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.16 Publications

Catalytic activityⁱ

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation3 Publications

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 GW2580.2 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	614	ATPCurated		1
Active siteⁱ	776	Proton acceptorPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	586 – 594	ATPPROSITE-ProRule annotation		9

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
cytokine binding
Source: UniProtKB
Inferred from direct assayⁱ
- 8007983
macrophage colony-stimulating factor receptor activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 19100238
protein homodimerization activity
Source: BHF-UCL
Inferred from physical interactionⁱ
- 19017797
protein phosphatase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16705167
transmembrane receptor protein tyrosine kinase activity
Source: MGI
Inferred from direct assayⁱ
- 2408759
transmembrane signaling receptor activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

axon guidance
Source: ParkinsonsUK-UCL
Inferred from mutant phenotypeⁱ
- 22542597
cell-cell junction maintenance Source: MGI
cell differentiation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cell proliferation Source: MGI
cellular response to cytokine stimulus
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20504948
cellular response to macrophage colony-stimulating factor stimulus
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 8007983
cytokine-mediated signaling pathway Source: MGI
forebrain neuron differentiation
Source: ParkinsonsUK-UCL
Inferred from mutant phenotypeⁱ
- 22542597
hemopoiesis Source: MGI
inflammatory response Source: UniProtKB-KW
innate immune response Source: UniProtKB-KW
macrophage colony-stimulating factor signaling pathway
Source: BHF-UCL
Inferred from direct assayⁱ
- 19017797
- 19100238
negative regulation of apoptotic process
Source: ParkinsonsUK-UCL
Inferred from mutant phenotypeⁱ
- 22542597
negative regulation of cell proliferation
Source: ParkinsonsUK-UCL
Inferred from mutant phenotypeⁱ
- 22542597
negative regulation of signal transduction
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
olfactory bulb development
Source: ParkinsonsUK-UCL
Inferred from mutant phenotypeⁱ
- 22542597
osteoclast differentiation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
peptidyl-tyrosine phosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 8007983
phosphatidylinositol-mediated signaling
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21610095
phosphatidylinositol metabolic process
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21610095
positive regulation of cell migration
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21610095
positive regulation of cell motility Source: MGI
positive regulation of cell proliferation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 8007983
positive regulation of chemokine secretion Source: MGI
positive regulation of ERK1 and ERK2 cascade
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 8007983
positive regulation of osteoclast differentiation Source: MGI
positive regulation of protein phosphorylation Source: MGI
positive regulation of protein serine/threonine kinase activity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21610095
positive regulation of protein tyrosine kinase activity Source: MGI
positive regulation of tyrosine phosphorylation of STAT protein
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 8007983
protein autophosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 20504948
- 8007983
regulation of actin cytoskeleton reorganization
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21610095
regulation of bone resorption Source: UniProtKB
regulation of cell shape
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21610095
ruffle organization
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21610095
transmembrane receptor protein tyrosine kinase signaling pathway
Source: BHF-UCL
Inferred from direct assayⁱ
- 19100238

View the 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 3474
Reactomeⁱ	R-MMU-449836 Other interleukin signaling

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:Csfmr, Fms
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 18

Organism-specific databases

MGIⁱ	MGI:1339758 Csf1r

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	20 – 515	ExtracellularSequence analysisAdd BLAST	496
Transmembraneⁱ	516 – 536	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	537 – 977	CytoplasmicSequence analysisAdd BLAST	441

Keywords - Cellular componentⁱ

Cell membrane, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Mice are born at slightly less than the expected Mendelian rate, and the number of surviving mice is significantly reduced after three weeks. Mice are considerably smaller than wild-type littermates and suffer from general skeletal deformities with shortened limbs, increased bone density, and decreased volume of femoral bone marrow. Mice have decreased numbers of circulating monocytes and lymphocytes, decreased numbers of tissue macrophages, paired with an increase in the number of circulating granulocytes. In addition, mice are deaf and have reduced male and female fertility. In females, the duration of the diestrous period is increased, and in pregnant females the lactating mammary gland fails to develop normally. Males mate less frequently and give rise to fewer pregnant females.1 Publication

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	544	Y → F: No effect on binding to THOC5. 1 Publication	1
Mutagenesisⁱ	559	Y → F: Reduced interaction with CBL. Prolonged signaling, due to reduced internalization and degradation. Reduced interaction with FYN. Promotes cell proliferation. Reduced autophosphorylation at Tyr-807. 3 Publications	1
Mutagenesisⁱ	614	K → A: Loss of kinase activity. 3 Publications	1
Mutagenesisⁱ	614	K → M: Loss of kinase activity. Abolishes binding to THOC5. 3 Publications	1
Mutagenesisⁱ	697	Y → F: Abolishes interaction with GRB2. 2 Publications	1
Mutagenesisⁱ	706	Y → F: No effect on binding to THOC5. Slightly reduced enhancement of cell proliferation. 2 Publications	1
Mutagenesisⁱ	706	Y → G: Slightly impaired signaling. 2 Publications	1
Mutagenesisⁱ	721	Y → F: Abolishes interaction with PIK3R1. Strongly reduced phosphorylation of PLCG2. No effect on binding to THOC5. 4 Publications	1
Mutagenesisⁱ	807	Y → F: Reduced kinase activity. Strongly reduced phosphorylation of PLCG2. Diminishes binding to THOC5. 3 Publications	1
Mutagenesisⁱ	807	Y → G: May alter protein folding or stability. Loss of kinase activity. No effect on interaction with PIK3R1. 3 Publications	1

Keywords - Diseaseⁱ

Proto-oncogene

Chemistry databases

ChEMBLⁱ	CHEMBL5570

ChEMBLⁱ

CHEMBL5570

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 19	Sequence analysisAdd BLAST		19
ChainⁱPRO_0000016766	20 – 977	Macrophage colony-stimulating factor 1 receptorAdd BLAST		958

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	42 ↔ 84	PROSITE-ProRule annotation1 Publication
Glycosylationⁱ	45	N-linked (GlcNAc...) asparagine1 Publication	1
Glycosylationⁱ	73	N-linked (GlcNAc...) asparagine1 Publication	1
Disulfide bondⁱ	127 ↔ 177	PROSITE-ProRule annotation1 Publication
Disulfide bondⁱ	224 ↔ 278	PROSITE-ProRule annotation1 Publication
Glycosylationⁱ	302	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	335	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	389	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	410	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	417 ↔ 483	PROSITE-ProRule annotation
Glycosylationⁱ	449	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	478	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	491	N-linked (GlcNAc...) asparagine1 Publication	1
Modified residueⁱ	544	Phosphotyrosine; by autocatalysisBy similarity	1
Modified residueⁱ	559	Phosphotyrosine; by autocatalysis3 Publications	1
Modified residueⁱ	697	Phosphotyrosine; by autocatalysis1 Publication	1
Modified residueⁱ	706	Phosphotyrosine; by autocatalysis4 Publications	1
Modified residueⁱ	711	PhosphoserineCombined sources	1
Modified residueⁱ	721	Phosphotyrosine; by autocatalysis3 Publications	1
Modified residueⁱ	807	Phosphotyrosine; by autocatalysis5 Publications	1
Modified residueⁱ	921	Phosphotyrosine; by autocatalysis1 Publication	1
Modified residueⁱ	974	Phosphotyrosine; by autocatalysis1 Publication	1

Post-translational modificationⁱ

Autophosphorylated in response to CSF1 or IL34 binding. Phosphorylation at Tyr-559 is important for normal down-regulation of signaling by ubiquitination, internalization and degradation. Phosphorylation at Tyr-559 and Tyr-807 is important for interaction with SRC family members, including FYN, YES1 and SRC, and for subsequent activation of these protein kinases. Phosphorylation at Tyr-697 and Tyr-921 is important for interaction with GRB2. Phosphorylation at Tyr-721 is important for interaction with PIK3R1. Phosphorylation at Tyr-721 and Tyr-807 is important for interaction with PLCG2. Phosphorylation at Tyr-974 is important for interaction with CBL. Dephosphorylation by PTPN2 negatively regulates downstream signaling and macrophage differentiation.9 Publications

Manual assertion based on experiment inⁱ

Ref.7
"Identification of tyrosine 706 in the kinase insert as the major colony-stimulating factor 1 (CSF-1)-stimulated autophosphorylation site in the CSF-1 receptor in a murine macrophage cell line."
van der Geer P., Hunter T.
Mol. Cell. Biol. 10:2991-3002(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-706 AND TYR-807.
Ref.8
"Tyrosine 706 and 807 phosphorylation site mutants in the murine colony-stimulating factor-1 receptor are unaffected in their ability to bind or phosphorylate phosphatidylinositol-3 kinase but show differential defects in their ability to induce early response gene transcription."
van der Geer P., Hunter T.
Mol. Cell. Biol. 11:4698-4709(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION AND PHOSPHORYLATION OF PIK3R1, INTERACTION WITH PIK3R1, PHOSPHORYLATION AT TYR-706 AND TYR-807, MUTAGENESIS OF TYR-706 AND TYR-807.
Ref.9
"Mutation of Tyr697, a GRB2-binding site, and Tyr721, a PI 3-kinase binding site, abrogates signal transduction by the murine CSF-1 receptor expressed in Rat-2 fibroblasts."
van der Geer P., Hunter T.
EMBO J. 12:5161-5172(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CSF1 RECEPTOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-697; TYR-706; TYR-721 AND TYR-807, MUTAGENESIS OF LYS-614; TYR-697 AND TYR-721, INTERACTION WITH GRB2.
Ref.10
"Tyrosine 569 in the c-Fms juxtamembrane domain is essential for kinase activity and macrophage colony-stimulating factor-dependent internalization."
Myles G.M., Brandt C.S., Carlberg K., Rohrschneider L.R.
Mol. Cell. Biol. 14:4843-4854(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CSF1 RECEPTOR IN CELL PROLIFERATION AND IN ACTIVATION OF AKT1; MAPK1/ERK2; MAPK3/ERK1; STAT3; STAT5A AND STAT5B, INTERACTION WITH CBL; YES1; FYN AND SRC, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-559 AND TYR-807, UBIQUITINATION, MUTAGENESIS OF TYR-559.
Ref.15
"C-Cbl binds the CSF-1 receptor at tyrosine 973, a novel phosphorylation site in the receptor's carboxy-terminus."
Wilhelmsen K., Burkhalter S., van der Geer P.
Oncogene 21:1079-1089(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBL, PHOSPHORYLATION AT TYR-974.
Ref.16
"A juxtamembrane tyrosine in the colony stimulating factor-1 receptor regulates ligand-induced Src association, receptor kinase function, and down-regulation."
Rohde C.M., Schrum J., Lee A.W.
J. Biol. Chem. 279:43448-43461(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-559, PHOSPHORYLATION AT TYR-559, DOMAIN, ACTIVITY REGULATION.
Ref.22
"c-Fms tyrosine 559 is a major mediator of M-CSF-induced proliferation of primary macrophages."
Takeshita S., Faccio R., Chappel J., Zheng L., Feng X., Weber J.D., Teitelbaum S.L., Ross F.P.
J. Biol. Chem. 282:18980-18990(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TYR-559, PHOSPHORYLATION AT TYR-921.
Ref.29
"Functional overlap but differential expression of CSF-1 and IL-34 in their CSF-1 receptor-mediated regulation of myeloid cells."
Wei S., Nandi S., Chitu V., Yeung Y.G., Yu W., Huang M., Williams L.T., Lin H., Stanley E.R.
J. Leukoc. Biol. 88:495-505(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS IL34 AND CSF1 RECEPTOR, FUNCTION IN ACTIVATION OF MAPK1/ERK2 AND MAPK3/ERK1, PHOSPHORYLATION AT TYR-559; TYR-807 AND TYR-721, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
Ref.32
"Phosphorylation of CSF-1R Y721 mediates its association with PI3K to regulate macrophage motility and enhancement of tumor cell invasion."
Sampaio N.G., Yu W., Cox D., Wyckoff J., Condeelis J., Stanley E.R., Pixley F.J.
J. Cell Sci. 124:2021-2031(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF CELL MOTILITY; CELL SHAPE; ACTIN CYTOSKELETON REORGANIZATION; PHOSPHORYLATION OF AKT1 AND REGULATION OF PHOSPHATIDYLINOSITOL METABOLISM, INTERACTION WITH PIK3R1 AND PLCG2, PHOSPHORYLATION AT TYR-706 AND TYR-721, MUTAGENESIS OF TYR-721.

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

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbⁱ	P09581
PeptideAtlas More...PeptideAtlasⁱ	P09581
PRIDEⁱ	P09581

PTM databases

iPTMnetⁱ	P09581
PhosphoSitePlusⁱ	P09581

Expressionⁱ

Tissue specificityⁱ

Widely expressed.1 Publication

Gene expression databases

Bgeeⁱ	ENSMUSG00000024621 Expressed in 294 organ(s), highest expression level in placenta
CleanExⁱ	MM_CSF1R
ExpressionAtlasⁱ	P09581 baseline and differential
Genevisibleⁱ	P09581 MM

Interactionⁱ

Subunit structureⁱ

Monomer. Homodimer. Interacts with CSF1 and IL34. Interaction with dimeric CSF1 or IL34 leads to receptor homodimerization. Interacts with INPPL1/SHIP2 and THOC5. 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 SLA2.10 Publications

Manual assertion based on experiment inⁱ

Ref.8
"Tyrosine 706 and 807 phosphorylation site mutants in the murine colony-stimulating factor-1 receptor are unaffected in their ability to bind or phosphorylate phosphatidylinositol-3 kinase but show differential defects in their ability to induce early response gene transcription."
van der Geer P., Hunter T.
Mol. Cell. Biol. 11:4698-4709(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION AND PHOSPHORYLATION OF PIK3R1, INTERACTION WITH PIK3R1, PHOSPHORYLATION AT TYR-706 AND TYR-807, MUTAGENESIS OF TYR-706 AND TYR-807.
Ref.9
"Mutation of Tyr697, a GRB2-binding site, and Tyr721, a PI 3-kinase binding site, abrogates signal transduction by the murine CSF-1 receptor expressed in Rat-2 fibroblasts."
van der Geer P., Hunter T.
EMBO J. 12:5161-5172(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CSF1 RECEPTOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-697; TYR-706; TYR-721 AND TYR-807, MUTAGENESIS OF LYS-614; TYR-697 AND TYR-721, INTERACTION WITH GRB2.
Ref.10
"Tyrosine 569 in the c-Fms juxtamembrane domain is essential for kinase activity and macrophage colony-stimulating factor-dependent internalization."
Myles G.M., Brandt C.S., Carlberg K., Rohrschneider L.R.
Mol. Cell. Biol. 14:4843-4854(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CSF1 RECEPTOR IN CELL PROLIFERATION AND IN ACTIVATION OF AKT1; MAPK1/ERK2; MAPK3/ERK1; STAT3; STAT5A AND STAT5B, INTERACTION WITH CBL; YES1; FYN AND SRC, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-559 AND TYR-807, UBIQUITINATION, MUTAGENESIS OF TYR-559.
Ref.11
"Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-gamma2 by the M-CSF receptor is necessary for differentiation signaling."
Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.
EMBO J. 16:5880-5893(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MACROPHAGE PROLIFERATION; MACROPHAGE DIFFERENTIATION; PHOSPHORYLATION OF PLCG2; PHOSPHORYLATION OF PIK3R1 AND PHOSPHORYLATION OF GRB2, CATALYTIC ACTIVITY, INTERACTION WITH PIK3R1; GRB2; PLCG2 AND FYN, MUTAGENESIS OF LYS-614; TYR-697; TYR-721 AND TYR-807.
Ref.12
"FMIP, a novel Fms-interacting protein, affects granulocyte/macrophage differentiation."
Tamura T., Mancini A., Joos H., Koch A., Hakim C., Dumanski J., Weidner K.M., Niemann H.
Oncogene 18:6488-6495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THOC5, MUTAGENESIS OF TYR-544; LYS-614; TYR-706; TYR-721 AND TYR-807.
Ref.15
"C-Cbl binds the CSF-1 receptor at tyrosine 973, a novel phosphorylation site in the receptor's carboxy-terminus."
Wilhelmsen K., Burkhalter S., van der Geer P.
Oncogene 21:1079-1089(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBL, PHOSPHORYLATION AT TYR-974.
Ref.17
"SHIP2 is recruited to the cell membrane upon macrophage colony-stimulating factor (M-CSF) stimulation and regulates M-CSF-induced signaling."
Wang Y., Keogh R.J., Hunter M.G., Mitchell C.A., Frey R.S., Javaid K., Malik A.B., Schurmans S., Tridandapani S., Marsh C.B.
J. Immunol. 173:6820-6830(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INPPL1.
Ref.21
"The Src-like adaptor protein 2 regulates colony-stimulating factor-1 receptor signaling and down-regulation."
Pakuts B., Debonneville C., Liontos L.M., Loreto M.P., McGlade C.J.
J. Biol. Chem. 282:17953-17963(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF SLA2, INTERACTION WITH SLA2 AND CBL, SUBCELLULAR LOCATION, UBIQUITINATION.
Ref.32
"Phosphorylation of CSF-1R Y721 mediates its association with PI3K to regulate macrophage motility and enhancement of tumor cell invasion."
Sampaio N.G., Yu W., Cox D., Wyckoff J., Condeelis J., Stanley E.R., Pixley F.J.
J. Cell Sci. 124:2021-2031(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF CELL MOTILITY; CELL SHAPE; ACTIN CYTOSKELETON REORGANIZATION; PHOSPHORYLATION OF AKT1 AND REGULATION OF PHOSPHATIDYLINOSITOL METABOLISM, INTERACTION WITH PIK3R1 AND PLCG2, PHOSPHORYLATION AT TYR-706 AND TYR-721, MUTAGENESIS OF TYR-721.
Ref.33
"Structure of macrophage colony stimulating factor bound to FMS: diverse signaling assemblies of class III receptor tyrosine kinases."
Chen X., Liu H., Focia P.J., Shim A.H., He X.
Proc. Natl. Acad. Sci. U.S.A. 105:18267-18272(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-296 IN COMPLEX WITH CSF1, GLYCOSYLATION AT ASN-45 AND ASN-73, SUBUNIT, DISULFIDE BONDS.

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
CSF1	P09603	2	EBI-6305373,EBI-2872294	From Homo sapiens.
Csf1	P07141	6	EBI-6305373,EBI-777188

GO - Molecular functionⁱ

cytokine binding
Source: UniProtKB
Inferred from direct assayⁱ
- 8007983
protein homodimerization activity
Source: BHF-UCL
Inferred from physical interactionⁱ
- 19017797
protein phosphatase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16705167

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	198928, 15 interactors
Database of interacting proteins More...DIPⁱ	DIP-46415N
IntActⁱ	P09581, 8 interactors
Molecular INTeraction database More...MINTⁱ	P09581
STRINGⁱ	10090.ENSMUSP00000025523

