CTDS1_HUMAN
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 03-AUG-2022, entry version 177.
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; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-751587, EBI-12000762;
CC Q9GZU7; Q8TBN0: RAB3IL1; NbExp=3; IntAct=EBI-751587, EBI-743796;
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};
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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; 50.
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 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; Q9GZU7; -.
DR PeptideAtlas; Q9GZU7; -.
DR PRIDE; Q9GZU7; -.
DR ProteomicsDB; 7655; -.
DR ProteomicsDB; 80150; -. [Q9GZU7-1]
DR ProteomicsDB; 80151; -. [Q9GZU7-2]
DR Antibodypedia; 34272; 425 antibodies from 33 providers.
DR DNASU; 58190; -.
DR Ensembl; ENST00000273062.7; ENSP00000273062.2; ENSG00000144579.8. [Q9GZU7-1]
DR Ensembl; ENST00000443891.5; ENSP00000392248.1; ENSG00000144579.8. [Q9GZU7-3]
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 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; CLCHDES; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; Q9GZU7; -.
DR TreeFam; TF313556; -.
DR PathwayCommons; Q9GZU7; -.
DR SignaLink; Q9GZU7; -.
DR SIGNOR; Q9GZU7; -.
DR BioGRID-ORCS; 58190; 31 hits in 1083 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 185 other tissues.
DR ExpressionAtlas; Q9GZU7; baseline and differential.
DR Genevisible; Q9GZU7; HS.
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:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
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 Gene3D; 3.40.50.1000; -; 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 Pfam; PF03031; NIF; 1.
DR SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02251; HIF-SF_euk; 1.
DR PROSITE; PS50969; FCP1; 1.
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
