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P07141

- CSF1_MOUSE

UniProt

P07141 - CSF1_MOUSE

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Protein

Macrophage colony-stimulating factor 1

Gene

Csf1

Organism
Mus musculus (Mouse)
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.

GO - Molecular functioni

  1. macrophage colony-stimulating factor receptor binding Source: BHF-UCL
  2. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

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

Keywords - Molecular functioni

Cytokine, Growth factor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Macrophage colony-stimulating factor 1
Short name:
CSF-1
Short name:
MCSF
Cleaved into the following chain:
Gene namesi
Name:Csf1
Synonyms:Csfm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1339753. Csf1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

A defect in Csf1 is the cause of osteopetrosis. Osteopetrotic mice (op/op) are severely deficient in mature macrophages and osteoclasts, display failed tooth eruption, and have a restricted capacity for bone remodeling.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 PublicationAdd
BLAST
Chaini33 – 552520Macrophage colony-stimulating factor 1PRO_0000005858Add
BLAST
Chaini33 – ?Processed macrophage colony-stimulating factor 1PRO_0000296232

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 1221 Publication
Disulfide bondi63 – 63Interchain1 Publication
Disulfide bondi80 ↔ 1711 Publication
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi134 ↔ 1781 Publication
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi189 – 189InterchainBy similarity
Disulfide bondi191 – 191InterchainBy similarity

Post-translational modificationi

N-glycosylated. The predominant soluble form is a chondroitin sulfate-containing proteoglycan.

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

MaxQBiP07141.
PaxDbiP07141.
PRIDEiP07141.

PTM databases

PhosphoSiteiP07141.

Expressioni

Gene expression databases

BgeeiP07141.
CleanExiMM_CSF1.
ExpressionAtlasiP07141. baseline and differential.
GenevestigatoriP07141.

Interactioni

Subunit structurei

Homodimer or heterodimer; disulfide-linked. Interacts with CSF1R.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Aar2Q8C1612EBI-777188,EBI-777252
Cldn11Q607712EBI-777188,EBI-309095
Csf1rP095814EBI-777188,EBI-6305373
Dync1h1Q9JHU42EBI-777188,EBI-645061
SrcP054802EBI-777188,EBI-298680

Protein-protein interaction databases

DIPiDIP-45278N.
IntActiP07141. 42 interactions.

Structurei

Secondary structure

1
552
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 415
Helixi45 – 5511
Beta strandi65 – 706
Turni72 – 743
Helixi78 – 9518
Helixi104 – 11815
Helixi119 – 1224
Turni131 – 1344
Beta strandi135 – 1406
Helixi142 – 16221
Turni164 – 1674
Helixi172 – 1776

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EJJX-ray2.40A/B36-180[»]
3UF5X-ray2.80A/B33-181[»]
4ADQX-ray4.50E/F/G/H33-181[»]
ProteinModelPortaliP07141.
SMRiP07141. Positions 36-180.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07141.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 492460ExtracellularSequence AnalysisAdd
BLAST
Topological domaini516 – 55237CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei493 – 51523HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43822.
GeneTreeiENSGT00390000015805.
HOGENOMiHOG000112010.
HOVERGENiHBG005410.
InParanoidiP07141.
KOiK05453.
OMAiDTGHERQ.
OrthoDBiEOG7GBFZ6.
PhylomeDBiP07141.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P07141-1) [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
MTARGAAGRC PSSTWLGSRL LLVCLLMSRS IAKEVSEHCS HMIGNGHLKV
60 70 80 90 100
LQQLIDSQME TSCQIAFEFV DQEQLDDPVC YLKKAFFLVQ DIIDETMRFK
110 120 130 140 150
DNTPNANATE RLQELSNNLN SCFTKDYEEQ NKACVRTFHE TPLQLLEKIK
160 170 180 190 200
NFFNETKNLL EKDWNIFTKN CNNSFAKCSS RDVVTKPDCN CLYPKATPSS
210 220 230 240 250
DPASASPHQP PAPSMAPLAG LAWDDSQRTE GSSLLPSELP LRIEDPGSAK
260 270 280 290 300
QRPPRSTCQT LESTEQPNHG DRLTEDSQPH PSAGGPVPGV EDILESSLGT
310 320 330 340 350
NWVLEEASGE ASEGFLTQEA KFSPSTPVGG SIQAETDRPR ALSASPFPKS
360 370 380 390 400
TEDQKPVDIT DRPLTEVNPM RPIGQTQNNT PEKTDGTSTL REDHQEPGSP
410 420 430 440 450
HIATPNPQRV SNSATPVAQL LLPKSHSWGI VLPLGELEGK RSTRDRRSPA
460 470 480 490 500
ELEGGSASEG AARPVARFNS IPLTDTGHVE QHEGSSDPQI PESVFHLLVP
510 520 530 540 550
GIILVLLTVG GLLFYKWKWR SHRDPQTLDS SVGRPEDSSL TQDEDRQVEL

PV
Length:552
Mass (Da):60,649
Last modified:February 1, 1996 - v2
Checksum:i3886D72D70E770AF
GO
Isoform 2 (identifier: P07141-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     182-476: Missing.

