CSF1R

Functionⁱ

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.14 Publications

Catalytic activityⁱ

ATP
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
L-tyrosyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
ADP
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O-phospho-L-tyrosyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10028
6 Publications
Manual assertion based on experiment inⁱ
- Ref.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, ACTIVITY REGULATION.
- Ref.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, ACTIVITY REGULATION.
- Ref.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, ACTIVITY REGULATION, MUTAGENESIS OF ASP-802.
- Ref.38
  "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.
- Ref.39
  "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.
- Ref.40
  "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, ACTIVITY REGULATION.
EC:
2.7.10.1
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10028
6 Publications
Manual assertion based on experiment inⁱ
- Ref.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, ACTIVITY REGULATION.
- Ref.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, ACTIVITY REGULATION.
- Ref.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, ACTIVITY REGULATION, MUTAGENESIS OF ASP-802.
- Ref.38
  "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.
- Ref.39
  "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.
- Ref.40
  "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, ACTIVITY REGULATION.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
ATP
+
L-tyrosyl-[protein]
L-tyrosine residue
zoom
=
ADP
+
H⁺
+
O-phospho-L-tyrosyl-[protein]
L-tyrosine-phosphate residue
zoom

Activity regulationⁱ

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 GW2580.7 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	616	ATPCurated		1
Active siteⁱ	778	Proton acceptorPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	588 – 596	ATPPROSITE-ProRule annotation		9

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Receptor, Transferase, Tyrosine-protein kinase
Biological process	Immunity, Inflammatory response, Innate immunity
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	2.7.10.1 2681
Reactomeⁱ	R-HSA-449836 Other interleukin signaling
SignaLinkⁱ	P07333
SIGNORⁱ	P07333

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Macrophage colony-stimulating factor 1 receptor Alternative name(s): CSF-1 receptor (EC:2.7.10.1) Short name: CSF-1-R Short name: CSF-1R Short name: M-CSF-R Proto-oncogene c-Fms CD_antigen: CD115
Gene namesⁱ	Name:CSF1R Synonyms:FMS
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 5

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000182578.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:2433 CSF1R
MIMⁱ	164770 gene
neXtProtⁱ	NX_P07333

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	20 – 517	ExtracellularSequence analysisAdd BLAST	498
Transmembraneⁱ	518 – 538	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	539 – 972	CytoplasmicSequence analysisAdd BLAST	434

Keywords - Cellular componentⁱ

Cell membrane, Membrane

Pathology & Biotechⁱ

Involvement in diseaseⁱ

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.

Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.

Leukoencephalopathy, diffuse hereditary, with spheroids (HDLS)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_067396	585 – 619	GKTLG…VKMLK → A in HDLS. 1 PublicationAdd BLAST	35
Natural variantⁱVAR_067397	589	G → E in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860268EnsemblClinVar.	1
Natural variantⁱVAR_067398	633	E → K in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860269EnsemblClinVar.	1
Natural variantⁱVAR_072081	653	C → R in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016559EnsemblClinVar.	1
Natural variantⁱVAR_067401	766	M → T in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860270EnsemblClinVar.	1
Natural variantⁱVAR_067402	770	A → P in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860271EnsemblClinVar.	1
Natural variantⁱVAR_067403	774 – 814	Missing in HDLS. 1 PublicationAdd BLAST	41
Natural variantⁱVAR_067404	775	I → N in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860273EnsemblClinVar.	1
Natural variantⁱVAR_067405	794	I → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860274EnsemblClinVar.	1
Natural variantⁱVAR_067406	837	D → Y in HDLS. 1 PublicationCorresponds to variant dbSNP:rs387906662EnsemblClinVar.	1
Natural variantⁱVAR_072082	843	I → F in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016558EnsemblClinVar.	1
Natural variantⁱVAR_067407	849	F → S in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860277EnsemblClinVar.	1
Natural variantⁱVAR_067408	849	Missing in HDLS. 1 Publication	1
Natural variantⁱVAR_067409	868	L → P in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860278EnsemblClinVar.	1
Natural variantⁱVAR_067410	875	M → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860279EnsemblClinVar.	1
Natural variantⁱVAR_067411	878	P → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860280EnsemblClinVar.	1
Natural variantⁱVAR_072083	906	I → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016560EnsemblClinVar.	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	301	L → S: Constitutive kinase activity. 1 Publication	1
Mutagenesisⁱ	708	Y → F: Impairs degradation of activated CSF1R. 1 Publication	1
Mutagenesisⁱ	802	D → V: Constitutive kinase activity. Loss of inhibition by imatinib. 2 Publications	1
Mutagenesisⁱ	809	Y → F: Reduced kinase activity. Reduced interaction with SRC, FYN and YES1. 1 Publication	1
Mutagenesisⁱ	969	Y → F: Abolishes down-regulation of activated CSF1R. 1 Publication	1

