Fibroblast growth factor receptor 4

FGFR4
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4QQ5, 4QQC, 4QQJ, 4QQT, 4QRC, 4R6V, 4TYE, 4TYG, 4TYI, 4TYJ, 4UXQ, 4XCU
Identifiers
Aliases	FGFR4, CD334, JTK2, TKF, fibroblast growth factor receptor 4
External IDs	OMIM: 134935 MGI: 95525 HomoloGene: 20461 GeneCards: FGFR4
Gene location (Human)
Chr.	Chromosome 5 (human)
End	177,098,144 bp
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)
End	55,316,572 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; upper lobe of left lung; ; right lung; ; body of pancreas; ; lower lobe of lung; ; spleen; ; right adrenal gland; ; kidney; ; metanephric glomerulus; ; gallbladder;
	Top expressed in
	left lung lobe; ; yolk sac; ; left lobe of liver; ; internal carotid artery; ; utricle; ; kidney; ; urethra; ; stria vascularis; ; adrenal gland; ; right lung;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity; nucleotide binding; protein kinase activity; heparin binding; kinase activity; protein binding; transmembrane receptor protein tyrosine kinase activity; protein tyrosine kinase activity; fibroblast growth factor binding; fibroblast growth factor-activated receptor activity; ATP binding; phosphatidylinositol-4,5-bisphosphate 3-kinase activity; 1-phosphatidylinositol-3-kinase activity; receptor tyrosine kinase; transmembrane signaling receptor activity;
Cellular component	integral component of membrane; endosome; Golgi apparatus; membrane; cell-cell junction; plasma membrane; integral component of plasma membrane; transport vesicle; extracellular region; endoplasmic reticulum; cytoplasm; receptor complex;
Biological process	glucose homeostasis; phosphorylation; phosphate ion homeostasis; response to bile acid; regulation of extracellular matrix disassembly; MAPK cascade; regulation of bile acid biosynthetic process; fibroblast growth factor receptor signaling pathway; regulation of lipid metabolic process; protein phosphorylation; positive regulation of gene expression; positive regulation of cell population proliferation; positive regulation of DNA biosynthetic process; positive regulation of ERK1 and ERK2 cascade; positive regulation of proteolysis; protein autophosphorylation; peptidyl-tyrosine phosphorylation; cell migration; phosphatidylinositol phosphate biosynthetic process; positive regulation of catalytic activity; phosphatidylinositol-3-phosphate biosynthetic process; positive regulation of protein kinase B signaling; cholesterol homeostasis; angiogenesis; negative regulation of signal transduction; cell differentiation; negative regulation of apoptotic process; transmembrane receptor protein tyrosine kinase signaling pathway; nervous system development;
	Sources:Amigo / QuickGO
Orthologs
	2264
	14186
	ENSG00000160867
	ENSMUSG00000005320
	P22455
	Q03142
	NM_001291980; NM_002011; NM_022963; NM_213647; NM_001354984
	NM_008011
	NP_001278909; NP_002002; NP_075252; NP_998812; NP_001341913
	NP_032037
	Wikidata
View/Edit Human	View/Edit Mouse

Fibroblast growth factor receptor 4 is a protein that in humans is encoded by the FGFR4 gene. FGFR4 has also been designated as CD334 (cluster of differentiation 334).

Template:PBB Summary

Interactions

Fibroblast growth factor receptor 4 has been shown to interact with FGF1.^[5]^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000160867 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000005320 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Loo, B B; Darwish K K; Vainikka S S; Saarikettu J J; Vihko P P; Hermonen J J; Goldman A A; Alitalo K K; Jalkanen M M (May 2000). "Production and characterization of the extracellular domain of recombinant human fibroblast growth factor receptor 4". Int. J. Biochem. Cell Biol. 32 (5). ENGLAND: 489–97. doi:10.1016/S1357-2725(99)00145-4. ISSN 1357-2725. PMID 10736564. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)
^ Kan, M; Wu X; Wang F; McKeehan W L (May 1999). "Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase". J. Biol. Chem. 274 (22). UNITED STATES: 15947–52. doi:10.1074/jbc.274.22.15947. ISSN 0021-9258. PMID 10336501. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)CS1 maint: unflagged free DOI (link)

External links

FGFR4+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Template:PBB Controls

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000160867 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000005320 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10736564-5] Loo, B B; Darwish K K; Vainikka S S; Saarikettu J J; Vihko P P; Hermonen J J; Goldman A A; Alitalo K K; Jalkanen M M (May 2000). "Production and characterization of the extracellular domain of recombinant human fibroblast growth factor receptor 4". Int. J. Biochem. Cell Biol. 32 (5). ENGLAND: 489–97. doi:10.1016/S1357-2725(99)00145-4. ISSN 1357-2725. PMID 10736564. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)

[pmid10336501-6] Kan, M; Wu X; Wang F; McKeehan W L (May 1999). "Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase". J. Biol. Chem. 274 (22). UNITED STATES: 15947–52. doi:10.1074/jbc.274.22.15947. ISSN 0021-9258. PMID 10336501. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)CS1 maint: unflagged free DOI (link)

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[5]

[6]

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Interactions

References

Further reading

External links