Note: No experimental confirmation available.

Show »
Length:257
Mass (Da):29,353
Checksum:iE1EF2A20C416E591
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31Missing in AAA37480. (PubMed:3493488)Curated
Sequence conflicti6 – 61A → R in AAA37480. (PubMed:3493488)Curated
Sequence conflicti7 – 82AG → PR in AAA37480. (PubMed:3493488)Curated
Sequence conflicti246 – 2461P → A in CAA28660. (PubMed:3494232)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti292 – 2921D → G.
Natural varianti345 – 3451S → P.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei182 – 476295Missing in isoform 2. 1 PublicationVSP_001189Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05010 mRNA. Translation: CAA28660.1.
M21952 mRNA. Translation: AAA37481.1.
M21149 mRNA. Translation: AAA37482.1.
M84361 mRNA. Translation: AAA03032.1.
AK138489 mRNA. Translation: BAE23681.1.
AK154872 mRNA. Translation: BAE32893.1.
AK160995 mRNA. Translation: BAE36140.1.
CH466607 Genomic DNA. Translation: EDL01916.1.
CH466607 Genomic DNA. Translation: EDL01919.1.
BC025593 mRNA. Translation: AAH25593.1.
BC066187 mRNA. Translation: AAH66187.1.
BC066200 mRNA. Translation: AAH66200.1.
BC066205 mRNA. Translation: AAH66205.1.
M15692 mRNA. Translation: AAA37480.1.
M81316 Unassigned DNA. Translation: AAA19866.1.
CCDSiCCDS17740.1. [P07141-1]
CCDS51044.1. [P07141-2]
PIRiA31401.
RefSeqiNP_001107001.1. NM_001113529.1. [P07141-2]
NP_001107002.1. NM_001113530.1. [P07141-1]
NP_031804.3. NM_007778.4. [P07141-1]
UniGeneiMm.795.

Genome annotation databases

EnsembliENSMUST00000014743; ENSMUSP00000014743; ENSMUSG00000014599. [P07141-1]
ENSMUST00000118593; ENSMUSP00000113136; ENSMUSG00000014599. [P07141-2]
ENSMUST00000120243; ENSMUSP00000113617; ENSMUSG00000014599. [P07141-1]
GeneIDi12977.
KEGGimmu:12977.
UCSCiuc008qxk.2. mouse. [P07141-1]
uc008qxl.2. mouse. [P07141-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05010 mRNA. Translation: CAA28660.1 .
M21952 mRNA. Translation: AAA37481.1 .
M21149 mRNA. Translation: AAA37482.1 .
M84361 mRNA. Translation: AAA03032.1 .
AK138489 mRNA. Translation: BAE23681.1 .
AK154872 mRNA. Translation: BAE32893.1 .
AK160995 mRNA. Translation: BAE36140.1 .
CH466607 Genomic DNA. Translation: EDL01916.1 .
CH466607 Genomic DNA. Translation: EDL01919.1 .
BC025593 mRNA. Translation: AAH25593.1 .
BC066187 mRNA. Translation: AAH66187.1 .
BC066200 mRNA. Translation: AAH66200.1 .
BC066205 mRNA. Translation: AAH66205.1 .
M15692 mRNA. Translation: AAA37480.1 .
M81316 Unassigned DNA. Translation: AAA19866.1 .
CCDSi CCDS17740.1. [P07141-1 ]
CCDS51044.1. [P07141-2 ]
PIRi A31401.
RefSeqi NP_001107001.1. NM_001113529.1. [P07141-2 ]
NP_001107002.1. NM_001113530.1. [P07141-1 ]
NP_031804.3. NM_007778.4. [P07141-1 ]
UniGenei Mm.795.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3EJJ X-ray 2.40 A/B 36-180 [» ]
3UF5 X-ray 2.80 A/B 33-181 [» ]
4ADQ X-ray 4.50 E/F/G/H 33-181 [» ]
ProteinModelPortali P07141.
SMRi P07141. Positions 36-180.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-45278N.
IntActi P07141. 42 interactions.

PTM databases

PhosphoSitei P07141.

Proteomic databases

MaxQBi P07141.
PaxDbi P07141.
PRIDEi P07141.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000014743 ; ENSMUSP00000014743 ; ENSMUSG00000014599 . [P07141-1 ]
ENSMUST00000118593 ; ENSMUSP00000113136 ; ENSMUSG00000014599 . [P07141-2 ]
ENSMUST00000120243 ; ENSMUSP00000113617 ; ENSMUSG00000014599 . [P07141-1 ]
GeneIDi 12977.
KEGGi mmu:12977.
UCSCi uc008qxk.2. mouse. [P07141-1 ]
uc008qxl.2. mouse. [P07141-2 ]

Organism-specific databases

CTDi 1435.
MGIi MGI:1339753. Csf1.

Phylogenomic databases

eggNOGi NOG43822.
GeneTreei ENSGT00390000015805.
HOGENOMi HOG000112010.
HOVERGENi HBG005410.
InParanoidi P07141.
KOi K05453.
OMAi DTGHERQ.
OrthoDBi EOG7GBFZ6.
PhylomeDBi P07141.
TreeFami TF337718.

Miscellaneous databases

EvolutionaryTracei P07141.
NextBioi 282746.
PROi P07141.
SOURCEi Search...

Gene expression databases

Bgeei P07141.
CleanExi MM_CSF1.
ExpressionAtlasi P07141. baseline and differential.
Genevestigatori P07141.

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. "Nucleotide sequence of a cDNA encoding murine CSF-1 (Macrophage-CSF)."
    Delamarter J.F., Hession C., Semon D., Gough N.M., Rothenbuhler R., Mermod J.-J.
    Nucleic Acids Res. 15:2389-2390(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "cDNA cloning and expression of murine macrophage colony-stimulating factor from L929 cells."
    Ladner M.B., Martin G.A., Noble J.A., Wittman V.P., Warren M.K., McGrogan M., Stanley E.R.
    Proc. Natl. Acad. Sci. U.S.A. 85:6706-6710(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Isolation and characterization of a cDNA clone encoding for rat CSF-1 gene. Post-transcriptional repression occurs in myogenic differentiation."
    Borycki A.G., Lenormund J., Guillier M., Leibovitch S.A.
    Biochim. Biophys. Acta 1174:143-152(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Head and Spinal cord.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Embryonic germ cell and Neural stem cell.
  7. "Cloning and tissue-specific expression of mouse macrophage colony-stimulating factor mRNA."
    Rajavashisth T.B., Eng R., Shadduck R.K., Waheed A., Ben-Avram C.M., Shively J.E., Lusis A.J.
    Proc. Natl. Acad. Sci. U.S.A. 84:1157-1161(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-100.
  8. Cited for: PROTEIN SEQUENCE OF 33-57.
  9. "Cloning and characterization of the murine promoter for the colony-stimulating factor-1-encoding gene."
    Harrington M.A., Edenberg H.J., Saxman S.M., Pedigo L.M., Daub R., Broxmeyer H.E.
    Gene 102:165-170(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-13.
  10. "Mutation of macrophage colony stimulating factor (Csf1) causes osteopetrosis in the tl rat."
    Dobbins D.E., Sood R., Hashiramoto A., Hansen C.T., Wilder R.L., Remmers E.F.
    Biochem. Biophys. Res. Commun. 294:1114-1120(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:8357831 ORIGINATES FROM MOUSE.
  11. "The osteopetrotic mutation toothless (tl) is a loss-of-function frameshift mutation in the rat Csf1 gene: evidence of a crucial role for CSF-1 in osteoclastogenesis and endochondral ossification."
    Van Wesenbeeck L., Odgren P.R., MacKay C.A., D'Angelo M., Safadi F.F., Popoff S.N., Van Hul W., Marks S.C. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 99:14303-14308(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:8357831 ORIGINATES FROM MOUSE.
  12. "The predominant form of secreted colony stimulating factor-1 is a proteoglycan."
    Price L.K.H., Choi H.U., Rosenberg L., Stanley E.R.
    J. Biol. Chem. 267:2190-2199(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  13. "The murine mutation osteopetrosis is in the coding region of the macrophage colony stimulating factor gene."
    Yoshida H., Hayashi S., Kunisada T., Ogawa M., Nishikawa S., Okamura H., Sudo T., Shultz L.D., Nishikawa S.
    Nature 345:442-444(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE.
  14. "Structure of macrophage colony stimulating factor bound to FMS: diverse signaling assemblies of class III receptor tyrosine kinases."
    Chen X., Liu H., Focia P.J., Shim A.H., He X.
    Proc. Natl. Acad. Sci. U.S.A. 105:18267-18272(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 36-180 IN COMPLEX WITH CSF1R, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiCSF1_MOUSE
AccessioniPrimary (citable) accession number: P07141
Secondary accession number(s): Q3U395, Q8R3C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3