UniProt ID | CSF1_HUMAN | |
---|---|---|
UniProt AC | P09603 | |
Protein Name | Macrophage colony-stimulating factor 1 | |
Gene Name | CSF1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 554 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . Processed macrophage colony-stimulating factor 1: Secreted, extracellular space. |
|
Protein Description | 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.. | |
Protein Sequence | MTAPGAAGRCPPTTWLGSLLLLVCLLASRSITEEVSEYCSHMIGSGHLQSLQRLIDSQMETSCQITFEFVDQEQLKDPVCYLKKAFLLVQDIMEDTMRFRDNTPNAIAIVQLQELSLRLKSCFTKDYEEHDKACVRTFYETPLQLLEKVKNVFNETKNLLDKDWNIFSKNCNNSFAECSSQDVVTKPDCNCLYPKAIPSSDPASVSPHQPLAPSMAPVAGLTWEDSEGTEGSSLLPGEQPLHTVDPGSAKQRPPRSTCQSFEPPETPVVKDSTIGGSPQPRPSVGAFNPGMEDILDSAMGTNWVPEEASGEASEIPVPQGTELSPSRPGGGSMQTEPARPSNFLSASSPLPASAKGQQPADVTGTALPRVGPVRPTGQDWNHTPQKTDHPSALLRDPPEPGSPRISSLRPQGLSNPSTLSAQPQLSRSHSSGSVLPLGELEGRRSTRDRRSPAEPEGGPASEGAARPLPRFNSVPLTDTGHERQSEGSFSPQLQESVFHLLVPSVILVLLAVGGLLFYRWRRRSHQEPQRADSPLEQPEGSPLTQDDRQVELPV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
116 | Phosphorylation | IVQLQELSLRLKSCF EEEHHHHHHHHHHHH | 15.64 | 24719451 | |
154 | N-linked_Glycosylation | EKVKNVFNETKNLLD HHHHHHHHHHHHHHH | 52.31 | UniProtKB CARBOHYD | |
168 | Phosphorylation | DKDWNIFSKNCNNSF HHHHHHHCCCCCCCC | 21.11 | 24719451 | |
172 | N-linked_Glycosylation | NIFSKNCNNSFAECS HHHCCCCCCCCCCCC | 57.48 | UniProtKB CARBOHYD | |
174 | Phosphorylation | FSKNCNNSFAECSSQ HCCCCCCCCCCCCCC | 16.31 | 29978859 | |
179 | Phosphorylation | NNSFAECSSQDVVTK CCCCCCCCCCCCCCC | 23.65 | 29978859 | |
180 | Phosphorylation | NSFAECSSQDVVTKP CCCCCCCCCCCCCCC | 41.90 | 29978859 | |
185 | Phosphorylation | CSSQDVVTKPDCNCL CCCCCCCCCCCCCEE | 36.39 | 29978859 | |
185 | O-linked_Glycosylation | CSSQDVVTKPDCNCL CCCCCCCCCCCCCEE | 36.39 | OGP | |
214 | O-linked_Glycosylation | PHQPLAPSMAPVAGL CCCCCCCCCCCCCCC | 23.20 | OGP | |
229 | O-linked_Glycosylation | TWEDSEGTEGSSLLP EEECCCCCCCCCCCC | 32.87 | OGP | |
232 | O-linked_Glycosylation | DSEGTEGSSLLPGEQ CCCCCCCCCCCCCCC | 16.16 | OGP | |
233 | O-linked_Glycosylation | SEGTEGSSLLPGEQP CCCCCCCCCCCCCCC | 44.79 | OGP | |
243 | O-linked_Glycosylation | PGEQPLHTVDPGSAK CCCCCCCCCCCCCCC | 34.00 | OGP | |
256 | O-linked_Glycosylation | AKQRPPRSTCQSFEP CCCCCCCCCCCCCCC | 39.03 | 55833937 | |
257 | O-linked_Glycosylation | KQRPPRSTCQSFEPP CCCCCCCCCCCCCCC | 18.82 | 55833943 | |
266 | O-linked_Glycosylation | QSFEPPETPVVKDST CCCCCCCCCCCCCCC | 27.45 | 55833949 | |
266 | Phosphorylation | QSFEPPETPVVKDST CCCCCCCCCCCCCCC | 27.45 | 8422357 | |
309 | O-linked_Glycosylation | NWVPEEASGEASEIP CCCCHHHCCCCCCCC | 40.21 | 3493529 | |
309 | O-linked_Glycosylation | NWVPEEASGEASEIP CCCCHHHCCCCCCCC | 40.21 | - | |
335 | O-linked_Glycosylation | PGGGSMQTEPARPSN CCCCCCCCCCCCCCC | 34.98 | OGP | |
345 | Phosphorylation | ARPSNFLSASSPLPA CCCCCCCCCCCCCCC | 23.20 | - | |
348 | Phosphorylation | SNFLSASSPLPASAK CCCCCCCCCCCCCCC | 30.12 | 22817900 | |
353 | Phosphorylation | ASSPLPASAKGQQPA CCCCCCCCCCCCCCC | 28.68 | - | |
363 | O-linked_Glycosylation | GQQPADVTGTALPRV CCCCCCCCCCCCCCC | 29.39 | 22171320 | |
365 | O-linked_Glycosylation | QPADVTGTALPRVGP CCCCCCCCCCCCCCC | 18.69 | 22171320 | |
376 | O-linked_Glycosylation | RVGPVRPTGQDWNHT CCCCCCCCCCCCCCC | 36.59 | 55830583 | |
383 | O-linked_Glycosylation | TGQDWNHTPQKTDHP CCCCCCCCCCCCCCH | 24.97 | 55830587 | |
387 | O-linked_Glycosylation | WNHTPQKTDHPSALL CCCCCCCCCCHHHHH | 34.00 | 55835443 | |
391 | O-linked_Glycosylation | PQKTDHPSALLRDPP CCCCCCHHHHHCCCC | 28.29 | 55835449 | |
402 | Phosphorylation | RDPPEPGSPRISSLR CCCCCCCCCCCHHCC | 23.01 | 26091039 | |
406 | Phosphorylation | EPGSPRISSLRPQGL CCCCCCCHHCCCCCC | 25.30 | 24719451 | |
407 | Phosphorylation | PGSPRISSLRPQGLS CCCCCCHHCCCCCCC | 26.48 | 25954137 | |
414 | Phosphorylation | SLRPQGLSNPSTLSA HCCCCCCCCHHHHCC | 54.22 | 29083192 | |
417 | O-linked_Glycosylation | PQGLSNPSTLSAQPQ CCCCCCHHHHCCCCC | 46.35 | OGP | |
417 | Phosphorylation | PQGLSNPSTLSAQPQ CCCCCCHHHHCCCCC | 46.35 | 29083192 | |
418 | Phosphorylation | QGLSNPSTLSAQPQL CCCCCHHHHCCCCCC | 26.45 | 29083192 | |
418 | O-linked_Glycosylation | QGLSNPSTLSAQPQL CCCCCHHHHCCCCCC | 26.45 | OGP | |
420 | O-linked_Glycosylation | LSNPSTLSAQPQLSR CCCHHHHCCCCCCCC | 25.58 | OGP | |
420 | Phosphorylation | LSNPSTLSAQPQLSR CCCHHHHCCCCCCCC | 25.58 | 29083192 | |
426 | O-linked_Glycosylation | LSAQPQLSRSHSSGS HCCCCCCCCCCCCCC | 26.87 | OGP | |
426 | Phosphorylation | LSAQPQLSRSHSSGS HCCCCCCCCCCCCCC | 26.87 | 29083192 | |
428 | Phosphorylation | AQPQLSRSHSSGSVL CCCCCCCCCCCCCEE | 25.09 | 23186163 | |
428 | O-linked_Glycosylation | AQPQLSRSHSSGSVL CCCCCCCCCCCCCEE | 25.09 | 55833541 | |
430 | O-linked_Glycosylation | PQLSRSHSSGSVLPL CCCCCCCCCCCEECC | 37.33 | 55833547 | |
430 | Phosphorylation | PQLSRSHSSGSVLPL CCCCCCCCCCCEECC | 37.33 | 26091039 | |
431 | Phosphorylation | QLSRSHSSGSVLPLG CCCCCCCCCCEECCH | 29.66 | 26091039 | |
431 | O-linked_Glycosylation | QLSRSHSSGSVLPLG CCCCCCCCCCEECCH | 29.66 | 55833553 | |
433 | Phosphorylation | SRSHSSGSVLPLGEL CCCCCCCCEECCHHC | 23.56 | 26091039 | |
433 | O-linked_Glycosylation | SRSHSSGSVLPLGEL CCCCCCCCEECCHHC | 23.56 | 55833557 | |
451 | O-linked_Glycosylation | RSTRDRRSPAEPEGG CCCCCCCCCCCCCCC | 29.38 | 55826469 | |
461 | Phosphorylation | EPEGGPASEGAARPL CCCCCCCCCCCCCCC | 39.43 | 19651622 | |
461 | O-linked_Glycosylation | EPEGGPASEGAARPL CCCCCCCCCCCCCCC | 39.43 | 19651622 | |
473 | Phosphorylation | RPLPRFNSVPLTDTG CCCCCCCCCCCCCCC | 23.54 | 26091039 | |
473 | O-linked_Glycosylation | RPLPRFNSVPLTDTG CCCCCCCCCCCCCCC | 23.54 | 55827109 | |
477 | O-linked_Glycosylation | RFNSVPLTDTGHERQ CCCCCCCCCCCCCCC | 25.99 | 55827115 | |
533 | Phosphorylation | QEPQRADSPLEQPEG CCCCCCCCCCCCCCC | 30.33 | 30266825 | |
541 | Phosphorylation | PLEQPEGSPLTQDDR CCCCCCCCCCCCCCC | 18.31 | 20639409 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
266 | T | Phosphorylation | Kinase | FAM20C | Q8IXL6 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CSF1_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CSF1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CBL_HUMAN | CBL | physical | 17353186 | |
FHL3_HUMAN | FHL3 | physical | 25416956 | |
SGTA_HUMAN | SGTA | physical | 25416956 | |
NT2NL_HUMAN | NOTCH2NL | physical | 25416956 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
H00027 | Ovarian cancer | |||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
D02664 | Mirimostim (JAN/INN); Leukoprol (TN) | |||||
D03498 | Cilmostim (USAN/INN); Macstim (TN) | |||||
D04661 | Lanimostim (USAN/INN) | |||||
D06402 | Sunitinib malate (JAN/USAN); Sutent (TN) | |||||
D08552 | Sunitinib (INN) | |||||
D09635 | Linifanib (USAN/INN) | |||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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O-linked Glycosylation | |
Reference | PubMed |
"Human urinary glycoproteomics; attachment site specific analysis ofN-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). Cited for: GLYCOSYLATION AT THR-363 AND THR-365, STRUCTURE OF CARBOHYDRATES, ANDMASS SPECTROMETRY. |