FES_MOUSE
ID FES_MOUSE Reviewed; 822 AA.
AC P16879; Q3TD20; Q62122; Q8CG02;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Tyrosine-protein kinase Fes/Fps;
DE EC=2.7.10.2;
DE AltName: Full=Proto-oncogene c-Fes;
GN Name=Fes; Synonyms=Fps;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3060793;
RA Wilks A.F., Kurban R.R.;
RT "Isolation and structural analysis of murine c-fes cDNA clones.";
RL Oncogene 3:289-294(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=129/SvJ;
RX PubMed=11909942; DOI=10.1128/mcb.22.8.2472-2486.2002;
RA Zirngibl R.A., Senis Y., Greer P.A.;
RT "Enhanced endotoxin sensitivity in fps/fes-null mice with minimal defects
RT in hematopoietic homeostasis.";
RL Mol. Cell. Biol. 22:2472-2486(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 680-749.
RX PubMed=2482828; DOI=10.1016/0378-1119(89)90465-4;
RA Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.;
RT "The application of the polymerase chain reaction to cloning members of the
RT protein tyrosine kinase family.";
RL Gene 85:67-74(1989).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=12901971; DOI=10.1016/s0301-472x(03)00107-3;
RA Senis Y.A., Craig A.W., Greer P.A.;
RT "Fps/Fes and Fer protein-tyrosine kinases play redundant roles in
RT regulating hematopoiesis.";
RL Exp. Hematol. 31:673-681(2003).
RN [7]
RP FUNCTION IN MAST CELL ACTIVATION AND PHOSPHORYLATION OF PECAM1,
RP PHOSPHORYLATION, AND ACTIVITY REGULATION.
RX PubMed=16731527; DOI=10.1074/jbc.m604252200;
RA Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.;
RT "Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to
RT platelet-endothelial cell adhesion molecule 1 to limit mast cell
RT activation.";
RL J. Biol. Chem. 281:20949-20957(2006).
RN [8]
RP FUNCTION, INTERACTION WITH KIT, PHOSPHORYLATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17595334; DOI=10.1182/blood-2007-02-076471;
RA Voisset E., Lopez S., Dubreuil P., De Sepulveda P.;
RT "The tyrosine kinase FES is an essential effector of KITD816V proliferation
RT signal.";
RL Blood 110:2593-2599(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [10]
RP FUNCTION.
RX PubMed=19892014; DOI=10.1016/j.cellsig.2009.10.014;
RA Smith J.A., Samayawardhena L.A., Craig A.W.;
RT "Fps/Fes protein-tyrosine kinase regulates mast cell adhesion and migration
RT downstream of Kit and beta1 integrin receptors.";
RL Cell. Signal. 22:427-436(2010).
RN [11]
RP ROLE AS TUMOR SUPPRESSOR IN A MELANOMA DISEASE MODEL.
RX PubMed=28463229; DOI=10.1172/jci91291;
RA Olvedy M., Tisserand J.C., Luciani F., Boeckx B., Wouters J., Lopez S.,
RA Rambow F., Aibar S., Thienpont B., Barra J., Koehler C., Radaelli E.,
RA Tartare-Deckert S., Aerts S., Dubreuil P., van den Oord J.J.,
RA Lambrechts D., De Sepulveda P., Marine J.C.;
RT "Comparative oncogenomics identifies tyrosine kinase FES as a tumor
RT suppressor in melanoma.";
RL J. Clin. Invest. 127:2310-2325(2017).
CC -!- FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface
CC receptors and plays a role in the regulation of the actin cytoskeleton,
CC microtubule assembly, cell attachment and cell spreading. Plays a role
CC in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated
CC signaling in mast cells. Acts down-stream of the activated FCER1
CC receptor and the mast/stem cell growth factor receptor KIT. Plays a
CC role in the regulation of mast cell degranulation. Plays a role in the
CC regulation of cell differentiation and promotes neurite outgrowth in
CC response to NGF signaling. Plays a role in cell scattering and cell
CC migration in response to HGF-induced activation of EZR. Phosphorylates
CC BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1,
CC PECAM1, STAT3 and TRIM28. {ECO:0000269|PubMed:16731527,
CC ECO:0000269|PubMed:17595334, ECO:0000269|PubMed:19892014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- ACTIVITY REGULATION: Kinase activity is tightly regulated. Activated in
CC response to signaling from a cell surface receptor. Activation probably
CC requires binding of a substrate via the SH2 domain, plus
CC autophosphorylation at Tyr-713. Present in an inactive form in the
CC absence of activating stimuli. {ECO:0000269|PubMed:16731527}.
