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Tyrosine-protein kinase Fer (EC 2.7.10.2) (Proto-oncogene c-Fer) (p94-Fer)

 FER_MOUSE               Reviewed;         823 AA.
P70451; Q61561; Q6PEE5; Q80UI3; Q8C481; Q9EQ77;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 2.
12-SEP-2018, entry version 154.
RecName: Full=Tyrosine-protein kinase Fer;
EC=2.7.10.2;
AltName: Full=Proto-oncogene c-Fer;
AltName: Full=p94-Fer;
Name=Fer; Synonyms=Fert2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Letwin K., Pawson T.;
"Murine Fer.";
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AUTOPHOSPHORYLATION, AND
TISSUE SPECIFICITY.
PubMed=2294399; DOI=10.1128/MCB.10.1.146;
Fischman K., Edman J.C., Shackleford G.M., Turner J.A., Rutter W.J.,
Nir U.;
"A murine fer testis-specific transcript (ferT) encodes a truncated
Fer protein.";
Mol. Cell. Biol. 10:146-153(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AUTOPHOSPHORYLATION,
INTERACTION WITH IRS1 AND PIK3R1, AND SUBUNIT.
PubMed=11006284; DOI=10.1074/jbc.M006665200;
Iwanishi M., Czech M.P., Cherniack A.D.;
"The protein-tyrosine kinase fer associates with signaling complexes
containing insulin receptor substrate-1 and phosphatidylinositol 3-
kinase.";
J. Biol. Chem. 275:38995-39000(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-823 (ISOFORM 5).
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
FUNCTION IN PHOSPHORYLATION OF CTNND1, AUTOPHOSPHORYLATION, AND
INTERACTION WITH CTNND1 AND PDGFR.
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).
[7]
FUNCTION IN PHOSPHORYLATION OF TMF1, AUTOPHOSPHORYLATION, MUTAGENESIS
OF GLY-571, AND CHARACTERIZATION OF ISOFORM 4.
PubMed=9742951; DOI=10.1016/S0014-5793(98)01003-5;
Schwartz Y., Ben-Dor I., Navon A., Motro B., Nir U.;
"Tyrosine phosphorylation of the TATA element modulatory factor by the
FER nuclear tyrosine kinases.";
FEBS Lett. 434:339-345(1998).
[8]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-715, AND MUTAGENESIS OF
TYR-715.
PubMed=10074905;
Ben-Dor I., Bern O., Tennenbaum T., Nir U.;
"Cell cycle-dependent nuclear accumulation of the p94fer tyrosine
kinase is regulated by its NH2 terminus and is affected by kinase
domain integrity and ATP binding.";
Cell Growth Differ. 10:113-129(1999).
[9]
CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF 135-LYS-LEU-136;
322-MET-LEU-323; LYS-592 AND ASP-743, AUTOPHOSPHORYLATION, AND TISSUE
SPECIFICITY.
PubMed=10391941; DOI=10.1074/jbc.274.28.19934;
Craig A.W., Zirngibl R., Greer P.;
"Disruption of coiled-coil domains in Fer protein-tyrosine kinase
abolishes trimerization but not kinase activation.";
J. Biol. Chem. 274:19934-19942(1999).
[10]
FUNCTION IN PHOSPHORYLATION OF STAT3, INTERACTION WITH STAT3,
AUTOPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=10878010; DOI=10.1074/jbc.M003402200;
Priel-Halachmi S., Ben-Dor I., Shpungin S., Tennenbaum T.,
Molavani H., Bachrach M., Salzberg S., Nir U.;
"FER kinase activation of Stat3 is determined by the N-terminal
sequence.";
J. Biol. Chem. 275:28902-28910(2000).
[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]
DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=11134346; DOI=10.1128/MCB.21.2.603-613.2001;
Craig A.W., Zirngibl R., Williams K., Cole L.A., Greer P.A.;
"Mice devoid of fer protein-tyrosine kinase activity are viable and
fertile but display reduced cortactin phosphorylation.";
Mol. Cell. Biol. 21:603-613(2001).
[13]
INTERACTION WITH PLEC.
PubMed=12200133; DOI=10.1016/S0006-291X(02)02007-7;
Lunter P.C., Wiche G.;
"Direct binding of plectin to Fer kinase and negative regulation of
its catalytic activity.";
Biochem. Biophys. Res. Commun. 296:904-910(2002).
[14]
FUNCTION IN RESPONSE TO LIPOPOLYSACCHARIDE AND LEUKOCYTE DIAPEDESIS.
PubMed=11994443; DOI=10.4049/jimmunol.168.10.4930;
McCafferty D.M., Craig A.W., Senis Y.A., Greer P.A.;
"Absence of Fer protein-tyrosine kinase exacerbates leukocyte
recruitment in response to endotoxin.";
J. Immunol. 168:4930-4935(2002).
[15]
DISRUPTION PHENOTYPE.
PubMed=12901971; DOI=10.1016/S0301-472X(03)00107-3;
Senis Y.A., Craig A.W., Greer P.A.;
"Fps/Fes and Fer protein-tyrosine kinases play redundant roles in
regulating hematopoiesis.";
Exp. Hematol. 31:673-681(2003).
[16]
INDUCTION BY INSULIN, AND INTERACTION WITH STAT3 AND JAK1.
PubMed=12738762; DOI=10.1210/me.2002-0328;
Taler M., Shpungin S., Salem Y., Malovani H., Pasder O., Nir U.;
"Fer is a downstream effector of insulin and mediates the activation
of signal transducer and activator of transcription 3 in myogenic
cells.";
Mol. Endocrinol. 17:1580-1592(2003).
[17]
FUNCTION IN PHOSPHORYLATION OF PTPN1.
PubMed=15226396; DOI=10.1242/jcs.01174;
Xu G., Craig A.W., Greer P., Miller M., Anastasiadis P.Z., Lilien J.,
Balsamo J.;
"Continuous association of cadherin with beta-catenin requires the
non-receptor tyrosine-kinase Fer.";
J. Cell Sci. 117:3207-3219(2004).
[18]
INTERACTION WITH TMF1.
PubMed=15467733; DOI=10.1038/sj.onc.1208149;
Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S.,
Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.;
"TMF/ARA160 is a BC-box-containing protein that mediates the
degradation of Stat3.";
Oncogene 23:8908-8919(2004).
[19]
FUNCTION IN PHOSPHORYLATION OF CTTN, PHOSPHORYLATION, AND SUBCELLULAR
LOCATION.
PubMed=16176974; DOI=10.1091/mbc.E05-05-0410;
El Sayegh T.Y., Arora P.D., Fan L., Laschinger C.A., Greer P.A.,
McCulloch C.A., Kapus A.;
"Phosphorylation of N-cadherin-associated cortactin by Fer kinase
regulates N-cadherin mobility and intercellular adhesion strength.";
Mol. Biol. Cell 16:5514-5527(2005).
[20]
FUNCTION IN MAST CELL ACTIVATION, FUNCTION IN PHOSPHORYLATION OF
PECAM1, PHOSPHORYLATION, AND ACTIVITY REGULATION.
PubMed=16731527; DOI=10.1074/jbc.M604252200;
Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.;
"Fer and Fps/Fes participate in a Lyn-dependent pathway from
FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit
mast cell activation.";
J. Biol. Chem. 281:20949-20957(2006).
[21]
FUNCTION, MUTAGENESIS OF PHE-606, AND INTERACTION WITH PPP1CA.
PubMed=16732323; DOI=10.1038/sj.onc.1209695;
Pasder O., Shpungin S., Salem Y., Makovsky A., Vilchick S.,
Michaeli S., Malovani H., Nir U.;
"Downregulation of Fer induces PP1 activation and cell-cycle arrest in
malignant cells.";
Oncogene 25:4194-4206(2006).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[23]
FUNCTION, AND ACTIVITY REGULATION.
PubMed=17606629; DOI=10.1128/MCB.01744-06;
Sangrar W., Gao Y., Scott M., Truesdell P., Greer P.A.;
"Fer-mediated cortactin phosphorylation is associated with efficient
fibroblast migration and is dependent on reactive oxygen species
generation during integrin-mediated cell adhesion.";
Mol. Cell. Biol. 27:6140-6152(2007).
[24]
FUNCTION IN STAT3 PHOSPHORYLATION, INTERACTION WITH HSP90,
PHOSPHORYLATION AT TYR-616, MUTAGENESIS OF TYR-616, UBIQUITINATION,
AND PROTEASOMAL DEGRADATION.
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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[27]
FUNCTION IN NEURONAL CELL DEATH AFTER BRAIN DAMAGE, AND INTERACTION
WITH NRP1.
PubMed=20133938; DOI=10.1074/jbc.M109.080689;
Jiang S.X., Whitehead S., Aylsworth A., Slinn J., Zurakowski B.,
Chan K., Li J., Hou S.T.;
"Neuropilin 1 directly interacts with Fer kinase to mediate semaphorin
3A-induced death of cortical neurons.";
J. Biol. Chem. 285:9908-9918(2010).
-!- 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).
Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11.
May phosphorylate JUP and PTPN1. Can phosphorylate STAT3 according
to PubMed:10878010 and PubMed:19159681, but clearly plays a
redundant role in STAT3 phosphorylation. According to
PubMed:11134346, cells where wild type FER has been replaced by a
kinase-dead mutant show no reduction in STAT3 phosphorylation.
Phosphorylates TMF1. Isoform 3 lacks kinase activity.
{ECO:0000269|PubMed:10878010, ECO:0000269|PubMed:11006284,
ECO:0000269|PubMed:11994443, ECO:0000269|PubMed:15226396,
ECO:0000269|PubMed:16176974, ECO:0000269|PubMed:16731527,
ECO:0000269|PubMed:16732323, ECO:0000269|PubMed:17606629,
ECO:0000269|PubMed:19159681, ECO:0000269|PubMed:20133938,
ECO:0000269|PubMed:7623846, ECO:0000269|PubMed:9742951}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:10391941}.
-!- ACTIVITY REGULATION: Activated by phosphatidic acid binding (By
similarity). Activated by hydrogen peroxide (in vitro). Activated
by reactive oxygen species (ROS). {ECO:0000250,
ECO:0000269|PubMed:16731527, ECO:0000269|PubMed:17606629}.
-!- SUBUNIT: Homotrimer. Isoform 4 is a monomer, due to the absence of
the N-terminal coiled coil domains. Interacts with CTNND1, EGFR,
FLT3, PECAM1 and PDGFR. Interacts (via SH2 domain) with CTTN.
Component of a complex that contains at least FER, CTTN and
PTK2/FAK1 (By similarity). Interacts with IRS1 and PIK3R1.
Interacts with STAT3. Interacts with PPP1CA and regulates its
phosphorylation at 'Thr-320'. Interacts with JAK1. Interacts with
HSP90; this stabilizes phosphorylated FER and protects FER against
proteasomal degradation. Interacts with ARHGDIA, NRP1, PLEC and
TMF1. {ECO:0000250, ECO:0000269|PubMed:10391941,
ECO:0000269|PubMed:10878010, ECO:0000269|PubMed:11006284,
ECO:0000269|PubMed:12200133, ECO:0000269|PubMed:12738762,
ECO:0000269|PubMed:15467733, ECO:0000269|PubMed:16732323,
ECO:0000269|PubMed:19159681, ECO:0000269|PubMed:20133938,
ECO:0000269|PubMed:7623846}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Cell projection {ECO:0000250}.
Cell junction {ECO:0000250}. Membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Nucleus. Cytoplasm, cell cortex {ECO:0000250}. Note=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 (By similarity).
Not detected in the nucleus, but detected in the nuclear area
surrounding the chromosomes after breakdown of the nuclear
envelope during mitosis (PubMed:11339827). {ECO:0000250,
ECO:0000269|PubMed:11339827}.
-!- SUBCELLULAR LOCATION: Isoform 4: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P70451-1; Sequence=Displayed;
Name=2;
IsoId=P70451-2; Sequence=VSP_021634;
Note=No experimental confirmation available.;
Name=3; Synonyms=iFer;
IsoId=P70451-3; Sequence=VSP_041769, VSP_041770;
Name=4; Synonyms=FerT, p51FerT;
IsoId=P70451-4; Sequence=VSP_041766, VSP_041767, VSP_041768;
Name=5;
IsoId=P70451-5; Sequence=VSP_041768;
-!- TISSUE SPECIFICITY: Detected in liver and testis. Isoform 4 is
detected only in testis (at protein level). Widely expressed.
{ECO:0000269|PubMed:10391941, ECO:0000269|PubMed:11134346,
ECO:0000269|PubMed:2294399}.
-!- INDUCTION: Up-regulated by insulin in myogenic cells (in vitro).
{ECO:0000269|PubMed:12738762}.
-!- DOMAIN: The coiled coil domains mediate homooligomerization and
are required for location at microtubules. {ECO:0000250}.
-!- DOMAIN: The N-terminal region including the first coiled coil
domain mediates interaction with phosphoinositide-containing
membranes. {ECO:0000250}.
-!- PTM: Autophosphorylated. {ECO:0000269|PubMed:10074905,
ECO:0000269|PubMed:16176974, ECO:0000269|PubMed:16731527,
ECO:0000269|PubMed:19159681}.
-!- PTM: Polyubiquitinated; this leads to proteasomal degradation.
{ECO:0000269|PubMed:19159681}.
-!- DISRUPTION PHENOTYPE: No visible phenotype, and the mice are
fertile. Mice have reduced CTTN phosphorylation. Mice lacking both
Fps/Fes and Fer activity are viable and fertile, but produce
slightly fewer pups per litter than normal. They display elevated
levels of circulating neutrophils, erythrocytes and platelets,
while other cell counts are normal. {ECO:0000269|PubMed:11134346,
ECO:0000269|PubMed:12901971}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; U76762; AAB18988.1; -; mRNA.
EMBL; M32054; AAA37617.1; -; mRNA.
EMBL; AF286537; AAG40730.1; -; mRNA.
EMBL; BC051249; AAH51249.1; -; mRNA.
EMBL; BC058100; AAH58100.1; -; mRNA.
EMBL; AK082799; BAC38626.1; -; mRNA.
CCDS; CCDS28936.1; -. [P70451-1]
CCDS; CCDS28937.1; -. [P70451-4]
PIR; I49663; I49663.
RefSeq; NP_001033086.2; NM_001037997.3. [P70451-1]
RefSeq; NP_001273344.1; NM_001286415.1. [P70451-2]
RefSeq; NP_032026.2; NM_008000.2. [P70451-4]
RefSeq; XP_006523703.1; XM_006523640.3. [P70451-1]
RefSeq; XP_006523704.1; XM_006523641.3. [P70451-1]
RefSeq; XP_006523706.1; XM_006523643.3. [P70451-5]
RefSeq; XP_011244595.1; XM_011246293.2. [P70451-5]
UniGene; Mm.151391; -.
UniGene; Mm.23039; -.
ProteinModelPortal; P70451; -.
SMR; P70451; -.
BioGrid; 199633; 3.
STRING; 10090.ENSMUSP00000000129; -.
iPTMnet; P70451; -.
PhosphoSitePlus; P70451; -.
MaxQB; P70451; -.
PaxDb; P70451; -.
PeptideAtlas; P70451; -.
PRIDE; P70451; -.
Ensembl; ENSMUST00000000129; ENSMUSP00000000129; ENSMUSG00000000127. [P70451-1]
Ensembl; ENSMUST00000038080; ENSMUSP00000037418; ENSMUSG00000000127. [P70451-4]
GeneID; 14158; -.
KEGG; mmu:14158; -.
UCSC; uc008dfo.2; mouse. [P70451-2]
UCSC; uc008dfp.1; mouse. [P70451-3]
UCSC; uc008dfq.3; mouse. [P70451-1]
UCSC; uc008dfr.2; mouse. [P70451-5]
UCSC; uc008dfs.2; mouse. [P70451-4]
CTD; 2241; -.
MGI; MGI:105917; Fer.
eggNOG; KOG0194; Eukaryota.
eggNOG; ENOG410Y6RP; LUCA.
GeneTree; ENSGT00760000119011; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG005655; -.
InParanoid; P70451; -.
KO; K08889; -.
OMA; QFADNLY; -.
OrthoDB; EOG091G01S4; -.
PhylomeDB; P70451; -.
TreeFam; TF315363; -.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
ChiTaRS; Fer; mouse.
PRO; PR:P70451; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000000127; Expressed in 263 organ(s), highest expression level in cochlea.
Genevisible; P70451; MM.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
GO; GO:0005154; F:epidermal growth factor receptor binding; ISS:UniProtKB.
GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0008157; F:protein phosphatase 1 binding; IPI:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; ISO:MGI.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0007155; P:cell adhesion; IMP:MGI.
GO; GO:0008283; P:cell proliferation; ISO:MGI.
GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IMP:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; ISO:MGI.
GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
GO; GO:0006935; P:chemotaxis; IMP:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0050904; P:diapedesis; IMP:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0035426; P:extracellular matrix-cell signaling; IMP:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase; IDA:UniProtKB.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISO:MGI.
GO; GO:0038109; P:Kit signaling pathway; IMP:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; IMP:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0010762; P:regulation of fibroblast migration; IMP:UniProtKB.
GO; GO:0010591; P:regulation of lamellipodium assembly; ISS:UniProtKB.
GO; GO:0043304; P:regulation of mast cell degranulation; IBA:GO_Central.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0036119; P:response to platelet-derived growth factor; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; IDA:MGI.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; ISO:MGI.
CDD; cd07686; F-BAR_Fer; 1.
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; IPR028539; Fer.
InterPro; IPR037452; Fer_F-BAR.
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.
PANTHER; PTHR24418:SF227; PTHR24418:SF227; 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;
Alternative splicing; ATP-binding; Cell junction; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Kinase; Lipid-binding; Membrane; Nucleotide-binding;
Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
SH2 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation.
CHAIN 1 823 Tyrosine-protein kinase Fer.
/FTId=PRO_0000260825.
DOMAIN 1 259 F-BAR. {ECO:0000255|PROSITE-
ProRule:PRU01077}.
DOMAIN 461 551 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 564 817 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 570 578 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 300 Important for interaction with membranes
containing phosphoinositides.
{ECO:0000250}.
COILED 123 185 {ECO:0000255}.
COILED 301 381 {ECO:0000255}.
ACT_SITE 685 685 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 592 592 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 402 402 Phosphotyrosine.
{ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:19131326}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:P16591}.
MOD_RES 616 616 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:19159681}.
MOD_RES 715 715 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10074905}.
VAR_SEQ 1 369 Missing (in isoform 4).
{ECO:0000303|PubMed:2294399}.
/FTId=VSP_041766.
VAR_SEQ 70 127 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021634.
