Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Macrophage colony-stimulating factor 1 receptor (CSF-1 receptor) (CSF-1-R) (CSF-1R) (M-CSF-R) (EC 2.7.10.1) (Proto-oncogene c-Fms) (CD antigen CD115)

 CSF1R_HUMAN             Reviewed;         972 AA.
P07333; B5A955; D3DQG2; Q6LDW5; Q6LDY4; Q86VW7;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
22-NOV-2017, entry version 204.
RecName: Full=Macrophage colony-stimulating factor 1 receptor;
AltName: Full=CSF-1 receptor;
Short=CSF-1-R;
Short=CSF-1R;
Short=M-CSF-R;
EC=2.7.10.1;
AltName: Full=Proto-oncogene c-Fms;
AltName: CD_antigen=CD115;
Flags: Precursor;
Name=CSF1R; Synonyms=FMS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2524025;
Hampe A., Shamoon B.M., Gobet M., Sherr C.J., Galibert F.;
"Nucleotide sequence and structural organization of the human FMS
proto-oncogene.";
Oncogene Res. 4:9-17(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2421165; DOI=10.1038/320277a0;
Coussens L., van Beveren C., Smith D., Chen E., Mitchell R.L.,
Isacke C.M., Verma I.M., Ullrich A.;
"Structural alteration of viral homologue of receptor proto-oncogene
fms at carboxyl terminus.";
Nature 320:277-280(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=9027509; DOI=10.1006/geno.1996.4482;
Andre C., Hampe A., Lachaume P., Martin E., Wang X.P., Manus V.,
Hu W.X., Galibert F.;
"Sequence analysis of two genomic regions containing the KIT and the
FMS receptor tyrosine kinase genes.";
Genomics 39:216-226(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=18593464; DOI=10.1186/ar2447;
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
"Novel splice variants derived from the receptor tyrosine kinase
superfamily are potential therapeutics for rheumatoid arthritis.";
Arthritis Res. Ther. 10:R73-R73(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
PubMed=2524648; DOI=10.1128/MCB.9.3.1336;
Visvader J., Verma I.M.;
"Differential transcription of exon 1 of the human c-fms gene in
placental trophoblasts and monocytes.";
Mol. Cell. Biol. 9:1336-1341(1989).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
PubMed=3525854;
Wheeler E.F., Roussel M.F., Hampe A., Walker M.H., Fried V.A.,
Look A.T., Rettenmier C.W., Sherr C.J.;
"The amino-terminal domain of the v-fms oncogene product includes a
functional signal peptide that directs synthesis of a transforming
glycoprotein in the absence of feline leukemia virus gag sequences.";
J. Virol. 59:224-233(1986).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
TISSUE=Placenta;
Flick M.B., Sapi E., Kacinski B.M.;
"Expression of a novel exon in the 5' UTR of human c-fms
transcripts.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-295.
PubMed=4028159; DOI=10.1016/0092-8674(85)90099-6;
Nienhuis A.W., Bunn H.F., Turner P.H., Gopal T.V., Nash W.G.,
O'Brien S.J., Sherr C.J.;
"Expression of the human c-fms proto-oncogene in hematopoietic cells
and its deletion in the 5q- syndrome.";
Cell 42:421-428(1985).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 874-972 (ISOFORM 1).
PubMed=3532121; DOI=10.1073/pnas.83.20.7800;
Browning P.J., Bunn H.F., Cline A., Shuman M., Nienhuis A.W.;
"'Replacement' of COOH-terminal truncation of v-fms with c-fms
sequences markedly reduces transformation potential.";
Proc. Natl. Acad. Sci. U.S.A. 83:7800-7804(1986).
[13]
FUNCTION IN CELL PROLIFERATION.
PubMed=7683918;
Bourette R.P., Mouchiroud G., Ouazana R., Morle F., Godet J.,
Blanchet J.P.;
"Expression of human colony-stimulating factor-1 (CSF-1) receptor in
murine pluripotent hematopoietic NFS-60 cells induces long-term
proliferation in response to CSF-1 without loss of erythroid
differentiation potential.";
Blood 81:2511-2520(1993).
[14]
INTERACTION WITH SRC; FYN AND YES1, AND MUTAGENESIS OF TYR-809.
PubMed=7681396;
Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D.,
Roussel M.F.;
"Activation of Src family kinases by colony stimulating factor-1, and
their association with its receptor.";
EMBO J. 12:943-950(1993).
[15]
INDUCTION BY GLUCOCORTICOIDS.
PubMed=7845678;
Sapi E., Flick M.B., Gilmore-Hebert M., Rodov S., Kacinski B.M.;
"Transcriptional regulation of the c-fms (CSF-1R) proto-oncogene in
human breast carcinoma cells by glucocorticoids.";
Oncogene 10:529-542(1995).
[16]
MUTAGENESIS OF TYR-708 AND ASP-802.
PubMed=10340379; DOI=10.1038/sj.onc.1202646;
Morley G.M., Uden M., Gullick W.J., Dibb N.J.;
"Cell specific transformation by c-fms activating loop mutations is
attributable to constitutive receptor degradation.";
Oncogene 18:3076-3084(1999).
[17]
FUNCTION IN CELLULAR SIGNALING; PHOSPHORYLATION OF INPP5D AND
ACTIVATION OF AKT1.
PubMed=12882960; DOI=10.1074/jbc.M305021200;
Baran C.P., Tridandapani S., Helgason C.D., Humphries R.K.,
Krystal G., Marsh C.B.;
"The inositol 5'-phosphatase SHIP-1 and the Src kinase Lyn negatively
regulate macrophage colony-stimulating factor-induced Akt activity.";
J. Biol. Chem. 278:38628-38636(2003).
[18]
FUNCTION IN REGULATION OF CELL PROLIFERATION; CELL ADHESION; CELL
SHAPE AND INTEGRITY OF CELL JUNCTIONS, MUTAGENESIS OF LEU-301 AND
TYR-969, AND ROLE IN DISEASE.
PubMed=15117969; DOI=10.1083/jcb.200309102;
Wrobel C.N., Debnath J., Lin E., Beausoleil S., Roussel M.F.,
Brugge J.S.;
"Autocrine CSF-1R activation promotes Src-dependent disruption of
mammary epithelial architecture.";
J. Cell Biol. 165:263-273(2004).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-302 AND ASN-353.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[20]
FUNCTION AS CSF1 RECEPTOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION,
ROLE IN DISEASE, AND ENZYME REGULATION.
