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P14238

- FES_FELCA

UniProt

P14238 - FES_FELCA

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Protein
Tyrosine-protein kinase Fes/Fps
Gene
FES, FPS
Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

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 By similarity.

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-711. Present in an inactive form in the absence of activating stimuli By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei588 – 5881ATP By similarity
Active sitei681 – 6811Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi565 – 5739ATP 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 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. regulation of cell adhesion Source: UniProtKB
  7. regulation of cell differentiation Source: UniProtKB
  8. regulation of cell motility Source: UniProtKB
  9. regulation of cell proliferation Source: UniProtKB
  10. regulation of cell shape Source: UniProtKB
  11. 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

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
OrganismiFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifieri9685 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
ProteomesiUP000011712: Unplaced

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. Golgi apparatus Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  4. cytosol Source: UniProtKB-SubCell
  5. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  6. focal adhesion Source: UniProtKB
  7. microtubule cytoskeleton Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene, Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 820820Tyrosine-protein kinase Fes/Fps
PRO_0000088085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphoserine By similarity
Modified residuei259 – 2591Phosphotyrosine By similarity
Modified residuei419 – 4191Phosphothreonine By similarity
Modified residuei711 – 7111Phosphotyrosine; by autocatalysis By similarity
Modified residuei714 – 7141Phosphoserine By similarity

Post-translational modificationi

Autophosphorylated on Tyr-711 in response to FGF2. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP14238.

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.

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000005663.

Structurei

3D structure databases

ProteinModelPortaliP14238.
SMRiP14238. Positions 447-819.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9494FCH
Add
BLAST
Domaini458 – 54790SH2
Add
BLAST
Domaini559 – 820262Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 298298Important for interaction with membranes containing phosphoinositides By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili123 – 16341 Reviewed prediction
Add
BLAST
Coiled coili318 – 38972 Reviewed prediction
Add
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, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG005655.

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.

P14238-1 [UniParc]FASTAAdd to Basket

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MGFSSELCSP QGHGAVQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH    50
MSLQDGGGRG TGPYSPISQS WAEITSQTEG LSRLLRQHAE DLNSGPLSKL 100
GLLIRERQQL RKTYSEQWQQ LQQELTKTHN QDIEKLKSQY RALARDSAQA 150
RRKYQEASKD KDRDKAKDKY VRSLWKLFAH HNRYVLGVRA AQLHHHHHHQ 200
LMLPGLLQSL QDLHQEMACI LKEILQEYLE ISSLVQDEVV AIHLEMAAAV 250
ARIQPEAEYQ GFLRQYGSTP DVPPCVTFDE SLLEEGEPLE PGELQLNELT 300
VESVQHTLTS VTDELTVATQ TVLSRQEAVA QLQRELQNEE QNTHPRERVQ 350
LLAKKQVLQE ALQALQVALC SQAKLQAQRE LLQAKLEQLG PGEPPPVLLL 400
QDDRHSTSSS EQEREGGRTP TLEILKSHIS GIFRPKFSLP PPLQLVPEVQ 450
KPLHEQLWYH GALPRAEVAE LLTHSGDFLV RESQGKQEYV LSVLWDGQPR 500
HFIIESADNL YRLEGDGFAS IPLLVDHLLR SQQPLTKKSG IVLNRAVPKD 550
KWVLNHEDLV LGEQIGRGNF GEVFSGRLRA DNTLVAVKSC RETLPPDIKA 600
KFLQEAKILK QYSHPNIVRL IGVCTQKQPI YIVMELVQGG DFLTFLRTEG 650
ARLRMKTLLQ MVGDAAAGME YLESKCCIHR DLAARNCLVT EKNVLKISDF 700
GMSREEADGI YAASGGLRQV PVKWTAPEAL NYGRYSSESD VWSFGILLWE 750
TFSLGASPYP NLSNQQTREF VEKGGRLPCP ELCPDAVFRL MEQCWAYEPG 800
QRPSFSAIYQ ELQSIRKRHR 820
Length:820
Mass (Da):92,975
Last modified:February 1, 1996 - v2
Checksum:iF3A52B750236834E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16705
, M16666, M16667, M16668, M16669, M16670, M16671, M16706, M16672, M16673, M16674, M16698, M16700, M16701, M16702, M16704 Genomic DNA. Translation: AAA30808.1.
PIRiA27824. TVCTFF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16705
, M16666 , M16667 , M16668 , M16669 , M16670 , M16671 , M16706 , M16672 , M16673 , M16674 , M16698 , M16700 , M16701 , M16702 , M16704 Genomic DNA. Translation: AAA30808.1 .
PIRi A27824. TVCTFF.

3D structure databases

ProteinModelPortali P14238.
SMRi P14238. Positions 447-819.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9685.ENSFCAP00000005663.

Proteomic databases

PRIDEi P14238.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG005655.

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

  1. "Structure of the feline c-fes/fps proto-oncogene: genesis of a retroviral oncogene."
    Roebroek A.J.M., Schalken J.A., Onnekink C., Bloemers H.P.J., van de Ven W.J.M.
    J. Virol. 61:2009-2016(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiFES_FELCA
AccessioniPrimary (citable) accession number: P14238
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 112 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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