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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei590 – 5901ATPPROSITE-ProRule annotation
Active sitei683 – 6831Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi567 – 5759ATPPROSITE-ProRule annotation

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.
ReactomeiREACT_307441. Sema3A PAK dependent Axon repulsion.
REACT_314392. CRMPs in Sema3A signaling.
REACT_327841. Signaling by SCF-KIT.
REACT_340782. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.

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 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 822822Tyrosine-protein kinase Fes/FpsPRO_0000088089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei261 – 2611PhosphotyrosineBy similarity
Modified residuei408 – 4081PhosphoserineBy similarity
Modified residuei411 – 4111PhosphoserineBy similarity
Modified residuei421 – 4211PhosphothreonineBy similarity
Modified residuei713 – 7131Phosphotyrosine; by autocatalysis1 Publication
Modified residuei716 – 7161PhosphoserineBy 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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP16879.
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 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

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 260260F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini460 – 54990SH2PROSITE-ProRule annotationAdd
BLAST
Domaini561 – 818258Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili133 – 16533Sequence AnalysisAdd
BLAST
Coiled coili320 – 36950Sequence AnalysisAdd
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).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

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
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.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1112QH → HS in CAA31138 (PubMed:3060793).Curated
Sequence conflicti413 – 4142Missing in CAA31138 (PubMed:3060793).Curated
Sequence conflicti413 – 4142Missing in AAN33122 (PubMed:11909942).Curated
Sequence conflicti467 – 4671R → W in CAA31138 (PubMed:3060793).Curated
Sequence conflicti477 – 4771S → T in CAA31138 (PubMed:3060793).Curated
Sequence conflicti477 – 4771S → T in AAN33122 (PubMed:11909942).Curated
Sequence conflicti500 – 5001Q → H in CAA31138 (PubMed:3060793).Curated
Sequence conflicti500 – 5001Q → H in AAN33122 (PubMed:11909942).Curated
Sequence conflicti509 – 5091S → L in CAA31138 (PubMed:3060793).Curated
Sequence conflicti509 – 5091S → L in AAN33122 (PubMed:11909942).Curated
Sequence conflicti664 – 6641V → M in CAA31138 (PubMed:3060793).Curated
Sequence conflicti716 – 7172SA → CS in CAA31138 (PubMed:3060793).Curated
Sequence conflicti716 – 7172SA → CS in AAA40012 (PubMed:2482828).Curated
Sequence conflicti749 – 7491L → P in AAA40012 (PubMed:2482828).Curated

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_006540604.2.
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_006540604.2.
UniGeneiMm.48757.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP16879.

Proteomic databases

MaxQBiP16879.
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

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000059550.
HOVERGENiHBG005655.
InParanoidiP16879.
KOiK07527.
OMAiYQGFLRQ.
OrthoDBiEOG708VXW.
PhylomeDBiP16879.
TreeFamiTF315363.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_307441. Sema3A PAK dependent Axon repulsion.
REACT_314392. CRMPs in Sema3A signaling.
REACT_327841. Signaling by SCF-KIT.
REACT_340782. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.

Miscellaneous databases

ChiTaRSiFes. mouse.
NextBioi285286.
PROiP16879.
SOURCEiSearch...

Gene expression databases

BgeeiP16879.
CleanExiMM_FES.
GenevestigatoriP16879.

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.
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...

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: April 1, 2015
This is version 141 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

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 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.