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Tyrosine-protein kinase Fer (EC 2.7.10.2) (Feline encephalitis virus-related kinase FER) (Fujinami poultry sarcoma/Feline sarcoma-related protein Fer) (Proto-oncogene c-Fer) (Tyrosine kinase 3) (p94-Fer)

 FER_HUMAN               Reviewed;         822 AA.
P16591; B2RCR4; B4DSQ2; H2FLB8;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 2.
27-SEP-2017, entry version 190.
RecName: Full=Tyrosine-protein kinase Fer;
EC=2.7.10.2;
AltName: Full=Feline encephalitis virus-related kinase FER;
AltName: Full=Fujinami poultry sarcoma/Feline sarcoma-related protein Fer;
AltName: Full=Proto-oncogene c-Fer;
AltName: Full=Tyrosine kinase 3;
AltName: Full=p94-Fer;
Name=FER; Synonyms=TYK3;
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), AND VARIANT VAL-439.
PubMed=2725517; DOI=10.1128/MCB.9.4.1587;
Hao Q.-L., Heisterkamp N., Groffen J.;
"Isolation and sequence analysis of a novel human tyrosine kinase
gene.";
Mol. Cell. Biol. 9:1587-1593(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE PROMOTER USAGE,
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=22223638; DOI=10.1074/jbc.M111.327106;
Makovski A., Yaffe E., Shpungin S., Nir U.;
"Intronic promoter drives the BORIS-regulated expression of FerT in
colon carcinoma cells.";
J. Biol. Chem. 287:6100-6112(2012).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 686-741.
PubMed=8247543;
Lee S.-T., Strunk K.M., Spritz R.A.;
"A survey of protein tyrosine kinase mRNAs expressed in normal human
melanocytes.";
Oncogene 8:3403-3410(1993).
[7]
TISSUE SPECIFICITY.
PubMed=2156206;
Krolewski J.J., Lee R., Eddy R., Shows T.B., Dalla-Favera R.;
"Identification and chromosomal mapping of new human tyrosine kinase
genes.";
Oncogene 5:277-282(1990).
[8]
SUBCELLULAR LOCATION.
PubMed=1990274; DOI=10.1128/MCB.11.2.1180;
Hao Q.-L., Ferris D.K., White G., Heisterkamp N., Groffen J.;
"Nuclear and cytoplasmic location of the FER tyrosine kinase.";
Mol. Cell. Biol. 11:1180-1183(1991).
[9]
FUNCTION IN PHOSPHORYLATION OF CTNND1, AUTOPHOSPHORYLATION, SUBUNIT,
AND INTERACTION WITH CTNND1.
PubMed=7623846; DOI=10.1128/MCB.15.8.4553;
Kim L., Wong T.W.;
"The cytoplasmic tyrosine kinase FER is associated with the catenin-
like substrate pp120 and is activated by growth factors.";
Mol. Cell. Biol. 15:4553-4561(1995).
[10]
FUNCTION IN PHOSPHORYLATION OF CTTN, INTERACTION WITH CTTN; CTNND1 AND
PDGFR, MUTAGENESIS OF LYS-591, AND SUBCELLULAR LOCATION.
PubMed=9722593; DOI=10.1074/jbc.273.36.23542;
Kim L., Wong T.W.;
"Growth factor-dependent phosphorylation of the actin-binding protein
cortactin is mediated by the cytoplasmic tyrosine kinase FER.";
J. Biol. Chem. 273:23542-23548(1998).
[11]
FUNCTION IN PHOSPHORYLATION OF PECAM1; PTPN11 AND GAB1, SUBCELLULAR
LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-483, AND INTERACTION
WITH PECAM1.
PubMed=12972546; DOI=10.1091/mbc.E03-02-0080;
Kogata N., Masuda M., Kamioka Y., Yamagishi A., Endo A., Okada M.,
Mochizuki N.;
"Identification of Fer tyrosine kinase localized on microtubules as a
platelet endothelial cell adhesion molecule-1 phosphorylating kinase
in vascular endothelial cells.";
Mol. Biol. Cell 14:3553-3564(2003).
[12]
FUNCTION IN PHOSPHORYLATION OF JUP AND IN REGULATION OF PROTEIN
PHOSPHORYLATION.
PubMed=14517306; DOI=10.1128/MCB.23.20.7391-7402.2003;
Miravet S., Piedra J., Castano J., Raurell I., Franci C., Dunach M.,
Garcia de Herreros A.;
"Tyrosine phosphorylation of plakoglobin causes contrary effects on
its association with desmosomes and adherens junction components and
modulates beta-catenin-mediated transcription.";
Mol. Cell. Biol. 23:7391-7402(2003).
[13]
SUBCELLULAR LOCATION, LIPID-BINDING, AND DOMAIN.
PubMed=16418535; DOI=10.1083/jcb.200508091;
Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T.,
Takenawa T.;
"Coordination between the actin cytoskeleton and membrane deformation
by a novel membrane tubulation domain of PCH proteins is involved in
endocytosis.";
J. Cell Biol. 172:269-279(2006).
[14]
IDENTIFICATION OF ISOFORM 3, AND TISSUE SPECIFICITY.
PubMed=18985748; DOI=10.1002/dvdy.21789;
Kierszenbaum A.L., Rivkin E., Tres L.L.;
"Expression of Fer testis (FerT) tyrosine kinase transcript variants
and distribution sites of FerT during the development of the acrosome-
acroplaxome-manchette complex in rat spermatids.";
Dev. Dyn. 237:3882-3891(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402 AND SER-434, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[16]
FUNCTION IN PHOSPHORYLATION OF PTK2/FAK1, FUNCTION IN REGULATION OF
ACTIN CYTOSKELETON, SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH CTTN
AND PTK2/FAK1.
PubMed=19339212; DOI=10.1016/j.bbamcr.2009.01.015;
Oh M.A., Choi S., Lee M.J., Choi M.C., Lee S.A., Ko W., Cance W.G.,
Oh E.S., Buday L., Kim S.H., Lee J.W.;
"Specific tyrosine phosphorylation of focal adhesion kinase mediated
by Fer tyrosine kinase in suspended hepatocytes.";
Biochim. Biophys. Acta 1793:781-791(2009).
[17]
INTERACTION WITH HSP90.
PubMed=19159681; DOI=10.1016/j.cellsig.2008.12.011;
Hikri E., Shpungin S., Nir U.;
"Hsp90 and a tyrosine embedded in the Hsp90 recognition loop are
required for the Fer tyrosine kinase activity.";
Cell. Signal. 21:588-596(2009).
[18]
FUNCTION IN IL6 SIGNALING PATHWAY; CELL PROLIFERATION AND IN
PHOSPHORYLATION OF STAT3, AND INTERACTION WITH STAT3.
PubMed=19147545; DOI=10.1158/1541-7786.MCR-08-0117;
Zoubeidi A., Rocha J., Zouanat F.Z., Hamel L., Scarlata E.,
Aprikian A.G., Chevalier S.;
"The Fer tyrosine kinase cooperates with interleukin-6 to activate
signal transducer and activator of transcription 3 and promote human
prostate cancer cell growth.";
Mol. Cancer Res. 7:142-155(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402 AND SER-434, 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).
[20]
FUNCTION IN REGULATION OF ACTIN CYTOSKELETON AND CELL MIGRATION,
CATALYTIC ACTIVITY, DOMAIN, LIPID-BINDING, AND ENZYME REGULATION.
PubMed=19738202; DOI=10.1126/scisignal.2000393;
Itoh T., Hasegawa J., Tsujita K., Kanaho Y., Takenawa T.;
"The tyrosine kinase Fer is a downstream target of the PLD-PA pathway
that regulates cell migration.";
Sci. Signal. 2:RA52-RA52(2009).
[21]
FUNCTION IN CELL PROLIFERATION, PHOSPHORYLATION, 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).
[22]
FUNCTION IN ACTIVATION OF NF-KAPPA-B DOWNSTREAM OF EGFR AND CELL
PROLIFERATION, INTERACTION WITH EGFR, AND PHOSPHORYLATION.
