FGF23
entrez
8074
canonical
uniprot
Q9GZV9
canonical
ensembl
ENSG00000118972
resolver
ensp
ENSP00000237837
resolver
enst
ENST00000237837
resolver
genesymbol
FGF23
resolver
genesymbol_syn
HYPF
resolver
hgnc
HGNC:3680
resolver
uniprot
Q4V758
resolver
uniprot_entry
FGF23_HUMAN
resolver
uniprot_sec
Q4V758
resolver
amino_acid_sequence
MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARNSYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPGMNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRARMTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRPFAKFI
uniprot
proteins
disease_involvement
DISEASE: 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. {ECO:0000269|PubMed:11062477, ECO:0000269|PubMed:11409890, ECO:0000269|PubMed:16638743}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Tumoral calcinosis, hyperphosphatemic, familial, 2 (HFTC2) [MIM:617993]: A form of hyperphosphatemic tumoral calcinosis, a rare autosomal recessive metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients have recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement. {ECO:0000269|PubMed:15590700, ECO:0000269|PubMed:16030159, ECO:0000269|PubMed:16151858, ECO:0000269|PubMed:24680727}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Regulator of phosphate homeostasis (PubMed:11062477). Inhibits renal tubular phosphate transport by reducing SLC34A1 levels (PubMed:11409890). Up-regulates 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 (PubMed:15040831). Negatively regulates osteoblast differentiation and matrix mineralization (PubMed:18282132). {ECO:0000250|UniProtKB:Q8VI82, ECO:0000269|PubMed:11062477, ECO:0000269|PubMed:11409890, ECO:0000269|PubMed:15040831, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:18282132}.
uniprot
proteins
mass_dalton
27954
uniprot
proteins
mutagenesis
MUTAGEN 178; /note="T->A: Loss of glycosylation."; /evidence="ECO:0000269|PubMed:31932717
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:11157998, ECO:0000269|PubMed:12130585, ECO:0000269|PubMed:15268897}.; PTM: O-glycosylated at Thr-171 and Thr-178 by GALNT3 and glycosylation of Thr-178 requires previous glycosylation at Thr171. 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. {ECO:0000269|PubMed:16638743, ECO:0000269|PubMed:31932717}.; PTM: Phosphorylation at Ser-180 mediated by FAM20C slows down glycosylation at Thr-178 notably. {ECO:0000269|PubMed:31932717}.
uniprot
proteins
protein_family
Heparin-binding growth factors family
uniprot
proteins
pubmed
11032749
uniprot
proteins
pubmed
11062477
uniprot
proteins
pubmed
11157998
uniprot
proteins
pubmed
11344269
uniprot
proteins
pubmed
11409890
uniprot
proteins
pubmed
12130585
uniprot
proteins
pubmed
12952917
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15040831
uniprot
proteins
pubmed
15268897
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15590700
uniprot
proteins
pubmed
16030159
uniprot
proteins
pubmed
16151858
uniprot
proteins
pubmed
16597617
uniprot
proteins
pubmed
16638743
uniprot
proteins
pubmed
17339340
uniprot
proteins
pubmed
18282132
uniprot
proteins
pubmed
20094046
uniprot
proteins
pubmed
24680727
uniprot
proteins
pubmed
31932717
uniprot
proteins
sequence_length
251
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16638743}. Note=Secretion is dependent on O-glycosylation.
uniprot
proteins