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P07333 (CSF1R_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Macrophage colony-stimulating factor 1 receptor
Alternative name(s):
CSF-1 receptor
Short name=CSF-1-R
Short name=CSF-1R
Short name=M-CSF-R
EC=2.7.10.1
Proto-oncogene c-Fms
CD_antigen=CD115
Gene names
Name:CSF1R
Synonyms:FMS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length972 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.13 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28 Ref.29 Ref.30 Ref.32 Ref.38

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.20 Ref.21 Ref.22 Ref.37 Ref.38 Ref.39

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. Ref.20 Ref.21 Ref.22 Ref.24 Ref.27 Ref.28 Ref.39

Subunit structure

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. Ref.14 Ref.28

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in bone marrow and in differentiated blood mononuclear cells.

Induction

Up-regulated by glucocorticoids. Ref.15 Ref.20 Ref.21 Ref.22 Ref.24 Ref.27 Ref.28 Ref.39

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. Ref.35 Ref.36

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. Ref.35 Ref.36

Post-translational modification

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. Ref.20 Ref.21 Ref.27 Ref.28 Ref.30

Ubiquitinated. Becomes rapidly polyubiquitinated after autophosphorylation, leading to its degradation. Ref.22

Involvement in disease

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. Ref.18 Ref.20 Ref.21 Ref.24 Ref.25 Ref.32

Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection. Ref.18 Ref.20 Ref.21 Ref.24 Ref.25 Ref.32

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.20 Ref.21 Ref.24 Ref.25 Ref.32 Ref.41

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processImmunity
Inflammatory response
Innate immunity
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Proto-oncogene
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from mutant phenotype Ref.13. Source: UniProtKB

cell-cell junction maintenance

Inferred from mutant phenotype Ref.18. Source: UniProtKB

cellular response to cytokine stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to macrophage colony-stimulating factor stimulus

Inferred from mutant phenotype Ref.30Ref.13. Source: UniProtKB

cytokine-mediated signaling pathway

Inferred from mutant phenotype Ref.30. Source: UniProtKB

hemopoiesis

Inferred from mutant phenotype Ref.13. Source: UniProtKB

inflammatory response

Traceable author statement Ref.34. Source: UniProtKB

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

macrophage colony-stimulating factor signaling pathway

Inferred from mutant phenotype Ref.30Ref.13. Source: GOC

macrophage differentiation

Traceable author statement Ref.34. Source: UniProtKB

mammary gland duct morphogenesis

Traceable author statement Ref.18. Source: UniProtKB

monocyte differentiation

Traceable author statement Ref.34. Source: UniProtKB

multicellular organismal development

Traceable author statement PubMed 8981357. Source: ProtInc

osteoclast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.30. Source: UniProtKB

phosphatidylinositol metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell motility

Inferred from mutant phenotype Ref.18. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype Ref.18Ref.30. Source: UniProtKB

positive regulation of chemokine secretion

Inferred from mutant phenotype Ref.29. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from mutant phenotype Ref.30. Source: UniProtKB

positive regulation of protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein tyrosine kinase activity

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of tyrosine phosphorylation of Stat3 protein

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.30. Source: UniProtKB

regulation of actin cytoskeleton reorganization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of bone resorption

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell shape

Inferred from mutant phenotype Ref.18. Source: UniProtKB

ruffle organization

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Traceable author statement PubMed 8981357. Source: ProtInc

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell surface

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

plasma membrane

Traceable author statement Ref.2. Source: ProtInc

receptor complex

Inferred from sequence or structural similarity PubMed 19017797. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cytokine binding

Inferred from direct assay Ref.30. Source: UniProtKB

macrophage colony-stimulating factor receptor activity

Inferred from mutant phenotype Ref.30Ref.13. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity PubMed 19017797. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07333-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P07333-2)

The sequence of this isoform differs from the canonical sequence as follows:
     297-306: ESAYLNLSSE → GTPSPSLCPA
     307-972: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 972953Macrophage colony-stimulating factor 1 receptor
PRO_0000016765