PubMed=16648572; DOI=10.1158/1535-7163.MCT-05-0359;
Guo J., Marcotte P.A., McCall J.O., Dai Y., Pease L.J.,
Michaelides M.R., Davidsen S.K., Glaser K.B.;
"Inhibition of phosphorylation of the colony-stimulating factor-1
receptor (c-Fms) tyrosine kinase in transfected cells by ABT-869 and
other tyrosine kinase inhibitors.";
Mol. Cancer Ther. 5:1007-1013(2006).
[21]
FUNCTION IN CELL PROLIFERATION, CATALYTIC ACTIVITY,
AUTOPHOSPHORYLATION, ROLE IN DISEASE, AND ENZYME REGULATION.
PubMed=17121910; DOI=10.1158/1535-7163.MCT-05-0313;
Ohno H., Kubo K., Murooka H., Kobayashi Y., Nishitoba T., Shibuya M.,
Yoneda T., Isoe T.;
"A c-fms tyrosine kinase inhibitor, Ki20227, suppresses osteoclast
differentiation and osteolytic bone destruction in a bone metastasis
model.";
Mol. Cancer Ther. 5:2634-2643(2006).
[22]
FUNCTION IN REGULATION OF CELL PROLIFERATION AND CELL SHAPE, CATALYTIC
ACTIVITY, UBIQUITINATION, ENZYME REGULATION, AND MUTAGENESIS OF
ASP-802.
PubMed=16170366; DOI=10.1038/sj.onc.1209007;
Taylor J.R., Brownlow N., Domin J., Dibb N.J.;
"FMS receptor for M-CSF (CSF-1) is sensitive to the kinase inhibitor
imatinib and mutation of Asp-802 to Val confers resistance.";
Oncogene 25:147-151(2006).
[23]
FUNCTION AS IL34 RECEPTOR.
PubMed=18467591; DOI=10.1126/science.1154370;
Lin H., Lee E., Hestir K., Leo C., Huang M., Bosch E., Halenbeck R.,
Wu G., Zhou A., Behrens D., Hollenbaugh D., Linnemann T., Qin M.,
Wong J., Chu K., Doberstein S.K., Williams L.T.;
"Discovery of a cytokine and its receptor by functional screening of
the extracellular proteome.";
Science 320:807-811(2008).
[24]
ROLE IN DISEASE, AND ENZYME REGULATION.
PubMed=18814279; DOI=10.1002/ijc.23903;
Hiraga T., Nakamura H.;
"Imatinib mesylate suppresses bone metastases of breast cancer by
inhibiting osteoclasts through the blockade of c-Fms signals.";
Int. J. Cancer 124:215-222(2009).
[25]
ROLE IN DISEASE.
PubMed=19934330; DOI=10.1158/0008-5472.CAN-09-1868;
Patsialou A., Wyckoff J., Wang Y., Goswami S., Stanley E.R.,
Condeelis J.S.;
"Invasion of human breast cancer cells in vivo requires both paracrine
and autocrine loops involving the colony-stimulating factor-1
receptor.";
Cancer Res. 69:9498-9506(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-699 AND SER-713, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[27]
AUTOPHOSPHORYLATION, AND ENZYME REGULATION.
PubMed=20156689; DOI=10.1016/j.bmc.2010.01.056;
Mashkani B., Griffith R., Ashman L.K.;
"Colony stimulating factor-1 receptor as a target for small molecule
inhibitors.";
Bioorg. Med. Chem. 18:1789-1797(2010).
[28]
FUNCTION AS RECEPTOR FOR IL34 AND CSF1, PHOSPHORYLATION AT TYR-546;
TYR-699; TYR-708; TYR-723 AND TYR-809, AUTOPHOSPHORYLATION, ENZYME
REGULATION, AND INTERACTION WITH IL34 AND CSF1.
PubMed=20489731; DOI=10.1038/cdd.2010.60;
Chihara T., Suzu S., Hassan R., Chutiwitoonchai N., Hiyoshi M.,
Motoyoshi K., Kimura F., Okada S.;
"IL-34 and M-CSF share the receptor Fms but are not identical in
biological activity and signal activation.";
Cell Death Differ. 17:1917-1927(2010).
[29]
FUNCTION IN RELEASE OF PROINFLAMMATORY CHEMOKINES.
PubMed=20829061; DOI=10.1016/j.cyto.2010.08.005;
Eda H., Zhang J., Keith R.H., Michener M., Beidler D.R., Monahan J.B.;
"Macrophage-colony stimulating factor and interleukin-34 induce
chemokines in human whole blood.";
Cytokine 52:215-220(2010).
[30]
FUNCTION AS IL34 AND CSF1 RECEPTOR; ACTIVATION OF MAPK1/ERK2;
MAPK3/ERK1; PHOSPHORYLATION AT TYR-723, AND AUTOPHOSPHORYLATION.
PubMed=20504948; DOI=10.1189/jlb.1209822;
Wei S., Nandi S., Chitu V., Yeung Y.G., Yu W., Huang M.,
Williams L.T., Lin H., Stanley E.R.;
"Functional overlap but differential expression of CSF-1 and IL-34 in
their CSF-1 receptor-mediated regulation of myeloid cells.";
J. Leukoc. Biol. 88:495-505(2010).
[31]
REVIEW ON FUNCTION; SIGNALING PATHWAYS AND PHOSPHORYLATION.
PubMed=15519852; DOI=10.1016/j.tcb.2004.09.016;
Pixley F.J., Stanley E.R.;
"CSF-1 regulation of the wandering macrophage: complexity in action.";
Trends Cell Biol. 14:628-638(2004).
[32]
REVIEW ON FUNCTION IN IMMUNITY AND INFLAMMATION, AND ROLE IN DISEASE.
PubMed=16337366; DOI=10.1016/j.coi.2005.11.006;
Chitu V., Stanley E.R.;
"Colony-stimulating factor-1 in immunity and inflammation.";
Curr. Opin. Immunol. 18:39-48(2006).
[33]
REVIEW ON FUNCTION; SIGNALING PATHWAYS AND PHOSPHORYLATION.
PubMed=18687298; DOI=10.1016/j.intimp.2008.04.016;
Douglass T.G., Driggers L., Zhang J.G., Hoa N., Delgado C.,
Williams C.C., Dan Q., Sanchez R., Jeffes E.W., Wepsic H.T.,
Myers M.P., Koths K., Jadus M.R.;
"Macrophage colony stimulating factor: not just for macrophages
anymore! A gateway into complex biologies.";
Int. Immunopharmacol. 8:1354-1376(2008).
[34]
REVIEW.
PubMed=19132917; DOI=10.1146/annurev.immunol.021908.132557;
Auffray C., Sieweke M.H., Geissmann F.;
"Blood monocytes: development, heterogeneity, and relationship with
dendritic cells.";
Annu. Rev. Immunol. 27:669-692(2009).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[36]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 538-922 IN COMPLEXES WITH
ARYLAMIDE AND QUINOLONE INHIBITORS, AND DOMAIN.
PubMed=17132624; DOI=10.1074/jbc.M608183200;
Schubert C., Schalk-Hihi C., Struble G.T., Ma H.C., Petrounia I.P.,
Brandt B., Deckman I.C., Patch R.J., Player M.R., Spurlino J.C.,
Springer B.A.;
"Crystal structure of the tyrosine kinase domain of colony-stimulating
factor-1 receptor (cFMS) in complex with two inhibitors.";
J. Biol. Chem. 282:4094-4101(2007).
[37]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 543-918 IN AUTOINHIBITED
CONFORMATION, AND DOMAIN.
PubMed=17292918; DOI=10.1016/j.jmb.2007.01.036;
Walter M., Lucet I.S., Patel O., Broughton S.E., Bamert R.,
Williams N.K., Fantino E., Wilks A.F., Rossjohn J.;
"The 2.7 A crystal structure of the autoinhibited human c-Fms kinase
domain.";
J. Mol. Biol. 367:839-847(2007).
[38]
X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 538-922 IN COMPLEX WITH
PYRIMIDINOPYRIDONE INHIBITOR, AND CATALYTIC ACTIVITY.
PubMed=18342505; DOI=10.1016/j.bmcl.2008.02.070;
Huang H., Hutta D.A., Hu H., DesJarlais R.L., Schubert C.,
Petrounia I.P., Chaikin M.A., Manthey C.L., Player M.R.;
"Design and synthesis of a pyrido[2,3-d]pyrimidin-5-one class of anti-
inflammatory FMS inhibitors.";
Bioorg. Med. Chem. Lett. 18:2355-2361(2008).
[39]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 538-922 IN COMPLEX WITH
INHIBITOR, CATALYTIC ACTIVITY, AND FUNCTION IN INFLAMMATION AND
DISEASE.
PubMed=19193011; DOI=10.1021/jm801406h;
Huang H., Hutta D.A., Rinker J.M., Hu H., Parsons W.H., Schubert C.,
DesJarlais R.L., Crysler C.S., Chaikin M.A., Donatelli R.R., Chen Y.,
Cheng D., Zhou Z., Yurkow E., Manthey C.L., Player M.R.;
"Pyrido[2,3-d]pyrimidin-5-ones: a novel class of antiinflammatory
macrophage colony-stimulating factor-1 receptor inhibitors.";
J. Med. Chem. 52:1081-1099(2009).
[40]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 538-922 IN COMPLEXES WITH
INHIBITORS, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=20137931; DOI=10.1016/j.bmcl.2010.01.078;
Meyers M.J., Pelc M., Kamtekar S., Day J., Poda G.I., Hall M.K.,
Michener M.L., Reitz B.A., Mathis K.J., Pierce B.S., Parikh M.D.,
Mischke D.A., Long S.A., Parlow J.J., Anderson D.R., Thorarensen A.;
"Structure-based drug design enables conversion of a DFG-in binding
CSF-1R kinase inhibitor to a DFG-out binding mode.";
Bioorg. Med. Chem. Lett. 20:1543-1547(2010).
[41]
VARIANTS [LARGE SCALE ANALYSIS] GLY-32; ARG-362; SER-413; VAL-536;
HIS-693; ASP-920 AND GLN-921.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[42]
VARIANTS HDLS 774-CYS--ASN-814 DEL; 585-GLY--LYS-619 DELINS ALA;
GLU-589; LYS-633; THR-766; PRO-770; ASN-775; THR-794; TYR-837;
SER-849; PHE-849 DEL; PRO-868; THR-875 AND THR-878, VARIANTS HIS-710;
ARG-747 AND ASP-920, AND CHARACTERIZATION OF VARIANTS HDLS LYS-633;
THR-766 AND THR-875.
PubMed=22197934; DOI=10.1038/ng.1027;
Rademakers R., Baker M., Nicholson A.M., Rutherford N.J., Finch N.,
Soto-Ortolaza A., Lash J., Wider C., Wojtas A., DeJesus-Hernandez M.,
Adamson J., Kouri N., Sundal C., Shuster E.A., Aasly J., MacKenzie J.,
Roeber S., Kretzschmar H.A., Boeve B.F., Knopman D.S., Petersen R.C.,
Cairns N.J., Ghetti B., Spina S., Garbern J., Tselis A.C., Uitti R.,
Das P., Van Gerpen J.A., Meschia J.F., Levy S., Broderick D.F.,
Graff-Radford N., Ross O.A., Miller B.B., Swerdlow R.H., Dickson D.W.,
Wszolek Z.K.;
"Mutations in the colony stimulating factor 1 receptor (CSF1R) gene
cause hereditary diffuse leukoencephalopathy with spheroids.";
Nat. Genet. 44:200-205(2012).
[43]
VARIANTS HDLS ARG-653; PHE-843 AND THR-906.
PubMed=24532199; DOI=10.1007/s00415-014-7257-3;
Battisti C., Di Donato I., Bianchi S., Monti L., Formichi P., Rufa A.,
Taglia I., Cerase A., Dotti M.T., Federico A.;
"Hereditary diffuse leukoencephalopathy with axonal spheroids: three
patients with stroke-like presentation carrying new mutations in the
CSF1R gene.";
J. Neurol. 261:768-772(2014).
-!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface
receptor for CSF1 and IL34 and plays an essential role in the
regulation of survival, proliferation and differentiation of
hematopoietic precursor cells, especially mononuclear phagocytes,
such as macrophages and monocytes. Promotes the release of
proinflammatory chemokines in response to IL34 and CSF1, and
thereby plays an important role in innate immunity and in
inflammatory processes. Plays an important role in the regulation
of osteoclast proliferation and differentiation, the regulation of
bone resorption, and is required for normal bone and tooth
development. Required for normal male and female fertility, and
for normal development of milk ducts and acinar structures in the
mammary gland during pregnancy. Promotes reorganization of the
actin cytoskeleton, regulates formation of membrane ruffles, cell
adhesion and cell migration, and promotes cancer cell invasion.
Activates several signaling pathways in response to ligand
binding. Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL.
Activation of PLCG2 leads to the production of the cellular
signaling molecules diacylglycerol and inositol 1,4,5-
trisphosphate, that then lead to the activation of protein kinase
C family members, especially PRKCD. Phosphorylation of PIK3R1, the
regulatory subunit of phosphatidylinositol 3-kinase, leads to
activation of the AKT1 signaling pathway. Activated CSF1R also
mediates activation of the MAP kinases MAPK1/ERK2 and/or
MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1.
Activated CSF1R transmits signals both via proteins that directly
interact with phosphorylated tyrosine residues in its
intracellular domain, or via adapter proteins, such as GRB2.
Promotes activation of STAT family members STAT3, STAT5A and/or
STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP-
1. Receptor signaling is down-regulated by protein phosphatases,
such as INPP5D/SHIP-1, that dephosphorylate the receptor and its
downstream effectors, and by rapid internalization of the
activated receptor. {ECO:0000269|PubMed:12882960,
ECO:0000269|PubMed:15117969, ECO:0000269|PubMed:16170366,
ECO:0000269|PubMed:16337366, ECO:0000269|PubMed:16648572,
ECO:0000269|PubMed:17121910, ECO:0000269|PubMed:18467591,
ECO:0000269|PubMed:18814279, ECO:0000269|PubMed:19193011,
ECO:0000269|PubMed:19934330, ECO:0000269|PubMed:20489731,
ECO:0000269|PubMed:20504948, ECO:0000269|PubMed:20829061,
ECO:0000269|PubMed:7683918}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:16170366,
ECO:0000269|PubMed:16648572, ECO:0000269|PubMed:17121910,
ECO:0000269|PubMed:18342505, ECO:0000269|PubMed:19193011,
ECO:0000269|PubMed:20137931}.
-!- ENZYME REGULATION: Present in an inactive conformation in the
absence of bound ligand. CSF1 or IL34 binding leads to
dimerization and activation by autophosphorylation on tyrosine
residues. Inhibited by imatinib/STI-571 (Gleevec), dasatinib,
sunitinib/SU11248, lestaurtinib/CEP-701, midostaurin/PKC-412,
Ki20227, linifanib/ABT-869, Axitinib/AG013736, sorafenib/BAY 43-
9006 and GW2580. {ECO:0000269|PubMed:16170366,
ECO:0000269|PubMed:16648572, ECO:0000269|PubMed:17121910,
ECO:0000269|PubMed:18814279, ECO:0000269|PubMed:20137931,
ECO:0000269|PubMed:20156689, ECO:0000269|PubMed:20489731}.
-!- SUBUNIT: Interacts with INPPL1/SHIP2 and THOC5 (By similarity).
Monomer. Homodimer. Interacts with CSF1 and IL34. Interaction with
dimeric CSF1 or IL34 leads to receptor homodimerization. Interacts
(tyrosine phosphorylated) with PLCG2 (via SH2 domain). Interacts
(tyrosine phosphorylated) with PIK3R1 (via SH2 domain). Interacts
(tyrosine phosphorylated) with FYN, YES1 and SRC (via SH2 domain).
Interacts (tyrosine phosphorylated) with CBL, GRB2 and SLA2.
{ECO:0000250, ECO:0000269|PubMed:18342505,
ECO:0000269|PubMed:19193011, ECO:0000269|PubMed:20489731,
ECO:0000269|PubMed:7681396}.
-!- INTERACTION:
P09603:CSF1; NbExp=13; IntAct=EBI-2835440, EBI-2872294;
Q6ZMJ4-1:IL34; NbExp=9; IntAct=EBI-2835440, EBI-15978980;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P07333-1; Sequence=Displayed;
Name=2;
IsoId=P07333-2; Sequence=VSP_047757, VSP_047758;
-!- TISSUE SPECIFICITY: Expressed in bone marrow and in differentiated
blood mononuclear cells.
-!- INDUCTION: Up-regulated by glucocorticoids.
{ECO:0000269|PubMed:7845678}.
-!- DOMAIN: The juxtamembrane domain functions as autoinhibitory
region. Phosphorylation of tyrosine residues in this region leads
to a conformation change and activation of the kinase.
-!- DOMAIN: The activation loop plays an important role in the
regulation of kinase activity. Phosphorylation of tyrosine
residues in this region leads to a conformation change and
activation of the kinase.
-!- PTM: Autophosphorylated in response to CSF1 or IL34 binding.
Phosphorylation at Tyr-561 is important for normal down-regulation
of signaling by ubiquitination, internalization and degradation.
Phosphorylation at Tyr-561 and Tyr-809 is important for
interaction with SRC family members, including FYN, YES1 and SRC,
and for subsequent activation of these protein kinases.
Phosphorylation at Tyr-699 and Tyr-923 is important for
interaction with GRB2. Phosphorylation at Tyr-723 is important for
interaction with PIK3R1. Phosphorylation at Tyr-708 is important
for normal receptor degradation. Phosphorylation at Tyr-723 and
Tyr-809 is important for interaction with PLCG2. Phosphorylation
at Tyr-969 is important for interaction with CBL.
Dephosphorylation by PTPN2 negatively regulates downstream
signaling and macrophage differentiation.
{ECO:0000269|PubMed:16170366, ECO:0000269|PubMed:20489731}.
-!- PTM: Ubiquitinated. Becomes rapidly polyubiquitinated after
autophosphorylation, leading to its degradation.
{ECO:0000269|PubMed:16170366}.
-!- DISEASE: Note=Aberrant expression of CSF1 or CSF1R can promote
cancer cell proliferation, invasion and formation of metastases.
Overexpression of CSF1 or CSF1R is observed in a significant
percentage of breast, ovarian, prostate, and endometrial cancers.
-!- DISEASE: Note=Aberrant expression of CSF1 or CSF1R may play a role
in inflammatory diseases, such as rheumatoid arthritis,
glomerulonephritis, atherosclerosis, and allograft rejection.
-!- DISEASE: Leukoencephalopathy, diffuse hereditary, with spheroids
(HDLS) [MIM:221820]: An autosomal dominant adult-onset rapidly
progressive neurodegenerative disorder characterized by variable
behavioral, cognitive, and motor changes. Patients often die of
dementia within 6 years of onset. Brain imaging shows patchy
abnormalities in the cerebral white matter, predominantly
affecting the frontal and parietal lobes.
{ECO:0000269|PubMed:22197934, ECO:0000269|PubMed:24532199}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CSF1RID40161ch5q32.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X03663; CAA27300.1; -; mRNA.
EMBL; U63963; AAB51696.1; -; Genomic_DNA.
EMBL; M25786; AAA58421.1; -; mRNA.
EMBL; EU826593; ACF47629.1; -; mRNA.
EMBL; AC011382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW61749.1; -; Genomic_DNA.
EMBL; CH471062; EAW61750.1; -; Genomic_DNA.
EMBL; BC047521; AAH47521.1; -; mRNA.
EMBL; M14002; AAA35849.1; -; Genomic_DNA.
EMBL; U78096; AAB51235.1; -; Genomic_DNA.
EMBL; M11067; AAA35848.1; -; Genomic_DNA.
EMBL; M14193; AAA35834.1; -; mRNA.
CCDS; CCDS4302.1; -. [P07333-1]
PIR; S08123; TVHUMD.
RefSeq; NP_001275634.1; NM_001288705.2. [P07333-1]
RefSeq; NP_005202.2; NM_005211.3. [P07333-1]
UniGene; Hs.586219; -.
PDB; 2I0V; X-ray; 2.80 A; A=538-678, A=753-922.
PDB; 2I0Y; X-ray; 1.90 A; A=538-678, A=753-922.
PDB; 2I1M; X-ray; 1.80 A; A=538-678, A=753-922.
PDB; 2OGV; X-ray; 2.70 A; A=543-918.
PDB; 3BEA; X-ray; 2.02 A; A=538-678, A=753-922.
PDB; 3DPK; X-ray; 1.95 A; A=538-678, A=771-922.
PDB; 3KRJ; X-ray; 2.10 A; A=538-678, A=753-922.
PDB; 3KRL; X-ray; 2.40 A; A=538-678, A=753-922.
PDB; 3LCD; X-ray; 2.50 A; A=538-919.
PDB; 3LCO; X-ray; 3.40 A; A=550-919.
PDB; 4DKD; X-ray; 3.00 A; C=20-299.
PDB; 4HW7; X-ray; 2.90 A; A=542-919.
PDB; 4LIQ; X-ray; 2.60 A; E=2-512.
PDB; 4R7H; X-ray; 2.80 A; A=542-919.
PDB; 4R7I; X-ray; 2.75 A; A=542-919.
PDB; 4WRL; X-ray; 2.80 A; A/C=20-296.
PDB; 4WRM; X-ray; 6.85 A; A=20-504.
PDBsum; 2I0V; -.
PDBsum; 2I0Y; -.
PDBsum; 2I1M; -.
PDBsum; 2OGV; -.
PDBsum; 3BEA; -.
PDBsum; 3DPK; -.
PDBsum; 3KRJ; -.
PDBsum; 3KRL; -.
PDBsum; 3LCD; -.
PDBsum; 3LCO; -.
PDBsum; 4DKD; -.
PDBsum; 4HW7; -.
PDBsum; 4LIQ; -.
PDBsum; 4R7H; -.
PDBsum; 4R7I; -.
PDBsum; 4WRL; -.
PDBsum; 4WRM; -.
ProteinModelPortal; P07333; -.
SMR; P07333; -.
BioGrid; 107823; 20.
DIP; DIP-59421N; -.
IntAct; P07333; 15.
MINT; MINT-8019993; -.
STRING; 9606.ENSP00000286301; -.
BindingDB; P07333; -.
ChEMBL; CHEMBL1844; -.
DrugBank; DB07167; 5-CYANO-FURAN-2-CARBOXYLIC ACID [5-HYDROXYMETHYL-2-(4-METHYL-PIPERIDIN-1-YL)-PHENYL]-AMIDE.
DrugBank; DB07202; 6-CHLORO-3-(3-METHYLISOXAZOL-5-YL)-4-PHENYLQUINOLIN-2(1H)-ONE.
DrugBank; DB06080; ABT-869.
DrugBank; DB00619; Imatinib.
DrugBank; DB01268; Sunitinib.
GuidetoPHARMACOLOGY; 1806; -.
iPTMnet; P07333; -.
PhosphoSitePlus; P07333; -.
BioMuta; CSF1R; -.
DMDM; 547770; -.
PaxDb; P07333; -.
PeptideAtlas; P07333; -.
PRIDE; P07333; -.
DNASU; 1436; -.
Ensembl; ENST00000286301; ENSP00000286301; ENSG00000182578. [P07333-1]
Ensembl; ENST00000543093; ENSP00000445282; ENSG00000182578. [P07333-2]
GeneID; 1436; -.
KEGG; hsa:1436; -.
UCSC; uc003lrm.3; human. [P07333-1]
CTD; 1436; -.
DisGeNET; 1436; -.
EuPathDB; HostDB:ENSG00000182578.13; -.
GeneCards; CSF1R; -.
GeneReviews; CSF1R; -.
HGNC; HGNC:2433; CSF1R.
HPA; CAB008970; -.
HPA; HPA012323; -.
MalaCards; CSF1R; -.
MIM; 164770; gene.
MIM; 221820; phenotype.
neXtProt; NX_P07333; -.
OpenTargets; ENSG00000182578; -.
Orphanet; 313808; Hereditary diffuse leukoencephalopathy with axonal spheroids and pigmented glia.
PharmGKB; PA26936; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000112008; -.
HOVERGEN; HBG004335; -.
InParanoid; P07333; -.
KO; K05090; -.
OMA; WKIIESY; -.
OrthoDB; EOG091G01TL; -.
PhylomeDB; P07333; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-449836; Other interleukin signaling.
SignaLink; P07333; -.
SIGNOR; P07333; -.
ChiTaRS; CSF1R; human.
EvolutionaryTrace; P07333; -.
GeneWiki; Colony_stimulating_factor_1_receptor; -.
GenomeRNAi; 1436; -.
PRO; PR:P07333; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000182578; -.
CleanEx; HS_CSF1R; -.
ExpressionAtlas; P07333; baseline and differential.
Genevisible; P07333; HS.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:1990682; C:CSF1-CSF1R complex; ISS:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019955; F:cytokine binding; IDA:UniProtKB.
GO; GO:0005011; F:macrophage colony-stimulating factor receptor activity; IMP:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0045217; P:cell-cell junction maintenance; IMP:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IMP:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0021879; P:forebrain neuron differentiation; IEA:Ensembl.
GO; GO:0030097; P:hemopoiesis; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0038145; P:macrophage colony-stimulating factor signaling pathway; ISS:BHF-UCL.
GO; GO:0030225; P:macrophage differentiation; TAS:UniProtKB.