PubMed=21518868; DOI=10.1073/pnas.1105369108;
Guo C., Stark G.R.;
"FER tyrosine kinase (FER) overexpression mediates resistance to
quinacrine through EGF-dependent activation of NF-kappaB.";
Proc. Natl. Acad. Sci. U.S.A. 108:7968-7973(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
STRUCTURE BY NMR OF 453-557.
Northeast structural genomics consortium (NESG);
"Solution structure of SH2 domain of proto-oncogene tyrosine-protein
kinase FER from Homo sapiens, Northeast structural genomics consortium
(NESG) target HR3461D.";
Submitted (AUG-2009) to the PDB data bank.
[25]
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).
[26]
VARIANT VAL-439.
PubMed=1651563; DOI=10.1126/science.1651563;
Nishisho I., Nakamura Y., Miyoshi Y., Miki Y., Ando H., Horii A.,
Koyama K., Utsunomiya J., Baba S., Hedge P., Markham A., Krush A.J.,
Petersen G.M., Hamilton S.R., Nilbert M.C., Levy D.B., Bryan T.M.,
Preisinger A.C., Smith K.J., Su L.-K., Kinzler K.W., Vogelstein B.;
"Mutations of chromosome 5q21 genes in FAP and colorectal cancer
patients.";
Science 253:665-669(1991).
[27]
VARIANTS [LARGE SCALE ANALYSIS] PHE-128; GLN-404; VAL-412; VAL-439;
PRO-443; CYS-460 AND GLN-813.
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 for growth factors and plays a role in the
regulation of the actin cytoskeleton, microtubule assembly,
lamellipodia formation, cell adhesion, cell migration and
chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts
downstream of EGFR to promote activation of NF-kappa-B and cell
proliferation. May play a role in the regulation of the mitotic
cell cycle. Plays a role in the insulin receptor signaling pathway
and in activation of phosphatidylinositol 3-kinase. Acts
downstream of the activated FCER1 receptor and plays a role in
FCER1 (high affinity immunoglobulin epsilon receptor)-mediated
signaling in mast cells. Plays a role in the regulation of mast
cell degranulation. Plays a role in leukocyte recruitment and
diapedesis in response to bacterial lipopolysaccharide (LPS).
Plays a role in synapse organization, trafficking of synaptic
vesicles, the generation of excitatory postsynaptic currents and
neuron-neuron synaptic transmission. Plays a role in neuronal cell
death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1,
GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can
phosphorylate STAT3, but the biological relevance of this depends
on cell type and stimulus. {ECO:0000269|PubMed:12972546,
ECO:0000269|PubMed:14517306, ECO:0000269|PubMed:19147545,
ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:19738202,
ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:21518868,
ECO:0000269|PubMed:22223638, ECO:0000269|PubMed:7623846,
ECO:0000269|PubMed:9722593}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:12972546,
ECO:0000269|PubMed:19738202}.
-!- ENZYME REGULATION: Activated by phosphatidic acid binding.
Activated by hydrogen peroxide (in vitro). Activated by reactive
oxygen species (ROS). {ECO:0000269|PubMed:19738202}.
-!- SUBUNIT: Homotrimer. Interacts with ARHGDIA, IRS1, JAK1, NRP1,
PIK3R1, PLEC and TMF1. Interacts with PPP1CA and regulates its
phosphorylation at 'Thr-320' (By similarity). Interacts with
CTNND1, EGFR, FLT3, PECAM1, PDGFR and STAT3. Interacts (via SH2
domain) with CTTN. Interacts with HSP90; this stabilizes
phosphorylated FER and protects FER against proteasomal
degradation. Component of a complex that contains at least FER,
CTTN and PTK2/FAK1. {ECO:0000250, ECO:0000269|PubMed:12972546,
ECO:0000269|PubMed:19147545, ECO:0000269|PubMed:19159681,
ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:20111072,
ECO:0000269|PubMed:21518868, ECO:0000269|PubMed:7623846,
ECO:0000269|PubMed:9722593}.
