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P09760

- FER_RAT

UniProt

P09760 - FER_RAT

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Protein
Tyrosine-protein kinase Fer
Gene
Fer, Fert2, Flk
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. 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. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this clearly depends on cell type and stimulus By similarity. Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei592 – 5921ATP By similarity
Active sitei685 – 6851Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi570 – 5789ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. Rab GTPase binding Source: RGD
  3. actin binding Source: RGD
  4. cadherin binding Source: RGD
  5. cell adhesion molecule binding Source: RGD
  6. cytoskeletal protein binding Source: RGD
  7. epidermal growth factor receptor binding Source: UniProtKB
  8. gamma-catenin binding Source: RGD
  9. lipid binding Source: UniProtKB
  10. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  11. protein kinase binding Source: RGD

GO - Biological processi

  1. Fc-epsilon receptor signaling pathway Source: UniProtKB
  2. Kit signaling pathway Source: UniProtKB
  3. actin cytoskeleton reorganization Source: UniProtKB
  4. cell proliferation Source: Ensembl
  5. cell-cell adhesion mediated by cadherin Source: UniProtKB
  6. cellular response to insulin stimulus Source: UniProtKB
  7. cellular response to macrophage colony-stimulating factor stimulus Source: Ensembl
  8. cellular response to reactive oxygen species Source: UniProtKB
  9. chemotaxis Source: Ensembl
  10. cytokine-mediated signaling pathway Source: UniProtKB
  11. diapedesis Source: UniProtKB
  12. extracellular matrix-cell signaling Source: UniProtKB
  13. insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
  14. interleukin-6-mediated signaling pathway Source: Ensembl
  15. microtubule cytoskeleton organization Source: UniProtKB
  16. mitotic cell cycle Source: Ensembl
  17. negative regulation of mast cell activation involved in immune response Source: UniProtKB
  18. peptidyl-tyrosine phosphorylation Source: UniProtKB
  19. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  20. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  21. positive regulation of actin filament polymerization Source: UniProtKB
  22. positive regulation of cell migration Source: UniProtKB
  23. protein autophosphorylation Source: Ensembl
  24. regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  25. regulation of fibroblast migration Source: Ensembl
  26. regulation of lamellipodium assembly Source: UniProtKB
  27. regulation of protein phosphorylation Source: UniProtKB
  28. response to lipopolysaccharide Source: UniProtKB
  29. response to platelet-derived growth factor Source: UniProtKB
  30. substrate adhesion-dependent cell spreading Source: UniProtKB
  31. tyrosine phosphorylation of Stat3 protein Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_195025. Signaling by SCF-KIT.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Fer (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene c-Fer
Tyrosine-protein kinase FLK
p94-Fer
Gene namesi
Name:Fer
Synonyms:Fert2, Flk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi1306273. Fert2.

Subcellular locationi

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.

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. cell cortex Source: UniProtKB-SubCell
  3. cell junction Source: UniProtKB-SubCell
  4. cytoplasm Source: UniProtKB
  5. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  6. lamellipodium Source: Ensembl
  7. microtubule cytoskeleton Source: Ensembl
  8. nuclear chromatin Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 823823Tyrosine-protein kinase Fer
PRO_0000088093Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei402 – 4021Phosphotyrosine By similarity
Modified residuei434 – 4341Phosphoserine By similarity
Modified residuei616 – 6161Phosphotyrosine; by autocatalysis By similarity
Modified residuei715 – 7151Phosphotyrosine; by autocatalysis By similarity

Post-translational modificationi

Autophosphorylated By similarity.
Polyubiquitinated; this leads to proteasomal degradation By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP09760.
PRIDEiP09760.

PTM databases

PhosphoSiteiP09760.

Expressioni

Gene expression databases

GenevestigatoriP09760.

Interactioni

Subunit structurei

Homotrimer. Interacts with IRS1, JAK1, NRP1, PIK3R1, PLEC and TMF1. Interacts with PPP1CA and regulates its phosphorylation at 'Thr-320'. Interacts with CTNND1, EGFR, FLT3, PECAM1, PDGFR and STAT3. Interacts (via SH2 domain) with CTTN. Interacts with HSP90; this stabilizes phosphorylated FER and protects FER against proteasomal degradation. Component of a complex that contains at least FER, CTTN and PTK2/FAK1 By similarity. Interacts with ARHGDIA.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021758.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5858FCH
Add
BLAST
Domaini461 – 55191SH2
Add
BLAST
Domaini564 – 815252Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 300300Important for interaction with membranes containing phosphoinositides By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili123 – 18563 Reviewed prediction
Add
BLAST
Coiled coili301 – 38282 Reviewed prediction
Add
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 FCH domain.
Contains 1 SH2 domain.

