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P78562

- PHEX_HUMAN

UniProt

P78562 - PHEX_HUMAN

Protein

Phosphate-regulating neutral endopeptidase

Gene

PHEX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Probably involved in bone and dentin mineralization and renal phosphate reabsorption.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi580 – 5801Zinc; catalyticPROSITE-ProRule annotation
    Active sitei581 – 5811PROSITE-ProRule annotation
    Metal bindingi584 – 5841Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi642 – 6421Zinc; catalyticPROSITE-ProRule annotation
    Active sitei646 – 6461Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-KW
    2. metalloendopeptidase activity Source: ProtInc
    3. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. bone mineralization Source: Ensembl
    2. cell-cell signaling Source: ProtInc
    3. cellular protein modification process Source: ProtInc
    4. organophosphate metabolic process Source: Ensembl
    5. proteolysis Source: UniProtKB
    6. skeletal system development Source: ProtInc

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Biomineralization

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM13.091.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphate-regulating neutral endopeptidase (EC:3.4.24.-)
    Alternative name(s):
    Metalloendopeptidase homolog PEX
    Vitamin D-resistant hypophosphatemic rickets protein
    X-linked hypophosphatemia protein
    Short name:
    HYP
    Gene namesi
    Name:PHEX
    Synonyms:PEX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8918. PHEX.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: Ensembl
    2. Golgi apparatus Source: Ensembl
    3. integral component of plasma membrane Source: ProtInc
    4. perinuclear region of cytoplasm Source: Ensembl
    5. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Hypophosphatemic rickets, X-linked dominant (XLHR) [MIM:307800]: A disorder characterized by impaired phosphate uptake in the kidney, which is likely to be caused by abnormal regulation of sodium phosphate cotransport in the proximal tubules. Clinical manifestations include skeletal deformities, growth failure, craniosynostosis, paravertebral calcifications, pseudofractures in lower extremities, and muscular hypotonia with onset in early childhood. X-linked hypophosphatemic rickets is the most common form of hypophosphatemia with an incidence of 1 in 20000.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti77 – 771C → S in XLHR. 1 Publication
    VAR_006738
    Natural varianti80 – 801F → S in XLHR; sporadic. 1 Publication
    VAR_010616
    Natural varianti85 – 851C → F in XLHR; sporadic. 1 Publication
    VAR_010617
    Natural varianti85 – 851C → R in XLHR. 1 Publication
    VAR_010618
    Natural varianti85 – 851C → Y in XLHR. 1 Publication
    VAR_006739
    Natural varianti138 – 1381L → P in XLHR. 1 Publication
    VAR_006740
    Natural varianti141 – 1411S → P in XLHR; sporadic. 1 Publication
    VAR_010619
    Natural varianti142 – 1421C → F in XLHR. 1 Publication
    VAR_010620
    Natural varianti160 – 1601L → R in XLHR. 1 Publication
    VAR_010621
    Natural varianti166 – 1661R → C in XLHR. 1 Publication
    VAR_006741
    Natural varianti237 – 2371D → G in XLHR; sporadic. 1 Publication
    VAR_010622
    Natural varianti252 – 2521F → S in XLHR. 1 Publication
    VAR_006742
    Natural varianti253 – 2531M → I in XLHR. 1 Publication
    VAR_006743
    Natural varianti317 – 3171Y → F in XLHR. 1 Publication
    VAR_010623
    Natural varianti341 – 3411Missing in XLHR; sporadic. 1 Publication
    VAR_010624
    Natural varianti444 – 4441W → WN in XLHR. 1 Publication
    VAR_010625
    Natural varianti530 – 5301W → C in XLHR. 1 Publication
    VAR_010626
    Natural varianti534 – 5341P → L in XLHR. 3 Publications
    VAR_006744
    Natural varianti555 – 5551L → P in XLHR. 1 Publication
    VAR_010627
    Natural varianti567 – 5671R → P in XLHR; sporadic. 1 Publication
    VAR_010628
    Natural varianti573 – 5731A → D in XLHR; sporadic. 1 Publication
    VAR_010629
    Natural varianti579 – 5791G → R in XLHR. 3 Publications
    VAR_006745
    Natural varianti579 – 5791G → V in XLHR. 1 Publication
    VAR_006746
    Natural varianti621 – 6211Q → R in XLHR. 1 Publication
    VAR_010630
    Natural varianti651 – 6511R → P in XLHR. 1 Publication
    VAR_010631
    Natural varianti680 – 6801N → K in XLHR; sporadic. 1 Publication
    VAR_010633
    Natural varianti680 – 6801Missing in XLHR. 1 Publication
    VAR_010632
    Natural varianti693 – 6931C → Y in XLHR; sporadic. 1 Publication
    VAR_010634
    Natural varianti720 – 7201A → T in XLHR. 1 Publication
    VAR_010635
    Natural varianti731 – 7311F → Y in XLHR. 1 Publication
    VAR_010636
    Natural varianti733 – 7331C → S in XLHR; sporadic. 1 Publication
    VAR_010637
    Natural varianti746 – 7461C → W in XLHR; sporadic. 1 Publication
    VAR_010638
    Natural varianti749 – 7491W → R in XLHR. 1 Publication
    VAR_010639

