FGFR4
entrez
2264
canonical
uniprot
P22455
canonical
ensembl
ENSG00000160867
resolver
ensp
ENSP00000292408
resolver
ensp
ENSP00000377254
resolver
ensp
ENSP00000377259
resolver
ensp
ENSP00000424960
resolver
ensp
ENSP00000555574
resolver
ensp
ENSP00000555578
resolver
ensp
ENSP00000631741
resolver
enst
ENST00000393648
resolver
enst
ENST00000885519
resolver
enst
ENST00000961682
resolver
genesymbol
FGFR4
resolver
genesymbol_syn
JTK2
resolver
genesymbol_syn
TKF
resolver
hgnc
HGNC:3691
resolver
uniprot
B4DVP5
resolver
uniprot
G3JVM2
resolver
uniprot
G3JVM5
resolver
uniprot
G3JVM7
resolver
uniprot
G3JVM9
resolver
uniprot
J3KPQ0
resolver
uniprot
O43785
resolver
uniprot
Q14309
resolver
uniprot
Q71TW8
resolver
uniprot
Q8TDA0
resolver
uniprot
Q96KE5
resolver
uniprot_entry
B4DVP5_HUMAN
resolver
uniprot_entry
FGFR4_HUMAN
resolver
uniprot_entry
J3KPQ0_HUMAN
resolver
uniprot_sec
G3JVM2
resolver
uniprot_sec
G3JVM5
resolver
uniprot_sec
G3JVM7
resolver
uniprot_sec
G3JVM9
resolver
uniprot_sec
O43785
resolver
uniprot_sec
Q14309
resolver
uniprot_sec
Q71TW8
resolver
uniprot_sec
Q8TDA0
resolver
uniprot_sec
Q96KE5
resolver
activity_regulation
ACTIVITY REGULATION: Present in an inactive conformation in the absence of bound ligand. Ligand binding leads to dimerization and activation by autophosphorylation on tyrosine residues. {ECO:0000269|PubMed:18480409}.
uniprot
proteins
amino_acid_sequence
MRLLLALLGVLLSVPGPPVLSLEASEEVELEPCLAPSLEQQEQELTVALGQPVRLCCGRAERGGHWYKEGSRLAPAGRVRGWRGRLEIASFLPEDAGRYLCLARGSMIVLQNLTLITGDSLTSSNDDEDPKSHRDPSNRHSYPQQAPYWTHPQRMEKKLHAVPAGNTVKFRCPAAGNPTPTIRWLKDGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENAVGSIRYNYLLDVLERSPHRPILQAGLPANTTAVVGSDVELLCKVYSDAQPHIQWLKHIVINGSSFGADGFPYVQVLKTADINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLSYQSAWLTVLPEEDPTWTAAAPEARYTDIILYASGSLALAVLLLLAGLYRGQALHGRHPRPPATVQKLSRFPLARQFSLESGSSGKSSSSLVRGVRLSSSGPALLAGLVSLDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVRAEAFGMDPARPDQASTVAVKMLKDNASDKDLADLVSEMEVMKLIGRHKNIINLLGVCTQEGPLYVIVECAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPVLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDNVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMDRPPHCPPELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPSGGDASSTCSSSDSVFSHDPLPLGSSSFPFGSGVQT
uniprot
proteins
disease_involvement
DISEASE: Note=FGFR4 variants may be involved in the pathogenesis of various cancers. Variant Arg-388 predisposes cancer patients to accelerated disease progression and may be associated with poor prognosis. It has been found in prostate cancer as well as cancers of the breast, colon, head and neck, larynx, lung, skin. {ECO:0000269|PubMed:11830541, ECO:0000269|PubMed:18670643, ECO:0000269|PubMed:18756523, ECO:0000269|PubMed:20638838, ECO:0000269|PubMed:20876804, ECO:0000269|PubMed:21349172, ECO:0000269|PubMed:21412156, ECO:0000269|PubMed:21882254, ECO:0000269|PubMed:26675719}.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Mutations that lead to constitutive kinase activation or impair normal FGFR4 inactivation lead to aberrant signaling. {ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:18480409, ECO:0000269|PubMed:18670643, ECO:0000269|PubMed:20018895, ECO:0000269|PubMed:20683963, ECO:0000269|PubMed:20798051, ECO:0000269|PubMed:20876804, ECO:0000269|PubMed:21653700, ECO:0000269|PubMed:7518429, ECO:0000269|PubMed:7680645, ECO:0000269|PubMed:8663044}.
uniprot
proteins
mass_dalton
87954
uniprot
proteins
mutagenesis
MUTAGEN 503; /note="K->R: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:17311277"; MUTAGEN 754; /note="Y->F: Loss of interaction with PLCG1."; /evidence="ECO:0000269|PubMed:7518429
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. Full maturation of the glycan chains in the Golgi is essential for high affinity interaction with FGF19.; PTM: Ubiquitinated. Subject to proteasomal degradation when not fully glycosylated. {ECO:0000269|PubMed:18480409}.; PTM: Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer. {ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:18670643, ECO:0000269|PubMed:7518429}.
uniprot
proteins
protein_family
Fibroblast growth factor receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10631118
uniprot
proteins
pubmed
11433297
uniprot
proteins
pubmed
11781352
uniprot
proteins
pubmed
11830541
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15863030
uniprot
proteins
pubmed
16597617
uniprot
proteins
pubmed
1709094
uniprot
proteins
pubmed
17311277
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17623664
uniprot
proteins
pubmed
18480409
uniprot
proteins
pubmed
18670643
uniprot
proteins
pubmed
18756523
uniprot
proteins
pubmed
20018895
uniprot
proteins
pubmed
20094046
uniprot
proteins
pubmed
20638838
uniprot
proteins
pubmed
20683963
uniprot
proteins
pubmed
20798051
uniprot
proteins
pubmed
20876804
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21349172
uniprot
proteins
pubmed
21412156
uniprot
proteins
pubmed
21653700
uniprot
proteins
pubmed
21882254
uniprot
proteins
pubmed
2247464
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26237043
uniprot
proteins
pubmed
26675719
uniprot
proteins
pubmed
7518429
uniprot
proteins
pubmed
7680645
uniprot
proteins
pubmed
8663044
uniprot
proteins
pubmed
9457674
uniprot
proteins
sequence_length
802
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endosome. Endoplasmic reticulum. Note=Internalized from the cell membrane to recycling endosomes, and from there back to the cell membrane.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
uniprot
proteins
transmembrane_region
TRANSMEM 370..390; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins