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Q9NRX4 (PHP14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
14 kDa phosphohistidine phosphatase

EC=3.1.3.-
Alternative name(s):
Phosphohistidine phosphatase 1
Protein janus-A homolog
Gene names
Name:PHPT1
Synonyms:PHP14
ORF Names:CGI-202, HSPC141
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length125 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exhibits phosphohistidine phosphatase activity.

Subunit structure

Monomer.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed abundantly in heart and skeletal muscle.

Sequence similarities

Belongs to the janus family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of ATP citrate synthase activity

Inferred from direct assay PubMed 18656514. Source: BHF-UCL

negative regulation of T cell receptor signaling pathway

Inferred from mutant phenotype PubMed 18796614. Source: BHF-UCL

negative regulation of lyase activity

Inferred from direct assay PubMed 20110805PubMed 20501872. Source: BHF-UCL

peptidyl-histidine dephosphorylation

Inferred from direct assay Ref.8PubMed 19138678. Source: BHF-UCL

positive regulation of cell motility

Inferred from mutant phenotype PubMed 19344975. Source: BHF-UCL

positive regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Inferred from direct assay PubMed 20501872. Source: BHF-UCL

regulation of actin cytoskeleton reorganization

Inferred from mutant phenotype PubMed 19344975. Source: BHF-UCL

   Cellular_componentcytosol

Inferred from direct assay PubMed 20501872. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

   Molecular_functioncalcium channel inhibitor activity

Inferred from direct assay PubMed 18796614. Source: BHF-UCL

ion channel binding

Inferred from physical interaction PubMed 18796614. Source: BHF-UCL

phosphohistidine phosphatase activity

Inferred from direct assay Ref.8PubMed 19138678PubMed 20501872. Source: BHF-UCL

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NRX4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NRX4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     96-125: AYGPAQHAISTEKIKAKYPDYEVTWANDGY → MRPTCVPLGASGPRIHHQGLWSCPARHFN

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.9
Chain2 – 12512414 kDa phosphohistidine phosphatase
PRO_0000206152

Regions

Region94 – 963Substrate binding

Sites

Active site531Proton acceptor Ref.14
Binding site211Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.11 Ref.12

Natural variations

Alternative sequence96 – 12530AYGPA…ANDGY → MRPTCVPLGASGPRIHHQGL WSCPARHFN in isoform 2.
VSP_041159

Experimental info

Mutagenesis211K → A: Decreased affinity for substrate and strongly reduced catalytic activity. Ref.14
Mutagenesis451R → A: Slightly decreased affinity for substrate, but no effect on catalytic activity. Ref.8 Ref.14
Mutagenesis531H → A: Loss of activity. Ref.8 Ref.14
Mutagenesis781R → A: Decreased affinity for substrate and reduced catalytic activity. Ref.8 Ref.14
Mutagenesis941S → A: Decreased affinity for substrate and strongly reduced catalytic activity.
Mutagenesis1021H → A: Decreased affinity for substrate and slightly reduced catalytic activity. Ref.8 Ref.14
Sequence conflict141I → T in CAB66579. Ref.4
Sequence conflict271V → I in CAB66579. Ref.4
Sequence conflict791I → T in CAB66579. Ref.4

Secondary structure

....................... 125
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 24F0CA2BADB78478

FASTA12513,833
        10         20         30         40         50         60 
MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA EYHADIYDKV 

        70         80         90        100        110        120 
SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA QHAISTEKIK AKYPDYEVTW 


ANDGY 

« Hide

Isoform 2 [UniParc].

Checksum: B504A355D275D9C6
Show »

FASTA12413,672

References

« Hide 'large scale' references
[1]"Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase."
Ek P., Pettersson G., Ek B., Gong F., Li J.-P., Zetterqvist O.
Eur. J. Biochem. 269:5016-5023(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-21; 49-59; 88-108 AND 111-125, CHARACTERIZATION.
Tissue: Embryonic kidney.
[2]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adrenal gland.
[3]"Identification of the human crooked neck gene by comparative gene identification."
Lai C.-H., Chiu J.-Y., Lin W.-C.
Biochim. Biophys. Acta 1517:449-454(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[5]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Lung.
[8]"Mutational study of human phosphohistidine phosphatase: effect on enzymatic activity."
Ma R., Kanders E., Sundh U.B., Geng M., Ek P., Zetterqvist O., Li J.-P.
Biochem. Biophys. Res. Commun. 337:887-891(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-45; HIS-53; ARG-78 AND HIS-102.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"First structure of a eukaryotic phosphohistidine phosphatase."
Busam R.D., Thorsell A.-G., Flores A., Hammarstroem M., Persson C., Hallberg B.M.
J. Biol. Chem. 281:33830-33834(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 5-125.
[14]"Solution structure and catalytic mechanism of human protein histidine phosphatase 1."
Gong W., Li Y., Cui G., Hu J., Fang H., Jin C., Xia B.
Biochem. J. 418:337-344(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEXES WITH PHOSPHATE, ACTIVE SITE, ENZYME ACTIVITY, MUTAGENESIS OF LYS-21; ARG-45; HIS-53; ARG-78 AND HIS-102.
[15]"Crystal structure of human phosphohistidine phosphatase. Northeast structural genomics consortium target HR1409."
Northeast structural genomics consortium (NESG)
Submitted (JAN-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF393504 mRNA. Translation: AAN52504.1.
AF164795 mRNA. Translation: AAF80759.1.
AF285119 mRNA. Translation: AAG01156.1.
AL136644 mRNA. Translation: CAB66579.1.
AL355987 Genomic DNA. Translation: CAI12692.1.
AL355987 Genomic DNA. Translation: CAI12693.1.
CH471090 Genomic DNA. Translation: EAW88289.1.
BC024648 mRNA. Translation: AAH24648.1.
BQ922335 mRNA. No translation available.
CCDSCCDS48060.1. [Q9NRX4-2]
CCDS7009.1. [Q9NRX4-1]
RefSeqNP_001129333.1. NM_001135861.2. [Q9NRX4-2]
NP_054891.2. NM_014172.5. [Q9NRX4-1]
UniGeneHs.409834.
Hs.731711.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AI6NMR-A1-125[»]
2HW4X-ray1.90A5-125[»]
2NMMX-ray2.70A/B/C1-125[»]
2OZWNMR-A1-125[»]
2OZXNMR-A1-125[»]
ProteinModelPortalQ9NRX4.
SMRQ9NRX4. Positions 1-125.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118854. 11 interactions.
DIPDIP-48597N.
IntActQ9NRX4. 2 interactions.
MINTMINT-1394164.
STRING9606.ENSP00000247665.

PTM databases

PhosphoSiteQ9NRX4.

Polymorphism databases

DMDM25008934.

Proteomic databases

MaxQBQ9NRX4.
PaxDbQ9NRX4.
PeptideAtlasQ9NRX4.
PRIDEQ9NRX4.

Protocols and materials databases

DNASU29085.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247665; ENSP00000247665; ENSG00000054148. [Q9NRX4-1]
ENST00000371661; ENSP00000360724; ENSG00000054148. [Q9NRX4-2]
ENST00000545326; ENSP00000444757; ENSG00000054148. [Q9NRX4-2]
GeneID29085.
KEGGhsa:29085.
UCSCuc004cjq.4. human. [Q9NRX4-1]
uc011mei.2. human. [Q9NRX4-2]

Organism-specific databases

CTD29085.
GeneCardsGC09P139743.
HGNCHGNC:30033. PHPT1.
HPACAB013584.
HPA020952.
MIM610167. gene.
neXtProtNX_Q9NRX4.
PharmGKBPA134948141.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG73026.
HOGENOMHOG000231559.
HOVERGENHBG053589.
KOK01112.
OMAGFGRANH.
OrthoDBEOG7S2215.
PhylomeDBQ9NRX4.
TreeFamTF315158.

Gene expression databases

BgeeQ9NRX4.
CleanExHS_PHPT1.
GenevestigatorQ9NRX4.

Family and domain databases

InterProIPR007702. Janus.
IPR028441. PHPT1.
[Graphical view]
PANTHERPTHR12258:SF10. PTHR12258:SF10. 1 hit.
PfamPF05005. Ocnus. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPHPT1. human.
EvolutionaryTraceQ9NRX4.
GeneWikiPHPT1.
GenomeRNAi29085.
NextBio52068.
PROQ9NRX4.
SOURCESearch...

Entry information

Entry namePHP14_HUMAN
AccessionPrimary (citable) accession number: Q9NRX4
Secondary accession number(s): B1AMX0, B1AMX1, Q9H0Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM