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P07333

- CSF1R_HUMAN

UniProt

P07333 - CSF1R_HUMAN

Protein

Macrophage colony-stimulating factor 1 receptor

Gene

CSF1R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 174 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Tyrosine-protein kinase that acts as cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines in response to IL34 and CSF1, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. Required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration, and promotes cancer cell invasion. Activates several signaling pathways in response to ligand binding. Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL. Activation of PLCG2 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, that then lead to the activation of protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1. Activated CSF1R transmits signals both via proteins that directly interact with phosphorylated tyrosine residues in its intracellular domain, or via adapter proteins, such as GRB2. Promotes activation of STAT family members STAT3, STAT5A and/or STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP-1. Receptor signaling is down-regulated by protein phosphatases, such as INPP5D/SHIP-1, that dephosphorylate the receptor and its downstream effectors, and by rapid internalization of the activated receptor.14 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.6 PublicationsPROSITE-ProRule annotation

    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 GW2580.7 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei616 – 6161ATPCurated
    Active sitei778 – 7781Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi588 – 5969ATPPROSITE-ProRule annotation

    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 homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. cell-cell junction maintenance Source: UniProtKB
    2. cell proliferation Source: UniProtKB
    3. cellular response to cytokine stimulus Source: UniProtKB
    4. cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
    5. cytokine-mediated signaling pathway Source: UniProtKB
    6. hemopoiesis Source: UniProtKB
    7. inflammatory response Source: UniProtKB
    8. innate immune response Source: UniProtKB-KW
    9. macrophage colony-stimulating factor signaling pathway Source: GOC
    10. macrophage differentiation Source: UniProtKB
    11. mammary gland duct morphogenesis Source: UniProtKB
    12. monocyte differentiation Source: UniProtKB
    13. multicellular organismal development Source: ProtInc
    14. osteoclast differentiation Source: UniProtKB
    15. peptidyl-tyrosine phosphorylation Source: UniProtKB
    16. phosphatidylinositol-mediated signaling Source: UniProtKB
    17. phosphatidylinositol metabolic process Source: UniProtKB
    18. positive regulation of cell migration Source: UniProtKB
    19. positive regulation of cell motility Source: UniProtKB
    20. positive regulation of cell proliferation Source: UniProtKB
    21. positive regulation of chemokine secretion Source: UniProtKB
    22. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    23. positive regulation of protein phosphorylation Source: UniProtKB
    24. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
    25. positive regulation of protein tyrosine kinase activity Source: UniProtKB
    26. positive regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
    27. protein autophosphorylation Source: UniProtKB
    28. regulation of actin cytoskeleton reorganization Source: UniProtKB
    29. regulation of bone resorption Source: UniProtKB
    30. regulation of cell shape Source: UniProtKB
    31. ruffle organization Source: UniProtKB
    32. signal transduction Source: ProtInc
    33. transmembrane receptor protein tyrosine kinase signaling pathway Source: UniProtKB

    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. 2681.
    SignaLinkiP07333.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Macrophage colony-stimulating factor 1 receptor
    Alternative name(s):
    CSF-1 receptor (EC:2.7.10.1)
    Short name:
    CSF-1-R
    Short name:
    CSF-1R
    Short name:
    M-CSF-R
    Proto-oncogene c-Fms
    CD_antigen: CD115
    Gene namesi
    Name:CSF1R
    Synonyms:FMS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:2433. CSF1R.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: ProtInc
    4. receptor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Aberrant expression of CSF1 or CSF1R can promote cancer cell proliferation, invasion and formation of metastases. Overexpression of CSF1 or CSF1R is observed in a significant percentage of breast, ovarian, prostate, and endometrial cancers.
    Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.
    Leukoencephalopathy, diffuse hereditary, with spheroids (HDLS) [MIM:221820]: An autosomal dominant adult-onset rapidly progressive neurodegenerative disorder characterized by variable behavioral, cognitive, and motor changes. Patients often die of dementia within 6 years of onset. Brain imaging shows patchy abnormalities in the cerebral white matter, predominantly affecting the frontal and parietal lobes.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti585 – 61935GKTLG…VKMLK → A in HDLS.
    VAR_067396Add
    BLAST
    Natural varianti589 – 5891G → E in HDLS. 1 Publication
    VAR_067397
    Natural varianti633 – 6331E → K in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 Publication
    VAR_067398
    Natural varianti766 – 7661M → T in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 Publication
    VAR_067401
    Natural varianti770 – 7701A → P in HDLS. 1 Publication
    VAR_067402
    Natural varianti774 – 81441Missing in HDLS.
    VAR_067403Add
    BLAST
    Natural varianti775 – 7751I → N in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 Publication
    VAR_067404
    Natural varianti794 – 7941I → T in HDLS. 1 Publication
    VAR_067405
    Natural varianti837 – 8371D → Y in HDLS. 1 Publication
    VAR_067406
    Natural varianti849 – 8491F → S in HDLS. 1 Publication
    VAR_067407
    Natural varianti849 – 8491Missing in HDLS. 1 Publication
    VAR_067408
    Natural varianti868 – 8681L → P in HDLS. 1 Publication
    VAR_067409
    Natural varianti875 – 8751M → T in HDLS. 1 Publication
    VAR_067410
    Natural varianti878 – 8781P → T in HDLS. 1 Publication
    VAR_067411

