CSF2R_HUMAN - dbPTM
CSF2R_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSF2R_HUMAN
UniProt AC P15509
Protein Name Granulocyte-macrophage colony-stimulating factor receptor subunit alpha
Gene Name CSF2RA
Organism Homo sapiens (Human).
Sequence Length 400
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Isoform 3: Secreted .
Isoform 4: Secreted .
Isoform 6: Secreted .
Protein Description Low affinity receptor for granulocyte-macrophage colony-stimulating factor. Transduces a signal that results in the proliferation, differentiation, and functional activation of hematopoietic cells..
Protein Sequence MLLLVTSLLLCELPHPAFLLIPEKSDLRTVAPASSLNVRFDSRTMNLSWDCQENTTFSKCFLTDKKNRVVEPRLSNNECSCTFREICLHEGVTFEVHVNTSQRGFQQKLLYPNSGREGTAAQNFSCFIYNADLMNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHLDNLSGLTSRNYFLVNGTSREIGIQFFDSLLDTKKIERFNPPSNVTVRCNTTHCLVRWKQPRTYQKLSYLDFQYQLDVHRKNTQPGTENLLINVSGDLENRYNFPSSEPRAKHSVKIRAADVRILNWSSWSEAIEFGSDDGNLGSVYIYVLLIVGTLVCGIVLGFLFKRFLRIQRLFPPVPQIKDKLNDNHEVEDEIIWEEFTPEEGKGYREEVLTVKEIT
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
34PhosphorylationLRTVAPASSLNVRFD
CCCCCCCCCEEEEEE		34.01-
46N-linked_GlycosylationRFDSRTMNLSWDCQE
EEECCCEEEEEEECC		30.25UniProtKB CARBOHYD
48PhosphorylationDSRTMNLSWDCQENT
ECCCEEEEEEECCCC		18.83-
54N-linked_GlycosylationLSWDCQENTTFSKCF
EEEEECCCCEEEEEE		20.67UniProtKB CARBOHYD
55PhosphorylationSWDCQENTTFSKCFL
EEEECCCCEEEEEEE		28.59-
56PhosphorylationWDCQENTTFSKCFLT
EEECCCCEEEEEEEE		37.18-
99N-linked_GlycosylationVTFEVHVNTSQRGFQ
CEEEEEEECCCCCEE		21.09UniProtKB CARBOHYD
123N-linked_GlycosylationREGTAAQNFSCFIYN
CCCCCHHCEEEEEEE		26.52UniProtKB CARBOHYD
135N-linked_GlycosylationIYNADLMNCTWARGP
EEECCCCCCEECCCC		27.62UniProtKB CARBOHYD
158UbiquitinationFLYIRNSKRRREIRC
EEEEECCCCCCEEEC		54.17-
182N-linked_GlycosylationHVGCHLDNLSGLTSR
EEEEEECCCCCCCCC		42.33UniProtKB CARBOHYD
195N-linked_GlycosylationSRNYFLVNGTSREIG
CCCEEEECCCCCHHH		50.61UniProtKB CARBOHYD
197PhosphorylationNYFLVNGTSREIGIQ
CEEEECCCCCHHHHH		21.2929083192
198PhosphorylationYFLVNGTSREIGIQF
EEEECCCCCHHHHHH		29.3429083192
217 (in isoform 6)Phosphorylation-39.86-
220 (in isoform 6)Phosphorylation-30.86-
221 (in isoform 6)Phosphorylation-39.37-
222PhosphorylationIERFNPPSNVTVRCN
CCCCCCCCCEEEEEC		45.2322210691
223N-linked_GlycosylationERFNPPSNVTVRCNT
CCCCCCCCEEEEECC		38.97UniProtKB CARBOHYD
224 (in isoform 6)Phosphorylation-6.50-
225PhosphorylationFNPPSNVTVRCNTTH
CCCCCCEEEEECCCE		13.3922210691
229N-linked_GlycosylationSNVTVRCNTTHCLVR
CCEEEEECCCEEEEE		37.1318692472
232UbiquitinationTVRCNTTHCLVRWKQ
EEEECCCEEEEEECC		10.8129967540
254UbiquitinationSYLDFQYQLDVHRKN
EEEEEEEEEEECCCC		22.0229967540
264UbiquitinationVHRKNTQPGTENLLI
ECCCCCCCCCCEEEE		50.0329967540
272N-linked_GlycosylationGTENLLINVSGDLEN
CCCEEEEEEECCCCC		23.13UniProtKB CARBOHYD
305N-linked_GlycosylationAADVRILNWSSWSEA
ECCEEEECCCCHHHH		33.92UniProtKB CARBOHYD
324 (in isoform 3)Phosphorylation-18.21-
353 (in isoform 5)Phosphorylation-29.59-
365UbiquitinationPVPQIKDKLNDNHEV
CCHHHHHHCCCCCCC		44.1629967540
387UbiquitinationEFTPEEGKGYREEVL
ECCCCCCCCCCEEEE		56.9229967540
395PhosphorylationGYREEVLTVKEIT--
CCCEEEEEEEECC--		34.4124719451
397UbiquitinationREEVLTVKEIT----
CEEEEEEEECC----		37.8629967540
399UbiquitinationEVLTVKEIT------
EEEEEEECC------		4.6129967540
421Ubiquitination----------------------------
----------------------------		29967540
431Ubiquitination--------------------------------------
--------------------------------------		29967540
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

Oops, there are no upstream regulatory protein records of CSF2R_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSF2R_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 CSF2R_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P85A_HUMANPIK3R1physical
12538575
IKKB_HUMANIKBKBphysical
12637324
FATE1_HUMANFATE1physical
25416956
Drug and Disease Associations
Kegg Disease
H01122 Pulmonary alveolar proteinosis (PAP)
OMIM Disease
300770Pulmonary surfactant metabolism dysfunction 4 (SMDP4)
Kegg Drug
D05066 Molgramostim (USAN/INN)
D05712 Regramostim (USAN/INN)
D05803 Sargramostim (USAN/INN); 1438 (genetical recombination) (JAN); Leukine (TN)
D09930 Mavrilimumab (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSF2R_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The structure of the GM-CSF receptor complex reveals a distinct modeof cytokine receptor activation.";
Hansen G., Hercus T.R., McClure B.J., Stomski F.C., Dottore M.,Powell J., Ramshaw H., Woodcock J.M., Xu Y., Guthridge M.,McKinstry W.J., Lopez A.F., Parker M.W.;
Cell 134:496-507(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 218-320 IN COMPLEX WITHCSF2RB AND CSF2, SUBUNIT, AND GLYCOSYLATION AT ASN-229.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory