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Tyrosine-protein kinase Fes/Fps (EC 2.7.10.2) (Feline sarcoma/Fujinami avian sarcoma oncogene homolog) (Proto-oncogene c-Fes) (Proto-oncogene c-Fps) (p93c-fes)

 FES_HUMAN               Reviewed;         822 AA.
P07332; B2R6E6; B4DUD0; E9PC94; E9PC95; Q2VXS7; Q2VXS8; Q2VXT0;
Q6GTU5;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 3.
12-SEP-2018, entry version 205.
RecName: Full=Tyrosine-protein kinase Fes/Fps;
EC=2.7.10.2;
AltName: Full=Feline sarcoma/Fujinami avian sarcoma oncogene homolog;
AltName: Full=Proto-oncogene c-Fes;
AltName: Full=Proto-oncogene c-Fps;
AltName: Full=p93c-fes;
Name=FES; Synonyms=FPS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2179816;
Alcalay M., Antolini F., van de Ven W.J.M., Lanfrancone L.,
Grignani F., Pelicci P.G.;
"Characterization of human and mouse c-fes cDNA clones and
identification of the 5' end of the gene.";
Oncogene 5:267-275(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=4065096;
Roebroek A.J.M., Schalken J.A., Verbeek J.S., van den Ouweland A.M.W.,
Onnekink C., Bloemers H.P.J., van de Ven W.J.M.;
"The structure of the human c-fes/fps proto-oncogene.";
EMBO J. 4:2897-2903(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
Lefebvre J.-C.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION IN CELL DIFFERENTIATION AND AS TUMOR SUPPRESSOR, AND
CATALYTIC ACTIVITY.
PubMed=2656706;
Yu G., Smithgall T.E., Glazer R.I.;
"K562 leukemia cells transfected with the human c-fes gene acquire the
ability to undergo myeloid differentiation.";
J. Biol. Chem. 264:10276-10281(1989).
[9]
PHOSPHORYLATION AT TYR-713, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
TYR-713.
PubMed=7687763;
Hjermstad S.J., Peters K.L., Briggs S.D., Glazer R.I., Smithgall T.E.;
"Regulation of the human c-fes protein tyrosine kinase (p93c-fes) by
its src homology 2 domain and major autophosphorylation site (Tyr-
713).";
Oncogene 8:2283-2292(1993).
[10]
FUNCTION IN PHOSPHORYLATION OF BCR, AUTOPHOSPHORYLATION, AND ACTIVITY
REGULATION.
PubMed=8955135; DOI=10.1074/jbc.271.51.32930;
Li J., Smithgall T.E.;
"Co-expression with BCR induces activation of the FES tyrosine kinase
and phosphorylation of specific N-terminal BCR tyrosine residues.";
J. Biol. Chem. 271:32930-32936(1996).
[11]
SUBCELLULAR LOCATION.
PubMed=11339827; DOI=10.1006/excr.2001.5217;
Zirngibl R., Schulze D., Mirski S.E., Cole S.P., Greer P.A.;
"Subcellular localization analysis of the closely related Fps/Fes and
Fer protein-tyrosine kinases suggests a distinct role for Fps/Fes in
vesicular trafficking.";
Exp. Cell Res. 266:87-94(2001).
[12]
FUNCTION IN CELL PROLIFERATION AND CELL SPREADING, CATALYTIC ACTIVITY,
AUTOPHOSPHORYLATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF LEU-145 AND
LEU-334.
PubMed=11509660; DOI=10.1128/MCB.21.18.6170-6180.2001;
Cheng H.Y., Schiavone A.P., Smithgall T.E.;
"A point mutation in the N-terminal coiled-coil domain releases c-Fes
tyrosine kinase activity and survival signaling in myeloid leukemia
cells.";
Mol. Cell. Biol. 21:6170-6180(2001).
[13]
REVIEW.
PubMed=11994747; DOI=10.1038/nrm783;
Greer P.;
"Closing in on the biological functions of Fps/Fes and Fer.";
Nat. Rev. Mol. Cell Biol. 3:278-289(2002).
[14]
FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON AND CELL
DIFFERENTIATION, AND INTERACTION WITH BCR.
PubMed=15302586; DOI=10.1016/j.yexcr.2004.05.010;
Laurent C.E., Smithgall T.E.;
"The c-Fes tyrosine kinase cooperates with the breakpoint cluster
region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-
dependent manner.";
Exp. Cell Res. 299:188-198(2004).
