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P09603

- CSF1_HUMAN

UniProt

P09603 - CSF1_HUMAN

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
    • BLAST
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      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.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

    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-SubCell
    7. receptor complex Source: BHF-UCL

    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

    ArrayExpressiP09603.
    BgeeiP09603.
    CleanExiHS_CSF1.
    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.
    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: P09603-1) [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

    MTAPGAAGRC PPTTWLGSLL LLVCLLASRS ITEEVSEYCS HMIGSGHLQS    50
    LQRLIDSQME TSCQITFEFV DQEQLKDPVC YLKKAFLLVQ DIMEDTMRFR 100
    DNTPNAIAIV QLQELSLRLK SCFTKDYEEH DKACVRTFYE TPLQLLEKVK 150
    NVFNETKNLL DKDWNIFSKN CNNSFAECSS QDVVTKPDCN CLYPKAIPSS 200
    DPASVSPHQP LAPSMAPVAG LTWEDSEGTE GSSLLPGEQP LHTVDPGSAK 250
    QRPPRSTCQS FEPPETPVVK DSTIGGSPQP RPSVGAFNPG MEDILDSAMG 300
    TNWVPEEASG EASEIPVPQG TELSPSRPGG GSMQTEPARP SNFLSASSPL 350
    PASAKGQQPA DVTGTALPRV GPVRPTGQDW NHTPQKTDHP SALLRDPPEP 400
    GSPRISSLRP QGLSNPSTLS AQPQLSRSHS SGSVLPLGEL EGRRSTRDRR 450
    SPAEPEGGPA SEGAARPLPR FNSVPLTDTG HERQSEGSFS PQLQESVFHL 500
    LVPSVILVLL AVGGLLFYRW RRRSHQEPQR ADSPLEQPEG SPLTQDDRQV 550
    ELPV 554
    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.
    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

    ArrayExpressi P09603.
    Bgeei P09603.
    CleanExi HS_CSF1.
    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

    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 1, 2014
    This is version 157 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