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UniProtKB - P07333 (CSF1R_HUMAN)

Entry version 225 (17 Jun 2020)
Sequence version 2 (01 Jun 1994)
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Protein

Macrophage colony-stimulating factor 1 receptor

Gene

CSF1R

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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, including the ERK1/2 and the JNK pathway (PubMed:20504948, PubMed:30982609). 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. In the central nervous system, may play a role in the development of microglia macrophages (PubMed:30982608).16 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei616ATPCurated1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei778Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi588 – 596ATPPROSITE-ProRule annotation9

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processImmunity, Inflammatory response, Innate immunity
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.10.1 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-449836 Other interleukin signaling
R-HSA-8853884 Transcriptional Regulation by VENTX

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P07333

SIGNOR Signaling Network Open Resource

More...SIGNORi		P07333

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CSF1R
Synonyms:FMS
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000182578.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:2433 CSF1R

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		164770 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P07333

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini20 – 517ExtracellularSequence analysisAdd BLAST498
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei518 – 538HelicalSequence analysisAdd BLAST21
Topological domaini539 – 972CytoplasmicSequence analysisAdd BLAST434

Keywords - Cellular componenti

Cell membrane, Membrane

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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)4 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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_067396585 – 619GKTLG…VKMLK → A in HDLS. 1 PublicationAdd BLAST35
Natural variantiVAR_067397589G → E in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860268EnsemblClinVar.1
Natural variantiVAR_067398633E → K in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860269EnsemblClinVar.1
Natural variantiVAR_072081653C → R in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016559EnsemblClinVar.1
Natural variantiVAR_083144765G → D in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs690016566EnsemblClinVar.1
Natural variantiVAR_067401766M → T in HDLS; impairs autophosphorylation upon stimulation with CSF1. 2 PublicationsCorresponds to variant dbSNP:rs281860270EnsemblClinVar.1
Natural variantiVAR_067402770A → P in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860271EnsemblClinVar.1
Natural variantiVAR_067403774 – 814Missing in HDLS. 1 PublicationAdd BLAST41
Natural variantiVAR_067404775I → N in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860273EnsemblClinVar.1
Natural variantiVAR_083145781A → E in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs587777247EnsemblClinVar.1
Natural variantiVAR_083146782R → H in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860281EnsemblClinVar.1
Natural variantiVAR_067405794I → T in HDLS; impairs autophosphorylation upon stimulation with CSF1. 2 PublicationsCorresponds to variant dbSNP:rs281860274EnsemblClinVar.1
Natural variantiVAR_083147824P → S in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 Publication1
Natural variantiVAR_067406837D → Y in HDLS. 1 PublicationCorresponds to variant dbSNP:rs387906662EnsemblClinVar.1
Natural variantiVAR_072082843I → F in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016558EnsemblClinVar.1
Natural variantiVAR_067407849F → S in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860277EnsemblClinVar.1
Natural variantiVAR_067408849Missing in HDLS. 1 Publication1
Natural variantiVAR_067409868L → P in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860278EnsemblClinVar.1
Natural variantiVAR_067410875M → T in HDLS; impairs autophosphorylation upon stimulation with CSF1. 2 PublicationsCorresponds to variant dbSNP:rs281860279EnsemblClinVar.1
Natural variantiVAR_067411878P → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860280EnsemblClinVar.1
Natural variantiVAR_072083906I → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016560EnsemblClinVar.1
Brain abnormalities, neurodegeneration, and dysosteosclerosis (BANDDOS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disease with variable manifestations. Main features are brain malformations with calcifying leukoencephalopathy, progressive neurodegeneration, and bone sclerotic features. The age at onset ranges from infancy to early adulthood. Neurologic features include loss of previous motor and language skills, cognitive impairment, spasticity, and focal seizures. Brain imaging shows periventricular white matter abnormalities and calcifications, large cisterna magna or Dandy-Walker malformation, and sometimes agenesis of the corpus callosum.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_083140132P → L in BANDDOS; impairs phosphorylation of JNK kinases upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs1351319114EnsemblClinVar.1
Natural variantiVAR_083141481 – 972Missing in BANDDOS. 1 PublicationCorresponds to variant dbSNP:rs917027829Add BLAST492
Natural variantiVAR_083142627Missing in BANDDOS; impairs phosphorylation of JNK kinases upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs1554101963Ensembl.1
Natural variantiVAR_083143643H → Q in BANDDOS. 1 PublicationCorresponds to variant dbSNP:rs184499252EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi301L → S: Constitutive kinase activity. 1 Publication1
Mutagenesisi708Y → F: Impairs degradation of activated CSF1R. 1 Publication1
Mutagenesisi802D → V: Constitutive kinase activity. Loss of inhibition by imatinib. 2 Publications1
Mutagenesisi809Y → F: Reduced kinase activity. Reduced interaction with SRC, FYN and YES1. 1 Publication1
Mutagenesisi969Y → F: Abolishes down-regulation of activated CSF1R. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration, Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		1436

