CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002490
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tyrosine-protein kinase Fes/Fps 
Protein Synonyms/Alias
 Feline sarcoma/Fujinami avian sarcoma oncogene homolog; Proto-oncogene c-Fes; Proto-oncogene c-Fps; p93c-fes 
Gene Name
 FES 
Gene Synonyms/Alias
 FPS 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
698VTEKNVLKISDFGMSubiquitination[1]
725GLRQVPVKWTAPEALubiquitination[1, 2, 3]
775QTREFVEKGGRLPCPubiquitination[1, 4]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 1 69 FCH.
 DOMAIN 460 549 SH2.
 DOMAIN 561 822 Protein kinase.
 NP_BIND 567 575 ATP (By similarity).
 REGION 1 300 Important for interaction with membranes
 ACT_SITE 683 683 Proton acceptor (By similarity).
 BINDING 590 590 ATP (By similarity).
 MOD_RES 64 64 Phosphoserine.
 MOD_RES 67 67 Phosphoserine.
 MOD_RES 261 261 Phosphotyrosine.
 MOD_RES 421 421 Phosphothreonine.
 MOD_RES 713 713 Phosphotyrosine; by autocatalysis.
 MOD_RES 716 716 Phosphoserine.  
Keyword
 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. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 822 AA 
Protein Sequence
MGFSSELCSP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH MSLQDSGGQS 60
RAISPDSPIS QSWAEITSQT EGLSRLLRQH AEDLNSGPLS KLSLLIRERQ QLRKTYSEQW 120
QQLQQELTKT HSQDIEKLKS QYRALARDSA QAKRKYQEAS KDKDRDKAKD KYVRSLWKLF 180
AHHNRYVLGV RAAQLHHQHH HQLLLPGLLR SLQDLHEEMA CILKEILQEY LEISSLVQDE 240
VVAIHREMAA AAARIQPEAE YQGFLRQYGS APDVPPCVTF DESLLEEGEP LEPGELQLNE 300
LTVESVQHTL TSVTDELAVA TEMVFRRQEM VTQLQQELRN EEENTHPRER VQLLGKRQVL 360
QEALQGLQVA LCSQAKLQAQ QELLQTKLEH LGPGEPPPVL LLQDDRHSTS SSEQEREGGR 420
TPTLEILKSH ISGIFRPKFS LPPPLQLIPE VQKPLHEQLW YHGAIPRAEV AELLVHSGDF 480
LVRESQGKQE YVLSVLWDGL PRHFIIQSLD NLYRLEGEGF PSIPLLIDHL LSTQQPLTKK 540
SGVVLHRAVP KDKWVLNHED LVLGEQIGRG NFGEVFSGRL RADNTLVAVK SCRETLPPDL 600
KAKFLQEARI LKQYSHPNIV RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT EGARLRVKTL 660
LQMVGDAAAG MEYLESKCCI HRDLAARNCL VTEKNVLKIS DFGMSREEAD GVYAASGGLR 720
QVPVKWTAPE ALNYGRYSSE SDVWSFGILL WETFSLGASP YPNLSNQQTR EFVEKGGRLP 780
CPELCPDAVF RLMEQCWAYE PGQRPSFSTI YQELQSIRKR HR 822 
Gene Ontology
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031234; C:extrinsic to internal side of plasma membrane; IDA:UniProtKB.
 GO:0005925; C:focal adhesion; IDA:UniProtKB.
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0034987; F:immunoglobulin receptor binding; IDA:UniProtKB.
 GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
 GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
 GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
 GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
 GO:0045639; P:positive regulation of myeloid cell differentiation; IMP:UniProtKB.
 GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
 GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
 GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
 GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
 GO:0042127; P:regulation of cell proliferation; IMP:UniProtKB.
 GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
 GO:0043304; P:regulation of mast cell degranulation; IMP:UniProtKB. 
Interpro
 IPR001060; FCH_dom.
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
 IPR000980; SH2.
 IPR008266; Tyr_kinase_AS.
 IPR020635; Tyr_kinase_cat_dom.
 IPR016250; Tyr_kinase_non-rcpt_Fes_subgr. 
Pfam
 PF00611; FCH
 PF07714; Pkinase_Tyr
 PF00017; SH2 
SMART
 SM00055; FCH
 SM00252; SH2
 SM00219; TyrKc 
PROSITE
 PS50133; FCH
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00109; PROTEIN_KINASE_TYR
 PS50001; SH2 
PRINTS
 PR00401; SH2DOMAIN.
 PR00109; TYRKINASE.