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P09769

- FGR_HUMAN

UniProt

P09769 - FGR_HUMAN

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Protein
Tyrosine-protein kinase Fgr
Gene
FGR, SRC2
Organism
Homo sapiens (Human)
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, FCGR2A and/or FCGR2B. 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. Required for normal ITGB1 and ITGB2 signaling, normal cell spreading and adhesion in neutrophils and macrophages. Functions as positive regulator of cell migration and regulates cytoskeleton reorganization via RAC1 activation. Phosphorylates SYK (in vitro) and promotes SYK-dependent activation of AKT1 and MAP kinase signaling. 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 HCLS1.4 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.3 Publications

Enzyme regulationi

Activated by autophosphorylation. Prior phosphorylation at Tyr-523 by SRC inhibits ulterior autophosphorylation at Tyr-412. 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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei291 – 2911ATP By similarity
Active sitei382 – 3821Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi269 – 2779ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. Fc-gamma receptor I complex binding Source: UniProtKB
  3. immunoglobulin receptor binding Source: UniProtKB
  4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  5. phosphotyrosine binding Source: UniProtKB
  6. protein binding Source: IntAct
  7. protein kinase binding Source: UniProtKB
  8. protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  2. blood coagulation Source: Reactome
  3. defense response to Gram-positive bacterium Source: UniProtKB
  4. immune response-regulating cell surface receptor signaling pathway Source: UniProtKB
  5. innate immune response Source: Reactome
  6. integrin-mediated signaling pathway Source: UniProtKB
  7. peptidyl-tyrosine phosphorylation Source: UniProtKB
  8. positive regulation of cell migration Source: UniProtKB
  9. positive regulation of cytokine secretion Source: UniProtKB
  10. positive regulation of mast cell degranulation Source: UniProtKB
  11. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  12. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  13. protein autophosphorylation Source: UniProtKB
  14. protein phosphorylation Source: ProtInc
  15. regulation of cell shape Source: UniProtKB
  16. regulation of innate immune response Source: UniProtKB
  17. regulation of phagocytosis Source: UniProtKB
  18. regulation of protein kinase activity Source: UniProtKB
  19. response to virus Source: ProtInc
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

ReactomeiREACT_160274. FCGR activation.
REACT_23879. Platelet sensitization by LDL.
SignaLinkiP09769.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Fgr (EC:2.7.10.2)
Alternative name(s):
Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog
Proto-oncogene c-Fgr
p55-Fgr
p58-Fgr
p58c-Fgr
Gene namesi
Name:FGR
Synonyms:SRC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3697. FGR.

Subcellular locationi

Cell membrane; Lipid-anchor; Cytoplasmic side Inferred. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionruffle membrane. Cytoplasmcytosol. Cytoplasmcytoskeleton. 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.2 Publications

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. mitochondrial inner membrane Source: UniProtKB-SubCell
  5. mitochondrial intermembrane space Source: UniProtKB-SubCell
  6. plasma membrane Source: UniProtKB
  7. ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Mutations that cause aberrant kinase activation can confer oncogene activity and promote aberrant cell proliferation.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi523 – 5231Y → F: Strongly increased catalytic activity. Functions as oncogene. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA28135.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 529528Tyrosine-protein kinase Fgr
PRO_0000088091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Lipidationi3 – 31S-palmitoyl cysteine By similarity
Lipidationi6 – 61S-palmitoyl cysteine By similarity
Modified residuei34 – 341Phosphotyrosine1 Publication
Modified residuei412 – 4121Phosphotyrosine1 Publication
Modified residuei523 – 5231Phosphotyrosine; by SRC1 Publication

Post-translational modificationi

Ubiquitinated. Becomes ubiquitinated in response to ITGB2 signaling; this does not lead to degradation.1 Publication
Phosphorylated. Autophosphorylated on tyrosine residues. Becomes phosphorylated in response to FCGR2A and/or FCGR2B engagement, cell adhesion and signaling by ITGB2. Prior phosphorylation at Tyr-523 by SRC inhibits ulterior autophosphorylation at Tyr-412.4 Publications

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP09769.
PRIDEiP09769.

PTM databases

PhosphoSiteiP09769.

Expressioni

Tissue specificityi

Detected in neutrophils, monocytes and natural killer cells (at protein level). Detected in monocytes and large lymphocytes.3 Publications

Gene expression databases

ArrayExpressiP09769.
BgeeiP09769.
CleanExiHS_FGR.
GenevestigatoriP09769.

Organism-specific databases

HPAiCAB018959.
HPA002024.

Interactioni

Subunit structurei

Interacts with ITGB1, ITGB2, MS4A2/FCER1B, FCER1G, FCGR2A and/or FCGR2B. 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. Interacts with PIK3R1 and FASLG By similarity.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ALOX5P099172EBI-1383732,EBI-79934
ARP102753EBI-1383732,EBI-608057
ERBB2P046263EBI-1383732,EBI-641062
HSP90AB1P082382EBI-1383732,EBI-352572
KITP107212EBI-1383732,EBI-1379503
METP085812EBI-1383732,EBI-1039152

Protein-protein interaction databases

BioGridi108559. 20 interactions.
DIPiDIP-1049N.
IntActiP09769. 12 interactions.
MINTiMINT-1209880.
STRINGi9606.ENSP00000363115.

Structurei

3D structure databases

ProteinModelPortaliP09769.
SMRiP09769. Positions 78-527.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 13862SH3
Add
BLAST
Domaini144 – 24198SH2
Add
BLAST
Domaini263 – 516254Protein kinase
Add
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP09769.
KOiK08891.
OMAiTWNGSTK.
OrthoDBiEOG7GTT2V.
PhylomeDBiP09769.
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.

P09769-1 [UniParc]FASTAAdd to Basket

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MGCVFCKKLE PVATAKEDAG LEGDFRSYGA ADHYGPDPTK ARPASSFAHI    50
PNYSNFSSQA INPGFLDSGT IRGVSGIGVT LFIALYDYEA RTEDDLTFTK 100
GEKFHILNNT EGDWWEARSL SSGKTGCIPS NYVAPVDSIQ AEEWYFGKIG 150
RKDAERQLLS PGNPQGAFLI RESETTKGAY SLSIRDWDQT RGDHVKHYKI 200
RKLDMGGYYI TTRVQFNSVQ ELVQHYMEVN DGLCNLLIAP CTIMKPQTLG 250
LAKDAWEISR SSITLERRLG TGCFGDVWLG TWNGSTKVAV KTLKPGTMSP 300
KAFLEEAQVM KLLRHDKLVQ LYAVVSEEPI YIVTEFMCHG SLLDFLKNPE 350
GQDLRLPQLV DMAAQVAEGM AYMERMNYIH RDLRAANILV GERLACKIAD 400
FGLARLIKDD EYNPCQGSKF PIKWTAPEAA LFGRFTIKSD VWSFGILLTE 450
LITKGRIPYP GMNKREVLEQ VEQGYHMPCP PGCPASLYEA MEQTWRLDPE 500
ERPTFEYLQS FLEDYFTSAE PQYQPGDQT 529
Length:529
Mass (Da):59,479
Last modified:January 1, 1990 - v2
Checksum:i6B8C1E08414E0F9C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti110 – 1101T → I.1 Publication
Corresponds to variant rs34597831 [ dbSNP | Ensembl ].
VAR_041700
Natural varianti130 – 1301S → R.1 Publication
Corresponds to variant rs35334091 [ dbSNP | Ensembl ].
VAR_041701

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19722 mRNA. Translation: AAA52451.1.
AL031729 Genomic DNA. Translation: CAB62998.1.
CH471059 Genomic DNA. Translation: EAX07748.1.
CH471059 Genomic DNA. Translation: EAX07749.1.
CH471059 Genomic DNA. Translation: EAX07750.1.
BC064382 mRNA. Translation: AAH64382.1.
X52207, X52208 Genomic DNA. Translation: CAA36457.2.
M12724
, M12719, M12720, M12721, M12722, M12723 Genomic DNA. Translation: AAA52762.1.
CCDSiCCDS305.1.
PIRiA27676. TVHUFR.
RefSeqiNP_001036194.1. NM_001042729.1.
NP_001036212.1. NM_001042747.1.
NP_005239.1. NM_005248.2.
XP_006710515.1. XM_006710452.1.
UniGeneiHs.1422.

Genome annotation databases

EnsembliENST00000374003; ENSP00000363115; ENSG00000000938.
ENST00000374004; ENSP00000363116; ENSG00000000938.
ENST00000374005; ENSP00000363117; ENSG00000000938.
ENST00000399173; ENSP00000382126; ENSG00000000938.
GeneIDi2268.
KEGGihsa:2268.
UCSCiuc001boj.3. human.

Polymorphism databases

DMDMi125358.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19722 mRNA. Translation: AAA52451.1 .
AL031729 Genomic DNA. Translation: CAB62998.1 .
CH471059 Genomic DNA. Translation: EAX07748.1 .
CH471059 Genomic DNA. Translation: EAX07749.1 .
CH471059 Genomic DNA. Translation: EAX07750.1 .
BC064382 mRNA. Translation: AAH64382.1 .
X52207 , X52208 Genomic DNA. Translation: CAA36457.2 .
M12724
, M12719 , M12720 , M12721 , M12722 , M12723 Genomic DNA. Translation: AAA52762.1 .
CCDSi CCDS305.1.
PIRi A27676. TVHUFR.
RefSeqi NP_001036194.1. NM_001042729.1.
NP_001036212.1. NM_001042747.1.
NP_005239.1. NM_005248.2.
XP_006710515.1. XM_006710452.1.
UniGenei Hs.1422.

3D structure databases

ProteinModelPortali P09769.
SMRi P09769. Positions 78-527.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108559. 20 interactions.
DIPi DIP-1049N.
IntActi P09769. 12 interactions.
MINTi MINT-1209880.
STRINGi 9606.ENSP00000363115.

Chemistry

BindingDBi P09769.
ChEMBLi CHEMBL4454.
GuidetoPHARMACOLOGYi 2024.

PTM databases

PhosphoSitei P09769.

Polymorphism databases

DMDMi 125358.

Proteomic databases

PaxDbi P09769.
PRIDEi P09769.

Protocols and materials databases

DNASUi 2268.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374003 ; ENSP00000363115 ; ENSG00000000938 .
ENST00000374004 ; ENSP00000363116 ; ENSG00000000938 .
ENST00000374005 ; ENSP00000363117 ; ENSG00000000938 .
ENST00000399173 ; ENSP00000382126 ; ENSG00000000938 .
GeneIDi 2268.
KEGGi hsa:2268.
UCSCi uc001boj.3. human.

Organism-specific databases

CTDi 2268.
GeneCardsi GC01M027938.
HGNCi HGNC:3697. FGR.
HPAi CAB018959.
HPA002024.
MIMi 164940. gene.
neXtProti NX_P09769.
PharmGKBi PA28135.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi P09769.
KOi K08891.
OMAi TWNGSTK.
OrthoDBi EOG7GTT2V.
PhylomeDBi P09769.
TreeFami TF351634.

Enzyme and pathway databases

Reactomei REACT_160274. FCGR activation.
REACT_23879. Platelet sensitization by LDL.
SignaLinki P09769.

Miscellaneous databases

ChiTaRSi FGR. human.
GeneWikii FGR_(gene).
GenomeRNAii 2268.
NextBioi 9223.
PROi P09769.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09769.
Bgeei P09769.
CleanExi HS_FGR.
Genevestigatori P09769.

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. "Primary structure of the human fgr proto-oncogene product p55c-fgr."
    Katamine S., Notario V., Rao C.D., Miki T., Cheah M.S.C., Tronick S.R., Robbins K.C.
    Mol. Cell. Biol. 8:259-266(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Brain.
  5. "Structure and expression of c-fgr protooncogene mRNA in Epstein-Barr virus converted cell lines."
    Brickell P.M., Patel M.
    Br. J. Cancer 58:704-709(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-177 AND 524-529.
  6. "Isolation and sequencing of cDNA clones homologous to the v-fgr oncogene from a human B lymphocyte cell line, IM-9."
    Inoue K., Ikawa S., Semba K., Sukegawa J., Yamamoto T., Toyoshima K.
    Oncogene 1:301-304(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-143.
  7. "Structure of the complete human c-fgr proto-oncogene and identification of multiple transcriptional start sites."
    Patel M., Leevers S.J., Brickell P.M.
    Oncogene 5:201-206(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-142.
  8. "Structure, expression, and chromosomal location of the human c-fgr gene."
    Nishizawa M., Semba K., Yoshida M.C., Yamamoto T., Sasaki M., Toyoshima K.
    Mol. Cell. Biol. 6:511-517(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-416.
  9. "Specific expression of human c-fgr in natural immunity effector cells."
    Inoue K., Yamamoto T., Toyoshima K.
    Mol. Cell. Biol. 10:1789-1792(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
  10. "Diverse biologic properties imparted by the c-fgr proto-oncogene."
    Sartor O., Moriuchi R., Sameshima J.H., Severino M., Gutkind J.S., Robbins K.C.
    J. Biol. Chem. 267:3460-3465(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS PROTO-ONCOGENE, ROLE IN DISEASE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-523.
  11. "Association of immunoglobulin G Fc receptor II with Src-like protein-tyrosine kinase Fgr in neutrophils."
    Hamada F., Aoki M., Akiyama T., Toyoshima K.
    Proc. Natl. Acad. Sci. U.S.A. 90:6305-6309(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCGR2A AND/OR FCGR2B, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
  12. "Beta 2 integrin-dependent protein tyrosine phosphorylation and activation of the FGR protein tyrosine kinase in human neutrophils."
    Berton G., Fumagalli L., Laudanna C., Sorio C.
    J. Cell Biol. 126:1111-1121(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, FUNCTION IN INTEGRIN SIGNALING.
  13. "Activation of SRC family kinases in human neutrophils. Evidence that p58C-FGR and p53/56LYN redistributed to a Triton X-100-insoluble cytoskeletal fraction, also enriched in the caveolar protein caveolin, display an enhanced kinase activity."
    Yan S.R., Fumagalli L., Berton G.
    FEBS Lett. 380:198-203(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION AT THE CYTOSKELETON, ENZYME REGULATION.
  14. "Clustering of beta(2)-integrins on human neutrophils activates dual signaling pathways to PtdIns 3-kinase."
    Axelsson L., Hellberg C., Melander F., Smith D., Zheng L., Andersson T.
    Exp. Cell Res. 256:257-263(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF PIK3R1, PHOSPHORYLATION, INTERACTION WITH ITGB2 AND PIK3R1.
  15. "Phosphatidic acid regulates tyrosine phosphorylating activity in human neutrophils: enhancement of Fgr activity."
    Sergeant S., Waite K.A., Heravi J., McPhail L.C.
    J. Biol. Chem. 276:4737-4746(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  16. "Fgr but not Syk tyrosine kinase is a target for beta 2 integrin-induced c-Cbl-mediated ubiquitination in adherent human neutrophils."
    Melander F., Andersson T., Dib K.
    Biochem. J. 370:687-694(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH CBL.
  17. "Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation."
    Zuccato E., Blott E.J., Holt O., Sigismund S., Shaw M., Bossi G., Griffiths G.M.
    J. Cell Sci. 120:191-199(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF FASLG, INTERACTION WITH FASLG.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-34; TYR-412 AND TYR-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-110 AND ARG-130.

Entry informationi

Entry nameiFGR_HUMAN
AccessioniPrimary (citable) accession number: P09769
Secondary accession number(s): D3DPL7, Q9UIQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 1, 1990
Last modified: September 3, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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