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Protein

Macrophage colony-stimulating factor 1 receptor

Gene

Csf1r

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Enzyme 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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei614ATPCurated1
Active sitei776Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi586 – 594ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cytokine binding Source: UniProtKB
  • macrophage colony-stimulating factor receptor activity Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • protein phosphatase binding Source: UniProtKB
  • transmembrane receptor protein tyrosine kinase activity Source: MGI

GO - Biological processi

  • axon guidance Source: ParkinsonsUK-UCL
  • cell-cell junction maintenance Source: MGI
  • cell proliferation Source: MGI
  • cellular response to cytokine stimulus Source: UniProtKB
  • cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
  • cytokine-mediated signaling pathway Source: MGI
  • forebrain neuron differentiation Source: ParkinsonsUK-UCL
  • hemopoiesis Source: MGI
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • macrophage colony-stimulating factor signaling pathway Source: BHF-UCL
  • negative regulation of apoptotic process Source: ParkinsonsUK-UCL
  • negative regulation of cell proliferation Source: ParkinsonsUK-UCL
  • olfactory bulb development Source: ParkinsonsUK-UCL
  • osteoclast differentiation Source: UniProtKB
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: UniProtKB
  • phosphatidylinositol metabolic process Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell motility Source: MGI
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of chemokine secretion Source: MGI
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of protein tyrosine kinase activity Source: MGI
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of actin cytoskeleton reorganization Source: UniProtKB
  • regulation of bone resorption Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • ruffle organization Source: UniProtKB
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiR-MMU-449147. Signaling by Interleukins.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1339758. Csf1r.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 515ExtracellularSequence analysisAdd BLAST496
Transmembranei516 – 536HelicalSequence analysisAdd BLAST21
Topological domaini537 – 977CytoplasmicSequence analysisAdd BLAST441

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • CSF1-CSF1R complex Source: BHF-UCL
  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: GOC
  • membrane Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

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 keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi544Y → F: No effect on binding to THOC5. 1 Publication1
Mutagenesisi559Y → 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 Publications1
Mutagenesisi614K → A: Loss of kinase activity. 3 Publications1
Mutagenesisi614K → M: Loss of kinase activity. Abolishes binding to THOC5. 3 Publications1
Mutagenesisi697Y → F: Abolishes interaction with GRB2. 2 Publications1
Mutagenesisi706Y → F: No effect on binding to THOC5. Slightly reduced enhancement of cell proliferation. 2 Publications1
Mutagenesisi706Y → G: Slightly impaired signaling. 2 Publications1
Mutagenesisi721Y → F: Abolishes interaction with PIK3R1. Strongly reduced phosphorylation of PLCG2. No effect on binding to THOC5. 4 Publications1
Mutagenesisi807Y → F: Reduced kinase activity. Strongly reduced phosphorylation of PLCG2. Diminishes binding to THOC5. 3 Publications1
Mutagenesisi807Y → G: May alter protein folding or stability. Loss of kinase activity. No effect on interaction with PIK3R1. 3 Publications1

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBLiCHEMBL5570.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001676620 – 977Macrophage colony-stimulating factor 1 receptorAdd BLAST958

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi42 ↔ 84PROSITE-ProRule annotation1 Publication
Glycosylationi45N-linked (GlcNAc...)1 Publication1
Glycosylationi73N-linked (GlcNAc...)1 Publication1
Disulfide bondi127 ↔ 177PROSITE-ProRule annotation1 Publication
Disulfide bondi224 ↔ 278PROSITE-ProRule annotation1 Publication
Glycosylationi302N-linked (GlcNAc...)Sequence analysis1
Glycosylationi335N-linked (GlcNAc...)Sequence analysis1
Glycosylationi389N-linked (GlcNAc...)Sequence analysis1
Glycosylationi410N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi417 ↔ 483PROSITE-ProRule annotation
Glycosylationi449N-linked (GlcNAc...)Sequence analysis1
Glycosylationi478N-linked (GlcNAc...)Sequence analysis1
Glycosylationi491N-linked (GlcNAc...)1 Publication1
Modified residuei544Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei559Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei697Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei706Phosphotyrosine; by autocatalysis4 Publications1
Modified residuei711PhosphoserineCombined sources1
Modified residuei721Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei807Phosphotyrosine; by autocatalysis5 Publications1
Modified residuei921Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei974Phosphotyrosine; by autocatalysis1 Publication1

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP09581.
PeptideAtlasiP09581.
PRIDEiP09581.

PTM databases

iPTMnetiP09581.
PhosphoSitePlusiP09581.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSMUSG00000024621.
CleanExiMM_CSF1R.
ExpressionAtlasiP09581. baseline and differential.
GenevisibleiP09581. 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

Binary interactionsi

WithEntry#Exp.IntActNotes
Csf1P071414EBI-6305373,EBI-777188

GO - Molecular functioni

  • cytokine binding Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • protein phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi198928. 15 interactors.
DIPiDIP-46415N.
IntActiP09581. 5 interactors.
MINTiMINT-8013693.
STRINGi10090.ENSMUSP00000025523.

Chemistry databases

BindingDBiP09581.

