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P07332

- FES_HUMAN

UniProt

P07332 - FES_HUMAN

Protein

Tyrosine-protein kinase Fes/Fps

Gene

FES

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (03 Oct 2006)
      Previous versions | rss
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    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 TRIM28.11 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.6 PublicationsPROSITE-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.2 Publications

    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

    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 tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell proliferation Source: ProtInc
    3. multicellular organismal development Source: ProtInc
    4. peptidyl-tyrosine phosphorylation Source: UniProtKB
    5. positive regulation of actin cytoskeleton reorganization Source: UniProtKB
    6. positive regulation of microtubule polymerization Source: UniProtKB
    7. positive regulation of myeloid cell differentiation Source: UniProtKB
    8. positive regulation of neuron projection development Source: UniProtKB
    9. protein autophosphorylation Source: UniProtKB
    10. protein phosphorylation Source: ProtInc
    11. regulation of cell adhesion Source: UniProtKB
    12. regulation of cell differentiation Source: UniProtKB
    13. regulation of cell motility Source: UniProtKB
    14. regulation of cell proliferation Source: UniProtKB
    15. regulation of cell shape Source: UniProtKB
    16. regulation of mast cell degranulation Source: UniProtKB
    17. regulation of vesicle-mediated transport Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_19199. CRMPs in Sema3A signaling.
    REACT_19236. Sema3A PAK dependent Axon repulsion.
    REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
    SignaLinkiP07332.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Fes/Fps (EC:2.7.10.2)
    Alternative name(s):
    Feline sarcoma/Fujinami avian sarcoma oncogene homolog
    Proto-oncogene c-Fes
    Proto-oncogene c-Fps
    p93c-fes
    Gene namesi
    Name:FES
    Synonyms:FPS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:3657. FES.

    Subcellular locationi

    Cytoplasmcytosol. Cytoplasmcytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle. Golgi apparatus. Cell junctionfocal adhesion
    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.

    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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Has been shown to act as proto-oncogene in some types of cancer, possibly due to abnormal activation of the kinase. Has been shown to act as tumor suppressor in other types of cancer. Expressed and present as activated kinase in a subset of acute myeloid leukemia patients; promotes survival of leukemia cells (PubMed:20111072). Expression is absent in K562 leukemia cells; ectopic expression of FSP/FES restores myeloid differentiation (PubMed:2656706). May function as tumor suppressor in colorectal cancer; expression is reduced or absent in samples from some colon cancer patients (PubMed:16455651). Ectopic expression of FSP/FES suppresses anchorage-independent growth in colon cancer cell lines (PubMed:16455651). Up-regulated in prostate cancer, and might be a predictor of recurrence after radical surgery (PubMed:21563194). May promote growth of renal carcinoma cells (PubMed:19082481).5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi113 – 1142RK → EE: Reduced binding to membranes containing phosphoinositides. 1 Publication
    Mutagenesisi113 – 1142RK → QQ: Reduced binding to membranes containing phosphoinositides. 1 Publication
    Mutagenesisi145 – 1451L → P: Constitutively activated kinase that can act as oncogene. Promotes myeloid cell survival and proliferation. 3 Publications
    Mutagenesisi334 – 3341L → P: Abolishes autophosphorylation. 2 Publications
    Mutagenesisi463 – 4631G → V: Abolishes kinase activity. 2 Publications
    Mutagenesisi483 – 4831R → M: Abolishes pTyr binding. Abolishes association with microtubules. Abolishes autophosphorylation. Reduced kinase activity. 3 Publications
    Mutagenesisi590 – 5901K → E: Abolishes kinase activity. 2 Publications
    Mutagenesisi704 – 7041M → V: Reduced autophosphorylation and strongly reduced kinase activity. 3 Publications
    Mutagenesisi706 – 7061R → Q: Negligible effect on autophosphorylation and kinase activity. 3 Publications
    Mutagenesisi713 – 7131Y → F: Reduces kinase activity by over 90%. 2 Publications
    Mutagenesisi743 – 7431V → M: Strongly reduced autophosphorylation and kinase activity. 3 Publications
    Mutagenesisi759 – 7591S → F: Reduced autophosphorylation and strongly reduced kinase activity. 3 Publications

