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UniProtKB - Q9GZV9 (FGF23_HUMAN)

Entry version 193 (13 Nov 2019)
Sequence version 1 (01 Mar 2001)
Previous versions | rss
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Protein

Fibroblast growth factor 23

Gene

FGF23

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGrowth factor
Biological processDifferentiation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-109704 PI3K Cascade
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-1839122 Signaling by activated point mutants of FGFR1
R-HSA-1839130 Signaling by activated point mutants of FGFR3
R-HSA-190322 FGFR4 ligand binding and activation
R-HSA-190372 FGFR3c ligand binding and activation
R-HSA-190373 FGFR1c ligand binding and activation
R-HSA-190374 FGFR1c and Klotho ligand binding and activation
R-HSA-190375 FGFR2c ligand binding and activation
R-HSA-2033514 FGFR3 mutant receptor activation
R-HSA-2033519 Activated point mutants of FGFR2
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-5654219 Phospholipase C-mediated cascade: FGFR1
R-HSA-5654221 Phospholipase C-mediated cascade, FGFR2
R-HSA-5654227 Phospholipase C-mediated cascade, FGFR3
R-HSA-5654228 Phospholipase C-mediated cascade, FGFR4
R-HSA-5654687 Downstream signaling of activated FGFR1
R-HSA-5654688 SHC-mediated cascade:FGFR1
R-HSA-5654689 PI-3K cascade:FGFR1
R-HSA-5654693 FRS-mediated FGFR1 signaling
R-HSA-5654695 PI-3K cascade:FGFR2
R-HSA-5654699 SHC-mediated cascade:FGFR2
R-HSA-5654700 FRS-mediated FGFR2 signaling
R-HSA-5654704 SHC-mediated cascade:FGFR3
R-HSA-5654706 FRS-mediated FGFR3 signaling
R-HSA-5654710 PI-3K cascade:FGFR3
R-HSA-5654712 FRS-mediated FGFR4 signaling
R-HSA-5654719 SHC-mediated cascade:FGFR4
R-HSA-5654720 PI-3K cascade:FGFR4
R-HSA-5654726 Negative regulation of FGFR1 signaling
R-HSA-5654727 Negative regulation of FGFR2 signaling
R-HSA-5654732 Negative regulation of FGFR3 signaling
R-HSA-5654733 Negative regulation of FGFR4 signaling
R-HSA-5655253 Signaling by FGFR2 in disease
R-HSA-5655302 Signaling by FGFR1 in disease
R-HSA-5658623 FGFRL1 modulation of FGFR1 signaling
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8853338 Signaling by FGFR3 point mutants in cancer
R-HSA-8957275 Post-translational protein phosphorylation

Protein family/group databases

Transport Classification Database

More...TCDBi		1.A.108.1.2 the fibroblast growth factor 2 (fgf2) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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:
Fibroblast growth factor 23 N-terminal peptide
Fibroblast growth factor 23 C-terminal peptide
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FGF23
Synonyms:HYPF
ORF Names:UNQ3027/PRO9828
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3680 FGF23

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605380 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9GZV9

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Hypophosphatemic rickets, autosomal dominant (ADHR)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010717176R → Q in ADHR; partially resistant to cleavage by furin. 2 PublicationsCorresponds to variant dbSNP:rs104894347EnsemblClinVar.1
Natural variantiVAR_010719179R → Q in ADHR; C-terminal processing is abolished; reduced proteolysis by PHEX; resistant to cleavage by furin. 3 PublicationsCorresponds to variant dbSNP:rs193922702EnsemblClinVar.1
Natural variantiVAR_010718179R → W in ADHR; C-terminal processing is abolished. 1 PublicationCorresponds to variant dbSNP:rs28937882EnsemblClinVar.1
Tumoral calcinosis, hyperphosphatemic, familial, 2 (HFTC2)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02383171S → G in HFTC2; only the C-terminal fragment is secreted, whereas the intact protein is retained in the Golgi complex. 1 PublicationCorresponds to variant dbSNP:rs104894342EnsemblClinVar.1
Natural variantiVAR_07171196M → T in HFTC2. 1 PublicationCorresponds to variant dbSNP:rs104894343EnsemblClinVar.1
Natural variantiVAR_071712129S → F in HFTC2; 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 PublicationCorresponds to variant dbSNP:rs104894344EnsemblClinVar.1
Natural variantiVAR_071713157F → L in HFTC2. 1 PublicationCorresponds to variant dbSNP:rs772964687Ensembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		8074

