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P07332

- FES_HUMAN

UniProt

P07332 - FES_HUMAN

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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

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 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
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. 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 vesicle Source: UniProtKB-KW
  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-KW
  7. microtubule cytoskeleton Source: UniProtKB
Complete GO annotation...

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. 2 Publications
Mutagenesisi334 – 3341L → P: Abolishes autophosphorylation. 1 Publication
Mutagenesisi463 – 4631G → V: Abolishes kinase activity. 1 Publication
Mutagenesisi483 – 4831R → M: Abolishes pTyr binding. Abolishes association with microtubules. Abolishes autophosphorylation. Reduced kinase activity. 2 Publications
Mutagenesisi590 – 5901K → E: Abolishes kinase activity. 1 Publication
Mutagenesisi704 – 7041M → V: Reduced autophosphorylation and strongly reduced kinase activity. 2 Publications
Mutagenesisi706 – 7061R → Q: Negligible effect on autophosphorylation and kinase activity. 2 Publications
Mutagenesisi713 – 7131Y → F: Reduces kinase activity by over 90%. 1 Publication
Mutagenesisi743 – 7431V → M: Strongly reduced autophosphorylation and kinase activity. 2 Publications
Mutagenesisi759 – 7591S → F: Reduced autophosphorylation and strongly reduced kinase activity. 2 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

BgeeiP07332.
CleanExiHS_FES.
ExpressionAtlasiP07332. baseline and differential.
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.
GeneTreeiENSGT00760000119011.
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

        10         20         30         40         50
MGFSSELCSP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH
60 70 80 90 100
MSLQDSGGQS RAISPDSPIS QSWAEITSQT EGLSRLLRQH AEDLNSGPLS
110 120 130 140 150
KLSLLIRERQ QLRKTYSEQW QQLQQELTKT HSQDIEKLKS QYRALARDSA
160 170 180 190 200
QAKRKYQEAS KDKDRDKAKD KYVRSLWKLF AHHNRYVLGV RAAQLHHQHH
210 220 230 240 250
HQLLLPGLLR SLQDLHEEMA CILKEILQEY LEISSLVQDE VVAIHREMAA
260 270 280 290 300
AAARIQPEAE YQGFLRQYGS APDVPPCVTF DESLLEEGEP LEPGELQLNE
310 320 330 340 350
LTVESVQHTL TSVTDELAVA TEMVFRRQEM VTQLQQELRN EEENTHPRER
360 370 380 390 400
VQLLGKRQVL QEALQGLQVA LCSQAKLQAQ QELLQTKLEH LGPGEPPPVL
410 420 430 440 450
LLQDDRHSTS SSEQEREGGR TPTLEILKSH ISGIFRPKFS LPPPLQLIPE
460 470 480 490 500
VQKPLHEQLW YHGAIPRAEV AELLVHSGDF LVRESQGKQE YVLSVLWDGL
510 520 530 540 550
PRHFIIQSLD NLYRLEGEGF PSIPLLIDHL LSTQQPLTKK SGVVLHRAVP
560 570 580 590 600
KDKWVLNHED LVLGEQIGRG NFGEVFSGRL RADNTLVAVK SCRETLPPDL
610 620 630 640 650
KAKFLQEARI LKQYSHPNIV RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT
660 670 680 690 700
EGARLRVKTL LQMVGDAAAG MEYLESKCCI HRDLAARNCL VTEKNVLKIS
710 720 730 740 750
DFGMSREEAD GVYAASGGLR QVPVKWTAPE ALNYGRYSSE SDVWSFGILL
760 770 780 790 800
WETFSLGASP YPNLSNQQTR EFVEKGGRLP CPELCPDAVF RLMEQCWAYE
810 820
PGQRPSFSTI YQELQSIRKR HR
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.
GeneTreei ENSGT00760000119011.
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

Bgeei P07332.
CleanExi HS_FES.
ExpressionAtlasi P07332. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 168 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