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi307800. phenotype.
    Orphaneti89936. X-linked hypophosphatemia.
    PharmGKBiPA33258.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 749749Phosphate-regulating neutral endopeptidasePRO_0000078228Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi71 – 711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi301 – 3011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi377 – 3771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi736 – 7361N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP78562.
    PRIDEiP78562.

    PTM databases

    PhosphoSiteiP78562.

    Expressioni

    Tissue specificityi

    Lymphocytes and fetal brain; not in adult brain, placenta, skeletal muscle and pancreas; not in adult and fetal heart, lung, liver and kidney.

    Gene expression databases

    ArrayExpressiP78562.
    BgeeiP78562.
    CleanExiHS_PHEX.
    GenevestigatoriP78562.

    Organism-specific databases

    HPAiHPA029582.

    Interactioni

    Protein-protein interaction databases

    BioGridi111270. 1 interaction.
    IntActiP78562. 1 interaction.
    STRINGi9606.ENSP00000368682.

    Structurei

    3D structure databases

    ProteinModelPortaliP78562.
    SMRiP78562. Positions 59-749.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini42 – 641600ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei21 – 4121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M13 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3590.
    HOGENOMiHOG000245574.
    HOVERGENiHBG005554.
    InParanoidiP78562.
    KOiK08636.
    OMAiKVGYPEF.
    OrthoDBiEOG7PZRWQ.
    PhylomeDBiP78562.
    TreeFamiTF315192.

    Family and domain databases

    Gene3Di3.40.390.10. 2 hits.
    InterProiIPR024079. MetalloPept_cat_dom.
    IPR000718. Peptidase_M13.
    IPR018497. Peptidase_M13_C.
    IPR008753. Peptidase_M13_N.
    [Graphical view]
    PANTHERiPTHR11733. PTHR11733. 1 hit.
    PfamiPF01431. Peptidase_M13. 1 hit.
    PF05649. Peptidase_M13_N. 1 hit.
    [Graphical view]
    PRINTSiPR00786. NEPRILYSIN.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P78562-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEAETGSSVE TGKKANRGTR IALVVFVGGT LVLGTILFLV SQGLLSLQAK    50
    QEYCLKPECI EAAAAILSKV NLSVDPCDNF FRFACDGWIS NNPIPEDMPS 100
    YGVYPWLRHN VDLKLKELLE KSISRRRDTE AIQKAKILYS SCMNEKAIEK 150
    ADAKPLLHIL RHSPFRWPVL ESNIGPEGVW SERKFSLLQT LATFRGQYSN 200
    SVFIRLYVSP DDKASNEHIL KLDQATLSLA VREDYLDNST EAKSYRDALY 250
    KFMVDTAVLL GANSSRAEHD MKSVLRLEIK IAEIMIPHEN RTSEAMYNKM 300
    NISELSAMIP QFDWLGYIKK VIDTRLYPHL KDISPSENVV VRVPQYFKDL 350
    FRILGSERKK TIANYLVWRM VYSRIPNLSR RFQYRWLEFS RVIQGTTTLL 400
    PQWDKCVNFI ESALPYVVGK MFVDVYFQED KKEMMEELVE GVRWAFIDML 450
    EKENEWMDAG TKRKAKEKAR AVLAKVGYPE FIMNDTHVNE DLKAIKFSEA 500
    DYFGNVLQTR KYLAQSDFFW LRKAVPKTEW FTNPTTVNAF YSASTNQIRF 550
    PAGELQKPFF WGTEYPRSLS YGAIGVIVGH EFTHGFDNNG RKYDKNGNLD 600
    PWWSTESEEK FKEKTKCMIN QYSNYYWKKA GLNVKGKRTL GENIADNGGL 650
    REAFRAYRKW INDRRQGLEE PLLPGITFTN NQLFFLSYAH VRCNSYRPEA 700
    AREQVQIGAH SPPQFRVNGA ISNFEEFQKA FNCPPNSTMN RGMDSCRLW 749
    Length:749
    Mass (Da):86,474
    Last modified:May 1, 1997 - v1
    Checksum:i7C4F9F3E2471C6A8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti363 – 3631A → D in AAC50552. (PubMed:7550339)Curated
    Sequence conflicti403 – 4031W → R in AAC50552. (PubMed:7550339)Curated
    Sequence conflicti641 – 6411G → A in AAC50552. (PubMed:7550339)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti77 – 771C → S in XLHR. 1 Publication
    VAR_006738
    Natural varianti80 – 801F → S in XLHR; sporadic. 1 Publication
    VAR_010616
    Natural varianti85 – 851C → F in XLHR; sporadic. 1 Publication
    VAR_010617
    Natural varianti85 – 851C → R in XLHR. 1 Publication
    VAR_010618
    Natural varianti85 – 851C → Y in XLHR. 1 Publication
    VAR_006739
    Natural varianti138 – 1381L → P in XLHR. 1 Publication
    VAR_006740
    Natural varianti141 – 1411S → P in XLHR; sporadic. 1 Publication
    VAR_010619
    Natural varianti142 – 1421C → F in XLHR. 1 Publication
    VAR_010620
    Natural varianti160 – 1601L → R in XLHR. 1 Publication
    VAR_010621
    Natural varianti166 – 1661R → C in XLHR. 1 Publication
    VAR_006741
    Natural varianti237 – 2371D → G in XLHR; sporadic. 1 Publication
    VAR_010622
    Natural varianti252 – 2521F → S in XLHR. 1 Publication
    VAR_006742
    Natural varianti253 – 2531M → I in XLHR. 1 Publication
    VAR_006743
    Natural varianti317 – 3171Y → F in XLHR. 1 Publication
    VAR_010623
    Natural varianti341 – 3411Missing in XLHR; sporadic. 1 Publication
    VAR_010624
    Natural varianti444 – 4441W → WN in XLHR. 1 Publication
    VAR_010625
    Natural varianti530 – 5301W → C in XLHR. 1 Publication
    VAR_010626
    Natural varianti534 – 5341P → L in XLHR. 3 Publications
    VAR_006744
    Natural varianti555 – 5551L → P in XLHR. 1 Publication
    VAR_010627
    Natural varianti567 – 5671R → P in XLHR; sporadic. 1 Publication
    VAR_010628
    Natural varianti573 – 5731A → D in XLHR; sporadic. 1 Publication
    VAR_010629
    Natural varianti579 – 5791G → R in XLHR. 3 Publications
    VAR_006745
    Natural varianti579 – 5791G → V in XLHR. 1 Publication
    VAR_006746
    Natural varianti621 – 6211Q → R in XLHR. 1 Publication
    VAR_010630
    Natural varianti651 – 6511R → P in XLHR. 1 Publication
    VAR_010631
    Natural varianti680 – 6801N → K in XLHR; sporadic. 1 Publication
    VAR_010633
    Natural varianti680 – 6801Missing in XLHR. 1 Publication
    VAR_010632
    Natural varianti693 – 6931C → Y in XLHR; sporadic. 1 Publication
    VAR_010634
    Natural varianti720 – 7201A → T in XLHR. 1 Publication
    VAR_010635
    Natural varianti731 – 7311F → Y in XLHR. 1 Publication
    VAR_010636
    Natural varianti733 – 7331C → S in XLHR; sporadic. 1 Publication
    VAR_010637
    Natural varianti746 – 7461C → W in XLHR; sporadic. 1 Publication
    VAR_010638
    Natural varianti749 – 7491W → R in XLHR. 1 Publication
    VAR_010639

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08111
    , Y08112, Y08113, Y08114, Y08115, Y08116, Y08117, Y08118, Y08119, Y08120, Y08121, Y08122, Y08123, Y08124, Y08125, Y08126, Y08127, Y08128, Y08129, Y08130, Y08131, Y08132 Genomic DNA. Translation: CAA69326.1.
    U75645 mRNA. Translation: AAB47749.1.
    U87284 mRNA. Translation: AAB47562.1.
    AD000712 mRNA. Translation: AAB51604.1.
    AH004966 Genomic DNA. Translation: AAB42219.1.
    U82970 mRNA. Translation: AAC24487.1.
    U73024 Genomic DNA. Translation: AAD08630.1.
    Y10196 Genomic DNA. Translation: CAA71258.1.
    BC105057 mRNA. Translation: AAI05058.1.
    BC105059 mRNA. Translation: AAI05060.1.
    U60475 mRNA. Translation: AAC50552.1.
    CCDSiCCDS14204.1.
    RefSeqiNP_000435.3. NM_000444.5.
    NP_001269683.1. NM_001282754.1.
    UniGeneiHs.495834.

    Genome annotation databases

    EnsembliENST00000379374; ENSP00000368682; ENSG00000102174.
    GeneIDi5251.
    KEGGihsa:5251.
    UCSCiuc004dah.3. human.

    Polymorphism databases

    DMDMi2499917.

    Cross-referencesi

    Web resourcesi

    PHEXdb

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08111
    , Y08112 , Y08113 , Y08114 , Y08115 , Y08116 , Y08117 , Y08118 , Y08119 , Y08120 , Y08121 , Y08122 , Y08123 , Y08124 , Y08125 , Y08126 , Y08127 , Y08128 , Y08129 , Y08130 , Y08131 , Y08132 Genomic DNA. Translation: CAA69326.1 .
    U75645 mRNA. Translation: AAB47749.1 .
    U87284 mRNA. Translation: AAB47562.1 .
    AD000712 mRNA. Translation: AAB51604.1 .
    AH004966 Genomic DNA. Translation: AAB42219.1 .
    U82970 mRNA. Translation: AAC24487.1 .
    U73024 Genomic DNA. Translation: AAD08630.1 .
    Y10196 Genomic DNA. Translation: CAA71258.1 .
    BC105057 mRNA. Translation: AAI05058.1 .
    BC105059 mRNA. Translation: AAI05060.1 .
    U60475 mRNA. Translation: AAC50552.1 .
    CCDSi CCDS14204.1.
    RefSeqi NP_000435.3. NM_000444.5.
    NP_001269683.1. NM_001282754.1.
    UniGenei Hs.495834.

    3D structure databases

    ProteinModelPortali P78562.
    SMRi P78562. Positions 59-749.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111270. 1 interaction.
    IntActi P78562. 1 interaction.
    STRINGi 9606.ENSP00000368682.

    Protein family/group databases

    MEROPSi M13.091.

    PTM databases

    PhosphoSitei P78562.

    Polymorphism databases

    DMDMi 2499917.

    Proteomic databases

    PaxDbi P78562.
    PRIDEi P78562.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379374 ; ENSP00000368682 ; ENSG00000102174 .
    GeneIDi 5251.
    KEGGi hsa:5251.
    UCSCi uc004dah.3. human.

    Organism-specific databases

    CTDi 5251.
    GeneCardsi GC0XP021960.
    GeneReviewsi PHEX.
    HGNCi HGNC:8918. PHEX.
    HPAi HPA029582.
    MIMi 300550. gene.
    307800. phenotype.
    neXtProti NX_P78562.
    Orphaneti 89936. X-linked hypophosphatemia.
    PharmGKBi PA33258.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3590.
    HOGENOMi HOG000245574.
    HOVERGENi HBG005554.
    InParanoidi P78562.
    KOi K08636.
    OMAi KVGYPEF.
    OrthoDBi EOG7PZRWQ.
    PhylomeDBi P78562.
    TreeFami TF315192.

    Miscellaneous databases

    ChiTaRSi PHEX. human.
    GeneWikii PHEX.
    GenomeRNAii 5251.
    NextBioi 20286.
    PROi P78562.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78562.
    Bgeei P78562.
    CleanExi HS_PHEX.
    Genevestigatori P78562.

    Family and domain databases

    Gene3Di 3.40.390.10. 2 hits.
    InterProi IPR024079. MetalloPept_cat_dom.
    IPR000718. Peptidase_M13.
    IPR018497. Peptidase_M13_C.
    IPR008753. Peptidase_M13_N.
    [Graphical view ]
    PANTHERi PTHR11733. PTHR11733. 1 hit.
    Pfami PF01431. Peptidase_M13. 1 hit.
    PF05649. Peptidase_M13_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00786. NEPRILYSIN.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic organization of the human PEX gene mutated in X-linked dominant hypophosphatemic rickets."
      Francis F., Strom T.M., Hennig S., Boeddrich A., Lorenz B., Brandau O., Mohnike K.L., Cagnoli M., Steffens C., Klages S., Borzym K., Pohl T., Oudet C.L., Econs M.J., Rowe P.S.N., Reinhardt R., Meitinger T., Lehrach H.
      Genome Res. 7:573-585(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS XLHR ARG-85; LEU-534; ARG-579 AND PRO-651.
    2. "Pex/PEX tissue distribution and evidence for a deletion in the 3' region of the Pex gene in X-linked hypophosphatemic mice."
      Beck L., Soumounou Y., Martel J., Krishnamurthy G., Gauthier C., Goodyer C.G., Tenenhouse H.S.
      J. Clin. Invest. 99:1200-1209(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning and sequencing of human PEX from a bone cDNA library: evidence for its developmental stage-specific regulation in osteoblasts."
      Guo R., Quarles L.D.
      J. Bone Miner. Res. 12:1009-1017(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Mutational analysis of the PEX gene in patients with X-linked hypophosphatemic rickets."
      Holm I.A., Huang X., Kunkel L.M.
      Am. J. Hum. Genet. 60:790-797(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS XLHR TYR-85; CYS-166; SER-252; ILE-253 AND VAL-579.
    6. Lipman M.L., Panda D., Henderson J.E., Shen Y., Goltzman D., Karaplis A.C.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    7. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
      Tissue: Brain.
    9. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-641.
    10. Cited for: VARIANTS XLHR SER-77; PRO-138; LEU-534 AND ARG-579.
    11. "A PHEX gene mutation is responsible for adult-onset vitamin D-resistant hypophosphatemic osteomalacia: evidence that the disorder is not a distinct entity from X-linked hypophosphatemic rickets."
      Econs M.J., Friedman N.E., Rowe P.S.N., Speer M.C., Francis F., Strom T.M., Oudet C.L., Smith J.A., Ninomiya J.T., Lee B.E., Bergen H.
      J. Clin. Endocrinol. Metab. 83:3459-3462(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XLHR PRO-555.
    12. Cited for: VARIANTS XLHR PHE-317; LEU-534; ARG-579; ARG-621; ASN-680 DEL; THR-720; TYR-731 AND ARG-749.
    13. "Non-random distribution of mutations in the PHEX gene, and under-detected missense mutations at non-conserved residues."
      Filisetti D., Ostermann G., von Bredow M., Strom T.M., Filler G., Ehrich J., Pannetier S., Garnier J.-M., Rowe P.S.N., Francis F., Julienne A., Hanauer A., Econs M.J., Oudet C.L.
      Eur. J. Hum. Genet. 7:615-619(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS XLHR SER-80; PHE-142; GLY-237; CYS-530; ASP-573; SER-733 AND TRP-746.
    14. "Identification of fifteen novel PHEX gene mutations in Finnish patients with hypophosphatemic rickets."
      Tyynismaa H., Kaitila I., Naentoe-Salonen K., Ala-Houhala M., Alitalo T.
      Hum. Mutat. 15:383-384(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS XLHR PHE-85; PRO-141; VAL-341 DEL; PRO-567; LYS-680 AND TYR-693.
    15. Cited for: VARIANTS XLHR ARG-160 AND ASN-444 INS.

    Entry informationi

    Entry nameiPHEX_HUMAN
    AccessioniPrimary (citable) accession number: P78562
    Secondary accession number(s): O00678
    , Q13646, Q2M325, Q93032, Q99827
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 146 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3