    Keywords - Diseasei

    Proto-oncogene, Tumor suppressor

    Organism-specific databases

    PharmGKBiPA28098.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 822822Tyrosine-protein kinase Fes/FpsPRO_0000088088Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei64 – 641Phosphoserine1 Publication
    Modified residuei67 – 671Phosphoserine1 Publication
    Modified residuei261 – 2611Phosphotyrosine1 Publication
    Modified residuei421 – 4211Phosphothreonine1 Publication
    Modified residuei713 – 7131Phosphotyrosine; by autocatalysis6 Publications
    Modified residuei716 – 7161Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylated on Tyr-713. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP07332.
    PaxDbiP07332.
    PRIDEiP07332.

    PTM databases

    PhosphoSiteiP07332.

    Expressioni

    Tissue specificityi

    Widely expressed. Detected in adult colon epithelium.2 Publications

    Gene expression databases

    ArrayExpressiP07332.
    BgeeiP07332.
    CleanExiHS_FES.
    GenevestigatoriP07332.

    Organism-specific databases

    HPAiHPA001376.

    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.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102753EBI-1055635,EBI-608057
    EZRP153118EBI-1055635,EBI-1056902
    GAB1Q134802EBI-1055635,EBI-517684
    KITP107212EBI-1055635,EBI-1379503

    Protein-protein interaction databases

    BioGridi108533. 22 interactions.
    IntActiP07332. 19 interactions.
    MINTiMINT-1497714.
    STRINGi9606.ENSP00000331504.

    Structurei

    Secondary structure

    1
    822
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 64
    Helixi10 – 5142
    Helixi68 – 9629
    Helixi98 – 13134
    Helixi133 – 15422
    Helixi167 – 20236
    Helixi204 – 23431
    Beta strandi236 – 2383
    Helixi239 – 25416
    Helixi257 – 2593
    Helixi262 – 2687
    Turni300 – 3023
    Helixi303 – 34442
    Helixi350 – 3534
    Helixi354 – 38936
    Turni390 – 3934
    Helixi450 – 4523
    Helixi455 – 4573
    Beta strandi461 – 4644
    Helixi467 – 4737
    Beta strandi479 – 4846
    Turni486 – 4894
    Beta strandi491 – 4944
    Beta strandi503 – 5064
    Beta strandi507 – 5093
    Beta strandi512 – 5176
    Beta strandi520 – 5223
    Helixi523 – 53311
    Turni539 – 5413
    Helixi558 – 5603
    Beta strandi561 – 57010
    Beta strandi573 – 5808
    Turni581 – 5833
    Beta strandi586 – 5916
    Helixi598 – 6014
    Helixi602 – 6054
    Helixi606 – 6116
    Beta strandi622 – 6265
    Beta strandi628 – 6314
    Beta strandi633 – 6375
    Helixi644 – 6518
    Helixi652 – 6543
    Helixi657 – 67620
    Helixi686 – 6883
    Beta strandi689 – 6913
    Beta strandi697 – 6993
    Helixi702 – 7043
    Beta strandi711 – 7144
    Beta strandi720 – 7234
    Helixi724 – 7263
    Helixi729 – 7346
    Beta strandi736 – 7383
    Helixi739 – 75416
    Turni755 – 7573
    Helixi766 – 7749
    Helixi787 – 79610
    Helixi801 – 8033
    Helixi807 – 82014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WQUNMR-A450-550[»]
    2DCRNMR-A450-550[»]
    3BKBX-ray1.78A448-822[»]
    3CBLX-ray1.75A448-822[»]
    3CD3X-ray1.98A448-822[»]
    4DYLX-ray2.18A1-405[»]
    4E93X-ray1.84A448-822[»]
    ProteinModelPortaliP07332.
    SMRiP07332. Positions 1-402, 449-821.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07332.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6969FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini460 – 54990SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini561 – 822262Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili125 – 16945Sequence AnalysisAdd
    BLAST
    Coiled coili324 – 36845Sequence AnalysisAdd
    BLAST

