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Q9GZV9

- FGF23_HUMAN

UniProt

Q9GZV9 - FGF23_HUMAN

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Protein

Fibroblast growth factor 23

Gene

FGF23

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

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
Complete GO annotation...

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
Complete GO annotation...

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.4 Publications
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
Natural varianti96 – 961M → T in HFTC. 1 Publication
VAR_071711
Natural varianti129 – 1291S → F in HFTC; full-length and N-terminal fragments are barely detectable, whereas a C-terminal fragment with the same molecular weight as that from wild-type can be detected. 1 Publication
VAR_071712
Natural varianti157 – 1571F → L in HFTC. 1 Publication
VAR_071713

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi193100. phenotype.
211900. phenotype.
Orphaneti89937. Autosomal dominant hypophosphatemic rickets.
306661. Familial 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.
GeneTreeiENSGT00530000063469.
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.
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

« Hide

        10         20         30         40         50
MLGARLRLWV CALCSVCSMS VLRAYPNASP LLGSSWGGLI HLYTATARNS
60 70 80 90 100
YHLQIHKNGH VDGAPHQTIY SALMIRSEDA GFVVITGVMS RRYLCMDFRG
110 120 130 140 150
NIFGSHYFDP ENCRFQHQTL ENGYDVYHSP QYHFLVSLGR AKRAFLPGMN
160 170 180 190 200
PPPYSQFLSR RNEIPLIHFN TPIPRRHTRS AEDDSERDPL NVLKPRARMT
210 220 230 240 250
PAPASCSQEL PSAEDNSPMA SDPLGVVRGG RVNTHAGGTG PEGCRPFAKF

I
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 varianti96 – 961M → T in HFTC. 1 Publication
VAR_071711
Natural varianti129 – 1291S → F in HFTC; full-length and N-terminal fragments are barely detectable, whereas a C-terminal fragment with the same molecular weight as that from wild-type can be detected. 1 Publication
VAR_071712
Natural varianti157 – 1571F → L in HFTC. 1 Publication
VAR_071713
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. Familial tumoral calcinosis.
PharmGKBi PA28119.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG270405.
GeneTreei ENSGT00530000063469.
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.
PRINTSi PR00262. IL1HBGF.
SMARTi SM00442. FGF. 1 hit.
[Graphical view ]
SUPFAMi SSF50353. SSF50353. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "A novel homozygous missense mutation in FGF23 causes Familial Tumoral Calcinosis associated with disseminated visceral calcification."
    Chefetz I., Heller R., Galli-Tsinopoulou A., Richard G., Wollnik B., Indelman M., Koerber F., Topaz O., Bergman R., Sprecher E., Schoenau E.
    Hum. Genet. 118:261-266(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HFTC THR-96.
  20. "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.
  21. Cited for: VARIANT HFTC PHE-129, CHARACTERIZATION OF VARIANT HFTC PHE-129.
  22. "A new missense mutation in FGF23 gene in a male with hyperostosis-hyperphosphatemia syndrome (HHS)."
    Abbasi F., Ghafouri-Fard S., Javaheri M., Dideban A., Ebrahimi A., Ebrahim-Habibi A.
    Gene 542:269-271(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HFTC LEU-157.

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 29, 2014
This is version 148 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

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