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P70451 (FER_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Synonyms:Fert2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length823 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 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). Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3 according to Ref.10 and Ref.24, but clearly plays a redundant role in STAT3 phosphorylation. According to Ref.12, cells where wild type FER has been replaced by a kinase-dead mutant show no reduction in STAT3 phosphorylation. Phosphorylates TMF1. Isoform 3 lacks kinase activity. Ref.3 Ref.6 Ref.7 Ref.10 Ref.14 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.26

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.9

Enzyme regulation

Activated by phosphatidic acid binding By similarity. Activated by hydrogen peroxide (in vitro). Activated by reactive oxygen species (ROS). Ref.20 Ref.23

Subunit structure

Homotrimer. Isoform 4 is a monomer, due to the absence of the N-terminal coiled coil domains. Interacts with CTNND1, EGFR, FLT3, PECAM1 and PDGFR. Interacts (via SH2 domain) with CTTN. Component of a complex that contains at least FER, CTTN and PTK2/FAK1 By similarity. Interacts with IRS1 and PIK3R1. Interacts with STAT3. Interacts with PPP1CA and regulates its phosphorylation at 'Thr-320'. Interacts with JAK1. Interacts with HSP90; this stabilizes phosphorylated FER and protects FER against proteasomal degradation. Interacts with ARHGDIA, NRP1, PLEC and TMF1. Ref.3 Ref.6 Ref.9 Ref.10 Ref.13 Ref.16 Ref.18 Ref.21 Ref.24 Ref.26

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. 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. Cytoplasmcell cortex By similarity. Note: 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. Not detected in the nucleus, but detected in the nuclear area surrounding the chromosomes after breakdown of the nuclear envelope during mitosis (Ref.11). Ref.8 Ref.10 Ref.11 Ref.19

Isoform 4: Nucleus Ref.8 Ref.10 Ref.11 Ref.19.

Tissue specificity

Detected in liver and testis. Isoform 4 is detected only in testis (at protein level). Widely expressed. Ref.2 Ref.9 Ref.12

Induction

Up-regulated by insulin in myogenic cells (in vitro). Ref.16 Ref.20 Ref.23

Domain

The coiled coil domains mediate homooligomerization and are required for location at microtubules By similarity. Ref.9

The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes By similarity. Ref.9

Post-translational modification

Autophosphorylated. Ref.2 Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.19 Ref.20 Ref.24

Polyubiquitinated; this leads to proteasomal degradation.

Disruption phenotype

No visible phenotype, and the mice are fertile. Mice have reduced CTTN phosphorylation. Mice lacking both Fps/Fes and Fer activity are viable and fertile, but produce slightly fewer pups per litter than normal. They display elevated levels of circulating neutrophils, erythrocytes and platelets, while other cell counts are normal. Ref.12 Ref.15

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
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   DomainCoiled coil
SH2 domain
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Inferred from mutant phenotype PubMed 12192036. Source: UniProtKB

Kit signaling pathway

Inferred from mutant phenotype PubMed 12192036. Source: UniProtKB

actin cytoskeleton reorganization

Inferred from mutant phenotype Ref.19. Source: UniProtKB

cell adhesion

Inferred from mutant phenotype PubMed 12192036. Source: MGI

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cell-cell adhesion mediated by cadherin

Inferred from mutant phenotype Ref.19. Source: UniProtKB

cellular response to insulin stimulus

Inferred from direct assay Ref.3. Source: UniProtKB

cellular response to macrophage colony-stimulating factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to reactive oxygen species

Inferred from mutant phenotype Ref.23. Source: UniProtKB

chemotaxis

Inferred from mutant phenotype PubMed 12192036. Source: MGI

cytokine-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

diapedesis

Inferred from mutant phenotype PubMed 16009680. Source: UniProtKB

extracellular matrix-cell signaling

Inferred from mutant phenotype Ref.23. Source: UniProtKB

insulin receptor signaling pathway via phosphatidylinositol 3-kinase

Inferred from direct assay Ref.3. Source: UniProtKB

interleukin-6-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

microtubule cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

negative regulation of mast cell activation involved in immune response

Inferred from mutant phenotype Ref.20. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

platelet-derived growth factor receptor signaling pathway

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of actin filament polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay PubMed 12192036. Source: MGI

protein phosphorylation

Inferred from direct assay PubMed 12192036. Source: MGI

regulation of epidermal growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of fibroblast migration

Inferred from mutant phenotype Ref.23. Source: UniProtKB

regulation of lamellipodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein phosphorylation

Inferred from mutant phenotype Ref.21. Source: UniProtKB

response to lipopolysaccharide

Inferred from mutant phenotype PubMed 16009680. Source: UniProtKB

response to platelet-derived growth factor

Inferred from direct assay Ref.6. Source: UniProtKB

signal transduction

Inferred from direct assay PubMed 12192036. Source: MGI

substrate adhesion-dependent cell spreading

Inferred from mutant phenotype Ref.19. Source: UniProtKB

tyrosine phosphorylation of Stat3 protein

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extrinsic component of cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from electronic annotation. Source: Ensembl

microtubule cytoskeleton

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

epidermal growth factor receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

lipid binding

Inferred from sequence or structural similarity. Source: UniProtKB

non-membrane spanning protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16. Source: MGI

protein kinase activity

Inferred from direct assay PubMed 12192036. Source: MGI

protein phosphatase 1 binding

Inferred from physical interaction Ref.21. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P70451-1)

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.
Isoform 2 (identifier: P70451-2)

The sequence of this isoform differs from the canonical sequence as follows:
     70-127: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P70451-3)

Also known as: iFer;

The sequence of this isoform differs from the canonical sequence as follows:
     491-542: GEYVLSVYSD...FNTKQVITKK → ESVSIRGHRV...GGSAQPHPKG
     543-823: Missing.
Isoform 4 (identifier: P70451-4)

Also known as: FerT; p51FerT;

The sequence of this isoform differs from the canonical sequence as follows:
     1-369: Missing.
     370-412: LRCTEAKCAA...EEDARSVTSM → MDKSMECPHC...PSSSEILRYK
     444-444: Missing.
Isoform 5 (identifier: P70451-5)

The sequence of this isoform differs from the canonical sequence as follows:
     444-444: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 823823Tyrosine-protein kinase Fer
PRO_0000260825

Regions

Domain1 – 5858FCH
Domain461 – 55191SH2
Domain564 – 817254Protein kinase
Nucleotide binding570 – 5789ATP By similarity
Region1 – 300300Important for interaction with membranes containing phosphoinositides By similarity
Coiled coil123 – 18563 Potential
Coiled coil301 – 38181 Potential

Sites

Active site6851Proton acceptor By similarity
Binding site5921ATP By similarity

Amino acid modifications

Modified residue4021Phosphotyrosine Ref.22 Ref.25
Modified residue4341Phosphoserine By similarity
Modified residue6161Phosphotyrosine; by autocatalysis Ref.24
Modified residue7151Phosphotyrosine; by autocatalysis By similarity

Natural variations

Alternative sequence1 – 369369Missing in isoform 4.
VSP_041766
Alternative sequence70 – 12758Missing in isoform 2.
VSP_021634
Alternative sequence370 – 41243LRCTE…SVTSM → MDKSMECPHCEGVLEPESDP QFSKKCSIPLSPGPSSSEIL RYK in isoform 4.
VSP_041767
Alternative sequence4441Missing in isoform 4 and isoform 5.
VSP_041768
Alternative sequence491 – 54252GEYVL…VITKK → ESVSIRGHRVFKHSPAYRSP LQYKASHHQEVWGGSAQPHP KG in isoform 3.
VSP_041769
Alternative sequence543 – 823281Missing in isoform 3.
VSP_041770

Experimental info

Mutagenesis135 – 1362KL → RP: Abolishes homooligomerization.
Mutagenesis322 – 3232ML → RP: Abolishes homooligomerization.
Mutagenesis5711G → R: Abolishes kinase activity. Ref.7
Mutagenesis5921K → R: Abolishes kinase activity. Ref.9
Mutagenesis6061F → A: Abolishes interaction with PPP1CA. Ref.21
Mutagenesis6161Y → F: Abolishes autophosphorylation. Ref.24
Mutagenesis7151Y → F: Abolishes autophosphorylation. Ref.8
Mutagenesis7431D → R: Abolishes kinase activity. Ref.9
Sequence conflict3281A → G in BAC38626. Ref.5
Sequence conflict3731T → S in AAB18988. Ref.1
Sequence conflict3731T → S in AAG40730. Ref.3
Sequence conflict7301P → A in AAA37617. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: F4C22E1E63721663

FASTA82394,579
        10         20         30         40         50         60 
MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC NQVDKESTVQ 

        70         80         90        100        110        120 
VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSYVGIHQQ 

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

       190        200        210        220        230        240 
LHNQYVLALK GAQLHQSQYY DTTLPLLLDS VQKMQEEMIK ALKGIFDDYS QITSLVTEEI 

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

       310        320        330        340        350        360 
TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES FETCEKKSDI VLLLGQKQAL 

       370        380        390        400        410        420 
EELKQSVQQL RCTEAKCAAQ KALLEQKVQE NDGKEPPPVV NYEEDARSVT SMERKERLSK 

       430        440        450        460        470        480 
FESIRHSIAG IIKSPKSVLG SSTQVCDVIS VGERPLAEHD WYHGAIPRIE AQELLKQQGD 

       490        500        510        520        530        540 
FLVRESHGKP GEYVLSVYSD GQRRHFIIQF VDNLYRFEGT GFSNIPQLID HHFNTKQVIT 

       550        560        570        580        590        600 
KKSGVVLLNP IPKDKKWVLN HEDVSLGELL GKGNFGEVYK GTLKDKTPVA IKTCKEDLPQ 

       610        620        630        640        650        660 
ELKIKFLQEA KILKQYDHPN IVKLIGVCTQ RQPVYIIMEL VPGGDFLTFL RKRKDELKLK 

       670        680        690        700        710        720 
QLVRFSLDVA AGMLYLESKN CIHRDLAARN CLVGENNTLK ISDFGMSRQE DGGVYSSSGL 

       730        740        750        760        770        780 
KQIPIKWTAP EALNYGRYSS ESDVWSFGIL LWETFSLGVC PYPGMTNQQA REQVERGYRM 

       790        800        810        820 
SAPQNCPEEV FTIMMKCWDY KPENRPKFND LHKELTVIKK MIT 

« Hide

Isoform 2 [UniParc].

Checksum: 91FCCCAAFEF1C283
Show »

FASTA76587,762
Isoform 3 (iFer) [UniParc].

Checksum: 7468E01E9EB6F6E2
Show »

FASTA53261,094
Isoform 4 (FerT) (p51FerT) [UniParc].

Checksum: 1CDAA93ED40B6A1D
Show »

FASTA45351,601
Isoform 5 [UniParc].

Checksum: F08F6BB10161D738
Show »

FASTA82294,451

References

« Hide 'large scale' references
[1]"Murine Fer."
Letwin K., Pawson T.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"A murine fer testis-specific transcript (ferT) encodes a truncated Fer protein."
Fischman K., Edman J.C., Shackleford G.M., Turner J.A., Rutter W.J., Nir U.
Mol. Cell. Biol. 10:146-153(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
[3]"The protein-tyrosine kinase fer associates with signaling complexes containing insulin receptor substrate-1 and phosphatidylinositol 3-kinase."
Iwanishi M., Czech M.P., Cherniack A.D.
J. Biol. Chem. 275:38995-39000(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH IRS1 AND PIK3R1, SUBUNIT.
[4]"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 2).
Strain: C57BL/6 and FVB/N-3.
Tissue: Brain and Mammary tumor.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-823 (ISOFORM 5).
Strain: C57BL/6J.
[6]"The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors."
Kim L., Wong T.W.
Mol. Cell. Biol. 15:4553-4561(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CTNND1, AUTOPHOSPHORYLATION, INTERACTION WITH CTNND1 AND PDGFR.
[7]"Tyrosine phosphorylation of the TATA element modulatory factor by the FER nuclear tyrosine kinases."
Schwartz Y., Ben-Dor I., Navon A., Motro B., Nir U.
FEBS Lett. 434:339-345(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TMF1, AUTOPHOSPHORYLATION, MUTAGENESIS OF GLY-571, CHARACTERIZATION OF ISOFORM 4.
[8]"Cell cycle-dependent nuclear accumulation of the p94fer tyrosine kinase is regulated by its NH2 terminus and is affected by kinase domain integrity and ATP binding."
Ben-Dor I., Bern O., Tennenbaum T., Nir U.
Cell Growth Differ. 10:113-129(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-715, MUTAGENESIS OF TYR-715.
[9]"Disruption of coiled-coil domains in Fer protein-tyrosine kinase abolishes trimerization but not kinase activation."
Craig A.W., Zirngibl R., Greer P.
J. Biol. Chem. 274:19934-19942(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF 135-LYS-LEU-136; 322-MET-LEU-323; LYS-592 AND ASP-743, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
[10]"FER kinase activation of Stat3 is determined by the N-terminal sequence."
Priel-Halachmi S., Ben-Dor I., Shpungin S., Tennenbaum T., Molavani H., Bachrach M., Salzberg S., Nir U.
J. Biol. Chem. 275:28902-28910(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF STAT3, INTERACTION WITH STAT3, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION.
[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]"Mice devoid of fer protein-tyrosine kinase activity are viable and fertile but display reduced cortactin phosphorylation."
Craig A.W., Zirngibl R., Williams K., Cole L.A., Greer P.A.
Mol. Cell. Biol. 21:603-613(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[13]"Direct binding of plectin to Fer kinase and negative regulation of its catalytic activity."
Lunter P.C., Wiche G.
Biochem. Biophys. Res. Commun. 296:904-910(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLEC.
[14]"Absence of Fer protein-tyrosine kinase exacerbates leukocyte recruitment in response to endotoxin."
McCafferty D.M., Craig A.W., Senis Y.A., Greer P.A.
J. Immunol. 168:4930-4935(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RESPONSE TO LIPOPOLYSACCHARIDE AND LEUKOCYTE DIAPEDESIS.
[15]"Fps/Fes and Fer protein-tyrosine kinases play redundant roles in regulating hematopoiesis."
Senis Y.A., Craig A.W., Greer P.A.
Exp. Hematol. 31:673-681(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[16]"Fer is a downstream effector of insulin and mediates the activation of signal transducer and activator of transcription 3 in myogenic cells."
Taler M., Shpungin S., Salem Y., Malovani H., Pasder O., Nir U.
Mol. Endocrinol. 17:1580-1592(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY INSULIN, INTERACTION WITH STAT3 AND JAK1.
[17]"Continuous association of cadherin with beta-catenin requires the non-receptor tyrosine-kinase Fer."
Xu G., Craig A.W., Greer P., Miller M., Anastasiadis P.Z., Lilien J., Balsamo J.
J. Cell Sci. 117:3207-3219(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PTPN1.
[18]"TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3."
Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S., Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.
Oncogene 23:8908-8919(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMF1.
[19]"Phosphorylation of N-cadherin-associated cortactin by Fer kinase regulates N-cadherin mobility and intercellular adhesion strength."
El Sayegh T.Y., Arora P.D., Fan L., Laschinger C.A., Greer P.A., McCulloch C.A., Kapus A.
Mol. Biol. Cell 16:5514-5527(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CTTN, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[20]"Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit mast cell activation."
Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.
J. Biol. Chem. 281:20949-20957(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MAST CELL ACTIVATION, FUNCTION IN PHOSPHORYLATION OF PECAM1, PHOSPHORYLATION, ENZYME REGULATION.
[21]"Downregulation of Fer induces PP1 activation and cell-cycle arrest in malignant cells."
Pasder O., Shpungin S., Salem Y., Makovsky A., Vilchick S., Michaeli S., Malovani H., Nir U.
Oncogene 25:4194-4206(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF PHE-606, INTERACTION WITH PPP1CA.
[22]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[23]"Fer-mediated cortactin phosphorylation is associated with efficient fibroblast migration and is dependent on reactive oxygen species generation during integrin-mediated cell adhesion."
Sangrar W., Gao Y., Scott M., Truesdell P., Greer P.A.
Mol. Cell. Biol. 27:6140-6152(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[24]"Hsp90 and a tyrosine embedded in the Hsp90 recognition loop are required for the Fer tyrosine kinase activity."
Hikri E., Shpungin S., Nir U.
Cell. Signal. 21:588-596(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN STAT3 PHOSPHORYLATION, INTERACTION WITH HSP90, PHOSPHORYLATION AT TYR-616, MUTAGENESIS OF TYR-616, UBIQUITINATION, PROTEASOMAL DEGRADATION.
[25]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[26]"Neuropilin 1 directly interacts with Fer kinase to mediate semaphorin 3A-induced death of cortical neurons."
Jiang S.X., Whitehead S., Aylsworth A., Slinn J., Zurakowski B., Chan K., Li J., Hou S.T.
J. Biol. Chem. 285:9908-9918(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEURONAL CELL DEATH AFTER BRAIN DAMAGE, INTERACTION WITH NRP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U76762 mRNA. Translation: AAB18988.1.
M32054 mRNA. Translation: AAA37617.1.
AF286537 mRNA. Translation: AAG40730.1.
BC051249 mRNA. Translation: AAH51249.1.
BC058100 mRNA. Translation: AAH58100.1.
AK082799 mRNA. Translation: BAC38626.1.
CCDSCCDS28936.1. [P70451-1]
CCDS28937.1. [P70451-4]
PIRI49663.
RefSeqNP_001033086.2. NM_001037997.3. [P70451-1]
NP_001273344.1. NM_001286415.1. [P70451-2]
NP_032026.2. NM_008000.2. [P70451-4]
XP_006523703.1. XM_006523640.1. [P70451-1]
XP_006523704.1. XM_006523641.1. [P70451-1]
XP_006523705.1. XM_006523642.1. [P70451-5]
XP_006523706.1. XM_006523643.1. [P70451-5]
UniGeneMm.151391.
Mm.23039.