Regions

Topological domain20 – 517498Extracellular Potential
Transmembrane518 – 53821Helical; Potential
Topological domain539 – 972434Cytoplasmic Potential
Domain21 – 10484Ig-like C2-type 1
Domain107 – 19791Ig-like C2-type 2
Domain203 – 29088Ig-like C2-type 3
Domain299 – 399101Ig-like C2-type 4
Domain402 – 502101Ig-like C2-type 5
Domain582 – 910329Protein kinase
Nucleotide binding588 – 5969ATP By similarity
Region542 – 57433Regulatory juxtamembrane domain
Region796 – 81823Activation loop

Sites

Active site7781Proton acceptor By similarity
Binding site6161ATP Probable

Amino acid modifications

Modified residue5461Phosphotyrosine; by autocatalysis Ref.28
Modified residue5611Phosphotyrosine; by autocatalysis By similarity
Modified residue6991Phosphotyrosine; by autocatalysis Ref.26 Ref.28
Modified residue7081Phosphotyrosine; by autocatalysis Ref.28
Modified residue7131Phosphoserine Ref.26
Modified residue7231Phosphotyrosine; by autocatalysis Ref.28 Ref.30
Modified residue8091Phosphotyrosine; by autocatalysis Ref.28
Modified residue9231Phosphotyrosine; by autocatalysis By similarity
Modified residue9691Phosphotyrosine; by autocatalysis By similarity
Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Ref.19
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Ref.19
Glycosylation4121N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 84 By similarity
Disulfide bond127 ↔ 177 By similarity
Disulfide bond224 ↔ 278 By similarity
Disulfide bond419 ↔ 485 By similarity

Natural variations

Alternative sequence297 – 30610ESAYLNLSSE → GTPSPSLCPA in isoform 2.
VSP_047757
Alternative sequence307 – 972666Missing in isoform 2.
VSP_047758
Natural variant321V → G. Ref.40
Corresponds to variant rs56048668 [ dbSNP | Ensembl ].
VAR_042038
Natural variant2451A → S.
Corresponds to variant rs41338945 [ dbSNP | Ensembl ].
VAR_061290
Natural variant2791V → M.
Corresponds to variant rs3829986 [ dbSNP | Ensembl ].
VAR_049718
Natural variant3621H → R. Ref.40
Corresponds to variant rs10079250 [ dbSNP | Ensembl ].
VAR_042039
Natural variant4131G → S. Ref.40
Corresponds to variant rs34951517 [ dbSNP | Ensembl ].
VAR_042040
Natural variant5361L → V. Ref.40
Corresponds to variant rs55942044 [ dbSNP | Ensembl ].
VAR_042041
Natural variant585 – 61935GKTLG…VKMLK → A in HDLS.
VAR_067396
Natural variant5891G → E in HDLS. Ref.41
VAR_067397
Natural variant6331E → K in HDLS; impairs autophosphorylation upon stimulation with CSF1. Ref.41
VAR_067398
Natural variant6931P → H in a lung squamous cell carcinoma sample; somatic mutation. Ref.40
VAR_042042
Natural variant7101R → H. Ref.41
VAR_067399
Natural variant7471G → R. Ref.41
Corresponds to variant rs41355444 [ dbSNP | Ensembl ].
VAR_067400
Natural variant7661M → T in HDLS; impairs autophosphorylation upon stimulation with CSF1. Ref.41
VAR_067401
Natural variant7701A → P in HDLS. Ref.41
VAR_067402
Natural variant774 – 81441Missing in HDLS.
VAR_067403
Natural variant7751I → N in HDLS; impairs autophosphorylation upon stimulation with CSF1. Ref.41
VAR_067404
Natural variant7941I → T in HDLS. Ref.41
VAR_067405
Natural variant8371D → Y in HDLS. Ref.41
VAR_067406
Natural variant8491F → S in HDLS. Ref.41
VAR_067407
Natural variant8491Missing in HDLS. Ref.41
VAR_067408
Natural variant8681L → P in HDLS. Ref.41
VAR_067409
Natural variant8751M → T in HDLS. Ref.41
VAR_067410
Natural variant8781P → T in HDLS. Ref.41
VAR_067411
Natural variant9201E → D. Ref.40 Ref.41
Corresponds to variant rs34030164 [ dbSNP | Ensembl ].
VAR_042043
Natural variant9211R → Q. Ref.40
Corresponds to variant rs56059682 [ dbSNP | Ensembl ].
VAR_042044
Natural variant9691Y → C.
Corresponds to variant rs1801271 [ dbSNP | Ensembl ].
VAR_011953

