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P16879

- FES_MOUSE

UniProt

P16879 - FES_MOUSE

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Protein

Tyrosine-protein kinase Fes/Fps

Gene
Fes, Fps
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei590 – 5901ATP By similarity
Active sitei683 – 6831Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi567 – 5759ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. immunoglobulin receptor binding Source: UniProtKB
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  4. phosphatidylinositol binding Source: UniProtKB
  5. protein binding Source: IntAct
  6. protein kinase activity Source: MGI
  7. protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. peptidyl-tyrosine phosphorylation Source: UniProtKB
  2. positive regulation of actin cytoskeleton reorganization Source: UniProtKB
  3. positive regulation of microtubule polymerization Source: UniProtKB
  4. positive regulation of myeloid cell differentiation Source: UniProtKB
  5. positive regulation of neuron projection development Source: UniProtKB
  6. protein autophosphorylation Source: Ensembl
  7. regulation of cell adhesion Source: UniProtKB
  8. regulation of cell differentiation Source: UniProtKB
  9. regulation of cell motility Source: UniProtKB
  10. regulation of cell proliferation Source: UniProtKB
  11. regulation of cell shape Source: UniProtKB
  12. regulation of mast cell degranulation Source: UniProtKB
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.
ReactomeiREACT_188578. Signaling by SCF-KIT.

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
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:95514. Fes.

Subcellular locationi

Cytoplasmcytosol By similarity. Cytoplasmcytoskeleton By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicle By similarity. Golgi apparatus By similarity. Cell junctionfocal adhesion By similarity
Note: Distributed throughout the cytosol when the kinase is not activated. Association with microtubules requires activation of the kinase activity. Shuttles between focal adhesions and cell-cell contacts in epithelial cells. Recruited to the lateral cell membrane in polarized epithelial cells by interaction with phosphorylated EZR. Detected at tubular membrane structures in the cytoplasm and at the cell periphery By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  5. focal adhesion Source: UniProtKB
  6. Golgi apparatus Source: UniProtKB-SubCell
  7. microtubule cytoskeleton Source: UniProtKB
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 822822Tyrosine-protein kinase Fes/FpsPRO_0000088089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671Phosphoserine By similarity
Modified residuei261 – 2611Phosphotyrosine By similarity
Modified residuei421 – 4211Phosphothreonine By similarity
Modified residuei713 – 7131Phosphotyrosine; by autocatalysis1 Publication
Modified residuei716 – 7161Phosphoserine By similarity

Post-translational modificationi

Autophosphorylated on Tyr-713 in response to FGF2. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK By similarity.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP16879.

PTM databases

PhosphoSiteiP16879.

Expressioni

Gene expression databases

BgeeiP16879.
CleanExiMM_FES.
GenevestigatoriP16879.

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 FCH domain) with soluble tubulin. Interacts (via SH2 domain) with microtubules By similarity.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi199634. 1 interaction.
IntActiP16879. 3 interactions.
MINTiMINT-1520684.

Structurei

3D structure databases

ProteinModelPortaliP16879.
SMRiP16879. Positions 1-402, 449-821.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9696FCHAdd
BLAST
Domaini460 – 54990SH2Add
BLAST
Domaini561 – 818258Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 300300Important for interaction with membranes containing phosphoinositides By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili133 – 16533 Reviewed predictionAdd
BLAST
Coiled coili320 – 36950 Reviewed predictionAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 FCH domain.
Contains 1 SH2 domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117264.
HOGENOMiHOG000059550.
HOVERGENiHBG005655.
InParanoidiP16879.
KOiK07527.
OMAiYQGFLRQ.
OrthoDBiEOG708VXW.
PhylomeDBiP16879.
TreeFamiTF315363.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR001060. 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]
PfamiPF00611. FCH. 1 hit.
PF07714. 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.
PROSITEiPS50133. FCH. 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