3D structure databases

ProteinModelPortalP70451.
SMRP70451. Positions 1-400, 453-820.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199633. 3 interactions.
STRING10090.ENSMUSP00000000129.

PTM databases

PhosphoSiteP70451.

Proteomic databases

MaxQBP70451.
PaxDbP70451.
PRIDEP70451.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000129; ENSMUSP00000000129; ENSMUSG00000000127. [P70451-1]
ENSMUST00000038080; ENSMUSP00000037418; ENSMUSG00000000127. [P70451-4]
GeneID14158.
KEGGmmu:14158.
UCSCuc008dfo.2. mouse. [P70451-2]
uc008dfp.1. mouse. [P70451-3]
uc008dfq.2. mouse. [P70451-1]
uc008dfr.2. mouse. [P70451-5]
uc008dfs.2. mouse. [P70451-4]

Organism-specific databases

CTD14158.
MGIMGI:105917. Fer.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117264.
HOGENOMHOG000233858.
HOVERGENHBG005655.
InParanoidQ9EQ77.
KOK08889.
OMAFVDNLYR.
OrthoDBEOG708VXW.
PhylomeDBP70451.
TreeFamTF315363.

Gene expression databases

ArrayExpressP70451.
BgeeP70451.
GenevestigatorP70451.

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:SF227. PTHR24418:SF227. 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

NextBio285280.
PROP70451.
SOURCESearch...

Entry information

Entry nameFER_MOUSE
AccessionPrimary (citable) accession number: P70451
Secondary accession number(s): Q61561 expand/collapse secondary AC list , Q6PEE5, Q80UI3, Q8C481, Q9EQ77
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 120 of the entry and version 2 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot