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P09603

- CSF1_HUMAN

UniProt

P09603 - CSF1_HUMAN

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Protein

Macrophage colony-stimulating factor 1

Gene

CSF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. cytokine activity Source: BHF-UCL
  2. growth factor activity Source: UniProtKB
  3. macrophage colony-stimulating factor receptor binding Source: UniProtKB
  4. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. branching involved in mammary gland duct morphogenesis Source: Ensembl
  2. cell differentiation Source: UniProtKB
  3. cell proliferation Source: UniProtKB
  4. developmental process involved in reproduction Source: BHF-UCL
  5. hemopoiesis Source: UniProtKB
  6. homeostasis of number of cells within a tissue Source: Ensembl
  7. inflammatory response Source: UniProtKB-KW
  8. innate immune response Source: UniProtKB-KW
  9. macrophage differentiation Source: UniProtKB
  10. mammary duct terminal end bud growth Source: Ensembl
  11. mammary gland fat development Source: Ensembl
  12. monocyte activation Source: BHF-UCL
  13. odontogenesis Source: Ensembl
  14. ossification Source: Ensembl
  15. osteoclast differentiation Source: BHF-UCL
  16. osteoclast proliferation Source: Ensembl
  17. positive regulation of cell-matrix adhesion Source: BHF-UCL
  18. positive regulation of cell migration Source: BHF-UCL
  19. positive regulation of cell proliferation Source: UniProtKB
  20. positive regulation of cellular protein metabolic process Source: BHF-UCL
  21. positive regulation of gene expression Source: BHF-UCL
  22. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  23. positive regulation of macrophage differentiation Source: BHF-UCL
  24. positive regulation of monocyte differentiation Source: BHF-UCL
  25. positive regulation of mononuclear cell proliferation Source: BHF-UCL
  26. positive regulation of multicellular organism growth Source: Ensembl
  27. positive regulation of odontogenesis of dentin-containing tooth Source: Ensembl
  28. positive regulation of osteoclast differentiation Source: BHF-UCL
  29. positive regulation of protein kinase activity Source: BHF-UCL
  30. positive regulation of Ras protein signal transduction Source: Ensembl
  31. regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  32. regulation of ossification Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

SignaLinkiP09603.

Names & Taxonomyi

Protein namesi
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:
Gene namesi
Name:CSF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2432. CSF1.

Subcellular locationi

Cell membrane 2 Publications; Single-pass type I membrane protein 2 Publications

GO - Cellular componenti

  1. extracellular space Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: UniProtKB
  5. perinuclear region of cytoplasm Source: BHF-UCL
  6. plasma membrane Source: UniProtKB-KW
  7. receptor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi489 – 55466Missing: Produces biologically active protein which is secreted. 1 PublicationAdd
BLAST

Organism-specific databases

PharmGKBiPA26935.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 PublicationAdd
BLAST
Chaini33 – 554522Macrophage colony-stimulating factor 1PRO_0000005857Add
BLAST
Chaini33 – ?Processed macrophage colony-stimulating factor 1PRO_0000296231

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 1221 Publication
Disulfide bondi63 – 63Interchain1 Publication
Disulfide bondi80 ↔ 1711 Publication
Disulfide bondi134 ↔ 1781 Publication
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi189 – 189Interchain1 Publication
Disulfide bondi191 – 191Interchain1 Publication
Glycosylationi363 – 3631O-linked (GalNAc...)1 Publication
Glycosylationi365 – 3651O-linked (GalNAc...)1 Publication

Post-translational modificationi

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.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

MaxQBiP09603.
PaxDbiP09603.
PRIDEiP09603.

PTM databases

PhosphoSiteiP09603.

Miscellaneous databases

PMAP-CutDBP09603.

Expressioni

Gene expression databases

BgeeiP09603.
CleanExiHS_CSF1.
ExpressionAtlasiP09603. baseline and differential.
GenevestigatoriP09603.

Interactioni

Subunit structurei

Homodimer or heterodimer; disulfide-linked. Interacts with CSF1R.4 Publications

Protein-protein interaction databases

BioGridi107822. 5 interactions.
DIPiDIP-41860N.
IntActiP09603. 2 interactions.
MINTiMINT-196477.
STRINGi9606.ENSP00000327513.

Structurei

Secondary structure

1
554
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 415
Helixi45 – 5713
Beta strandi65 – 706
Turni72 – 743
Helixi78 – 9619
Helixi104 – 11815
Beta strandi119 – 1235
Helixi128 – 1303
Beta strandi135 – 1406
Helixi142 – 16221
Helixi166 – 1683
Helixi172 – 1765

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP09603.
SMRiP09603. Positions 36-180.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09603.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 496464LumenalSequence AnalysisAdd
BLAST
Topological domaini518 – 55437CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei497 – 51721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni406 – 42621O-glycosylated at one siteAdd
BLAST

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43822.
GeneTreeiENSGT00390000015805.
HOVERGENiHBG005410.
InParanoidiP09603.
KOiK05453.
OMAiDTGHERQ.
OrthoDBiEOG7GBFZ6.
PhylomeDBiP09603.
TreeFamiTF337718.

Family and domain databases

InterProiIPR009079. 4_helix_cytokine-like_core.
IPR008001. MCSF-1.
[Graphical view]
PANTHERiPTHR10058. PTHR10058. 1 hit.
PfamiPF05337. CSF-1. 2 hits.
[Graphical view]
PIRSFiPIRSF001948. MCSF-1. 1 hit.
SUPFAMiSSF47266. SSF47266. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P09603) [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

        10         20         30         40         50
MTAPGAAGRC PPTTWLGSLL LLVCLLASRS ITEEVSEYCS HMIGSGHLQS
60 70 80 90 100
LQRLIDSQME TSCQITFEFV DQEQLKDPVC YLKKAFLLVQ DIMEDTMRFR
110 120 130 140 150
DNTPNAIAIV QLQELSLRLK SCFTKDYEEH DKACVRTFYE TPLQLLEKVK
160 170 180 190 200
NVFNETKNLL DKDWNIFSKN CNNSFAECSS QDVVTKPDCN CLYPKAIPSS
210 220 230 240 250
DPASVSPHQP LAPSMAPVAG LTWEDSEGTE GSSLLPGEQP LHTVDPGSAK
260 270 280 290 300
QRPPRSTCQS FEPPETPVVK DSTIGGSPQP RPSVGAFNPG MEDILDSAMG
310 320 330 340 350
TNWVPEEASG EASEIPVPQG TELSPSRPGG GSMQTEPARP SNFLSASSPL
360 370 380 390 400
PASAKGQQPA DVTGTALPRV GPVRPTGQDW NHTPQKTDHP SALLRDPPEP
410 420 430 440 450
GSPRISSLRP QGLSNPSTLS AQPQLSRSHS SGSVLPLGEL EGRRSTRDRR
460 470 480 490 500
SPAEPEGGPA SEGAARPLPR FNSVPLTDTG HERQSEGSFS PQLQESVFHL
510 520 530 540 550
LVPSVILVLL AVGGLLFYRW RRRSHQEPQR ADSPLEQPEG SPLTQDDRQV

ELPV
Length:554
Mass (Da):60,179
Last modified:November 2, 2010 - v2
Checksum:i656B0894F9255AED
GO
Isoform 2 (identifier: P09603-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     365-480: Missing.

Show »
Length:438
Mass (Da):47,903
Checksum:i1B6A3CDBE1C06775
GO
Isoform 3 (identifier: P09603-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:256
Mass (Da):29,215
Checksum:i0656D858DE1A4086
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691F → S AA sequence (PubMed:3498652)Curated
Sequence conflicti91 – 911D → Y in AAB59527. (PubMed:2996129)Curated
Sequence conflicti91 – 911D → Y in AAA59572. (PubMed:2460758)Curated
Sequence conflicti91 – 911D → Y in AAA64849. (PubMed:2460758)Curated
Sequence conflicti91 – 911D → Y in AAA52120. (PubMed:1791839)Curated
Sequence conflicti104 – 1063PNA → ANP in AAA52117. (PubMed:3493529)Curated
Sequence conflicti364 – 3641G → A in AAA52117. (PubMed:3493529)Curated
Sequence conflicti374 – 3741R → M in AAA52117. (PubMed:3493529)Curated
Sequence conflicti412 – 4121G → A in AAA52117. (PubMed:3493529)Curated
Sequence conflicti450 – 4501R → T in AAA52117. (PubMed:3493529)Curated
Sequence conflicti457 – 4582GG → AA in AAA52117. (PubMed:3493529)Curated
Sequence conflicti480 – 4801Missing in AAA59573. (PubMed:2660794)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti341 – 3411S → N.
Corresponds to variant rs12565736 [ dbSNP | Ensembl ].
VAR_048810
Natural varianti408 – 4081L → P.1 Publication
Corresponds to variant rs1058885 [ dbSNP | Ensembl ].
VAR_020454
Natural varianti438 – 4381G → R.
Corresponds to variant rs2229165 [ dbSNP | Ensembl ].
VAR_029320
Natural varianti489 – 4891F → S.9 Publications
Corresponds to variant rs333971 [ dbSNP | Ensembl ].
VAR_048811
Natural varianti496 – 4961S → F.
Corresponds to variant rs12721516 [ dbSNP | Ensembl ].
VAR_020455
Natural varianti531 – 5311A → V.
Corresponds to variant rs2229167 [ dbSNP | Ensembl ].
VAR_022146

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei182 – 479298Missing in isoform 3. 1 PublicationVSP_001187Add
BLAST
Alternative sequencei365 – 480116Missing in isoform 2. CuratedVSP_001188Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS30797.1. [P09603-3]
CCDS816.1. [P09603-1]
CCDS817.1. [P09603-2]
PIRiA47583. FQHUMP.
RefSeqiNP_000748.3. NM_000757.5.
NP_757349.1. NM_172210.2.
NP_757350.1. NM_172211.3.
NP_757351.1. NM_172212.2.
UniGeneiHs.173894.

Genome annotation databases

EnsembliENST00000329608; ENSP00000327513; ENSG00000184371. [P09603-1]
ENST00000369801; ENSP00000358816; ENSG00000184371. [P09603-2]
ENST00000369802; ENSP00000358817; ENSG00000184371. [P09603-1]
ENST00000420111; ENSP00000407317; ENSG00000184371. [P09603-3]
GeneIDi1435.
KEGGihsa:1435.
UCSCiuc001dyt.2. human. [P09603-2]
uc001dyu.2. human. [P09603-1]
uc021orj.2. human. [P09603-3]

Polymorphism databases

DMDMi311033367.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS30797.1. [P09603-3 ]
CCDS816.1. [P09603-1 ]
CCDS817.1. [P09603-2 ]
PIRi A47583. FQHUMP.
RefSeqi NP_000748.3. NM_000757.5.
NP_757349.1. NM_172210.2.
NP_757350.1. NM_172211.3.
NP_757351.1. NM_172212.2.
UniGenei Hs.173894.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P09603.
SMRi P09603. Positions 36-180.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107822. 5 interactions.
DIPi DIP-41860N.
IntActi P09603. 2 interactions.
MINTi MINT-196477.
STRINGi 9606.ENSP00000327513.

PTM databases

PhosphoSitei P09603.

Polymorphism databases

DMDMi 311033367.

Proteomic databases

MaxQBi P09603.
PaxDbi P09603.
PRIDEi P09603.

Protocols and materials databases

DNASUi 1435.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000329608 ; ENSP00000327513 ; ENSG00000184371 . [P09603-1 ]
ENST00000369801 ; ENSP00000358816 ; ENSG00000184371 . [P09603-2 ]
ENST00000369802 ; ENSP00000358817 ; ENSG00000184371 . [P09603-1 ]
ENST00000420111 ; ENSP00000407317 ; ENSG00000184371 . [P09603-3 ]
GeneIDi 1435.
KEGGi hsa:1435.
UCSCi uc001dyt.2. human. [P09603-2 ]
uc001dyu.2. human. [P09603-1 ]
uc021orj.2. human. [P09603-3 ]

Organism-specific databases

CTDi 1435.
GeneCardsi GC01P110453.
HGNCi HGNC:2432. CSF1.
MIMi 120420. gene.
neXtProti NX_P09603.
PharmGKBi PA26935.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43822.
GeneTreei ENSGT00390000015805.
HOVERGENi HBG005410.
InParanoidi P09603.
KOi K05453.
OMAi DTGHERQ.
OrthoDBi EOG7GBFZ6.
PhylomeDBi P09603.
TreeFami TF337718.

Enzyme and pathway databases

SignaLinki P09603.

Miscellaneous databases

ChiTaRSi CSF1. human.
EvolutionaryTracei P09603.
GeneWikii Macrophage_colony-stimulating_factor.
GenomeRNAii 1435.
NextBioi 5857.
PMAP-CutDB P09603.
PROi P09603.
SOURCEi Search...

Gene expression databases

Bgeei P09603.
CleanExi HS_CSF1.
ExpressionAtlasi P09603. baseline and differential.
Genevestigatori P09603.

Family and domain databases

InterProi IPR009079. 4_helix_cytokine-like_core.
IPR008001. MCSF-1.
[Graphical view ]
PANTHERi PTHR10058. PTHR10058. 1 hit.
Pfami PF05337. CSF-1. 2 hits.
[Graphical view ]
PIRSFi PIRSF001948. MCSF-1. 1 hit.
SUPFAMi SSF47266. SSF47266. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiCSF1_HUMAN
AccessioniPrimary (citable) accession number: P09603
Secondary accession number(s): A8K6J5
, Q13130, Q14086, Q14806, Q5VVF3, Q5VVF4, Q9UQR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 2, 2010
Last modified: October 29, 2014
This is version 158 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3