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Reviewed, UniProtKB/Swiss-Prot P07333 (CSF1R_HUMAN)

Last modified June 16, 2009. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Macrophage colony-stimulating factor 1 receptor
      Short name=CSF-1-R
    EC=2.7.10.1
Alternative name(s):
    Fms proto-oncogene
    c-fms
    CD_antigen=CD115
Gene names
Name: CSF1R
Synonyms: FMS
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length972 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Protein tyrosine-kinase transmembrane receptor for CSF1 and IL34. Ref.11

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Interacts with INPPL1/SHIP2 and THOC5 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in bone marrow and in differentiated blood mononuclear cells.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 972953Macrophage colony-stimulating factor 1 receptor
PRO_0000016765

Regions

Topological domain20 – 512493Extracellular Potential
Transmembrane513 – 53725 Potential
Topological domain538 – 972435Cytoplasmic Potential
Domain21 – 10484Ig-like C2-type 1
Domain107 – 19791Ig-like C2-type 2
Domain203 – 29088Ig-like C2-type 3
Domain299 – 399101Ig-like C2-type 4
Domain402 – 502101Ig-like C2-type 5
Domain582 – 910329Protein kinase
Nucleotide binding588 – 5969ATP By similarity

Sites

Active site7781Proton acceptor By similarity
Binding site6161ATP By similarity

Amino acid modifications

Modified residue5551Phosphoserine Ref.10
Modified residue5561Phosphotyrosine Ref.10
Modified residue5621Phosphothreonine Ref.10
Modified residue5671Phosphothreonine Ref.10
Modified residue6991Phosphotyrosine; by autocatalysis By similarity
Modified residue7081Phosphotyrosine; by autocatalysis By similarity
Modified residue7161Phosphoserine By similarity
Modified residue8091Phosphotyrosine; by autocatalysis By similarity
Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Ref.9
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Ref.9
Glycosylation4121N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 84 Potential
Disulfide bond127 ↔ 177 Potential
Disulfide bond224 ↔ 278 Potential
Disulfide bond419 ↔ 485 Potential

Natural variations

Natural variant321V → G Ref.12
VAR_042038
Natural variant2791V → M: dbSNP rs3829986.
VAR_049718
Natural variant3621H → R: dbSNP rs10079250. Ref.12
VAR_042039
Natural variant4131G → S Ref.12
VAR_042040
Natural variant5361L → V Ref.12
VAR_042041
Natural variant6931P → H in a lung squamous cell carcinoma sample; somatic mutation. Ref.12
VAR_042042
Natural variant9201E → D: dbSNP rs34030164. Ref.12
VAR_042043
Natural variant9211R → Q Ref.12
VAR_042044
Natural variant9691Y → C: dbSNP rs1801271.
VAR_011953

Experimental info

Sequence conflict541P → A in CAA27300. Ref.2

Secondary structure

................................................ 972
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07333-1 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: A8D99BE237573FE8

FASTA972107,984
        10         20         30         40         50         60 
MGPGVLLLLL VATAWHGQGI PVIEPSVPEL VVKPGATVTL RCVGNGSVEW DGPPSPHWTL 

        70         80         90        100        110        120 
YSDGSSSILS TNNATFQNTG TYRCTEPGDP LGGSAAIHLY VKDPARPWNV LAQEVVVFED 

       130        140        150        160        170        180 
QDALLPCLLT DPVLEAGVSL VRVRGRPLMR HTNYSFSPWH GFTIHRAKFI QSQDYQCSAL 

       190        200        210        220        230        240 
MGGRKVMSIS IRLKVQKVIP GPPALTLVPA ELVRIRGEAA QIVCSASSVD VNFDVFLQHN 

       250        260        270        280        290        300 
NTKLAIPQQS DFHNNRYQKV LTLNLDQVDF QHAGNYSCVA SNVQGKHSTS MFFRVVESAY 

       310        320        330        340        350        360 
LNLSSEQNLI QEVTVGEGLN LKVMVEAYPG LQGFNWTYLG PFSDHQPEPK LANATTKDTY 

       370        380        390        400        410        420 
RHTFTLSLPR LKPSEAGRYS FLARNPGGWR ALTFELTLRY PPEVSVIWTF INGSGTLLCA 

       430        440        450        460        470        480 
ASGYPQPNVT WLQCSGHTDR CDEAQVLQVW DDPYPEVLSQ EPFHKVTVQS LLTVETLEHN 

       490        500        510        520        530        540 
QTYECRAHNS VGSGSWAFIP ISAGAHTHPP DEFLFTPVVV ACMSIMALLL LLLLLLLYKY 