GO; GO:0060603; P:mammary gland duct morphogenesis; TAS:UniProtKB.
GO; GO:0030224; P:monocyte differentiation; TAS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0021772; P:olfactory bulb development; IEA:Ensembl.
GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:2000147; P:positive regulation of cell motility; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0090197; P:positive regulation of chemokine secretion; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0045124; P:regulation of bone resorption; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0031529; P:ruffle organization; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR030658; CSF-1_receptor.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF00047; ig; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500947; CSF-1_receptor; 1.
SMART; SM00409; IG; 5.
SMART; SM00408; IGc2; 2.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 5.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Disease mutation; Disulfide bond; Glycoprotein;
Immunity; Immunoglobulin domain; Inflammatory response;
Innate immunity; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Proto-oncogene; Receptor; Reference proteome; Repeat;
Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 972 Macrophage colony-stimulating factor 1
receptor.
/FTId=PRO_0000016765.
TOPO_DOM 20 517 Extracellular. {ECO:0000255}.
TRANSMEM 518 538 Helical. {ECO:0000255}.
TOPO_DOM 539 972 Cytoplasmic. {ECO:0000255}.
DOMAIN 21 104 Ig-like C2-type 1.
DOMAIN 107 197 Ig-like C2-type 2.
DOMAIN 203 290 Ig-like C2-type 3.
DOMAIN 299 399 Ig-like C2-type 4.
DOMAIN 402 502 Ig-like C2-type 5.
DOMAIN 582 910 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 588 596 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 542 574 Regulatory juxtamembrane domain.
REGION 796 818 Activation loop.
ACT_SITE 778 778 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 616 616 ATP. {ECO:0000305}.
MOD_RES 546 546 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:20489731}.
MOD_RES 561 561 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09581}.
MOD_RES 699 699 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:20489731}.
MOD_RES 708 708 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:20489731}.
MOD_RES 713 713 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 723 723 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:20489731}.
MOD_RES 809 809 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:20489731}.
MOD_RES 923 923 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 969 969 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09581}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 412 412 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 480 480 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 42 84 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 127 177 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 224 278 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 419 485 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 297 306 ESAYLNLSSE -> GTPSPSLCPA (in isoform 2).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_047757.
VAR_SEQ 307 972 Missing (in isoform 2).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_047758.
VARIANT 32 32 V -> G (in dbSNP:rs56048668).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042038.
VARIANT 245 245 A -> S (in dbSNP:rs41338945).
/FTId=VAR_061290.
VARIANT 279 279 V -> M (in dbSNP:rs3829986).
/FTId=VAR_049718.
VARIANT 362 362 H -> R (in dbSNP:rs10079250).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042039.
VARIANT 413 413 G -> S (in dbSNP:rs34951517).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042040.
VARIANT 536 536 L -> V (in dbSNP:rs55942044).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042041.
VARIANT 585 619 GKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLK -> A
(in HDLS). {ECO:0000269|PubMed:22197934}.
/FTId=VAR_067396.
VARIANT 589 589 G -> E (in HDLS; dbSNP:rs281860268).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067397.
VARIANT 633 633 E -> K (in HDLS; impairs
autophosphorylation upon stimulation with
CSF1; dbSNP:rs281860269).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067398.
VARIANT 653 653 C -> R (in HDLS; dbSNP:rs690016559).
{ECO:0000269|PubMed:24532199}.
/FTId=VAR_072081.
VARIANT 693 693 P -> H (in a lung squamous cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042042.
VARIANT 710 710 R -> H (in dbSNP:rs201569135).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067399.
VARIANT 747 747 G -> R (in dbSNP:rs41355444).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067400.
VARIANT 766 766 M -> T (in HDLS; impairs
autophosphorylation upon stimulation with
CSF1; dbSNP:rs281860270).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067401.
VARIANT 770 770 A -> P (in HDLS; dbSNP:rs281860271).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067402.
VARIANT 774 814 Missing (in HDLS).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067403.
VARIANT 775 775 I -> N (in HDLS; impairs
autophosphorylation upon stimulation with
CSF1; dbSNP:rs281860273).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067404.
VARIANT 794 794 I -> T (in HDLS; dbSNP:rs281860274).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067405.
VARIANT 837 837 D -> Y (in HDLS; dbSNP:rs387906662).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067406.
VARIANT 843 843 I -> F (in HDLS; dbSNP:rs690016558).
{ECO:0000269|PubMed:24532199}.
/FTId=VAR_072082.
VARIANT 849 849 F -> S (in HDLS; dbSNP:rs281860277).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067407.
VARIANT 849 849 Missing (in HDLS).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067408.
VARIANT 868 868 L -> P (in HDLS; dbSNP:rs281860278).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067409.
VARIANT 875 875 M -> T (in HDLS; dbSNP:rs281860279).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067410.
VARIANT 878 878 P -> T (in HDLS; dbSNP:rs281860280).
{ECO:0000269|PubMed:22197934}.
/FTId=VAR_067411.
VARIANT 906 906 I -> T (in HDLS; dbSNP:rs690016560).
{ECO:0000269|PubMed:24532199}.
/FTId=VAR_072083.
VARIANT 920 920 E -> D (in dbSNP:rs34030164).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:22197934}.
/FTId=VAR_042043.
VARIANT 921 921 R -> Q (in dbSNP:rs56059682).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042044.
VARIANT 969 969 Y -> C (in dbSNP:rs1801271).
/FTId=VAR_011953.
MUTAGEN 301 301 L->S: Constitutive kinase activity.
{ECO:0000269|PubMed:15117969}.
MUTAGEN 708 708 Y->F: Impairs degradation of activated
CSF1R. {ECO:0000269|PubMed:10340379}.
MUTAGEN 802 802 D->V: Constitutive kinase activity. Loss
of inhibition by imatinib.
{ECO:0000269|PubMed:10340379,
ECO:0000269|PubMed:16170366}.
MUTAGEN 809 809 Y->F: Reduced kinase activity. Reduced
interaction with SRC, FYN and YES1.
{ECO:0000269|PubMed:7681396}.
MUTAGEN 969 969 Y->F: Abolishes down-regulation of
activated CSF1R.
{ECO:0000269|PubMed:15117969}.
CONFLICT 54 54 P -> A (in Ref. 2; CAA27300).
{ECO:0000305}.
CONFLICT 247 247 P -> H (in Ref. 7; AAH47521).
{ECO:0000305}.
CONFLICT 354 354 A -> V (in Ref. 7; AAH47521).
{ECO:0000305}.
