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P15328

- FOLR1_HUMAN

UniProt

P15328 - FOLR1_HUMAN

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Protein

Folate receptor alpha

Gene

FOLR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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. brush border membrane Source: Ensembl
  3. cell surface Source: UniProtKB
  4. cytoplasmic vesicle Source: UniProtKB-KW
  5. endosome Source: UniProtKB-KW
  6. extracellular vesicular exosome Source: UniProtKB
  7. integral component of plasma membrane Source: ProtInc
  8. membrane Source: ProtInc
  9. plasma membrane Source: UniProtKB
Complete GO annotation...

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

BgeeiP15328.
CleanExiHS_FOLR1.
ExpressionAtlasiP15328. baseline and differential.
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.
GeneTreeiENSGT00390000010470.
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

        10         20         30         40         50
MAQRMTTQLL LLLVWVAVVG EAQTRIAWAR TELLNVCMNA KHHKEKPGPE
60 70 80 90 100
DKLHEQCRPW RKNACCSTNT SQEAHKDVSY LYRFNWNHCG EMAPACKRHF
110 120 130 140 150
IQDTCLYECS PNLGPWIQQV DQSWRKERVL NVPLCKEDCE QWWEDCRTSY
160 170 180 190 200
TCKSNWHKGW NWTSGFNKCA VGAACQPFHF YFPTPTVLCN EIWTHSYKVS
210 220 230 240 250
NYSRGSGRCI QMWFDPAQGN PNEEVARFYA AAMSGAGPWA AWPFLLSLAL

MLLWLLS
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.
DrugBanki DB00563. Methotrexate.

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.
GeneTreei ENSGT00390000010470.
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

Bgeei P15328.
CleanExi HS_FOLR1.
ExpressionAtlasi P15328. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 140 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