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Protein

Tyrosine-protein kinase Fes/Fps

Gene

Fes

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 TRIM28.3 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Enzyme regulationi

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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei590ATPPROSITE-ProRule annotation1
Active sitei683Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi567 – 575ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiR-MMU-1433557. Signaling by SCF-KIT.
R-MMU-399954. Sema3A PAK dependent Axon repulsion.
R-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-MMU-399956. CRMPs in Sema3A signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Fes/Fps (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene c-Fes
Gene namesi
Name:Fes
Synonyms:Fps
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:95514. Fes.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice are fertile and healthy, display slightly reduced numbers of myeloid cells and are more sensitive to lipopolysaccharide (LPS). Mice lacking both Fps/Fes and Fer activity are viable and fertile, but produce fewer offspring than normal. They display elevated levels of circulating neutrophils, erythrocytes and platelets, while other cell counts are normal.2 Publications

Keywords - Diseasei

Proto-oncogene, Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000880891 – 822Tyrosine-protein kinase Fes/FpsAdd BLAST822

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei67PhosphoserineBy similarity1
Modified residuei261PhosphotyrosineBy similarity1
Modified residuei408PhosphoserineBy similarity1
Modified residuei411PhosphoserineBy similarity1
Modified residuei421PhosphothreonineBy similarity1
Modified residuei713Phosphotyrosine; by autocatalysisCombined sources1
Modified residuei716PhosphoserineBy similarity1

Post-translational modificationi

Autophosphorylated on Tyr-713 in response to FGF2. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP16879.
PaxDbiP16879.
PeptideAtlasiP16879.
PRIDEiP16879.

PTM databases

iPTMnetiP16879.
PhosphoSitePlusiP16879.

Expressioni

Gene expression databases

BgeeiENSMUSG00000053158.
CleanExiMM_FES.
ExpressionAtlasiP16879. baseline and differential.
GenevisibleiP16879. MM.

Interactioni

Subunit structurei

Homooligomer. Interacts with BCR. Interacts (when activated, via coiled coil domain) with TRIM28. Interacts (via SH2 domain) with phosphorylated EZR, MS4A2/FCER1B and HCLS1/HS1. Interacts with phosphorylated KIT. Interacts with FLT3. Interacts (via F-BAR domain) with soluble tubulin. Interacts (via SH2 domain) with microtubules (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
H2-K1P019013EBI-771815,EBI-1265227
Ptpn11P352352EBI-771815,EBI-397236

GO - Molecular functioni

  • immunoglobulin receptor binding Source: UniProtKB
  • microtubule binding Source: MGI
  • receptor binding Source: GO_Central

Protein-protein interaction databases

BioGridi199634. 1 interactor.
IntActiP16879. 3 interactors.
MINTiMINT-1520684.
STRINGi10090.ENSMUSP00000079733.

Structurei

3D structure databases

ProteinModelPortaliP16879.
SMRiP16879.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 260F-BARPROSITE-ProRule annotationAdd BLAST260
Domaini460 – 549SH2PROSITE-ProRule annotationAdd BLAST90
Domaini561 – 818Protein kinasePROSITE-ProRule annotationAdd BLAST258

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 300Important for interaction with membranes containing phosphoinositidesBy similarityAdd BLAST300

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili133 – 165Sequence analysisAdd BLAST33
Coiled coili320 – 369Sequence analysisAdd BLAST50

