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P09581

- CSF1R_MOUSE

UniProt

P09581 - CSF1R_MOUSE

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Protein

Macrophage colony-stimulating factor 1 receptor

Gene
Csf1r, Csfmr, Fms
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.3 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei614 – 6141ATP Inferred
Active sitei776 – 7761Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi586 – 5949ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cytokine binding Source: UniProtKB
  3. macrophage colony-stimulating factor receptor activity Source: UniProtKB
  4. protein binding Source: IntAct
  5. protein homodimerization activity Source: BHF-UCL
  6. protein phosphatase binding Source: UniProtKB

GO - Biological processi

  1. cell-cell junction maintenance Source: Ensembl
  2. cell proliferation Source: Ensembl
  3. cellular response to cytokine stimulus Source: UniProtKB
  4. cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
  5. inflammatory response Source: UniProtKB-KW
  6. innate immune response Source: UniProtKB-KW
  7. macrophage colony-stimulating factor signaling pathway Source: GOC
  8. osteoclast differentiation Source: UniProtKB
  9. peptidyl-tyrosine phosphorylation Source: UniProtKB
  10. phosphatidylinositol-mediated signaling Source: UniProtKB
  11. phosphatidylinositol metabolic process Source: UniProtKB
  12. positive regulation of cell migration Source: UniProtKB
  13. positive regulation of cell proliferation Source: UniProtKB
  14. positive regulation of chemokine secretion Source: Ensembl
  15. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  16. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  17. positive regulation of protein tyrosine kinase activity Source: Ensembl
  18. positive regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  19. protein autophosphorylation Source: UniProtKB
  20. regulation of actin cytoskeleton reorganization Source: UniProtKB
  21. regulation of bone resorption Source: UniProtKB
  22. regulation of cell shape Source: UniProtKB
  23. ruffle organization Source: UniProtKB
  24. 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.

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
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1339758. Csf1r.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein
Note: The autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 515496Extracellular Reviewed predictionAdd
BLAST
Transmembranei516 – 53621Helical; Reviewed predictionAdd
BLAST
Topological domaini537 – 977441Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: MGI
  4. receptor complex Source: BHF-UCL
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi544 – 5441Y → F: No effect on binding to THOC5. 1 Publication
Mutagenesisi559 – 5591Y → 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
Mutagenesisi614 – 6141K → A: Loss of kinase activity. 3 Publications
Mutagenesisi614 – 6141K → M: Loss of kinase activity. Abolishes binding to THOC5. 3 Publications
Mutagenesisi697 – 6971Y → F: Abolishes interaction with GRB2. 2 Publications
Mutagenesisi706 – 7061Y → F: No effect on binding to THOC5. Slightly reduced enhancement of cell proliferation. 2 Publications
Mutagenesisi706 – 7061Y → G: Slightly impaired signaling. 2 Publications
Mutagenesisi721 – 7211Y → F: Abolishes interaction with PIK3R1. Strongly reduced phosphorylation of PLCG2. No effect on binding to THOC5. 4 Publications
Mutagenesisi807 – 8071Y → F: Reduced kinase activity. Strongly reduced phosphorylation of PLCG2. Diminishes binding to THOC5. 3 Publications
Mutagenesisi807 – 8071Y → G: May alter protein folding or stability. Loss of kinase activity. No effect on interaction with PIK3R1. 3 Publications

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed predictionAdd
BLAST
Chaini20 – 977958Macrophage colony-stimulating factor 1 receptorPRO_0000016766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 841 Publication
Glycosylationi45 – 451N-linked (GlcNAc...)1 Publication
Glycosylationi73 – 731N-linked (GlcNAc...)1 Publication
Disulfide bondi127 ↔ 1771 Publication
Disulfide bondi224 ↔ 2781 Publication
Glycosylationi302 – 3021N-linked (GlcNAc...) Reviewed prediction
Glycosylationi335 – 3351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi389 – 3891N-linked (GlcNAc...) Reviewed prediction
Glycosylationi410 – 4101N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi417 ↔ 483 By similarity
Glycosylationi449 – 4491N-linked (GlcNAc...) Reviewed prediction
Glycosylationi478 – 4781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi491 – 4911N-linked (GlcNAc...)1 Publication
Modified residuei544 – 5441Phosphotyrosine; by autocatalysis By similarity
Modified residuei559 – 5591Phosphotyrosine; by autocatalysis3 Publications
Modified residuei697 – 6971Phosphotyrosine; by autocatalysis1 Publication
Modified residuei706 – 7061Phosphotyrosine; by autocatalysis4 Publications
Modified residuei711 – 7111Phosphoserine By similarity
Modified residuei721 – 7211Phosphotyrosine; by autocatalysis3 Publications
Modified residuei807 – 8071Phosphotyrosine; by autocatalysis5 Publications
Modified residuei921 – 9211Phosphotyrosine; by autocatalysis Inferred
Modified residuei974 – 9741Phosphotyrosine; by autocatalysis1 Publication

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.10 Publications
Ubiquitinated. Becomes rapidly polyubiquitinated after autophosphorylation, leading to its degradation.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP09581.
PaxDbiP09581.
PRIDEiP09581.

PTM databases

PhosphoSiteiP09581.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

ArrayExpressiP09581.
BgeeiP09581.
CleanExiMM_CSF1R.
GenevestigatoriP09581.

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

Protein-protein interaction databases

BioGridi198928. 15 interactions.
DIPiDIP-46415N.
IntActiP09581. 5 interactions.
MINTiMINT-8013693.

Structurei

Secondary structure

1
977
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 254
Beta strandi27 – 326
Beta strandi38 – 436
Beta strandi49 – 513
Beta strandi55 – 606
Beta strandi64 – 663
Beta strandi68 – 736
Helixi76 – 783
Beta strandi80 – 856
Beta strandi95 – 1017
Beta strandi107 – 1115
Beta strandi113 – 1186
Beta strandi123 – 1253
Beta strandi127 – 1304
Helixi132 – 1365
Beta strandi137 – 1426
Helixi143 – 1453
Beta strandi154 – 1574
Turni158 – 1603
Beta strandi161 – 1666
Helixi169 – 1713
Beta strandi173 – 1819
Beta strandi184 – 1874
Beta strandi191 – 1988
Beta strandi204 – 21310
Beta strandi216 – 2183
Beta strandi220 – 23112
Beta strandi234 – 2396
Beta strandi248 – 2525
Beta strandi254 – 26714
Beta strandi270 – 2723
Beta strandi274 – 2818
Beta strandi286 – 2949

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EJJX-ray2.40X20-296[»]
4EXPX-ray2.80X20-298[»]
ProteinModelPortaliP09581.
SMRiP09581. Positions 20-496, 541-916.

Miscellaneous databases

EvolutionaryTraceiP09581.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 10481Ig-like C2-type 1Add
BLAST
Domaini107 – 19791Ig-like C2-type 2Add
BLAST
Domaini204 – 29895Ig-like C2-type 3Add
BLAST
Domaini299 – 39799Ig-like C2-type 4Add
BLAST
Domaini398 – 503106Ig-like C2-type 5Add
BLAST
Domaini580 – 913334Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni540 – 57233Regulatory juxtamembrane domain By similarityAdd
BLAST
Regioni794 – 81623Activation loop By similarityAdd
BLAST

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.1 Publication
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.1 Publication

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000112008.
HOVERGENiHBG004335.
InParanoidiP09581.
KOiK05090.
OMAiVECVAFN.
OrthoDBiEOG7KSX7R.
PhylomeDBiP09581.
TreeFamiTF325768.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
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]
PfamiPF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500947. CSF-1_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. 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

