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UniProtKB/Swiss-Prot entry P07333


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CSF1R_HUMAN
Primary accession number P07333
Secondary accession numbers Q6LDW5 Q6LDY4
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on June 1, 1994 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 118)
Name and origin of the protein
Protein name Macrophage colony-stimulating factor 1 receptor [Precursor]
Synonyms CSF-1-R
EC 2.7.10.1
Fms proto-oncogene
c-fms
CD115 antigen
Gene name
Name: CSF1R
Synonyms: FMS
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2524025 [NCBI, ExPASy, EBI, Israel, Japan]
Hampe A., Shamoon B.M., Gobet M., Sherr C.J., Galibert F.;
"Nucleotide sequence and structural organization of the human FMS proto-oncogene.";
Oncogene Res. 4:9-17(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/320277a0; PubMed=2421165 [NCBI, ExPASy, EBI, Israel, Japan]
Coussens L., van Beveren C., Smith D., Chen E., Mitchell R.L., Isacke C.M., Verma I.M., Ullrich A.;
"Structural alteration of viral homologue of receptor proto-oncogene fms at carboxyl terminus.";
Nature 320:277-280(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
DOI=10.1006/geno.1996.4482; PubMed=9027509 [NCBI, ExPASy, EBI, Israel, Japan]
Andre C., Hampe A., Lachaume P., Martin E., Wang X.P., Manus V., Hu W.X., Galibert F.;
"Sequence analysis of two genomic regions containing the KIT and the FMS receptor tyrosine kinase genes.";
Genomics 39:216-226(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
PubMed=2524648 [NCBI, ExPASy, EBI, Israel, Japan]
Visvader J., Verma I.M.;
"Differential transcription of exon 1 of the human c-fms gene in placental trophoblasts and monocytes.";
Mol. Cell. Biol. 9:1336-1341(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
PubMed=3525854 [NCBI, ExPASy, EBI, Israel, Japan]
Wheeler E.F., Roussel M.F., Hampe A., Walker M.H., Fried V.A., Look A.T., Rettenmier C.W., Sherr C.J.;
"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.";
J. Virol. 59:224-233(1986).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
TISSUE=Placenta;
Flick M.B., Sapi E., Kacinski B.M.;
"Expression of a novel exon in the 5' UTR of human c-fms transcripts.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-295.
DOI=10.1016/0092-8674(85)90099-6; PubMed=4028159 [NCBI, ExPASy, EBI, Israel, Japan]
Nienhuis A.W., Bunn H.F., Turner P.H., Gopal T.V., Nash W.G., O'Brien S.J., Sherr C.J.;
"Expression of the human c-fms proto-oncogene in hematopoietic cells and its deletion in the 5q- syndrome.";
Cell 42:421-428(1985).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 874-972.
DOI=10.1073/pnas.83.20.7800; PubMed=3532121 [NCBI, ExPASy, EBI, Israel, Japan]
Browning P.J., Bunn H.F., Cline A., Shuman M., Nienhuis A.W.;
"'Replacement' of COOH-terminal truncation of v-fms with c-fms sequences markedly reduces transformation potential.";
Proc. Natl. Acad. Sci. U.S.A. 83:7800-7804(1986).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-302 AND ASN-353, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555; TYR-556; THR-562 AND THR-567, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[11]
FUNCTION AS IL34 RECEPTOR.
DOI=10.1126/science.1154370; PubMed=18467591 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Discovery of a cytokine and its receptor by functional screening of the extracellular proteome.";
Science 320:807-811(2008).
[12]
VARIANTS [LARGE SCALE ANALYSIS] GLY-32; ARG-362; SER-413; VAL-536; HIS-693; ASP-920 AND GLN-921.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X03663; CAA27300.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U63963; AAB51696.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M25786; AAA58421.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14002; AAA35849.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U78096; AAB51235.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11067; AAA35848.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14193; AAA35834.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00011218; -.
PIR S08123; TVHUMD.
RefSeq NP_005202.2; -.
UniGene Hs.586219
3D structure databases
PDB
2I0V; X-ray; 2.80 A; A=538-922.[ExPASy / RCSB / EBI]
2I0Y; X-ray; 1.90 A; A=538-922.[ExPASy / RCSB / EBI]
2I1M; X-ray; 1.80 A; A=538-922.[ExPASy / RCSB / EBI]
2OGV; X-ray; 2.70 A; A=543-918.[ExPASy / RCSB / EBI]
3BEA; X-ray; 2.02 A; A=538-922.[ExPASy / RCSB / EBI]
3DPK; X-ray; 1.95 A; A=538-922.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2I0V; -.
2I0Y; -.
2I1M; -.
2OGV; -.
3BEA; -.
3DPK; -.
ModBase P07333.
PTM databases
PhosphoSite P07333; -.
Enzyme and pathway databases
BRENDA 2.7.10.1; 247.
Pathway_Interaction_DB avb3_integrin_pathway; Integrins in angiogenesis.
ptp1bpathway; Signaling events mediated by PTP1B.
Organism-specific databases
GeneCards GC05M149413; -.
HGNC HGNC:2433; CSF1R.
GenAtlas CSF1R.
HPA CAB008970; -.
HPA012323; -.
MIM 164770; gene. [NCBI / EBI]
PharmGKB PA26936; -.
Gene expression databases
Bgee P07333; -.
CleanEx HS_CSF1R; -.
GermOnline ENSG00000182578; Homo sapiens.
Ontologies
GO
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0043235; Cellular component: receptor complex (inferred from sequence or structural similarity from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019955; Molecular function: cytokine binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005011; Molecular function: macrophage colony stimulating factor receptor activity (traceable author statement from ProtInc).
GO:0042803; Molecular function: protein homodimerization activity (inferred from sequence or structural similarity from UniProtKB).
GO:0008283; Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0007275; Biological process: multicellular organismal development (traceable author statement from ProtInc).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0007169; Biological process: transmembrane receptor protein tyrosine kinase signaling pathway (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013151; 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 of domain structure.
Gene3D G3DSA:2.60.40.10; Ig-like_fold; 3.
Pfam PF00047; ig; 2.
PF07714; Pkinase_Tyr; 1.
PF07686; V-set; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000615; TyrPK_CSF1-R; 1.
ProDom PD000001; Prot_kinase; 2.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00409; IG; 3.
SM00408; IGc2; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS50835; IG_LIKE; 3.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS00240; RECEPTOR_TYR_KIN_III; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P07333; -.
PRIDE P07333; -.
Genome annotation databases
Ensembl ENSG00000182578; Homo sapiens. [Contig view]
GeneID 1436; -.
KEGG hsa:1436; -.
Phylogenomic databases
HOGENOM P07333; -.
HOVERGEN P07333; -.
OMA P07333; KEDAVLK.
Other
DrugBank DB00619; Imatinib.
DB01268; Sunitinib.
NextBio 5867; -.
SOURCE CSF1R; Homo sapiens.
ProtoNet P07333.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Proto-oncogene; Receptor; Repeat; Signal; Transferase; Transmembrane; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    19  19     Potential. 
CHAIN   20   972  953     Macrophage colony-stimulating factor 1 receptor. PRO_0000016765
TOPO_DOM   20   512  493     Extracellular (Potential). 
TRANSMEM   513   537  25     Potential. 
TOPO_DOM   538   972  435     Cytoplasmic (Potential). 
DOMAIN   21   104  84     Ig-like C2-type 1. 
DOMAIN   107   197  91     Ig-like C2-type 2. 
DOMAIN   203   290  88     Ig-like C2-type 3. 
DOMAIN   299   399  101     Ig-like C2-type 4. 
DOMAIN   402   502  101     Ig-like C2-type 5. 
DOMAIN   582   910  329     Protein kinase. 
NP_BIND   588   596  9     ATP (By similarity). 
ACT_SITE   778   778        Proton acceptor (By similarity). 
BINDING   616   616        ATP (By similarity). 
MOD_RES   555   555        Phosphoserine. 
MOD_RES   556   556        Phosphotyrosine. 
MOD_RES   562   562        Phosphothreonine. 
MOD_RES   567   567        Phosphothreonine. 
MOD_RES   699   699        Phosphotyrosine; by autocatalysis (By similarity). 
MOD_RES   708   708        Phosphotyrosine; by autocatalysis (By similarity). 
MOD_RES   716   716        Phosphoserine (By similarity). 
MOD_RES   809   809        Phosphotyrosine; by autocatalysis (By similarity). 
CARBOHYD   45    45        N-linked (GlcNAc...) (Potential). 
CARBOHYD   73    73        N-linked (GlcNAc...) (Potential). 
CARBOHYD   153   153        N-linked (GlcNAc...) (Potential). 
CARBOHYD   240   240        N-linked (GlcNAc...) (Potential). 
CARBOHYD   275   275        N-linked (GlcNAc...) (Potential). 
CARBOHYD   302   302        N-linked (GlcNAc...). 
CARBOHYD   335   335        N-linked (GlcNAc...) (Potential). 
CARBOHYD   353   353        N-linked (GlcNAc...). 
CARBOHYD   412   412        N-linked (GlcNAc...) (Potential). 
CARBOHYD   428   428        N-linked (GlcNAc...) (Potential). 
CARBOHYD   480   480        N-linked (GlcNAc...) (Potential). 
DISULFID   42    84        Potential. 
DISULFID   127   177        Potential. 
DISULFID   224   278        Potential. 
DISULFID   419   485        Potential. 
VARIANT   32    32  1     V -> G. VAR_042038 
VARIANT   279   279  1     V -> M (in dbSNP:rs3829986 [NCBI]). VAR_049718 
VARIANT   362   362  1     H -> R (in dbSNP:rs10079250 [NCBI]). VAR_042039 
VARIANT   413   413  1     G -> S. VAR_042040 
VARIANT   536   536  1     L -> V. VAR_042041 
VARIANT   693   693  1     P -> H (in a lung squamous cell carcinoma sample; somatic mutation). VAR_042042 
VARIANT   920   920  1     E -> D (in dbSNP:rs34030164 [NCBI]). VAR_042043 
VARIANT   921   921  1     R -> Q. VAR_042044 
VARIANT   969   969  1     Y -> C (in dbSNP:rs1801271 [NCBI]). VAR_011953 
CONFLICT   54    54        P -> A (in Ref. 2; CAA27300). 
HELIX   579   581  3      
STRAND   582   590  9      
STRAND   592   604  13      
TURN   605   608  4      
STRAND   612   618  7      
HELIX   624   640  17      
STRAND   649   653  5      
STRAND   655   658  4      
STRAND   660   664  5      
HELIX   671   676  6      
HELIX   752   771  20      
HELIX   781   783  3      
STRAND   784   786  3      
HELIX   788   790  3      
STRAND   792   794  3      
HELIX   798   800  3      
STRAND   809   811  3      
HELIX   819   821  3      
HELIX   824   828  5      
HELIX   834   849  16      
HELIX   863   871  9      
HELIX   883   892  10      
HELIX   897   899  3      
HELIX   903   911  9      
HELIX   917   920  4      
Sequence information
Length: 972 AA [This is the length of the unprocessed precursor] Molecular weight: 107984 Da [This is the MW of the unprocessed precursor] CRC64: A8D99BE237573FE8 [This is a checksum on the sequence]
        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 

P07333 in FASTA format

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