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Q9GZV9

- FGF23_HUMAN

UniProt

Q9GZV9 - FGF23_HUMAN

Protein

Fibroblast growth factor 23

Gene

FGF23

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Regulator of phosphate homeostasis. Inhibits renal tubular phosphate transport by reducing SLC34A1 levels. Upregulates EGR1 expression in the presence of KL By similarity. Acts directly on the parathyroid to decrease PTH secretion By similarity. Regulator of vitamin-D metabolism. Negatively regulates osteoblast differentiation and matrix mineralization.By similarity5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei179 – 1802Cleavage; by proprotein convertases

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. cellular phosphate ion homeostasis Source: Ensembl
    3. epidermal growth factor receptor signaling pathway Source: Reactome
    4. Fc-epsilon receptor signaling pathway Source: Reactome
    5. fibroblast growth factor receptor signaling pathway Source: Reactome
    6. innate immune response Source: Reactome
    7. insulin receptor signaling pathway Source: Reactome
    8. negative regulation of bone mineralization Source: UniProtKB
    9. negative regulation of hormone secretion Source: UniProtKB
    10. negative regulation of osteoblast differentiation Source: UniProtKB
    11. neurotrophin TRK receptor signaling pathway Source: Reactome
    12. phosphate-containing compound metabolic process Source: Ensembl
    13. phosphate ion homeostasis Source: UniProtKB
    14. phosphatidylinositol-mediated signaling Source: Reactome
    15. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
    16. positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway Source: Ensembl
    17. positive regulation of transcription, DNA-templated Source: Ensembl
    18. positive regulation of vitamin D 24-hydroxylase activity Source: UniProtKB
    19. regulation of phosphate transport Source: UniProtKB
    20. vitamin D catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Growth factor

    Keywords - Biological processi

    Differentiation

    Enzyme and pathway databases

    ReactomeiREACT_111184. Negative regulation of FGFR signaling.
    REACT_120863. Activated point mutants of FGFR2.
    REACT_121153. Signaling by activated point mutants of FGFR1.
    REACT_121249. Signaling by FGFR3 mutants.
    REACT_121337. Signaling by activated point mutants of FGFR3.
    REACT_121398. Signaling by FGFR mutants.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_21247. FRS2-mediated cascade.
    REACT_21270. PI-3K cascade.
    REACT_21310. Phospholipase C-mediated cascade.
    REACT_21374. SHC-mediated cascade.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_9413. FGFR2c ligand binding and activation.
    REACT_9452. FGFR4 ligand binding and activation.
    REACT_9484. FGFR1c and Klotho ligand binding and activation.
    REACT_9510. FGFR3c ligand binding and activation.
    REACT_9515. FGFR1c ligand binding and activation.
    REACT_976. PI3K Cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibroblast growth factor 23
    Short name:
    FGF-23
    Alternative name(s):
    Phosphatonin
    Tumor-derived hypophosphatemia-inducing factor
    Cleaved into the following 2 chains:
    Gene namesi
    Name:FGF23
    Synonyms:HYPF
    ORF Names:UNQ3027/PRO9828
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:3680. FGF23.

    Subcellular locationi

    Secreted 1 Publication
    Note: Secretion is dependent on O-glycosylation.

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Hypophosphatemic rickets, autosomal dominant (ADHR) [MIM:193100]: A disease characterized by isolated renal phosphate wasting, hypophosphatemia, and inappropriately normal 1,25-dihydroxyvitamin D3 (calcitriol) levels. Patients frequently present with bone pain, rickets, and tooth abscesses.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti176 – 1761R → Q in ADHR; partially resistant to cleavage by furin. 1 Publication
    VAR_010717
    Natural varianti179 – 1791R → Q in ADHR; C-terminal processing is abolished; reduced proteolysis by PHEX; resistant to cleavage by furin. 1 Publication
    VAR_010719
    Natural varianti179 – 1791R → W in ADHR; C-terminal processing is abolished. 1 Publication
    Corresponds to variant rs28937882 [ dbSNP | Ensembl ].
    VAR_010718
    Tumoral calcinosis, hyperphosphatemic, familial (HFTC) [MIM:211900]: A severe metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients manifest recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711S → G in HFTC; only the C-terminal fragment is secreted, whereas the intact protein is retained in the Golgi complex. 1 Publication
    VAR_023831

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi193100. phenotype.
    211900. phenotype.
    Orphaneti89937. Autosomal dominant hypophosphatemic rickets.
    306661. Hypercalcemic tumoral calcinosis.
    PharmGKBiPA28119.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 251227Fibroblast growth factor 23PRO_0000008998Add
    BLAST
    Chaini25 – 179155Fibroblast growth factor 23 N-terminal peptidePRO_0000352875Add
    BLAST
    Chaini180 – 25172Fibroblast growth factor 23 C-terminal peptidePRO_0000352876Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi95 ↔ 113
    Glycosylationi178 – 1781O-linked (GalNAc)1 Publication

    Post-translational modificationi

    Following secretion this protein is inactivated by cleavage into a N-terminal fragment and a C-terminal fragment. The processing is effected by proprotein convertases.
    O-glycosylated by GALT3. Glycosylation is necessary for secretion; it blocks processing by proprotein convertases when the O-glycan is alpha 2,6-sialylated. Competition between proprotein convertase cleavage and block of cleavage by O-glycosylation determines the level of secreted active FGF23.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9GZV9.
    PRIDEiQ9GZV9.

