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P09603 (CSF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Macrophage colony-stimulating factor 1

Short name=CSF-1
Short name=M-CSF
Short name=MCSF
Alternative name(s):
Lanimostim

Cleaved into the following chain:

  1. Processed macrophage colony-stimulating factor 1
Gene names
Name:CSF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytokine that 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, 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 development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance. Ref.19 Ref.21 Ref.22 Ref.23

Subunit structure

Homodimer or heterodimer; disulfide-linked. Interacts with CSF1R. Ref.15 Ref.16 Ref.17 Ref.23

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.15 Ref.16.

Processed macrophage colony-stimulating factor 1: Secretedextracellular space Ref.15 Ref.16.

Post-translational modification

N- and O-glycosylated. Glycosylation and proteolytic cleavage yield different soluble forms. One high molecular weight soluble form is a proteoglycan containing chondroitin sulfate. O-glycosylated with core 1 or possibly core 8 glycans. Isoform 1 is N- and O-glycosylated. Isoform 3 is only N-glycosylated. Ref.15 Ref.16 Ref.24 Ref.25

Involvement in disease

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. Ref.19 Ref.21

Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection. Ref.19 Ref.21

Ontologies

Keywords
   Biological processImmunity
Inflammatory response
Innate immunity
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionCytokine
Growth factor
   PTMDisulfide bond
Glycoprotein
Proteoglycan
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbranching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Non-traceable author statement Ref.10. Source: UniProtKB

cell proliferation

Non-traceable author statement Ref.10. Source: UniProtKB

developmental process involved in reproduction

Inferred from sequence or structural similarity PubMed 19017797. Source: BHF-UCL

hemopoiesis

Non-traceable author statement Ref.10. Source: UniProtKB

homeostasis of number of cells within a tissue

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

macrophage differentiation

Traceable author statement Ref.3. Source: UniProtKB

mammary duct terminal end bud growth

Inferred from electronic annotation. Source: Ensembl

mammary gland fat development

Inferred from electronic annotation. Source: Ensembl

monocyte activation

Non-traceable author statement PubMed 18566389. Source: BHF-UCL

odontogenesis

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from electronic annotation. Source: Ensembl

osteoclast differentiation

Inferred from direct assay PubMed 18606301. Source: BHF-UCL

osteoclast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of Ras protein signal transduction

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from sequence or structural similarity PubMed 18566389. Source: BHF-UCL

positive regulation of cell proliferation

Traceable author statement Ref.3. Source: UniProtKB

positive regulation of cell-matrix adhesion

Inferred from sequence or structural similarity PubMed 18566389. Source: BHF-UCL

positive regulation of cellular protein metabolic process

Inferred from direct assay PubMed 1739124. Source: BHF-UCL

positive regulation of gene expression

Inferred from direct assay PubMed 10666185PubMed 1739124. Source: BHF-UCL

positive regulation of macrophage derived foam cell differentiation

Inferred from direct assay PubMed 17244792. Source: BHF-UCL

positive regulation of macrophage differentiation

Inferred from direct assay Ref.3. Source: BHF-UCL

positive regulation of monocyte differentiation

Inferred from sequence or structural similarity PubMed 18566389. Source: BHF-UCL

positive regulation of mononuclear cell proliferation

Inferred from direct assay Ref.3. Source: BHF-UCL

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoclast differentiation

Inferred from direct assay PubMed 15304486. Source: BHF-UCL

positive regulation of protein kinase activity

Inferred from sequence or structural similarity PubMed 18566389. Source: BHF-UCL

regulation of macrophage derived foam cell differentiation

Non-traceable author statement PubMed 18566389. Source: BHF-UCL

regulation of ossification

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular space

Inferred from direct assay Ref.3. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Non-traceable author statement Ref.3. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 1739124. Source: BHF-UCL

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

receptor complex

Inferred from sequence or structural similarity PubMed 19017797. Source: BHF-UCL

   Molecular_functioncytokine activity

Inferred from direct assay Ref.3. Source: BHF-UCL

growth factor activity

Non-traceable author statement Ref.10. Source: UniProtKB

macrophage colony-stimulating factor receptor binding

Traceable author statement Ref.3. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 3264878. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P09603-1)

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.
Isoform 2 (identifier: P09603-2)

The sequence of this isoform differs from the canonical sequence as follows:
     365-480: Missing.
Isoform 3 (identifier: P09603-3)

The sequence of this isoform differs from the canonical sequence as follows:
     182-479: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Ref.1 Ref.11 Ref.12
Chain33 – 554522Macrophage colony-stimulating factor 1
PRO_0000005857
Chain33 – ?Processed macrophage colony-stimulating factor 1PRO_0000296231

Regions

Topological domain33 – 496464Lumenal Potential
Transmembrane497 – 51721Helical; Potential
Topological domain518 – 55437Cytoplasmic Potential
Region406 – 42621O-glycosylated at one site

Amino acid modifications

Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation3631O-linked (GalNAc...) Ref.24
Glycosylation3651O-linked (GalNAc...) Ref.24
Disulfide bond39 ↔ 122 Ref.17
Disulfide bond63Interchain Ref.17
Disulfide bond80 ↔ 171 Ref.17
Disulfide bond134 ↔ 178 Ref.17
Disulfide bond189Interchain Ref.17
Disulfide bond191Interchain Ref.17

Natural variations

Alternative sequence182 – 479298Missing in isoform 3.
VSP_001187
Alternative sequence365 – 480116Missing in isoform 2.
VSP_001188
Natural variant3411S → N.
Corresponds to variant rs12565736 [ dbSNP | Ensembl ].
VAR_048810
Natural variant4081L → P. Ref.4
Corresponds to variant rs1058885 [ dbSNP | Ensembl ].
VAR_020454
Natural variant4381G → R.
Corresponds to variant rs2229165 [ dbSNP | Ensembl ].
VAR_029320
Natural variant4891F → S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10
Corresponds to variant rs333971 [ dbSNP | Ensembl ].
VAR_048811
Natural variant4961S → F.
Corresponds to variant rs12721516 [ dbSNP | Ensembl ].
VAR_020455
Natural variant5311A → V.
Corresponds to variant rs2229167 [ dbSNP | Ensembl ].
VAR_022146

Experimental info

Mutagenesis489 – 55466Missing: Produces biologically active protein which is secreted. Ref.3
Sequence conflict691F → S AA sequence Ref.12
Sequence conflict911D → Y in AAB59527. Ref.1
Sequence conflict911D → Y in AAA59572. Ref.3
Sequence conflict911D → Y in AAA64849. Ref.3
Sequence conflict911D → Y in AAA52120. Ref.10
Sequence conflict104 – 1063PNA → ANP in AAA52117. Ref.2
Sequence conflict3641G → A in AAA52117. Ref.2
Sequence conflict3741R → M in AAA52117. Ref.2
Sequence conflict4121G → A in AAA52117. Ref.2
Sequence conflict4501R → T in AAA52117. Ref.2
Sequence conflict457 – 4582GG → AA in AAA52117. Ref.2
Sequence conflict4801Missing in AAA59573. Ref.4

Secondary structure

........................ 554
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: 656B0894F9255AED

FASTA55460,179
        10         20         30         40         50         60 
MTAPGAAGRC PPTTWLGSLL LLVCLLASRS ITEEVSEYCS HMIGSGHLQS LQRLIDSQME 

        70         80         90        100        110        120 
TSCQITFEFV DQEQLKDPVC YLKKAFLLVQ DIMEDTMRFR DNTPNAIAIV QLQELSLRLK 

       130        140        150        160        170        180 
SCFTKDYEEH DKACVRTFYE TPLQLLEKVK NVFNETKNLL DKDWNIFSKN CNNSFAECSS 

       190        200        210        220        230        240 
QDVVTKPDCN CLYPKAIPSS DPASVSPHQP LAPSMAPVAG LTWEDSEGTE GSSLLPGEQP 

       250        260        270        280        290        300 
LHTVDPGSAK QRPPRSTCQS FEPPETPVVK DSTIGGSPQP RPSVGAFNPG MEDILDSAMG 

       310        320        330        340        350        360 
TNWVPEEASG EASEIPVPQG TELSPSRPGG GSMQTEPARP SNFLSASSPL PASAKGQQPA 

       370        380        390        400        410        420 
DVTGTALPRV GPVRPTGQDW NHTPQKTDHP SALLRDPPEP GSPRISSLRP QGLSNPSTLS 

       430        440        450        460        470        480 
AQPQLSRSHS SGSVLPLGEL EGRRSTRDRR SPAEPEGGPA SEGAARPLPR FNSVPLTDTG 

       490        500        510        520        530        540 
HERQSEGSFS PQLQESVFHL LVPSVILVLL AVGGLLFYRW RRRSHQEPQR ADSPLEQPEG 

       550 
SPLTQDDRQV ELPV 

« Hide

Isoform 2 [UniParc].

Checksum: 1B6A3CDBE1C06775
Show »

FASTA43847,903
Isoform 3 [UniParc].

Checksum: 0656D858DE1A4086
Show »

FASTA25629,215

References

« Hide 'large scale' references
[1]"Molecular cloning of a complementary DNA encoding human macrophage-specific colony-stimulating factor (CSF-1)."
Kawasaki E.S., Ladner M.B., Wang A.M., van Arsdell J.N., Warren M.K., Coyne M.Y., Schweickart V.L., Lee M.-T., Wilson K.J., Boosman A., Stanley E.R., Ralph P., Mark D.F.
Science 230:291-296(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-44 (ISOFORM 3), VARIANT SER-489.
Tissue: Pancreatic carcinoma and Urine.
[2]"Human CSF-1: molecular cloning and expression of 4-kb cDNA encoding the human urinary protein."
Wong G.G., Temple P.A., Leary A.C., Witek-Giannotti J.S., Yang Y.C., Ciarletta A.B., Chung M., Murtha P., Kriz R., Kaufman R.J., Ferenz C.R., Sibley B.S., Turner K.J., Hewick R.M., Clark S.C., Yanai N., Yokota H., Yamada M. expand/collapse author list , Saito M., Motoyoshi K., Takaku F.
Science 235:1504-1508(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT SER-489.
Tissue: Trophoblast and Urine.
[3]"Human macrophage-colony stimulating factor: alternative RNA and protein processing from a single gene."
Cerretti D.P., Wignall J., Anderson D., Tushinski R.J., Gallis B.M., Stya M., Gillis S., Urdal D.L., Cosman D.
Mol. Immunol. 25:761-770(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, MUTAGENESIS OF ISOFORM 3, VARIANT SER-489.
Tissue: Pancreatic carcinoma.
[4]"Amino-terminal region of human macrophage colony-stimulating factor (M-CSF) is sufficient for its in vitro biological activity: molecular cloning and expression of carboxyl-terminal deletion mutants of human M-CSF."
Takahashi M., Hirato T., Takano M., Nishida T., Nagamura K., Kamogashira T., Nakai S., Hirai Y.
Biochem. Biophys. Res. Commun. 161:892-901(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PRO-408 AND SER-489.
Tissue: T lymphoblast.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-489.
Tissue: Placenta.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-489.
[8]"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), VARIANT SER-489.
Tissue: Kidney.
[9]"Human CSF-1: gene structure and alternative splicing of mRNA precursors."
Ladner M.B., Martin G.A., Noble J.A., Nikoloff D.M., Tal R., Kawasaki E.S., White T.J.
EMBO J. 6:2693-2698(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-13 AND 19-554 (ISOFORM 1), VARIANT SER-489.
Tissue: Pancreatic carcinoma.
[10]"Expression of colony-stimulating factor-1 (CSF-1) messenger RNA in human endometrial glands during the menstrual cycle: molecular cloning of a novel transcript that predicts a cell surface form of CSF-1."
Pampfer S., Tabibzadeh S., Chuan F.-C., Pollard J.W.
Mol. Endocrinol. 5:1931-1938(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-554 (ISOFORM 3), VARIANT SER-489.
Tissue: Endometrium.
[11]"The structure of recombinant human carboxy-terminal-truncated macrophage colony-stimulating factor derived from mammalian cells."
Yamanishi K., Yasuda S., Masui Y., Nishida T., Shindo Y., Takano M., Ohmoto Y., Takahashi M., Adachi M.
J. Biochem. 114:255-262(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-185 (ISOFORM 1).
Tissue: T lymphoblast.
[12]"Macrophage colony-stimulating factor purified from normal human urine. Amino-terminal sequence and amino acid composition."
Sakai N., Umeda T., Suzuki H., Ishimatsu Y., Shikita M.
FEBS Lett. 222:341-344(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-76.
[13]"Macrophage colony-stimulating factor is produced by human T lymphoblastoid cell line, CEM-ON: identification by amino-terminal amino acid sequence analysis."
Takahashi M., Hong Y.M., Yasuda S., Takano M., Kawai K., Nakai S., Hirai Y.
Biochem. Biophys. Res. Commun. 152:1401-1409(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-61.
[14]"Synthesis of membrane-bound colony-stimulating factor 1 (CSF-1) and downmodulation of CSF-1 receptors in NIH 3T3 cells transformed by cotransfection of the human CSF-1 and c-fms (CSF-1 receptor) genes."
Rettenmier C.W., Roussel M.F., Ashmun R.A., Ralph P., Price K., Sherr C.J.
Mol. Cell. Biol. 7:2378-2387(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION (ISOFORM 3).
[15]"Differential processing of colony-stimulating factor 1 precursors encoded by two human cDNAs."
Rettenmier C.W., Roussel M.F.
Mol. Cell. Biol. 8:5026-5034(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, SUBUNIT, GLYCOSYLATION, SUBCELLULAR LOCATION.
[16]"Identification of a high molecular weight macrophage colony-stimulating factor as a glycosaminoglycan-containing species."
Suzu S., Ohtsuki T., Yanai N., Takatsu Z., Kawashima T., Takaku F., Nagata N., Motoyoshi K.
J. Biol. Chem. 267:4345-4348(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, SUBUNIT, SUBCELLULAR LOCATION, STRUCTURE OF CARBOHYDRATES.
[17]"Assignment of the inter- and intramolecular disulfide linkages in recombinant human macrophage colony stimulating factor using fast atom bombardment mass spectrometry."
Glocker M.O., Arbogast B., Schreurs J., Deinzer M.L.
Biochemistry 32:482-488(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[18]"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 AND SIGNALING PATHWAYS.
[19]"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.
[20]"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 AND SIGNALING PATHWAYS.
[21]"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.
[22]"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.
[23]"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, INTERACTION WITH CSF1R.
[24]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-363 AND THR-365, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
[25]"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
Halim A., Ruetschi U., Larson G., Nilsson J.
J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
[26]"Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor."
Pandit J., Bohm A., Jancarik J., Halenbeck R., Koths K., Kim S.H.
Science 258:1358-1362(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 33-190.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11296, M11038, M11295 Genomic DNA. Translation: AAB59527.1.
M37435 mRNA. Translation: AAA52117.1.
M64592 mRNA. Translation: AAA59572.1.
U22386 mRNA. Translation: AAA64849.1.
M27087 mRNA. Translation: AAA59573.1.
AK291660 mRNA. Translation: BAF84349.1.
AL450468 Genomic DNA. Translation: CAH71146.1.
AL450468 Genomic DNA. Translation: CAH71147.1.
CH471122 Genomic DNA. Translation: EAW56416.1.
BC021117 mRNA. Translation: AAH21117.1.
X05825 mRNA. Translation: CAA29265.1.
X06106 Genomic DNA. Translation: CAA29479.1.
M76453 mRNA. Translation: AAA52120.2.
PIRFQHUMP. A47583.
RefSeqNP_000748.3. NM_000757.5.
NP_757349.1. NM_172210.2.
NP_757350.1. NM_172211.3.
NP_757351.1. NM_172212.2.
UniGeneHs.173894.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HMCX-ray2.50A/B36-181[»]
3UEZX-ray3.41E/F/G/H33-181[»]
3UF2X-ray2.75A/B/C/D/E/F/G/H/I/J33-181[»]
4ADFX-ray4.40G/H/I/J/K/L/S/T/U/V/W/X33-181[»]
4FA8X-ray2.20E/F/G36-180[»]
ProteinModelPortalP09603.
SMRP09603. Positions 36-180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107822. 5 interactions.
DIPDIP-41860N.
IntActP09603. 2 interactions.
MINTMINT-196477.
STRING9606.ENSP00000327513.

PTM databases

PhosphoSiteP09603.

Polymorphism databases

DMDM311033367.

Proteomic databases

PaxDbP09603.
PRIDEP09603.

Protocols and materials databases

DNASU1435.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329608; ENSP00000327513; ENSG00000184371. [P09603-1]
ENST00000344188; ENSP00000342718; ENSG00000184371. [P09603-2]
ENST00000369801; ENSP00000358816; ENSG00000184371. [P09603-2]
ENST00000369802; ENSP00000358817; ENSG00000184371. [P09603-1]
ENST00000420111; ENSP00000407317; ENSG00000184371. [P09603-3]
GeneID1435.
KEGGhsa:1435.
UCSCuc001dyt.2. human. [P09603-2]
uc001dyu.2. human. [P09603-1]
uc021orj.2. human. [P09603-3]

Organism-specific databases

CTD1435.
GeneCardsGC01P110453.
HGNCHGNC:2432. CSF1.
MIM120420. gene.
neXtProtNX_P09603.
PharmGKBPA26935.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43822.
HOVERGENHBG005410.
InParanoidP09603.
KOK05453.
OMADTGHERQ.
OrthoDBEOG7GBFZ6.
PhylomeDBP09603.
TreeFamTF337718.

Enzyme and pathway databases

SignaLinkP09603.

Gene expression databases

ArrayExpressP09603.
BgeeP09603.
CleanExHS_CSF1.
GenevestigatorP09603.

Family and domain databases

InterProIPR009079. 4_helix_cytokine-like_core.
IPR008001. MCSF-1.
[Graphical view]
PANTHERPTHR10058. PTHR10058. 1 hit.
PfamPF05337. CSF-1. 2 hits.
[Graphical view]
PIRSFPIRSF001948. MCSF-1. 1 hit.
SUPFAMSSF47266. SSF47266. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCSF1. human.
EvolutionaryTraceP09603.
GeneWikiMacrophage_colony-stimulating_factor.
GenomeRNAi1435.
NextBio5857.
PMAP-CutDBP09603.
PROP09603.
SOURCESearch...

Entry information

Entry nameCSF1_HUMAN
AccessionPrimary (citable) accession number: P09603
Secondary accession number(s): A8K6J5 expand/collapse secondary AC list , Q13130, Q14086, Q14806, Q5VVF3, Q5VVF4, Q9UQR8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM