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P14234

- FGR_MOUSE

UniProt

P14234 - FGR_MOUSE

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Protein

Tyrosine-protein kinase Fgr

Gene

Fgr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors devoid of kinase activity and contributes to the regulation of immune responses, including neutrophil, monocyte, macrophage and mast cell functions, cytoskeleton remodeling in response to extracellular stimuli, phagocytosis, cell adhesion and migration. Promotes mast cell degranulation, release of inflammatory cytokines and IgE-mediated anaphylaxis. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as MS4A2/FCER1B, FCER1G and FCGR2. Acts downstream of ITGB1 and ITGB2, and regulates actin cytoskeleton reorganization, cell spreading and adhesion. Depending on the context, activates or inhibits cellular responses. Functions as negative regulator of ITGB2 signaling, phagocytosis and SYK activity in monocytes (PubMed:11672534). Required for normal ITGB1 and ITGB2 signaling, normal cell spreading and adhesion in neutrophils and macrophages (PubMed:8666673 and PubMed:9687507). Functions as positive regulator of cell migration and regulates cytoskeleton reorganization via RAC1 activation (PubMed:15561106). Phosphorylates SYK (in vitro) and promotes SYK-dependent activation of AKT1 and MAP kinase signaling (PubMed:21746961). Phosphorylates PLD2 in antigen-stimulated mast cells, leading to PLD2 activation and the production of the signaling molecules lysophosphatidic acid and diacylglycerol. Promotes activation of PIK3R1. Phosphorylates FASLG, and thereby regulates its ubiquitination and subsequent internalization. Phosphorylates ABL1. Promotes phosphorylation of CBL, CTTN, PIK3R1, PTK2/FAK1, PTK2B/PYK2 and VAV2. Phosphorylates HCLS1 that has already been phosphorylated by SYK, but not unphosphorylated HCLS1.8 Publications

Catalytic activityi

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

Enzyme regulationi

Activated by autophosphorylation. Prior phosphorylation at Tyr-511 by SRC inhibits ulterior autophosphorylation at Tyr-400. Activated by phorbol myristate acetate, phosphatidic acid and poly-Lys. Binding (via SH2 domain) of HCLS1 that is already phosphorylated by SYK strongly increases kinase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei279 – 2791ATPPROSITE-ProRule annotation
Active sitei370 – 3701Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi257 – 2659ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. immunoglobulin receptor binding Source: UniProtKB
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  4. phosphotyrosine binding Source: UniProtKB
  5. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. defense response to Gram-positive bacterium Source: UniProtKB
  2. innate immune response Source: UniProtKB-KW
  3. integrin-mediated signaling pathway Source: UniProtKB
  4. peptidyl-tyrosine phosphorylation Source: UniProtKB
  5. positive regulation of cell migration Source: UniProtKB
  6. positive regulation of cytokine secretion Source: UniProtKB
  7. positive regulation of mast cell degranulation Source: UniProtKB
  8. positive regulation of phosphatidylinositol 3-kinase activity Source: Ensembl
  9. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  10. protein autophosphorylation Source: Ensembl
  11. regulation of actin cytoskeleton organization Source: UniProtKB
  12. regulation of cell shape Source: UniProtKB
  13. regulation of innate immune response Source: UniProtKB
  14. regulation of phagocytosis Source: UniProtKB
  15. regulation of protein kinase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_196487. FCGR activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Fgr (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene c-Fgr
p55-Fgr
Gene namesi
Name:Fgr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:95527. Fgr.