Experimental info

Mutagenesis3011L → S: Constitutive kinase activity. Ref.18
Mutagenesis7081Y → F: Impairs degradation of activated CSF1R. Ref.16
Mutagenesis8021D → V: Constitutive kinase activity. Loss of inhibition by imatinib. Ref.16 Ref.22
Mutagenesis8091Y → F: Reduced kinase activity. Reduced interaction with SRC, FYN and YES1. Ref.14
Mutagenesis9691Y → F: Abolishes down-regulation of activated CSF1R. Ref.18
Sequence conflict541P → A in CAA27300. Ref.2
Sequence conflict2471P → H in AAH47521. Ref.7
Sequence conflict3541A → V in AAH47521. Ref.7
Sequence conflict6291A → S in AAH47521. Ref.7

Secondary structure

........................................................................................................... 972
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 1994. Version 2.
Checksum: A8D99BE237573FE8

FASTA972107,984
        10         20         30         40         50         60 
MGPGVLLLLL VATAWHGQGI PVIEPSVPEL VVKPGATVTL RCVGNGSVEW DGPPSPHWTL 

        70         80         90        100        110        120 
YSDGSSSILS TNNATFQNTG TYRCTEPGDP LGGSAAIHLY VKDPARPWNV LAQEVVVFED 

       130        140        150        160        170        180 
QDALLPCLLT DPVLEAGVSL VRVRGRPLMR HTNYSFSPWH GFTIHRAKFI QSQDYQCSAL 

       190        200        210        220        230        240 
MGGRKVMSIS IRLKVQKVIP GPPALTLVPA ELVRIRGEAA QIVCSASSVD VNFDVFLQHN 

       250        260        270        280        290        300 
NTKLAIPQQS DFHNNRYQKV LTLNLDQVDF QHAGNYSCVA SNVQGKHSTS MFFRVVESAY 

       310        320        330        340        350        360 
LNLSSEQNLI QEVTVGEGLN LKVMVEAYPG LQGFNWTYLG PFSDHQPEPK LANATTKDTY 

       370        380        390        400        410        420 
RHTFTLSLPR LKPSEAGRYS FLARNPGGWR ALTFELTLRY PPEVSVIWTF INGSGTLLCA 

       430        440        450        460        470        480 
ASGYPQPNVT WLQCSGHTDR CDEAQVLQVW DDPYPEVLSQ EPFHKVTVQS LLTVETLEHN 

       490        500        510        520        530        540 
QTYECRAHNS VGSGSWAFIP ISAGAHTHPP DEFLFTPVVV ACMSIMALLL LLLLLLLYKY 

       550        560        570        580        590        600 
KQKPKYQVRW KIIESYEGNS YTFIDPTQLP YNEKWEFPRN NLQFGKTLGA GAFGKVVEAT 

       610        620        630        640        650        660 
AFGLGKEDAV LKVAVKMLKS TAHADEKEAL MSELKIMSHL GQHENIVNLL GACTHGGPVL 

       670        680        690        700        710        720 
VITEYCCYGD LLNFLRRKAE AMLGPSLSPG QDPEGGVDYK NIHLEKKYVR RDSGFSSQGV 