MELGPPLVLL LATVWHGQGA PVIEPSGPEL VVEPGETVTL RCVSNGSVEW    50
DGPISPYWTL DPESPGSTLT TRNATFKNTG TYRCTELEDP MAGSTTIHLY 100
VKDPAHSWNL LAQEVTVVEG QEAVLPCLIT DPALKDSVSL MREGGRQVLR 150
KTVYFFSPWR GFIIRKAKVL DSNTYVCKTM VNGRESTSTG IWLKVNRVHP 200
EPPQIKLEPS KLVRIRGEAA QIVCSATNAE VGFNVILKRG DTKLEIPLNS 250
DFQDNYYKKV RALSLNAVDF QDAGIYSCVA SNDVGTRTAT MNFQVVESAY 300
LNLTSEQSLL QEVSVGDSLI LTVHADAYPS IQHYNWTYLG PFFEDQRKLE 350
FITQRAIYRY TFKLFLNRVK ASEAGQYFLM AQNKAGWNNL TFELTLRYPP 400
EVSVTWMPVN GSDVLFCDVS GYPQPSVTWM ECRGHTDRCD EAQALQVWND 450
THPEVLSQKP FDKVIIQSQL PIGTLKHNMT YFCKTHNSVG NSSQYFRAVS 500
LGQSKQLPDE SLFTPVVVAC MSVMSLLVLL LLLLLYKYKQ KPKYQVRWKI 550
IERYEGNSYT FIDPTQLPYN EKWEFPRNNL QFGKTLGAGA FGKVVEATAF 600
GLGKEDAVLK VAVKMLKSTA HADEKEALMS ELKIMSHLGQ HENIVNLLGA 650
CTHGGPVLVI TEYCCYGDLL NFLRRKAEAM LGPSLSPGQD SEGDSSYKNI 700
HLEKKYVRRD SGFSSQGVDT YVEMRPVSTS SSDSFFKQDL DKEASRPLEL 750
WDLLHFSSQV AQGMAFLASK NCIHRDVAAR NVLLTSGHVA KIGDFGLARD 800
IMNDSNYVVK GNARLPVKWM APESIFDCVY TVQSDVWSYG ILLWEIFSLG 850
LNPYPGILVN NKFYKLVKDG YQMAQPVFAP KNIYSIMQSC WDLEPTRRPT 900
FQQICFLLQE QARLERRDQD YANLPSSGGS SGSDSGGGSS GGSSSEPEEE 950
SSSEHLACCE PGDIAQPLLQ PNNYQFC 977
Length:977
Mass (Da):109,179
Last modified:May 10, 2002 - v3
Checksum:i7EDF8310CCF98906
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571Y → I in CAA29666. 1 Publication
Sequence conflicti72 – 721R → S in CAA29666. 1 Publication
Sequence conflicti162 – 1621F → S in CAA29666. 1 Publication
Sequence conflicti446 – 4472QV → HL in CAA29666. 1 Publication
Sequence conflicti474 – 4741T → P in CAA29666. 1 Publication
Sequence conflicti660 – 6601I → Y in CAA29666. 1 Publication
Sequence conflicti669 – 6691L → H in CAA29666. 1 Publication
Sequence conflicti744 – 7441A → H in CAA29666. 1 Publication
Sequence conflicti814 – 8141Missing in CAA29666. 1 Publication
Sequence conflicti830 – 8301Y → I in CAA29666. 1 Publication
Sequence conflicti858 – 8581L → H in CAA29666. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006525646.1. XM_006525583.1.
XP_006525647.1. XM_006525584.1.
XP_006525648.1. XM_006525585.1.
XP_006525649.1. XM_006525586.1.
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:
EMBL
GenBank
DDBJ
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_006525646.1. XM_006525583.1.
XP_006525647.1. XM_006525584.1.
XP_006525648.1. XM_006525585.1.
XP_006525649.1. XM_006525586.1.
UniGenei Mm.22574.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 20-496, 541-916.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198928. 15 interactions.
DIPi DIP-46415N.
IntActi P09581. 5 interactions.
MINTi MINT-8013693.

Chemistry

ChEMBLi CHEMBL5570.

PTM databases

PhosphoSitei P09581.

Proteomic databases

MaxQBi P09581.
PaxDbi P09581.
PRIDEi P09581.

Protocols and materials databases

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 COG0515.
HOGENOMi HOG000112008.
HOVERGENi HBG004335.
InParanoidi P09581.
KOi K05090.
OMAi VECVAFN.
OrthoDBi EOG7KSX7R.
PhylomeDBi P09581.
TreeFami TF325768.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.

Miscellaneous databases

ChiTaRSi CSF1R. mouse.
EvolutionaryTracei P09581.
NextBioi 282750.
PROi P09581.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09581.
Bgeei P09581.
CleanExi MM_CSF1R.
Genevestigatori P09581.

Family and domain databases

Gene3Di 2.60.40.10. 5 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
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 ]
Pfami PF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF500947. CSF-1_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTi SM00409. IG. 3 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Murine c-fms cDNA: cloning, sequence analysis and retroviral expression."
    Rothwell V.M., Rohrschneider L.R.
    Oncogene Res. 1:311-324(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Rothwell V.M.
    Submitted (SEP-1988) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Reassessment of the murine c-fms proto-oncogene sequence."
    de Parseval N., Bordereaux D., Gisselbrecht S., Sola B.
    Nucleic Acids Res. 21:750-750(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Liver and Urinary bladder.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  6. "Expression of mRNA encoding the macrophage colony-stimulating factor receptor (c-fms) is controlled by a constitutive promoter and tissue-specific transcription elongation."
    Yue X., Favot P., Dunn T.L., Cassady A.I., Hume D.A.
    Mol. Cell. Biol. 13:3191-3201(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
  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.
  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.
  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.
  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.
  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.
  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.
  13. "Both src-dependent and -independent mechanisms mediate phosphatidylinositol 3-kinase regulation of colony-stimulating factor 1-activated mitogen-activated protein kinases in myeloid progenitors."
    Lee A.W., States D.J.
    Mol. Cell. Biol. 20:6779-6798(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Targeted disruption of the mouse colony-stimulating factor 1 receptor gene results in osteopetrosis, mononuclear phagocyte deficiency, increased primitive progenitor cell frequencies, and reproductive defects."
    Dai X.M., Ryan G.R., Hapel A.J., Dominguez M.G., Russell R.G., Kapp S., Sylvestre V., Stanley E.R.
    Blood 99:111-120(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  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.
  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, ENZYME REGULATION.
  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.
  18. "Activated c-Fms recruits Vav and Rac during CSF-1-induced cytoskeletal remodeling and spreading in osteoclasts."
    Sakai H., Chen Y., Itokawa T., Yu K.P., Zhu M.L., Insogna K.
    Bone 39:1290-1301(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-491.
    Strain: C57BL/6.
    Tissue: Plasma.
  20. "T-cell protein tyrosine phosphatase (Tcptp) is a negative regulator of colony-stimulating factor 1 signaling and macrophage differentiation."
    Simoncic P.D., Bourdeau A., Lee-Loy A., Rohrschneider L.R., Tremblay M.L., Stanley E.R., McGlade C.J.
    Mol. Cell. Biol. 26:4149-4160(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2.
  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.
  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.
  23. "M-CSF regulates the cytoskeleton via recruitment of a multimeric signaling complex to c-Fms Tyr-559/697/721."
    Faccio R., Takeshita S., Colaianni G., Chappel J., Zallone A., Teitelbaum S.L., Ross F.P.
    J. Biol. Chem. 282:18991-18999(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "Src-family kinases play an essential role in differentiation signaling downstream of macrophage colony-stimulating factor receptors mediating persistent phosphorylation of phospholipase C-gamma2 and MAP kinases ERK1 and ERK2."
    Bourgin-Hierle C., Gobert-Gosse S., Therier J., Grasset M.F., Mouchiroud G.
    Leukemia 22:161-169(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SIGNALING PATHWAY.
  25. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Imatinib mesylate suppresses bone metastases of breast cancer by inhibiting osteoclasts through the blockade of c-Fms signals."
    Hiraga T., Nakamura H.
    Int. J. Cancer 124:215-222(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN OSTEOCLAST DIFFERENTIATION, ROLE IN DISEASE, ENZYME REGULATION.
  27. "c-Fms-mediated differentiation and priming of monocyte lineage cells play a central role in autoimmune arthritis."
    Paniagua R.T., Chang A., Mariano M.M., Stein E.A., Wang Q., Lindstrom T.M., Sharpe O., Roscow C., Ho P.P., Lee D.M., Robinson W.H.
    Arthritis Res. Ther. 12:R32-R32(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN DISEASE.
  28. "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.
  29. "Control of macrophage lineage populations by CSF-1 receptor and GM-CSF in homeostasis and inflammation."
    Lenzo J.C., Turner A.L., Cook A.D., Vlahos R., Anderson G.P., Reynolds E.C., Hamilton J.A.
    Immunol. Cell Biol. 90:429-440(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "A CSF-1 receptor phosphotyrosine 559 signaling pathway regulates receptor ubiquitination and tyrosine phosphorylation."
    Xiong Y., Song D., Cai Y., Yu W., Yeung Y.G., Stanley E.R.
    J. Biol. Chem. 286:952-960(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  31. "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.
  32. "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.

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: July 9, 2014
This is version 176 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

External Data

Dasty 3

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