Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9NRX4

- PHP14_HUMAN

UniProt

Q9NRX4 - PHP14_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

14 kDa phosphohistidine phosphatase

Gene

PHPT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Exhibits phosphohistidine phosphatase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211Substrate
Active sitei53 – 531Proton acceptor1 Publication

GO - Molecular functioni

  1. calcium channel inhibitor activity Source: BHF-UCL
  2. ion channel binding Source: BHF-UCL
  3. phosphohistidine phosphatase activity Source: BHF-UCL
  4. phosphoprotein phosphatase activity Source: UniProtKB-KW

GO - Biological processi

  1. negative regulation of ATP citrate synthase activity Source: BHF-UCL
  2. negative regulation of lyase activity Source: BHF-UCL
  3. negative regulation of T cell receptor signaling pathway Source: BHF-UCL
  4. peptidyl-histidine dephosphorylation Source: BHF-UCL
  5. positive regulation of cell motility Source: BHF-UCL
  6. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
  7. protein dephosphorylation Source: BHF-UCL
  8. regulation of actin cytoskeleton reorganization Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
14 kDa phosphohistidine phosphatase (EC:3.1.3.-)
Alternative name(s):
Phosphohistidine phosphatase 1
Protein janus-A homolog
Gene namesi
Name:PHPT1
Synonyms:PHP14
ORF Names:CGI-202, HSPC141
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:30033. PHPT1.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211K → A: Decreased affinity for substrate and strongly reduced catalytic activity. 1 Publication
Mutagenesisi45 – 451R → A: Slightly decreased affinity for substrate, but no effect on catalytic activity. 2 Publications
Mutagenesisi53 – 531H → A: Loss of activity. 2 Publications
Mutagenesisi78 – 781R → A: Decreased affinity for substrate and reduced catalytic activity. 2 Publications
Mutagenesisi94 – 941S → A: Decreased affinity for substrate and strongly reduced catalytic activity.
Mutagenesisi102 – 1021H → A: Decreased affinity for substrate and slightly reduced catalytic activity. 2 Publications

Organism-specific databases

PharmGKBiPA134948141.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 12512414 kDa phosphohistidine phosphatasePRO_0000206152Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NRX4.
PaxDbiQ9NRX4.
PeptideAtlasiQ9NRX4.
PRIDEiQ9NRX4.

PTM databases

PhosphoSiteiQ9NRX4.

Expressioni

Tissue specificityi

Expressed abundantly in heart and skeletal muscle.

Gene expression databases

BgeeiQ9NRX4.
CleanExiHS_PHPT1.
ExpressionAtlasiQ9NRX4. baseline and differential.
GenevestigatoriQ9NRX4.

Organism-specific databases

HPAiCAB013584.
HPA020952.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi118854. 11 interactions.
DIPiDIP-48597N.
IntActiQ9NRX4. 2 interactions.
MINTiMINT-1394164.
STRINGi9606.ENSP00000247665.

Structurei

Secondary structure

1
125
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi11 – 144Combined sources
Beta strandi17 – 2812Combined sources
Helixi31 – 333Combined sources
Beta strandi40 – 467Combined sources
Helixi53 – 6614Combined sources
Beta strandi70 – 8213Combined sources
Turni83 – 864Combined sources
Beta strandi87 – 915Combined sources
Turni95 – 973Combined sources
Helixi102 – 11211Combined sources
Beta strandi116 – 1205Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AI6NMR-A1-125[»]
2HW4X-ray1.90A5-125[»]
2NMMX-ray2.70A/B/C1-125[»]
2OZWNMR-A1-125[»]
2OZXNMR-A1-125[»]
ProteinModelPortaliQ9NRX4.
SMRiQ9NRX4. Positions 1-125.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NRX4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 963Substrate binding

Sequence similaritiesi

Belongs to the janus family.Curated

Phylogenomic databases

eggNOGiNOG73026.
GeneTreeiENSGT00390000002738.
HOGENOMiHOG000231559.
HOVERGENiHBG053589.
InParanoidiQ9NRX4.
KOiK01112.
OMAiGFGRANH.
OrthoDBiEOG7S2215.
PhylomeDBiQ9NRX4.
TreeFamiTF315158.