Keywords - Diseaseⁱ

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNET More...DisGeNETⁱ	1436
GeneReviewsⁱ	CSF1R
MalaCards human disease database More...MalaCardsⁱ	CSF1R
MIMⁱ	221820 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000182578
Orphanetⁱ	313808 Hereditary diffuse leukoencephalopathy with axonal spheroids and pigmented glia
PharmGKBⁱ	PA26936

Miscellaneous databases

Pharosⁱ	P07333 Tclin

Pharosⁱ

P07333 Tclin

Chemistry databases

ChEMBLⁱ	CHEMBL1844
Drug and drug target database More...DrugBankⁱ	DB07167 5-CYANO-FURAN-2-CARBOXYLIC ACID [5-HYDROXYMETHYL-2-(4-METHYL-PIPERIDIN-1-YL)-PHENYL]-AMIDE DB07202 6-CHLORO-3-(3-METHYLISOXAZOL-5-YL)-4-PHENYLQUINOLIN-2(1H)-ONE DB06080 ABT-869 DB12147 Erdafitinib DB12010 Fostamatinib DB00619 Imatinib DB01268 Sunitinib
DrugCentral More...DrugCentralⁱ	P07333
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	1806

Polymorphism and mutation databases

BioMutaⁱ	CSF1R
DMDMⁱ	547770

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 19	Sequence analysisAdd BLAST		19
ChainⁱPRO_0000016765	20 – 972	Macrophage colony-stimulating factor 1 receptorAdd BLAST		953

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	42 ↔ 84	PROSITE-ProRule annotation
Glycosylationⁱ	45	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	73	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	127 ↔ 177	PROSITE-ProRule annotation
Glycosylationⁱ	153	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	224 ↔ 278	PROSITE-ProRule annotation
Glycosylationⁱ	240	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	275	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	302	N-linked (GlcNAc...) asparagine1 Publication	1
Glycosylationⁱ	335	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	353	N-linked (GlcNAc...) asparagine1 Publication	1
Glycosylationⁱ	412	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	419 ↔ 485	PROSITE-ProRule annotation
Glycosylationⁱ	428	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	480	N-linked (GlcNAc...) asparagineSequence analysis	1
Modified residueⁱ	546	Phosphotyrosine; by autocatalysis1 Publication	1
Modified residueⁱ	561	Phosphotyrosine; by autocatalysisBy similarity	1
Modified residueⁱ	699	Phosphotyrosine; by autocatalysisCombined sources1 Publication	1
Modified residueⁱ	708	Phosphotyrosine; by autocatalysis1 Publication	1
Modified residueⁱ	713	PhosphoserineCombined sources	1
Modified residueⁱ	723	Phosphotyrosine; by autocatalysis1 Publication	1
Modified residueⁱ	809	Phosphotyrosine; by autocatalysis1 Publication	1
Modified residueⁱ	923	Phosphotyrosine; by autocatalysisBy similarity	1
Modified residueⁱ	969	Phosphotyrosine; by autocatalysisBy similarity	1

Post-translational modificationⁱ

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.2 Publications

Ubiquitinated. Becomes rapidly polyubiquitinated after autophosphorylation, leading to its degradation.1 Publication

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P07333
jPOSTⁱ	P07333
MassIVEⁱ	P07333
PaxDbⁱ	P07333
PeptideAtlas More...PeptideAtlasⁱ	P07333
PRIDEⁱ	P07333
ProteomicsDBⁱ	51993 [P07333-1] 5930

PTM databases

GlyConnectⁱ	1955
iPTMnetⁱ	P07333
PhosphoSitePlusⁱ	P07333

Expressionⁱ

Tissue specificityⁱ

Expressed in bone marrow and in differentiated blood mononuclear cells.

Inductionⁱ

Up-regulated by glucocorticoids.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000182578 Expressed in 202 organ(s), highest expression level in spleen
ExpressionAtlasⁱ	P07333 baseline and differential
Genevisibleⁱ	P07333 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB008970 HPA012323

HPAⁱ

CAB008970
HPA012323

Interactionⁱ

Subunit structureⁱ

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.

By similarity4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	P09603	13	EBI-2835440,EBI-2872294
	Q6ZMJ4-1	9	EBI-2835440,EBI-15978980

Show more details

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	107823, 30 interactors
Database of interacting proteins More...DIPⁱ	DIP-59421N
IntActⁱ	P07333, 17 interactors
Molecular INTeraction database More...MINTⁱ	P07333
STRINGⁱ	9606.ENSP00000286301

Chemistry databases

BindingDBⁱ

P07333

Miscellaneous databases

RNActⁱ	P07333 protein

RNActⁱ

P07333 protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	22 – 25	Combined sources	4
Beta strandⁱ	27 – 32	Combined sources	6
Beta strandⁱ	38 – 43	Combined sources	6
Beta strandⁱ	49 – 51	Combined sources	3
Turnⁱ	55 – 57	Combined sources	3
Beta strandⁱ	58 – 62	Combined sources	5
Beta strandⁱ	64 – 73	Combined sources	10
Helixⁱ	76 – 78	Combined sources	3
Beta strandⁱ	80 – 85	Combined sources	6
Beta strandⁱ	95 – 101	Combined sources	7
Beta strandⁱ	108 – 111	Combined sources	4
Beta strandⁱ	113 – 118	Combined sources	6
Beta strandⁱ	123 – 125	Combined sources	3
Beta strandⁱ	127 – 130	Combined sources	4
Helixⁱ	132 – 137	Combined sources	6
Beta strandⁱ	139 – 142	Combined sources	4
Helixⁱ	143 – 145	Combined sources	3
Beta strandⁱ	154 – 157	Combined sources	4
Turnⁱ	158 – 160	Combined sources	3
Beta strandⁱ	161 – 166	Combined sources	6
Helixⁱ	169 – 171	Combined sources	3
Beta strandⁱ	173 – 181	Combined sources	9
Beta strandⁱ	184 – 187	Combined sources	4
Beta strandⁱ	191 – 196	Combined sources	6
Beta strandⁱ	204 – 208	Combined sources	5
Beta strandⁱ	210 – 215	Combined sources	6
Beta strandⁱ	216 – 218	Combined sources	3
Beta strandⁱ	220 – 231	Combined sources	12
Beta strandⁱ	234 – 239	Combined sources	6
Beta strandⁱ	248 – 252	Combined sources	5
Beta strandⁱ	257 – 267	Combined sources	11
Turnⁱ	270 – 272	Combined sources	3
Beta strandⁱ	274 – 282	Combined sources	9
Beta strandⁱ	285 – 298	Combined sources	14
Beta strandⁱ	300 – 304	Combined sources	5
Beta strandⁱ	309 – 314	Combined sources	6
Beta strandⁱ	319 – 329	Combined sources	11
Beta strandⁱ	332 – 338	Combined sources	7
Beta strandⁱ	340 – 342	Combined sources	3
Beta strandⁱ	351 – 354	Combined sources	4
Beta strandⁱ	361 – 368	Combined sources	8
Helixⁱ	373 – 375	Combined sources	3
Beta strandⁱ	377 – 385	Combined sources	9
Beta strandⁱ	388 – 411	Combined sources	24
Beta strandⁱ	414 – 425	Combined sources	12
Beta strandⁱ	428 – 437	Combined sources	10
Turnⁱ	443 – 445	Combined sources	3
Beta strandⁱ	446 – 454	Combined sources	9
Beta strandⁱ	456 – 459	Combined sources	4
Beta strandⁱ	466 – 473	Combined sources	8
Beta strandⁱ	479 – 488	Combined sources	10
Beta strandⁱ	493 – 498	Combined sources	6
Beta strandⁱ	551 – 553	Combined sources	3
Beta strandⁱ	556 – 560	Combined sources	5
Helixⁱ	566 – 568	Combined sources	3
Helixⁱ	573 – 575	Combined sources	3
Beta strandⁱ	581 – 590	Combined sources	10
Beta strandⁱ	592 – 601	Combined sources	10
Beta strandⁱ	605 – 607	Combined sources	3
Beta strandⁱ	612 – 618	Combined sources	7
Helixⁱ	624 – 640	Combined sources	17
Beta strandⁱ	649 – 653	Combined sources	5
Beta strandⁱ	655 – 658	Combined sources	4
Beta strandⁱ	660 – 664	Combined sources	5
Helixⁱ	671 – 682	Combined sources	12
Turnⁱ	684 – 686	Combined sources	3
Turnⁱ	742 – 744	Combined sources	3
Helixⁱ	753 – 771	Combined sources	19
Helixⁱ	781 – 783	Combined sources	3
Beta strandⁱ	785 – 787	Combined sources	3
Helixⁱ	788 – 790	Combined sources	3
Beta strandⁱ	791 – 794	Combined sources	4
Helixⁱ	798 – 800	Combined sources	3
Helixⁱ	803 – 805	Combined sources	3
Turnⁱ	806 – 808	Combined sources	3
Beta strandⁱ	809 – 811	Combined sources	3
Beta strandⁱ	815 – 817	Combined sources	3
Helixⁱ	819 – 821	Combined sources	3
Helixⁱ	824 – 829	Combined sources	6
Helixⁱ	834 – 848	Combined sources	15
Turnⁱ	849 – 851	Combined sources	3
Helixⁱ	863 – 871	Combined sources	9
Helixⁱ	883 – 892	Combined sources	10
Helixⁱ	897 – 899	Combined sources	3
Helixⁱ	903 – 920	Combined sources	18

Show more details

3D structure databases

SMRⁱ	P07333
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P07333

EvolutionaryTraceⁱ

P07333

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	21 – 104	Ig-like C2-type 1Add BLAST	84
Domainⁱ	107 – 197	Ig-like C2-type 2Add BLAST	91
Domainⁱ	203 – 290	Ig-like C2-type 3Add BLAST	88
Domainⁱ	299 – 399	Ig-like C2-type 4Add BLAST	101
Domainⁱ	402 – 502	Ig-like C2-type 5Add BLAST	101
Domainⁱ	582 – 910	Protein kinasePROSITE-ProRule annotationAdd BLAST	329

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	542 – 574	Regulatory juxtamembrane domainAdd BLAST		33
Regionⁱ	796 – 818	Activation loopAdd BLAST		23

Domainⁱ

The juxtamembrane domain functions as autoinhibitory region. Phosphorylation of tyrosine residues in this region leads to a conformation change and activation of the kinase.

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.

Sequence similaritiesⁱ

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

Keywords - Domainⁱ

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG0200 Eukaryota COG0515 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000155506
HOGENOMⁱ	HOG000112008
InParanoidⁱ	P07333
KEGG Orthology (KO) More...KOⁱ	K05090
OMAⁱ	TFQQICF
Database of Orthologous Groups More...OrthoDBⁱ	592753at2759
PhylomeDBⁱ	P07333
TreeFamⁱ	TF325768

Family and domain databases

Gene3Dⁱ	2.60.40.10, 5 hits
InterProⁱ	View protein in InterPro IPR030658 CSF-1_receptor IPR007110 Ig-like_dom IPR036179 Ig-like_dom_sf IPR013783 Ig-like_fold IPR003599 Ig_sub IPR003598 Ig_sub2 IPR013151 Immunoglobulin IPR011009 Kinase-like_dom_sf 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 IPR001824 Tyr_kinase_rcpt_3_CS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00047 ig, 1 hit PF07714 Pkinase_Tyr, 1 hit
PIRSFⁱ	PIRSF500947 CSF-1_receptor, 1 hit
SMARTⁱ	View protein in SMART SM00409 IG, 5 hits SM00408 IGc2, 2 hits SM00219 TyrKc, 1 hit
SUPFAMⁱ	SSF48726 SSF48726, 5 hits SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS50835 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

