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P15328

- FOLR1_HUMAN

UniProt

P15328 - FOLR1_HUMAN

Protein

Folate receptor alpha

Gene

FOLR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    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.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei103 – 1031Folate1 Publication
    Binding sitei107 – 1071Folate1 Publication
    Binding sitei196 – 1961Folate1 Publication

    GO - Molecular functioni

    1. folic acid binding Source: UniProtKB
    2. folic acid transporter activity Source: UniProtKB
    3. receptor activity Source: ProtInc

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. folic acid metabolic process Source: Ensembl
    3. folic acid transport Source: UniProtKB
    4. receptor-mediated endocytosis Source: ProtInc

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Folate-binding

    Protein family/group databases

    TCDBi9.B.92.1.1. the folate receptor (fr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Folate receptor alpha
    Short name:
    FR-alpha
    Alternative name(s):
    Adult folate-binding protein
    Short name:
    FBP
    Folate receptor 1
    Folate receptor, adult
    KB cells FBP
    Ovarian tumor-associated antigen MOv18
    Gene namesi
    Name:FOLR1
    Synonyms:FOLR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3791. FOLR1.

    Subcellular locationi

    Cell membrane; Lipid-anchorGPI-anchor. Secreted Curated. Cytoplasmic vesicle. Cytoplasmic vesicleclathrin-coated vesicle. Endosome. Apical cell membrane By similarity
    Note: Endocytosed into cytoplasmic vesicles and then recycled to the cell membrane.

    GO - Cellular componenti

    1. anchored component of external side of plasma membrane Source: UniProtKB
    2. apical plasma membrane Source: UniProtKB-SubCell
    3. brush border membrane Source: Ensembl
    4. clathrin-coated vesicle Source: UniProtKB-SubCell
    5. endosome Source: UniProtKB-SubCell
    6. extracellular vesicular exosome Source: UniProt
    7. integral component of plasma membrane Source: ProtInc
    8. membrane Source: ProtInc
    9. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Endosome, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Neurodegeneration due to cerebral folate transport deficiency (NCFTD) [MIM:613068]: A neurodegenerative disorder resulting from brain-specific folate deficiency early in life. Onset is apparent in late infancy with severe developmental regression, movement disturbances, epilepsy and leukodystrophy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi82 – 821Y → A: Slightly reduced affinity for folate. 1 Publication
    Mutagenesisi103 – 1031D → A: Strongly reduced affinity for folate. 1 Publication
    Mutagenesisi107 – 1071Y → A: Moderately reduced affinity for folate. 1 Publication
    Mutagenesisi124 – 1241W → A: Moderately reduced affinity for folate. 1 Publication
    Mutagenesisi125 – 1251R → A: Moderately reduced affinity for folate. 1 Publication
    Mutagenesisi128 – 1281R → A: Moderately reduced affinity for folate. 1 Publication
    Mutagenesisi157 – 1571H → A: Moderately reduced affinity for folate. 1 Publication
    Mutagenesisi162 – 1621W → A: Moderately reduced affinity for folate. 1 Publication
    Mutagenesisi196 – 1961S → A: Moderately reduced affinity for folate. 1 Publication

    Keywords - Diseasei

    Neurodegeneration

    Organism-specific databases

    MIMi613068. phenotype.
    Orphaneti217382. Neurodegenerative syndrome due to cerebral folate transport deficiency.
    PharmGKBiPA28207.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 234210Folate receptor alphaPRO_0000008802Add
    BLAST
    Propeptidei235 – 25723Removed in mature formPRO_0000008803Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi37 ↔ 65
    Disulfide bondi57 ↔ 105
    Disulfide bondi66 ↔ 109
    Glycosylationi69 – 691N-linked (GlcNAc...)2 Publications
    Disulfide bondi89 ↔ 175
    Disulfide bondi96 ↔ 146
    Disulfide bondi135 ↔ 209
    Disulfide bondi139 ↔ 189
    Disulfide bondi152 ↔ 169
    Glycosylationi161 – 1611N-linked (GlcNAc...)3 Publications
    Glycosylationi201 – 2011N-linked (GlcNAc...)3 Publications
    Lipidationi234 – 2341GPI-anchor amidated serine2 Publications

    Post-translational modificationi

    The secreted form is derived from the membrane-bound form either by cleavage of the GPI anchor, or/and by proteolysis catalyzed by a metalloprotease.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiP15328.
    PaxDbiP15328.
    PeptideAtlasiP15328.
    PRIDEiP15328.

    Expressioni

    Tissue specificityi

    Primarily expressed in tissues of epithelial origin. Expression is increased in malignant tissues. Expressed in kidney, lung and cerebellum. Detected in placenta and thymus epithelium.3 Publications

    Gene expression databases

    ArrayExpressiP15328.
    BgeeiP15328.
    CleanExiHS_FOLR1.
    GenevestigatoriP15328.

    Interactioni

    Protein-protein interaction databases

    BioGridi108631. 14 interactions.
    IntActiP15328. 11 interactions.
    STRINGi9606.ENSP00000308137.

    Structurei

    Secondary structure

    1
    257
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 333
    Beta strandi48 – 503
    Turni53 – 564
    Helixi58 – 603
    Beta strandi63 – 675
    Helixi68 – 736
    Turni81 – 833
    Turni86 – 894
    Helixi94 – 10916
    Helixi114 – 1163
    Beta strandi117 – 1226
    Beta strandi124 – 1263
    Helixi136 – 14510
    Turni146 – 1483
    Beta strandi150 – 1523
    Beta strandi156 – 1583
    Helixi172 – 1743
    Helixi178 – 1814
    Helixi185 – 1917
    Turni192 – 1954
    Beta strandi206 – 2105
    Helixi216 – 2183
    Helixi222 – 23211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4KM6X-ray1.55A30-234[»]
    4KM7X-ray1.80A/B28-234[»]
    4KMXX-ray2.20A28-234[»]
    4LRHX-ray2.80A/B/C/D/E/F/G/H23-235[»]
    ProteinModelPortaliP15328.
    SMRiP15328. Positions 30-233.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni124 – 1285Folate binding
    Regioni157 – 1626Folate binding

    Sequence similaritiesi

    Belongs to the folate receptor family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG26606.
    HOGENOMiHOG000006539.
    HOVERGENiHBG039612.
    InParanoidiP15328.
    KOiK13649.
    OMAiNWTSGFN.
    OrthoDBiEOG7K6PW3.
    PhylomeDBiP15328.
    TreeFamiTF328532.

    Family and domain databases

    InterProiIPR004269. Folate_rcpt.
    IPR018143. Folate_rcpt-like.
    [Graphical view]
    PANTHERiPTHR10517. PTHR10517. 1 hit.
    PfamiPF03024. Folate_rec. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15328-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQRMTTQLL LLLVWVAVVG EAQTRIAWAR TELLNVCMNA KHHKEKPGPE    50
    DKLHEQCRPW RKNACCSTNT SQEAHKDVSY LYRFNWNHCG EMAPACKRHF 100
    IQDTCLYECS PNLGPWIQQV DQSWRKERVL NVPLCKEDCE QWWEDCRTSY 150
    TCKSNWHKGW NWTSGFNKCA VGAACQPFHF YFPTPTVLCN EIWTHSYKVS 200
    NYSRGSGRCI QMWFDPAQGN PNEEVARFYA AAMSGAGPWA AWPFLLSLAL 250
    MLLWLLS 257
    Length:257
    Mass (Da):29,819
    Last modified:June 1, 1994 - v3
    Checksum:iD458D8BB047C96A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti180 – 1801F → L in BAD97247. 1 PublicationCurated
    Sequence conflicti184 – 1841T → S in AAA74896. (PubMed:2538429)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281W → R.
    Corresponds to variant rs7928649 [ dbSNP | Ensembl ].
    VAR_059284
    Natural varianti160 – 1601W → C.
    Corresponds to variant rs1801932 [ dbSNP | Ensembl ].
    VAR_011963

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05013 mRNA. Translation: AAA35823.1.
    M28099 mRNA. Translation: AAA35822.1.
    X62753 mRNA. Translation: CAA44610.1.
    U20391 Genomic DNA. Translation: AAB05827.1.
    U78793 mRNA. Translation: AAB39751.1.
    U78794 mRNA. Translation: AAB39752.1.
    BT007158 mRNA. Translation: AAP35822.1.
    CR542019 mRNA. Translation: CAG46816.1.
    AK223527 mRNA. Translation: BAD97247.1.
    CH471076 Genomic DNA. Translation: EAW74848.1.
    BC002947 mRNA. Translation: AAH02947.1.
    M25317 mRNA. Translation: AAA74896.1.
    CCDSiCCDS8211.1.
    PIRiA44904. A45753.
    RefSeqiNP_000793.1. NM_000802.3.
    NP_057936.1. NM_016724.2.
    NP_057937.1. NM_016725.2.
    NP_057941.1. NM_016729.2.
    UniGeneiHs.73769.

    Genome annotation databases

    EnsembliENST00000312293; ENSP00000308137; ENSG00000110195.
    ENST00000393676; ENSP00000377281; ENSG00000110195.
    ENST00000393679; ENSP00000377284; ENSG00000110195.
    ENST00000393681; ENSP00000377286; ENSG00000110195.
    GeneIDi2348.
    KEGGihsa:2348.
    UCSCiuc001orz.2. human.

    Polymorphism databases

    DMDMi544337.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05013 mRNA. Translation: AAA35823.1 .
    M28099 mRNA. Translation: AAA35822.1 .
    X62753 mRNA. Translation: CAA44610.1 .
    U20391 Genomic DNA. Translation: AAB05827.1 .
    U78793 mRNA. Translation: AAB39751.1 .
    U78794 mRNA. Translation: AAB39752.1 .
    BT007158 mRNA. Translation: AAP35822.1 .
    CR542019 mRNA. Translation: CAG46816.1 .
    AK223527 mRNA. Translation: BAD97247.1 .
    CH471076 Genomic DNA. Translation: EAW74848.1 .
    BC002947 mRNA. Translation: AAH02947.1 .
    M25317 mRNA. Translation: AAA74896.1 .
    CCDSi CCDS8211.1.
    PIRi A44904. A45753.
    RefSeqi NP_000793.1. NM_000802.3.
    NP_057936.1. NM_016724.2.
    NP_057937.1. NM_016725.2.
    NP_057941.1. NM_016729.2.
    UniGenei Hs.73769.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4KM6 X-ray 1.55 A 30-234 [» ]
    4KM7 X-ray 1.80 A/B 28-234 [» ]
    4KMX X-ray 2.20 A 28-234 [» ]
    4LRH X-ray 2.80 A/B/C/D/E/F/G/H 23-235 [» ]
    ProteinModelPortali P15328.
    SMRi P15328. Positions 30-233.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108631. 14 interactions.
    IntActi P15328. 11 interactions.
    STRINGi 9606.ENSP00000308137.

    Chemistry

    BindingDBi P15328.
    ChEMBLi CHEMBL2121.

    Protein family/group databases

    TCDBi 9.B.92.1.1. the folate receptor (fr) family.

    Polymorphism databases

    DMDMi 544337.

    Proteomic databases

    MaxQBi P15328.
    PaxDbi P15328.
    PeptideAtlasi P15328.
    PRIDEi P15328.

    Protocols and materials databases

    DNASUi 2348.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312293 ; ENSP00000308137 ; ENSG00000110195 .
    ENST00000393676 ; ENSP00000377281 ; ENSG00000110195 .
    ENST00000393679 ; ENSP00000377284 ; ENSG00000110195 .
    ENST00000393681 ; ENSP00000377286 ; ENSG00000110195 .
    GeneIDi 2348.
    KEGGi hsa:2348.
    UCSCi uc001orz.2. human.

    Organism-specific databases

    CTDi 2348.
    GeneCardsi GC11P071900.
    HGNCi HGNC:3791. FOLR1.
    MIMi 136430. gene.
    613068. phenotype.
    neXtProti NX_P15328.
    Orphaneti 217382. Neurodegenerative syndrome due to cerebral folate transport deficiency.
    PharmGKBi PA28207.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG26606.
    HOGENOMi HOG000006539.
    HOVERGENi HBG039612.
    InParanoidi P15328.
    KOi K13649.
    OMAi NWTSGFN.
    OrthoDBi EOG7K6PW3.
    PhylomeDBi P15328.
    TreeFami TF328532.

    Miscellaneous databases

    GeneWikii Folate_receptor_1.
    GenomeRNAii 2348.
    NextBioi 9519.
    PROi P15328.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15328.
    Bgeei P15328.
    CleanExi HS_FOLR1.
    Genevestigatori P15328.

    Family and domain databases

    InterProi IPR004269. Folate_rcpt.
    IPR018143. Folate_rcpt-like.
    [Graphical view ]
    PANTHERi PTHR10517. PTHR10517. 1 hit.
    Pfami PF03024. Folate_rec. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of the human folate-binding protein cDNA from placenta and malignant tissue culture (KB) cells."
      Elwood P.C.
      J. Biol. Chem. 264:14893-14901(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY.
    2. "Complementary DNA for the folate binding protein correctly predicts anchoring to the membrane by glycosyl-phosphatidylinositol."
      Lacey S.W., Sanders J.M., Rothberg K.G., Anderson R.G.W., Kamen B.A.
      J. Clin. Invest. 84:715-720(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. "Folate-binding protein is a marker for ovarian cancer."
      Campbell I.G., Jones T.A., Foulkes W.D., Trowsdale J.
      Cancer Res. 51:5329-5338(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.
    4. "Cloning of a tumor-associated antigen: MOv18 and MOv19 antibodies recognize a folate-binding protein."
      Coney L.R., Tomassetti A., Carayannopoulos L., Frasca V., Kamen B.A., Colnaghi M.I., Zurawski V.R. Jr.
      Cancer Res. 51:6125-6132(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-56.
      Tissue: Ovarian carcinoma.
    5. "Genomic organization of the gene and a related pseudogene for a human folate binding protein."
      Sadasivan E., Cedeno M., Rothenberg S.P.
      Biochim. Biophys. Acta 1131:91-94(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "The divergent 5' termini of the alpha human folate receptor (hFR) mRNAs originate from two tissue-specific promoters and alternative splicing: characterization of the alpha hFR gene structure."
      Elwood P.C., Nachmanoff K., Saikawa Y., Page S.T., Pacheco P., Roberts S., Chung K.-N.
      Biochemistry 36:1467-1478(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF 1-56, TISSUE SPECIFICITY.
      Tissue: Lymphocyte.
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney proximal tubule.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    12. "The complete amino acid sequence of a human folate binding protein from KB cells determined from the cDNA."
      Sadasivan E., Rothenberg S.P.
      J. Biol. Chem. 264:5806-5811(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-249.
    13. "Purified membrane and soluble folate binding proteins from cultured KB cells have similar amino acid compositions and molecular weights but differ in fatty acid acylation."
      Luhrs C.A., Pitiranggon P., da Costa M., Rothenberg S.P., Slomiany B.L., Brink L., Tous G.I., Stein S.
      Proc. Natl. Acad. Sci. U.S.A. 84:6546-6549(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-43, SUBCELLULAR LOCATION.
    14. "UMSCC38 cells amplified at 11q13 for the folate receptor synthesize a mutant nonfunctional folate receptor."
      Orr R.B., Kamen B.A.
      Cancer Res. 54:3905-3911(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "Preferred sites of glycosylphosphatidylinositol modification in folate receptors and constraints in the primary structure of the hydrophobic portion of the signal."
      Yan W., Ratnam M.
      Biochemistry 34:14594-14600(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR AT SER-234, SUBCELLULAR LOCATION.
    16. Cited for: FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION.
    17. "Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."
      Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.
      Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Computational approach for identification and characterization of GPI-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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR AT SER-234, IDENTIFICATION BY MASS SPECTROMETRY.
    20. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
      Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
      Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-161 AND ASN-201.
      Tissue: Milk.
    21. "Folate receptor alpha defect causes cerebral folate transport deficiency: a treatable neurodegenerative disorder associated with disturbed myelin metabolism."
      Steinfeld R., Grapp M., Kraetzner R., Dreha-Kulaczewski S., Helms G., Dechent P., Wevers R., Grosso S., Gaertner J.
      Am. J. Hum. Genet. 85:354-363(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN NEURODEGENERATION DUE TO CEREBRAL FOLATE TRANSPORT DEFICIENCY.
    22. "Structural basis for molecular recognition of folic acid by folate receptors."
      Chen C., Ke J., Zhou X.E., Yi W., Brunzelle J.S., Li J., Yong E.L., Xu H.E., Melcher K.
      Nature 500:486-489(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-235 IN COMPLEX WITH FOLATE, FUNCTION, MUTAGENESIS OF TYR-82; ASP-103; TYR-107; TRP-124; ARG-125; ARG-128; HIS-157; TRP-162 AND SER-196, DISULFIDE BONDS, GLYCOSYLATION AT ASN-69; ASN-161 AND ASN-201.
    23. "Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition."
      Wibowo A.S., Singh M., Reeder K.M., Carter J.J., Kovach A.R., Meng W., Ratnam M., Zhang F., Dann C.E. III
      Proc. Natl. Acad. Sci. U.S.A. 110:15180-15188(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 30-234, FUNCTION, GLYCOSYLATION AT ASN-69; ASN-161 AND ASN-201, DISULFIDE BONDS.

    Entry informationi

    Entry nameiFOLR1_HUMAN
    AccessioniPrimary (citable) accession number: P15328
    Secondary accession number(s): Q53EW2
    , Q6FGT8, Q6LC90, Q9UCT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3