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi301 – 3011L → S: Constitutive kinase activity. 1 Publication
    Mutagenesisi708 – 7081Y → F: Impairs degradation of activated CSF1R. 1 Publication
    Mutagenesisi802 – 8021D → V: Constitutive kinase activity. Loss of inhibition by imatinib. 2 Publications
    Mutagenesisi809 – 8091Y → F: Reduced kinase activity. Reduced interaction with SRC, FYN and YES1. 1 Publication
    Mutagenesisi969 – 9691Y → F: Abolishes down-regulation of activated CSF1R. 1 Publication

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi221820. phenotype.
    Orphaneti313808. Adult-onset leukoencephalopathy with axonal spheroids and pigmented glia.
    PharmGKBiPA26936.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 972953Macrophage colony-stimulating factor 1 receptorPRO_0000016765Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi42 ↔ 84PROSITE-ProRule annotation
    Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi127 ↔ 177PROSITE-ProRule annotation
    Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi224 ↔ 278PROSITE-ProRule annotation
    Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi302 – 3021N-linked (GlcNAc...)1 Publication
    Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi353 – 3531N-linked (GlcNAc...)1 Publication
    Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi419 ↔ 485PROSITE-ProRule annotation
    Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis
    Modified residuei546 – 5461Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei561 – 5611Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei699 – 6991Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei708 – 7081Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei713 – 7131Phosphoserine1 Publication
    Modified residuei723 – 7231Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei809 – 8091Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei923 – 9231Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei969 – 9691Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated in response to CSF1 or IL34 binding. Phosphorylation at Tyr-561 is important for normal down-regulation of signaling by ubiquitination, internalization and degradation. Phosphorylation at Tyr-561 and Tyr-809 is important for interaction with SRC family members, including FYN, YES1 and SRC, and for subsequent activation of these protein kinases. Phosphorylation at Tyr-699 and Tyr-923 is important for interaction with GRB2. Phosphorylation at Tyr-723 is important for interaction with PIK3R1. Phosphorylation at Tyr-708 is important for normal receptor degradation. Phosphorylation at Tyr-723 and Tyr-809 is important for interaction with PLCG2. Phosphorylation at Tyr-969 is important for interaction with CBL. Dephosphorylation by PTPN2 negatively regulates downstream signaling and macrophage differentiation.3 Publications
    Ubiquitinated. Becomes rapidly polyubiquitinated after autophosphorylation, leading to its degradation.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP07333.
    PeptideAtlasiP07333.
    PRIDEiP07333.

    PTM databases

    PhosphoSiteiP07333.

    Expressioni

    Tissue specificityi

    Expressed in bone marrow and in differentiated blood mononuclear cells.

    Inductioni

    Up-regulated by glucocorticoids.1 Publication

    Gene expression databases

    ArrayExpressiP07333.
    BgeeiP07333.
    CleanExiHS_CSF1R.
    GenevestigatoriP07333.

    Organism-specific databases

    HPAiCAB008970.
    HPA012323.

    Interactioni

    Subunit structurei

    Interacts with INPPL1/SHIP2 and THOC5 By similarity. Monomer. Homodimer. Interacts with CSF1 and IL34. Interaction with dimeric CSF1 or IL34 leads to receptor homodimerization. Interacts (tyrosine phosphorylated) with PLCG2 (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1 (via SH2 domain). Interacts (tyrosine phosphorylated) with FYN, YES1 and SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with CBL, GRB2 and SLA2.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi107823. 18 interactions.
    DIPiDIP-59421N.
    IntActiP07333. 12 interactions.
    MINTiMINT-8019993.
    STRINGi9606.ENSP00000286301.