MGFSSELCSP QGHGAVQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH    50
MSLQDSGGQS WSSGPDSPVS QSWAEITSQT ENLSRVLRQH AEDLNSGPLS 100
KLSVLIRERQ HLRKTYNEQW QQLQQELTKT HSQDIEKLKT QYRTLVRDST 150
QARRKYQEAS KDKDRDKAKD KYVRSLWKLF AHHNRYVLGV RAAQLHHHHH 200
HRFMLPGLLQ SLQDLHEEMA GILKDILQEY LEISSLVQDD VASIHRELAA 250
AAARIQPEFE YLGFLRQYGS TPDVPPCVTF DESLLEDGEQ LEPGELQLNE 300
LTLESVQHTL TSVTDELAVA TKEVLSRQEM VSQLQRELQS EEQNTHPRER 350
VQLLSKRQML QEAIQGLQIA LCSQDKLQAQ QELLQSKMEQ LGTGEPPAVP 400
LLQDDRHSTS STEQEREGGR TPTLEILKSH FSGIFRPKFS IPPPLQLVPE 450
VQKPLYEQLW YHGAIPRAEV AELLTHSGDF LVRESQGKQE YVLSVMWDGQ 500
PRHFIIQSSD NLYRLEGDGF PSIPLLITHL LSSQQPLTKK SGVVLFRAVP 550
KDKWVLKHED LVLGEQIGRG NFGEVFSGRL RADNTPVAVK SCRETLPPDL 600
KAKFLQEARI LKQYNHPNIV RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT 650
EGARLRVKTL LQMVGDAAAG MEYLESKCCI HRDLAARNCL VTEKNVLKIS 700
DFGMSREEAD GIYAASAGLR QVPVKWTAPE ALNYGRYSSE SDVWSFGILL 750
WETFSLGASP YPNLTNQQTR EFVEKGHRLP CPELCPDAVF RLMEQCWAYE 800
PGQRPSFSII CQELHSIRKR HR 822
Length:822
Mass (Da):93,779
Last modified:January 15, 2008 - v2
Checksum:i939280C56ACF25EE
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1112QH → HS in CAA31138. 1 Publication
Sequence conflicti413 – 4142Missing in CAA31138. 1 Publication
Sequence conflicti413 – 4142Missing in AAN33122. 1 Publication
Sequence conflicti467 – 4671R → W in CAA31138. 1 Publication
Sequence conflicti477 – 4771S → T in CAA31138. 1 Publication
Sequence conflicti477 – 4771S → T in AAN33122. 1 Publication
Sequence conflicti500 – 5001Q → H in CAA31138. 1 Publication
Sequence conflicti500 – 5001Q → H in AAN33122. 1 Publication
Sequence conflicti509 – 5091S → L in CAA31138. 1 Publication
Sequence conflicti509 – 5091S → L in AAN33122. 1 Publication
Sequence conflicti664 – 6641V → M in CAA31138. 1 Publication
Sequence conflicti716 – 7172SA → CS in CAA31138. 1 Publication
Sequence conflicti716 – 7172SA → CS in AAA40012. 1 Publication
Sequence conflicti749 – 7491L → P in AAA40012. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006540604.1.
UniGeneiMm.48757.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS39999.1.
PIRi I48347.
RefSeqi NP_034324.2. NM_010194.2.
XP_006540667.1. XM_006540604.1.
UniGenei Mm.48757.

3D structure databases

ProteinModelPortali P16879.
SMRi P16879. Positions 1-402, 449-821.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199634. 1 interaction.
IntActi P16879. 3 interactions.
MINTi MINT-1520684.

PTM databases

PhosphoSitei P16879.

Proteomic databases

PRIDEi P16879.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000080932 ; ENSMUSP00000079733 ; ENSMUSG00000053158 .
GeneIDi 14159.
KEGGi mmu:14159.
UCSCi uc009ias.1. mouse.

Organism-specific databases

CTDi 2242.
MGIi MGI:95514. Fes.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117264.
HOGENOMi HOG000059550.
HOVERGENi HBG005655.
InParanoidi P16879.
KOi K07527.
OMAi YQGFLRQ.
OrthoDBi EOG708VXW.
PhylomeDBi P16879.
TreeFami TF315363.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_188578. Signaling by SCF-KIT.

Miscellaneous databases

NextBioi 285286.
PROi P16879.
SOURCEi Search...

Gene expression databases

Bgeei P16879.
CleanExi MM_FES.
Genevestigatori P16879.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi 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 ]
Pfami PF00611. FCH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000632. TyrPK_fps. 1 hit.
PRINTSi PR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00055. FCH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50133. FCH. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and structural analysis of murine c-fes cDNA clones."
    Wilks A.F., Kurban R.R.
    Oncogene 3:289-294(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Enhanced endotoxin sensitivity in fps/fes-null mice with minimal defects in hematopoietic homeostasis."
    Zirngibl R.A., Senis Y., Greer P.A.
    Mol. Cell. Biol. 22:2472-2486(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
    Strain: 129/SvJ.
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Spleen.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family."
    Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.
    Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 680-749.
  6. "Fps/Fes and Fer protein-tyrosine kinases play redundant roles in regulating hematopoiesis."
    Senis Y.A., Craig A.W., Greer P.A.
    Exp. Hematol. 31:673-681(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. "Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit mast cell activation."
    Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.
    J. Biol. Chem. 281:20949-20957(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAST CELL ACTIVATION AND PHOSPHORYLATION OF PECAM1, PHOSPHORYLATION, ENZYME REGULATION.
  8. "The tyrosine kinase FES is an essential effector of KITD816V proliferation signal."
    Voisset E., Lopez S., Dubreuil P., De Sepulveda P.
    Blood 110:2593-2599(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KIT, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  10. "Fps/Fes protein-tyrosine kinase regulates mast cell adhesion and migration downstream of Kit and beta1 integrin receptors."
    Smith J.A., Samayawardhena L.A., Craig A.W.
    Cell. Signal. 22:427-436(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

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: September 3, 2014
This is version 134 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

External Data

Dasty 3

Similar proteinsi