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P70451

- FER_MOUSE

UniProt

P70451 - FER_MOUSE

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Protein

Tyrosine-protein kinase Fer

Gene

Fer

Organism
Mus musculus (Mouse)
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). Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3 according to PubMed:10878010 and PubMed:19159681, but clearly plays a redundant role in STAT3 phosphorylation. According to PubMed:11134346, cells where wild type FER has been replaced by a kinase-dead mutant show no reduction in STAT3 phosphorylation.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.12 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

Enzyme regulationi

Activated by phosphatidic acid binding (By similarity). Activated by hydrogen peroxide (in vitro). Activated by reactive oxygen species (ROS).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei592 – 5921ATPPROSITE-ProRule annotation
Active sitei685 – 6851Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi570 – 5789ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. epidermal growth factor receptor binding Source: UniProtKB
  3. lipid binding Source: UniProtKB
  4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  5. protein kinase activity Source: MGI
  6. protein phosphatase 1 binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. cell adhesion Source: MGI
  3. cell-cell adhesion mediated by cadherin Source: UniProtKB
  4. cell proliferation Source: Ensembl
  5. cellular response to insulin stimulus Source: UniProtKB
  6. cellular response to macrophage colony-stimulating factor stimulus Source: Ensembl
  7. cellular response to reactive oxygen species Source: UniProtKB
  8. chemotaxis Source: MGI
  9. cytokine-mediated signaling pathway Source: UniProtKB
  10. diapedesis Source: UniProtKB
  11. extracellular matrix-cell signaling Source: UniProtKB
  12. Fc-epsilon receptor signaling pathway Source: UniProtKB
  13. insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
  14. interleukin-6-mediated signaling pathway Source: Ensembl
  15. Kit signaling pathway Source: UniProtKB
  16. microtubule cytoskeleton organization Source: UniProtKB
  17. mitotic cell cycle Source: Ensembl
  18. negative regulation of mast cell activation involved in immune response Source: UniProtKB
  19. peptidyl-tyrosine phosphorylation Source: UniProtKB
  20. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  21. positive regulation of actin filament polymerization Source: UniProtKB
  22. positive regulation of cell migration Source: UniProtKB
  23. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  24. protein autophosphorylation Source: MGI
  25. protein phosphorylation Source: MGI
  26. regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  27. regulation of fibroblast migration Source: UniProtKB
  28. regulation of lamellipodium assembly Source: UniProtKB
  29. regulation of protein phosphorylation Source: UniProtKB
  30. response to lipopolysaccharide Source: UniProtKB
  31. response to platelet-derived growth factor Source: UniProtKB
  32. signal transduction Source: MGI
  33. substrate adhesion-dependent cell spreading Source: UniProtKB
  34. 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_188578. 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
p94-Fer
Gene namesi
Name:Fer
Synonyms:Fert2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:105917. Fer.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeleton. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projection By similarity. Cell junction By similarity. Membrane By similarity; Peripheral membrane protein By similarity; 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 (PubMed:11339827).By similarity1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi135 – 1362KL → RP: Abolishes homooligomerization. 1 Publication
Mutagenesisi322 – 3232ML → RP: Abolishes homooligomerization. 1 Publication
Mutagenesisi571 – 5711G → R: Abolishes kinase activity. 1 Publication
Mutagenesisi592 – 5921K → R: Abolishes kinase activity. 1 Publication
Mutagenesisi606 – 6061F → A: Abolishes interaction with PPP1CA. 1 Publication
Mutagenesisi616 – 6161Y → F: Abolishes autophosphorylation. 1 Publication
Mutagenesisi715 – 7151Y → F: Abolishes autophosphorylation. 1 Publication
Mutagenesisi743 – 7431D → R: Abolishes kinase activity. 1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 823823Tyrosine-protein kinase FerPRO_0000260825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei402 – 4021Phosphotyrosine2 Publications
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei616 – 6161Phosphotyrosine; by autocatalysis1 Publication
Modified residuei715 – 7151Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Autophosphorylated.6 Publications
Polyubiquitinated; this leads to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP70451.
PaxDbiP70451.
PRIDEiP70451.