       550        560        570        580        590        600 
KQKPKYQVRW KIIESYEGNS YTFIDPTQLP YNEKWEFPRN NLQFGKTLGA GAFGKVVEAT 

       610        620        630        640        650        660 
AFGLGKEDAV LKVAVKMLKS TAHADEKEAL MSELKIMSHL GQHENIVNLL GACTHGGPVL 

       670        680        690        700        710        720 
VITEYCCYGD LLNFLRRKAE AMLGPSLSPG QDPEGGVDYK NIHLEKKYVR RDSGFSSQGV 

       730        740        750        760        770        780 
DTYVEMRPVS TSSNDSFSEQ DLDKEDGRPL ELRDLLHFSS QVAQGMAFLA SKNCIHRDVA 

       790        800        810        820        830        840 
ARNVLLTNGH VAKIGDFGLA RDIMNDSNYI VKGNARLPVK WMAPESIFDC VYTVQSDVWS 

       850        860        870        880        890        900 
YGILLWEIFS LGLNPYPGIL VNSKFYKLVK DGYQMAQPAF APKNIYSIMQ ACWALEPTHR 

       910        920        930        940        950        960 
PTFQQICSFL QEQAQEDRRE RDYTNLPSSS RSGGSGSSSS ELEEESSSEH LTCCEQGDIA 

       970 
QPLLQPNNYQ FC 

« Hide

References

« Hide 'large scale' references
[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: 2524025] [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: 2421165] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 9027509] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[4]"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: 2524648] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[5]"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: 3525854] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[6]"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.
[7]"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: 4028159] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-295.
[8]"'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: 3532121] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 874-972.
[9]"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: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-302 AND ASN-353, MASS SPECTROMETRY.
Tissue: Plasma.
[10]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555; TYR-556; THR-562 AND THR-567, MASS SPECTROMETRY.
[11]"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: 18467591] [Abstract]
Cited for: FUNCTION AS IL34 RECEPTOR.
[12]"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. expand/collapse author list , 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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-32; ARG-362; SER-413; VAL-536; HIS-693; ASP-920 AND GLN-921.
+Additional computationally mapped references.

Cross-references

Sequence databases

X03663 mRNA. Translation: CAA27300.1.
U63963 Genomic DNA. Translation: AAB51696.1.
M25786 mRNA. Translation: AAA58421.1.
M14002 Genomic DNA. Translation: AAA35849.1.
U78096 Genomic DNA. Translation: AAB51235.1.
M11067 Genomic DNA. Translation: AAA35848.1.
M14193 mRNA. Translation: AAA35834.1.
IPIIPI00011218.
PIRTVHUMD. S08123.
RefSeqNP_005202.2.
UniGeneHs.586219
Hs.654394

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2I0VX-ray2.80A538-922[»]
2I0YX-ray1.90A538-922[»]
2I1MX-ray1.80A538-922[»]
2OGVX-ray2.70A543-918[»]
3BEAX-ray2.02A538-922[»]
3DPKX-ray1.95A538-922[»]
ModBaseSearch...

PTM databases

PhosphoSiteP07333.

Proteomic databases

PeptideAtlasP07333.
PRIDEP07333.

Genome annotation databases

EnsemblENSG00000182578. Homo sapiens. [Contig view]
GeneID1436.
KEGGhsa:1436.

Organism-specific databases

GeneCardsGC05M149413.
HGNCHGNC:2433. CSF1R.
HPACAB008970.
HPA012323.
MIM164770. gene.
PharmGKBPA26936.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP07333.
HOVERGENP07333.
OMAP07333. KEDAVLK.

Enzyme and pathway databases

BRENDA2.7.10.1. 247.
Pathway_Interaction_DBavb3_integrin_pathway. Integrins in angiogenesis.
ptp1bpathway. Signaling events mediated by PTP1B.

Gene expression databases

BgeeP07333.
CleanExHS_CSF1R.
GermOnlineENSG00000182578. Homo sapiens.

Family and domain databases

InterProIPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001824. Recept_tyr_kinase-III_CS.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
IPR016243. TyrPK_CSF1-R.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 3 hits.
PfamPF00047. ig. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PIRSFPIRSF000615. TyrPK_CSF1-R. 1 hit.
ProDomPD000001. Prot_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00409. IG. 3 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS50835. 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]
ProtoNetSearch...

Other Resources

DrugBankDB00619. Imatinib.
DB01268. Sunitinib.
NextBio5867.
SOURCESearch...

Entry information

Entry nameCSF1R_HUMAN
AccessionPrimary (citable) accession number: P07333
Secondary accession number(s): Q6LDW5, Q6LDY4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 1, 1994
Last modified: June 16, 2009
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents