Receptor 4 fibroblastnog faktora rasta
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Receptor 4 fibroblastnog faktora rasta | |||||||||||
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Dostupne strukture | |||||||||||
4TYG, 4TYI, 4TYE, 4TYJ[1] | |||||||||||
Identifikatori | |||||||||||
Simboli | FGFR4; CD334; JTK2; TKF | ||||||||||
Vanjski ID | OMIM: 134935 MGI: 95525 HomoloGene: 20461 GeneCards: FGFR4 Gene | ||||||||||
EC broj | 2.7.10.1 | ||||||||||
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Pregled RNK izražavanja | |||||||||||
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podaci | |||||||||||
Ortolozi | |||||||||||
Vrsta | Čovek | Miš | |||||||||
Entrez | 2264 | 14186 | |||||||||
Ensembl | ENSG00000160867 | ENSMUSG00000005320 | |||||||||
UniProt | P22455 | Q03142 | |||||||||
Ref. Sekv. (iRNK) | NM_001291980 | NM_008011 | |||||||||
Ref. Sekv. (protein) | NP_001278909 | NP_032037 | |||||||||
Lokacija (UCSC) | Chr 5: 176.51 - 176.53 Mb | Chr 13: 55.15 - 55.17 Mb | |||||||||
PubMed pretraga | [1] | [2] |
Receptor 4 fibroblastnog faktora rasta je protein koji je kod ljudi kodiran FGFR4 genom. FGFR4 se takođe označava sa CD334 (klaster diferencijacije 334).
Funkcija
Protein kodiran ovim genom je član familije receptora fibroblastnih faktora rasta (FGFR) među kojima je aminokiselinska sekvenca visoko konzervirana tokom evolucije. Članovi FGFR familije se međusobno razlikuju po nihovom afinitetu za ligande i tkivnoj distribuciji. Reprezentativni protein pune dužine se sastoji od ekstracelularnog regiona, sastavljenog od tri imunoglobulinu slična domena, jednog hidrofobnog jednoprolaznog membranskog segmenta i citoplazmatičnog tirozinskog kinaznog domena. Ekstracelularna porcija proteina interaguje sa fibroblastnim faktorima rasta, čime se pokreće signalna kaslada koja utiče na mitogenezu i diferencijaciju. Ovaj član familije se vezuje za kisele i bazne fibroblastne faktore rasta. Genomska organizacija ovog gena, u poređenju sa članovima 1-3, obuhvata 18 eksona umesto 19 ili 20. Mada su alternativno splajsovane varijante poznate, nema dokaza da se C-terminalna polovina IgIII domena ovog proteina razlikuje među izoformama. Ovaj protein preferentno vezuje kisele fibroblastne faktore rasta i mada njegova specifična funkcija nije poznata, on je prekomerno izražen u uzorcima ginekoloških tumora, što sugeriše da učestvuje u tumogenezi u dojkama i jajnicima.[2] }}
Interakcije
Receptor 4 fibroblastnog faktora rasta formira interakcije sa FGF1.[3][4]
Povezano
- Klaster diferencijacije
Reference
- ↑ Lesca, E., Lammens, A., Huber, R., Augustin, M.. „Structural analysis of the human Fibroblast Growth Factor Receptor 4 kinase”. J. Mol. Biol.. DOI:10.1016/j.jmb.2014.09.004.
- ↑ „Entrez Gene: FGFR4 fibroblast growth factor receptor 4”.
- ↑ Loo, B B; Darwish K K; Vainikka S S; Saarikettu J J; Vihko P P; Hermonen J J; Goldman A A; Alitalo K K i dr.. (May 2000). „Production and characterization of the extracellular domain of recombinant human fibroblast growth factor receptor 4”. Int. J. Biochem. Cell Biol. (ENGLAND) 32 (5): 489–97. DOI:10.1016/S1357-2725(99)00145-4. ISSN 1357-2725. PMID 10736564.
- ↑ 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. (UNITED STATES) 274 (22): 15947–52. DOI:10.1074/jbc.274.22.15947. ISSN 0021-9258. PMID 10336501.
Literatura
- Doherty P, Smith P, Walsh FS (1997). „Shared cell adhesion molecule (CAM) homology domains point to CAMs signalling via FGF receptors.”. Perspectives on developmental neurobiology 4 (2–3): 157–68. PMID 9168198.
- Warrington JA, Bailey SK, Armstrong E, et al. (1992). „A radiation hybrid map of 18 growth factor, growth factor receptor, hormone receptor, or neurotransmitter receptor genes on the distal region of the long arm of chromosome 5”. Genomics 13 (3): 803–8. DOI:10.1016/0888-7543(92)90156-M. PMID 1322355.
- Armstrong E, Partanen J, Cannizzaro L, et al. (1992). „Localization of the fibroblast growth factor receptor-4 gene to chromosome region 5q33-qter”. Genes Chromosomes Cancer 4 (1): 94–8. DOI:10.1002/gcc.2870040116. PMID 1377018.
- Vainikka S, Partanen J, Bellosta P, et al. (1992). „Fibroblast growth factor receptor-4 shows novel features in genomic structure, ligand binding and signal transduction”. EMBO J. 11 (12): 4273–80. PMC 557000. PMID 1385111.
- Partanen J, Mäkelä TP, Eerola E, et al. (1991). „FGFR-4, a novel acidic fibroblast growth factor receptor with a distinct expression pattern”. EMBO J. 10 (6): 1347–54. PMC 452793. PMID 1709094.
- Holtrich U, Bräuninger A, Strebhardt K, Rübsamen-Waigmann H (1992). „Two additional protein-tyrosine kinases expressed in human lung: fourth member of the fibroblast growth factor receptor family and an intracellular protein-tyrosine kinase”. Proc. Natl. Acad. Sci. U.S.A. 88 (23): 10411–5. DOI:10.1073/pnas.88.23.10411. PMC 52938. PMID 1720539.
- Partanen J, Mäkelä TP, Alitalo R, et al. (1991). „Putative tyrosine kinases expressed in K-562 human leukemia cells”. Proc. Natl. Acad. Sci. U.S.A. 87 (22): 8913–7. DOI:10.1073/pnas.87.22.8913. PMC 55070. PMID 2247464.
- Vainikka S, Joukov V, Wennström S, et al. (1994). „Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1”. J. Biol. Chem. 269 (28): 18320–6. PMID 7518429.
- Wen Z, Zhong Z, Darnell JE (1995). „Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation”. Cell 82 (2): 241–50. DOI:10.1016/0092-8674(95)90311-9. PMID 7543024.
- Quelle FW, Thierfelder W, Witthuhn BA, et al. (1995). „Phosphorylation and activation of the DNA binding activity of purified Stat1 by the Janus protein-tyrosine kinases and the epidermal growth factor receptor”. J. Biol. Chem. 270 (35): 20775–80. DOI:10.1074/jbc.270.35.20775. PMID 7657660.
- Ron D, Reich R, Chedid M, et al. (1993). „Fibroblast growth factor receptor 4 is a high affinity receptor for both acidic and basic fibroblast growth factor but not for keratinocyte growth factor”. J. Biol. Chem. 268 (8): 5388–94. PMID 7680645.
- Shuai K, Stark GR, Kerr IM, Darnell JE (1993). „A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma”. Science 261 (5129): 1744–6. DOI:10.1126/science.7690989. PMID 7690989.
- Jaakkola S, Salmikangas P, Nylund S, et al. (1993). „Amplification of fgfr4 gene in human breast and gynecological cancers”. Int. J. Cancer 54 (3): 378–82. DOI:10.1002/ijc.2910540305. PMID 8099571.
- Maruyama K, Sugano S (1994). „Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene 138 (1–2): 171–4. DOI:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Reich-Slotky R, Shaoul E, Berman B, et al. (1996). „Chimeric molecules between keratinocyte growth factor and basic fibroblast growth factor define domains that confer receptor binding specificities”. J. Biol. Chem. 270 (50): 29813–8. DOI:10.1074/jbc.270.50.29813. PMID 8530375.
- Vainikka S, Joukov V, Klint P, Alitalo K (1996). „Association of a 85-kDa serine kinase with activated fibroblast growth factor receptor-4”. J. Biol. Chem. 271 (3): 1270–3. DOI:10.1074/jbc.271.3.1270. PMID 8576110.
- Kaptein A, Paillard V, Saunders M (1996). „Dominant negative stat3 mutant inhibits interleukin-6-induced Jak-STAT signal transduction”. J. Biol. Chem. 271 (11): 5961–4. DOI:10.1074/jbc.271.11.5961. PMID 8626374.
- Ornitz DM, Xu J, Colvin JS, et al. (1996). „Receptor specificity of the fibroblast growth factor family”. J. Biol. Chem. 271 (25): 15292–7. DOI:10.1074/jbc.271.25.15292. PMID 8663044.
- Agnès F, Toux MM, André C, Galibert F (1997). „Genomic organization of the extracellular coding region of the human FGFR4 and FLT4 genes: evolution of the genes encoding receptor tyrosine kinases with immunoglobulin-like domains”. J. Mol. Evol. 45 (1): 43–9. DOI:10.1007/PL00006199. PMID 9211733.
Vanjske veze
- MeSH FGFR4+protein,+human
- p
- r
- u
Receptorske tirozinske kinaze (EC 2.7.10.1) | |||||||||||||||||||||||||||||||||||||||||||
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Nereceptorske tirozinske kinaze (EC 2.7.10.2) | |||||||||||||||||||||||
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