Subcellular locationi

Cell membrane 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell projectionruffle membrane 1 Publication. Cytoplasmcytosol 1 Publication. Cytoplasmcytoskeleton 1 Publication. Mitochondrion inner membrane By similarity. Mitochondrion intermembrane space By similarity
Note: Detected in mitochondrial intermembrane space and at inner membranes By similarity. Colocalizes with actin fibers at membrane ruffles. Detected at plasma membrane lipid rafts.By similarity

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-KW
  3. cytosol Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
  5. mitochondrial inner membrane Source: UniProtKB-KW
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice lacking both Fgr and Hck are normal and fertile, but show increased susceptibility to infection with Listeria monocytogenes. In addition, their polymorphonuclear leukocytes show defects in cell spreading and adhesion.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 77Missing: Abolishes localization at the cell membrane. 1 Publication
Mutagenesisi279 – 2791K → R: Loss of kinase activity. 1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedCurated
Chaini2 – 517516Tyrosine-protein kinase FgrPRO_0000088092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Lipidationi3 – 31S-palmitoyl cysteine1 Publication
Lipidationi6 – 61S-palmitoyl cysteine1 Publication
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei32 – 321PhosphotyrosineBy similarity
Modified residuei400 – 4001Phosphotyrosine; alternate1 Publication
Modified residuei400 – 4001Phosphotyrosine; by autocatalysis; alternateBy similarity
Modified residuei511 – 5111Phosphotyrosine; by SRCBy similarity

Post-translational modificationi

Ubiquitinated. Becomes ubiquitinated in response to ITGB2 signaling; this does not lead to degradation By similarity.By similarity
Phosphorylated. Autophosphorylated on tyrosine residues. Becomes phosphorylated in response to FCGR2 engagement, cell adhesion and signaling by ITGB2. Prior phosphorylation at Tyr-511 by SRC inhibits ulterior autophosphorylation at Tyr-400 By similarity.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP14234.
PaxDbiP14234.
PRIDEiP14234.

PTM databases

PhosphoSiteiP14234.

Expressioni

Gene expression databases

BgeeiP14234.
GenevestigatoriP14234.

Interactioni

Subunit structurei

Interacts with ITGB1, ITGB2, MS4A2/FCER1B, FCER1G and FCGR2. Interacts (via SH2 domain) with SYK (tyrosine phosphorylated). Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with PTK2/FAK1. Interacts (via SH2 domain) with HCLS1 (tyrosine phosphorylated by SYK). Interacts with SIRPA and PTPNS1. Interacts (not phosphorylated on tyrosine residues) with CBL; FGR tyrosine phosphorylation promotes dissociation By similarity.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ClnkQ9QZE23EBI-7587024,EBI-8040679

Protein-protein interaction databases

BioGridi199663. 1 interaction.
IntActiP14234. 3 interactions.
MINTiMINT-85500.
STRINGi10090.ENSMUSP00000030693.

Structurei

3D structure databases

ProteinModelPortaliP14234.
SMRiP14234. Positions 37-515.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 12662SH3PROSITE-ProRule annotationAdd
BLAST
Domaini132 – 22998SH2PROSITE-ProRule annotationAdd
BLAST
Domaini251 – 504254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP14234.
KOiK08891.
OMAiTWNGSTK.
OrthoDBiEOG7GTT2V.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR028459. FGR.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24418:SF224. PTHR24418:SF224. 1 hit.
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14234-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGCVFCKKLE PASKEDVGLE GDFRSQTAEE RYFPDPTQGR TSSVFPQPTS
60 70 80 90 100
PAFLNTGNMR SISGTGVTIF VALYDYEART GDDLTFTKGE KFHILNNTEY
110 120 130 140 150
DWWEARSLSS GHRGYVPSNY VAPVDSIQAE EWYFGKISRK DAERQLLSSG
160 170 180 190 200
NPQGAFLIRE SETTKGAYSL SIRDWDQNRG DHIKHYKIRK LDTGGYYITT
210 220 230 240 250
RAQFDSIQDL VRHYMEVNDG LCYLLTAPCT TTKPQTLGLA KDAWEIDRNS
260 270 280 290 300
IALERRLGTG CFGDVWLGTW NCSTKVAVKT LKPGTMSPKA FLEEAQIMKL
310 320 330 340 350
LRHDKLVQLY AVVSEEPIYI VTEFMCYGSL LDFLKDREGQ NLMLPHLVDM
360 370 380 390 400
AAQVAEGMAY MERMNYIHRD LRAANILVGE YLICKIADFG LARLIEDNEY
410 420 430 440 450
NPQQGTKFPI KWTAPEAALF GRFTVKSDVW SFGILLTELI TKGRVPYPGM
460 470 480 490 500
NNREVLEQVE HGYHMPCPPG CPASLYEVME QAWRLDPEER PTFEYLQSFL
510
EDYFTSTEPQ YQPGDQT
Length:517
Mass (Da):58,867
Last modified:July 27, 2011 - v2
Checksum:i87DF5B19BF3F4734
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331F → Y in CAA34463. (PubMed:2674853)Curated
Sequence conflicti33 – 331F → Y in CAA36437. (PubMed:2179817)Curated
Sequence conflicti41 – 411T → N in CAA34463. (PubMed:2674853)Curated
Sequence conflicti212 – 2121R → Q in CAA34463. (PubMed:2674853)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16440 mRNA. Translation: CAA34463.1.
X52191 mRNA. Translation: CAA36437.1.
AK036438 mRNA. Translation: BAC29429.1.
AK036476 mRNA. Translation: BAC29445.1.
AK038141 mRNA. Translation: BAC29939.1.
AK155902 mRNA. Translation: BAE33493.1.
AL627184 Genomic DNA. Translation: CAM14378.1.
CH466552 Genomic DNA. Translation: EDL30081.1.
CH466552 Genomic DNA. Translation: EDL30082.1.
CCDSiCCDS18739.1.
PIRiA43807.
RefSeqiNP_034338.3. NM_010208.4.
XP_006538607.1. XM_006538544.1.
XP_006538608.1. XM_006538545.1.
UniGeneiMm.271665.

Genome annotation databases

EnsembliENSMUST00000030693; ENSMUSP00000030693; ENSMUSG00000028874.
ENSMUST00000171223; ENSMUSP00000128411; ENSMUSG00000028874.
GeneIDi14191.
KEGGimmu:14191.
UCSCiuc012dmj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16440 mRNA. Translation: CAA34463.1 .
X52191 mRNA. Translation: CAA36437.1 .
AK036438 mRNA. Translation: BAC29429.1 .
AK036476 mRNA. Translation: BAC29445.1 .
AK038141 mRNA. Translation: BAC29939.1 .
AK155902 mRNA. Translation: BAE33493.1 .
AL627184 Genomic DNA. Translation: CAM14378.1 .
CH466552 Genomic DNA. Translation: EDL30081.1 .
CH466552 Genomic DNA. Translation: EDL30082.1 .
CCDSi CCDS18739.1.
PIRi A43807.
RefSeqi NP_034338.3. NM_010208.4.
XP_006538607.1. XM_006538544.1.
XP_006538608.1. XM_006538545.1.
UniGenei Mm.271665.

3D structure databases

ProteinModelPortali P14234.
SMRi P14234. Positions 37-515.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199663. 1 interaction.
IntActi P14234. 3 interactions.
MINTi MINT-85500.
STRINGi 10090.ENSMUSP00000030693.

Chemistry

ChEMBLi CHEMBL2034795.

PTM databases

PhosphoSitei P14234.

Proteomic databases

MaxQBi P14234.
PaxDbi P14234.
PRIDEi P14234.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030693 ; ENSMUSP00000030693 ; ENSMUSG00000028874 .
ENSMUST00000171223 ; ENSMUSP00000128411 ; ENSMUSG00000028874 .
GeneIDi 14191.
KEGGi mmu:14191.
UCSCi uc012dmj.1. mouse.

Organism-specific databases

CTDi 2268.
MGIi MGI:95527. Fgr.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118938.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi P14234.
KOi K08891.
OMAi TWNGSTK.
OrthoDBi EOG7GTT2V.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_196487. FCGR activation.

Miscellaneous databases

NextBioi 285410.
PROi P14234.
SOURCEi Search...

Gene expression databases

Bgeei P14234.
Genevestigatori P14234.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR028459. FGR.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
PANTHERi PTHR24418:SF224. PTHR24418:SF224. 1 hit.
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the murine c-fgr proto-oncogene cDNA and induction of c-fgr expression by proliferation and activation factors in normal bone marrow-derived monocytic cells."
    Yi T.L., Willman C.L.
    Oncogene 4:1081-1087(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: DBA/2J.
  2. "Molecular cloning and sequencing of the murine c-fgr gene."
    King F.J., Cole M.D.
    Oncogene 5:337-344(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Monocytic leukemia.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Bone and Thymus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Functional overlap in the src gene family: inactivation of hck and fgr impairs natural immunity."
    Lowell C.A., Soriano P., Varmus H.E.
    Genes Dev. 8:387-398(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN IMMUNITY TO LISTERIA INFECTION.
  7. "Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions."
    Lowell C.A., Fumagalli L., Berton G.
    J. Cell Biol. 133:895-910(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN CELL ADHESION AND INTEGRIN SIGNALING.
  8. "A beta 1 integrin signaling pathway involving Src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration."
    Meng F., Lowell C.A.
    EMBO J. 17:4391-4403(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ITGB1 SIGNALING, FUNCTION IN PHOSPHORYLATION OF CBL, INTERACTION WITH CBL.
  9. "Negative regulation of phagocytosis in murine macrophages by the Src kinase family member, Fgr."
    Gresham H.D., Dale B.M., Potter J.W., Chang P.W., Vines C.M., Lowell C.A., Lagenaur C.F., Willman C.L.
    J. Exp. Med. 191:515-528(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIRPA AND PTPNS1, MUTAGENESIS OF LYS-279, FUNCTION AS NEGATIVE REGULATOR OF PHAGOCYTOSIS.
  10. "Inhibition of beta 2 integrin receptor and Syk kinase signaling in monocytes by the Src family kinase Fgr."
    Vines C.M., Potter J.W., Xu Y., Geahlen R.L., Costello P.S., Tybulewicz V.L., Lowell C.A., Chang P.W., Gresham H.D., Willman C.L.
    Immunity 15:507-519(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS NEGATIVE REGULATOR OF SYK AND INTEGRIN SIGNALING, INTERACTION WITH SYK.
  11. "The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization."
    Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G.
    Exp. Cell Res. 302:253-269(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF CELL MIGRATION; ACTIVATION OF RAC1 AND IN PHOSPHORYLATION OF PIK3R1; PTK2/FAK1; VAV2; PTK2B/PYK2 AND CTTN, CATALYTIC ACTIVITY, INTERACTION WITH PTK2/FAK1, MYRISTOYLATION, PALMITOYLATION, MUTAGENESIS OF 1-MET--LYS-7, SUBCELLULAR LOCATION.
  12. "Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2."
    Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
    Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT3.
  13. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND TYR-400, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration."
    Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G.
    FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF CELL MIGRATION, INTERACTION WITH ABL1; ITGB1 AND ITGB2.
  15. "The Src family kinase Fgr is critical for activation of mast cells and IgE-mediated anaphylaxis in mice."
    Lee J.H., Kim J.W., Kim do K., Kim H.S., Park H.J., Park D.K., Kim A.R., Kim B., Beaven M.A., Park K.L., Kim Y.M., Choi W.S.
    J. Immunol. 187:1807-1815(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SYK; MAST CELL DEGRANULATION AND RELEASE OF CYTOKINES, INTERACTION WITH FCER1G.

Entry informationi

Entry nameiFGR_MOUSE
AccessioniPrimary (citable) accession number: P14234
Secondary accession number(s): Q61404, Q8BGM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 146 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