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P07141

- CSF1_MOUSE

UniProt

P07141 - CSF1_MOUSE

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
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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 binding Source: IntAct
    3. 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

    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-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. perinuclear region of cytoplasm Source: Ensembl
    4. plasma membrane Source: UniProtKB-SubCell
    5. receptor complex Source: BHF-UCL

    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

    PaxDbiP07141.
    PRIDEiP07141.

    PTM databases

    PhosphoSiteiP07141.

    Expressioni

    Gene expression databases

    ArrayExpressiP07141.
    BgeeiP07141.
    CleanExiMM_CSF1.
    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.
    InParanoidiQ3U395.
    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

    MTARGAAGRC PSSTWLGSRL LLVCLLMSRS IAKEVSEHCS HMIGNGHLKV    50
    LQQLIDSQME TSCQIAFEFV DQEQLDDPVC YLKKAFFLVQ DIIDETMRFK 100
    DNTPNANATE RLQELSNNLN SCFTKDYEEQ NKACVRTFHE TPLQLLEKIK 150
    NFFNETKNLL EKDWNIFTKN CNNSFAKCSS RDVVTKPDCN CLYPKATPSS 200
    DPASASPHQP PAPSMAPLAG LAWDDSQRTE GSSLLPSELP LRIEDPGSAK 250
    QRPPRSTCQT LESTEQPNHG DRLTEDSQPH PSAGGPVPGV EDILESSLGT 300
    NWVLEEASGE ASEGFLTQEA KFSPSTPVGG SIQAETDRPR ALSASPFPKS 350
    TEDQKPVDIT DRPLTEVNPM RPIGQTQNNT PEKTDGTSTL REDHQEPGSP 400
    HIATPNPQRV SNSATPVAQL LLPKSHSWGI VLPLGELEGK RSTRDRRSPA 450
    ELEGGSASEG AARPVARFNS IPLTDTGHVE QHEGSSDPQI PESVFHLLVP 500
    GIILVLLTVG GLLFYKWKWR SHRDPQTLDS SVGRPEDSSL TQDEDRQVEL 550
    PV 552
    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

    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 Q3U395.
    KOi K05453.
    OMAi DTGHERQ.
    OrthoDBi EOG7GBFZ6.
    PhylomeDBi P07141.
    TreeFami TF337718.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi P07141.
    Bgeei P07141.
    CleanExi MM_CSF1.
    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

    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 1, 2014
    This is version 141 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