Protein:CSF2RA |
Protein Summary |
Gene summary |
| Gene name: CSF2RA | ASpdb.0 ID: 1438 | Gene | Gene symbol | CSF2RA | Gene ID | 1438 |
| Gene name | colony stimulating factor 2 receptor subunit alpha |
| Synonyms | CD116|CDw116|CSF2R|CSF2RAX|CSF2RAY|CSF2RX|CSF2RY|GM-CSF-R-alpha|GMCSFR|GMCSFR-alpha|GMR|GMR-alpha|SMDP4|alphaGMR |
| Cytomap | X;Y |
| Type of gene | protein-coding |
| Description | granulocyte-macrophage colony-stimulating factor receptor subunit alphaCD116 antigenGM-CSF receptor alpha subunitalpha-GM-CSF receptorcolony stimulating factor 2 receptor alpha subunitcolony stimulating factor 2 receptor, alpha, low-affinity (granulo |
| Modification date | 20240411 |
| UniProtAcc | P15509 |
Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | CSF2RA | GO:0007259 | cell surface receptor signaling pathway via JAK-STAT | 18692472 |
| Gene | CSF2RA | GO:0030526 | granulocyte macrophage colony-stimulating factor receptor complex | 27396825 |
| Gene | CSF2RA | GO:0038157 | granulocyte-macrophage colony-stimulating factor signaling pathway | 18692472 |
| Gene | CSF2RA | GO:0070665 | positive regulation of leukocyte proliferation | 18692472 |
AS Summary |
Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| P15509-1 | P15509-1_4rs1_B.pdb | 4RS1 | X-ray | 2.68 | B | 35 | 315 |
ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| P15509 | CSF2RA | P15509-1 | P15509-2 | 400 | 410 | 376 | 400 | Substitution | IIWEEFTPEEGKGYREEVLTVKEIT | MGPQRHHRCGWNLYPTPGPSPGSGSSPRLGSESSL | 376 | 410 |
| P15509 | CSF2RA | P15509-1 | P15509-3 | 400 | 333 | 318 | 333 | Substitution | DDGNLGSVYIYVLLIV | LGYSGCSRQFHRSKTN | 318 | 333 |
| P15509 | CSF2RA | P15509-1 | P15509-3 | 400 | 333 | 334 | 400 | Deletion | none | none | 333 | 333 |
| P15509 | CSF2RA | P15509-1 | P15509-4 | 400 | 286 | 271 | 286 | Substitution | INVSGDLENRYNFPSS | VVLTTGTSALCTFMCS | 271 | 286 |
| P15509 | CSF2RA | P15509-1 | P15509-4 | 400 | 286 | 287 | 400 | Deletion | none | none | 286 | 286 |
| P15509 | CSF2RA | P15509-1 | P15509-5 | 400 | 377 | 316 | 400 | Substitution | GSDDGNLGSVYIYVLLIVGTLVCGIVLGFLFKRFLRIQRLFPPVPQIKDKLNDNHEVEDEIIWEEFTPEEGKGYREEVLTVKEIT | DHLGGIHPRGRERLPRRGLDREGNYLRPRGCRNGMDISASATRGNCFLDDAVNLYIIFYVFI | 316 | 377 |
| P15509 | CSF2RA | P15509-1 | P15509-6 | 400 | 233 | 216 | 233 | Substitution | ERFNPPSNVTVRCNTTHC | GSLGYSGCSRQFHRSKTN | 216 | 233 |
| P15509 | CSF2RA | P15509-1 | P15509-6 | 400 | 233 | 234 | 400 | Deletion | none | none | 233 | 233 |
| P15509 | CSF2RA | P15509-1 | P15509-7 | 400 | 434 | 315 | 315 | Substitution | F | FGSHSVTQAGVQWHNLGSLQPPSPRLKRFSCLRLP | 315 | 349 |
| P15509 | CSF2RA | P15509-1 | P15509-8 | 400 | 267 | 1 | 133 | Deletion | none | none | 0 | 0 |
Multiple sequence alignment of our canonical and alternatively spliced CSF2RA |
Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of CSF2RA |
| UniProt-id | ENSG | ENST | ENSP |
| P15509-1 | ENSG00000198223.18 | ENST00000381524.8 | ENSP00000370935.3 |
| P15509-1 | ENSG00000198223.18 | ENST00000381529.9 | ENSP00000370940.3 |
| P15509-1 | ENSG00000198223.18 | ENST00000432318.8 | ENSP00000416437.2 |
| P15509-1 | ENSG00000292357.1 | ENST00000711129.1 | ENSP00000518635.1 |
| P15509-1 | ENSG00000292357.1 | ENST00000711131.1 | ENSP00000518633.1 |
| P15509-1 | ENSG00000292357.1 | ENST00000711137.1 | ENSP00000518637.1 |
| P15509-2 | ENSG00000198223.18 | ENST00000381509.8 | ENSP00000370920.3 |
| P15509-2 | ENSG00000292357.1 | ENST00000711220.1 | ENSP00000518632.1 |
| P15509-3 | ENSG00000198223.18 | ENST00000381500.6 | ENSP00000370911.1 |
| P15509-3 | ENSG00000292357.1 | ENST00000711226.1 | ENSP00000518627.1 |
| P15509-5 | ENSG00000198223.18 | ENST00000355432.8 | ENSP00000347606.3 |
| P15509-5 | ENSG00000292357.1 | ENST00000711223.1 | ENSP00000518630.1 |
| P15509-6 | ENSG00000198223.18 | ENST00000355805.7 | ENSP00000348058.2 |
| P15509-6 | ENSG00000292357.1 | ENST00000711224.1 | ENSP00000518629.1 |
| P15509-7 | ENSG00000198223.18 | ENST00000498153.7 | ENSP00000512483.1 |
| P15509-7 | ENSG00000292357.1 | ENST00000711138.1 | ENSP00000518638.1 |
| UniProt-id | NM ID | NP ID |
| P15509-1 | NM_001161529.1 | NP_001155001.1 |
| P15509-1 | NM_006140.4 | NP_006131.2 |
| P15509-1 | NM_172245.2 | NP_758448.1 |
| P15509-2 | NM_001161531.1 | NP_001155003.1 |
| P15509-3 | NM_172247.2 | NP_758450.1 |
| P15509-3 | XM_011545627.2 | XP_011543929.1 |
| P15509-3 | XM_011545628.2 | XP_011543930.1 |
| P15509-3 | XM_011546174.2 | XP_011544476.1 |
| P15509-3 | XM_011546175.2 | XP_011544477.1 |
| P15509-5 | NM_172246.2 | NP_758449.1 |
| P15509-6 | NM_172249.2 | NP_758452.1 |
| P15509-7 | NM_001161530.1 | NP_001155002.1 |
| P15509-8 | NM_001161532.1 | NP_001155004.1 |
Amino acid sequences of our canonical and alternatively spliced CSF2RA |
| accession_id | Protein sequence |
| P15509-1 | MLLLVTSLLLCELPHPAFLLIPEKSDLRTVAPASSLNVRFDSRTMNLSWDCQENTTFSKCFLTDKKNRVVEPRLSNNECSCTFREICLHE GVTFEVHVNTSQRGFQQKLLYPNSGREGTAAQNFSCFIYNADLMNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHL DNLSGLTSRNYFLVNGTSREIGIQFFDSLLDTKKIERFNPPSNVTVRCNTTHCLVRWKQPRTYQKLSYLDFQYQLDVHRKNTQPGTENLL INVSGDLENRYNFPSSEPRAKHSVKIRAADVRILNWSSWSEAIEFGSDDGNLGSVYIYVLLIVGTLVCGIVLGFLFKRFLRIQRLFPPVP |
| P15509-2 | MLLLVTSLLLCELPHPAFLLIPEKSDLRTVAPASSLNVRFDSRTMNLSWDCQENTTFSKCFLTDKKNRVVEPRLSNNECSCTFREICLHE GVTFEVHVNTSQRGFQQKLLYPNSGREGTAAQNFSCFIYNADLMNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHL DNLSGLTSRNYFLVNGTSREIGIQFFDSLLDTKKIERFNPPSNVTVRCNTTHCLVRWKQPRTYQKLSYLDFQYQLDVHRKNTQPGTENLL INVSGDLENRYNFPSSEPRAKHSVKIRAADVRILNWSSWSEAIEFGSDDGNLGSVYIYVLLIVGTLVCGIVLGFLFKRFLRIQRLFPPVP |
| P15509-3 | MLLLVTSLLLCELPHPAFLLIPEKSDLRTVAPASSLNVRFDSRTMNLSWDCQENTTFSKCFLTDKKNRVVEPRLSNNECSCTFREICLHE GVTFEVHVNTSQRGFQQKLLYPNSGREGTAAQNFSCFIYNADLMNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHL DNLSGLTSRNYFLVNGTSREIGIQFFDSLLDTKKIERFNPPSNVTVRCNTTHCLVRWKQPRTYQKLSYLDFQYQLDVHRKNTQPGTENLL |
| P15509-4 | MLLLVTSLLLCELPHPAFLLIPEKSDLRTVAPASSLNVRFDSRTMNLSWDCQENTTFSKCFLTDKKNRVVEPRLSNNECSCTFREICLHE GVTFEVHVNTSQRGFQQKLLYPNSGREGTAAQNFSCFIYNADLMNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHL DNLSGLTSRNYFLVNGTSREIGIQFFDSLLDTKKIERFNPPSNVTVRCNTTHCLVRWKQPRTYQKLSYLDFQYQLDVHRKNTQPGTENLL |
| P15509-5 | MLLLVTSLLLCELPHPAFLLIPEKSDLRTVAPASSLNVRFDSRTMNLSWDCQENTTFSKCFLTDKKNRVVEPRLSNNECSCTFREICLHE GVTFEVHVNTSQRGFQQKLLYPNSGREGTAAQNFSCFIYNADLMNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHL DNLSGLTSRNYFLVNGTSREIGIQFFDSLLDTKKIERFNPPSNVTVRCNTTHCLVRWKQPRTYQKLSYLDFQYQLDVHRKNTQPGTENLL INVSGDLENRYNFPSSEPRAKHSVKIRAADVRILNWSSWSEAIEFDHLGGIHPRGRERLPRRGLDREGNYLRPRGCRNGMDISASATRGN |
| P15509-6 | MLLLVTSLLLCELPHPAFLLIPEKSDLRTVAPASSLNVRFDSRTMNLSWDCQENTTFSKCFLTDKKNRVVEPRLSNNECSCTFREICLHE GVTFEVHVNTSQRGFQQKLLYPNSGREGTAAQNFSCFIYNADLMNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHL |
| P15509-7 | MLLLVTSLLLCELPHPAFLLIPEKSDLRTVAPASSLNVRFDSRTMNLSWDCQENTTFSKCFLTDKKNRVVEPRLSNNECSCTFREICLHE GVTFEVHVNTSQRGFQQKLLYPNSGREGTAAQNFSCFIYNADLMNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHL DNLSGLTSRNYFLVNGTSREIGIQFFDSLLDTKKIERFNPPSNVTVRCNTTHCLVRWKQPRTYQKLSYLDFQYQLDVHRKNTQPGTENLL INVSGDLENRYNFPSSEPRAKHSVKIRAADVRILNWSSWSEAIEFGSHSVTQAGVQWHNLGSLQPPSPRLKRFSCLRLPGSDDGNLGSVY |
| P15509-8 | MNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHLDNLSGLTSRNYFLVNGTSREIGIQFFDSLLDTKKIERFNPPSN VTVRCNTTHCLVRWKQPRTYQKLSYLDFQYQLDVHRKNTQPGTENLLINVSGDLENRYNFPSSEPRAKHSVKIRAADVRILNWSSWSEAI |
Protein Functional Features |
Main function of this protein. (from UniProt) |
| CSF2RA (go to UniProt):P15509 |
Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P15509 | Topological domain | 23 | 320 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=318;End=333 |
| P15509 | Topological domain | 23 | 320 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=271;End=286 |
| P15509 | Topological domain | 23 | 320 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=287;End=400 |
| P15509 | Topological domain | 23 | 320 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=316;End=400 |
| P15509 | Topological domain | 23 | 320 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=216;End=233 |
| P15509 | Topological domain | 23 | 320 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=234;End=400 |
| P15509 | Topological domain | 23 | 320 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=315;End=315 |
| P15509 | Topological domain | 23 | 320 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=1;End=133 |
| P15509 | Transmembrane | 321 | 346 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=318;End=333 |
| P15509 | Transmembrane | 321 | 346 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=334;End=400 |
| P15509 | Transmembrane | 321 | 346 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=287;End=400 |
| P15509 | Transmembrane | 321 | 346 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=316;End=400 |
| P15509 | Transmembrane | 321 | 346 | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=234;End=400 |
| P15509 | Topological domain | 347 | 400 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=376;End=400 |
| P15509 | Topological domain | 347 | 400 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=334;End=400 |
| P15509 | Topological domain | 347 | 400 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=287;End=400 |
| P15509 | Topological domain | 347 | 400 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=316;End=400 |
| P15509 | Topological domain | 347 | 400 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=234;End=400 |
| P15509 | Domain | 220 | 320 | Note=Fibronectin type-III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Substitution;Start=318;End=333 |
| P15509 | Domain | 220 | 320 | Note=Fibronectin type-III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Substitution;Start=271;End=286 |
| P15509 | Domain | 220 | 320 | Note=Fibronectin type-III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Deletion;Start=287;End=400 |
| P15509 | Domain | 220 | 320 | Note=Fibronectin type-III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Substitution;Start=316;End=400 |
| P15509 | Domain | 220 | 320 | Note=Fibronectin type-III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Substitution;Start=216;End=233 |
| P15509 | Domain | 220 | 320 | Note=Fibronectin type-III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Deletion;Start=234;End=400 |
| P15509 | Domain | 220 | 320 | Note=Fibronectin type-III;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 | Type=Substitution;Start=315;End=315 |
| P15509 | Motif | 306 | 310 | Note=WSXWS motif | Type=Deletion;Start=287;End=400 |
| P15509 | Motif | 306 | 310 | Note=WSXWS motif | Type=Deletion;Start=234;End=400 |
| P15509 | Motif | 355 | 363 | Note=Box 1 motif | Type=Deletion;Start=334;End=400 |
| P15509 | Motif | 355 | 363 | Note=Box 1 motif | Type=Deletion;Start=287;End=400 |
| P15509 | Motif | 355 | 363 | Note=Box 1 motif | Type=Substitution;Start=316;End=400 |
| P15509 | Motif | 355 | 363 | Note=Box 1 motif | Type=Deletion;Start=234;End=400 |
Gene Isoform Structures and Expression Levels for CSF2RA |
Gene structures of our canonical and alternative spliced genes of CSF2RA* Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
Expression levels of gene isoforms across GTEx. |
Expression levels of gene isoforms across TCGA. |
Protein Structures |
PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of P15509-1 |
| 3D view using mol* of P15509-2 |
| 3D view using mol* of P15509-3 |
| 3D view using mol* of P15509-4 |
| 3D view using mol* of P15509-5 |
| 3D view using mol* of P15509-6 |
| 3D view using mol* of P15509-7 |
| 3D view using mol* of P15509-8 |
pLDDT Score Distribution |
pLDDT score distribution of the predicted protein structures from AlphaFold2* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
Ramachandran Plot of Protein Structures |
Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of P15509-1 |
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| Ramachandran plot of P15509-6 |
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| Ramachandran plot of P15509-7 |
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Potential Active Site Information |
The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P15509-1 | 1.073 | 109 | 1.004 | 188.993 | 0.331 | 0.808 | 1.157 | 0.88 | 1.289 | 0.683 | 0.683 | 42,43,44,45,82,83,84,85,86,155,156,157,159,160,162 ,189,190,191,193,209 |
| P15509-2 | 1.065 | 98 | 1.028 | 179.389 | 0.347 | 0.807 | 1.174 | 1.001 | 1.186 | 0.844 | 0.61 | 42,43,44,45,82,83,84,85,86,155,156,157,158,159,160 ,189,190,191,209 |
| P15509-3 | 1.066 | 103 | 1.012 | 172.529 | 0.368 | 0.797 | 1.105 | 0.757 | 1.247 | 0.607 | 0.678 | 44,45,46,82,83,84,85,86,155,156,157,158,159,160,18 9,190,191,209 |
| P15509-4 | 1.066 | 98 | 1.03 | 163.268 | 0.391 | 0.808 | 1.073 | 0.757 | 1.182 | 0.641 | 0.536 | 44,45,82,83,84,85,86,155,156,157,159,160,162,189,1 90,191,209 |
| P15509-5 | 1.078 | 107 | 1.016 | 184.191 | 0.34 | 0.815 | 1.132 | 1.132 | 1.266 | 0.894 | 0.512 | 42,43,44,45,46,82,83,84,85,86,155,156,157,159,160, 189,190,191,209 |
| P15509-6 | 1.072 | 115 | 1.086 | 257.936 | 0.398 | 0.802 | 1.058 | 1.004 | 1.03 | 0.975 | 1.116 | 43,44,45,46,82,83,84,85,86,155,156,157,159,160,162 ,189,190,191,209 |
| P15509-7 | 1.088 | 100 | 1.04 | 181.104 | 0.346 | 0.829 | 1.142 | 1.149 | 1.218 | 0.943 | 0.475 | 44,45,46,82,83,84,85,86,155,156,157,159,160,189,19 0,191,209 |
| P15509-8 | 1.009 | 137 | 1.082 | 382.445 | 0.717 | 0.61 | 0.789 | 1.076 | 0.688 | 1.563 | 0.631 | 1,2,3,4,5,6,7,8,9,10,11,12,17,19,50,53,57,59,61,68 ,69,70,71,73,74,75,77,79,82,83,84,85,86,87,88,89,1 05,106,107,108,109,110,174,175 |
Protein Structure and Feature Comparision |
Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of P15509-1_P15509-1_4rs1_B.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P15509-1_4rs1_B_P15509-2.pdb |
| 3D view using mol* of P15509-1_4rs1_B_P15509-3.pdb |
| 3D view using mol* of P15509-1_4rs1_B_P15509-4.pdb |
| 3D view using mol* of P15509-1_4rs1_B_P15509-5.pdb |
| 3D view using mol* of P15509-1_4rs1_B_P15509-6.pdb |
| 3D view using mol* of P15509-1_4rs1_B_P15509-7.pdb |
| 3D view using mol* of P15509-1_4rs1_B_P15509-8.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P15509-1_P15509-2.pdb |
| 3D view using mol* of P15509-1_P15509-3.pdb |
| 3D view using mol* of P15509-1_P15509-4.pdb |
| 3D view using mol* of P15509-1_P15509-5.pdb |
| 3D view using mol* of P15509-1_P15509-6.pdb |
| 3D view using mol* of P15509-1_P15509-7.pdb |
| 3D view using mol* of P15509-1_P15509-8.pdb |
Protein Feature Comparison of the protein sequendary structures among the protiens. |
Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
Protein-Protein Interaction |
Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to CSF2RA |
Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| P15509 | CSF2RA | DB05194 | KB002 | investigational | |
| P15509 | CSF2RA | DB05386 | Regramostim | investigational | |
| P15509 | CSF2RA | DB10770 | Foreskin fibroblast (neonatal) | approved | agonist |
| P15509 | CSF2RA | DB11338 | Clove oil | approved, nutraceutical | |
| P15509 | CSF2RA | DB00020 | Sargramostim | approved, investigational | agonist |
| P15509 | CSF2RA | DB10772 | Foreskin keratinocyte (neonatal) | approved | agonist |
Related Diseases to CSF2RA |
Previous studies relating to the alternative splicing of CSF2RA and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| CSF2RA | 9625584 | Cloning and sequencing of an alternative splicing-derived cDNA variant of the GM-CSF receptor alpha subunit, which encodes a truncated protein. | GM-CSF interacts with the low affinity GM-CSF receptor alpha-subunit, which leads to high affinity association with the alpha-subunit/common beta-subunit complex and transduction of intracellular signals leading to proliferation, differentiation, and/or activation of hemopoietic cells, predominantly in the neutrophil and monocyte/macrophage lineages. Several alternative splicing-derived variants of the GM-CSF receptor alpha-subunit have been described previously by this and other laboratories. A newly discovered alternative-splicing derived variant was isolated from the peripheral blood mononuclear cells of a patient with juvenile myelomonocytic leukemia. This variant lacks 397 base pairs corresponding to exons 8-11 of the wild type GM-CSF receptor alpha-subunit cDNA and potentially encodes a 233 amino acid protein lacking a membrane-anchoring domain and creating the fourth known potential soluble isoform of the alpha-subunit of the GM-CSF receptor. | D015477 | Leukemia, Myelomonocytic, Chronic |
Clinically important variants in CSF2RA |
(ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
| P15509 | P15509-1 | CSF2RA | single nucleotide variant | p.Arg164Gln | Benign/Likely benign |
| P15509 | P15509-1 | CSF2RA | single nucleotide variant | p.Arg164Gln | Benign/Likely benign |
| P15509 | P15509-1 | CSF2RA | single nucleotide variant | p.Arg164Gln | Benign/Likely benign |
| P15509 | P15509-1 | CSF2RA | single nucleotide variant | p.Arg164Gln | Benign/Likely benign |
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