P09603 (CSF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	554 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 membrane protein Ref.15 Ref.16. Processed macrophage colony-stimulating factor 1: Secreted › extracellular 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.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 process	Immunity Inflammatory response Innate immunity
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Cytokine Growth factor
PTM	Disulfide bond Glycoprotein Proteoglycan
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	branching involved in mammary gland duct morphogenesis Inferred from electronic annotation. Source: Compara 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 homeostasis of number of cells within a tissue Inferred from electronic annotation. Source: Compara 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: Compara mammary gland fat development Inferred from electronic annotation. Source: Compara monocyte activation Non-traceable author statement PubMed 18566389. Source: BHF-UCL odontogenesis Inferred from electronic annotation. Source: Compara ossification Inferred from electronic annotation. Source: Compara osteoclast differentiation Inferred from direct assay PubMed 18606301. Source: BHF-UCL positive regulation of Ras protein signal transduction Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from sequence or structural similarity PubMed 18566389. Source: BHF-UCL positive regulation of cell-matrix adhesion Inferred from sequence or structural similarity PubMed 18566389. 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: Compara positive regulation of odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara 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 ossification Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Inferred from direct assay Ref.3. Source: BHF-UCL integral to 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_function	cytokine 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Ref.1 Ref.11 Ref.12

Chain

33 – 554

522

Macrophage colony-stimulating factor 1

PRO_0000005857

Chain

33 – ?

Processed macrophage colony-stimulating factor 1

PRO_0000296231

Regions

Topological domain

33 – 496

464

Lumenal Potential

Transmembrane

497 – 517

21

Helical; Potential

Topological domain

518 – 554

37

Cytoplasmic Potential

Region

406 – 426

21

O-glycosylated at one site

Amino acid modifications

Glycosylation

154

1

N-linked (GlcNAc...) Potential

Glycosylation

172

1

N-linked (GlcNAc...) Potential

Glycosylation

363

1

O-linked (GalNAc...) Ref.24

Glycosylation

365

1

O-linked (GalNAc...) Ref.24

Disulfide bond

39 ↔ 122

Ref.17

Disulfide bond

63

Interchain Ref.17

Disulfide bond

80 ↔ 171

Ref.17

Disulfide bond

134 ↔ 178

Ref.17

Disulfide bond

189

Interchain Ref.17

Disulfide bond

191

Interchain Ref.17

Natural variations

Alternative sequence

182 – 479

298

Missing in isoform 3.

VSP_001187

Alternative sequence

365 – 480

116

Missing in isoform 2.

VSP_001188

Natural variant

341

1

S → N.
Corresponds to variant rs12565736 [ dbSNP | Ensembl ].

VAR_048810

Natural variant

408

1

L → P. Ref.4
Corresponds to variant rs1058885 [ dbSNP | Ensembl ].

VAR_020454

Natural variant

438

1

G → R.
Corresponds to variant rs2229165 [ dbSNP | Ensembl ].

VAR_029320

Natural variant

489

1

F → 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 variant

496

1

S → F.

VAR_020455

Natural variant

531

1

A → V.
Corresponds to variant rs2229167 [ dbSNP | Ensembl ].

VAR_022146

Experimental info

Mutagenesis

489 – 554

66

Missing: Produces biologically active protein which is secreted. Ref.3

Sequence conflict

69

1

F → S AA sequence Ref.12

Sequence conflict

91

1

D → Y in AAB59527. Ref.1

Sequence conflict

91

1

D → Y in AAA59572. Ref.3

Sequence conflict

91

1

D → Y in AAA64849. Ref.3

Sequence conflict

91

1

D → Y in AAA52120. Ref.10

Sequence conflict

104 – 106

3

PNA → ANP in AAA52117. Ref.2

Sequence conflict

364

1

G → A in AAA52117. Ref.2

Sequence conflict

374

1

R → M in AAA52117. Ref.2

Sequence conflict

412

1

G → A in AAA52117. Ref.2

Sequence conflict

450

1

R → T in AAA52117. Ref.2

Sequence conflict

457 – 458

2

GG → AA in AAA52117. Ref.2

Sequence conflict

480

1

Missing in AAA59573. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

554

Helix Strand Turn

Details...

Helix

37 – 41

5

Helix

45 – 57

13

Beta strand

65 – 70

6

Turn

72 – 74

3

Helix

78 – 96

19

Helix

104 – 118

15

Beta strand

119 – 123

5

Helix

128 – 130

3

Beta strand

135 – 140

6

Helix

142 – 162

21

Helix

166 – 168

3

Helix

172 – 176

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 2, 2010. Version 2. Checksum: 656B0894F9255AED	FASTA	554	60,179
	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
	Isoform 2 [UniParc]. Checksum: 1B6A3CDBE1C06775	FASTA	438	47,903
	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 DVTGHERQSE GSFSPQLQES VFHLLVPSVI LVLLAVGGLL FYRWRRRSHQ EPQRADSPLE 430 QPEGSPLTQD DRQVELPV
	Isoform 3 [UniParc]. Checksum: 0656D858DE1A4086	FASTA	256	29,215
	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 QGHERQSEGS FSPQLQESVF HLLVPSVILV LLAVGGLLFY RWRRRSHQEP QRADSPLEQP 250 EGSPLTQDDR QVELPV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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 CARBOHYDTATES.
[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, 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, 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.

IPI

IPI00015881.
IPI00218201.
IPI00218202.

PIR

FQHUMP. A47583.

RefSeq

NP_000748.3. NM_000757.5.
NP_757349.1. NM_172210.2.
NP_757350.1. NM_172211.3.
NP_757351.1. NM_172212.2.

UniGene

Hs.173894.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HMC	X-ray	2.50	A/B	36-181	[»]
3UEZ	X-ray	3.41	E/F/G/H	33-181	[»]
3UF2	X-ray	2.75	A/B/C/D/E/F/G/H/I/J	33-181	[»]
4ADF	X-ray	4.40	G/H/I/J/K/L/S/T/U/V/W/X	33-181	[»]
4FA8	X-ray	2.20	E/F/G	36-180	[»]

ProteinModelPortal

P09603.

SMR

P09603. Positions 36-180.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41860N.

IntAct

P09603. 2 interactions.

STRING

9606.ENSP00000327513.

PTM databases

PhosphoSite

P09603.

Polymorphism databases

DMDM

311033367.

Proteomic databases

PaxDb

P09603.

PRIDE

P09603.

Protocols and materials databases

DNASU

1435.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000329608; ENSP00000327513; ENSG00000184371.
ENST00000344188; ENSP00000342718; ENSG00000184371.
ENST00000369801; ENSP00000358816; ENSG00000184371.
ENST00000369802; ENSP00000358817; ENSG00000184371.
ENST00000420111; ENSP00000407317; ENSG00000184371.

GeneID

1435.

KEGG

hsa:1435.

UCSC

uc001dyt.2. human.
uc001dyu.2. human.
uc021ori.1. human.

Organism-specific databases

CTD

1435.

GeneCards

GC01P110453.

HGNC

HGNC:2432. CSF1.

MIM

120420. gene.

neXtProt

NX_P09603.

PharmGKB

PA26935.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG43822.

HOVERGEN

HBG005410.

InParanoid

P09603.

KO

K05453.

OMA

DTGHERQ.

OrthoDB

EOG4RR6H2.

PhylomeDB

P09603.

Enzyme and pathway databases

Pathway_Interaction_DB

avb3_integrin_pathway. Integrins in angiogenesis.
ptp1bpathway. Signaling events mediated by PTP1B.

Gene expression databases

ArrayExpress

P09603.

Bgee

P09603.

CleanEx

HS_CSF1.

Genevestigator

P09603.

GermOnline

ENSG00000184371. Homo sapiens.

Family and domain databases

InterPro

IPR009079. 4_helix_cytokine-like_core.
IPR008001. MCSF-1.
[Graphical view]

PANTHER

PTHR10058. PTHR10058. 1 hit.

Pfam

PF05337. CSF-1. 2 hits.
[Graphical view]

PIRSF

PIRSF001948. MCSF-1. 1 hit.

SUPFAM

SSF47266. 4_helix_cytokine. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

CSF1. human.

EvolutionaryTrace

P09603.

GenomeRNAi

1435.

NextBio

5857.

PMAP-CutDB

P09603.

SOURCE

Search...

Entry information

Entry name

CSF1_HUMAN

Accession

Primary (citable) accession number: P09603
Secondary accession number(s): A8K6J5 , Q13130, Q14086, Q14806, Q5VVF3, Q5VVF4, Q9UQR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 2, 2010
Last modified:	May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.