-!- INTERACTION:
O42486:Bcat (xeno); NbExp=2; IntAct=EBI-1380661, EBI-972394;
Q16543:CDC37; NbExp=2; IntAct=EBI-1380661, EBI-295634;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
membrane; Peripheral membrane protein; Cytoplasmic side. Cell
projection. Cell junction. Membrane; Peripheral membrane protein;
Cytoplasmic side. Nucleus. Cytoplasm, cell cortex. Note=Associated
with the chromatin. Detected on microtubules in polarized and
motile vascular endothelial cells. Colocalizes with F-actin at the
cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-
cell contacts.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
Name=1; Synonyms=p94;
IsoId=P16591-1; Sequence=Displayed;
Name=2;
IsoId=P16591-2; Sequence=VSP_041765;
Name=3; Synonyms=FerT, p47;
IsoId=P16591-3; Sequence=VSP_043846, VSP_043847;
Note=Produced by alternative promoter usage.;
-!- TISSUE SPECIFICITY: Isoform 1 is detected in normal colon and in
fibroblasts (at protein level). Isoform 3 is detected in normal
testis, in colon carcinoma-derived metastases in lung, liver and
ovary, and in colon carcinoma and hepato carcinoma cell lines (at
protein level). Isoform 3 is not detected in normal colon or in
normal fibroblasts (at protein level). Widely expressed.
{ECO:0000269|PubMed:18985748, ECO:0000269|PubMed:2156206,
ECO:0000269|PubMed:22223638}.
-!- DOMAIN: The coiled coil domains mediate homooligomerization and
are required for location at microtubules.
-!- DOMAIN: The N-terminal region including the first coiled coil
domain mediates interaction with phosphoinositide-containing
membranes.
-!- PTM: Autophosphorylated. {ECO:0000269|PubMed:20111072,
ECO:0000269|PubMed:21518868}.
-!- PTM: Polyubiquitinated; this leads to proteasomal degradation.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; J03358; AAA61190.1; -; mRNA.
EMBL; JQ412173; AEY69041.1; -; mRNA.
EMBL; AK299855; BAG61714.1; -; mRNA.
EMBL; AK315234; BAG37661.1; -; mRNA.
EMBL; AC034207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC109481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC116428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471086; EAW49055.1; -; Genomic_DNA.
CCDS; CCDS4098.1; -. [P16591-1]
CCDS; CCDS78044.1; -. [P16591-3]
PIR; A31943; TVHUFE.
RefSeq; NP_001294957.1; NM_001308028.1. [P16591-2]
RefSeq; NP_001294960.1; NM_001308031.1. [P16591-3]
RefSeq; NP_001294967.1; NM_001308038.1.
RefSeq; NP_005237.2; NM_005246.3. [P16591-1]
RefSeq; XP_011541573.1; XM_011543271.2. [P16591-1]
RefSeq; XP_016864719.1; XM_017009230.1. [P16591-1]
RefSeq; XP_016864720.1; XM_017009231.1. [P16591-1]
UniGene; Hs.107418; -.
UniGene; Hs.221472; -.
UniGene; Hs.625304; -.
PDB; 2KK6; NMR; -; A=453-557.
PDBsum; 2KK6; -.
ProteinModelPortal; P16591; -.
SMR; P16591; -.
BioGrid; 108532; 21.
IntAct; P16591; 19.
MINT; MINT-261636; -.
STRING; 9606.ENSP00000281092; -.
BindingDB; P16591; -.
ChEMBL; CHEMBL3982; -.
GuidetoPHARMACOLOGY; 2022; -.
iPTMnet; P16591; -.
PhosphoSitePlus; P16591; -.
BioMuta; FER; -.
DMDM; 97536202; -.
EPD; P16591; -.
PaxDb; P16591; -.
PeptideAtlas; P16591; -.
PRIDE; P16591; -.
DNASU; 2241; -.
Ensembl; ENST00000281092; ENSP00000281092; ENSG00000151422. [P16591-1]
Ensembl; ENST00000618353; ENSP00000484767; ENSG00000151422. [P16591-3]
GeneID; 2241; -.
KEGG; hsa:2241; -.
UCSC; uc031skp.2; human. [P16591-1]
CTD; 2241; -.
DisGeNET; 2241; -.
EuPathDB; HostDB:ENSG00000151422.12; -.
GeneCards; FER; -.
HGNC; HGNC:3655; FER.
HPA; CAB022464; -.
HPA; HPA007641; -.
MIM; 176942; gene.
neXtProt; NX_P16591; -.
OpenTargets; ENSG00000151422; -.
PharmGKB; PA28095; -.
eggNOG; KOG0194; Eukaryota.
eggNOG; ENOG410Y6RP; LUCA.
GeneTree; ENSGT00760000119011; -.
HOGENOM; HOG000059550; -.
HOVERGEN; HBG005655; -.
InParanoid; P16591; -.
KO; K08889; -.
OMA; FMTLRVK; -.
OrthoDB; EOG091G01S4; -.
PhylomeDB; P16591; -.
TreeFam; TF315363; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
SignaLink; P16591; -.
SIGNOR; P16591; -.
ChiTaRS; FER; human.
EvolutionaryTrace; P16591; -.
GeneWiki; FER_(gene); -.
GenomeRNAi; 2241; -.
PRO; PR:P16591; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000151422; -.
CleanEx; HS_FER; -.
ExpressionAtlas; P16591; baseline and differential.
Genevisible; P16591; HS.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0008157; F:protein phosphatase 1 binding; IEA:Ensembl.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IMP:UniProtKB.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISS:UniProtKB.
GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0050904; P:diapedesis; ISS:UniProtKB.
GO; GO:0035426; P:extracellular matrix-cell signaling; ISS:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase; ISS:UniProtKB.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0038109; P:Kit signaling pathway; ISS:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; ISS:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:CACAO.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
GO; GO:0010762; P:regulation of fibroblast migration; IEA:Ensembl.
GO; GO:0010591; P:regulation of lamellipodium assembly; IDA:UniProtKB.
GO; GO:0043304; P:regulation of mast cell degranulation; IBA:GO_Central.
GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0036119; P:response to platelet-derived growth factor; ISS:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IDA:UniProtKB.
CDD; cd10361; SH2_Fps_family; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR027267; AH/BAR-dom.
InterPro; IPR031160; F_BAR.
InterPro; IPR001060; FCH_dom.
InterPro; IPR028539; Fer.
InterPro; IPR035849; Fes/Fps/Fer_SH2.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR016250; Tyr-prot_kinase_Fes/Fps.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
PANTHER; PTHR24418:SF329; PTHR24418:SF329; 1.
Pfam; PF00611; FCH; 1.
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 promoter usage; Alternative splicing;
ATP-binding; Cell junction; Cell membrane; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Kinase;
Lipid-binding; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome; SH2 domain;
Transferase; Tyrosine-protein kinase; Ubl conjugation.
CHAIN 1 822 Tyrosine-protein kinase Fer.
/FTId=PRO_0000088084.
DOMAIN 1 259 F-BAR. {ECO:0000255|PROSITE-
ProRule:PRU01077}.
DOMAIN 460 550 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 563 816 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 569 577 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 300 Important for interaction with membranes
containing phosphoinositides.
COILED 123 185 {ECO:0000255}.
COILED 301 390 {ECO:0000255}.
ACT_SITE 684 684 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 591 591 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 402 402 Phosphotyrosine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 615 615 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P70451}.
MOD_RES 714 714 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P70451}.
VAR_SEQ 1 369 Missing (in isoform 3).
{ECO:0000303|PubMed:22223638}.
/FTId=VSP_043846.
VAR_SEQ 1 175 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041765.
VAR_SEQ 370 412 LRCTEAKFSAQKELLEQKVQENDGKEPPPVVNYEEDARSVT
SM -> MEQKMKCPHCKDQLESGFGSQSCKTCALMFSSEPS
TSEVHRDQ (in isoform 3).
{ECO:0000303|PubMed:22223638}.
/FTId=VSP_043847.
VARIANT 128 128 V -> F (in dbSNP:rs35150210).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041691.
VARIANT 404 404 E -> Q (in an ovarian Endometrioid
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041692.
VARIANT 412 412 M -> V (in dbSNP:rs33940843).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041693.
VARIANT 439 439 L -> V (in dbSNP:rs34499946).
{ECO:0000269|PubMed:1651563,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:2725517}.
/FTId=VAR_006282.
VARIANT 443 443 A -> P (in dbSNP:rs34259824).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041694.
VARIANT 460 460 W -> C (in a lung small cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041695.
VARIANT 507 507 I -> T (in dbSNP:rs34204308).
/FTId=VAR_051695.
VARIANT 813 813 E -> Q (in dbSNP:rs56097357).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041696.
MUTAGEN 483 483 R->Q: Abolishes kinase activity.
Abolishes location at microtubules.
{ECO:0000269|PubMed:12972546}.
MUTAGEN 591 591 K->R: Abolishes kinase activity.
{ECO:0000269|PubMed:9722593}.
CONFLICT 219 219 I -> L (in Ref. 3; BAG61714).
{ECO:0000305}.
CONFLICT 234 234 S -> N (in Ref. 3; BAG61714).
{ECO:0000305}.
CONFLICT 426 426 H -> Q (in Ref. 3; BAG61714).
{ECO:0000305}.
CONFLICT 447 447 M -> L (in Ref. 2; AEY69041).
{ECO:0000305}.
CONFLICT 485 485 S -> G (in Ref. 2; AEY69041).
{ECO:0000305}.
CONFLICT 492 492 Y -> H (in Ref. 2; AEY69041).
{ECO:0000305}.
CONFLICT 505 505 F -> L (in Ref. 3; BAG61714).
{ECO:0000305}.
CONFLICT 558 558 L -> F (in Ref. 2; AEY69041).
{ECO:0000305}.
CONFLICT 730 730 E -> G (in Ref. 3; BAG61714).
{ECO:0000305}.
TURN 455 457 {ECO:0000244|PDB:2KK6}.
STRAND 461 464 {ECO:0000244|PDB:2KK6}.
HELIX 467 472 {ECO:0000244|PDB:2KK6}.
STRAND 480 484 {ECO:0000244|PDB:2KK6}.
STRAND 492 498 {ECO:0000244|PDB:2KK6}.
STRAND 501 510 {ECO:0000244|PDB:2KK6}.
STRAND 513 518 {ECO:0000244|PDB:2KK6}.
STRAND 520 522 {ECO:0000244|PDB:2KK6}.
HELIX 524 533 {ECO:0000244|PDB:2KK6}.
TURN 540 542 {ECO:0000244|PDB:2KK6}.
SEQUENCE 822 AA; 94638 MW; BD42DF6C03419C76 CRC64;
MGFGSDLKNS HEAVLKLQDW ELRLLETVKK FMALRIKSDK EYASTLQNLC NQVDKESTVQ
MNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSYIGVHQQ
IEAEMIKVTK TELEKLKCSY RQLIKEMNSA KEKYKEALAK GKETEKAKER YDKATMKLHM
LHNQYVLALK GAQLHQNQYY DITLPLLLDS LQKMQEEMIK ALKGIFDEYS QITSLVTEEI
VNVHKEIQMS VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL
TAESLQVMLK TLAEELMQTQ QMLLNKEEAV LELEKRIEES SETCEKKSDI VLLLSQKQAL
EELKQSVQQL RCTEAKFSAQ KELLEQKVQE NDGKEPPPVV NYEEDARSVT SMERKERLSK
FESIRHSIAG IIRSPKSALG SSALSDMISI SEKPLAEQDW YHGAIPRIEA QELLKKQGDF
LVRESHGKPG EYVLSVYSDG QRRHFIIQYV DNMYRFEGTG FSNIPQLIDH HYTTKQVITK
KSGVVLLNPI PKDKKWILSH EDVILGELLG KGNFGEVYKG TLKDKTSVAV KTCKEDLPQE
LKIKFLQEAK ILKQYDHPNI VKLIGVCTQR QPVYIIMELV SGGDFLTFLR RKKDELKLKQ
LVKFSLDAAA GMLYLESKNC IHRDLAARNC LVGENNVLKI SDFGMSRQED GGVYSSSGLK
QIPIKWTAPE ALNYGRYSSE SDVWSFGILL WETFSLGVCP YPGMTNQQAR EQVERGYRMS
APQHCPEDIS KIMMKCWDYK PENRPKFSEL QKELTIIKRK LT


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