    PTM databases

    PhosphoSiteiQ9GZV9.

    Expressioni

    Tissue specificityi

    Expressed in osteogenic cells particularly during phases of active bone remodeling. In adult trabecular bone, expressed in osteocytes and flattened bone-lining cells (inactive osteoblasts).1 Publication

    Gene expression databases

    BgeeiQ9GZV9.
    CleanExiHS_FGF23.
    GenevestigatoriQ9GZV9.

    Interactioni

    Subunit structurei

    Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by KL and heparan sulfate glycosaminoglycans that function as coreceptors By similarity.By similarity

    Protein-protein interaction databases

    BioGridi113748. 1 interaction.
    DIPiDIP-58507N.
    IntActiQ9GZV9. 1 interaction.
    STRINGi9606.ENSP00000237837.

    Structurei

    Secondary structure

    1
    251
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 434
    Beta strandi47 – 493
    Beta strandi52 – 554
    Beta strandi61 – 666
    Turni69 – 713
    Beta strandi73 – 775
    Helixi79 – 813
    Beta strandi82 – 876
    Turni88 – 914
    Beta strandi92 – 965
    Beta strandi102 – 1076
    Turni110 – 1123
    Beta strandi115 – 1195
    Beta strandi125 – 1284
    Turni130 – 1323
    Beta strandi138 – 1403
    Helixi153 – 1553
    Beta strandi157 – 1615
    Helixi166 – 1683

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P39X-ray1.50A25-179[»]
    ProteinModelPortaliQ9GZV9.
    SMRiQ9GZV9. Positions 29-170.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9GZV9.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG270405.
    HOGENOMiHOG000112573.
    HOVERGENiHBG051613.
    InParanoidiQ9GZV9.
    KOiK04358.
    OMAiDVYHSPQ.
    OrthoDBiEOG71K63W.
    PhylomeDBiQ9GZV9.
    TreeFamiTF335872.

    Family and domain databases

    InterProiIPR008996. Cytokine_IL1-like.
    IPR028304. FGF23.
    IPR002209. Fibroblast_GF_fam.
    IPR028142. IL-1_fam/FGF_fam.
    [Graphical view]
    PANTHERiPTHR11486. PTHR11486. 1 hit.
    PTHR11486:SF69. PTHR11486:SF69. 1 hit.
    PfamiPF00167. FGF. 1 hit.
    [Graphical view]
    PRINTSiPR00262. IL1HBGF.
    SMARTiSM00442. FGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF50353. SSF50353. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9GZV9-1 [UniParc]FASTAAdd to Basket

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    MLGARLRLWV CALCSVCSMS VLRAYPNASP LLGSSWGGLI HLYTATARNS    50
    YHLQIHKNGH VDGAPHQTIY SALMIRSEDA GFVVITGVMS RRYLCMDFRG 100
    NIFGSHYFDP ENCRFQHQTL ENGYDVYHSP QYHFLVSLGR AKRAFLPGMN 150
    PPPYSQFLSR RNEIPLIHFN TPIPRRHTRS AEDDSERDPL NVLKPRARMT 200
    PAPASCSQEL PSAEDNSPMA SDPLGVVRGG RVNTHAGGTG PEGCRPFAKF 250
    I 251
    Length:251
    Mass (Da):27,954
    Last modified:March 1, 2001 - v1
    Checksum:i6093BD0CC50C2489
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711S → G in HFTC; only the C-terminal fragment is secreted, whereas the intact protein is retained in the Golgi complex. 1 Publication
    VAR_023831
    Natural varianti176 – 1761R → Q in ADHR; partially resistant to cleavage by furin. 1 Publication
    VAR_010717
    Natural varianti179 – 1791R → Q in ADHR; C-terminal processing is abolished; reduced proteolysis by PHEX; resistant to cleavage by furin. 1 Publication
    VAR_010719
    Natural varianti179 – 1791R → W in ADHR; C-terminal processing is abolished. 1 Publication
    Corresponds to variant rs28937882 [ dbSNP | Ensembl ].
    VAR_010718
    Natural varianti195 – 1951P → S.1 Publication
    Corresponds to variant rs13312793 [ dbSNP | Ensembl ].
    VAR_018887
    Natural varianti239 – 2391T → M.2 Publications
    Corresponds to variant rs7955866 [ dbSNP | Ensembl ].
    VAR_010720

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037973 mRNA. Translation: BAB13477.1.
    AF263537 mRNA. Translation: AAG09917.1.
    AB047858 mRNA. Translation: BAB55889.1.
    AY358323 mRNA. Translation: AAQ88689.1.
    AY566236 Genomic DNA. Translation: AAS59157.1.
    BC069333 mRNA. Translation: AAH69333.1.
    BC096713 mRNA. Translation: AAH96713.1.
    BC098147 mRNA. Translation: AAH98147.1.
    BC098252 mRNA. Translation: AAH98252.1.
    CCDSiCCDS8526.1.
    RefSeqiNP_065689.1. NM_020638.2.
    UniGeneiHs.287370.

    Genome annotation databases

    EnsembliENST00000237837; ENSP00000237837; ENSG00000118972.
    GeneIDi8074.
    KEGGihsa:8074.
    UCSCiuc001qmq.1. human.

    Polymorphism databases

    DMDMi13626688.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037973 mRNA. Translation: BAB13477.1 .
    AF263537 mRNA. Translation: AAG09917.1 .
    AB047858 mRNA. Translation: BAB55889.1 .
    AY358323 mRNA. Translation: AAQ88689.1 .
    AY566236 Genomic DNA. Translation: AAS59157.1 .
    BC069333 mRNA. Translation: AAH69333.1 .
    BC096713 mRNA. Translation: AAH96713.1 .
    BC098147 mRNA. Translation: AAH98147.1 .
    BC098252 mRNA. Translation: AAH98252.1 .
    CCDSi CCDS8526.1.
    RefSeqi NP_065689.1. NM_020638.2.
    UniGenei Hs.287370.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2P39 X-ray 1.50 A 25-179 [» ]
    ProteinModelPortali Q9GZV9.
    SMRi Q9GZV9. Positions 29-170.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113748. 1 interaction.
    DIPi DIP-58507N.
    IntActi Q9GZV9. 1 interaction.
    STRINGi 9606.ENSP00000237837.

    PTM databases

    PhosphoSitei Q9GZV9.

    Polymorphism databases

    DMDMi 13626688.

    Proteomic databases

    PaxDbi Q9GZV9.
    PRIDEi Q9GZV9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000237837 ; ENSP00000237837 ; ENSG00000118972 .
    GeneIDi 8074.
    KEGGi hsa:8074.
    UCSCi uc001qmq.1. human.

    Organism-specific databases

    CTDi 8074.
    GeneCardsi GC12M004477.
    HGNCi HGNC:3680. FGF23.
    MIMi 193100. phenotype.
    211900. phenotype.
    605380. gene.
    neXtProti NX_Q9GZV9.
    Orphaneti 89937. Autosomal dominant hypophosphatemic rickets.
    306661. Hypercalcemic tumoral calcinosis.
    PharmGKBi PA28119.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270405.
    HOGENOMi HOG000112573.
    HOVERGENi HBG051613.
    InParanoidi Q9GZV9.
    KOi K04358.
    OMAi DVYHSPQ.
    OrthoDBi EOG71K63W.
    PhylomeDBi Q9GZV9.
    TreeFami TF335872.

    Enzyme and pathway databases

    Reactomei REACT_111184. Negative regulation of FGFR signaling.
    REACT_120863. Activated point mutants of FGFR2.
    REACT_121153. Signaling by activated point mutants of FGFR1.
    REACT_121249. Signaling by FGFR3 mutants.
    REACT_121337. Signaling by activated point mutants of FGFR3.
    REACT_121398. Signaling by FGFR mutants.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_21247. FRS2-mediated cascade.
    REACT_21270. PI-3K cascade.
    REACT_21310. Phospholipase C-mediated cascade.
    REACT_21374. SHC-mediated cascade.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_9413. FGFR2c ligand binding and activation.
    REACT_9452. FGFR4 ligand binding and activation.
    REACT_9484. FGFR1c and Klotho ligand binding and activation.
    REACT_9510. FGFR3c ligand binding and activation.
    REACT_9515. FGFR1c ligand binding and activation.
    REACT_976. PI3K Cascade.

    Miscellaneous databases

    EvolutionaryTracei Q9GZV9.
    GeneWikii Fibroblast_growth_factor_23.
    GenomeRNAii 8074.
    NextBioi 30678.
    PROi Q9GZV9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9GZV9.
    CleanExi HS_FGF23.
    Genevestigatori Q9GZV9.

    Family and domain databases

    InterProi IPR008996. Cytokine_IL1-like.
    IPR028304. FGF23.
    IPR002209. Fibroblast_GF_fam.
    IPR028142. IL-1_fam/FGF_fam.
    [Graphical view ]
    PANTHERi PTHR11486. PTHR11486. 1 hit.
    PTHR11486:SF69. PTHR11486:SF69. 1 hit.
    Pfami PF00167. FGF. 1 hit.
    [Graphical view ]
    PRINTSi PR00262. IL1HBGF.
    SMARTi SM00442. FGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50353. SSF50353. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel fibroblast growth factor, FGF-23, preferentially expressed in the ventrolateral thalamic nucleus of the brain."
      Yamashita T., Yoshioka M., Itoh N.
      Biochem. Biophys. Res. Commun. 277:494-498(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23."
      White K.E., Evans W.E., O'Riordan J.L.H., Speer M.C., Econs M.J., Lorenz-Depiereux B., Grabowski M., Meitinger T., Strom T.M.
      Nat. Genet. 26:345-348(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANTS ADHR GLN-176; GLN-179 AND TRP-179, VARIANT MET-239.
    3. "Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia."
      Shimada T., Mizutani S., Muto T., Yoneya T., Hino R., Takeda S., Takeuchi Y., Fujita T., Fukumoto S., Yamashita T.
      Proc. Natl. Acad. Sci. U.S.A. 98:6500-6505(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. NIEHS SNPs program
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-195 AND MET-239.
    6. "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].
    7. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-39.
    8. "FGF-23 inhibits renal tubular phosphate transport and is a PHEX substrate."
      Bowe A.E., Finnegan R., Jan de Beur S.M., Cho J., Levine M.A., Kumar R., Schiavi S.C.
      Biochem. Biophys. Res. Commun. 284:977-981(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION OF VARIANT ADHR GLN-179.
    9. "The autosomal dominant hypophosphatemic rickets (ADHR) gene is a secreted polypeptide overexpressed by tumors that cause phosphate wasting."
      White K.E., Jonsson K.B., Carn G., Hampson G., Spector T.D., Mannstadt M., Lorenz-Depiereux B., Miyauchi A., Yang I.M., Ljunggren O., Meitinger T., Strom T.M., Jueppner H., Econs M.J.
      J. Clin. Endocrinol. Metab. 86:497-500(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    10. "Mutant FGF-23 responsible for autosomal dominant hypophosphatemic rickets is resistant to proteolytic cleavage and causes hypophosphatemia in vivo."
      Shimada T., Muto T., Urakawa I., Yoneya T., Yamazaki Y., Okawa K., Takeuchi Y., Fujita T., Fukumoto S., Yamashita T.
      Endocrinology 143:3179-3182(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    11. Cited for: TISSUE SPECIFICITY.
    12. "FGF23 is processed by proprotein convertases but not by PHEX."
      Benet-Pages A., Lorenz-Depiereux B., Zischka H., White K.E., Econs M.J., Strom T.M.
      Bone 35:455-462(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING BY PROPROTEIN CONVERTASES.
    13. "FGF-23 is a potent regulator of vitamin D metabolism and phosphate homeostasis."
      Shimada T., Hasegawa H., Yamazaki Y., Muto T., Hino R., Takeuchi Y., Fujita T., Nakahara K., Fukumoto S., Yamashita T.
      J. Bone Miner. Res. 19:429-435(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family."
      Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M., Ornitz D.M.
      J. Biol. Chem. 281:15694-15700(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, FUNCTION IN STIMULATION OF CELL PROLIFERATION.
    15. "Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation."
      Kato K., Jeanneau C., Tarp M.A., Benet-Pages A., Lorenz-Depiereux B., Bennett E.P., Mandel U., Strom T.M., Clausen H.
      J. Biol. Chem. 281:18370-18377(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT THR-178, CHARACTERIZATION OF VARIANTS ADHR GLN-176 AND GLN-179, IDENTIFICATION BY MASS SPECTROMETRY.
    16. "Overexpression of fibroblast growth factor 23 suppresses osteoblast differentiation and matrix mineralization in vitro."
      Wang H., Yoshiko Y., Yamamoto R., Minamizaki T., Kozai K., Tanne K., Aubin J.E., Maeda N.
      J. Bone Miner. Res. 23:939-948(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Fibroblast growth factor signalling: from development to cancer."
      Turner N., Grose R.
      Nat. Rev. Cancer 10:116-129(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 25-179.
    19. "An FGF23 missense mutation causes familial tumoral calcinosis with hyperphosphatemia."
      Benet-Pages A., Orlik P., Strom T.M., Lorenz-Depiereux B.
      Hum. Mol. Genet. 14:385-390(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HFTC GLY-71.

    Entry informationi

    Entry nameiFGF23_HUMAN
    AccessioniPrimary (citable) accession number: Q9GZV9
    Secondary accession number(s): Q4V758
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 147 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 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3