    Domaini

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

    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.
    InParanoidiP07332.
    KOiK07527.
    OMAiYQGFLRQ.
    OrthoDBiEOG708VXW.
    PhylomeDBiP07332.
    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]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P07332-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGFSSELCSP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH    50
    MSLQDSGGQS RAISPDSPIS QSWAEITSQT EGLSRLLRQH AEDLNSGPLS 100
    KLSLLIRERQ QLRKTYSEQW QQLQQELTKT HSQDIEKLKS QYRALARDSA 150
    QAKRKYQEAS KDKDRDKAKD KYVRSLWKLF AHHNRYVLGV RAAQLHHQHH 200
    HQLLLPGLLR SLQDLHEEMA CILKEILQEY LEISSLVQDE VVAIHREMAA 250
    AAARIQPEAE YQGFLRQYGS APDVPPCVTF DESLLEEGEP LEPGELQLNE 300
    LTVESVQHTL TSVTDELAVA TEMVFRRQEM VTQLQQELRN EEENTHPRER 350
    VQLLGKRQVL QEALQGLQVA LCSQAKLQAQ QELLQTKLEH LGPGEPPPVL 400
    LLQDDRHSTS SSEQEREGGR TPTLEILKSH ISGIFRPKFS LPPPLQLIPE 450
    VQKPLHEQLW YHGAIPRAEV AELLVHSGDF LVRESQGKQE YVLSVLWDGL 500
    PRHFIIQSLD NLYRLEGEGF PSIPLLIDHL LSTQQPLTKK SGVVLHRAVP 550
    KDKWVLNHED LVLGEQIGRG NFGEVFSGRL RADNTLVAVK SCRETLPPDL 600
    KAKFLQEARI LKQYSHPNIV RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT 650
    EGARLRVKTL LQMVGDAAAG MEYLESKCCI HRDLAARNCL VTEKNVLKIS 700
    DFGMSREEAD GVYAASGGLR QVPVKWTAPE ALNYGRYSSE SDVWSFGILL 750
    WETFSLGASP YPNLSNQQTR EFVEKGGRLP CPELCPDAVF RLMEQCWAYE 800
    PGQRPSFSTI YQELQSIRKR HR 822
    Length:822
    Mass (Da):93,497
    Last modified:October 3, 2006 - v3
    Checksum:i4C2A90555857F045
    GO
    Isoform 2 (identifier: P07332-2) [UniParc]FASTAAdd to Basket

    Also known as: Variant 1

    The sequence of this isoform differs from the canonical sequence as follows:
         72-129: Missing.
         441-510: Missing.

    Show »
    Length:694
    Mass (Da):78,633
    Checksum:i9BFFA652C8C3B8EB
    GO
    Isoform 3 (identifier: P07332-3) [UniParc]FASTAAdd to Basket

    Also known as: Variant 3

    The sequence of this isoform differs from the canonical sequence as follows:
         72-129: Missing.

    Show »
    Length:764
    Mass (Da):86,663
    Checksum:i3F3713631F1D08A2
    GO
    Isoform 4 (identifier: P07332-4) [UniParc]FASTAAdd to Basket

    Also known as: Variant 4

    The sequence of this isoform differs from the canonical sequence as follows:
         441-510: Missing.

    Show »
    Length:752
    Mass (Da):85,466
    Checksum:i0580B667FEF3FDD1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti719 – 7191L → S in CAA36438. (PubMed:2179816)Curated
    Sequence conflicti719 – 7191L → S in AAS82866. 1 PublicationCurated
    Sequence conflicti719 – 7191L → S in AAS82869. 1 PublicationCurated
    Sequence conflicti719 – 7191L → S in AAS82868. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti85 – 851R → C.1 Publication
    Corresponds to variant rs56041861 [ dbSNP | Ensembl ].
    VAR_041697
    Natural varianti246 – 2461R → Q.1 Publication
    Corresponds to variant rs34573430 [ dbSNP | Ensembl ].
    VAR_041698
    Natural varianti323 – 3231M → V.1 Publication
    Corresponds to variant rs56296062 [ dbSNP | Ensembl ].
    VAR_041699

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei72 – 12958Missing in isoform 2 and isoform 3. 2 PublicationsVSP_041748Add
    BLAST
    Alternative sequencei441 – 51070Missing in isoform 2 and isoform 4. 2 PublicationsVSP_041749Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52192 mRNA. Translation: CAA36438.1.
    X06292 Genomic DNA. Translation: CAA29619.1.
    AY513654 mRNA. Translation: AAS82866.1.
    AY513656 mRNA. Translation: AAS82868.1.
    AY513657 mRNA. Translation: AAS82869.1.
    AK300595 mRNA. Translation: BAG62292.1.
    AK312545 mRNA. Translation: BAG35443.1.
    AC124248 Genomic DNA. No translation available.
    CH471101 Genomic DNA. Translation: EAX02114.1.
    BC035357 mRNA. Translation: AAH35357.1.
    CCDSiCCDS10365.1. [P07332-1]
    CCDS45349.1. [P07332-4]
    CCDS45350.1. [P07332-3]
    CCDS45351.1. [P07332-2]
    PIRiA24673. TVHUFF.
    RefSeqiNP_001137255.1. NM_001143783.1. [P07332-3]
    NP_001137256.1. NM_001143784.1. [P07332-4]
    NP_001137257.1. NM_001143785.1. [P07332-2]
    NP_001996.1. NM_002005.3. [P07332-1]
    XP_005254934.1. XM_005254877.1. [P07332-1]
    XP_005254937.1. XM_005254880.1. [P07332-3]
    XP_005254938.1. XM_005254881.1. [P07332-3]
    XP_005254939.1. XM_005254882.1. [P07332-4]
    UniGeneiHs.7636.

    Genome annotation databases

    EnsembliENST00000328850; ENSP00000331504; ENSG00000182511. [P07332-1]
    ENST00000394300; ENSP00000377837; ENSG00000182511. [P07332-3]
    ENST00000414248; ENSP00000414629; ENSG00000182511. [P07332-2]
    ENST00000444422; ENSP00000400868; ENSG00000182511. [P07332-4]
    GeneIDi2242.
    KEGGihsa:2242.
    UCSCiuc002bpv.3. human. [P07332-1]
    uc002bpx.3. human. [P07332-4]
    uc002bpy.3. human. [P07332-3]
    uc010uqj.2. human. [P07332-2]

    Polymorphism databases

    DMDMi115502390.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52192 mRNA. Translation: CAA36438.1 .
    X06292 Genomic DNA. Translation: CAA29619.1 .
    AY513654 mRNA. Translation: AAS82866.1 .
    AY513656 mRNA. Translation: AAS82868.1 .
    AY513657 mRNA. Translation: AAS82869.1 .
    AK300595 mRNA. Translation: BAG62292.1 .
    AK312545 mRNA. Translation: BAG35443.1 .
    AC124248 Genomic DNA. No translation available.
    CH471101 Genomic DNA. Translation: EAX02114.1 .
    BC035357 mRNA. Translation: AAH35357.1 .
    CCDSi CCDS10365.1. [P07332-1 ]
    CCDS45349.1. [P07332-4 ]
    CCDS45350.1. [P07332-3 ]
    CCDS45351.1. [P07332-2 ]
    PIRi A24673. TVHUFF.
    RefSeqi NP_001137255.1. NM_001143783.1. [P07332-3 ]
    NP_001137256.1. NM_001143784.1. [P07332-4 ]
    NP_001137257.1. NM_001143785.1. [P07332-2 ]
    NP_001996.1. NM_002005.3. [P07332-1 ]
    XP_005254934.1. XM_005254877.1. [P07332-1 ]
    XP_005254937.1. XM_005254880.1. [P07332-3 ]
    XP_005254938.1. XM_005254881.1. [P07332-3 ]
    XP_005254939.1. XM_005254882.1. [P07332-4 ]
    UniGenei Hs.7636.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WQU NMR - A 450-550 [» ]
    2DCR NMR - A 450-550 [» ]
    3BKB X-ray 1.78 A 448-822 [» ]
    3CBL X-ray 1.75 A 448-822 [» ]
    3CD3 X-ray 1.98 A 448-822 [» ]
    4DYL X-ray 2.18 A 1-405 [» ]
    4E93 X-ray 1.84 A 448-822 [» ]
    ProteinModelPortali P07332.
    SMRi P07332. Positions 1-402, 449-821.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108533. 22 interactions.
    IntActi P07332. 19 interactions.
    MINTi MINT-1497714.
    STRINGi 9606.ENSP00000331504.

    Chemistry

    BindingDBi P07332.
    ChEMBLi CHEMBL5455.
    GuidetoPHARMACOLOGYi 2023.

    PTM databases

    PhosphoSitei P07332.

    Polymorphism databases

    DMDMi 115502390.

    Proteomic databases

    MaxQBi P07332.
    PaxDbi P07332.
    PRIDEi P07332.

    Protocols and materials databases

    DNASUi 2242.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328850 ; ENSP00000331504 ; ENSG00000182511 . [P07332-1 ]
    ENST00000394300 ; ENSP00000377837 ; ENSG00000182511 . [P07332-3 ]
    ENST00000414248 ; ENSP00000414629 ; ENSG00000182511 . [P07332-2 ]
    ENST00000444422 ; ENSP00000400868 ; ENSG00000182511 . [P07332-4 ]
    GeneIDi 2242.
    KEGGi hsa:2242.
    UCSCi uc002bpv.3. human. [P07332-1 ]
    uc002bpx.3. human. [P07332-4 ]
    uc002bpy.3. human. [P07332-3 ]
    uc010uqj.2. human. [P07332-2 ]

    Organism-specific databases

    CTDi 2242.
    GeneCardsi GC15P091426.
    HGNCi HGNC:3657. FES.
    HPAi HPA001376.
    MIMi 190030. gene.
    neXtProti NX_P07332.
    PharmGKBi PA28098.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG005655.
    InParanoidi P07332.
    KOi K07527.
    OMAi YQGFLRQ.
    OrthoDBi EOG708VXW.
    PhylomeDBi P07332.
    TreeFami TF315363.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_19199. CRMPs in Sema3A signaling.
    REACT_19236. Sema3A PAK dependent Axon repulsion.
    REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
    SignaLinki P07332.

    Miscellaneous databases

    EvolutionaryTracei P07332.
    GeneWikii Feline_sarcoma_oncogene.
    GenomeRNAii 2242.
    NextBioi 9069.
    PROi P07332.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07332.
    Bgeei P07332.
    CleanExi HS_FES.
    Genevestigatori P07332.

    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. "Characterization of human and mouse c-fes cDNA clones and identification of the 5' end of the gene."
      Alcalay M., Antolini F., van de Ven W.J.M., Lanfrancone L., Grignani F., Pelicci P.G.
      Oncogene 5:267-275(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The structure of the human c-fes/fps proto-oncogene."
      Roebroek A.J.M., Schalken J.A., Verbeek J.S., van den Ouweland A.M.W., Onnekink C., Bloemers H.P.J., van de Ven W.J.M.
      EMBO J. 4:2897-2903(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    3. Lefebvre J.-C.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Tongue.
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Brain.
    8. "K562 leukemia cells transfected with the human c-fes gene acquire the ability to undergo myeloid differentiation."
      Yu G., Smithgall T.E., Glazer R.I.
      J. Biol. Chem. 264:10276-10281(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL DIFFERENTIATION AND AS TUMOR SUPPRESSOR, CATALYTIC ACTIVITY.
    9. "Regulation of the human c-fes protein tyrosine kinase (p93c-fes) by its src homology 2 domain and major autophosphorylation site (Tyr-713)."
      Hjermstad S.J., Peters K.L., Briggs S.D., Glazer R.I., Smithgall T.E.
      Oncogene 8:2283-2292(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-713, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-713.
    10. "Co-expression with BCR induces activation of the FES tyrosine kinase and phosphorylation of specific N-terminal BCR tyrosine residues."
      Li J., Smithgall T.E.
      J. Biol. Chem. 271:32930-32936(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BCR, AUTOPHOSPHORYLATION, ENZYME REGULATION.
    11. "Subcellular localization analysis of the closely related Fps/Fes and Fer protein-tyrosine kinases suggests a distinct role for Fps/Fes in vesicular trafficking."
      Zirngibl R., Schulze D., Mirski S.E., Cole S.P., Greer P.A.
      Exp. Cell Res. 266:87-94(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "A point mutation in the N-terminal coiled-coil domain releases c-Fes tyrosine kinase activity and survival signaling in myeloid leukemia cells."
      Cheng H.Y., Schiavone A.P., Smithgall T.E.
      Mol. Cell. Biol. 21:6170-6180(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL PROLIFERATION AND CELL SPREADING, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-145 AND LEU-334.
    13. "Closing in on the biological functions of Fps/Fes and Fer."
      Greer P.
      Nat. Rev. Mol. Cell Biol. 3:278-289(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    14. "The c-Fes tyrosine kinase cooperates with the breakpoint cluster region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-dependent manner."
      Laurent C.E., Smithgall T.E.
      Exp. Cell Res. 299:188-198(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON AND CELL DIFFERENTIATION, INTERACTION WITH BCR.
    15. "The human c-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly."
      Laurent C.E., Delfino F.J., Cheng H.Y., Smithgall T.E.
      Mol. Cell. Biol. 24:9351-9358(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-713, PHOSPHORYLATION BY HCK, MUTAGENESIS OF LEU-145; ARG-483 AND LYS-590.
    16. "An identity crisis for fps/fes: oncogene or tumor suppressor?"
      Sangrar W., Zirgnibl R.A., Gao Y., Muller W.J., Jia Z., Greer P.A.
      Cancer Res. 65:3518-3522(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF MET-704; ARG-706; VAL-743 AND SER-759.
    17. "Expression of c-Fes protein isoforms correlates with differentiation in myeloid leukemias."
      Carlson A., Berkowitz J.M., Browning D., Slamon D.J., Gasson J.C., Yates K.E.
      DNA Cell Biol. 24:311-316(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    18. "The KRAB-associated co-repressor KAP-1 is a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase."
      Delfino F.J., Shaffer J.M., Smithgall T.E.
      Biochem. J. 399:141-150(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM28.
    19. "A growth-suppressive function for the c-fes protein-tyrosine kinase in colorectal cancer."
      Delfino F.J., Stevenson H., Smithgall T.E.
      J. Biol. Chem. 281:8829-8835(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN STAT3 PHOSPHORYLATION, ROLE AS PUTATIVE TUMOR SUPPRESSOR IN COLON CANCER, MUTAGENESIS OF MET-704; ARG-706; VAL-743 AND SER-759, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    20. "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 IN KIT SIGNALING, POSSIBLE ROLE IN CANCER CELL PROLIFERATION.
    21. "Spatial recruitment and activation of the Fes kinase by ezrin promotes HGF-induced cell scattering."
      Naba A., Reverdy C., Louvard D., Arpin M.
      EMBO J. 27:38-50(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CYTOSKELETON REORGANIZATION, INTERACTION WITH EZR, PHOSPHORYLATION AT TYR-713, SUBCELLULAR LOCATION.
    22. "Bimolecular fluorescence complementation demonstrates that the c-Fes protein-tyrosine kinase forms constitutive oligomers in living cells."
      Shaffer J.M., Hellwig S., Smithgall T.E.
      Biochemistry 48:4780-4788(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-713, PHOSPHORYLATION BY HCK, DOMAIN.
    23. "Promoter methylation blocks FES protein-tyrosine kinase gene expression in colorectal cancer."
      Shaffer J.M., Smithgall T.E.
      Genes Chromosomes Cancer 48:272-284(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, ROLE AS PUTATIVE TUMOR SUPPRESSOR IN COLON CANCER.
    24. "Downregulation of the c-Fes protein-tyrosine kinase inhibits the proliferation of human renal carcinoma cells."
      Kanda S., Miyata Y., Kanetake H., Smithgall T.E.
      Int. J. Oncol. 34:89-96(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PUTATIVE ROLE IN RENAL CARCINOMA.
    25. "Contributions of F-BAR and SH2 domains of Fes protein tyrosine kinase for coupling to the FcepsilonRI pathway in mast cells."
      McPherson V.A., Everingham S., Karisch R., Smith J.A., Udell C.M., Zheng J., Jia Z., Craig A.W.
      Mol. Cell. Biol. 29:389-401(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MS4A2/FCER1B AND HCLS1/HS1, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH PHOSPHOINOSITIDE-CONTAINING MEMBRANES, MUTAGENESIS OF 113-ARG-LYS-114.
    26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-67; TYR-261; TYR-713 AND SER-716, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. Cited for: FUNCTION, PHOSPHORYLATION AT THR-421, INTERACTION WITH FLT3.
    28. "Structure and regulation of the c-Fes protein-tyrosine kinase."
      Hellwig S., Smithgall T.E.
      Front. Biosci. 16:3146-3155(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    29. "Pathological significance and predictive value for biochemical recurrence of c-Fes expression in prostate cancer."
      Miyata Y., Watanabe S.I., Matsuo T., Hayashi T., Sakai H., Xuan J.W., Greer P.A., Kanda S.
      Prostate 72:201-208(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE ROLE IN PROSTATE CANCER.
    30. "Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes."
      Scott A., Pantoja-Uceda D., Koshiba S., Inoue M., Kigawa T., Terada T., Shirouzu M., Tanaka A., Sugano S., Yokoyama S., Guentert P.
      J. Biomol. NMR 31:357-361(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 450-550.
    31. "Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation."
      Filippakopoulos P., Kofler M., Hantschel O., Gish G.D., Grebien F., Salah E., Neudecker P., Kay L.E., Turk B.E., Superti-Furga G., Pawson T., Knapp S.
      Cell 134:793-803(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 448-822 OF UNPHOSPHORYLATED APOPROTEIN AND IN COMPLEX WITH STAUROSPORINE AND A SUBSTRATE PEPTIDE, CATALYTIC ACTIVITY, ENZYME REGULATION, PHOSPHORYLATION AT TYR-713, NMR SPECTROSCOPY, MUTAGENESIS OF GLY-463 AND ARG-483.
    32. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-85; GLN-246 AND VAL-323.

    Entry informationi

    Entry nameiFES_HUMAN
    AccessioniPrimary (citable) accession number: P07332
    Secondary accession number(s): B2R6E6
    , B4DUD0, E9PC94, E9PC95, Q2VXS7, Q2VXS8, Q2VXT0, Q6GTU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 167 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Cellular homolog of retroviral oncogenes. In contrast to the viral oncoproteins, the kinase activity of cellular FSP/FES is tightly regulated, and the kinase is inactive in normal cells in the absence of activating stimuli (PubMed:15485904).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3