Tyrosine-protein kinase Fer - Canis familiaris (Dog)

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Q9TTY2 (FER_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Fer
EC=2.7.10.2

Alternative name(s):
Proto-oncogene c-Fer
p94-Fer

Gene names

Name:

FER

Organism

Canis familiaris (Dog) (Canis lupus familiaris)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	823 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton 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. Cytoplasm › cell cortex By similarity. Note: Associated with the chromatin. Detected on microtubles 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 component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Nucleus
Disease	Proto-oncogene
Domain	Coiled coil SH2 domain
Ligand	ATP-binding Lipid-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cell 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 function	ATP 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: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 823

823

Tyrosine-protein kinase Fer

PRO_0000260824

Regions

Domain

1 – 58

FCH

Domain

460 – 550

SH2

Domain

563 – 816

254

Protein kinase

Nucleotide binding

569 – 577

ATP By similarity

Region

1 – 300

300

Important for interaction with membranes containing phosphoinositides By similarity

Coiled coil

123 – 185

Potential

Coiled coil

301 – 390

Potential

Sites

Active site

684

Proton acceptor By similarity

Binding site

591

ATP By similarity

Amino acid modifications

Modified residue

402

Phosphotyrosine By similarity

Modified residue

410

Phosphothreonine By similarity

Modified residue

411

Phosphoserine By similarity

Modified residue

434

Phosphoserine By similarity

Modified residue

714

Phosphotyrosine; by autocatalysis By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9TTY2 [UniParc].

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

FASTA

823

94,611

        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

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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: 10687853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Prostate.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF187884 mRNA. Translation: AAF00543.1.
RefSeq	NP_001003141.1. NM_001003141.1.
UniGene	Cfa.3618.
3D structure databases
HSSP	HSSP built from PDB template 1WQU based on UniProtKB P07332.
ProteinModelPortal	Q9TTY2.
SMR	Q9TTY2. Positions 449-820.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	403754.
KEGG	cfa:403754.
Organism-specific databases
CTD	2241.
Phylogenomic databases
eggNOG	maNOG10060.
GeneTree	ENSGT00600000084126.
HOVERGEN	HBG005655.
InParanoid	Q9TTY2.
OrthoDB	EOG4JM7P1.
Family and domain databases
InterPro	IPR001060. FCH. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase. IPR000980. SH2. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. IPR016250. Tyr_kinase_non-rcpt_Fes_subgr. [Graphical view]
Gene3D	G3DSA:3.30.505.10. SH2. 1 hit.
KO	K08889.
Pfam	PF00611. FCH. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. [Graphical view]
PIRSF	PIRSF000632. TyrPK_fps. 1 hit.
PRINTS	PR00401. SH2DOMAIN. PR00109. TYRKINASE.
SMART	SM00055. FCH. 1 hit. SM00252. SH2. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	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]
ProtoNet	Search...

Entry information

Entry name

FER_CANFA

Accession

Primary (citable) accession number: Q9TTY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents