CSF1_HUMAN - dbPTM
CSF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
116PhosphorylationIVQLQELSLRLKSCF
EEEHHHHHHHHHHHH
15.6424719451
154N-linked_GlycosylationEKVKNVFNETKNLLD
HHHHHHHHHHHHHHH
52.31UniProtKB CARBOHYD
168PhosphorylationDKDWNIFSKNCNNSF
HHHHHHHCCCCCCCC
21.1124719451
172N-linked_GlycosylationNIFSKNCNNSFAECS
HHHCCCCCCCCCCCC
57.48UniProtKB CARBOHYD
174PhosphorylationFSKNCNNSFAECSSQ
HCCCCCCCCCCCCCC
16.3129978859
179PhosphorylationNNSFAECSSQDVVTK
CCCCCCCCCCCCCCC
23.6529978859
180PhosphorylationNSFAECSSQDVVTKP
CCCCCCCCCCCCCCC
41.9029978859
185PhosphorylationCSSQDVVTKPDCNCL
CCCCCCCCCCCCCEE
36.3929978859
185O-linked_GlycosylationCSSQDVVTKPDCNCL
CCCCCCCCCCCCCEE
36.39OGP
214O-linked_GlycosylationPHQPLAPSMAPVAGL
CCCCCCCCCCCCCCC
23.20OGP
229O-linked_GlycosylationTWEDSEGTEGSSLLP
EEECCCCCCCCCCCC
32.87OGP
232O-linked_GlycosylationDSEGTEGSSLLPGEQ
CCCCCCCCCCCCCCC
16.16OGP
233O-linked_GlycosylationSEGTEGSSLLPGEQP
CCCCCCCCCCCCCCC
44.79OGP
243O-linked_GlycosylationPGEQPLHTVDPGSAK
CCCCCCCCCCCCCCC
34.00OGP
256O-linked_GlycosylationAKQRPPRSTCQSFEP
CCCCCCCCCCCCCCC
39.0355833937
257O-linked_GlycosylationKQRPPRSTCQSFEPP
CCCCCCCCCCCCCCC
18.8255833943
266O-linked_GlycosylationQSFEPPETPVVKDST
CCCCCCCCCCCCCCC
27.4555833949
266PhosphorylationQSFEPPETPVVKDST
CCCCCCCCCCCCCCC
27.458422357
309O-linked_GlycosylationNWVPEEASGEASEIP
CCCCHHHCCCCCCCC
40.213493529
309O-linked_GlycosylationNWVPEEASGEASEIP
CCCCHHHCCCCCCCC
40.21-
335O-linked_GlycosylationPGGGSMQTEPARPSN
CCCCCCCCCCCCCCC
34.98OGP
345PhosphorylationARPSNFLSASSPLPA
CCCCCCCCCCCCCCC
23.20-
348PhosphorylationSNFLSASSPLPASAK
CCCCCCCCCCCCCCC
30.1222817900
353PhosphorylationASSPLPASAKGQQPA
CCCCCCCCCCCCCCC
28.68-
363O-linked_GlycosylationGQQPADVTGTALPRV
CCCCCCCCCCCCCCC
29.3922171320
365O-linked_GlycosylationQPADVTGTALPRVGP
CCCCCCCCCCCCCCC
18.6922171320
376O-linked_GlycosylationRVGPVRPTGQDWNHT
CCCCCCCCCCCCCCC
36.5955830583
383O-linked_GlycosylationTGQDWNHTPQKTDHP
CCCCCCCCCCCCCCH
24.9755830587
387O-linked_GlycosylationWNHTPQKTDHPSALL
CCCCCCCCCCHHHHH
34.0055835443
391O-linked_GlycosylationPQKTDHPSALLRDPP
CCCCCCHHHHHCCCC
28.2955835449
402PhosphorylationRDPPEPGSPRISSLR
CCCCCCCCCCCHHCC
23.0126091039
406PhosphorylationEPGSPRISSLRPQGL
CCCCCCCHHCCCCCC
25.3024719451
407PhosphorylationPGSPRISSLRPQGLS
CCCCCCHHCCCCCCC
26.4825954137
414PhosphorylationSLRPQGLSNPSTLSA
HCCCCCCCCHHHHCC
54.2229083192
417O-linked_GlycosylationPQGLSNPSTLSAQPQ
CCCCCCHHHHCCCCC
46.35OGP
417PhosphorylationPQGLSNPSTLSAQPQ
CCCCCCHHHHCCCCC
46.3529083192
418PhosphorylationQGLSNPSTLSAQPQL
CCCCCHHHHCCCCCC
26.4529083192
418O-linked_GlycosylationQGLSNPSTLSAQPQL
CCCCCHHHHCCCCCC
26.45OGP
420O-linked_GlycosylationLSNPSTLSAQPQLSR
CCCHHHHCCCCCCCC
25.58OGP
420PhosphorylationLSNPSTLSAQPQLSR
CCCHHHHCCCCCCCC
25.5829083192
426O-linked_GlycosylationLSAQPQLSRSHSSGS
HCCCCCCCCCCCCCC
26.87OGP
426PhosphorylationLSAQPQLSRSHSSGS
HCCCCCCCCCCCCCC
26.8729083192
428PhosphorylationAQPQLSRSHSSGSVL
CCCCCCCCCCCCCEE
25.0923186163
428O-linked_GlycosylationAQPQLSRSHSSGSVL
CCCCCCCCCCCCCEE
25.0955833541
430O-linked_GlycosylationPQLSRSHSSGSVLPL
CCCCCCCCCCCEECC
37.3355833547
430PhosphorylationPQLSRSHSSGSVLPL
CCCCCCCCCCCEECC
37.3326091039
431PhosphorylationQLSRSHSSGSVLPLG
CCCCCCCCCCEECCH
29.6626091039
431O-linked_GlycosylationQLSRSHSSGSVLPLG
CCCCCCCCCCEECCH
29.6655833553
433PhosphorylationSRSHSSGSVLPLGEL
CCCCCCCCEECCHHC
23.5626091039
433O-linked_GlycosylationSRSHSSGSVLPLGEL
CCCCCCCCEECCHHC
23.5655833557
451O-linked_GlycosylationRSTRDRRSPAEPEGG
CCCCCCCCCCCCCCC
29.3855826469
461PhosphorylationEPEGGPASEGAARPL
CCCCCCCCCCCCCCC
39.4319651622
461O-linked_GlycosylationEPEGGPASEGAARPL
CCCCCCCCCCCCCCC
39.4319651622
473PhosphorylationRPLPRFNSVPLTDTG
CCCCCCCCCCCCCCC
23.5426091039
473O-linked_GlycosylationRPLPRFNSVPLTDTG
CCCCCCCCCCCCCCC
23.5455827109
477O-linked_GlycosylationRFNSVPLTDTGHERQ
CCCCCCCCCCCCCCC
25.9955827115
533PhosphorylationQEPQRADSPLEQPEG
CCCCCCCCCCCCCCC
30.3330266825
541PhosphorylationPLEQPEGSPLTQDDR
CCCCCCCCCCCCCCC
18.3120639409

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
266TPhosphorylationKinaseFAM20CQ8IXL6
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSF1_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBL_HUMANCBLphysical
17353186
FHL3_HUMANFHL3physical
25416956
SGTA_HUMANSGTAphysical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956

Drug and Disease Associations
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.
Regulatory Network of CSF1_HUMAN

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"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.

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