Chemistry databases

BindingDBⁱ

P09581

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
Beta strandⁱ	55 – 60	Combined sources	6
Beta strandⁱ	64 – 66	Combined sources	3
Beta strandⁱ	68 – 73	Combined sources	6
Helixⁱ	76 – 78	Combined sources	3
Beta strandⁱ	80 – 85	Combined sources	6
Beta strandⁱ	95 – 101	Combined sources	7
Beta strandⁱ	107 – 111	Combined sources	5
Beta strandⁱ	113 – 118	Combined sources	6
Beta strandⁱ	123 – 125	Combined sources	3
Beta strandⁱ	127 – 130	Combined sources	4
Helixⁱ	132 – 136	Combined sources	5
Beta strandⁱ	137 – 142	Combined sources	6
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 – 198	Combined sources	8
Beta strandⁱ	204 – 213	Combined sources	10
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	254 – 267	Combined sources	14
Beta strandⁱ	270 – 272	Combined sources	3
Beta strandⁱ	274 – 281	Combined sources	8
Beta strandⁱ	286 – 294	Combined sources	9

Show more details

3D structure databases

ProteinModelPortalⁱ	P09581
SMRⁱ	P09581
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P09581

EvolutionaryTraceⁱ

P09581

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	24 – 104	Ig-like C2-type 1Add BLAST	81
Domainⁱ	107 – 197	Ig-like C2-type 2Add BLAST	91
Domainⁱ	204 – 298	Ig-like C2-type 3Add BLAST	95
Domainⁱ	299 – 397	Ig-like C2-type 4Add BLAST	99
Domainⁱ	398 – 503	Ig-like C2-type 5Add BLAST	106
Domainⁱ	580 – 913	Protein kinasePROSITE-ProRule annotationAdd BLAST	334

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	540 – 572	Regulatory juxtamembrane domainBy similarityAdd BLAST		33
Regionⁱ	794 – 816	Activation loopBy similarityAdd 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 (By similarity).By similarity

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 (By similarity).By similarity

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	ENSGT00760000118923
HOGENOMⁱ	HOG000112008
HOVERGENⁱ	HBG004335
InParanoidⁱ	P09581
KEGG Orthology (KO) More...KOⁱ	K05090
OMAⁱ	KYVRRDS
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G01TL
PhylomeDBⁱ	P09581
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, 4 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

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P09581-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MELGPPLVLL LATVWHGQGA PVIEPSGPEL VVEPGETVTL RCVSNGSVEW 
        60         70         80         90        100
DGPISPYWTL DPESPGSTLT TRNATFKNTG TYRCTELEDP MAGSTTIHLY 
       110        120        130        140        150
VKDPAHSWNL LAQEVTVVEG QEAVLPCLIT DPALKDSVSL MREGGRQVLR 
       160        170        180        190        200
KTVYFFSPWR GFIIRKAKVL DSNTYVCKTM VNGRESTSTG IWLKVNRVHP 
       210        220        230        240        250
EPPQIKLEPS KLVRIRGEAA QIVCSATNAE VGFNVILKRG DTKLEIPLNS 
       260        270        280        290        300
DFQDNYYKKV RALSLNAVDF QDAGIYSCVA SNDVGTRTAT MNFQVVESAY 
       310        320        330        340        350
LNLTSEQSLL QEVSVGDSLI LTVHADAYPS IQHYNWTYLG PFFEDQRKLE 
       360        370        380        390        400
FITQRAIYRY TFKLFLNRVK ASEAGQYFLM AQNKAGWNNL TFELTLRYPP 
       410        420        430        440        450
EVSVTWMPVN GSDVLFCDVS GYPQPSVTWM ECRGHTDRCD EAQALQVWND 
       460        470        480        490        500
THPEVLSQKP FDKVIIQSQL PIGTLKHNMT YFCKTHNSVG NSSQYFRAVS 
       510        520        530        540        550
LGQSKQLPDE SLFTPVVVAC MSVMSLLVLL LLLLLYKYKQ KPKYQVRWKI 
       560        570        580        590        600
IERYEGNSYT FIDPTQLPYN EKWEFPRNNL QFGKTLGAGA FGKVVEATAF 
       610        620        630        640        650
GLGKEDAVLK VAVKMLKSTA HADEKEALMS ELKIMSHLGQ HENIVNLLGA 
       660        670        680        690        700
CTHGGPVLVI TEYCCYGDLL NFLRRKAEAM LGPSLSPGQD SEGDSSYKNI 
       710        720        730        740        750
HLEKKYVRRD SGFSSQGVDT YVEMRPVSTS SSDSFFKQDL DKEASRPLEL 
       760        770        780        790        800
WDLLHFSSQV AQGMAFLASK NCIHRDVAAR NVLLTSGHVA KIGDFGLARD 
       810        820        830        840        850
IMNDSNYVVK GNARLPVKWM APESIFDCVY TVQSDVWSYG ILLWEIFSLG 
       860        870        880        890        900
LNPYPGILVN NKFYKLVKDG YQMAQPVFAP KNIYSIMQSC WDLEPTRRPT 
       910        920        930        940        950
FQQICFLLQE QARLERRDQD YANLPSSGGS SGSDSGGGSS GGSSSEPEEE 
       960        970 
SSSEHLACCE PGDIAQPLLQ PNNYQFC