CONFLICT 629 629 A -> S (in Ref. 7; AAH47521).
{ECO:0000305}.
STRAND 22 25 {ECO:0000244|PDB:4LIQ}.
STRAND 27 32 {ECO:0000244|PDB:4LIQ}.
STRAND 38 43 {ECO:0000244|PDB:4LIQ}.
STRAND 49 51 {ECO:0000244|PDB:4LIQ}.
TURN 55 57 {ECO:0000244|PDB:4LIQ}.
STRAND 58 62 {ECO:0000244|PDB:4LIQ}.
STRAND 64 73 {ECO:0000244|PDB:4LIQ}.
HELIX 76 78 {ECO:0000244|PDB:4LIQ}.
STRAND 80 85 {ECO:0000244|PDB:4LIQ}.
STRAND 95 101 {ECO:0000244|PDB:4LIQ}.
STRAND 108 111 {ECO:0000244|PDB:4LIQ}.
STRAND 113 118 {ECO:0000244|PDB:4LIQ}.
STRAND 123 125 {ECO:0000244|PDB:4LIQ}.
STRAND 127 130 {ECO:0000244|PDB:4LIQ}.
HELIX 132 137 {ECO:0000244|PDB:4LIQ}.
STRAND 139 142 {ECO:0000244|PDB:4LIQ}.
HELIX 143 145 {ECO:0000244|PDB:4WRL}.
STRAND 154 157 {ECO:0000244|PDB:4LIQ}.
TURN 158 160 {ECO:0000244|PDB:4LIQ}.
STRAND 161 166 {ECO:0000244|PDB:4LIQ}.
HELIX 169 171 {ECO:0000244|PDB:4LIQ}.
STRAND 173 181 {ECO:0000244|PDB:4LIQ}.
STRAND 184 187 {ECO:0000244|PDB:4LIQ}.
STRAND 191 196 {ECO:0000244|PDB:4LIQ}.
STRAND 204 208 {ECO:0000244|PDB:4LIQ}.
STRAND 210 215 {ECO:0000244|PDB:4LIQ}.
STRAND 216 218 {ECO:0000244|PDB:4DKD}.
STRAND 220 231 {ECO:0000244|PDB:4LIQ}.
STRAND 234 239 {ECO:0000244|PDB:4LIQ}.
STRAND 248 252 {ECO:0000244|PDB:4LIQ}.
STRAND 257 267 {ECO:0000244|PDB:4LIQ}.
TURN 270 272 {ECO:0000244|PDB:4LIQ}.
STRAND 274 282 {ECO:0000244|PDB:4LIQ}.
STRAND 285 298 {ECO:0000244|PDB:4LIQ}.
STRAND 300 304 {ECO:0000244|PDB:4LIQ}.
STRAND 309 314 {ECO:0000244|PDB:4LIQ}.
STRAND 319 329 {ECO:0000244|PDB:4LIQ}.
STRAND 332 338 {ECO:0000244|PDB:4LIQ}.
STRAND 340 342 {ECO:0000244|PDB:4LIQ}.
STRAND 351 354 {ECO:0000244|PDB:4LIQ}.
STRAND 361 368 {ECO:0000244|PDB:4LIQ}.
HELIX 373 375 {ECO:0000244|PDB:4LIQ}.
STRAND 377 385 {ECO:0000244|PDB:4LIQ}.
STRAND 388 411 {ECO:0000244|PDB:4LIQ}.
STRAND 414 425 {ECO:0000244|PDB:4LIQ}.
STRAND 428 437 {ECO:0000244|PDB:4LIQ}.
TURN 443 445 {ECO:0000244|PDB:4LIQ}.
STRAND 446 454 {ECO:0000244|PDB:4LIQ}.
STRAND 456 459 {ECO:0000244|PDB:4LIQ}.
STRAND 466 473 {ECO:0000244|PDB:4LIQ}.
STRAND 479 488 {ECO:0000244|PDB:4LIQ}.
STRAND 493 498 {ECO:0000244|PDB:4LIQ}.
STRAND 551 553 {ECO:0000244|PDB:4R7H}.
STRAND 556 559 {ECO:0000244|PDB:3KRJ}.
HELIX 566 568 {ECO:0000244|PDB:3KRJ}.
HELIX 573 575 {ECO:0000244|PDB:2I1M}.
STRAND 581 590 {ECO:0000244|PDB:2I1M}.
STRAND 592 601 {ECO:0000244|PDB:2I1M}.
STRAND 605 607 {ECO:0000244|PDB:2I1M}.
STRAND 612 618 {ECO:0000244|PDB:2I1M}.
HELIX 624 640 {ECO:0000244|PDB:2I1M}.
STRAND 649 653 {ECO:0000244|PDB:2I1M}.
STRAND 655 658 {ECO:0000244|PDB:2I1M}.
STRAND 660 664 {ECO:0000244|PDB:2I1M}.
HELIX 671 682 {ECO:0000244|PDB:2I1M}.
TURN 684 686 {ECO:0000244|PDB:4R7I}.
HELIX 753 771 {ECO:0000244|PDB:2I1M}.
HELIX 781 783 {ECO:0000244|PDB:2I1M}.
STRAND 785 787 {ECO:0000244|PDB:2I1M}.
HELIX 788 790 {ECO:0000244|PDB:2I1M}.
STRAND 791 794 {ECO:0000244|PDB:2I1M}.
HELIX 798 800 {ECO:0000244|PDB:2I1M}.
HELIX 803 805 {ECO:0000244|PDB:2I1M}.
TURN 806 808 {ECO:0000244|PDB:3LCO}.
STRAND 809 811 {ECO:0000244|PDB:2I1M}.
STRAND 815 817 {ECO:0000244|PDB:4R7I}.
HELIX 819 821 {ECO:0000244|PDB:2I1M}.
HELIX 824 829 {ECO:0000244|PDB:2I1M}.
HELIX 834 848 {ECO:0000244|PDB:2I1M}.
TURN 849 851 {ECO:0000244|PDB:2I1M}.
HELIX 863 871 {ECO:0000244|PDB:2I1M}.
HELIX 883 892 {ECO:0000244|PDB:2I1M}.
HELIX 897 899 {ECO:0000244|PDB:2I1M}.
HELIX 903 920 {ECO:0000244|PDB:2I1M}.
SEQUENCE 972 AA; 107984 MW; A8D99BE237573FE8 CRC64;
MGPGVLLLLL VATAWHGQGI PVIEPSVPEL VVKPGATVTL RCVGNGSVEW DGPPSPHWTL
YSDGSSSILS TNNATFQNTG TYRCTEPGDP LGGSAAIHLY VKDPARPWNV LAQEVVVFED
QDALLPCLLT DPVLEAGVSL VRVRGRPLMR HTNYSFSPWH GFTIHRAKFI QSQDYQCSAL
MGGRKVMSIS IRLKVQKVIP GPPALTLVPA ELVRIRGEAA QIVCSASSVD VNFDVFLQHN
NTKLAIPQQS DFHNNRYQKV LTLNLDQVDF QHAGNYSCVA SNVQGKHSTS MFFRVVESAY
LNLSSEQNLI QEVTVGEGLN LKVMVEAYPG LQGFNWTYLG PFSDHQPEPK LANATTKDTY
RHTFTLSLPR LKPSEAGRYS FLARNPGGWR ALTFELTLRY PPEVSVIWTF INGSGTLLCA
ASGYPQPNVT WLQCSGHTDR CDEAQVLQVW DDPYPEVLSQ EPFHKVTVQS LLTVETLEHN
QTYECRAHNS VGSGSWAFIP ISAGAHTHPP DEFLFTPVVV ACMSIMALLL LLLLLLLYKY
KQKPKYQVRW KIIESYEGNS YTFIDPTQLP YNEKWEFPRN NLQFGKTLGA GAFGKVVEAT
AFGLGKEDAV LKVAVKMLKS TAHADEKEAL MSELKIMSHL GQHENIVNLL GACTHGGPVL
VITEYCCYGD LLNFLRRKAE AMLGPSLSPG QDPEGGVDYK NIHLEKKYVR RDSGFSSQGV
DTYVEMRPVS TSSNDSFSEQ DLDKEDGRPL ELRDLLHFSS QVAQGMAFLA SKNCIHRDVA
ARNVLLTNGH VAKIGDFGLA RDIMNDSNYI VKGNARLPVK WMAPESIFDC VYTVQSDVWS
YGILLWEIFS LGLNPYPGIL VNSKFYKLVK DGYQMAQPAF APKNIYSIMQ ACWALEPTHR
PTFQQICSFL QEQAQEDRRE RDYTNLPSSS RSGGSGSSSS ELEEESSSEH LTCCEQGDIA
QPLLQPNNYQ FC


Related products :

Catalog number Product name Quantity
E1594m ELISA kit Csf1r,CSF-1-R,Csfmr,Fms,Macrophage colony-stimulating factor 1 receptor,Mouse,Mus musculus,Proto-oncogene c-Fms 96T
E1594r ELISA kit Csf1r,CSF-1-R,Csfmr,Fms,Macrophage colony-stimulating factor 1 receptor,Proto-oncogene c-Fms,Rat,Rattus norvegicus 96T
U1594h CLIA CSF1R,CSF-1-R,FMS,Homo sapiens,Human,Macrophage colony-stimulating factor 1 receptor,Proto-oncogene c-Fms 96T
U1594m CLIA Csf1r,CSF-1-R,Csfmr,Fms,Macrophage colony-stimulating factor 1 receptor,Mouse,Mus musculus,Proto-oncogene c-Fms 96T
U1594r CLIA Csf1r,CSF-1-R,Csfmr,Fms,Macrophage colony-stimulating factor 1 receptor,Proto-oncogene c-Fms,Rat,Rattus norvegicus 96T
E1594h ELISA kit CSF1R,CSF-1-R,FMS,Homo sapiens,Human,Macrophage colony-stimulating factor 1 receptor,Proto-oncogene c-Fms 96T
E1594r ELISA Csf1r,CSF-1-R,Csfmr,Fms,Macrophage colony-stimulating factor 1 receptor,Proto-oncogene c-Fms,Rat,Rattus norvegicus 96T
E1594m ELISA Csf1r,CSF-1-R,Csfmr,Fms,Macrophage colony-stimulating factor 1 receptor,Mouse,Mus musculus,Proto-oncogene c-Fms 96T
E1594h ELISA CSF1R,CSF-1-R,FMS,Homo sapiens,Human,Macrophage colony-stimulating factor 1 receptor,Proto-oncogene c-Fms 96T
YHB1936Hu Human Macrophage Colony-Stimulating Factor Receptor,M-CSFR-CD115 ELISA Kit 96T
YHB1936Hu Human Macrophage Colony-Stimulating Factor Receptor,M-CSFR-CD115 ELISA Kit 48T
UB-E02723 Human Macrophage Colony-Stimulating Factor Receptor(M-CSFR per CD115)ELISA Kit 96T
E0236Hu Human Macrophage Colony-Stimulating Factor Receptor,M-CSFR-CD115 ELISA Kit 48T
E0236Hu Human Macrophage Colony-Stimulating Factor Receptor,M-CSFR per CD115 ELISA Kit 48T
E0236Hu Human Macrophage Colony-Stimulating Factor Receptor,M-CSFR per CD115 ELISA Kit 96T
E0236Hu Human Macrophage Colony-Stimulating Factor Receptor,M-CSFR-CD115 ELISA Kit 96T
YHB0888Mo Mouse Macrophage Colony-Stimulating Factor Receptor,M-CSFR-CD115 ELISA Kit 48T
YHB0888Mo Mouse Macrophage Colony-Stimulating Factor Receptor,M-CSFR-CD115 ELISA Kit 96T
U0978r CLIA Epidermal growth factor receptor-related protein,Erbb2,Neu,p185erbB2,p185neu,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Rat,Rattus norvegicus,Receptor tyrosine-protein kinase erbB-2 96T
E0978r ELISA Epidermal growth factor receptor-related protein,Erbb2,Neu,p185erbB2,p185neu,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Rat,Rattus norvegicus,Receptor tyrosine-protein kinase erbB-2 96T
E0978r ELISA kit Epidermal growth factor receptor-related protein,Erbb2,Neu,p185erbB2,p185neu,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Rat,Rattus norvegicus,Receptor tyrosine-protein kinase erbB-2 96T
EH3341 Macrophage Colony Stimulating Factor Receptor Elisa Kit 96T
E02M0008 Rat Macrophage colony-stimulating factor receptor ELISA 96T/kit
E02M0008 Rat Macrophage colony-stimulating factor receptor Elisa Kit 96 Tests/kit
18-785-210280 Met (Ab-1349) - EC 2.7.10.1; HGF receptor; Scatter factor receptor; SF receptor; HGF_SF receptor; Met proto-oncogene tyrosine kinase; c-Met Polyclonal 0.1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur