT" FT STRAND 123..131 FT /evidence="ECO:0007829|PDB:2GHT" FT HELIX 135..145 FT /evidence="ECO:0007829|PDB:2GHT" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:2GHT" FT HELIX 156..166 FT /evidence="ECO:0007829|PDB:2GHT" FT STRAND 172..176 FT /evidence="ECO:0007829|PDB:2GHT" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:2GHT" FT STRAND 181..184 FT /evidence="ECO:0007829|PDB:2GHT" FT STRAND 187..189 FT /evidence="ECO:0007829|PDB:2GHT" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:2GHT" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:3L0C" FT HELIX 199..201 FT /evidence="ECO:0007829|PDB:2GHT" FT STRAND 202..205 FT /evidence="ECO:0007829|PDB:2GHT" FT HELIX 209..212 FT /evidence="ECO:0007829|PDB:2GHT" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:1TA0" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:4YH1" FT HELIX 233..244 FT /evidence="ECO:0007829|PDB:2GHT" FT HELIX 251..254 FT /evidence="ECO:0007829|PDB:2GHT" SQ SEQUENCE 261 AA; 29203 MW; 75A430BCA2748FEA CRC64; MDSSAVITQI SKEEARGPLR GKGDQKSAAS QKPRSRGILH SLFCCVCRDD GEALPAHSGA PLLVEENGAI PKQTPVQYLL PEAKAQDSDK ICVVIDLDET LVHSSFKPVN NADFIIPVEI DGVVHQVYVL KRPHVDEFLQ RMGELFECVL FTASLAKYAD PVADLLDKWG AFRARLFRES CVFHRGNYVK DLSRLGRDLR RVLILDNSPA SYVFHPDNAV PVASWFDNMS DTELHDLLPF FEQLSRVDDV YSVLRQPRPG S //