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		FGF23

MalaCards human disease database

More...MalaCardsi		FGF23
MIMi193100 phenotype
617993 phenotype

Open Targets

More...OpenTargetsi		ENSG00000118972

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		89937 Autosomal dominant hypophosphatemic rickets
306661 Familial hyperphosphatemic tumoral calcinosis/Hyperphosphatemic hyperostosis syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28119

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9GZV9

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3713913

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		FGF23

Domain mapping of disease mutations (DMDM)

More...DMDMi		13626688

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 241 PublicationAdd BLAST24
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000899825 – 251Fibroblast growth factor 23Add BLAST227
ChainiPRO_000035287525 – 179Fibroblast growth factor 23 N-terminal peptideAdd BLAST155
ChainiPRO_0000352876180 – 251Fibroblast growth factor 23 C-terminal peptideAdd BLAST72

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi95 ↔ 113
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi178O-linked (GalNAc) threonine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei179 – 180Cleavage; by proprotein convertases2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9GZV9

PeptideAtlas

More...PeptideAtlasi		Q9GZV9

PRoteomics IDEntifications database

More...PRIDEi		Q9GZV9

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		80160

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9GZV9

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q9GZV9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000118972 Expressed in 21 organ(s), highest expression level in right atrium auricular region

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9GZV9 HS

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		113748, 3 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9GZV9

Database of interacting proteins

More...DIPi		DIP-58507N

Protein interaction database and analysis system

More...IntActi		Q9GZV9, 6 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000237837

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1251
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9GZV9

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9GZV9

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the heparin-binding growth factors family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3885 Eukaryota
ENOG4111IPH LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160821

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000112573

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9GZV9

KEGG Orthology (KO)

More...KOi		K22428

Identification of Orthologs from Complete Genome Data

More...OMAi		SPESCRF

Database of Orthologous Groups

More...OrthoDBi		1345259at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9GZV9

TreeFam database of animal gene trees

More...TreeFami		TF335872

Family and domain databases

Conserved Domains Database

More...CDDi		cd00058 FGF, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR028304 FGF23
IPR002209 Fibroblast_GF_fam
IPR008996 IL1/FGF

The PANTHER Classification System

More...PANTHERi		PTHR11486 PTHR11486, 1 hit
PTHR11486:SF69 PTHR11486:SF69, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00167 FGF, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00442 FGF, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50353 SSF50353, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6093BD0CC50C2489
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02383171S → G in HFTC2; only the C-terminal fragment is secreted, whereas the intact protein is retained in the Golgi complex. 1 PublicationCorresponds to variant dbSNP:rs104894342EnsemblClinVar.1
Natural variantiVAR_07171196M → T in HFTC2. 1 PublicationCorresponds to variant dbSNP:rs104894343EnsemblClinVar.1
Natural variantiVAR_071712129S → F in HFTC2; 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 PublicationCorresponds to variant dbSNP:rs104894344EnsemblClinVar.1
Natural variantiVAR_071713157F → L in HFTC2. 1 PublicationCorresponds to variant dbSNP:rs772964687Ensembl.1
Natural variantiVAR_010717176R → Q in ADHR; partially resistant to cleavage by furin. 2 PublicationsCorresponds to variant dbSNP:rs104894347EnsemblClinVar.1
Natural variantiVAR_010719179R → Q in ADHR; C-terminal processing is abolished; reduced proteolysis by PHEX; resistant to cleavage by furin. 3 PublicationsCorresponds to variant dbSNP:rs193922702EnsemblClinVar.1
Natural variantiVAR_010718179R → W in ADHR; C-terminal processing is abolished. 1 PublicationCorresponds to variant dbSNP:rs28937882EnsemblClinVar.1
Natural variantiVAR_018887195P → S1 PublicationCorresponds to variant dbSNP:rs13312793Ensembl.1
Natural variantiVAR_010720239T → M2 PublicationsCorresponds to variant dbSNP:rs7955866EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS8526.1

NCBI Reference Sequences

More...RefSeqi		NP_065689.1, NM_020638.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000237837; ENSP00000237837; ENSG00000118972

Database of genes from NCBI RefSeq genomes

More...GeneIDi		8074

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:8074

UCSC genome browser

More...UCSCi		uc001qmq.1 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2P39X-ray1.50A25-179[»]
5W21X-ray3.00B25-204[»]
SMRiQ9GZV9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi113748, 3 interactors
CORUMiQ9GZV9
DIPiDIP-58507N
IntActiQ9GZV9, 6 interactors
STRINGi9606.ENSP00000237837

