FOLR1_HUMAN - dbPTM
FOLR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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.
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
69N-linked_GlycosylationKNACCSTNTSQEAHK
HCCCCCCCCCHHHHH
22.8023934049
97UbiquitinationGEMAPACKRHFIQDT
CCCCHHHHHHHCCCC
51.52-
136UbiquitinationVLNVPLCKEDCEQWW
HCCCCCCHHHHHHHH
65.36-
161N-linked_GlycosylationSNWHKGWNWTSGFNK
CCCCCCCCCCCCCCC
40.5918780401
189S-palmitoylationFPTPTVLCNEIWTHS
CCCCCEECCCHHCCE
3.5929575903
201N-linked_GlycosylationTHSYKVSNYSRGSGR
CCEECCCCCCCCCCC
41.6118780401
201N-linked_GlycosylationTHSYKVSNYSRGSGR
CCEECCCCCCCCCCC
41.6120068230
234GPI-anchorRFYAAAMSGAGPWAA
HHHHHHHCCCCHHHH
22.297578066

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 FOLR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOLR1_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 FOLR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GSHR_HUMANGSRphysical
22939629
PSB2_HUMANPSMB2physical
22939629
IMDH2_HUMANIMPDH2physical
22939629
IRAK3_HUMANIRAK3physical
21988832
CNDH2_HUMANNCAPH2physical
21988832

Drug and Disease Associations
Kegg Disease
H01295 Neurodegeneration due to cerebral folate transport deficiency
OMIM Disease
613068Neurodegeneration 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.
Regulatory Network of FOLR1_HUMAN

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Related Literatures of Post-Translational Modification
GPI-anchor
ReferencePubMed
"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
ReferencePubMed
"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.

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