[15]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TUBULIN AND
MICROTUBULES, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-713,
PHOSPHORYLATION BY HCK, AND MUTAGENESIS OF LEU-145; ARG-483 AND
LYS-590.
PubMed=15485904; DOI=10.1128/MCB.24.21.9351-9358.2004;
Laurent C.E., Delfino F.J., Cheng H.Y., Smithgall T.E.;
"The human c-Fes tyrosine kinase binds tubulin and microtubules
through separate domains and promotes microtubule assembly.";
Mol. Cell. Biol. 24:9351-9358(2004).
[16]
CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF MET-704;
ARG-706; VAL-743 AND SER-759.
PubMed=15867340; DOI=10.1158/0008-5472.CAN-04-3468;
Sangrar W., Zirgnibl R.A., Gao Y., Muller W.J., Jia Z., Greer P.A.;
"An identity crisis for fps/fes: oncogene or tumor suppressor?";
Cancer Res. 65:3518-3522(2005).
[17]
ALTERNATIVE SPLICING.
PubMed=15869408; DOI=10.1089/dna.2005.24.311;
Carlson A., Berkowitz J.M., Browning D., Slamon D.J., Gasson J.C.,
Yates K.E.;
"Expression of c-Fes protein isoforms correlates with differentiation
in myeloid leukemias.";
DNA Cell Biol. 24:311-316(2005).
[18]
INTERACTION WITH TRIM28.
PubMed=16792528; DOI=10.1042/BJ20060194;
Delfino F.J., Shaffer J.M., Smithgall T.E.;
"The KRAB-associated co-repressor KAP-1 is a coiled-coil binding
partner, substrate and activator of the c-Fes protein tyrosine
kinase.";
Biochem. J. 399:141-150(2006).
[19]
FUNCTION IN STAT3 PHOSPHORYLATION, ROLE AS PUTATIVE TUMOR SUPPRESSOR
IN COLON CANCER, MUTAGENESIS OF MET-704; ARG-706; VAL-743 AND SER-759,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16455651; DOI=10.1074/jbc.M507331200;
Delfino F.J., Stevenson H., Smithgall T.E.;
"A growth-suppressive function for the c-fes protein-tyrosine kinase
in colorectal cancer.";
J. Biol. Chem. 281:8829-8835(2006).
[20]
FUNCTION IN KIT SIGNALING, AND POSSIBLE ROLE IN CANCER CELL
PROLIFERATION.
PubMed=17595334; DOI=10.1182/blood-2007-02-076471;
Voisset E., Lopez S., Dubreuil P., De Sepulveda P.;
"The tyrosine kinase FES is an essential effector of KITD816V
proliferation signal.";
Blood 110:2593-2599(2007).
[21]
FUNCTION IN CYTOSKELETON REORGANIZATION, INTERACTION WITH EZR,
PHOSPHORYLATION AT TYR-713, AND SUBCELLULAR LOCATION.
PubMed=18046454; DOI=10.1038/sj.emboj.7601943;
Naba A., Reverdy C., Louvard D., Arpin M.;
"Spatial recruitment and activation of the Fes kinase by ezrin
promotes HGF-induced cell scattering.";
EMBO J. 27:38-50(2008).
[22]
SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-713,
PHOSPHORYLATION BY HCK, AND DOMAIN.
PubMed=19382747; DOI=10.1021/bi900238f;
Shaffer J.M., Hellwig S., Smithgall T.E.;
"Bimolecular fluorescence complementation demonstrates that the c-Fes
protein-tyrosine kinase forms constitutive oligomers in living
cells.";
Biochemistry 48:4780-4788(2009).
[23]
FUNCTION, TISSUE SPECIFICITY, AND ROLE AS PUTATIVE TUMOR SUPPRESSOR IN
COLON CANCER.
PubMed=19051325; DOI=10.1002/gcc.20638;
Shaffer J.M., Smithgall T.E.;
"Promoter methylation blocks FES protein-tyrosine kinase gene
expression in colorectal cancer.";
Genes Chromosomes Cancer 48:272-284(2009).
[24]
PUTATIVE ROLE IN RENAL CARCINOMA.
PubMed=19082481;
Kanda S., Miyata Y., Kanetake H., Smithgall T.E.;
"Downregulation of the c-Fes protein-tyrosine kinase inhibits the
proliferation of human renal carcinoma cells.";
Int. J. Oncol. 34:89-96(2009).
