UniProt ID | FOLR1_HUMAN | |
---|---|---|
UniProt AC | P15328 | |
Protein Name | Folate receptor alpha | |
Gene Name | FOLR1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 257 | |
Subcellular Localization |
Cell membrane Lipid-anchor, GPI-anchor. Secreted . Cytoplasmic vesicle. Cytoplasmic vesicle, clathrin-coated vesicle. Endosome. Apical cell membrane. Endocytosed into cytoplasmic vesicles and then recycled to the cell membrane. |
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Protein Description | Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH. Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release. Required for normal embryonic development and normal cell proliferation.. | |
Protein Sequence | MAQRMTTQLLLLLVWVAVVGEAQTRIAWARTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCLYECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPTVLCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMSGAGPWAAWPFLLSLALMLLWLLS | |
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 |
---|---|---|---|---|---|
69 | N-linked_Glycosylation | KNACCSTNTSQEAHK HCCCCCCCCCHHHHH | 22.80 | 23934049 | |
97 | Ubiquitination | GEMAPACKRHFIQDT CCCCHHHHHHHCCCC | 51.52 | - | |
136 | Ubiquitination | VLNVPLCKEDCEQWW HCCCCCCHHHHHHHH | 65.36 | - | |
161 | N-linked_Glycosylation | SNWHKGWNWTSGFNK CCCCCCCCCCCCCCC | 40.59 | 18780401 | |
189 | S-palmitoylation | FPTPTVLCNEIWTHS CCCCCEECCCHHCCE | 3.59 | 29575903 | |
201 | N-linked_Glycosylation | THSYKVSNYSRGSGR CCEECCCCCCCCCCC | 41.61 | 18780401 | |
201 | N-linked_Glycosylation | THSYKVSNYSRGSGR CCEECCCCCCCCCCC | 41.61 | 20068230 | |
234 | GPI-anchor | RFYAAAMSGAGPWAA HHHHHHHCCCCHHHH | 22.29 | 7578066 |
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 FOLR1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of FOLR1_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 FOLR1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
GSHR_HUMAN | GSR | physical | 22939629 | |
PSB2_HUMAN | PSMB2 | physical | 22939629 | |
IMDH2_HUMAN | IMPDH2 | physical | 22939629 | |
IRAK3_HUMAN | IRAK3 | physical | 21988832 | |
CNDH2_HUMAN | NCAPH2 | physical | 21988832 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
H01295 | Neurodegeneration due to cerebral folate transport deficiency | |||||
OMIM Disease | ||||||
613068 | Neurodegeneration due to cerebral folate transport deficiency (NCFTD) | |||||
Kegg Drug | ||||||
D09343 | Farletuzumab (genetical recombination) (JAN); Farletuzumab (USAN) | |||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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GPI-anchor | |
Reference | PubMed |
"Computational approach for identification and characterization ofGPI-anchored peptides in proteomics experiments."; Omaetxebarria M.J., Elortza F., Rodriguez-Suarez E., Aloria K.,Arizmendi J.M., Jensen O.N., Matthiesen R.; Proteomics 7:1951-1960(2007). Cited for: GPI-ANCHOR AT SER-234, AND MASS SPECTROMETRY. | |
"Modification-specific proteomics of plasma membrane proteins:identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."; Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,Brodbeck U., Peck S.C., Jensen O.N.; J. Proteome Res. 5:935-943(2006). Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. | |
"Proteomic analysis of glycosylphosphatidylinositol-anchored membraneproteins."; Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C.,Jensen O.N.; Mol. Cell. Proteomics 2:1261-1270(2003). Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. | |
"Preferred sites of glycosylphosphatidylinositol modification infolate receptors and constraints in the primary structure of thehydrophobic portion of the signal."; Yan W., Ratnam M.; Biochemistry 34:14594-14600(1995). Cited for: GPI-ANCHOR AT SER-234. | |
N-linked Glycosylation | |
Reference | PubMed |
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry."; Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; Proteomics 8:3833-3847(2008). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-161 AND ASN-201, AND MASSSPECTROMETRY. |