VAR_SEQ 370 412 LRCTEAKCAAQKALLEQKVQENDGKEPPPVVNYEEDARSVT
SM -> MDKSMECPHCEGVLEPESDPQFSKKCSIPLSPGPS
SSEILRYK (in isoform 4).
{ECO:0000303|PubMed:2294399}.
/FTId=VSP_041767.
VAR_SEQ 444 444 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:2294399}.
/FTId=VSP_041768.
VAR_SEQ 491 542 GEYVLSVYSDGQRRHFIIQFVDNLYRFEGTGFSNIPQLIDH
HFNTKQVITKK -> ESVSIRGHRVFKHSPAYRSPLQYKAS
HHQEVWGGSAQPHPKG (in isoform 3).
{ECO:0000303|PubMed:11006284}.
/FTId=VSP_041769.
VAR_SEQ 543 823 Missing (in isoform 3).
{ECO:0000303|PubMed:11006284}.
/FTId=VSP_041770.
MUTAGEN 135 136 KL->RP: Abolishes homooligomerization.
{ECO:0000269|PubMed:10391941}.
MUTAGEN 322 323 ML->RP: Abolishes homooligomerization.
{ECO:0000269|PubMed:10391941}.
MUTAGEN 571 571 G->R: Abolishes kinase activity.
{ECO:0000269|PubMed:9742951}.
MUTAGEN 592 592 K->R: Abolishes kinase activity.
{ECO:0000269|PubMed:10391941}.
MUTAGEN 606 606 F->A: Abolishes interaction with PPP1CA.
{ECO:0000269|PubMed:16732323}.
MUTAGEN 616 616 Y->F: Abolishes autophosphorylation.
{ECO:0000269|PubMed:19159681}.
MUTAGEN 715 715 Y->F: Abolishes autophosphorylation.
{ECO:0000269|PubMed:10074905}.
MUTAGEN 743 743 D->R: Abolishes kinase activity.
{ECO:0000269|PubMed:10391941}.
CONFLICT 328 328 A -> G (in Ref. 5; BAC38626).
{ECO:0000305}.
CONFLICT 373 373 T -> S (in Ref. 1; AAB18988 and 3;
AAG40730). {ECO:0000305}.
CONFLICT 730 730 P -> A (in Ref. 2; AAA37617).
{ECO:0000305}.
SEQUENCE 823 AA; 94579 MW; F4C22E1E63721663 CRC64;
MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC NQVDKESTVQ
VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSYVGIHQQ
IEAEMIKVTK TELEKLKSSY RQLIKEMNSA KEKYKEALAK GKETEKAKER YDKATMKLHM
LHNQYVLALK GAQLHQSQYY DTTLPLLLDS VQKMQEEMIK ALKGIFDDYS QITSLVTEEI
VNVHKEIQMS VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL
TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES FETCEKKSDI VLLLGQKQAL
EELKQSVQQL RCTEAKCAAQ KALLEQKVQE NDGKEPPPVV NYEEDARSVT SMERKERLSK
FESIRHSIAG IIKSPKSVLG SSTQVCDVIS VGERPLAEHD WYHGAIPRIE AQELLKQQGD
FLVRESHGKP GEYVLSVYSD GQRRHFIIQF VDNLYRFEGT GFSNIPQLID HHFNTKQVIT
KKSGVVLLNP IPKDKKWVLN HEDVSLGELL GKGNFGEVYK GTLKDKTPVA IKTCKEDLPQ
ELKIKFLQEA KILKQYDHPN IVKLIGVCTQ RQPVYIIMEL VPGGDFLTFL RKRKDELKLK
QLVRFSLDVA AGMLYLESKN CIHRDLAARN CLVGENNTLK ISDFGMSRQE DGGVYSSSGL
KQIPIKWTAP EALNYGRYSS ESDVWSFGIL LWETFSLGVC PYPGMTNQQA REQVERGYRM
SAPQNCPEEV FTIMMKCWDY KPENRPKFND LHKELTVIKK MIT


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