       730        740        750        760        770        780 
DTYVEMRPVS TSSNDSFSEQ DLDKEDGRPL ELRDLLHFSS QVAQGMAFLA SKNCIHRDVA 

       790        800        810        820        830        840 
ARNVLLTNGH VAKIGDFGLA RDIMNDSNYI VKGNARLPVK WMAPESIFDC VYTVQSDVWS 

       850        860        870        880        890        900 
YGILLWEIFS LGLNPYPGIL VNSKFYKLVK DGYQMAQPAF APKNIYSIMQ ACWALEPTHR 

       910        920        930        940        950        960 
PTFQQICSFL QEQAQEDRRE RDYTNLPSSS RSGGSGSSSS ELEEESSSEH LTCCEQGDIA 

       970 
QPLLQPNNYQ FC 

« Hide

Isoform 2 [UniParc].

Checksum: DDAEA1B05EAAF3C2
Show »

FASTA30633,248

References

« Hide 'large scale' references
[1]"Nucleotide sequence and structural organization of the human FMS proto-oncogene."
Hampe A., Shamoon B.M., Gobet M., Sherr C.J., Galibert F.
Oncogene Res. 4:9-17(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural alteration of viral homologue of receptor proto-oncogene fms at carboxyl terminus."
Coussens L., van Beveren C., Smith D., Chen E., Mitchell R.L., Isacke C.M., Verma I.M., Ullrich A.
Nature 320:277-280(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Sequence analysis of two genomic regions containing the KIT and the FMS receptor tyrosine kinase genes."
Andre C., Hampe A., Lachaume P., Martin E., Wang X.P., Manus V., Hu W.X., Galibert F.
Genomics 39:216-226(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[4]"Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]"The DNA sequence and comparative analysis of human chromosome 5."
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. expand/collapse author list , 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.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[8]"Differential transcription of exon 1 of the human c-fms gene in placental trophoblasts and monocytes."
Visvader J., Verma I.M.
Mol. Cell. Biol. 9:1336-1341(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[9]"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."
Wheeler E.F., Roussel M.F., Hampe A., Walker M.H., Fried V.A., Look A.T., Rettenmier C.W., Sherr C.J.
J. Virol. 59:224-233(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[10]"Expression of a novel exon in the 5' UTR of human c-fms transcripts."
Flick M.B., Sapi E., Kacinski B.M.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
Tissue: Placenta.
[11]"Expression of the human c-fms proto-oncogene in hematopoietic cells and its deletion in the 5q- syndrome."
Nienhuis A.W., Bunn H.F., Turner P.H., Gopal T.V., Nash W.G., O'Brien S.J., Sherr C.J.
Cell 42:421-428(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-295.
[12]"'Replacement' of COOH-terminal truncation of v-fms with c-fms sequences markedly reduces transformation potential."
Browning P.J., Bunn H.F., Cline A., Shuman M., Nienhuis A.W.
Proc. Natl. Acad. Sci. U.S.A. 83:7800-7804(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 874-972 (ISOFORM 1).
[13]"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."
Bourette R.P., Mouchiroud G., Ouazana R., Morle F., Godet J., Blanchet J.P.
Blood 81:2511-2520(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION.
[14]"Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor."
Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D., Roussel M.F.
EMBO J. 12:943-950(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRC; FYN AND YES1, MUTAGENESIS OF TYR-809.
[15]"Transcriptional regulation of the c-fms (CSF-1R) proto-oncogene in human breast carcinoma cells by glucocorticoids."
Sapi E., Flick M.B., Gilmore-Hebert M., Rodov S., Kacinski B.M.
Oncogene 10:529-542(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY GLUCOCORTICOIDS.
[16]"Cell specific transformation by c-fms activating loop mutations is attributable to constitutive receptor degradation."
Morley G.M., Uden M., Gullick W.J., Dibb N.J.
Oncogene 18:3076-3084(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-708 AND ASP-802.
[17]"The inositol 5'-phosphatase SHIP-1 and the Src kinase Lyn negatively regulate macrophage colony-stimulating factor-induced Akt activity."
Baran C.P., Tridandapani S., Helgason C.D., Humphries R.K., Krystal G., Marsh C.B.
J. Biol. Chem. 278:38628-38636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELLULAR SIGNALING; PHOSPHORYLATION OF INPP5D AND ACTIVATION OF AKT1.