Keywords - Domaini

Coiled coil, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117264.
HOGENOMiHOG000233858.
HOVERGENiHBG001540.
InParanoidiP09760.
KOiK08889.
OMAiFVDNLYR.
OrthoDBiEOG708VXW.
TreeFamiTF315363.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR001060. 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]
PANTHERiPTHR24418:SF227. PTHR24418:SF227. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFiPIRSF000632. TyrPK_fps. 1 hit.
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00055. FCH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50133. FCH. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09760-1 [UniParc]FASTAAdd to Basket

« Hide

MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC    50
NQVDKDSTVQ VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL 100
TMMIKDKQQV KKSYVGIHQQ IEAEMIKVTK TELEKLKSSY RQLIKEMNSA 150
KEKYKEALAK GKETEKAKER CDKATMKLHM LHNQYVLALK GAQLHQSQYY 200
DTTLPLLLDS VQKMQEEMIK ALKGIFDEYS EITSLVTEEI VNVHKEIQMS 250
VDQIDPSTEY NDFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL 300
TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES SETCAKKSDI 350
VLLLGQKQAL EELKQSVQQL RCTEAKCAAQ KELLEQKVQE NDGKEPPPVV 400
NYEEDARSVT SMERKERLSK FESIRHSIAG IIKSPKSVLG SSTQLSDVIS 450
VGEKPLAEHD WYHGAIPRIE AQELLKQQGD FLVRESHGKP GEYVLSVYSD 500
GQRRHFIIQF VDNLYRFEGT GFSNIPQLID HHFNTKQVIT KKSGVVLLNP 550
IPKDKKWVLN HEDVSLGELL GKGNFGEVYK GTLKDKTPVA VKTCKEDLPQ 600
ELKIKFLQEA KILKQYDHPN IVKLIGVCTQ RQPVYIIMEL VPGGDFLSFL 650
RKRKDELKLK QLVRFSLDVA AGMLYLEGKN CIHRDLAARN CLVGENNTLK 700
ISDFGMSRQE DGGVYSSSGL KQIPIKWTAP EALNYGRYSS ESDVWSFGIL 750
LWETFSLGVC PYPGMTNQQA REQVERGYRM SAPQNCPEEI FTIMMKCWDY 800
KPENRPKFSD LHKELTAIKK KIT 823
Length:823
Mass (Da):94,314
Last modified:September 21, 2011 - v2
Checksum:iCA4F31E375F747DA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti501 – 5011G → R in CAA31778. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13412 mRNA. Translation: CAA31778.1.
PIRiS04328.
RefSeqiXP_006245662.1. XM_006245600.1.
UniGeneiRn.102629.

Genome annotation databases

EnsembliENSRNOT00000021758; ENSRNOP00000021758; ENSRNOG00000015898.
GeneIDi301737.
KEGGirno:301737.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13412 mRNA. Translation: CAA31778.1 .
PIRi S04328.
RefSeqi XP_006245662.1. XM_006245600.1.
UniGenei Rn.102629.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000021758.

PTM databases

PhosphoSitei P09760.

Proteomic databases

PaxDbi P09760.
PRIDEi P09760.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021758 ; ENSRNOP00000021758 ; ENSRNOG00000015898 .
GeneIDi 301737.
KEGGi rno:301737.

Organism-specific databases

CTDi 14158.
RGDi 1306273. Fert2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117264.
HOGENOMi HOG000233858.
HOVERGENi HBG001540.
InParanoidi P09760.
KOi K08889.
OMAi FVDNLYR.
OrthoDBi EOG708VXW.
TreeFami TF315363.

Enzyme and pathway databases

Reactomei REACT_195025. Signaling by SCF-KIT.

Miscellaneous databases

PROi P09760.

Gene expression databases

Genevestigatori P09760.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR001060. 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 ]
PANTHERi PTHR24418:SF227. PTHR24418:SF227. 1 hit.
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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned using anti-phosphotyrosine antibody."
    Letwin K., Yee S.P., Pawson T.
    Oncogene 3:621-627(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-823.
    Strain: Wistar.
    Tissue: Brain.
  3. "Synapses are regulated by the cytoplasmic tyrosine kinase Fer in a pathway mediated by p120catenin, Fer, SHP-2, and beta-catenin."
    Lee S.H., Peng I.F., Ng Y.G., Yanagisawa M., Bamji S.X., Elia L.P., Balsamo J., Lilien J., Anastasiadis P.Z., Ullian E.M., Reichardt L.F.
    J. Cell Biol. 183:893-908(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SYNAPSE ORGANIZATION AND SYNAPTIC TRANSMISSION.
  4. "The Fer tyrosine kinase regulates interactions of Rho GDP-Dissociation Inhibitor alpha with the small GTPase Rac."
    Fei F., Kweon S.M., Haataja L., De Sepulveda P., Groffen J., Heisterkamp N.
    BMC Biochem. 11:48-48(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGDIA.

Entry informationi

Entry nameiFER_RAT
AccessioniPrimary (citable) accession number: P09760
Secondary accession number(s): F1MA12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: September 21, 2011
Last modified: September 3, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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