    Structurei

    Secondary structure

    1
    972
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 254
    Beta strandi38 – 436
    Beta strandi66 – 738
    Helixi76 – 783
    Beta strandi82 – 843
    Beta strandi95 – 973
    Beta strandi108 – 1114
    Beta strandi113 – 1186
    Beta strandi127 – 1315
    Helixi132 – 1354
    Beta strandi136 – 1427
    Helixi143 – 1453
    Beta strandi158 – 1603
    Beta strandi163 – 1664
    Helixi169 – 1713
    Beta strandi173 – 1797
    Beta strandi191 – 1966
    Beta strandi204 – 2107
    Beta strandi216 – 2183
    Beta strandi220 – 23112
    Beta strandi234 – 2363
    Beta strandi239 – 2413
    Beta strandi248 – 2536
    Beta strandi256 – 26712
    Beta strandi274 – 2818
    Beta strandi286 – 2938
    Beta strandi556 – 5605
    Helixi566 – 5683
    Helixi573 – 5753
    Beta strandi581 – 59010
    Beta strandi592 – 60110
    Beta strandi605 – 6073
    Beta strandi612 – 6187
    Helixi624 – 64017
    Beta strandi649 – 6535
    Beta strandi655 – 6584
    Beta strandi660 – 6645
    Helixi671 – 6788
    Turni742 – 7443
    Helixi753 – 77119
    Helixi781 – 7833
    Beta strandi785 – 7873
    Helixi788 – 7903
    Beta strandi791 – 7944
    Helixi798 – 8003
    Helixi803 – 8053
    Turni806 – 8083
    Beta strandi809 – 8113
    Beta strandi815 – 8173
    Helixi819 – 8213
    Helixi824 – 8296
    Helixi834 – 84815
    Turni849 – 8513
    Helixi863 – 8719
    Helixi883 – 89210
    Helixi897 – 8993
    Helixi903 – 92018

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I0VX-ray2.80A538-678[»]
    A753-922[»]
    2I0YX-ray1.90A538-678[»]
    A753-922[»]
    2I1MX-ray1.80A538-678[»]
    A753-922[»]
    2OGVX-ray2.70A543-918[»]
    3BEAX-ray2.02A538-678[»]
    A753-922[»]
    3DPKX-ray1.95A183-334[»]
    A538-678[»]
    3KRJX-ray2.10A538-678[»]
    A753-922[»]
    3KRLX-ray2.40A538-678[»]
    A753-922[»]
    3LCDX-ray2.50A538-919[»]
    3LCOX-ray3.40A550-919[»]
    4DKDX-ray3.00C20-299[»]
    4HW7X-ray2.90A542-919[»]
    4LIQX-ray2.60E2-512[»]
    ProteinModelPortaliP07333.
    SMRiP07333. Positions 20-498, 544-945.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07333.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 517498ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini539 – 972434CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei518 – 53821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 10484Ig-like C2-type 1Add
    BLAST
    Domaini107 – 19791Ig-like C2-type 2Add
    BLAST
    Domaini203 – 29088Ig-like C2-type 3Add
    BLAST
    Domaini299 – 399101Ig-like C2-type 4Add
    BLAST
    Domaini402 – 502101Ig-like C2-type 5Add
    BLAST
    Domaini582 – 910329Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni542 – 57433Regulatory juxtamembrane domainAdd
    BLAST
    Regioni796 – 81823Activation loopAdd
    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.
    The activation loop plays an important role in the regulation of kinase activity. Phosphorylation of tyrosine residues in this region leads to a conformation change and activation of the kinase.

    Sequence similaritiesi

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

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000112008.
    HOVERGENiHBG004335.
    InParanoidiP07333.
    KOiK05090.
    OMAiVECVAFN.
    PhylomeDBiP07333.
    TreeFamiTF325768.

    Family and domain databases

    Gene3Di2.60.40.10. 5 hits.
    InterProiIPR007110. 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]
    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. 3 hits.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS50835. IG_LIKE. 3 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

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

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

    « Hide

    MGPGVLLLLL VATAWHGQGI PVIEPSVPEL VVKPGATVTL RCVGNGSVEW    50
    DGPPSPHWTL YSDGSSSILS TNNATFQNTG TYRCTEPGDP LGGSAAIHLY 100
    VKDPARPWNV LAQEVVVFED QDALLPCLLT DPVLEAGVSL VRVRGRPLMR 150
    HTNYSFSPWH GFTIHRAKFI QSQDYQCSAL MGGRKVMSIS IRLKVQKVIP 200
    GPPALTLVPA ELVRIRGEAA QIVCSASSVD VNFDVFLQHN NTKLAIPQQS 250
    DFHNNRYQKV LTLNLDQVDF QHAGNYSCVA SNVQGKHSTS MFFRVVESAY 300
    LNLSSEQNLI QEVTVGEGLN LKVMVEAYPG LQGFNWTYLG PFSDHQPEPK 350
    LANATTKDTY RHTFTLSLPR LKPSEAGRYS FLARNPGGWR ALTFELTLRY 400
    PPEVSVIWTF INGSGTLLCA ASGYPQPNVT WLQCSGHTDR CDEAQVLQVW 450
    DDPYPEVLSQ EPFHKVTVQS LLTVETLEHN QTYECRAHNS VGSGSWAFIP 500
    ISAGAHTHPP DEFLFTPVVV ACMSIMALLL LLLLLLLYKY KQKPKYQVRW 550
    KIIESYEGNS YTFIDPTQLP YNEKWEFPRN NLQFGKTLGA GAFGKVVEAT 600
    AFGLGKEDAV LKVAVKMLKS TAHADEKEAL MSELKIMSHL GQHENIVNLL 650
    GACTHGGPVL VITEYCCYGD LLNFLRRKAE AMLGPSLSPG QDPEGGVDYK 700
    NIHLEKKYVR RDSGFSSQGV DTYVEMRPVS TSSNDSFSEQ DLDKEDGRPL 750
    ELRDLLHFSS QVAQGMAFLA SKNCIHRDVA ARNVLLTNGH VAKIGDFGLA 800
    RDIMNDSNYI VKGNARLPVK WMAPESIFDC VYTVQSDVWS YGILLWEIFS 850
    LGLNPYPGIL VNSKFYKLVK DGYQMAQPAF APKNIYSIMQ ACWALEPTHR 900
    PTFQQICSFL QEQAQEDRRE RDYTNLPSSS RSGGSGSSSS ELEEESSSEH 950
    LTCCEQGDIA QPLLQPNNYQ FC 972
    Length:972
    Mass (Da):107,984
    Last modified:June 1, 1994 - v2
    Checksum:iA8D99BE237573FE8
    GO
    Isoform 2 (identifier: P07333-2) [UniParc]FASTAAdd to Basket

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

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541P → A in CAA27300. (PubMed:2421165)Curated
    Sequence conflicti247 – 2471P → H in AAH47521. (PubMed:15489334)Curated
    Sequence conflicti354 – 3541A → V in AAH47521. (PubMed:15489334)Curated
    Sequence conflicti629 – 6291A → S in AAH47521. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321V → G.1 Publication
    Corresponds to variant rs56048668 [ dbSNP | Ensembl ].
    VAR_042038
    Natural varianti245 – 2451A → S.
    Corresponds to variant rs41338945 [ dbSNP | Ensembl ].
    VAR_061290
    Natural varianti279 – 2791V → M.
    Corresponds to variant rs3829986 [ dbSNP | Ensembl ].
    VAR_049718
    Natural varianti362 – 3621H → R.1 Publication
    Corresponds to variant rs10079250 [ dbSNP | Ensembl ].
    VAR_042039
    Natural varianti413 – 4131G → S.1 Publication
    Corresponds to variant rs34951517 [ dbSNP | Ensembl ].
    VAR_042040
    Natural varianti536 – 5361L → V.1 Publication
    Corresponds to variant rs55942044 [ dbSNP | Ensembl ].
    VAR_042041
    Natural varianti585 – 61935GKTLG…VKMLK → A in HDLS.
    VAR_067396Add
    BLAST
    Natural varianti589 – 5891G → E in HDLS. 1 Publication
    VAR_067397
    Natural varianti633 – 6331E → K in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 Publication
    VAR_067398
    Natural varianti693 – 6931P → H in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
    VAR_042042
    Natural varianti710 – 7101R → H.1 Publication
    VAR_067399
    Natural varianti747 – 7471G → R.1 Publication
    Corresponds to variant rs41355444 [ dbSNP | Ensembl ].
    VAR_067400
    Natural varianti766 – 7661M → T in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 Publication
    VAR_067401
    Natural varianti770 – 7701A → P in HDLS. 1 Publication
    VAR_067402
    Natural varianti774 – 81441Missing in HDLS.
    VAR_067403Add
    BLAST
    Natural varianti775 – 7751I → N in HDLS; impairs autophosphorylation upon stimulation with CSF1. 1 Publication
    VAR_067404
    Natural varianti794 – 7941I → T in HDLS. 1 Publication
    VAR_067405
    Natural varianti837 – 8371D → Y in HDLS. 1 Publication
    VAR_067406
    Natural varianti849 – 8491F → S in HDLS. 1 Publication
    VAR_067407
    Natural varianti849 – 8491Missing in HDLS. 1 Publication
    VAR_067408
    Natural varianti868 – 8681L → P in HDLS. 1 Publication
    VAR_067409
    Natural varianti875 – 8751M → T in HDLS. 1 Publication
    VAR_067410
    Natural varianti878 – 8781P → T in HDLS. 1 Publication
    VAR_067411
    Natural varianti920 – 9201E → D.2 Publications
    Corresponds to variant rs34030164 [ dbSNP | Ensembl ].
    VAR_042043
    Natural varianti921 – 9211R → Q.1 Publication
    Corresponds to variant rs56059682 [ dbSNP | Ensembl ].
    VAR_042044
    Natural varianti969 – 9691Y → C.
    Corresponds to variant rs1801271 [ dbSNP | Ensembl ].
    VAR_011953