Length:977

Mass (Da):109,179

Last modified:May 10, 2002 - v3

Checksum:ⁱ7EDF8310CCF98906

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	57	Y → I in CAA29666 (PubMed:2966922).Curated	1
Sequence conflictⁱ	72	R → S in CAA29666 (PubMed:2966922).Curated	1
Sequence conflictⁱ	162	F → S in CAA29666 (PubMed:2966922).Curated	1
Sequence conflictⁱ	446 – 447	QV → HL in CAA29666 (PubMed:2966922).Curated	2
Sequence conflictⁱ	474	T → P in CAA29666 (PubMed:2966922).Curated	1
Sequence conflictⁱ	660	I → Y in CAA29666 (PubMed:2966922).Curated	1
Sequence conflictⁱ	669	L → H in CAA29666 (PubMed:2966922).Curated	1
Sequence conflictⁱ	744	A → H in CAA29666 (PubMed:2966922).Curated	1
Sequence conflictⁱ	814	Missing in CAA29666 (PubMed:2966922).Curated	1
Sequence conflictⁱ	830	Y → I in CAA29666 (PubMed:2966922).Curated	1
Sequence conflictⁱ	858	L → H in CAA29666 (PubMed:2966922).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X06368 mRNA Translation: CAA29666.1 AK004947 mRNA Translation: BAB23691.1 AK079247 mRNA Translation: BAC37587.1 AK143545 mRNA Translation: BAE25430.1 AK154653 mRNA Translation: BAE32744.1 BC043054 mRNA Translation: AAH43054.1 S62219 Genomic DNA No translation available.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS29280.1
PIRⁱ	S01880 TVMSMD
NCBI Reference Sequences More...RefSeqⁱ	NP_001032948.2, NM_001037859.2 XP_006525647.1, XM_006525584.1 XP_006525648.1, XM_006525585.3 XP_006525649.1, XM_006525586.3 XP_017173299.1, XM_017317810.1
UniGeneⁱ	Mm.22574

Genome annotation databases

Ensemblⁱ	ENSMUST00000025523; ENSMUSP00000025523; ENSMUSG00000024621 ENSMUST00000115268; ENSMUSP00000110923; ENSMUSG00000024621
GeneIDⁱ	12978
KEGGⁱ	mmu:12978
UCSC genome browser More...UCSCⁱ	uc008fbn.1 mouse

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P09581	Colony stimulating factor 1 receptor		MOUSE		977	UniRef100_P09581

Protein	Similar proteins		Species	Score	Length	Source
P09581	Macrophage colony-stimulating factor 1 receptor		RAT		978	UniRef90_P09581
Colony stimulating factor 1 receptor		MOUSE		977
Macrophage colony-stimulating factor receptor 1 (Fragment)		Mus sp.		16
UPI000A30E265		MUSPA		975
Colony stimulating factor 1 receptor (Fragment)		MOUSE		16
+7