PTM databases

PhosphoSiteiP70451.

Expressioni

Tissue specificityi

Detected in liver and testis. Isoform 4 is detected only in testis (at protein level). Widely expressed.3 Publications

Inductioni

Up-regulated by insulin in myogenic cells (in vitro).1 Publication

Gene expression databases

BgeeiP70451.
ExpressionAtlasiP70451. baseline and differential.
GenevestigatoriP70451.

Interactioni

Subunit structurei

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.By similarity10 Publications

Protein-protein interaction databases

BioGridi199633. 3 interactions.
STRINGi10090.ENSMUSP00000000129.

Structurei

3D structure databases

ProteinModelPortaliP70451.
SMRiP70451. Positions 1-400, 453-820.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5858FCHPROSITE-ProRule annotationAdd
BLAST
Domaini461 – 55191SH2PROSITE-ProRule annotationAdd
BLAST
Domaini564 – 817254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 300300Important for interaction with membranes containing phosphoinositidesBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili123 – 18563Sequence AnalysisAdd
BLAST
Coiled coili301 – 38181Sequence AnalysisAdd
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

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.
HOGENOMiHOG000233858.
HOVERGENiHBG005655.
InParanoidiP70451.
KOiK08889.
OMAiFVDNLYR.
OrthoDBiEOG708VXW.
PhylomeDBiP70451.
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]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P70451-1) [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
MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC
60 70 80 90 100
NQVDKESTVQ VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL
110 120 130 140 150
TMMIKDKQQV KKSYVGIHQQ IEAEMIKVTK TELEKLKSSY RQLIKEMNSA
160 170 180 190 200
KEKYKEALAK GKETEKAKER YDKATMKLHM LHNQYVLALK GAQLHQSQYY
210 220 230 240 250
DTTLPLLLDS VQKMQEEMIK ALKGIFDDYS QITSLVTEEI VNVHKEIQMS
260 270 280 290 300
VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL
310 320 330 340 350
TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES FETCEKKSDI
360 370 380 390 400
VLLLGQKQAL EELKQSVQQL RCTEAKCAAQ KALLEQKVQE NDGKEPPPVV
410 420 430 440 450
NYEEDARSVT SMERKERLSK FESIRHSIAG IIKSPKSVLG SSTQVCDVIS
460 470 480 490 500
VGERPLAEHD WYHGAIPRIE AQELLKQQGD FLVRESHGKP GEYVLSVYSD
510 520 530 540 550
GQRRHFIIQF VDNLYRFEGT GFSNIPQLID HHFNTKQVIT KKSGVVLLNP
560 570 580 590 600
IPKDKKWVLN HEDVSLGELL GKGNFGEVYK GTLKDKTPVA IKTCKEDLPQ
610 620 630 640 650
ELKIKFLQEA KILKQYDHPN IVKLIGVCTQ RQPVYIIMEL VPGGDFLTFL
660 670 680 690 700
RKRKDELKLK QLVRFSLDVA AGMLYLESKN CIHRDLAARN CLVGENNTLK
710 720 730 740 750
ISDFGMSRQE DGGVYSSSGL KQIPIKWTAP EALNYGRYSS ESDVWSFGIL
760 770 780 790 800
LWETFSLGVC PYPGMTNQQA REQVERGYRM SAPQNCPEEV FTIMMKCWDY
810 820
KPENRPKFND LHKELTVIKK MIT
Length:823
Mass (Da):94,579
Last modified:November 28, 2006 - v2
Checksum:iF4C22E1E63721663
GO
Isoform 2 (identifier: P70451-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     70-127: Missing.

Note: No experimental confirmation available.

Show »
Length:765
Mass (Da):87,762
Checksum:i91FCCCAAFEF1C283
GO
Isoform 3 (identifier: P70451-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:532
Mass (Da):61,094
Checksum:i7468E01E9EB6F6E2
GO
Isoform 4 (identifier: P70451-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:453
Mass (Da):51,601
Checksum:i1CDAA93ED40B6A1D
GO
Isoform 5 (identifier: P70451-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:822
Mass (Da):94,451
Checksum:iF08F6BB10161D738
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti328 – 3281A → G in BAC38626. (PubMed:16141072)Curated
Sequence conflicti373 – 3731T → S in AAB18988. 1 PublicationCurated
Sequence conflicti373 – 3731T → S in AAG40730. (PubMed:11006284)Curated
Sequence conflicti730 – 7301P → A in AAA37617. (PubMed:2294399)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 369369Missing in isoform 4. 1 PublicationVSP_041766Add
BLAST
Alternative sequencei70 – 12758Missing in isoform 2. 1 PublicationVSP_021634Add
BLAST
Alternative sequencei370 – 41243LRCTE…SVTSM → MDKSMECPHCEGVLEPESDP QFSKKCSIPLSPGPSSSEIL RYK in isoform 4. 1 PublicationVSP_041767Add
BLAST
Alternative sequencei444 – 4441Missing in isoform 4 and isoform 5. 2 PublicationsVSP_041768
Alternative sequencei491 – 54252GEYVL…VITKK → ESVSIRGHRVFKHSPAYRSP LQYKASHHQEVWGGSAQPHP KG in isoform 3. 1 PublicationVSP_041769Add
BLAST
Alternative sequencei543 – 823281Missing in isoform 3. 1 PublicationVSP_041770Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS28936.1. [P70451-1]
CCDS28937.1. [P70451-4]
PIRiI49663.
RefSeqiNP_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]
UniGeneiMm.151391.
Mm.23039.

Genome annotation databases

EnsembliENSMUST00000000129; ENSMUSP00000000129; ENSMUSG00000000127. [P70451-1]
ENSMUST00000038080; ENSMUSP00000037418; ENSMUSG00000000127. [P70451-4]
GeneIDi14158.
KEGGimmu:14158.
UCSCiuc008dfo.2. mouse. [P70451-2]
uc008dfp.1. mouse. [P70451-3]
uc008dfq.2. mouse. [P70451-1]
uc008dfr.2. mouse. [P70451-5]
uc008dfs.2. mouse. [P70451-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS28936.1. [P70451-1 ]
CCDS28937.1. [P70451-4 ]
PIRi I49663.
RefSeqi NP_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 ]
UniGenei Mm.151391.
Mm.23039.

3D structure databases

ProteinModelPortali P70451.
SMRi P70451. Positions 1-400, 453-820.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199633. 3 interactions.
STRINGi 10090.ENSMUSP00000000129.

PTM databases

PhosphoSitei P70451.

Proteomic databases

MaxQBi P70451.
PaxDbi P70451.
PRIDEi P70451.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000000129 ; ENSMUSP00000000129 ; ENSMUSG00000000127 . [P70451-1 ]
ENSMUST00000038080 ; ENSMUSP00000037418 ; ENSMUSG00000000127 . [P70451-4 ]
GeneIDi 14158.
KEGGi mmu:14158.
UCSCi uc008dfo.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

CTDi 14158.
MGIi MGI:105917. Fer.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119011.
HOGENOMi HOG000233858.
HOVERGENi HBG005655.
InParanoidi P70451.
KOi K08889.
OMAi FVDNLYR.
OrthoDBi EOG708VXW.
PhylomeDBi P70451.
TreeFami TF315363.

Enzyme and pathway databases

Reactomei REACT_188578. Signaling by SCF-KIT.

Miscellaneous databases

NextBioi 285280.
PROi P70451.
SOURCEi Search...

Gene expression databases

Bgeei P70451.
ExpressionAtlasi P70451. baseline and differential.
Genevestigatori P70451.

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. "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.
    , 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. 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.

Entry informationi

Entry nameiFER_MOUSE
AccessioniPrimary (citable) accession number: P70451
Secondary accession number(s): Q61561
, Q6PEE5, Q80UI3, Q8C481, Q9EQ77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: October 29, 2014
This is version 123 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3