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei297 – 30610ESAYLNLSSE → GTPSPSLCPA in isoform 2. 1 PublicationVSP_047757
    Alternative sequencei307 – 972666Missing in isoform 2. 1 PublicationVSP_047758Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03663 mRNA. Translation: CAA27300.1.
    U63963 Genomic DNA. Translation: AAB51696.1.
    M25786 mRNA. Translation: AAA58421.1.
    EU826593 mRNA. Translation: ACF47629.1.
    AC011382 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61749.1.
    CH471062 Genomic DNA. Translation: EAW61750.1.
    BC047521 mRNA. Translation: AAH47521.1.
    M14002 Genomic DNA. Translation: AAA35849.1.
    U78096 Genomic DNA. Translation: AAB51235.1.
    M11067 Genomic DNA. Translation: AAA35848.1.
    M14193 mRNA. Translation: AAA35834.1.
    CCDSiCCDS4302.1. [P07333-1]
    PIRiS08123. TVHUMD.
    RefSeqiNP_001275634.1. NM_001288705.1. [P07333-1]
    NP_005202.2. NM_005211.3. [P07333-1]
    UniGeneiHs.586219.

    Genome annotation databases

    EnsembliENST00000286301; ENSP00000286301; ENSG00000182578. [P07333-1]
    ENST00000543093; ENSP00000445282; ENSG00000182578. [P07333-2]
    GeneIDi1436.
    KEGGihsa:1436.
    UCSCiuc003lrl.3. human. [P07333-1]

    Polymorphism databases

    DMDMi547770.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03663 mRNA. Translation: CAA27300.1 .
    U63963 Genomic DNA. Translation: AAB51696.1 .
    M25786 mRNA. Translation: AAA58421.1 .
    EU826593 mRNA. Translation: ACF47629.1 .
    AC011382 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61749.1 .
    CH471062 Genomic DNA. Translation: EAW61750.1 .
    BC047521 mRNA. Translation: AAH47521.1 .
    M14002 Genomic DNA. Translation: AAA35849.1 .
    U78096 Genomic DNA. Translation: AAB51235.1 .
    M11067 Genomic DNA. Translation: AAA35848.1 .
    M14193 mRNA. Translation: AAA35834.1 .
    CCDSi CCDS4302.1. [P07333-1 ]
    PIRi S08123. TVHUMD.
    RefSeqi NP_001275634.1. NM_001288705.1. [P07333-1 ]
    NP_005202.2. NM_005211.3. [P07333-1 ]
    UniGenei Hs.586219.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I0V X-ray 2.80 A 538-678 [» ]
    A 753-922 [» ]
    2I0Y X-ray 1.90 A 538-678 [» ]
    A 753-922 [» ]
    2I1M X-ray 1.80 A 538-678 [» ]
    A 753-922 [» ]
    2OGV X-ray 2.70 A 543-918 [» ]
    3BEA X-ray 2.02 A 538-678 [» ]
    A 753-922 [» ]
    3DPK X-ray 1.95 A 183-334 [» ]
    A 538-678 [» ]
    3KRJ X-ray 2.10 A 538-678 [» ]
    A 753-922 [» ]
    3KRL X-ray 2.40 A 538-678 [» ]
    A 753-922 [» ]
    3LCD X-ray 2.50 A 538-919 [» ]
    3LCO X-ray 3.40 A 550-919 [» ]
    4DKD X-ray 3.00 C 20-299 [» ]
    4HW7 X-ray 2.90 A 542-919 [» ]
    4LIQ X-ray 2.60 E 2-512 [» ]
    ProteinModelPortali P07333.
    SMRi P07333. Positions 20-498, 544-945.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107823. 18 interactions.
    DIPi DIP-59421N.
    IntActi P07333. 12 interactions.
    MINTi MINT-8019993.
    STRINGi 9606.ENSP00000286301.

    Chemistry

    BindingDBi P07333.
    ChEMBLi CHEMBL1844.
    DrugBanki DB00619. Imatinib.
    DB01268. Sunitinib.
    GuidetoPHARMACOLOGYi 1806.

    PTM databases

    PhosphoSitei P07333.

    Polymorphism databases

    DMDMi 547770.

    Proteomic databases

    PaxDbi P07333.
    PeptideAtlasi P07333.
    PRIDEi P07333.

    Protocols and materials databases

    DNASUi 1436.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286301 ; ENSP00000286301 ; ENSG00000182578 . [P07333-1 ]
    ENST00000543093 ; ENSP00000445282 ; ENSG00000182578 . [P07333-2 ]
    GeneIDi 1436.
    KEGGi hsa:1436.
    UCSCi uc003lrl.3. human. [P07333-1 ]

    Organism-specific databases

    CTDi 1436.
    GeneCardsi GC05M149413.
    GeneReviewsi CSF1R.
    HGNCi HGNC:2433. CSF1R.
    HPAi CAB008970.
    HPA012323.
    MIMi 164770. gene.
    221820. phenotype.
    neXtProti NX_P07333.
    Orphaneti 313808. Adult-onset leukoencephalopathy with axonal spheroids and pigmented glia.
    PharmGKBi PA26936.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000112008.
    HOVERGENi HBG004335.
    InParanoidi P07333.
    KOi K05090.
    OMAi VECVAFN.
    PhylomeDBi P07333.
    TreeFami TF325768.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    SignaLinki P07333.

    Miscellaneous databases

    ChiTaRSi CSF1R. human.
    EvolutionaryTracei P07333.
    GeneWikii Colony_stimulating_factor_1_receptor.
    GenomeRNAii 1436.
    NextBioi 35477774.
    PROi P07333.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07333.
    Bgeei P07333.
    CleanExi HS_CSF1R.
    Genevestigatori P07333.

    Family and domain databases

    Gene3Di 2.60.40.10. 5 hits.
    InterProi 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 ]
    Pfami PF00047. ig. 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. 3 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and structural organization of the human FMS proto-oncogene."
      Hampe A., Shamoon B.M., Gobet M., Sherr C.J., Galibert F.
      Oncogene Res. 4:9-17(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Structural alteration of viral homologue of receptor proto-oncogene fms at carboxyl terminus."
      Coussens L., van Beveren C., Smith D., Chen E., Mitchell R.L., Isacke C.M., Verma I.M., Ullrich A.
      Nature 320:277-280(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Sequence analysis of two genomic regions containing the KIT and the FMS receptor tyrosine kinase genes."
      Andre C., Hampe A., Lachaume P., Martin E., Wang X.P., Manus V., Hu W.X., Galibert F.
      Genomics 39:216-226(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    4. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
      Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
      Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Brain.
    8. "Differential transcription of exon 1 of the human c-fms gene in placental trophoblasts and monocytes."
      Visvader J., Verma I.M.
      Mol. Cell. Biol. 9:1336-1341(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
    9. "The amino-terminal domain of the v-fms oncogene product includes a functional signal peptide that directs synthesis of a transforming glycoprotein in the absence of feline leukemia virus gag sequences."
      Wheeler E.F., Roussel M.F., Hampe A., Walker M.H., Fried V.A., Look A.T., Rettenmier C.W., Sherr C.J.
      J. Virol. 59:224-233(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
    10. "Expression of a novel exon in the 5' UTR of human c-fms transcripts."
      Flick M.B., Sapi E., Kacinski B.M.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
      Tissue: Placenta.
    11. "Expression of the human c-fms proto-oncogene in hematopoietic cells and its deletion in the 5q- syndrome."
      Nienhuis A.W., Bunn H.F., Turner P.H., Gopal T.V., Nash W.G., O'Brien S.J., Sherr C.J.
      Cell 42:421-428(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-295.
    12. "'Replacement' of COOH-terminal truncation of v-fms with c-fms sequences markedly reduces transformation potential."
      Browning P.J., Bunn H.F., Cline A., Shuman M., Nienhuis A.W.
      Proc. Natl. Acad. Sci. U.S.A. 83:7800-7804(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 874-972 (ISOFORM 1).
    13. "Expression of human colony-stimulating factor-1 (CSF-1) receptor in murine pluripotent hematopoietic NFS-60 cells induces long-term proliferation in response to CSF-1 without loss of erythroid differentiation potential."
      Bourette R.P., Mouchiroud G., Ouazana R., Morle F., Godet J., Blanchet J.P.
      Blood 81:2511-2520(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL PROLIFERATION.
    14. "Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor."
      Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D., Roussel M.F.
      EMBO J. 12:943-950(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRC; FYN AND YES1, MUTAGENESIS OF TYR-809.
    15. "Transcriptional regulation of the c-fms (CSF-1R) proto-oncogene in human breast carcinoma cells by glucocorticoids."
      Sapi E., Flick M.B., Gilmore-Hebert M., Rodov S., Kacinski B.M.
      Oncogene 10:529-542(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY GLUCOCORTICOIDS.
    16. "Cell specific transformation by c-fms activating loop mutations is attributable to constitutive receptor degradation."
      Morley G.M., Uden M., Gullick W.J., Dibb N.J.
      Oncogene 18:3076-3084(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-708 AND ASP-802.
    17. "The inositol 5'-phosphatase SHIP-1 and the Src kinase Lyn negatively regulate macrophage colony-stimulating factor-induced Akt activity."
      Baran C.P., Tridandapani S., Helgason C.D., Humphries R.K., Krystal G., Marsh C.B.
      J. Biol. Chem. 278:38628-38636(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELLULAR SIGNALING; PHOSPHORYLATION OF INPP5D AND ACTIVATION OF AKT1.
    18. "Autocrine CSF-1R activation promotes Src-dependent disruption of mammary epithelial architecture."
      Wrobel C.N., Debnath J., Lin E., Beausoleil S., Roussel M.F., Brugge J.S.
      J. Cell Biol. 165:263-273(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF CELL PROLIFERATION; CELL ADHESION; CELL SHAPE AND INTEGRITY OF CELL JUNCTIONS, MUTAGENESIS OF LEU-301 AND TYR-969, ROLE IN DISEASE.
    19. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-302 AND ASN-353.
      Tissue: Plasma.
    20. "Inhibition of phosphorylation of the colony-stimulating factor-1 receptor (c-Fms) tyrosine kinase in transfected cells by ABT-869 and other tyrosine kinase inhibitors."
      Guo J., Marcotte P.A., McCall J.O., Dai Y., Pease L.J., Michaelides M.R., Davidsen S.K., Glaser K.B.
      Mol. Cancer Ther. 5:1007-1013(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS CSF1 RECEPTOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ROLE IN DISEASE, ENZYME REGULATION.
    21. "A c-fms tyrosine kinase inhibitor, Ki20227, suppresses osteoclast differentiation and osteolytic bone destruction in a bone metastasis model."
      Ohno H., Kubo K., Murooka H., Kobayashi Y., Nishitoba T., Shibuya M., Yoneda T., Isoe T.
      Mol. Cancer Ther. 5:2634-2643(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL PROLIFERATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ROLE IN DISEASE, ENZYME REGULATION.
    22. "FMS receptor for M-CSF (CSF-1) is sensitive to the kinase inhibitor imatinib and mutation of Asp-802 to Val confers resistance."
      Taylor J.R., Brownlow N., Domin J., Dibb N.J.
      Oncogene 25:147-151(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF CELL PROLIFERATION AND CELL SHAPE, CATALYTIC ACTIVITY, UBIQUITINATION, ENZYME REGULATION, MUTAGENESIS OF ASP-802.
