Full text data of PHPT1
PHPT1
(PHP14)
[Confidence: low (only semi-automatic identification from reviews)]
14 kDa phosphohistidine phosphatase; 3.1.3.- (Phosphohistidine phosphatase 1; Protein janus-A homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
14 kDa phosphohistidine phosphatase; 3.1.3.- (Phosphohistidine phosphatase 1; Protein janus-A homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NRX4
ID PHP14_HUMAN Reviewed; 125 AA.
AC Q9NRX4; B1AMX0; B1AMX1; Q9H0Y3;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=14 kDa phosphohistidine phosphatase;
DE EC=3.1.3.-;
DE AltName: Full=Phosphohistidine phosphatase 1;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-21;
RP 49-59; 88-108 AND 111-125, 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
RT phosphohistidine 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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
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 [13]
RP STRUCTURE BY NMR IN COMPLEXES WITH PHOSPHATE, ACTIVE SITE, ENZYME
RP ACTIVITY, AND MUTAGENESIS OF LYS-21; ARG-45; HIS-53; ARG-78 AND
RP 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 [14]
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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
CC muscle.
CC -!- SIMILARITY: Belongs to the janus family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; CAI12692.1; -; Genomic_DNA.
DR EMBL; AL355987; CAI12693.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88289.1; -; Genomic_DNA.
DR EMBL; BC024648; AAH24648.1; -; mRNA.
DR EMBL; BQ922335; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_054891.2; NM_014172.4.
DR UniGene; Hs.409834; -.
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 ProteinModelPortal; Q9NRX4; -.
DR SMR; Q9NRX4; 1-125.
DR DIP; DIP-48597N; -.
DR IntAct; Q9NRX4; 2.
DR MINT; MINT-1394164; -.
DR STRING; 9606.ENSP00000247665; -.
DR PhosphoSite; Q9NRX4; -.
DR DMDM; 25008934; -.
DR PaxDb; Q9NRX4; -.
DR PeptideAtlas; Q9NRX4; -.
DR PRIDE; Q9NRX4; -.
DR DNASU; 29085; -.
DR Ensembl; ENST00000247665; ENSP00000247665; ENSG00000054148.
DR Ensembl; ENST00000371661; ENSP00000360724; ENSG00000054148.
DR Ensembl; ENST00000545326; ENSP00000444757; ENSG00000054148.
DR GeneID; 29085; -.
DR KEGG; hsa:29085; -.
DR UCSC; uc004cjq.4; human.
DR CTD; 29085; -.
DR GeneCards; GC09P139743; -.
DR HGNC; HGNC:30033; PHPT1.
DR HPA; CAB013584; -.
DR HPA; HPA020952; -.
DR MIM; 610167; gene.
DR neXtProt; NX_Q9NRX4; -.
DR PharmGKB; PA134948141; -.
DR eggNOG; NOG73026; -.
DR HOGENOM; HOG000231559; -.
DR HOVERGEN; HBG053589; -.
DR KO; K01112; -.
DR OMA; EVTWADD; -.
DR OrthoDB; EOG7S2215; -.
DR PhylomeDB; Q9NRX4; -.
DR ChiTaRS; PHPT1; human.
DR EvolutionaryTrace; Q9NRX4; -.
DR GeneWiki; PHPT1; -.
DR GenomeRNAi; 29085; -.
DR NextBio; 52068; -.
DR PRO; PR:Q9NRX4; -.
DR Bgee; Q9NRX4; -.
DR CleanEx; HS_PHPT1; -.
DR Genevestigator; Q9NRX4; -.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0008969; F:phosphohistidine phosphatase activity; IDA:BHF-UCL.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
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:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:BHF-UCL.
DR InterPro; IPR007702; Janus.
DR InterPro; IPR028441; PHPT1.
DR PANTHER; PTHR12258:SF2; PTHR12258:SF2; 1.
DR Pfam; PF05005; Ocnus; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Protein phosphatase;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 125 14 kDa phosphohistidine phosphatase.
FT /FTId=PRO_0000206152.
FT REGION 94 96 Substrate binding.
FT ACT_SITE 53 53 Proton acceptor.
FT BINDING 21 21 Substrate.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 96 125 AYGPAQHAISTEKIKAKYPDYEVTWANDGY -> MRPTCVP
FT LGASGPRIHHQGLWSCPARHFN (in isoform 2).
FT /FTId=VSP_041159.
FT MUTAGEN 21 21 K->A: Decreased affinity for substrate
FT and strongly reduced catalytic activity.
FT MUTAGEN 45 45 R->A: Slightly decreased affinity for
FT substrate, but no effect on catalytic
FT activity.
FT MUTAGEN 53 53 H->A: Loss of activity.
FT MUTAGEN 78 78 R->A: Decreased affinity for substrate
FT and reduced catalytic activity.
FT MUTAGEN 94 94 S->A: Decreased affinity for substrate
FT and strongly reduced catalytic activity.
FT MUTAGEN 102 102 H->A: Decreased affinity for substrate
FT and slightly reduced catalytic activity.
FT CONFLICT 14 14 I -> T (in Ref. 4; CAB66579).
FT CONFLICT 27 27 V -> I (in Ref. 4; CAB66579).
FT CONFLICT 79 79 I -> T (in Ref. 4; CAB66579).
FT HELIX 6 8
FT STRAND 11 14
FT STRAND 17 28
FT HELIX 31 33
FT STRAND 40 46
FT HELIX 53 66
FT STRAND 70 82
FT TURN 83 86
FT STRAND 87 91
FT TURN 95 97
FT HELIX 102 112
FT STRAND 116 120
SQ SEQUENCE 125 AA; 13833 MW; 24F0CA2BADB78478 CRC64;
MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA EYHADIYDKV
SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA QHAISTEKIK AKYPDYEVTW
ANDGY
//
ID PHP14_HUMAN Reviewed; 125 AA.
AC Q9NRX4; B1AMX0; B1AMX1; Q9H0Y3;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=14 kDa phosphohistidine phosphatase;
DE EC=3.1.3.-;
DE AltName: Full=Phosphohistidine phosphatase 1;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-21;
RP 49-59; 88-108 AND 111-125, 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
RT phosphohistidine 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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
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 [13]
RP STRUCTURE BY NMR IN COMPLEXES WITH PHOSPHATE, ACTIVE SITE, ENZYME
RP ACTIVITY, AND MUTAGENESIS OF LYS-21; ARG-45; HIS-53; ARG-78 AND
RP 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 [14]
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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
CC muscle.
CC -!- SIMILARITY: Belongs to the janus family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; CAI12692.1; -; Genomic_DNA.
DR EMBL; AL355987; CAI12693.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88289.1; -; Genomic_DNA.
DR EMBL; BC024648; AAH24648.1; -; mRNA.
DR EMBL; BQ922335; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_054891.2; NM_014172.4.
DR UniGene; Hs.409834; -.
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 ProteinModelPortal; Q9NRX4; -.
DR SMR; Q9NRX4; 1-125.
DR DIP; DIP-48597N; -.
DR IntAct; Q9NRX4; 2.
DR MINT; MINT-1394164; -.
DR STRING; 9606.ENSP00000247665; -.
DR PhosphoSite; Q9NRX4; -.
DR DMDM; 25008934; -.
DR PaxDb; Q9NRX4; -.
DR PeptideAtlas; Q9NRX4; -.
DR PRIDE; Q9NRX4; -.
DR DNASU; 29085; -.
DR Ensembl; ENST00000247665; ENSP00000247665; ENSG00000054148.
DR Ensembl; ENST00000371661; ENSP00000360724; ENSG00000054148.
DR Ensembl; ENST00000545326; ENSP00000444757; ENSG00000054148.
DR GeneID; 29085; -.
DR KEGG; hsa:29085; -.
DR UCSC; uc004cjq.4; human.
DR CTD; 29085; -.
DR GeneCards; GC09P139743; -.
DR HGNC; HGNC:30033; PHPT1.
DR HPA; CAB013584; -.
DR HPA; HPA020952; -.
DR MIM; 610167; gene.
DR neXtProt; NX_Q9NRX4; -.
DR PharmGKB; PA134948141; -.
DR eggNOG; NOG73026; -.
DR HOGENOM; HOG000231559; -.
DR HOVERGEN; HBG053589; -.
DR KO; K01112; -.
DR OMA; EVTWADD; -.
DR OrthoDB; EOG7S2215; -.
DR PhylomeDB; Q9NRX4; -.
DR ChiTaRS; PHPT1; human.
DR EvolutionaryTrace; Q9NRX4; -.
DR GeneWiki; PHPT1; -.
DR GenomeRNAi; 29085; -.
DR NextBio; 52068; -.
DR PRO; PR:Q9NRX4; -.
DR Bgee; Q9NRX4; -.
DR CleanEx; HS_PHPT1; -.
DR Genevestigator; Q9NRX4; -.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0008969; F:phosphohistidine phosphatase activity; IDA:BHF-UCL.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
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:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:BHF-UCL.
DR InterPro; IPR007702; Janus.
DR InterPro; IPR028441; PHPT1.
DR PANTHER; PTHR12258:SF2; PTHR12258:SF2; 1.
DR Pfam; PF05005; Ocnus; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Protein phosphatase;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 125 14 kDa phosphohistidine phosphatase.
FT /FTId=PRO_0000206152.
FT REGION 94 96 Substrate binding.
FT ACT_SITE 53 53 Proton acceptor.
FT BINDING 21 21 Substrate.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 96 125 AYGPAQHAISTEKIKAKYPDYEVTWANDGY -> MRPTCVP
FT LGASGPRIHHQGLWSCPARHFN (in isoform 2).
FT /FTId=VSP_041159.
FT MUTAGEN 21 21 K->A: Decreased affinity for substrate
FT and strongly reduced catalytic activity.
FT MUTAGEN 45 45 R->A: Slightly decreased affinity for
FT substrate, but no effect on catalytic
FT activity.
FT MUTAGEN 53 53 H->A: Loss of activity.
FT MUTAGEN 78 78 R->A: Decreased affinity for substrate
FT and reduced catalytic activity.
FT MUTAGEN 94 94 S->A: Decreased affinity for substrate
FT and strongly reduced catalytic activity.
FT MUTAGEN 102 102 H->A: Decreased affinity for substrate
FT and slightly reduced catalytic activity.
FT CONFLICT 14 14 I -> T (in Ref. 4; CAB66579).
FT CONFLICT 27 27 V -> I (in Ref. 4; CAB66579).
FT CONFLICT 79 79 I -> T (in Ref. 4; CAB66579).
FT HELIX 6 8
FT STRAND 11 14
FT STRAND 17 28
FT HELIX 31 33
FT STRAND 40 46
FT HELIX 53 66
FT STRAND 70 82
FT TURN 83 86
FT STRAND 87 91
FT TURN 95 97
FT HELIX 102 112
FT STRAND 116 120
SQ SEQUENCE 125 AA; 13833 MW; 24F0CA2BADB78478 CRC64;
MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA EYHADIYDKV
SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA QHAISTEKIK AKYPDYEVTW
ANDGY
//
MIM
610167
*RECORD*
*FIELD* NO
610167
*FIELD* TI
*610167 PHOSPHOHISTIDINE PHOSPHATASE 1; PHPT1
;;SEX-REGULATED PROTEIN JANUS-A
*FIELD* TX
read more
DESCRIPTION
PHPT1 is an EDTA-insensitive phosphohistidine phosphatase that catalyzes
the dephosphorylation of phosphopeptide I (Ek et al., 2002).
CLONING
By database analysis with partial peptide sequences of a
phosphohistidine phosphatase purified from porcine liver cytosol as
probe, Ek et al. (2002) identified a homologous human sequence from
adrenal gland. Using PCR techniques, they cloned a full-length human
PHPT1 cDNA from embryonic kidney (HEK293) cells. The deduced 125-amino
acid PHPT1 protein migrated as a single, approximately 14 kD band by
SDS-PAGE. Northern blot analysis detected a 0.6-kb transcript, with
highest expression in heart and skeletal muscle and lower expression in
several other tissues including pancreas, liver, and kidney.
GENE FUNCTION
Ek et al. (2002) found that recombinant PHPT1 overexpressed and purified
from bacteria displayed specific phosphohistidine phosphatase activity
toward phosphopeptide I. No activity was detected towards phosphoserine,
phosphothreonine, or phosphotyrosine peptides.
GENE STRUCTURE
Ek et al. (2002) determined that the PHPT1 gene contains 3 exons.
MAPPING
By sequence analysis, Ek et al. (2002) mapped the PHPT1 gene to
chromosome 9q34.3.
*FIELD* RF
1. Ek, P.; Pettersson, G.; Ek, B.; Gong, F.; Li, J.-P.; Zetterqvist,
O.: Identification and characterization of a mammalian 14-kDa phosphohistidine
phosphatase. Europ. J. Biochem. 269: 5016-5023, 2002.
*FIELD* CD
Dorothy S. Reilly: 6/7/2006
*FIELD* ED
carol: 06/08/2006
carol: 6/8/2006
*RECORD*
*FIELD* NO
610167
*FIELD* TI
*610167 PHOSPHOHISTIDINE PHOSPHATASE 1; PHPT1
;;SEX-REGULATED PROTEIN JANUS-A
*FIELD* TX
read more
DESCRIPTION
PHPT1 is an EDTA-insensitive phosphohistidine phosphatase that catalyzes
the dephosphorylation of phosphopeptide I (Ek et al., 2002).
CLONING
By database analysis with partial peptide sequences of a
phosphohistidine phosphatase purified from porcine liver cytosol as
probe, Ek et al. (2002) identified a homologous human sequence from
adrenal gland. Using PCR techniques, they cloned a full-length human
PHPT1 cDNA from embryonic kidney (HEK293) cells. The deduced 125-amino
acid PHPT1 protein migrated as a single, approximately 14 kD band by
SDS-PAGE. Northern blot analysis detected a 0.6-kb transcript, with
highest expression in heart and skeletal muscle and lower expression in
several other tissues including pancreas, liver, and kidney.
GENE FUNCTION
Ek et al. (2002) found that recombinant PHPT1 overexpressed and purified
from bacteria displayed specific phosphohistidine phosphatase activity
toward phosphopeptide I. No activity was detected towards phosphoserine,
phosphothreonine, or phosphotyrosine peptides.
GENE STRUCTURE
Ek et al. (2002) determined that the PHPT1 gene contains 3 exons.
MAPPING
By sequence analysis, Ek et al. (2002) mapped the PHPT1 gene to
chromosome 9q34.3.
*FIELD* RF
1. Ek, P.; Pettersson, G.; Ek, B.; Gong, F.; Li, J.-P.; Zetterqvist,
O.: Identification and characterization of a mammalian 14-kDa phosphohistidine
phosphatase. Europ. J. Biochem. 269: 5016-5023, 2002.
*FIELD* CD
Dorothy S. Reilly: 6/7/2006
*FIELD* ED
carol: 06/08/2006
carol: 6/8/2006