CC -!- SUBUNIT: Homooligomer. Interacts with BCR. Interacts (when activated,
CC via coiled coil domain) with TRIM28. Interacts (via SH2 domain) with
CC phosphorylated EZR, MS4A2/FCER1B and HCLS1/HS1. Interacts with
CC phosphorylated KIT. Interacts with FLT3. Interacts (via F-BAR domain)
CC with soluble tubulin. Interacts (via SH2 domain) with microtubules (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P16879; P01901: H2-K1; NbExp=3; IntAct=EBI-771815, EBI-1265227;
CC P16879; P35235: Ptpn11; NbExp=2; IntAct=EBI-771815, EBI-397236;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC Cytoplasmic vesicle {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell
CC junction, focal adhesion {ECO:0000250}. Note=Distributed throughout the
CC cytosol when the kinase is not activated. Association with microtubules
CC requires activation of the kinase activity. Shuttles between focal
CC adhesions and cell-cell contacts in epithelial cells. Recruited to the
CC lateral cell membrane in polarized epithelial cells by interaction with
CC phosphorylated EZR. Detected at tubular membrane structures in the
CC cytoplasm and at the cell periphery (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The coiled coil domains are important for regulating the kinase
CC activity. They mediate homooligomerization and probably also
CC interaction with other proteins (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The N-terminal region including the first coiled coil domain
CC mediates interaction with phosphoinositide-containing membranes.
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated on Tyr-713 in response to FGF2. Phosphorylated
CC by LYN in response to FCER1 activation. Phosphorylated by HCK (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are fertile and
CC healthy, display slightly reduced numbers of myeloid cells and are more
CC sensitive to lipopolysaccharide (LPS). Mice lacking both Fps/Fes and
CC Fer activity are viable and fertile, but produce fewer offspring than
CC normal. They display elevated levels of circulating neutrophils,
CC erythrocytes and platelets, while other cell counts are normal.
CC {ECO:0000269|PubMed:11909942, ECO:0000269|PubMed:12901971}.
CC -!- MISCELLANEOUS: In a BRAF V600E-driven, PTEN deficient and FES deficient
CC melanoma model, tumor growth is accelerated due to an increased
CC proliferation of melanoma cells. {ECO:0000269|PubMed:28463229}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X12616; CAA31138.1; -; mRNA.
DR EMBL; AF542394; AAN33122.1; -; Genomic_DNA.
DR EMBL; M33421; AAA40012.1; -; mRNA.
DR EMBL; AK143639; BAE25475.1; -; mRNA.
DR EMBL; AK170418; BAE41784.1; -; mRNA.
DR EMBL; BC129919; AAI29920.1; -; mRNA.
DR CCDS; CCDS39999.1; -.
DR PIR; I48347; I48347.
DR RefSeq; NP_034324.2; NM_010194.2.
DR RefSeq; XP_006540667.1; XM_006540604.3.
DR AlphaFoldDB; P16879; -.
DR SMR; P16879; -.
DR BioGRID; 199634; 13.
DR IntAct; P16879; 2.
DR STRING; 10090.ENSMUSP00000079733; -.
DR iPTMnet; P16879; -.
DR PhosphoSitePlus; P16879; -.
DR jPOST; P16879; -.
DR MaxQB; P16879; -.
DR PaxDb; P16879; -.
DR PeptideAtlas; P16879; -.
DR PRIDE; P16879; -.
DR ProteomicsDB; 270982; -.
DR Antibodypedia; 734; 468 antibodies from 35 providers.
DR DNASU; 14159; -.
DR Ensembl; ENSMUST00000080932; ENSMUSP00000079733; ENSMUSG00000053158.
DR GeneID; 14159; -.
DR KEGG; mmu:14159; -.
DR UCSC; uc009ias.1; mouse.
DR CTD; 2242; -.
DR MGI; MGI:95514; Fes.
DR VEuPathDB; HostDB:ENSMUSG00000053158; -.
DR eggNOG; KOG0194; Eukaryota.
DR GeneTree; ENSGT00940000158881; -.
DR HOGENOM; CLU_005265_0_1_1; -.
DR InParanoid; P16879; -.
DR OMA; RAKDKYV; -.
DR OrthoDB; 556386at2759; -.
DR PhylomeDB; P16879; -.
DR TreeFam; TF315363; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR BioGRID-ORCS; 14159; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Fes; mouse.
DR PRO; PR:P16879; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P16879; protein.
DR Bgee; ENSMUSG00000053158; Expressed in granulocyte and 164 other tissues.
DR ExpressionAtlas; P16879; baseline and differential.
DR Genevisible; P16879; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034987; F:immunoglobulin receptor binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071305; P:cellular response to vitamin D; ISO:MGI.
DR GO; GO:0007098; P:centrosome cycle; IMP:MGI.
DR GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0045657; P:positive regulation of monocyte differentiation; ISO:MGI.
DR GO; GO:0045639; P:positive regulation of myeloid cell differentiation; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; ISS:UniProtKB.
DR GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0043304; P:regulation of mast cell degranulation; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR035849; Fes/Fps/Fer_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016250; Tyr-prot_kinase_Fes/Fps.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PIRSF; PIRSF000632; TyrPK_fps; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell junction; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Golgi apparatus; Kinase; Lipid-binding;
KW Membrane; Nucleotide-binding; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transferase; Tumor suppressor; Tyrosine-protein kinase.
FT CHAIN 1..822
FT /note="Tyrosine-protein kinase Fes/Fps"
FT /id="PRO_0000088089"
FT DOMAIN 1..260
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 460..549
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 561..818
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..300
FT /note="Important for interaction with membranes containing
FT phosphoinositides"
FT /evidence="ECO:0000250"
FT REGION 392..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 133..165
FT /evidence="ECO:0000255"
FT COILED 320..369
FT /evidence="ECO:0000255"
FT ACT_SITE 683
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 567..575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07332"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07332"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07332"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07332"
FT MOD_RES 421
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07332"
FT MOD_RES 713
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07332"
FT CONFLICT 110..111
FT /note="QH -> HS (in Ref. 1; CAA31138)"
FT /evidence="ECO:0000305"
FT CONFLICT 413..414
FT /note="Missing (in Ref. 1; CAA31138 and 2; AAN33122)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="R -> W (in Ref. 1; CAA31138)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="S -> T (in Ref. 1; CAA31138 and 2; AAN33122)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="Q -> H (in Ref. 1; CAA31138 and 2; AAN33122)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="S -> L (in Ref. 1; CAA31138 and 2; AAN33122)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="V -> M (in Ref. 1; CAA31138)"
FT /evidence="ECO:0000305"
FT CONFLICT 716..717
FT /note="SA -> CS (in Ref. 1; CAA31138 and 5; AAA40012)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="L -> P (in Ref. 5; AAA40012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 822 AA; 93779 MW; 939280C56ACF25EE CRC64;
MGFSSELCSP QGHGAVQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH MSLQDSGGQS
WSSGPDSPVS QSWAEITSQT ENLSRVLRQH AEDLNSGPLS KLSVLIRERQ HLRKTYNEQW
QQLQQELTKT HSQDIEKLKT QYRTLVRDST QARRKYQEAS KDKDRDKAKD KYVRSLWKLF
AHHNRYVLGV RAAQLHHHHH HRFMLPGLLQ SLQDLHEEMA GILKDILQEY LEISSLVQDD
VASIHRELAA AAARIQPEFE YLGFLRQYGS TPDVPPCVTF DESLLEDGEQ LEPGELQLNE
LTLESVQHTL TSVTDELAVA TKEVLSRQEM VSQLQRELQS EEQNTHPRER VQLLSKRQML
QEAIQGLQIA LCSQDKLQAQ QELLQSKMEQ LGTGEPPAVP LLQDDRHSTS STEQEREGGR
TPTLEILKSH FSGIFRPKFS IPPPLQLVPE VQKPLYEQLW YHGAIPRAEV AELLTHSGDF
LVRESQGKQE YVLSVMWDGQ PRHFIIQSSD NLYRLEGDGF PSIPLLITHL LSSQQPLTKK
SGVVLFRAVP KDKWVLKHED LVLGEQIGRG NFGEVFSGRL RADNTPVAVK SCRETLPPDL
KAKFLQEARI LKQYNHPNIV RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT EGARLRVKTL
LQMVGDAAAG MEYLESKCCI HRDLAARNCL VTEKNVLKIS DFGMSREEAD GIYAASAGLR
QVPVKWTAPE ALNYGRYSSE SDVWSFGILL WETFSLGASP YPNLTNQQTR EFVEKGHRLP
CPELCPDAVF RLMEQCWAYE PGQRPSFSII CQELHSIRKR HR