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P07333-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGPGVLLLLL VATAWHGQGI PVIEPSVPEL VVKPGATVTL RCVGNGSVEW 
        60         70         80         90        100
DGPPSPHWTL YSDGSSSILS TNNATFQNTG TYRCTEPGDP LGGSAAIHLY 
       110        120        130        140        150
VKDPARPWNV LAQEVVVFED QDALLPCLLT DPVLEAGVSL VRVRGRPLMR 
       160        170        180        190        200
HTNYSFSPWH GFTIHRAKFI QSQDYQCSAL MGGRKVMSIS IRLKVQKVIP 
       210        220        230        240        250
GPPALTLVPA ELVRIRGEAA QIVCSASSVD VNFDVFLQHN NTKLAIPQQS 
       260        270        280        290        300
DFHNNRYQKV LTLNLDQVDF QHAGNYSCVA SNVQGKHSTS MFFRVVESAY 
       310        320        330        340        350
LNLSSEQNLI QEVTVGEGLN LKVMVEAYPG LQGFNWTYLG PFSDHQPEPK 
       360        370        380        390        400
LANATTKDTY RHTFTLSLPR LKPSEAGRYS FLARNPGGWR ALTFELTLRY 
       410        420        430        440        450
PPEVSVIWTF INGSGTLLCA ASGYPQPNVT WLQCSGHTDR CDEAQVLQVW 
       460        470        480        490        500
DDPYPEVLSQ EPFHKVTVQS LLTVETLEHN QTYECRAHNS VGSGSWAFIP 
       510        520        530        540        550
ISAGAHTHPP DEFLFTPVVV ACMSIMALLL LLLLLLLYKY KQKPKYQVRW 
       560        570        580        590        600
KIIESYEGNS YTFIDPTQLP YNEKWEFPRN NLQFGKTLGA GAFGKVVEAT 
       610        620        630        640        650
AFGLGKEDAV LKVAVKMLKS TAHADEKEAL MSELKIMSHL GQHENIVNLL 
       660        670        680        690        700
GACTHGGPVL VITEYCCYGD LLNFLRRKAE AMLGPSLSPG QDPEGGVDYK 
       710        720        730        740        750
NIHLEKKYVR RDSGFSSQGV DTYVEMRPVS TSSNDSFSEQ DLDKEDGRPL 
       760        770        780        790        800
ELRDLLHFSS QVAQGMAFLA SKNCIHRDVA ARNVLLTNGH VAKIGDFGLA 
       810        820        830        840        850
RDIMNDSNYI VKGNARLPVK WMAPESIFDC VYTVQSDVWS YGILLWEIFS 
       860        870        880        890        900
LGLNPYPGIL VNSKFYKLVK DGYQMAQPAF APKNIYSIMQ ACWALEPTHR 
       910        920        930        940        950
PTFQQICSFL QEQAQEDRRE RDYTNLPSSS RSGGSGSSSS ELEEESSSEH 
       960        970 
LTCCEQGDIA QPLLQPNNYQ FC

Length:972

Mass (Da):107,984

Last modified:June 1, 1994 - v2

Checksum:ⁱA8D99BE237573FE8

GO

Isoform 2 (identifier: P07333-2) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MGPGVLLLLL VATAWHGQGI PVIEPSVPEL VVKPGATVTL RCVGNGSVEW 
        60         70         80         90        100
DGPPSPHWTL YSDGSSSILS TNNATFQNTG TYRCTEPGDP LGGSAAIHLY 
       110        120        130        140        150
VKDPARPWNV LAQEVVVFED QDALLPCLLT DPVLEAGVSL VRVRGRPLMR 
       160        170        180        190        200
HTNYSFSPWH GFTIHRAKFI QSQDYQCSAL MGGRKVMSIS IRLKVQKVIP 
       210        220        230        240        250
GPPALTLVPA ELVRIRGEAA QIVCSASSVD VNFDVFLQHN NTKLAIPQQS 
       260        270        280        290        300
DFHNNRYQKV LTLNLDQVDF QHAGNYSCVA SNVQGKHSTS MFFRVVGTPS 

PSLCPA

Show »

Length:306

Mass (Da):33,248

Checksum:ⁱDDAEA1B05EAAF3C2

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E9PEK4	E9PEK4_HUMAN	Macrophage colony-stimulating facto... Macrophage colony-stimulating factor 1 receptor	CSF1R	671	Annotation score:
H0YAL5	H0YAL5_HUMAN	Macrophage colony-stimulating facto... Macrophage colony-stimulating factor 1 receptor	CSF1R	64	Annotation score:
D6RGW1	D6RGW1_HUMAN	Macrophage colony-stimulating facto... Macrophage colony-stimulating factor 1 receptor	CSF1R	49	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	54	P → A in CAA27300 (PubMed:2421165).Curated	1
Sequence conflictⁱ	247	P → H in AAH47521 (PubMed:15489334).Curated	1
Sequence conflictⁱ	354	A → V in AAH47521 (PubMed:15489334).Curated	1
Sequence conflictⁱ	629	A → S in AAH47521 (PubMed:15489334).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_042038	32	V → G1 PublicationCorresponds to variant dbSNP:rs56048668EnsemblClinVar.	1
Natural variantⁱVAR_061290	245	A → S. Corresponds to variant dbSNP:rs41338945EnsemblClinVar.	1
Natural variantⁱVAR_049718	279	V → M. Corresponds to variant dbSNP:rs3829986EnsemblClinVar.	1
Natural variantⁱVAR_042039	362	H → R1 PublicationCorresponds to variant dbSNP:rs10079250EnsemblClinVar.	1
Natural variantⁱVAR_042040	413	G → S1 PublicationCorresponds to variant dbSNP:rs34951517EnsemblClinVar.	1
Natural variantⁱVAR_042041	536	L → V1 PublicationCorresponds to variant dbSNP:rs55942044EnsemblClinVar.	1
Natural variantⁱVAR_067396	585 – 619	GKTLG…VKMLK → A in HDLS. 1 PublicationAdd BLAST	35
Natural variantⁱVAR_067397	589	G → E in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860268EnsemblClinVar.	1
Natural variantⁱVAR_067398	633	E → K in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860269EnsemblClinVar.	1
Natural variantⁱVAR_072081	653	C → R in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016559EnsemblClinVar.	1
Natural variantⁱVAR_042042	693	P → H in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication	1
Natural variantⁱVAR_067399	710	R → H1 PublicationCorresponds to variant dbSNP:rs201569135Ensembl.	1
Natural variantⁱVAR_067400	747	G → R1 PublicationCorresponds to variant dbSNP:rs41355444EnsemblClinVar.	1
Natural variantⁱVAR_067401	766	M → T in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860270EnsemblClinVar.	1
Natural variantⁱVAR_067402	770	A → P in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860271EnsemblClinVar.	1
Natural variantⁱVAR_067403	774 – 814	Missing in HDLS. 1 PublicationAdd BLAST	41
Natural variantⁱVAR_067404	775	I → N in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860273EnsemblClinVar.	1
Natural variantⁱVAR_067405	794	I → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860274EnsemblClinVar.	1
Natural variantⁱVAR_067406	837	D → Y in HDLS. 1 PublicationCorresponds to variant dbSNP:rs387906662EnsemblClinVar.	1
Natural variantⁱVAR_072082	843	I → F in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016558EnsemblClinVar.	1
Natural variantⁱVAR_067407	849	F → S in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860277EnsemblClinVar.	1
Natural variantⁱVAR_067408	849	Missing in HDLS. 1 Publication	1
Natural variantⁱVAR_067409	868	L → P in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860278EnsemblClinVar.	1
Natural variantⁱVAR_067410	875	M → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860279EnsemblClinVar.	1
Natural variantⁱVAR_067411	878	P → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860280EnsemblClinVar.	1
Natural variantⁱVAR_072083	906	I → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016560EnsemblClinVar.	1
Natural variantⁱVAR_042043	920	E → D2 PublicationsCorresponds to variant dbSNP:rs34030164EnsemblClinVar.	1
Natural variantⁱVAR_042044	921	R → Q1 PublicationCorresponds to variant dbSNP:rs56059682Ensembl.	1
Natural variantⁱVAR_011953	969	Y → C. Corresponds to variant dbSNP:rs1801271EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_047757	297 – 306	ESAYLNLSSE → GTPSPSLCPA in isoform 2. 1 Publication		10
Alternative sequenceⁱVSP_047758	307 – 972	Missing in isoform 2. 1 PublicationAdd BLAST		666

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS4302.1 [P07333-1]
PIRⁱ	S08123 TVHUMD
NCBI Reference Sequences More...RefSeqⁱ	NP_001275634.1, NM_001288705.2 [P07333-1] NP_005202.2, NM_005211.3 [P07333-1]

Genome annotation databases

Ensemblⁱ	ENST00000286301; ENSP00000286301; ENSG00000182578 [P07333-1] ENST00000543093; ENSP00000445282; ENSG00000182578 [P07333-2]
GeneIDⁱ	1436
KEGGⁱ	hsa:1436
UCSC genome browser More...UCSCⁱ	uc003lrm.3 human [P07333-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P07333	Uncharacterized protein		MACMU		1150	UniRef90_P07333
Colony stimulating factor 1 receptor		MACFA		991
CSF1R isoform 2		PONAB		983
Macrophage colony-stimulating factor 1 receptor (Fragment)		HUMAN		49
CSF1R isoform 9 (Fragment)		PANTR		49
+10
P07333-2	cDNA FLJ60487, highly similar to Macrophage colony-stimulating factor 1receptor (CSF-1-R)		HUMAN		343	UniRef90_P07333-2
CSF1R isoform 7		PANTR		306
Colony stimulating factor 1 receptor		GORGO		306
Colony stimulating factor 1 receptor		COLAP		306
Colony stimulating factor 1 receptor		PAPAN		306
+7

Protein	Similar proteins		Species	Score	Length	Source
P07333	Tyrosine-protein kinase transforming protein fms		FSVMD		978	UniRef50_P07333
Macrophage colony-stimulating factor 1 receptor		FELCA		980
Macrophage colony-stimulating factor 1 receptor		RAT		978
Macrophage colony-stimulating factor 1 receptor	)	MOUSE		977
Uncharacterized protein		MACMU		1150
+164
P07333-2	cDNA FLJ60487, highly similar to Macrophage colony-stimulating factor 1receptor (CSF-1-R)		HUMAN		343	UniRef50_P07333-2
Colony stimulating factor 1 receptor		MACNE		306
CSF1R isoform 7		PANTR		306
Colony stimulating factor 1 receptor		NOMLE		306
Colony stimulating factor 1 receptor		MACFA		306
+16

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
CCDSⁱ	CCDS4302.1 [P07333-1]
PIRⁱ	S08123 TVHUMD
RefSeqⁱ	NP_001275634.1, NM_001288705.2 [P07333-1] NP_005202.2, NM_005211.3 [P07333-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2I0V	X-ray	2.80	A	538-678	[»]
				A	753-922	[»]
	2I0Y	X-ray	1.90	A	538-678	[»]
				A	753-922	[»]
	2I1M	X-ray	1.80	A	538-678	[»]
				A	753-922	[»]
	2OGV	X-ray	2.70	A	543-918	[»]
	3BEA	X-ray	2.02	A	538-678	[»]
				A	753-922	[»]
	3DPK	X-ray	1.95	A	538-678	[»]
				A	771-922	[»]
	3KRJ	X-ray	2.10	A	538-678	[»]
				A	753-922	[»]
	3KRL	X-ray	2.40	A	538-678	[»]
				A	753-922	[»]
	3LCD	X-ray	2.50	A	538-919	[»]
	3LCO	X-ray	3.40	A	550-919	[»]
	4DKD	X-ray	3.00	C	20-299	[»]
	4HW7	X-ray	2.90	A	542-919	[»]
	4LIQ	X-ray	2.60	E	2-512	[»]
	4R7H	X-ray	2.80	A	542-919	[»]
	4R7I	X-ray	2.75	A	542-919	[»]
	4WRL	X-ray	2.80	A/C	20-296	[»]
	4WRM	X-ray	6.85	A	20-504	[»]
	6IG8	X-ray	1.80	A	550-919	[»]
	6N33	X-ray	2.25	A	542-919	[»]
SMRⁱ	P07333
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	107823, 30 interactors
DIPⁱ	DIP-59421N
IntActⁱ	P07333, 17 interactors
MINTⁱ	P07333
STRINGⁱ	9606.ENSP00000286301

Chemistry databases

BindingDBⁱ	P07333
ChEMBLⁱ	CHEMBL1844
DrugBankⁱ	DB07167 5-CYANO-FURAN-2-CARBOXYLIC ACID [5-HYDROXYMETHYL-2-(4-METHYL-PIPERIDIN-1-YL)-PHENYL]-AMIDE DB07202 6-CHLORO-3-(3-METHYLISOXAZOL-5-YL)-4-PHENYLQUINOLIN-2(1H)-ONE DB06080 ABT-869 DB12147 Erdafitinib DB12010 Fostamatinib DB00619 Imatinib DB01268 Sunitinib
DrugCentralⁱ	P07333
GuidetoPHARMACOLOGYⁱ	1806

PTM databases

GlyConnectⁱ	1955
iPTMnetⁱ	P07333
PhosphoSitePlusⁱ	P07333

Polymorphism and mutation databases

BioMutaⁱ	CSF1R
DMDMⁱ	547770

Proteomic databases

EPDⁱ	P07333
jPOSTⁱ	P07333
MassIVEⁱ	P07333
PaxDbⁱ	P07333
PeptideAtlasⁱ	P07333
PRIDEⁱ	P07333
ProteomicsDBⁱ	51993 [P07333-1] 5930

Protocols and materials databases

ABCDⁱ	P07333
The DNASU plasmid repository More...DNASUⁱ	1436

Genome annotation databases

Ensemblⁱ	ENST00000286301; ENSP00000286301; ENSG00000182578 [P07333-1] ENST00000543093; ENSP00000445282; ENSG00000182578 [P07333-2]
GeneIDⁱ	1436
KEGGⁱ	hsa:1436
UCSCⁱ	uc003lrm.3 human [P07333-1]

Organism-specific databases

CTDⁱ	1436
DisGeNETⁱ	1436
EuPathDBⁱ	HostDB:ENSG00000182578.13
GeneCardsⁱ	CSF1R
GeneReviewsⁱ	CSF1R
HGNCⁱ	HGNC:2433 CSF1R
HPAⁱ	CAB008970 HPA012323
MalaCardsⁱ	CSF1R
MIMⁱ	164770 gene 221820 phenotype
neXtProtⁱ	NX_P07333
OpenTargetsⁱ	ENSG00000182578
Orphanetⁱ	313808 Hereditary diffuse leukoencephalopathy with axonal spheroids and pigmented glia
PharmGKBⁱ	PA26936
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0200 Eukaryota COG0515 LUCA
GeneTreeⁱ	ENSGT00940000155506
HOGENOMⁱ	HOG000112008
InParanoidⁱ	P07333
KOⁱ	K05090
OMAⁱ	TFQQICF
OrthoDBⁱ	592753at2759
PhylomeDBⁱ	P07333
TreeFamⁱ	TF325768

Enzyme and pathway databases

BRENDAⁱ	2.7.10.1 2681
Reactomeⁱ	R-HSA-449836 Other interleukin signaling
SignaLinkⁱ	P07333
SIGNORⁱ	P07333

Miscellaneous databases

ChiTaRSⁱ	CSF1R human
EvolutionaryTraceⁱ	P07333
GeneWikiⁱ	Colony_stimulating_factor_1_receptor
GenomeRNAiⁱ	1436
Pharosⁱ	P07333 Tclin
Protein Ontology More...PROⁱ	PR:P07333
RNActⁱ	P07333 protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000182578 Expressed in 202 organ(s), highest expression level in spleen
ExpressionAtlasⁱ	P07333 baseline and differential
Genevisibleⁱ	P07333 HS

Family and domain databases

Gene3Dⁱ	2.60.40.10, 5 hits
InterProⁱ	View protein in InterPro IPR030658 CSF-1_receptor IPR007110 Ig-like_dom IPR036179 Ig-like_dom_sf IPR013783 Ig-like_fold IPR003599 Ig_sub IPR003598 Ig_sub2 IPR013151 Immunoglobulin IPR011009 Kinase-like_dom_sf 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 IPR001824 Tyr_kinase_rcpt_3_CS
Pfamⁱ	View protein in Pfam PF00047 ig, 1 hit PF07714 Pkinase_Tyr, 1 hit
PIRSFⁱ	PIRSF500947 CSF-1_receptor, 1 hit
SMARTⁱ	View protein in SMART SM00409 IG, 5 hits SM00408 IGc2, 2 hits SM00219 TyrKc, 1 hit
SUPFAMⁱ	SSF48726 SSF48726, 5 hits SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS50835 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
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CSF1R_HUMAN
Accessionⁱ	P07333Primary (citable) accession number: P07333 Secondary accession number(s): B5A955 , D3DQG2, Q6LDW5, Q6LDY4, Q86VW7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
	Last sequence update:	June 1, 1994
	Last modified:	December 11, 2019
	This is version 222 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human and mouse protein kinases
Human and mouse protein kinases: classification and index
Human cell differentiation molecules
CD nomenclature of surface proteins of human leucocytes and list of entries

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P07333 (CSF1R_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Macrophage colony-stimulating factor 1 receptor

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Nucleus

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Your basket is currently empty. ⁱ

Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