[18]"Autocrine CSF-1R activation promotes Src-dependent disruption of mammary epithelial architecture."
Wrobel C.N., Debnath J., Lin E., Beausoleil S., Roussel M.F., Brugge J.S.
J. Cell Biol. 165:263-273(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF CELL PROLIFERATION; CELL ADHESION; CELL SHAPE AND INTEGRITY OF CELL JUNCTIONS, MUTAGENESIS OF LEU-301 AND TYR-969, ROLE IN DISEASE.
[19]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-302 AND ASN-353.
Tissue: Plasma.
[20]"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."
Guo J., Marcotte P.A., McCall J.O., Dai Y., Pease L.J., Michaelides M.R., Davidsen S.K., Glaser K.B.
Mol. Cancer Ther. 5:1007-1013(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CSF1 RECEPTOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ROLE IN DISEASE, ENZYME REGULATION.
[21]"A c-fms tyrosine kinase inhibitor, Ki20227, suppresses osteoclast differentiation and osteolytic bone destruction in a bone metastasis model."
Ohno H., Kubo K., Murooka H., Kobayashi Y., Nishitoba T., Shibuya M., Yoneda T., Isoe T.
Mol. Cancer Ther. 5:2634-2643(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ROLE IN DISEASE, ENZYME REGULATION.
[22]"FMS receptor for M-CSF (CSF-1) is sensitive to the kinase inhibitor imatinib and mutation of Asp-802 to Val confers resistance."
Taylor J.R., Brownlow N., Domin J., Dibb N.J.
Oncogene 25:147-151(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF CELL PROLIFERATION AND CELL SHAPE, CATALYTIC ACTIVITY, UBIQUITINATION, ENZYME REGULATION, MUTAGENESIS OF ASP-802.
[23]"Discovery of a cytokine and its receptor by functional screening of the extracellular proteome."
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.
Science 320:807-811(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS IL34 RECEPTOR.
[24]"Imatinib mesylate suppresses bone metastases of breast cancer by inhibiting osteoclasts through the blockade of c-Fms signals."
Hiraga T., Nakamura H.
Int. J. Cancer 124:215-222(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN DISEASE, ENZYME REGULATION.
[25]"Invasion of human breast cancer cells in vivo requires both paracrine and autocrine loops involving the colony-stimulating factor-1 receptor."
Patsialou A., Wyckoff J., Wang Y., Goswami S., Stanley E.R., Condeelis J.S.
Cancer Res. 69:9498-9506(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN DISEASE.
[26]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-699 AND SER-713, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Colony stimulating factor-1 receptor as a target for small molecule inhibitors."
Mashkani B., Griffith R., Ashman L.K.
Bioorg. Med. Chem. 18:1789-1797(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION, ENZYME REGULATION.
[28]"IL-34 and M-CSF share the receptor Fms but are not identical in biological activity and signal activation."
Chihara T., Suzu S., Hassan R., Chutiwitoonchai N., Hiyoshi M., Motoyoshi K., Kimura F., Okada S.
Cell Death Differ. 17:1917-1927(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS RECEPTOR FOR IL34 AND CSF1, PHOSPHORYLATION AT TYR-546; TYR-699; TYR-708; TYR-723 AND TYR-809, AUTOPHOSPHORYLATION, ENZYME REGULATION, INTERACTION WITH IL34 AND CSF1.
[29]"Macrophage-colony stimulating factor and interleukin-34 induce chemokines in human whole blood."
Eda H., Zhang J., Keith R.H., Michener M., Beidler D.R., Monahan J.B.
Cytokine 52:215-220(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RELEASE OF PROINFLAMMATORY CHEMOKINES.
[30]"Functional overlap but differential expression of CSF-1 and IL-34 in their CSF-1 receptor-mediated regulation of myeloid cells."
Wei S., Nandi S., Chitu V., Yeung Y.G., Yu W., Huang M., Williams L.T., Lin H., Stanley E.R.
J. Leukoc. Biol. 88:495-505(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS IL34 AND CSF1 RECEPTOR; ACTIVATION OF MAPK1/ERK2; MAPK3/ERK1; PHOSPHORYLATION AT TYR-723, AUTOPHOSPHORYLATION.
[31]"CSF-1 regulation of the wandering macrophage: complexity in action."
Pixley F.J., Stanley E.R.
Trends Cell Biol. 14:628-638(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION; SIGNALING PATHWAYS AND PHOSPHORYLATION.
[32]"Colony-stimulating factor-1 in immunity and inflammation."
Chitu V., Stanley E.R.
Curr. Opin. Immunol. 18:39-48(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN IMMUNITY AND INFLAMMATION, ROLE IN DISEASE.
[33]"Macrophage colony stimulating factor: not just for macrophages anymore! A gateway into complex biologies."
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.
Int. Immunopharmacol. 8:1354-1376(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION; SIGNALING PATHWAYS AND PHOSPHORYLATION.
[34]"Blood monocytes: development, heterogeneity, and relationship with dendritic cells."
Auffray C., Sieweke M.H., Geissmann F.
Annu. Rev. Immunol. 27:669-692(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[35]"Crystal structure of the tyrosine kinase domain of colony-stimulating factor-1 receptor (cFMS) in complex with two inhibitors."
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.
J. Biol. Chem. 282:4094-4101(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 538-922 IN COMPLEXES WITH ARYLAMIDE AND QUINOLONE INHIBITORS, DOMAIN.
[36]"The 2.7 A crystal structure of the autoinhibited human c-Fms kinase domain."
Walter M., Lucet I.S., Patel O., Broughton S.E., Bamert R., Williams N.K., Fantino E., Wilks A.F., Rossjohn J.
J. Mol. Biol. 367:839-847(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 543-918 IN AUTOINHIBITED CONFORMATION, DOMAIN.
[37]"Design and synthesis of a pyrido[2,3-d]pyrimidin-5-one class of anti-inflammatory FMS inhibitors."
Huang H., Hutta D.A., Hu H., DesJarlais R.L., Schubert C., Petrounia I.P., Chaikin M.A., Manthey C.L., Player M.R.
Bioorg. Med. Chem. Lett. 18:2355-2361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 538-922 IN COMPLEX WITH PYRIMIDINOPYRIDONE INHIBITOR, CATALYTIC ACTIVITY.
[38]"Pyrido[2,3-d]pyrimidin-5-ones: a novel class of antiinflammatory macrophage colony-stimulating factor-1 receptor inhibitors."
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.
J. Med. Chem. 52:1081-1099(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 538-922 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY, FUNCTION IN INFLAMMATION AND DISEASE.
[39]"Structure-based drug design enables conversion of a DFG-in binding CSF-1R kinase inhibitor to a DFG-out binding mode."
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.
Bioorg. Med. Chem. Lett. 20:1543-1547(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 538-922 IN COMPLEXES WITH INHIBITORS, CATALYTIC ACTIVITY, ENZYME REGULATION.
[40]"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. expand/collapse author list , 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] GLY-32; ARG-362; SER-413; VAL-536; HIS-693; ASP-920 AND GLN-921.
[41]"Mutations in the colony stimulating factor 1 receptor (CSF1R) gene cause hereditary diffuse leukoencephalopathy with spheroids."
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. expand/collapse author list , 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.
Nat. Genet. 44:200-205(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, CHARACTERIZATION OF VARIANTS HDLS LYS-633; THR-766 AND THR-875.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03663 mRNA. Translation: CAA27300.1.
U63963 Genomic DNA. Translation: AAB51696.1.
M25786 mRNA. Translation: AAA58421.1.
EU826593 mRNA. Translation: ACF47629.1.
AC011382 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61749.1.
CH471062 Genomic DNA. Translation: EAW61750.1.
BC047521 mRNA. Translation: AAH47521.1.
M14002 Genomic DNA. Translation: AAA35849.1.
U78096 Genomic DNA. Translation: AAB51235.1.
M11067 Genomic DNA. Translation: AAA35848.1.
M14193 mRNA. Translation: AAA35834.1.
CCDSCCDS4302.1. [P07333-1]
PIRTVHUMD. S08123.
RefSeqNP_001275634.1. NM_001288705.1. [P07333-1]
NP_005202.2. NM_005211.3. [P07333-1]
UniGeneHs.586219.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I0VX-ray2.80A538-678[»]
A753-922[»]
2I0YX-ray1.90A538-678[»]
A753-922[»]
2I1MX-ray1.80A538-678[»]
A753-922[»]
2OGVX-ray2.70A543-918[»]
3BEAX-ray2.02A538-678[»]
A753-922[»]
3DPKX-ray1.95A183-334[»]
A538-678[»]
3KRJX-ray2.10A538-678[»]
A753-922[»]
3KRLX-ray2.40A538-678[»]
A753-922[»]
3LCDX-ray2.50A538-919[»]
3LCOX-ray3.40A550-919[»]
4DKDX-ray3.00C20-299[»]
4HW7X-ray2.90A542-919[»]
ProteinModelPortalP07333.
SMRP07333. Positions 20-498, 544-945.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107823. 18 interactions.
DIPDIP-59421N.
IntActP07333. 9 interactions.
MINTMINT-8019993.
STRING9606.ENSP00000286301.

Chemistry

BindingDBP07333.
ChEMBLCHEMBL1844.
DrugBankDB00619. Imatinib.
DB01268. Sunitinib.
GuidetoPHARMACOLOGY1806.

PTM databases

PhosphoSiteP07333.

Polymorphism databases

DMDM547770.

Proteomic databases

PaxDbP07333.
PeptideAtlasP07333.
PRIDEP07333.

Protocols and materials databases

DNASU1436.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286301; ENSP00000286301; ENSG00000182578. [P07333-1]
ENST00000543093; ENSP00000445282; ENSG00000182578. [P07333-2]
GeneID1436.
KEGGhsa:1436.
UCSCuc003lrl.3. human. [P07333-1]

Organism-specific databases

CTD1436.
GeneCardsGC05M149413.
GeneReviewsCSF1R.
HGNCHGNC:2433. CSF1R.
HPACAB008970.
HPA012323.
MIM164770. gene.
221820. phenotype.
neXtProtNX_P07333.
Orphanet313808. Adult-onset leukoencephalopathy with axonal spheroids and pigmented glia.
PharmGKBPA26936.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000112008.
HOVERGENHBG004335.
InParanoidP07333.
KOK05090.
OMAVECVAFN.
PhylomeDBP07333.
TreeFamTF325768.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkP07333.

Gene expression databases

ArrayExpressP07333.
BgeeP07333.
CleanExHS_CSF1R.
GenevestigatorP07333.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]
PfamPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF500947. CSF-1_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTSM00409. IG. 3 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCSF1R. human.
EvolutionaryTraceP07333.
GeneWikiColony_stimulating_factor_1_receptor.
GenomeRNAi1436.
NextBio35477774.
PROP07333.
SOURCESearch...

Entry information

Entry nameCSF1R_HUMAN
AccessionPrimary (citable) accession number: P07333
Secondary accession number(s): B5A955 expand/collapse secondary AC list , D3DQG2, Q6LDW5, Q6LDY4, Q86VW7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 172 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries