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Protein

Granulocyte-macrophage colony-stimulating factor

Gene

Csf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

GO - Molecular functioni

  1. cytokine activity Source: MGI

GO - Biological processi

  1. cellular response to lipopolysaccharide Source: Ensembl
  2. dendritic cell differentiation Source: MGI
  3. embryonic placenta development Source: MGI
  4. epithelial fluid transport Source: Ensembl
  5. immune response Source: InterPro
  6. macrophage activation Source: Ensembl
  7. myeloid dendritic cell differentiation Source: MGI
  8. negative regulation of cytolysis Source: MGI
  9. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  10. positive regulation of cell proliferation Source: MGI
  11. positive regulation of DNA replication Source: MGI
  12. positive regulation of gene expression Source: MGI
  13. positive regulation of interleukin-23 production Source: MGI
  14. positive regulation of macrophage derived foam cell differentiation Source: MGI
  15. positive regulation of podosome assembly Source: MGI
  16. positive regulation of tyrosine phosphorylation of Stat5 protein Source: MGI
  17. regulation of cell proliferation Source: MGI
  18. regulation of gene expression Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor

Enzyme and pathway databases

ReactomeiREACT_210793. Interleukin receptor SHC signaling.
REACT_220092. GPVI-mediated activation cascade.
REACT_223974. G beta:gamma signalling through PI3Kgamma.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Granulocyte-macrophage colony-stimulating factor
Short name:
GM-CSF
Alternative name(s):
Colony-stimulating factor
Short name:
CSF
Gene namesi
Name:Csf2
Synonyms:Csfgm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1339752. Csf2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381E → P: Reduction in bioactivity. 1 Publication
Mutagenesisi73 – 731L → P: 25-fold reduction in bioactivity. 1 Publication
Mutagenesisi77 – 771E → P: 50-fold reduction in bioactivity. 1 Publication
Mutagenesisi80 – 801L → P: 450-fold reduction in bioactivity. 1 Publication
Mutagenesisi124 – 1241L → P: 5500-fold reduction in bioactivity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Add
BLAST
Chaini18 – 141124Granulocyte-macrophage colony-stimulating factorPRO_0000005866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi22 – 221O-linked (GalNAc...)By similarity
Glycosylationi27 – 271O-linked (GalNAc...)By similarity
Disulfide bondi68 ↔ 1101 Publication
Glycosylationi83 – 831N-linked (GlcNAc...)
Glycosylationi92 – 921N-linked (GlcNAc...)
Disulfide bondi102 ↔ 1351 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP01587.

PTM databases

PhosphoSiteiP01587.

Expressioni

Gene expression databases

BgeeiP01587.
ExpressionAtlasiP01587. baseline and differential.
GenevestigatoriP01587.

Interactioni

Subunit structurei

Monomer. The signaling GM-CSF receptor complex is a dodecamer of two head-to-head hexamers of two alpha, two beta, and two ligand subunits (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP01587.
SMRiP01587. Positions 21-138.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GM-CSF family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42131.
HOGENOMiHOG000037940.
HOVERGENiHBG000532.
InParanoidiP01587.
KOiK05427.
OMAiTCLQTRL.
OrthoDBiEOG7J9VRQ.
PhylomeDBiP01587.
TreeFamiTF338611.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000773. GM_colony-stim-fac.
[Graphical view]
PANTHERiPTHR10059. PTHR10059. 1 hit.
PfamiPF01109. GM_CSF. 1 hit.
[Graphical view]
PRINTSiPR00693. GMCSFACTOR.
ProDomiPD007349. GM_colony-stim-fac. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00040. CSF2. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00702. GM_CSF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01587-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWLQNLLFLG IVVYSLSAPT RSPITVTRPW KHVEAIKEAL NLLDDMPVTL
60 70 80 90 100
NEEVEVVSNE FSFKKLTCVQ TRLKIFEQGL RGNFTKLKGA LNMTASYYQT
110 120 130 140
YCPPTPETDC ETQVTTYADF IDSLKTFLTD IPFECKKPGQ K
Length:141
Mass (Da):16,091
Last modified:April 1, 1988 - v1
Checksum:i209C7CBB4FF77349
GO

Sequence cautioni

The sequence CAA26192.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251T → I in CAA29336. (PubMed:6610831)Curated
Sequence conflicti25 – 251T → I AA sequence (PubMed:3871523)Curated
Sequence conflicti114 – 1141V → A in AAA37483. (PubMed:3898082)Curated
Sequence conflicti139 – 1391G → S in CAA29336. (PubMed:6610831)Curated
Sequence conflicti139 – 1391G → V in CAA26820. (PubMed:3876931)Curated
Sequence conflicti139 – 1391G → V no nucleotide entry (PubMed:3902470)Curated
Sequence conflicti139 – 1391G → V in CAA26192. (PubMed:3874057)Curated
Sequence conflicti139 – 1391G → V in CAA26193. (PubMed:3874057)Curated
Sequence conflicti139 – 1391G → V in AAA37483. (PubMed:3898082)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03020 Genomic DNA. Translation: CAA26821.1.
X03019 mRNA. Translation: CAA26820.1.
X02333 mRNA. Translation: CAA26193.1.
X02333 mRNA. Translation: CAA26192.1. Different initiation.
X05906 mRNA. Translation: CAA29336.1.
M11848 mRNA. Translation: AAA37483.1.
CCDSiCCDS24692.1.
PIRiI48368. FQMSGM.
RefSeqiNP_034099.2. NM_009969.4.
UniGeneiMm.4922.

Genome annotation databases

EnsembliENSMUST00000019060; ENSMUSP00000019060; ENSMUSG00000018916.
GeneIDi12981.
KEGGimmu:12981.
UCSCiuc007ixm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03020 Genomic DNA. Translation: CAA26821.1.
X03019 mRNA. Translation: CAA26820.1.
X02333 mRNA. Translation: CAA26193.1.
X02333 mRNA. Translation: CAA26192.1. Different initiation.
X05906 mRNA. Translation: CAA29336.1.
M11848 mRNA. Translation: AAA37483.1.
CCDSiCCDS24692.1.
PIRiI48368. FQMSGM.
RefSeqiNP_034099.2. NM_009969.4.
UniGeneiMm.4922.

3D structure databases

ProteinModelPortaliP01587.
SMRiP01587. Positions 21-138.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiP01587.

Proteomic databases

PRIDEiP01587.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019060; ENSMUSP00000019060; ENSMUSG00000018916.
GeneIDi12981.
KEGGimmu:12981.
UCSCiuc007ixm.1. mouse.

Organism-specific databases

CTDi1437.
MGIiMGI:1339752. Csf2.

Phylogenomic databases

eggNOGiNOG42131.
HOGENOMiHOG000037940.
HOVERGENiHBG000532.
InParanoidiP01587.
KOiK05427.
OMAiTCLQTRL.
OrthoDBiEOG7J9VRQ.
PhylomeDBiP01587.
TreeFamiTF338611.

Enzyme and pathway databases

ReactomeiREACT_210793. Interleukin receptor SHC signaling.
REACT_220092. GPVI-mediated activation cascade.
REACT_223974. G beta:gamma signalling through PI3Kgamma.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.

Miscellaneous databases

ChiTaRSiCsf2. mouse.
NextBioi282756.
PROiP01587.
SOURCEiSearch...

Gene expression databases

BgeeiP01587.
ExpressionAtlasiP01587. baseline and differential.
GenevestigatoriP01587.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000773. GM_colony-stim-fac.
[Graphical view]
PANTHERiPTHR10059. PTHR10059. 1 hit.
PfamiPF01109. GM_CSF. 1 hit.
[Graphical view]
PRINTSiPR00693. GMCSFACTOR.
ProDomiPD007349. GM_colony-stim-fac. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00040. CSF2. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00702. GM_CSF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structure of the chromosomal gene for granulocyte-macrophage colony stimulating factor: comparison of the mouse and human genes."
    Miyatake S., Otsuka T., Yokota T., Lee F., Arai K.
    EMBO J. 4:2561-2568(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The structure and expression of the murine gene encoding granulocyte-macrophage colony stimulating factor: evidence for utilisation of alternative promoters."
    Stanley E.R., Metcalf D., Sobieszczuk P., Gough N.M., Dunn A.R.
    EMBO J. 4:2569-2573(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Recombinant murine GM-CSF from E. coli has biological activity and is neutralized by a specific antiserum."
    Delamarter J.F., Mermod J.-J., Liang C.M., Eliason J.F., Thatcher D.R.
    EMBO J. 4:2575-2581(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Structure and expression of the mRNA for murine granulocyte-macrophage colony stimulating factor."
    Gough N.M., Metcalf D., Gough J., Grail D., Dunn A.R.
    EMBO J. 4:645-653(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  5. "Molecular cloning of cDNA encoding a murine haematopoietic growth regulator, granulocyte-macrophage colony stimulating factor."
    Gough N.M., Gough J., Metcalf D., Kelso A., Grail D., Nicola N.A., Burgess A.W., Dunn A.R.
    Nature 309:763-767(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-141.
    Tissue: Lung.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-141.
  7. "Purification and partial amino acid sequence of asialo murine granulocyte-macrophage colony stimulating factor."
    Sparrow L.G., Metcalf D., Hunkapiller M.W., Hood L.E., Burgess A.W.
    Proc. Natl. Acad. Sci. U.S.A. 82:292-296(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-57.
  8. "Characterization of human and mouse granulocyte-macrophage-colony-stimulating factors derived from Escherichia coli."
    Schrimser J.L., Rose K., Simona M.G., Wingfield P.
    Biochem. J. 247:195-199(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  9. "Single proline substitutions in predicted alpha-helices of murine granulocyte-macrophage colony-stimulating factor result in a loss in bioactivity and altered glycosylation."
    Altmann S.W., Johnson G.D., Prystowsky M.B.
    J. Biol. Chem. 266:5333-5341(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.

Entry informationi

Entry nameiCSF2_MOUSE
AccessioniPrimary (citable) accession number: P01587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: February 4, 2015
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.