    23. "Discovery of a cytokine and its receptor by functional screening of the extracellular proteome."
      Lin H., Lee E., Hestir K., Leo C., Huang M., Bosch E., Halenbeck R., Wu G., Zhou A., Behrens D., Hollenbaugh D., Linnemann T., Qin M., Wong J., Chu K., Doberstein S.K., Williams L.T.
      Science 320:807-811(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS IL34 RECEPTOR.
    24. "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: ROLE IN DISEASE, ENZYME REGULATION.
    25. "Invasion of human breast cancer cells in vivo requires both paracrine and autocrine loops involving the colony-stimulating factor-1 receptor."
      Patsialou A., Wyckoff J., Wang Y., Goswami S., Stanley E.R., Condeelis J.S.
      Cancer Res. 69:9498-9506(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN DISEASE.
    26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-699 AND SER-713, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Colony stimulating factor-1 receptor as a target for small molecule inhibitors."
      Mashkani B., Griffith R., Ashman L.K.
      Bioorg. Med. Chem. 18:1789-1797(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOPHOSPHORYLATION, ENZYME REGULATION.
    28. "IL-34 and M-CSF share the receptor Fms but are not identical in biological activity and signal activation."
      Chihara T., Suzu S., Hassan R., Chutiwitoonchai N., Hiyoshi M., Motoyoshi K., Kimura F., Okada S.
      Cell Death Differ. 17:1917-1927(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS RECEPTOR FOR IL34 AND CSF1, PHOSPHORYLATION AT TYR-546; TYR-699; TYR-708; TYR-723 AND TYR-809, AUTOPHOSPHORYLATION, ENZYME REGULATION, INTERACTION WITH IL34 AND CSF1.
    29. "Macrophage-colony stimulating factor and interleukin-34 induce chemokines in human whole blood."
      Eda H., Zhang J., Keith R.H., Michener M., Beidler D.R., Monahan J.B.
      Cytokine 52:215-220(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RELEASE OF PROINFLAMMATORY CHEMOKINES.
    30. "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; ACTIVATION OF MAPK1/ERK2; MAPK3/ERK1; PHOSPHORYLATION AT TYR-723, AUTOPHOSPHORYLATION.
    31. "CSF-1 regulation of the wandering macrophage: complexity in action."
      Pixley F.J., Stanley E.R.
      Trends Cell Biol. 14:628-638(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION; SIGNALING PATHWAYS AND PHOSPHORYLATION.
    32. "Colony-stimulating factor-1 in immunity and inflammation."
      Chitu V., Stanley E.R.
      Curr. Opin. Immunol. 18:39-48(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN IMMUNITY AND INFLAMMATION, ROLE IN DISEASE.
    33. "Macrophage colony stimulating factor: not just for macrophages anymore! A gateway into complex biologies."
      Douglass T.G., Driggers L., Zhang J.G., Hoa N., Delgado C., Williams C.C., Dan Q., Sanchez R., Jeffes E.W., Wepsic H.T., Myers M.P., Koths K., Jadus M.R.
      Int. Immunopharmacol. 8:1354-1376(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION; SIGNALING PATHWAYS AND PHOSPHORYLATION.
    34. "Blood monocytes: development, heterogeneity, and relationship with dendritic cells."
      Auffray C., Sieweke M.H., Geissmann F.
      Annu. Rev. Immunol. 27:669-692(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    35. "Crystal structure of the tyrosine kinase domain of colony-stimulating factor-1 receptor (cFMS) in complex with two inhibitors."
      Schubert C., Schalk-Hihi C., Struble G.T., Ma H.C., Petrounia I.P., Brandt B., Deckman I.C., Patch R.J., Player M.R., Spurlino J.C., Springer B.A.
      J. Biol. Chem. 282:4094-4101(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 538-922 IN COMPLEXES WITH ARYLAMIDE AND QUINOLONE INHIBITORS, DOMAIN.
    36. "The 2.7 A crystal structure of the autoinhibited human c-Fms kinase domain."
      Walter M., Lucet I.S., Patel O., Broughton S.E., Bamert R., Williams N.K., Fantino E., Wilks A.F., Rossjohn J.
      J. Mol. Biol. 367:839-847(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 543-918 IN AUTOINHIBITED CONFORMATION, DOMAIN.
    37. "Design and synthesis of a pyrido[2,3-d]pyrimidin-5-one class of anti-inflammatory FMS inhibitors."
      Huang H., Hutta D.A., Hu H., DesJarlais R.L., Schubert C., Petrounia I.P., Chaikin M.A., Manthey C.L., Player M.R.
      Bioorg. Med. Chem. Lett. 18:2355-2361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 538-922 IN COMPLEX WITH PYRIMIDINOPYRIDONE INHIBITOR, CATALYTIC ACTIVITY.
    38. "Pyrido[2,3-d]pyrimidin-5-ones: a novel class of antiinflammatory macrophage colony-stimulating factor-1 receptor inhibitors."
      Huang H., Hutta D.A., Rinker J.M., Hu H., Parsons W.H., Schubert C., DesJarlais R.L., Crysler C.S., Chaikin M.A., Donatelli R.R., Chen Y., Cheng D., Zhou Z., Yurkow E., Manthey C.L., Player M.R.
      J. Med. Chem. 52:1081-1099(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 538-922 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY, FUNCTION IN INFLAMMATION AND DISEASE.
    39. "Structure-based drug design enables conversion of a DFG-in binding CSF-1R kinase inhibitor to a DFG-out binding mode."
      Meyers M.J., Pelc M., Kamtekar S., Day J., Poda G.I., Hall M.K., Michener M.L., Reitz B.A., Mathis K.J., Pierce B.S., Parikh M.D., Mischke D.A., Long S.A., Parlow J.J., Anderson D.R., Thorarensen A.
      Bioorg. Med. Chem. Lett. 20:1543-1547(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 538-922 IN COMPLEXES WITH INHIBITORS, CATALYTIC ACTIVITY, ENZYME REGULATION.
    40. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-32; ARG-362; SER-413; VAL-536; HIS-693; ASP-920 AND GLN-921.
    41. Cited for: VARIANTS HDLS 774-CYS--ASN-814 DEL; 585-GLY--LYS-619 DELINS ALA; GLU-589; LYS-633; THR-766; PRO-770; ASN-775; THR-794; TYR-837; SER-849; PHE-849 DEL; PRO-868; THR-875 AND THR-878, VARIANTS HIS-710; ARG-747 AND ASP-920, CHARACTERIZATION OF VARIANTS HDLS LYS-633; THR-766 AND THR-875.

    Entry informationi

    Entry nameiCSF1R_HUMAN
    AccessioniPrimary (citable) accession number: P07333
    Secondary accession number(s): B5A955
    , D3DQG2, Q6LDW5, Q6LDY4, Q86VW7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 174 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3