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P14238

- FES_FELCA

UniProt

P14238 - FES_FELCA

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Protein

Tyrosine-protein kinase Fes/Fps

Gene

FES

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).By similarity

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei588 – 5881ATPPROSITE-ProRule annotation
Active sitei681 – 6811Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi565 – 5739ATPPROSITE-ProRule annotation

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 By similarity; Peripheral membrane protein By similarity; 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).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. Golgi apparatus Source: UniProtKB-KW
  6. 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/FpsPRO_0000088085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651PhosphoserineBy similarity
Modified residuei259 – 2591PhosphotyrosineBy similarity
Modified residuei419 – 4191PhosphothreonineBy similarity
Modified residuei711 – 7111Phosphotyrosine; by autocatalysisBy similarity
Modified residuei714 – 7141PhosphoserineBy 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).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).By similarity

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000005663.

Structurei

3D structure databases

ProteinModelPortaliP14238.
SMRiP14238. Positions 447-819.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9494FCHPROSITE-ProRule annotationAdd
BLAST
Domaini458 – 54790SH2PROSITE-ProRule annotationAdd
BLAST
Domaini559 – 820262Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 298298Important for interaction with membranes containing phosphoinositidesBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili123 – 16341Sequence AnalysisAdd
BLAST
Coiled coili318 – 38972Sequence 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 FCH domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG005655.
InParanoidiP14238.

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGFSSELCSP QGHGAVQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH
60 70 80 90 100
MSLQDGGGRG TGPYSPISQS WAEITSQTEG LSRLLRQHAE DLNSGPLSKL
110 120 130 140 150
GLLIRERQQL RKTYSEQWQQ LQQELTKTHN QDIEKLKSQY RALARDSAQA
160 170 180 190 200
RRKYQEASKD KDRDKAKDKY VRSLWKLFAH HNRYVLGVRA AQLHHHHHHQ
210 220 230 240 250
LMLPGLLQSL QDLHQEMACI LKEILQEYLE ISSLVQDEVV AIHLEMAAAV
260 270 280 290 300
ARIQPEAEYQ GFLRQYGSTP DVPPCVTFDE SLLEEGEPLE PGELQLNELT
310 320 330 340 350
VESVQHTLTS VTDELTVATQ TVLSRQEAVA QLQRELQNEE QNTHPRERVQ
360 370 380 390 400
LLAKKQVLQE ALQALQVALC SQAKLQAQRE LLQAKLEQLG PGEPPPVLLL
410 420 430 440 450
QDDRHSTSSS EQEREGGRTP TLEILKSHIS GIFRPKFSLP PPLQLVPEVQ
460 470 480 490 500
KPLHEQLWYH GALPRAEVAE LLTHSGDFLV RESQGKQEYV LSVLWDGQPR
510 520 530 540 550
HFIIESADNL YRLEGDGFAS IPLLVDHLLR SQQPLTKKSG IVLNRAVPKD
560 570 580 590 600
KWVLNHEDLV LGEQIGRGNF GEVFSGRLRA DNTLVAVKSC RETLPPDIKA
610 620 630 640 650
KFLQEAKILK QYSHPNIVRL IGVCTQKQPI YIVMELVQGG DFLTFLRTEG
660 670 680 690 700
ARLRMKTLLQ MVGDAAAGME YLESKCCIHR DLAARNCLVT EKNVLKISDF
710 720 730 740 750
GMSREEADGI YAASGGLRQV PVKWTAPEAL NYGRYSSESD VWSFGILLWE
760 770 780 790 800
TFSLGASPYP NLSNQQTREF VEKGGRLPCP ELCPDAVFRL MEQCWAYEPG
810 820
QRPSFSAIYQ ELQSIRKRHR
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.
InParanoidi P14238.

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: October 29, 2014
This is version 114 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