Family and domain databases

InterProiIPR007702. Janus.
IPR028441. PHPT1.
[Graphical view]
PANTHERiPTHR12258:SF10. PTHR12258:SF10. 1 hit.
PfamiPF05005. Ocnus. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NRX4-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA
60 70 80 90 100
EYHADIYDKV SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA
110 120
QHAISTEKIK AKYPDYEVTW ANDGY
Length:125
Mass (Da):13,833
Last modified:October 1, 2000 - v1
Checksum:i24F0CA2BADB78478
GO
Isoform 2 (identifier: Q9NRX4-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:124
Mass (Da):13,672
Checksum:iB504A355D275D9C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141I → T in CAB66579. (PubMed:11230166)Curated
Sequence conflicti27 – 271V → I in CAB66579. (PubMed:11230166)Curated
Sequence conflicti79 – 791I → T in CAB66579. (PubMed:11230166)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei96 – 12530AYGPA…ANDGY → MRPTCVPLGASGPRIHHQGL WSCPARHFN in isoform 2. 1 PublicationVSP_041159Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48060.1. [Q9NRX4-2]
CCDS7009.1. [Q9NRX4-1]
RefSeqiNP_001129333.1. NM_001135861.2. [Q9NRX4-2]
NP_054891.2. NM_014172.5. [Q9NRX4-1]
UniGeneiHs.409834.
Hs.731711.

Genome annotation databases

EnsembliENST00000247665; ENSP00000247665; ENSG00000054148. [Q9NRX4-1]
ENST00000371661; ENSP00000360724; ENSG00000054148. [Q9NRX4-2]
GeneIDi29085.
KEGGihsa:29085.
UCSCiuc004cjq.4. human. [Q9NRX4-1]
uc011mei.2. human. [Q9NRX4-2]

Polymorphism databases

DMDMi25008934.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS48060.1. [Q9NRX4-2 ]
CCDS7009.1. [Q9NRX4-1 ]
RefSeqi NP_001129333.1. NM_001135861.2. [Q9NRX4-2 ]
NP_054891.2. NM_014172.5. [Q9NRX4-1 ]
UniGenei Hs.409834.
Hs.731711.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AI6 NMR - A 1-125 [» ]
2HW4 X-ray 1.90 A 5-125 [» ]
2NMM X-ray 2.70 A/B/C 1-125 [» ]
2OZW NMR - A 1-125 [» ]
2OZX NMR - A 1-125 [» ]
ProteinModelPortali Q9NRX4.
SMRi Q9NRX4. Positions 1-125.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118854. 11 interactions.
DIPi DIP-48597N.
IntActi Q9NRX4. 2 interactions.
MINTi MINT-1394164.
STRINGi 9606.ENSP00000247665.

PTM databases

PhosphoSitei Q9NRX4.

Polymorphism databases

DMDMi 25008934.

Proteomic databases

MaxQBi Q9NRX4.
PaxDbi Q9NRX4.
PeptideAtlasi Q9NRX4.
PRIDEi Q9NRX4.

Protocols and materials databases

DNASUi 29085.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000247665 ; ENSP00000247665 ; ENSG00000054148 . [Q9NRX4-1 ]
ENST00000371661 ; ENSP00000360724 ; ENSG00000054148 . [Q9NRX4-2 ]
GeneIDi 29085.
KEGGi hsa:29085.
UCSCi uc004cjq.4. human. [Q9NRX4-1 ]
uc011mei.2. human. [Q9NRX4-2 ]

Organism-specific databases

CTDi 29085.
GeneCardsi GC09P139743.
HGNCi HGNC:30033. PHPT1.
HPAi CAB013584.
HPA020952.
MIMi 610167. gene.
neXtProti NX_Q9NRX4.
PharmGKBi PA134948141.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG73026.
GeneTreei ENSGT00390000002738.
HOGENOMi HOG000231559.
HOVERGENi HBG053589.
InParanoidi Q9NRX4.
KOi K01112.
OMAi GFGRANH.
OrthoDBi EOG7S2215.
PhylomeDBi Q9NRX4.
TreeFami TF315158.

Miscellaneous databases

ChiTaRSi PHPT1. human.
EvolutionaryTracei Q9NRX4.
GeneWikii PHPT1.
GenomeRNAii 29085.
NextBioi 52068.
PROi Q9NRX4.
SOURCEi Search...

Gene expression databases

Bgeei Q9NRX4.
CleanExi HS_PHPT1.
ExpressionAtlasi Q9NRX4. baseline and differential.
Genevestigatori Q9NRX4.

Family and domain databases

InterProi IPR007702. Janus.
IPR028441. PHPT1.
[Graphical view ]
PANTHERi PTHR12258:SF10. PTHR12258:SF10. 1 hit.
Pfami PF05005. Ocnus. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.
    , 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. 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).

Entry informationi

Entry nameiPHP14_HUMAN
AccessioniPrimary (citable) accession number: Q9NRX4
Secondary accession number(s): B1AMX0, B1AMX1, Q9H0Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3