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		CSF1R

MalaCards human disease database

More...MalaCardsi		CSF1R
MIMi221820 phenotype
618476 phenotype

Open Targets

More...OpenTargetsi		ENSG00000182578

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		556985 Early-onset calcifying leukoencephalopathy-skeletal dysplasia
313808 Hereditary diffuse leukoencephalopathy with axonal spheroids and pigmented glia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26936

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P07333 Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...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
DB12978 Pexidartinib
DB01268 Sunitinib

DrugCentral

More...DrugCentrali		P07333

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1806

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CSF1R

Domain mapping of disease mutations (DMDM)

More...DMDMi		547770

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 19Sequence analysisAdd BLAST19
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001676520 – 972Macrophage colony-stimulating factor 1 receptorAdd BLAST953

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi42 ↔ 84PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi45N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi73N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi127 ↔ 177PROSITE-ProRule annotation
Glycosylationi153N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi224 ↔ 278PROSITE-ProRule annotation
Glycosylationi240N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi275N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi302N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi335N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi353N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi412N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi419 ↔ 485PROSITE-ProRule annotation
Glycosylationi428N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi480N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei546Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei561Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei699Phosphotyrosine; by autocatalysisCombined sources1 Publication1
Modified residuei708Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei713PhosphoserineCombined sources1
Modified residuei723Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei809Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei923Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei969Phosphotyrosine; by autocatalysisBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated in response to CSF1 or IL34 binding (PubMed:24336230, PubMed:20489731, PubMed:23408870). 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.4 Publications
Ubiquitinated. Becomes rapidly polyubiquitinated after autophosphorylation, leading to its degradation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P07333

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P07333

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P07333

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P07333

PeptideAtlas

More...PeptideAtlasi		P07333

PRoteomics IDEntifications database

More...PRIDEi		P07333

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51993 [P07333-1]
5930

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1955

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P07333

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P07333

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in bone marrow and in differentiated blood mononuclear cells.

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by glucocorticoids.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000182578 Expressed in spleen and 201 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P07333 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P07333 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000182578 Tissue enhanced (blood, lymphoid tissue)

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		107823, 30 interactors

Database of interacting proteins

More...DIPi		DIP-59421N

Protein interaction database and analysis system

More...IntActi		P07333, 31 interactors

Molecular INTeraction database

More...MINTi		P07333

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000286301

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P07333

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P07333 protein

<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

1972
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P07333

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P07333

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini21 – 104Ig-like C2-type 1Add BLAST84
Domaini107 – 197Ig-like C2-type 2Add BLAST91
Domaini203 – 290Ig-like C2-type 3Add BLAST88
Domaini299 – 399Ig-like C2-type 4Add BLAST101
Domaini402 – 502Ig-like C2-type 5Add BLAST101
Domaini582 – 910Protein kinasePROSITE-ProRule annotationAdd BLAST329

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni542 – 574Regulatory juxtamembrane domainAdd BLAST33
Regioni796 – 818Activation loopAdd BLAST23

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<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

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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0200 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155506

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000288_49_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07333

KEGG Orthology (KO)

More...KOi		K05090

Identification of Orthologs from Complete Genome Data

More...OMAi		TFQQICF

Database of Orthologous Groups

More...OrthoDBi		236292at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P07333

TreeFam database of animal gene trees

More...TreeFami		TF325768

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.10, 5 hits

Integrated resource of protein families, domains and functional sites

More...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

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF500947 CSF-1_receptor, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00409 IG, 5 hits
SM00408 IGc2, 2 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48726 SSF48726, 5 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA8D99BE237573FE8
GO
Isoform 2 (identifier: P07333-2) [UniParc]FASTAAdd to basket

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

Show »
Length:306
Mass (Da):33,248
Checksum:iDDAEA1B05EAAF3C2
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PEK4E9PEK4_HUMAN
Macrophage colony-stimulating facto...
CSF1R
671Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YAL5H0YAL5_HUMAN
Macrophage colony-stimulating facto...
CSF1R
64Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6RGW1D6RGW1_HUMAN
Macrophage colony-stimulating facto...
CSF1R
49Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti54P → A in CAA27300 (PubMed:2421165).Curated1
Sequence conflicti247P → H in AAH47521 (PubMed:15489334).Curated1
Sequence conflicti354A → V in AAH47521 (PubMed:15489334).Curated1
Sequence conflicti629A → S in AAH47521 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04203832V → G1 PublicationCorresponds to variant dbSNP:rs56048668EnsemblClinVar.1
Natural variantiVAR_083140132P → L in BANDDOS; impairs phosphorylation of JNK kinases upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs1351319114EnsemblClinVar.1
Natural variantiVAR_061290245A → S. Corresponds to variant dbSNP:rs41338945EnsemblClinVar.1
Natural variantiVAR_049718279V → M. Corresponds to variant dbSNP:rs3829986EnsemblClinVar.1
Natural variantiVAR_042039362H → R1 PublicationCorresponds to variant dbSNP:rs10079250EnsemblClinVar.1
Natural variantiVAR_042040413G → S1 PublicationCorresponds to variant dbSNP:rs34951517EnsemblClinVar.1
Natural variantiVAR_083141481 – 972Missing in BANDDOS. 1 PublicationCorresponds to variant dbSNP:rs917027829Add BLAST492
Natural variantiVAR_042041536L → V1 PublicationCorresponds to variant dbSNP:rs55942044EnsemblClinVar.1
Natural variantiVAR_067396585 – 619GKTLG…VKMLK → A in HDLS. 1 PublicationAdd BLAST35
Natural variantiVAR_067397589G → E in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860268EnsemblClinVar.1
Natural variantiVAR_083142627Missing in BANDDOS; impairs phosphorylation of JNK kinases upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs1554101963Ensembl.1
Natural variantiVAR_067398633E → K in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860269EnsemblClinVar.1
Natural variantiVAR_083143643H → Q in BANDDOS. 1 PublicationCorresponds to variant dbSNP:rs184499252EnsemblClinVar.1
Natural variantiVAR_072081653C → R in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016559EnsemblClinVar.1
Natural variantiVAR_042042693P → H in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_067399710R → H1 PublicationCorresponds to variant dbSNP:rs201569135Ensembl.1
Natural variantiVAR_067400747G → R1 PublicationCorresponds to variant dbSNP:rs41355444EnsemblClinVar.1
Natural variantiVAR_083144765G → D in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs690016566EnsemblClinVar.1
Natural variantiVAR_067401766M → T in HDLS; impairs autophosphorylation upon stimulation with CSF1. 2 PublicationsCorresponds to variant dbSNP:rs281860270EnsemblClinVar.1
Natural variantiVAR_067402770A → P in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860271EnsemblClinVar.1
Natural variantiVAR_067403774 – 814Missing in HDLS. 1 PublicationAdd BLAST41
Natural variantiVAR_067404775I → N in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860273EnsemblClinVar.1
Natural variantiVAR_083145781A → E in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs587777247EnsemblClinVar.1
Natural variantiVAR_083146782R → H in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 PublicationCorresponds to variant dbSNP:rs281860281EnsemblClinVar.1
Natural variantiVAR_067405794I → T in HDLS; impairs autophosphorylation upon stimulation with CSF1. 2 PublicationsCorresponds to variant dbSNP:rs281860274EnsemblClinVar.1
Natural variantiVAR_083147824P → S in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 Publication1
Natural variantiVAR_067406837D → Y in HDLS. 1 PublicationCorresponds to variant dbSNP:rs387906662EnsemblClinVar.1
Natural variantiVAR_072082843I → F in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016558EnsemblClinVar.1
Natural variantiVAR_067407849F → S in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860277EnsemblClinVar.1
Natural variantiVAR_067408849Missing in HDLS. 1 Publication1
Natural variantiVAR_067409868L → P in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860278EnsemblClinVar.1
Natural variantiVAR_067410875M → T in HDLS; impairs autophosphorylation upon stimulation with CSF1. 2 PublicationsCorresponds to variant dbSNP:rs281860279EnsemblClinVar.1
Natural variantiVAR_067411878P → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs281860280EnsemblClinVar.1
Natural variantiVAR_072083906I → T in HDLS. 1 PublicationCorresponds to variant dbSNP:rs690016560EnsemblClinVar.1
Natural variantiVAR_042043920E → D2 PublicationsCorresponds to variant dbSNP:rs34030164EnsemblClinVar.1
Natural variantiVAR_042044921R → Q1 PublicationCorresponds to variant dbSNP:rs56059682Ensembl.1
Natural variantiVAR_011953969Y → C. Corresponds to variant dbSNP:rs1801271EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047757297 – 306ESAYLNLSSE → GTPSPSLCPA in isoform 2. 1 Publication10
Alternative sequenceiVSP_047758307 – 972Missing in isoform 2. 1 PublicationAdd BLAST666

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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]

Protein sequence database of the Protein Information Resource

More...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

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000286301; ENSP00000286301; ENSG00000182578 [P07333-1]
ENST00000543093; ENSP00000445282; ENSG00000182578 [P07333-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1436

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1436

UCSC genome browser

More...UCSCi		uc003lrm.3 human [P07333-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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%5Freferences%5Fsection">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

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
CCDSiCCDS4302.1 [P07333-1]
PIRiS08123 TVHUMD
RefSeqiNP_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 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-ray1.95A538-678[»]
A771-922[»]
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[»]
4LIQX-ray2.60E2-512[»]
4R7HX-ray2.80A542-919[»]
4R7IX-ray2.75A542-919[»]
4WRLX-ray2.80A/C20-296[»]
4WRMX-ray6.85A20-504[»]
6IG8X-ray1.80A550-919[»]
6N33X-ray2.25A542-919[»]
6T2WX-ray1.70A542-919[»]
SMRiP07333
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi107823, 30 interactors
DIPiDIP-59421N
IntActiP07333, 31 interactors
MINTiP07333
STRINGi9606.ENSP00000286301

Chemistry databases

BindingDBiP07333
ChEMBLiCHEMBL1844
DrugBankiDB07167 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
DB12978 Pexidartinib
DB01268 Sunitinib
DrugCentraliP07333
GuidetoPHARMACOLOGYi1806

PTM databases

GlyConnecti1955
iPTMnetiP07333
PhosphoSitePlusiP07333

Polymorphism and mutation databases

BioMutaiCSF1R
DMDMi547770

Proteomic databases

EPDiP07333
jPOSTiP07333
MassIVEiP07333
PaxDbiP07333
PeptideAtlasiP07333
PRIDEiP07333
ProteomicsDBi51993 [P07333-1]
5930

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P07333 61 sequenced antibodies

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1201 1726 antibodies

The DNASU plasmid repository

More...DNASUi		1436

Genome annotation databases

EnsembliENST00000286301; ENSP00000286301; ENSG00000182578 [P07333-1]
ENST00000543093; ENSP00000445282; ENSG00000182578 [P07333-2]
GeneIDi1436
KEGGihsa:1436
UCSCiuc003lrm.3 human [P07333-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1436
DisGeNETi1436
EuPathDBiHostDB:ENSG00000182578.13

GeneCards: human genes, protein and diseases

More...GeneCardsi		CSF1R
GeneReviewsiCSF1R
HGNCiHGNC:2433 CSF1R
HPAiENSG00000182578 Tissue enhanced (blood, lymphoid tissue)
MalaCardsiCSF1R
MIMi164770 gene
221820 phenotype
618476 phenotype
neXtProtiNX_P07333
OpenTargetsiENSG00000182578
Orphaneti556985 Early-onset calcifying leukoencephalopathy-skeletal dysplasia
313808 Hereditary diffuse leukoencephalopathy with axonal spheroids and pigmented glia
PharmGKBiPA26936

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000155506
HOGENOMiCLU_000288_49_0_1
InParanoidiP07333
KOiK05090
OMAiTFQQICF
OrthoDBi236292at2759
PhylomeDBiP07333
TreeFamiTF325768

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-449836 Other interleukin signaling
R-HSA-8853884 Transcriptional Regulation by VENTX
SignaLinkiP07333
SIGNORiP07333

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		1436 1 hit in 817 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CSF1R human
EvolutionaryTraceiP07333

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Colony_stimulating_factor_1_receptor

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		1436
PharosiP07333 Tclin

Protein Ontology

More...PROi		PR:P07333
RNActiP07333 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000182578 Expressed in spleen and 201 other tissues
ExpressionAtlasiP07333 baseline and differential
GenevisibleiP07333 HS

Family and domain databases

Gene3Di2.60.40.10, 5 hits
InterProiView 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
PfamiView protein in Pfam
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PIRSFiPIRSF500947 CSF-1_receptor, 1 hit
SMARTiView protein in SMART
SM00409 IG, 5 hits
SM00408 IGc2, 2 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 5 hits
SSF56112 SSF56112, 1 hit
PROSITEiView 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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCSF1R_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07333
Secondary accession number(s): B5A955
, D3DQG2, Q6LDW5, Q6LDY4, Q86VW7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 1, 1994
Last modified: June 17, 2020
This is version 225 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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