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Q9TTY2 (FER_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Fer

EC=2.7.10.2
Alternative name(s):
Proto-oncogene c-Fer
p94-Fer
Gene names
Name:FER
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length823 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell attachment and cell migration. Acts downstream of EGFR, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11 By similarity.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Homotrimer. Interacts with CTNND1, EGFR, FLT3, IRS1, PECAM1, PIK3R1 and PDGFR. Interacts (via SH2 domain) with CTTN. Component of a complex that contains at least FER, CTTN and PTK2/FAK1 By similarity.

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projection By similarity. Cell junction By similarity. Membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Nucleus By similarity. Cytoplasmcell cortex By similarity. Note: Associated with the chromatin. Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts By similarity.

Domain

The coiled coil domains mediate homooligomerization and are required for location at microtubules By similarity.

The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes By similarity.

Post-translational modification

Autophosphorylated By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.

Contains 1 FCH domain.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   DiseaseProto-oncogene
   DomainCoiled coil
SH2 domain
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from electronic annotation. Source: InterPro

cell proliferation

Inferred from electronic annotation. Source: InterPro

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: InterPro

positive regulation of cell migration

Inferred from electronic annotation. Source: InterPro

regulation of epidermal growth factor receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 823823Tyrosine-protein kinase Fer
PRO_0000260824

Regions

Domain1 – 5858FCH
Domain460 – 55091SH2
Domain563 – 816254Protein kinase
Nucleotide binding569 – 5779ATP By similarity
Region1 – 300300Important for interaction with membranes containing phosphoinositides By similarity
Coiled coil123 – 18563 Potential
Coiled coil301 – 39090 Potential

Sites

Active site6841Proton acceptor By similarity
Binding site5911ATP By similarity

Amino acid modifications

Modified residue4021Phosphotyrosine By similarity
Modified residue4341Phosphoserine By similarity
Modified residue6151Phosphotyrosine By similarity
Modified residue7141Phosphotyrosine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9TTY2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 33E88A6A15B37897

FASTA82394,611
        10         20         30         40         50         60 
MGFGSDLKNS HEAVLKLQDW ELRLLETVKK FMALRIKSDK EYASTLQNLC NQVDKESTVQ 

        70         80         90        100        110        120 
MNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSFIGVHQQ 

       130        140        150        160        170        180 
IEAEMIKVTK TELEKLKSSY RQLIKEMNSA KEKYKEALAK GKETEKAKER YDKATMKLHV 

       190        200        210        220        230        240 
LHNQYVLALK GAQLHQNQYY DTTLPLLLDS LQKMQEEMIK ALKGIFDEYS QITSLVTEEI 

       250        260        270        280        290        300 
VNVHKEIQMS VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL 

       310        320        330        340        350        360 
TAESLQVMLK TLAEELIQTQ QMLVNKEEAV LELEKRIEES SKTCEKKSDI VLLLSQKQTL 

       370        380        390        400        410        420 
EELKQSVQQL RCTEAKFTAQ KELLEQKVQE NEGKEPPPVV NYEEDARSVT SMERKERLSK 

       430        440        450        460        470        480 
FESIRHSIAG IIRSPKSALG SSTFSDTIPI SEKPLAEQDW YHGAIPRIEA QDLLKQQGDF 

       490        500        510        520        530        540 
LVRESHGKPG EYVLSVYSDG QRRHFIIQFV DNLYRFEGTG FSNIPQLIDH HYTTKQVITK 

       550        560        570        580        590        600 
KSGVVLLNPI PKDKKWVLNH EDVTLGELLG KGNFGEVYKG ILKDKTAVAV KTCKEDLPQE 

       610        620        630        640        650        660 
LKIKFLQEAK ILKQYDHPNI VKLIGVCTQR QPIYIIMELV PGGDFLSFLR KKKDEIKLKQ 

       670        680        690        700        710        720 
LVKFSLDAAS GMSYLESKNC IHRDLAARNC LVGENNVLKI SDFGMSRQED GGVYSSSGLK 

       730        740        750        760        770        780 
QIPIKWTAPE ALNYGRYSSE SDVWSFGILL WETFSLGVCP YPGMTNQQAT EQVERGYRIS 

       790        800        810        820 
APQHCPEDIF KIMMKCWDYK PENRPKFSEL QKELTVIKKK VTQ 

« Hide

References

[1]"Links between Fer tyrosine kinase expression levels and prostate cell proliferation."
Allard P., Zoubeidi A., Nguyen L.T., Tessier S., Tanguay S., Chevrette M., Aprikian A., Chevalier S.
Mol. Cell. Endocrinol. 159:63-77(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Prostate.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF187884 mRNA. Translation: AAF00543.1.
RefSeqNP_001003141.1. NM_001003141.1.
UniGeneCfa.3618.

3D structure databases

ProteinModelPortalQ9TTY2.
SMRQ9TTY2. Positions 449-820.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000011047.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403754.
KEGGcfa:403754.

Organism-specific databases

CTD2241.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000059550.
HOVERGENHBG005655.
InParanoidQ9TTY2.
KOK08889.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR001060. FCH_dom.
IPR028539. Fer.
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]
PANTHERPTHR24418:SF86. PTHR24418:SF86. 1 hit.
PfamPF00611. FCH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFPIRSF000632. TyrPK_fps. 1 hit.
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTSM00055. FCH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50133. 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]
ProtoNetSearch...

Other

NextBio20817256.

Entry information

Entry nameFER_CANFA
AccessionPrimary (citable) accession number: Q9TTY2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families