Structurei

Secondary structure

1977
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 25Combined sources4
Beta strandi27 – 32Combined sources6
Beta strandi38 – 43Combined sources6
Beta strandi49 – 51Combined sources3
Beta strandi55 – 60Combined sources6
Beta strandi64 – 66Combined sources3
Beta strandi68 – 73Combined sources6
Helixi76 – 78Combined sources3
Beta strandi80 – 85Combined sources6
Beta strandi95 – 101Combined sources7
Beta strandi107 – 111Combined sources5
Beta strandi113 – 118Combined sources6
Beta strandi123 – 125Combined sources3
Beta strandi127 – 130Combined sources4
Helixi132 – 136Combined sources5
Beta strandi137 – 142Combined sources6
Helixi143 – 145Combined sources3
Beta strandi154 – 157Combined sources4
Turni158 – 160Combined sources3
Beta strandi161 – 166Combined sources6
Helixi169 – 171Combined sources3
Beta strandi173 – 181Combined sources9
Beta strandi184 – 187Combined sources4
Beta strandi191 – 198Combined sources8
Beta strandi204 – 213Combined sources10
Beta strandi216 – 218Combined sources3
Beta strandi220 – 231Combined sources12
Beta strandi234 – 239Combined sources6
Beta strandi248 – 252Combined sources5
Beta strandi254 – 267Combined sources14
Beta strandi270 – 272Combined sources3
Beta strandi274 – 281Combined sources8
Beta strandi286 – 294Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EJJX-ray2.40X20-296[»]
4EXPX-ray2.80X20-298[»]
ProteinModelPortaliP09581.
SMRiP09581.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09581.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 104Ig-like C2-type 1Add BLAST81
Domaini107 – 197Ig-like C2-type 2Add BLAST91
Domaini204 – 298Ig-like C2-type 3Add BLAST95
Domaini299 – 397Ig-like C2-type 4Add BLAST99
Domaini398 – 503Ig-like C2-type 5Add BLAST106
Domaini580 – 913Protein kinasePROSITE-ProRule annotationAdd BLAST334

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni540 – 572Regulatory juxtamembrane domainBy similarityAdd BLAST33
Regioni794 – 816Activation loopBy similarityAdd BLAST23

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
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112008.
HOVERGENiHBG004335.
InParanoidiP09581.
KOiK05090.
OMAiWKIIESY.
OrthoDBiEOG091G01TL.
PhylomeDBiP09581.
TreeFamiTF325768.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR030658. CSF-1_receptor.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]
PANTHERiPTHR24416:SF47. PTHR24416:SF47. 3 hits.
PfamiPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500947. CSF-1_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09581-1 [UniParc]FASTAAdd 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 keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti57Y → I in CAA29666 (PubMed:2966922).Curated1
Sequence conflicti72R → S in CAA29666 (PubMed:2966922).Curated1
Sequence conflicti162F → S in CAA29666 (PubMed:2966922).Curated1
Sequence conflicti446 – 447QV → HL in CAA29666 (PubMed:2966922).Curated2
Sequence conflicti474T → P in CAA29666 (PubMed:2966922).Curated1
Sequence conflicti660I → Y in CAA29666 (PubMed:2966922).Curated1
Sequence conflicti669L → H in CAA29666 (PubMed:2966922).Curated1
Sequence conflicti744A → H in CAA29666 (PubMed:2966922).Curated1
Sequence conflicti814Missing in CAA29666 (PubMed:2966922).Curated1
Sequence conflicti830Y → I in CAA29666 (PubMed:2966922).Curated1
Sequence conflicti858L → H in CAA29666 (PubMed:2966922).Curated1

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.
CCDSiCCDS29280.1.
PIRiS01880. TVMSMD.
RefSeqiNP_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.
UniGeneiMm.22574.

Genome annotation databases

EnsembliENSMUST00000025523; ENSMUSP00000025523; ENSMUSG00000024621.
ENSMUST00000115268; ENSMUSP00000110923; ENSMUSG00000024621.
GeneIDi12978.
KEGGimmu:12978.
UCSCiuc008fbn.1. mouse.

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.
CCDSiCCDS29280.1.
PIRiS01880. TVMSMD.
RefSeqiNP_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.
UniGeneiMm.22574.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EJJX-ray2.40X20-296[»]
4EXPX-ray2.80X20-298[»]
ProteinModelPortaliP09581.
SMRiP09581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198928. 15 interactors.
DIPiDIP-46415N.
IntActiP09581. 5 interactors.
MINTiMINT-8013693.
STRINGi10090.ENSMUSP00000025523.

Chemistry databases

BindingDBiP09581.
ChEMBLiCHEMBL5570.

PTM databases

iPTMnetiP09581.
PhosphoSitePlusiP09581.

Proteomic databases

PaxDbiP09581.
PeptideAtlasiP09581.
PRIDEiP09581.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025523; ENSMUSP00000025523; ENSMUSG00000024621.
ENSMUST00000115268; ENSMUSP00000110923; ENSMUSG00000024621.
GeneIDi12978.
KEGGimmu:12978.
UCSCiuc008fbn.1. mouse.

Organism-specific databases

CTDi1436.
MGIiMGI:1339758. Csf1r.

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112008.
HOVERGENiHBG004335.
InParanoidiP09581.
KOiK05090.
OMAiWKIIESY.
OrthoDBiEOG091G01TL.
PhylomeDBiP09581.
TreeFamiTF325768.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiR-MMU-449147. Signaling by Interleukins.

Miscellaneous databases

ChiTaRSiCsf1r. mouse.
EvolutionaryTraceiP09581.
PROiP09581.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024621.
CleanExiMM_CSF1R.
ExpressionAtlasiP09581. baseline and differential.
GenevisibleiP09581. MM.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR030658. CSF-1_receptor.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]
PANTHERiPTHR24416:SF47. PTHR24416:SF47. 3 hits.
PfamiPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500947. CSF-1_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCSF1R_MOUSE
AccessioniPrimary (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 2, 2016
This is version 199 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.