[25]
FUNCTION, INTERACTION WITH MS4A2/FCER1B AND HCLS1/HS1, SUBCELLULAR
LOCATION, PHOSPHORYLATION, INTERACTION WITH
PHOSPHOINOSITIDE-CONTAINING MEMBRANES, AND MUTAGENESIS OF
113-ARG-LYS-114.
PubMed=19001085; DOI=10.1128/MCB.00904-08;
McPherson V.A., Everingham S., Karisch R., Smith J.A., Udell C.M.,
Zheng J., Jia Z., Craig A.W.;
"Contributions of F-BAR and SH2 domains of Fes protein tyrosine kinase
for coupling to the FcepsilonRI pathway in mast cells.";
Mol. Cell. Biol. 29:389-401(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-67; TYR-261;
TYR-713 AND SER-716, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[27]
FUNCTION, PHOSPHORYLATION AT THR-421, AND INTERACTION WITH FLT3.
PubMed=20111072; DOI=10.1038/leu.2009.301;
Voisset E., Lopez S., Chaix A., Georges C., Hanssens K., Prebet T.,
Dubreuil P., De Sepulveda P.;
"FES kinases are required for oncogenic FLT3 signaling.";
Leukemia 24:721-728(2010).
[28]
REVIEW.
PubMed=21622225; DOI=10.2741/3902;
Hellwig S., Smithgall T.E.;
"Structure and regulation of the c-Fes protein-tyrosine kinase.";
Front. Biosci. 16:3146-3155(2011).
[29]
POSSIBLE ROLE IN PROSTATE CANCER.
PubMed=21563194; DOI=10.1002/pros.21422;
Miyata Y., Watanabe S.I., Matsuo T., Hayashi T., Sakai H., Xuan J.W.,
Greer P.A., Kanda S.;
"Pathological significance and predictive value for biochemical
recurrence of c-Fes expression in prostate cancer.";
Prostate 72:201-208(2012).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-411, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
STRUCTURE BY NMR OF 450-550.
PubMed=15929003; DOI=10.1007/s10858-005-0946-6;
Scott A., Pantoja-Uceda D., Koshiba S., Inoue M., Kigawa T.,
Terada T., Shirouzu M., Tanaka A., Sugano S., Yokoyama S.,
Guentert P.;
"Solution structure of the Src homology 2 domain from the human feline
sarcoma oncogene Fes.";
J. Biomol. NMR 31:357-361(2005).
[32]
X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 448-822 OF UNPHOSPHORYLATED
APOPROTEIN AND IN COMPLEX WITH STAUROSPORINE AND A SUBSTRATE PEPTIDE,
CATALYTIC ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT TYR-713,
NMR SPECTROSCOPY, AND MUTAGENESIS OF GLY-463 AND ARG-483.
PubMed=18775312; DOI=10.1016/j.cell.2008.07.047;
Filippakopoulos P., Kofler M., Hantschel O., Gish G.D., Grebien F.,
Salah E., Neudecker P., Kay L.E., Turk B.E., Superti-Furga G.,
Pawson T., Knapp S.;
"Structural coupling of SH2-kinase domains links Fes and Abl substrate
recognition and kinase activation.";
Cell 134:793-803(2008).
[33]
VARIANTS [LARGE SCALE ANALYSIS] CYS-85; GLN-246 AND VAL-323.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Tyrosine-protein kinase that acts downstream of cell
surface receptors and plays a role in the regulation of the actin
cytoskeleton, microtubule assembly, cell attachment and cell
spreading. Plays a role in FCER1 (high affinity immunoglobulin
epsilon receptor)-mediated signaling in mast cells. Acts down-
stream of the activated FCER1 receptor and the mast/stem cell
growth factor receptor KIT. Plays a role in the regulation of mast
cell degranulation. Plays a role in the regulation of cell
differentiation and promotes neurite outgrowth in response to NGF
signaling. Plays a role in cell scattering and cell migration in
response to HGF-induced activation of EZR. Phosphorylates BCR and
down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1,
PECAM1, STAT3 and TRIM28. {ECO:0000269|PubMed:11509660,
ECO:0000269|PubMed:15302586, ECO:0000269|PubMed:15485904,
ECO:0000269|PubMed:16455651, ECO:0000269|PubMed:17595334,
ECO:0000269|PubMed:18046454, ECO:0000269|PubMed:19001085,
ECO:0000269|PubMed:19051325, ECO:0000269|PubMed:20111072,
ECO:0000269|PubMed:2656706, ECO:0000269|PubMed:8955135}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:11509660,
ECO:0000269|PubMed:15485904, ECO:0000269|PubMed:15867340,
ECO:0000269|PubMed:18775312, ECO:0000269|PubMed:2656706,
ECO:0000269|PubMed:7687763}.
