FES
entrez
2242
canonical
uniprot
P07332
canonical
ensembl
ENSG00000182511
resolver
ensp
ENSP00000331504
resolver
ensp
ENSP00000377837
resolver
ensp
ENSP00000400868
resolver
ensp
ENSP00000414629
resolver
ensp
ENSP00000435811
resolver
ensp
ENSP00000577278
resolver
ensp
ENSP00000577279
resolver
ensp
ENSP00000577285
resolver
ensp
ENSP00000577289
resolver
ensp
ENSP00000577295
resolver
ensp
ENSP00000633683
resolver
ensp
ENSP00000633692
resolver
ensp
ENSP00000633696
resolver
ensp
ENSP00000681432
resolver
genesymbol
FES
resolver
genesymbol_syn
FPS
resolver
hgnc
HGNC:3657
resolver
uniprot
B2R6E6
resolver
uniprot
B4DUD0
resolver
uniprot
E9PC94
resolver
uniprot
E9PC95
resolver
uniprot
Q2VXS7
resolver
uniprot
Q2VXS8
resolver
uniprot
Q2VXT0
resolver
uniprot
Q6GTU5
resolver
uniprot_entry
FES_HUMAN
resolver
uniprot_sec
B2R6E6
resolver
uniprot_sec
B4DUD0
resolver
uniprot_sec
E9PC94
resolver
uniprot_sec
E9PC95
resolver
uniprot_sec
Q2VXS7
resolver
uniprot_sec
Q2VXS8
resolver
uniprot_sec
Q2VXT0
resolver
uniprot_sec
Q6GTU5
resolver
activity_regulation
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}.
uniprot
proteins
amino_acid_sequence
MGFSSELCSPQGHGVLQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSRAISPDSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLSLLIRERQQLRKTYSEQWQQLQQELTKTHSQDIEKLKSQYRALARDSAQAKRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHHHQLLLPGLLRSLQDLHEEMACILKEILQEYLEISSLVQDEVVAIHREMAAAAARIQPEAEYQGFLRQYGSAPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELAVATEMVFRRQEMVTQLQQELRNEEENTHPRERVQLLGKRQVLQEALQGLQVALCSQAKLQAQQELLQTKLEHLGPGEPPPVLLLQDDRHSTSSSEQEREGGRTPTLEILKSHISGIFRPKFSLPPPLQLIPEVQKPLHEQLWYHGAIPRAEVAELLVHSGDFLVRESQGKQEYVLSVLWDGLPRHFIIQSLDNLYRLEGEGFPSIPLLIDHLLSTQQPLTKKSGVVLHRAVPKDKWVLNHEDLVLGEQIGRGNFGEVFSGRLRADNTLVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGARLRVKTLLQMVGDAAAGMEYLESKCCIHRDLAARNCLVTEKNVLKISDFGMSREEADGVYAASGGLRQVPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGASPYPNLSNQQTREFVEKGGRLPCPELCPDAVFRLMEQCWAYEPGQRPSFSTIYQELQSIRKRHR
uniprot
proteins
disease_involvement
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). May function as tumor suppressor in melanoma by preventing melanoma cell proliferation; expression is reduced or absent in samples from some melanoma patients (PubMed:28463229). 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:16455651). May promote growth of renal carcinoma cells (PubMed:19082481). {ECO:0000269|PubMed:16455651, ECO:0000269|PubMed:19082481, ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:2656706, ECO:0000269|PubMed:28463229}.
uniprot
proteins
ec_number
2.7.10.2
uniprot
proteins
function
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}.
uniprot
proteins
mass_dalton
93497
uniprot
proteins
mutagenesis
MUTAGEN 113..114; /note="RK->EE: Reduced binding to membranes containing phosphoinositides."; /evidence="ECO:0000269|PubMed:19001085"; MUTAGEN 113..114; /note="RK->QQ: Reduced binding to membranes containing phosphoinositides."; /evidence="ECO:0000269|PubMed:19001085"; MUTAGEN 145; /note="L->P: Constitutively activated kinase that can act as oncogene. Promotes myeloid cell survival and proliferation."; /evidence="ECO:0000269|PubMed:11509660, ECO:0000269|PubMed:15485904"; MUTAGEN 334; /note="L->P: Abolishes autophosphorylation."; /evidence="ECO:0000269|PubMed:11509660"; MUTAGEN 463; /note="G->V: Abolishes kinase activity."; /evidence="ECO:0000269|PubMed:18775312"; MUTAGEN 483; /note="R->M: Abolishes pTyr binding. Abolishes association with microtubules. Abolishes autophosphorylation. Reduced kinase activity."; /evidence="ECO:0000269|PubMed:15485904, ECO:0000269|PubMed:18775312"; MUTAGEN 590; /note="K->E: Abolishes kinase activity. Fails to inhibit proliferation of melanoma cells."; /evidence="ECO:0000269|PubMed:15485904, ECO:0000269|PubMed:28463229"; MUTAGEN 704; /note="M->V: Reduced autophosphorylation and strongly reduced kinase activity."; /evidence="ECO:0000269|PubMed:15867340, ECO:0000269|PubMed:16455651"; MUTAGEN 706; /note="R->Q: Negligible effect on autophosphorylation and kinase activity."; /evidence="ECO:0000269|PubMed:15867340, ECO:0000269|PubMed:16455651"; MUTAGEN 713; /note="Y->F: Reduces kinase activity by over 90%."; /evidence="ECO:0000269|PubMed:7687763"; MUTAGEN 743; /note="V->M: Strongly reduced autophosphorylation and kinase activity."; /evidence="ECO:0000269|PubMed:15867340, ECO:0000269|PubMed:16455651"; MUTAGEN 759; /note="S->F: Reduced autophosphorylation and strongly reduced kinase activity."; /evidence="ECO:0000269|PubMed:15867340, ECO:0000269|PubMed:16455651
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
protein_family
Fes/fps subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
11339827
uniprot
proteins
pubmed
11509660
uniprot
proteins
pubmed
11994747
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15302586
uniprot
proteins
pubmed
15485904
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15867340
uniprot
proteins
pubmed
15869408
uniprot
proteins
pubmed
15929003
uniprot
proteins
pubmed
16455651
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
16792528
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17595334
uniprot
proteins
pubmed
18046454
uniprot
proteins
pubmed
18775312
uniprot
proteins
pubmed
19001085
uniprot
proteins
pubmed
19051325
uniprot
proteins
pubmed
19082481
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19382747
uniprot
proteins
pubmed
20111072
uniprot
proteins
pubmed
21563194
uniprot
proteins
pubmed
21622225
uniprot
proteins
pubmed
2179816
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2656706
uniprot
proteins
pubmed
28463229
uniprot
proteins
pubmed
4065096
uniprot
proteins
pubmed
7687763
uniprot
proteins
pubmed
8955135
uniprot
proteins
sequence_length
822
uniprot
proteins
subcellular_location
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.
uniprot
proteins