PHP14_HUMAN
ID PHP14_HUMAN Reviewed; 125 AA.
AC Q9NRX4; B1AMX0; B1AMX1; Q9H0Y3;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=14 kDa phosphohistidine phosphatase {ECO:0000303|PubMed:12383260};
DE EC=3.9.1.3 {ECO:0000269|PubMed:19836471, ECO:0000269|PubMed:25574816};
DE AltName: Full=Phosphohistidine phosphatase 1 {ECO:0000303|PubMed:25574816};
DE Short=PHPT1 {ECO:0000303|PubMed:25574816};
DE AltName: Full=Protein histidine phosphatase {ECO:0000303|PubMed:19836471};
DE Short=PHP {ECO:0000303|PubMed:19836471};
DE AltName: Full=Protein janus-A homolog;
GN Name=PHPT1; Synonyms=PHP14; ORFNames=CGI-202, HSPC141;
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] (ISOFORM 1), PROTEIN SEQUENCE OF 2-21; 49-59;
RP 88-108 AND 111-125, TISSUE SPECIFICITY, SUBUNIT, AND CHARACTERIZATION.
RC TISSUE=Embryonic kidney;
RX PubMed=12383260; DOI=10.1046/j.1432-1033.2002.03206.x;
RA Ek P., Pettersson G., Ek B., Gong F., Li J.-P., Zetterqvist O.;
RT "Identification and characterization of a mammalian 14-kDa phosphohistidine
RT phosphatase.";
RL Eur. J. Biochem. 269:5016-5023(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11342225; DOI=10.1016/s0167-4781(00)00295-5;
RA Lai C.-H., Chiu J.-Y., Lin W.-C.;
RT "Identification of the human crooked neck gene by comparative gene
RT identification.";
RL Biochim. Biophys. Acta 1517:449-454(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Lung;
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 MUTAGENESIS OF ARG-45; HIS-53; ARG-78 AND HIS-102.
RX PubMed=16219293; DOI=10.1016/j.bbrc.2005.09.134;
RA Ma R., Kanders E., Sundh U.B., Geng M., Ek P., Zetterqvist O., Li J.-P.;
RT "Mutational study of human phosphohistidine phosphatase: effect on
RT enzymatic activity.";
RL Biochem. Biophys. Res. Commun. 337:887-891(2005).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND ENZYME KINETICS.
RX PubMed=19836471; DOI=10.1016/j.bbapap.2009.10.007;
RA Attwood P.V., Ludwig K., Bergander K., Besant P.G., Adina-Zada A.,
RA Krieglstein J., Klumpp S.;
RT "Chemical phosphorylation of histidine-containing peptides based on the
RT sequence of histone H4 and their dephosphorylation by protein histidine
RT phosphatase.";
RL Biochim. Biophys. Acta 1804:199-205(2010).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25574816; DOI=10.3109/03009734.2014.996720;
RA Ek P., Ek B., Zetterqvist O.;
RT "Phosphohistidine phosphatase 1 (PHPT1) also dephosphorylates phospholysine
RT of chemically phosphorylated histone H1 and polylysine.";
RL Ups. J. Med. Sci. 120:20-27(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 5-125.
RX PubMed=16990267; DOI=10.1074/jbc.c600231200;
RA Busam R.D., Thorsell A.-G., Flores A., Hammarstroem M., Persson C.,
RA Hallberg B.M.;
RT "First structure of a eukaryotic phosphohistidine phosphatase.";
RL J. Biol. Chem. 281:33830-33834(2006).
RN [16]
RP STRUCTURE BY NMR IN COMPLEXES WITH PHOSPHATE, ACTIVE SITE, ENZYME ACTIVITY,
RP AND MUTAGENESIS OF LYS-21; ARG-45; HIS-53; ARG-78 AND HIS-102.
RX PubMed=18991813; DOI=10.1042/bj20081571;
RA Gong W., Li Y., Cui G., Hu J., Fang H., Jin C., Xia B.;
RT "Solution structure and catalytic mechanism of human protein histidine
RT phosphatase 1.";
RL Biochem. J. 418:337-344(2009).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of human phosphohistidine phosphatase. Northeast
RT structural genomics consortium target HR1409.";
RL Submitted (JAN-2007) to the PDB data bank.
CC -!- FUNCTION: Exhibits phosphohistidine phosphatase activity.
CC {ECO:0000269|PubMed:19836471, ECO:0000269|PubMed:25574816}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(pros)-phospho-L-histidyl-[protein] = L-histidyl-
CC [protein] + phosphate; Xref=Rhea:RHEA:47964, Rhea:RHEA-COMP:9745,
CC Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15377, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:64837; EC=3.9.1.3;
CC Evidence={ECO:0000269|PubMed:19836471, ECO:0000269|PubMed:25574816};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(tele)-phospho-L-histidyl-[protein] = L-histidyl-
CC [protein] + phosphate; Xref=Rhea:RHEA:47960, Rhea:RHEA-COMP:9745,
CC Rhea:RHEA-COMP:10719, ChEBI:CHEBI:15377, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83586; EC=3.9.1.3;
CC Evidence={ECO:0000269|PubMed:19836471, ECO:0000269|PubMed:25574816};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12383260}.
CC -!- INTERACTION:
CC Q9NRX4; P54253: ATXN1; NbExp=8; IntAct=EBI-740955, EBI-930964;
CC Q9NRX4; O15554: KCNN4; NbExp=2; IntAct=EBI-740955, EBI-2924473;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRX4-2; Sequence=VSP_041159;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in heart and skeletal muscle.
CC {ECO:0000269|PubMed:12383260}.
CC -!- SIMILARITY: Belongs to the janus family. {ECO:0000305}.
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DR EMBL; AF393504; AAN52504.1; -; mRNA.
DR EMBL; AF164795; AAF80759.1; -; mRNA.
DR EMBL; AF285119; AAG01156.1; -; mRNA.
DR EMBL; AL136644; CAB66579.1; -; mRNA.
DR EMBL; AL355987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88289.1; -; Genomic_DNA.
DR EMBL; BC024648; AAH24648.1; -; mRNA.
DR EMBL; BQ922335; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS48060.1; -. [Q9NRX4-2]
DR CCDS; CCDS7009.1; -. [Q9NRX4-1]
DR RefSeq; NP_001129333.1; NM_001135861.2. [Q9NRX4-2]
DR RefSeq; NP_054891.2; NM_014172.5. [Q9NRX4-1]
DR PDB; 2AI6; NMR; -; A=1-125.
DR PDB; 2HW4; X-ray; 1.90 A; A=5-125.
DR PDB; 2NMM; X-ray; 2.70 A; A/B/C=1-125.
DR PDB; 2OZW; NMR; -; A=1-125.
DR PDB; 2OZX; NMR; -; A=1-125.
DR PDBsum; 2AI6; -.
DR PDBsum; 2HW4; -.
DR PDBsum; 2NMM; -.
DR PDBsum; 2OZW; -.
DR PDBsum; 2OZX; -.
DR AlphaFoldDB; Q9NRX4; -.
DR BMRB; Q9NRX4; -.
DR SMR; Q9NRX4; -.
DR BioGRID; 118854; 51.
DR DIP; DIP-48597N; -.
DR IntAct; Q9NRX4; 8.
DR STRING; 9606.ENSP00000247665; -.
DR DEPOD; PHPT1; -.
DR iPTMnet; Q9NRX4; -.
DR MetOSite; Q9NRX4; -.
DR PhosphoSitePlus; Q9NRX4; -.
DR BioMuta; PHPT1; -.
DR DMDM; 25008934; -.
DR EPD; Q9NRX4; -.
DR jPOST; Q9NRX4; -.
DR MassIVE; Q9NRX4; -.
DR MaxQB; Q9NRX4; -.
DR PaxDb; Q9NRX4; -.
DR PeptideAtlas; Q9NRX4; -.
DR PRIDE; Q9NRX4; -.
DR ProteomicsDB; 82435; -. [Q9NRX4-1]
DR ProteomicsDB; 82436; -. [Q9NRX4-2]
DR TopDownProteomics; Q9NRX4-1; -. [Q9NRX4-1]
DR Antibodypedia; 18807; 382 antibodies from 31 providers.
DR DNASU; 29085; -.
DR Ensembl; ENST00000247665.12; ENSP00000247665.10; ENSG00000054148.18. [Q9NRX4-1]
DR Ensembl; ENST00000371661.5; ENSP00000360724.1; ENSG00000054148.18. [Q9NRX4-2]
DR GeneID; 29085; -.
DR KEGG; hsa:29085; -.
DR MANE-Select; ENST00000247665.12; ENSP00000247665.10; NM_014172.6; NP_054891.2.
DR UCSC; uc064xew.1; human. [Q9NRX4-1]
DR CTD; 29085; -.
DR DisGeNET; 29085; -.
DR GeneCards; PHPT1; -.
DR HGNC; HGNC:30033; PHPT1.