-!- ACTIVITY REGULATION: Kinase activity is tightly regulated.
Activated in response to signaling from a cell surface receptor.
Activation probably requires binding of a substrate via the SH2
domain, plus autophosphorylation at Tyr-713. Present in an
inactive form in the absence of activating stimuli.
{ECO:0000269|PubMed:18775312, ECO:0000269|PubMed:8955135}.
-!- SUBUNIT: Homooligomer. Interacts with BCR. Interacts (when
activated, via coiled coil domain) with TRIM28. Interacts (via SH2
domain) with phosphorylated EZR, MS4A2/FCER1B and HCLS1/HS1.
Interacts with phosphorylated KIT. Interacts with FLT3. Interacts
(via F-BAR domain) with soluble tubulin. Interacts (via SH2
domain) with microtubules. {ECO:0000269|PubMed:11509660,
ECO:0000269|PubMed:15302586, ECO:0000269|PubMed:15485904,
ECO:0000269|PubMed:16792528, ECO:0000269|PubMed:18046454,
ECO:0000269|PubMed:18775312, ECO:0000269|PubMed:19001085,
ECO:0000269|PubMed:19382747, ECO:0000269|PubMed:20111072}.
-!- INTERACTION:
P10275:AR; NbExp=3; IntAct=EBI-1055635, EBI-608057;
P15311:EZR; NbExp=8; IntAct=EBI-1055635, EBI-1056902;
Q13480:GAB1; NbExp=2; IntAct=EBI-1055635, EBI-517684;
P10721:KIT; NbExp=2; IntAct=EBI-1055635, EBI-1379503;
P54274:TERF1; NbExp=2; IntAct=EBI-1055635, EBI-710997;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton.
Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Cytoplasmic vesicle. Golgi apparatus. Cell junction, focal
adhesion. Note=Distributed throughout the cytosol when the kinase
is not activated. Association with microtubules requires
activation of the kinase activity. Shuttles between focal
adhesions and cell-cell contacts in epithelial cells. Recruited to
the lateral cell membrane in polarized epithelial cells by
interaction with phosphorylated EZR. Detected at tubular membrane
structures in the cytoplasm and at the cell periphery.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P07332-1; Sequence=Displayed;
Name=2; Synonyms=Variant 1;
IsoId=P07332-2; Sequence=VSP_041748, VSP_041749;
Name=3; Synonyms=Variant 3;
IsoId=P07332-3; Sequence=VSP_041748;
Name=4; Synonyms=Variant 4;
IsoId=P07332-4; Sequence=VSP_041749;
-!- TISSUE SPECIFICITY: Widely expressed. Detected in adult colon
epithelium. {ECO:0000269|PubMed:16455651,
ECO:0000269|PubMed:19051325}.
-!- DOMAIN: The coiled coil domains are important for regulating the
kinase activity. They mediate homooligomerization and probably
also interaction with other proteins.
-!- DOMAIN: The N-terminal region including the first coiled coil
domain mediates interaction with phosphoinositide-containing
membranes.
-!- PTM: Autophosphorylated on Tyr-713. Phosphorylated by LYN in
response to FCER1 activation. Phosphorylated by HCK.
{ECO:0000269|PubMed:15485904, ECO:0000269|PubMed:18046454,
ECO:0000269|PubMed:18775312, ECO:0000269|PubMed:19001085,
ECO:0000269|PubMed:19382747, ECO:0000269|PubMed:20111072,
ECO:0000269|PubMed:7687763}.
-!- DISEASE: Note=Has been shown to act as proto-oncogene in some
types of cancer, possibly due to abnormal activation of the
kinase. Has been shown to act as tumor suppressor in other types
of cancer. Expressed and present as activated kinase in a subset
of acute myeloid leukemia patients; promotes survival of leukemia
cells (PubMed:20111072). Expression is absent in K562 leukemia
cells; ectopic expression of FSP/FES restores myeloid
differentiation (PubMed:2656706). May function as tumor suppressor
in colorectal cancer; expression is reduced or absent in samples
from some colon cancer patients (PubMed:16455651). Ectopic
expression of FSP/FES suppresses anchorage-independent growth in
colon cancer cell lines (PubMed:16455651). Up-regulated in
prostate cancer, and might be a predictor of recurrence after
radical surgery (PubMed:21563194). May promote growth of renal
carcinoma cells (PubMed:19082481). {ECO:0000269|PubMed:16455651,
ECO:0000269|PubMed:19082481, ECO:0000269|PubMed:20111072,
ECO:0000269|PubMed:21563194, ECO:0000269|PubMed:2656706}.
-!- MISCELLANEOUS: Cellular homolog of retroviral oncogenes. In
contrast to the viral oncoproteins, the kinase activity of
cellular FSP/FES is tightly regulated, and the kinase is inactive
in normal cells in the absence of activating stimuli
(PubMed:15485904). {ECO:0000305|PubMed:15485904}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; X52192; CAA36438.1; -; mRNA.
EMBL; X06292; CAA29619.1; -; Genomic_DNA.
EMBL; AY513654; AAS82866.1; -; mRNA.
EMBL; AY513656; AAS82868.1; -; mRNA.
EMBL; AY513657; AAS82869.1; -; mRNA.
EMBL; AK300595; BAG62292.1; -; mRNA.
EMBL; AK312545; BAG35443.1; -; mRNA.
EMBL; AC124248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471101; EAX02114.1; -; Genomic_DNA.
EMBL; BC035357; AAH35357.1; -; mRNA.
CCDS; CCDS10365.1; -. [P07332-1]
CCDS; CCDS45349.1; -. [P07332-4]
CCDS; CCDS45350.1; -. [P07332-3]
CCDS; CCDS45351.1; -. [P07332-2]
PIR; A24673; TVHUFF.
RefSeq; NP_001137255.1; NM_001143783.1. [P07332-3]
RefSeq; NP_001137256.1; NM_001143784.1. [P07332-4]
RefSeq; NP_001137257.1; NM_001143785.1. [P07332-2]
RefSeq; NP_001996.1; NM_002005.3. [P07332-1]
RefSeq; XP_005254937.1; XM_005254880.1. [P07332-3]
RefSeq; XP_005254939.1; XM_005254882.1. [P07332-4]
RefSeq; XP_016877494.1; XM_017022005.1. [P07332-1]
RefSeq; XP_016877495.1; XM_017022006.1. [P07332-3]
RefSeq; XP_016877496.1; XM_017022007.1. [P07332-4]
RefSeq; XP_016877497.1; XM_017022008.1. [P07332-2]
RefSeq; XP_016877498.1; XM_017022009.1. [P07332-1]
RefSeq; XP_016877499.1; XM_017022010.1. [P07332-3]
UniGene; Hs.7636; -.
PDB; 1WQU; NMR; -; A=450-550.
PDB; 2DCR; NMR; -; A=450-550.
PDB; 3BKB; X-ray; 1.78 A; A=448-822.
PDB; 3CBL; X-ray; 1.75 A; A=448-822.
PDB; 3CD3; X-ray; 1.98 A; A=448-822.
PDB; 4DYL; X-ray; 2.18 A; A=1-405.
PDB; 4E93; X-ray; 1.84 A; A=448-822.
PDBsum; 1WQU; -.
PDBsum; 2DCR; -.
PDBsum; 3BKB; -.
PDBsum; 3CBL; -.
PDBsum; 3CD3; -.
PDBsum; 4DYL; -.
PDBsum; 4E93; -.
ProteinModelPortal; P07332; -.
SMR; P07332; -.
BioGrid; 108533; 25.
IntAct; P07332; 22.
MINT; P07332; -.
STRING; 9606.ENSP00000331504; -.
BindingDB; P07332; -.
ChEMBL; CHEMBL5455; -.
GuidetoPHARMACOLOGY; 2023; -.
iPTMnet; P07332; -.
PhosphoSitePlus; P07332; -.
BioMuta; FES; -.
DMDM; 115502390; -.
EPD; P07332; -.
MaxQB; P07332; -.
PaxDb; P07332; -.
PeptideAtlas; P07332; -.
PRIDE; P07332; -.
ProteomicsDB; 51989; -.