Protein	Similar proteins		Species	Score	Length	Source
P09581	Macrophage colony-stimulating factor 1 receptor	)	HUMAN		972	UniRef50_P07333
Macrophage colony-stimulating factor 1 receptor		RAT		978
Uncharacterized protein		MACFA		1055
Uncharacterized protein		MACMU		1016
CSF1R isoform 2		PONAB		983
+204

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X06368 mRNA Translation: CAA29666.1 AK004947 mRNA Translation: BAB23691.1 AK079247 mRNA Translation: BAC37587.1 AK143545 mRNA Translation: BAE25430.1 AK154653 mRNA Translation: BAE32744.1 BC043054 mRNA Translation: AAH43054.1 S62219 Genomic DNA No translation available.
CCDSⁱ	CCDS29280.1
PIRⁱ	S01880 TVMSMD
RefSeqⁱ	NP_001032948.2, NM_001037859.2 XP_006525647.1, XM_006525584.1 XP_006525648.1, XM_006525585.3 XP_006525649.1, XM_006525586.3 XP_017173299.1, XM_017317810.1
UniGeneⁱ	Mm.22574

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
	3EJJ	X-ray	2.40	X	20-296	[»]
	4EXP	X-ray	2.80	X	20-298	[»]
ProteinModelPortalⁱ	P09581
SMRⁱ	P09581
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	198928, 15 interactors
DIPⁱ	DIP-46415N
IntActⁱ	P09581, 8 interactors
MINTⁱ	P09581
STRINGⁱ	10090.ENSMUSP00000025523

Chemistry databases

BindingDBⁱ	P09581
ChEMBLⁱ	CHEMBL5570

PTM databases

iPTMnetⁱ	P09581
PhosphoSitePlusⁱ	P09581

Proteomic databases

PaxDbⁱ	P09581
PeptideAtlasⁱ	P09581
PRIDEⁱ	P09581

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000025523; ENSMUSP00000025523; ENSMUSG00000024621 ENSMUST00000115268; ENSMUSP00000110923; ENSMUSG00000024621
GeneIDⁱ	12978
KEGGⁱ	mmu:12978
UCSCⁱ	uc008fbn.1 mouse

Organism-specific databases

CTDⁱ	1436
MGIⁱ	MGI:1339758 Csf1r

Phylogenomic databases

eggNOGⁱ	KOG0200 Eukaryota COG0515 LUCA
GeneTreeⁱ	ENSGT00760000118923
HOGENOMⁱ	HOG000112008
HOVERGENⁱ	HBG004335
InParanoidⁱ	P09581
KOⁱ	K05090
OMAⁱ	KYVRRDS
OrthoDBⁱ	EOG091G01TL
PhylomeDBⁱ	P09581
TreeFamⁱ	TF325768

Enzyme and pathway databases

BRENDAⁱ	2.7.10.1 3474
Reactomeⁱ	R-MMU-449836 Other interleukin signaling

Miscellaneous databases

ChiTaRSⁱ	Csf1r mouse
EvolutionaryTraceⁱ	P09581
Protein Ontology More...PROⁱ	PR:P09581
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000024621 Expressed in 294 organ(s), highest expression level in placenta
CleanExⁱ	MM_CSF1R
ExpressionAtlasⁱ	P09581 baseline and differential
Genevisibleⁱ	P09581 MM

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, 4 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...

Entry informationⁱ

Entry nameⁱ	CSF1R_MOUSE
Accessionⁱ	P09581Primary (citable) accession number: P09581 Secondary accession number(s): Q3U3P1, Q9DBH9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	May 10, 2002
	Last modified:	November 7, 2018
	This is version 211 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human and mouse protein kinases
Human and mouse protein kinases: classification and index

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UniProtKB - P09581 (CSF1R_MOUSE)

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Macrophage colony-stimulating factor 1 receptor

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<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

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<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

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Plasma Membrane

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Topology

Keywords - Cellular componenti

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Keywords - Diseasei

Chemistry 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

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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

<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

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Chemistry 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

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Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

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Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

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Miscellaneous databases

Gene expression databases

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<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 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

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Documents

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Functionⁱ

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

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