Chemistry databases

ChEMBLiCHEMBL3713913

Protein family/group databases

TCDBi1.A.108.1.2 the fibroblast growth factor 2 (fgf2) family

PTM databases

iPTMnetiQ9GZV9
PhosphoSitePlusiQ9GZV9

Polymorphism and mutation databases

BioMutaiFGF23
DMDMi13626688

Proteomic databases

PaxDbiQ9GZV9
PeptideAtlasiQ9GZV9
PRIDEiQ9GZV9
ProteomicsDBi80160

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		Q9GZV9

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8074
DisGeNETi8074

GeneCards: human genes, protein and diseases

More...GeneCardsi		FGF23
GeneReviewsiFGF23
HGNCiHGNC:3680 FGF23
MalaCardsiFGF23
MIMi193100 phenotype
605380 gene
617993 phenotype
neXtProtiNX_Q9GZV9
OpenTargetsiENSG00000118972
Orphaneti89937 Autosomal dominant hypophosphatemic rickets
306661 Familial hyperphosphatemic tumoral calcinosis/Hyperphosphatemic hyperostosis syndrome
PharmGKBiPA28119

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3885 Eukaryota
ENOG4111IPH LUCA
GeneTreeiENSGT00940000160821
HOGENOMiHOG000112573
InParanoidiQ9GZV9
KOiK22428
OMAiSPESCRF
OrthoDBi1345259at2759
PhylomeDBiQ9GZV9
TreeFamiTF335872

Enzyme and pathway databases

ReactomeiR-HSA-109704 PI3K Cascade
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-1839122 Signaling by activated point mutants of FGFR1
R-HSA-1839130 Signaling by activated point mutants of FGFR3
R-HSA-190322 FGFR4 ligand binding and activation
R-HSA-190372 FGFR3c ligand binding and activation
R-HSA-190373 FGFR1c ligand binding and activation
R-HSA-190374 FGFR1c and Klotho ligand binding and activation
R-HSA-190375 FGFR2c ligand binding and activation
R-HSA-2033514 FGFR3 mutant receptor activation
R-HSA-2033519 Activated point mutants of FGFR2
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-5654219 Phospholipase C-mediated cascade: FGFR1
R-HSA-5654221 Phospholipase C-mediated cascade, FGFR2
R-HSA-5654227 Phospholipase C-mediated cascade, FGFR3
R-HSA-5654228 Phospholipase C-mediated cascade, FGFR4
R-HSA-5654687 Downstream signaling of activated FGFR1
R-HSA-5654688 SHC-mediated cascade:FGFR1
R-HSA-5654689 PI-3K cascade:FGFR1
R-HSA-5654693 FRS-mediated FGFR1 signaling
R-HSA-5654695 PI-3K cascade:FGFR2
R-HSA-5654699 SHC-mediated cascade:FGFR2
R-HSA-5654700 FRS-mediated FGFR2 signaling
R-HSA-5654704 SHC-mediated cascade:FGFR3
R-HSA-5654706 FRS-mediated FGFR3 signaling
R-HSA-5654710 PI-3K cascade:FGFR3
R-HSA-5654712 FRS-mediated FGFR4 signaling
R-HSA-5654719 SHC-mediated cascade:FGFR4
R-HSA-5654720 PI-3K cascade:FGFR4
R-HSA-5654726 Negative regulation of FGFR1 signaling
R-HSA-5654727 Negative regulation of FGFR2 signaling
R-HSA-5654732 Negative regulation of FGFR3 signaling
R-HSA-5654733 Negative regulation of FGFR4 signaling
R-HSA-5655253 Signaling by FGFR2 in disease
R-HSA-5655302 Signaling by FGFR1 in disease
R-HSA-5658623 FGFRL1 modulation of FGFR1 signaling
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8853338 Signaling by FGFR3 point mutants in cancer
R-HSA-8957275 Post-translational protein phosphorylation

Miscellaneous databases

EvolutionaryTraceiQ9GZV9

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Fibroblast_growth_factor_23

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		8074
PharosiQ9GZV9

Protein Ontology

More...PROi		PR:Q9GZV9

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000118972 Expressed in 21 organ(s), highest expression level in right atrium auricular region
GenevisibleiQ9GZV9 HS

Family and domain databases

CDDicd00058 FGF, 1 hit
InterProiView protein in InterPro
IPR028304 FGF23
IPR002209 Fibroblast_GF_fam
IPR008996 IL1/FGF
PANTHERiPTHR11486 PTHR11486, 1 hit
PTHR11486:SF69 PTHR11486:SF69, 1 hit
PfamiView protein in Pfam
PF00167 FGF, 1 hit
SMARTiView protein in SMART
SM00442 FGF, 1 hit
SUPFAMiSSF50353 SSF50353, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFGF23_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9GZV9
Secondary accession number(s): Q4V758
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: November 13, 2019
This is version 193 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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