ProteomicsDB; 51990; -. [P07332-2]
ProteomicsDB; 51991; -. [P07332-3]
ProteomicsDB; 51992; -. [P07332-4]
DNASU; 2242; -.
Ensembl; ENST00000328850; ENSP00000331504; ENSG00000182511. [P07332-1]
Ensembl; ENST00000394300; ENSP00000377837; ENSG00000182511. [P07332-3]
Ensembl; ENST00000414248; ENSP00000414629; ENSG00000182511. [P07332-2]
Ensembl; ENST00000444422; ENSP00000400868; ENSG00000182511. [P07332-4]
GeneID; 2242; -.
KEGG; hsa:2242; -.
UCSC; uc002bpv.4; human. [P07332-1]
CTD; 2242; -.
DisGeNET; 2242; -.
EuPathDB; HostDB:ENSG00000182511.11; -.
GeneCards; FES; -.
HGNC; HGNC:3657; FES.
HPA; HPA001376; -.
MIM; 190030; gene.
neXtProt; NX_P07332; -.
OpenTargets; ENSG00000182511; -.
PharmGKB; PA28098; -.
eggNOG; KOG0194; Eukaryota.
eggNOG; ENOG410Y6RP; LUCA.
GeneTree; ENSGT00760000119011; -.
HOVERGEN; HBG005655; -.
InParanoid; P07332; -.
KO; K07527; -.
OMA; PKDKWAL; -.
OrthoDB; EOG091G01S4; -.
PhylomeDB; P07332; -.
TreeFam; TF315363; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
SignaLink; P07332; -.
SIGNOR; P07332; -.
EvolutionaryTrace; P07332; -.
GeneWiki; Feline_sarcoma_oncogene; -.
GenomeRNAi; 2242; -.
PRO; PR:P07332; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000182511; Expressed in 114 organ(s), highest expression level in spleen.
CleanEx; HS_FES; -.
ExpressionAtlas; P07332; baseline and differential.
Genevisible; P07332; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0034987; F:immunoglobulin receptor binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0007098; P:centrosome cycle; IEA:Ensembl.
GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0001578; P:microtubule bundle formation; IEA:Ensembl.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
GO; GO:0045639; P:positive regulation of myeloid cell differentiation; IMP:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0045595; P:regulation of cell differentiation; IMP:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0043304; P:regulation of mast cell degranulation; IMP:UniProtKB.
GO; GO:0060627; P:regulation of vesicle-mediated transport; TAS:UniProtKB.
CDD; cd10361; SH2_Fps_family; 1.
Gene3D; 1.20.1270.60; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR031160; F_BAR.
InterPro; IPR001060; FCH_dom.
InterPro; IPR035849; Fes/Fps/Fer_SH2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR016250; Tyr-prot_kinase_Fes/Fps.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
PIRSF; PIRSF000632; TyrPK_fps; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00055; FCH; 1.
SMART; SM00252; SH2; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51741; F_BAR; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell junction;
Cell membrane; Coiled coil; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Golgi apparatus; Kinase;
Lipid-binding; Membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome; SH2 domain;
Transferase; Tumor suppressor; Tyrosine-protein kinase.
CHAIN 1 822 Tyrosine-protein kinase Fes/Fps.
/FTId=PRO_0000088088.
DOMAIN 1 260 F-BAR. {ECO:0000255|PROSITE-
ProRule:PRU01077}.
DOMAIN 460 549 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 561 822 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 567 575 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 300 Important for interaction with membranes
containing phosphoinositides.
COILED 125 169 {ECO:0000255}.
COILED 324 368 {ECO:0000255}.
ACT_SITE 683 683 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 590 590 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 261 261 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 421 421 Phosphothreonine.
{ECO:0000269|PubMed:20111072}.
MOD_RES 713 713 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:15485904,
ECO:0000269|PubMed:18046454,
ECO:0000269|PubMed:18775312,
ECO:0000269|PubMed:19382747,
ECO:0000269|PubMed:7687763}.
MOD_RES 716 716 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
VAR_SEQ 72 129 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_041748.
VAR_SEQ 441 510 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_041749.
VARIANT 85 85 R -> C (in dbSNP:rs56041861).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041697.
VARIANT 246 246 R -> Q (in dbSNP:rs34573430).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041698.
VARIANT 323 323 M -> V (in dbSNP:rs56296062).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041699.
MUTAGEN 113 114 RK->EE: Reduced binding to membranes
containing phosphoinositides.
{ECO:0000269|PubMed:19001085}.
MUTAGEN 113 114 RK->QQ: Reduced binding to membranes
containing phosphoinositides.
{ECO:0000269|PubMed:19001085}.
MUTAGEN 145 145 L->P: Constitutively activated kinase
that can act as oncogene. Promotes
myeloid cell survival and proliferation.
{ECO:0000269|PubMed:11509660,
ECO:0000269|PubMed:15485904}.
MUTAGEN 334 334 L->P: Abolishes autophosphorylation.
{ECO:0000269|PubMed:11509660}.
MUTAGEN 463 463 G->V: Abolishes kinase activity.
{ECO:0000269|PubMed:18775312}.
MUTAGEN 483 483 R->M: Abolishes pTyr binding. Abolishes
association with microtubules. Abolishes
autophosphorylation. Reduced kinase
activity. {ECO:0000269|PubMed:15485904,
ECO:0000269|PubMed:18775312}.
MUTAGEN 590 590 K->E: Abolishes kinase activity.
{ECO:0000269|PubMed:15485904}.
MUTAGEN 704 704 M->V: Reduced autophosphorylation and
strongly reduced kinase activity.
{ECO:0000269|PubMed:15867340,
ECO:0000269|PubMed:16455651}.
MUTAGEN 706 706 R->Q: Negligible effect on
autophosphorylation and kinase activity.
{ECO:0000269|PubMed:15867340,
ECO:0000269|PubMed:16455651}.
MUTAGEN 713 713 Y->F: Reduces kinase activity by over
90%. {ECO:0000269|PubMed:7687763}.
MUTAGEN 743 743 V->M: Strongly reduced
autophosphorylation and kinase activity.
{ECO:0000269|PubMed:15867340,
ECO:0000269|PubMed:16455651}.
MUTAGEN 759 759 S->F: Reduced autophosphorylation and
strongly reduced kinase activity.
{ECO:0000269|PubMed:15867340,
ECO:0000269|PubMed:16455651}.
CONFLICT 719 719 L -> S (in Ref. 1; CAA36438 and 3;
AAS82866/AAS82869/AAS82868).
{ECO:0000305}.
HELIX 3 6 {ECO:0000244|PDB:4DYL}.
HELIX 10 51 {ECO:0000244|PDB:4DYL}.
HELIX 68 96 {ECO:0000244|PDB:4DYL}.
HELIX 98 131 {ECO:0000244|PDB:4DYL}.
HELIX 133 154 {ECO:0000244|PDB:4DYL}.
HELIX 167 202 {ECO:0000244|PDB:4DYL}.
HELIX 204 234 {ECO:0000244|PDB:4DYL}.
STRAND 236 238 {ECO:0000244|PDB:4DYL}.
HELIX 239 254 {ECO:0000244|PDB:4DYL}.
HELIX 257 259 {ECO:0000244|PDB:4DYL}.
HELIX 262 268 {ECO:0000244|PDB:4DYL}.
TURN 300 302 {ECO:0000244|PDB:4DYL}.
HELIX 303 344 {ECO:0000244|PDB:4DYL}.
HELIX 350 353 {ECO:0000244|PDB:4DYL}.
HELIX 354 389 {ECO:0000244|PDB:4DYL}.
TURN 390 393 {ECO:0000244|PDB:4DYL}.
HELIX 450 452 {ECO:0000244|PDB:3CBL}.
HELIX 455 457 {ECO:0000244|PDB:3CBL}.
STRAND 461 464 {ECO:0000244|PDB:1WQU}.
HELIX 467 473 {ECO:0000244|PDB:3CBL}.
STRAND 479 484 {ECO:0000244|PDB:3CBL}.
TURN 486 489 {ECO:0000244|PDB:3BKB}.
STRAND 491 494 {ECO:0000244|PDB:3CBL}.
STRAND 503 506 {ECO:0000244|PDB:3CBL}.
STRAND 507 509 {ECO:0000244|PDB:3BKB}.
STRAND 512 517 {ECO:0000244|PDB:3BKB}.
STRAND 520 522 {ECO:0000244|PDB:3BKB}.
HELIX 523 533 {ECO:0000244|PDB:3CBL}.
TURN 539 541 {ECO:0000244|PDB:3BKB}.
HELIX 558 560 {ECO:0000244|PDB:3CBL}.
STRAND 561 570 {ECO:0000244|PDB:3CBL}.
STRAND 573 580 {ECO:0000244|PDB:3CBL}.
TURN 581 583 {ECO:0000244|PDB:3CBL}.
STRAND 586 591 {ECO:0000244|PDB:3CBL}.
HELIX 598 601 {ECO:0000244|PDB:3CBL}.
HELIX 602 605 {ECO:0000244|PDB:3CBL}.
HELIX 606 611 {ECO:0000244|PDB:3CBL}.
STRAND 622 626 {ECO:0000244|PDB:3CBL}.
STRAND 628 631 {ECO:0000244|PDB:3CBL}.
STRAND 633 637 {ECO:0000244|PDB:3CBL}.
HELIX 644 651 {ECO:0000244|PDB:3CBL}.
HELIX 652 654 {ECO:0000244|PDB:3CBL}.
HELIX 657 676 {ECO:0000244|PDB:3CBL}.
HELIX 686 688 {ECO:0000244|PDB:3CBL}.
STRAND 689 691 {ECO:0000244|PDB:3CBL}.
STRAND 697 699 {ECO:0000244|PDB:3CBL}.
HELIX 702 704 {ECO:0000244|PDB:3CBL}.
STRAND 711 714 {ECO:0000244|PDB:3CBL}.
STRAND 720 723 {ECO:0000244|PDB:3CBL}.
HELIX 724 726 {ECO:0000244|PDB:3CBL}.
HELIX 729 734 {ECO:0000244|PDB:3CBL}.
STRAND 736 738 {ECO:0000244|PDB:3CBL}.
HELIX 739 754 {ECO:0000244|PDB:3CBL}.
TURN 755 757 {ECO:0000244|PDB:4E93}.
HELIX 766 774 {ECO:0000244|PDB:3CBL}.
HELIX 787 796 {ECO:0000244|PDB:3CBL}.
HELIX 801 803 {ECO:0000244|PDB:3CBL}.
HELIX 807 820 {ECO:0000244|PDB:3CBL}.
SEQUENCE 822 AA; 93497 MW; 4C2A90555857F045 CRC64;
MGFSSELCSP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH MSLQDSGGQS
RAISPDSPIS QSWAEITSQT EGLSRLLRQH AEDLNSGPLS KLSLLIRERQ QLRKTYSEQW
QQLQQELTKT HSQDIEKLKS QYRALARDSA QAKRKYQEAS KDKDRDKAKD KYVRSLWKLF
AHHNRYVLGV RAAQLHHQHH HQLLLPGLLR SLQDLHEEMA CILKEILQEY LEISSLVQDE
VVAIHREMAA AAARIQPEAE YQGFLRQYGS APDVPPCVTF DESLLEEGEP LEPGELQLNE
LTVESVQHTL TSVTDELAVA TEMVFRRQEM VTQLQQELRN EEENTHPRER VQLLGKRQVL
QEALQGLQVA LCSQAKLQAQ QELLQTKLEH LGPGEPPPVL LLQDDRHSTS SSEQEREGGR
TPTLEILKSH ISGIFRPKFS LPPPLQLIPE VQKPLHEQLW YHGAIPRAEV AELLVHSGDF
LVRESQGKQE YVLSVLWDGL PRHFIIQSLD NLYRLEGEGF PSIPLLIDHL LSTQQPLTKK
SGVVLHRAVP KDKWVLNHED LVLGEQIGRG NFGEVFSGRL RADNTLVAVK SCRETLPPDL
KAKFLQEARI LKQYSHPNIV RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT EGARLRVKTL
LQMVGDAAAG MEYLESKCCI HRDLAARNCL VTEKNVLKIS DFGMSREEAD GVYAASGGLR
QVPVKWTAPE ALNYGRYSSE SDVWSFGILL WETFSLGASP YPNLSNQQTR EFVEKGGRLP
CPELCPDAVF RLMEQCWAYE PGQRPSFSTI YQELQSIRKR HR


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10-782-55042 Transcription factor AP-1 - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 N_A 0.05 mg
18-785-210083 c-Jun (Phospho-Thr93) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
28-797 The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex 0.1 mg
31-233 The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex 0.1 mg
18-785-210080 c-Jun (Phospho-Ser63) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
28-798 The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex 0.05 mg
18-785-210083 c-Jun (Phospho-Thr93) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-003-43188 Transcription factor AP-1 - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg Protein A


 

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