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P07333

- CSF1R_HUMAN

UniProt

P07333 - CSF1R_HUMAN

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Protein
Macrophage colony-stimulating factor 1 receptor
Gene
CSF1R, FMS
Organism
Homo sapiens (Human)
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.14 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.6 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 GW2580.7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei616 – 6161ATP Inferred
Active sitei778 – 7781Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi588 – 5969ATP 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 homodimerization activity Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. cell-cell junction maintenance 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 metabolic process Source: UniProtKB
  17. phosphatidylinositol-mediated signaling Source: UniProtKB
  18. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  19. positive regulation of cell migration Source: UniProtKB
  20. positive regulation of cell motility Source: UniProtKB
  21. positive regulation of cell proliferation Source: UniProtKB
  22. positive regulation of chemokine secretion 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
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. 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 517498Extracellular Reviewed prediction
Add
BLAST
Transmembranei518 – 53821Helical; Reviewed prediction
Add
BLAST
Topological domaini539 – 972434Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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.6 Publications
Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.6 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.7 Publications
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 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 972953Macrophage colony-stimulating factor 1 receptor
PRO_0000016765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 84 By similarity
Glycosylationi45 – 451N-linked (GlcNAc...) Reviewed prediction
Glycosylationi73 – 731N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi127 ↔ 177 By similarity
Glycosylationi153 – 1531N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi224 ↔ 278 By similarity
Glycosylationi240 – 2401N-linked (GlcNAc...) Reviewed prediction
Glycosylationi275 – 2751N-linked (GlcNAc...) Reviewed prediction
Glycosylationi302 – 3021N-linked (GlcNAc...)1 Publication
Glycosylationi335 – 3351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi353 – 3531N-linked (GlcNAc...)1 Publication
Glycosylationi412 – 4121N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi419 ↔ 485 By similarity
Glycosylationi428 – 4281N-linked (GlcNAc...) Reviewed prediction
Glycosylationi480 – 4801N-linked (GlcNAc...) Reviewed prediction
Modified residuei546 – 5461Phosphotyrosine; by autocatalysis1 Publication
Modified residuei561 – 5611Phosphotyrosine; by autocatalysis By similarity
Modified residuei699 – 6991Phosphotyrosine; by autocatalysis2 Publications
Modified residuei708 – 7081Phosphotyrosine; by autocatalysis1 Publication
Modified residuei713 – 7131Phosphoserine1 Publication
Modified residuei723 – 7231Phosphotyrosine; by autocatalysis2 Publications
Modified residuei809 – 8091Phosphotyrosine; by autocatalysis1 Publication
Modified residuei923 – 9231Phosphotyrosine; by autocatalysis By similarity
Modified residuei969 – 9691Phosphotyrosine; by autocatalysis By 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.5 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.8 Publications

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 SLA2.2 Publications

Protein-protein interaction databases

BioGridi107823. 18 interactions.
DIPiDIP-59421N.
IntActiP07333. 9 interactions.
MINTiMINT-8019993.
STRINGi9606.ENSP00000286301.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP07333.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni542 – 57433Regulatory juxtamembrane domain
Add
BLAST
Regioni796 – 81823Activation loop
Add
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.2 Publications
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.2 Publications

Sequence similaritiesi

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

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.
VSP_047757
Alternative sequencei307 – 972666Missing in isoform 2.
VSP_047758Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541P → A in CAA27300. 1 Publication
Sequence conflicti247 – 2471P → H in AAH47521. 1 Publication
Sequence conflicti354 – 3541A → V in AAH47521. 1 Publication
Sequence conflicti629 – 6291A → S in AAH47521. 1 Publication

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...

Protein-protein interaction databases

BioGridi 107823. 18 interactions.
DIPi DIP-59421N.
IntActi P07333. 9 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 173 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

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