Domaini

The coiled coil domains are important for regulating the kinase activity. They mediate homooligomerization and probably also interaction with other proteins (By similarity).By similarity
The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.PROSITE-ProRule annotation
Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0194. Eukaryota.
ENOG410Y6RP. LUCA.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000059550.
HOVERGENiHBG005655.
InParanoidiP16879.
KOiK07527.
OMAiEGFPSIP.
OrthoDBiEOG091G01S4.
PhylomeDBiP16879.
TreeFamiTF315363.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR016250. Tyr-prot_kinase_Fes/Fps.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24418:SF197. PTHR24418:SF197. 1 hit.
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFiPIRSF000632. TyrPK_fps. 1 hit.
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00055. FCH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFSSELCSP QGHGAVQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH
60 70 80 90 100
MSLQDSGGQS WSSGPDSPVS QSWAEITSQT ENLSRVLRQH AEDLNSGPLS
110 120 130 140 150
KLSVLIRERQ HLRKTYNEQW QQLQQELTKT HSQDIEKLKT QYRTLVRDST
160 170 180 190 200
QARRKYQEAS KDKDRDKAKD KYVRSLWKLF AHHNRYVLGV RAAQLHHHHH
210 220 230 240 250
HRFMLPGLLQ SLQDLHEEMA GILKDILQEY LEISSLVQDD VASIHRELAA
260 270 280 290 300
AAARIQPEFE YLGFLRQYGS TPDVPPCVTF DESLLEDGEQ LEPGELQLNE
310 320 330 340 350
LTLESVQHTL TSVTDELAVA TKEVLSRQEM VSQLQRELQS EEQNTHPRER
360 370 380 390 400
VQLLSKRQML QEAIQGLQIA LCSQDKLQAQ QELLQSKMEQ LGTGEPPAVP
410 420 430 440 450
LLQDDRHSTS STEQEREGGR TPTLEILKSH FSGIFRPKFS IPPPLQLVPE
460 470 480 490 500
VQKPLYEQLW YHGAIPRAEV AELLTHSGDF LVRESQGKQE YVLSVMWDGQ
510 520 530 540 550
PRHFIIQSSD NLYRLEGDGF PSIPLLITHL LSSQQPLTKK SGVVLFRAVP
560 570 580 590 600
KDKWVLKHED LVLGEQIGRG NFGEVFSGRL RADNTPVAVK SCRETLPPDL
610 620 630 640 650
KAKFLQEARI LKQYNHPNIV RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT
660 670 680 690 700
EGARLRVKTL LQMVGDAAAG MEYLESKCCI HRDLAARNCL VTEKNVLKIS
710 720 730 740 750
DFGMSREEAD GIYAASAGLR QVPVKWTAPE ALNYGRYSSE SDVWSFGILL
760 770 780 790 800
WETFSLGASP YPNLTNQQTR EFVEKGHRLP CPELCPDAVF RLMEQCWAYE
810 820
PGQRPSFSII CQELHSIRKR HR
Length:822
Mass (Da):93,779
Last modified:January 15, 2008 - v2
Checksum:i939280C56ACF25EE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti110 – 111QH → HS in CAA31138 (PubMed:3060793).Curated2
Sequence conflicti413 – 414Missing in CAA31138 (PubMed:3060793).Curated2
Sequence conflicti413 – 414Missing in AAN33122 (PubMed:11909942).Curated2
Sequence conflicti467R → W in CAA31138 (PubMed:3060793).Curated1
Sequence conflicti477S → T in CAA31138 (PubMed:3060793).Curated1
Sequence conflicti477S → T in AAN33122 (PubMed:11909942).Curated1
Sequence conflicti500Q → H in CAA31138 (PubMed:3060793).Curated1
Sequence conflicti500Q → H in AAN33122 (PubMed:11909942).Curated1
Sequence conflicti509S → L in CAA31138 (PubMed:3060793).Curated1
Sequence conflicti509S → L in AAN33122 (PubMed:11909942).Curated1
Sequence conflicti664V → M in CAA31138 (PubMed:3060793).Curated1
Sequence conflicti716 – 717SA → CS in CAA31138 (PubMed:3060793).Curated2
Sequence conflicti716 – 717SA → CS in AAA40012 (PubMed:2482828).Curated2
Sequence conflicti749L → P in AAA40012 (PubMed:2482828).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12616 mRNA. Translation: CAA31138.1.
AF542394 Genomic DNA. Translation: AAN33122.1.
M33421 mRNA. Translation: AAA40012.1.
AK143639 mRNA. Translation: BAE25475.1.
AK170418 mRNA. Translation: BAE41784.1.
BC129919 mRNA. Translation: AAI29920.1.
CCDSiCCDS39999.1.
PIRiI48347.
RefSeqiNP_034324.2. NM_010194.2.
XP_006540667.1. XM_006540604.3.
UniGeneiMm.48757.

Genome annotation databases

EnsembliENSMUST00000080932; ENSMUSP00000079733; ENSMUSG00000053158.
GeneIDi14159.
KEGGimmu:14159.
UCSCiuc009ias.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12616 mRNA. Translation: CAA31138.1.
AF542394 Genomic DNA. Translation: AAN33122.1.
M33421 mRNA. Translation: AAA40012.1.
AK143639 mRNA. Translation: BAE25475.1.
AK170418 mRNA. Translation: BAE41784.1.
BC129919 mRNA. Translation: AAI29920.1.
CCDSiCCDS39999.1.
PIRiI48347.
RefSeqiNP_034324.2. NM_010194.2.
XP_006540667.1. XM_006540604.3.
UniGeneiMm.48757.

3D structure databases

ProteinModelPortaliP16879.
SMRiP16879.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199634. 1 interactor.
IntActiP16879. 3 interactors.
MINTiMINT-1520684.
STRINGi10090.ENSMUSP00000079733.

PTM databases

iPTMnetiP16879.
PhosphoSitePlusiP16879.

Proteomic databases

MaxQBiP16879.
PaxDbiP16879.
PeptideAtlasiP16879.
PRIDEiP16879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000080932; ENSMUSP00000079733; ENSMUSG00000053158.
GeneIDi14159.
KEGGimmu:14159.
UCSCiuc009ias.1. mouse.

Organism-specific databases

CTDi2242.
MGIiMGI:95514. Fes.

Phylogenomic databases

eggNOGiKOG0194. Eukaryota.
ENOG410Y6RP. LUCA.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000059550.
HOVERGENiHBG005655.
InParanoidiP16879.
KOiK07527.
OMAiEGFPSIP.
OrthoDBiEOG091G01S4.
PhylomeDBiP16879.
TreeFamiTF315363.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiR-MMU-1433557. Signaling by SCF-KIT.
R-MMU-399954. Sema3A PAK dependent Axon repulsion.
R-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-MMU-399956. CRMPs in Sema3A signaling.

Miscellaneous databases

ChiTaRSiFes. mouse.
PROiP16879.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000053158.
CleanExiMM_FES.
ExpressionAtlasiP16879. baseline and differential.
GenevisibleiP16879. MM.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR016250. Tyr-prot_kinase_Fes/Fps.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24418:SF197. PTHR24418:SF197. 1 hit.
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFiPIRSF000632. TyrPK_fps. 1 hit.
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00055. FCH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFES_MOUSE
AccessioniPrimary (citable) accession number: P16879
Secondary accession number(s): Q3TD20, Q62122, Q8CG02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 15, 2008
Last modified: November 30, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.