DR HPA; ENSG00000054148; Tissue enhanced (tongue).
DR MIM; 610167; gene.
DR neXtProt; NX_Q9NRX4; -.
DR OpenTargets; ENSG00000054148; -.
DR PharmGKB; PA134948141; -.
DR VEuPathDB; HostDB:ENSG00000054148; -.
DR eggNOG; ENOG502S4DR; Eukaryota.
DR GeneTree; ENSGT00390000002738; -.
DR HOGENOM; CLU_120717_0_1_1; -.
DR InParanoid; Q9NRX4; -.
DR OMA; MCTQTRA; -.
DR OrthoDB; 1529401at2759; -.
DR PhylomeDB; Q9NRX4; -.
DR TreeFam; TF315158; -.
DR BioCyc; MetaCyc:ENSG00000054148-MON; -.
DR BRENDA; 3.9.1.3; 2681.
DR PathwayCommons; Q9NRX4; -.
DR SignaLink; Q9NRX4; -.
DR BioGRID-ORCS; 29085; 21 hits in 1078 CRISPR screens.
DR ChiTaRS; PHPT1; human.
DR EvolutionaryTrace; Q9NRX4; -.
DR GeneWiki; PHPT1; -.
DR GenomeRNAi; 29085; -.
DR Pharos; Q9NRX4; Tbio.
DR PRO; PR:Q9NRX4; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9NRX4; protein.
DR Bgee; ENSG00000054148; Expressed in apex of heart and 155 other tissues.
DR ExpressionAtlas; Q9NRX4; baseline and differential.
DR Genevisible; Q9NRX4; HS.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0101006; F:protein histidine phosphatase activity; IDA:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:2000984; P:negative regulation of ATP citrate synthase activity; IDA:BHF-UCL.
DR GO; GO:0051350; P:negative regulation of lyase activity; IDA:BHF-UCL.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0035971; P:peptidyl-histidine dephosphorylation; IDA:BHF-UCL.
DR GO; GO:2000147; P:positive regulation of cell motility; IMP:BHF-UCL.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:BHF-UCL.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:BHF-UCL.
DR Gene3D; 3.50.20.20; -; 1.
DR InterPro; IPR007702; Janus.
DR InterPro; IPR038596; Janus_sf.
DR InterPro; IPR028441; PHPT1.
DR PANTHER; PTHR12258; PTHR12258; 1.
DR PANTHER; PTHR12258:SF10; PTHR12258:SF10; 1.
DR Pfam; PF05005; Ocnus; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Protein phosphatase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12383260,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..125
FT /note="14 kDa phosphohistidine phosphatase"
FT /id="PRO_0000206152"
FT ACT_SITE 53
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:18991813"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18991813"
FT BINDING 94..96
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18991813"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT VAR_SEQ 96..125
FT /note="AYGPAQHAISTEKIKAKYPDYEVTWANDGY -> MRPTCVPLGASGPRIHHQ
FT GLWSCPARHFN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041159"
FT MUTAGEN 21
FT /note="K->A: Decreased affinity for substrate and strongly
FT reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:18991813"
FT MUTAGEN 45
FT /note="R->A: Slightly decreased affinity for substrate, but
FT no effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:16219293,
FT ECO:0000269|PubMed:18991813"
FT MUTAGEN 53
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16219293,
FT ECO:0000269|PubMed:18991813"
FT MUTAGEN 78
FT /note="R->A: Decreased affinity for substrate and reduced
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:16219293,
FT ECO:0000269|PubMed:18991813"
FT MUTAGEN 94
FT /note="S->A: Decreased affinity for substrate and strongly
FT reduced catalytic activity."
FT MUTAGEN 102
FT /note="H->A: Decreased affinity for substrate and slightly
FT reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:16219293,
FT ECO:0000269|PubMed:18991813"
FT CONFLICT 14
FT /note="I -> T (in Ref. 4; CAB66579)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="V -> I (in Ref. 4; CAB66579)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="I -> T (in Ref. 4; CAB66579)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2HW4"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:2HW4"
FT STRAND 17..28
FT /evidence="ECO:0007829|PDB:2HW4"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2AI6"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:2HW4"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:2HW4"
FT STRAND 70..82
FT /evidence="ECO:0007829|PDB:2HW4"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:2HW4"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:2HW4"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2HW4"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:2HW4"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2HW4"
SQ SEQUENCE 125 AA; 13833 MW; 24F0CA2BADB78478 CRC64;
MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA EYHADIYDKV
SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA QHAISTEKIK AKYPDYEVTW
ANDGY
