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Q05932

- FOLC_HUMAN

UniProt

Q05932 - FOLC_HUMAN

Protein

Folylpolyglutamate synthase, mitochondrial

Gene

FPGS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Unsubstitued reduced folates are the preferred substrates. Metabolizes methotrexate (MTX) to polyglutamates.4 Publications

    Catalytic activityi

    ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).6 Publications

    Cofactori

    A monovalent cation. K+ is most effective, followed by NH4+ and Rb+. Na+, Li+ and Cs+ are ineffective.1 Publication

    Enzyme regulationi

    Activated by 10 mM sodium bicarbonate.1 Publication

    Kineticsi

    1. KM=201 µM for L-glutamate (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    2. KM=200 µM for MgATP (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    3. KM=59 µM for pteroylglutamic acid (PteGlu) (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    4. KM=16 µM for PteGlu2 (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    5. KM=20 µM for PteGlu3 (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    6. KM=12 µM for PteGlu4 (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    7. KM=64 µM for PteGlu5 (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    8. KM=0.81 µM for H2PteGlu (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    9. KM=47 µM for H2PteGlu2 (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    10. KM=1.6 µM for (6ambo)-tetrahydropteroylpoly-gamma-glutamate (H4PteGlu) (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    11. KM=4.4 µM for (6S)-H4PteGlu (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    12. KM=3.3 µM for (6S)-H4PteGlu2 (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    13. KM=1.4 µM for (6S)-H4PteGlu3 (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    14. KM=1.6 µM for (6S)-H4PteGlu4 (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    15. KM=1.4 µM for (6S)-H4PteGlu5 (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    16. KM=3.7 µM for (6R)-10-formyl-H4PteGlu (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    17. KM=2.7 µM for (6R)-10-formyl-H4PteGlu2 (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    18. KM=105 µM for (6S)-5-formyl-H4PteGlu (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    19. KM=13 µM for (6S)-5-formyl-H4PteGlu2 (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    20. KM=48 µM for (6S)-5-methyl-H4PteGlu (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    21. KM=4.4 µM for aminopterin (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    22. KM=55.5 µM for methotrexate (isoform 2, PubMed:17875718, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)2 Publications
    23. KM=52.6 µM for methotrexate (isoform 1, PubMed:17875718, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)2 Publications
    24. KM=71 µM for methotrexate (Glu-1) (isoform 2, PubMed:8662720, at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    25. KM=50 µM for methotrexate (Glu-2) (isoform 2, PubMed:8662720, at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    26. KM=148 µM for methotrexate (Glu-3) (isoform 2, PubMed:8662720, at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    27. KM=5.3 µM for 5-deazaacyclotetrahydrofolate (isoform 2, at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    28. KM=2.8 µM for 2-methyl-5,8-dideazaisofolate (isoform 2, at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)2 Publications
    29. KM=1702 µM for glutamic acid (isoform 2, PubMed:17875718, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)2 Publications
    30. KM=2068 µM for glutamic acid (isoform 1, PubMed:17875718, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)2 Publications

    Vmax=0.34 µmol/h/mg enzyme with methotrexate as substrate (isoform 2, PubMed:17875718, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)2 Publications

    Vmax=0.05 µmol/h/mg enzyme with methotrexate as substrate (isoform 1, PubMed:17875718, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)2 Publications

    Vmax=1.26 µmol/h/mg enzyme with glutamic acid as substrate (isoform 2, PubMed:17875718, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)2 Publications

    Vmax=0.25 µmol/h/mg enzyme with glutamic acid as substrate (isoform 1, PubMed:17875718, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)2 Publications

    pH dependencei

    Optimum pH is 9.6 (isoform 2).2 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi103 – 1097ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. tetrahydrofolylpolyglutamate synthase activity Source: ProtInc

    GO - Biological processi

    1. brain development Source: Ensembl
    2. folic acid metabolic process Source: Reactome
    3. liver development Source: Ensembl
    4. nucleobase-containing compound metabolic process Source: ProtInc
    5. one-carbon metabolic process Source: UniProtKB-KW
    6. organ regeneration Source: Ensembl
    7. small molecule metabolic process Source: Reactome
    8. vitamin metabolic process Source: Reactome
    9. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06237-MONOMER.
    ReactomeiREACT_11167. Metabolism of folate and pterines.
    UniPathwayiUPA00850.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Folylpolyglutamate synthase, mitochondrial (EC:6.3.2.17)
    Alternative name(s):
    Folylpoly-gamma-glutamate synthetase
    Short name:
    FPGS
    Tetrahydrofolylpolyglutamate synthase
    Short name:
    Tetrahydrofolate synthase
    Gene namesi
    Name:FPGS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:3824. FPGS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome
    3. mitochondrial inner membrane Source: UniProtKB-SubCell
    4. mitochondrial matrix Source: Reactome
    5. mitochondrion Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    MIMi136510. gene+phenotype.
    PharmGKBiPA167.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4242MitochondrionAdd
    BLAST
    Chaini43 – 587545Folylpolyglutamate synthase, mitochondrialPRO_0000010097Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ05932.
    PaxDbiQ05932.
    PRIDEiQ05932.

    PTM databases

    PhosphoSiteiQ05932.

    Expressioni

    Gene expression databases

    ArrayExpressiQ05932.
    BgeeiQ05932.
    CleanExiHS_FPGS.
    GenevestigatoriQ05932.

    Organism-specific databases

    HPAiHPA050488.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi108639. 1 interaction.
    STRINGi9606.ENSP00000362344.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05932.
    SMRiQ05932. Positions 60-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the folylpolyglutamate synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0285.
    HOGENOMiHOG000181278.
    HOVERGENiHBG003086.
    InParanoidiQ05932.
    KOiK01930.
    OMAiIPEMVEY.
    OrthoDBiEOG7T7GTN.
    PhylomeDBiQ05932.
    TreeFamiTF313956.

    Family and domain databases

    Gene3Di3.40.1190.10. 1 hit.
    3.90.190.20. 3 hits.
    InterProiIPR001645. Folylpolyglutamate_synth.
    IPR018109. Folylpolyglutamate_synth_CS.
    IPR023600. Folylpolyglutamate_synth_euk.
    IPR004101. Mur_ligase_C.
    IPR013221. Mur_ligase_cen.
    [Graphical view]
    PANTHERiPTHR11136. PTHR11136. 1 hit.
    PIRSFiPIRSF038895. FPGS. 1 hit.
    SUPFAMiSSF53244. SSF53244. 1 hit.
    SSF53623. SSF53623. 1 hit.
    TIGRFAMsiTIGR01499. folC. 1 hit.
    PROSITEiPS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
    PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. Align

    Isoform 1 (identifier: Q05932-1) [UniParc]FASTAAdd to Basket

    Also known as: Mitochondrial

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSRARSHLRA ALFLAAASAR GITTQVAARR GLSAWPVPQE PSMEYQDAVR    50
    MLNTLQTNAG YLEQVKRQRG DPQTQLEAME LYLARSGLQV EDLDRLNIIH 100
    VTGTKGKGST CAFTECILRS YGLKTGFFSS PHLVQVRERI RINGQPISPE 150
    LFTKYFWRLY HRLEETKDGS CVSMPPYFRF LTLMAFHVFL QEKVDLAVVE 200
    VGIGGAYDCT NIIRKPVVCG VSSLGIDHTS LLGDTVEKIA WQKGGIFKQG 250
    VPAFTVLQPE GPLAVLRDRA QQISCPLYLC PMLEALEEGG PPLTLGLEGE 300
    HQRSNAALAL QLAHCWLQRQ DRHGAGEPKA SRPGLLWQLP LAPVFQPTSH 350
    MRLGLRNTEW PGRTQVLRRG PLTWYLDGAH TASSAQACVR WFRQALQGRE 400
    RPSGGPEVRV LLFNATGDRD PAALLKLLQP CQFDYAVFCP NLTEVSSTGN 450
    ADQQNFTVTL DQVLLRCLEH QQHWNHLDEE QASPDLWSAP SPEPGGSASL 500
    LLAPHPPHTC SASSLVFSCI SHALQWISQG RDPIFQPPSP PKGLLTHPVA 550
    HSGASILREA AAIHVLVTGS LHLVGGVLKL LEPALSQ 587
    Length:587
    Mass (Da):64,609
    Last modified:October 1, 1996 - v3
    Checksum:i5AF81409F5F77E5C
    GO
    Isoform 2 (identifier: Q05932-2) [UniParc]FASTAAdd to Basket

    Also known as: Cytoplasmic

    The sequence of this isoform differs from the canonical sequence as follows:
         1-42: Missing.

    Note: Produced by alternative initiation at Met-43 of isoform 1.

    Show »
    Length:545
    Mass (Da):60,167
    Checksum:i59650383900A309E
    GO
    Isoform 3 (identifier: Q05932-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-42: Missing.
         43-50: Missing.

    Note: Produced by alternative splicing of isoform 1.

    Show »
    Length:537
    Mass (Da):59,174
    Checksum:i4FA022E884342D11
    GO
    Isoform 4 (identifier: Q05932-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         168-193: Missing.

    Note: Produced by alternative splicing of isoform 1.

    Show »
    Length:561
    Mass (Da):61,562
    Checksum:i243138601850E090
    GO

    Sequence cautioni

    The sequence AAA35852.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011V → A in BAG51826. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131F → L.1 Publication
    Corresponds to variant rs11554717 [ dbSNP | Ensembl ].
    VAR_066016
    Natural varianti22 – 221I → V.3 Publications
    Corresponds to variant rs10760502 [ dbSNP | Ensembl ].
    VAR_059305
    Natural varianti437 – 4371V → D.
    Corresponds to variant rs12686275 [ dbSNP | Ensembl ].
    VAR_043929
    Natural varianti466 – 4661R → C Expression reduced by 1.86-fold and Vmax with methotrexate as substrate reduced significantly. The intrinsic clearance of methotrexate is significantly reduced. Km of glutamic acid is increased 3.5-fold and apparent Vmax of it is reduced 3.4-fold. Reaction velocity at 100 nmol/L of pemetrexed is significantly reduced and folic acid dose-response curve is shifted to the right which corresponds to 4.32-fold increase in the EC(50) for folic acid. IC(50) of methotrexate is 1.84-fold higher and accumulation of a lower ratio of long-chain methotrexate polyglutamates to short-chain polyglutamates is detected. All results are for isoform 2 variant in comparison to the wild-type of it. 1 Publication
    Corresponds to variant rs35789560 [ dbSNP | Ensembl ].
    VAR_066017
    Natural varianti489 – 4891A → V.2 Publications
    Corresponds to variant rs17855900 [ dbSNP | Ensembl ].
    VAR_043930
    Natural varianti499 – 4991S → F Expression reduced by 2.11-fold and Vmax with methotrexate as substrate reduced significantly. The intrinsic clearance of methotrexate is significantly reduced. Apparent Vmax for glutamic acid is reduced 5-fold. Reaction velocity at 100 nmol/L of pemetrexed is significantly reduced and folic acid dose-response curve is shifted to the right which corresponds to 4.28-fold increase in the EC(50) for folic acid. IC(50) of methotrexate is 1.64-fold higher and accumulation of a lower ratio of long-chain methotrexate polyglutamates to short-chain polyglutamates is detected. All results are for isoform 2 variant in comparison to the wild-type of it. 1 Publication
    Corresponds to variant rs200314440 [ dbSNP | Ensembl ].
    VAR_066018
    Natural varianti528 – 5281S → T.
    Corresponds to variant rs34354111 [ dbSNP | Ensembl ].
    VAR_043931

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4242Missing in isoform 2 and isoform 3. 1 PublicationVSP_018733Add
    BLAST
    Alternative sequencei43 – 508Missing in isoform 3. 1 PublicationVSP_041959
    Alternative sequencei168 – 19326Missing in isoform 4. 1 PublicationVSP_041960Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK056920 mRNA. Translation: BAG51826.1.
    AK295309 mRNA. Translation: BAH12029.1.
    AL162586 Genomic DNA. Translation: CAI39770.1.
    AL162586 Genomic DNA. Translation: CAI39773.1.
    BC064393 mRNA. Translation: AAH64393.1.
    AH006037 Genomic DNA. Translation: AAC13871.1.
    M98045 mRNA. Translation: AAA35852.1. Different initiation.
    U14939 Genomic DNA. Translation: AAA85815.1.
    AH003340 Genomic DNA. Translation: AAA87568.1.
    CCDSiCCDS35148.1. [Q05932-1]
    CCDS35149.1. [Q05932-3]
    PIRiA46281.
    RefSeqiNP_001018088.1. NM_001018078.2. [Q05932-3]
    NP_001275732.1. NM_001288803.1. [Q05932-4]
    NP_004948.4. NM_004957.5. [Q05932-1]
    UniGeneiHs.335084.

    Genome annotation databases

    EnsembliENST00000373225; ENSP00000362322; ENSG00000136877. [Q05932-3]
    ENST00000373247; ENSP00000362344; ENSG00000136877. [Q05932-1]
    ENST00000393706; ENSP00000377309; ENSG00000136877. [Q05932-4]
    GeneIDi2356.
    KEGGihsa:2356.
    UCSCiuc004bsg.1. human. [Q05932-1]
    uc011mal.1. human. [Q05932-4]

    Polymorphism databases

    DMDMi1706884.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK056920 mRNA. Translation: BAG51826.1 .
    AK295309 mRNA. Translation: BAH12029.1 .
    AL162586 Genomic DNA. Translation: CAI39770.1 .
    AL162586 Genomic DNA. Translation: CAI39773.1 .
    BC064393 mRNA. Translation: AAH64393.1 .
    AH006037 Genomic DNA. Translation: AAC13871.1 .
    M98045 mRNA. Translation: AAA35852.1 . Different initiation.
    U14939 Genomic DNA. Translation: AAA85815.1 .
    AH003340 Genomic DNA. Translation: AAA87568.1 .
    CCDSi CCDS35148.1. [Q05932-1 ]
    CCDS35149.1. [Q05932-3 ]
    PIRi A46281.
    RefSeqi NP_001018088.1. NM_001018078.2. [Q05932-3 ]
    NP_001275732.1. NM_001288803.1. [Q05932-4 ]
    NP_004948.4. NM_004957.5. [Q05932-1 ]
    UniGenei Hs.335084.

    3D structure databases

    ProteinModelPortali Q05932.
    SMRi Q05932. Positions 60-441.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108639. 1 interaction.
    STRINGi 9606.ENSP00000362344.

    Chemistry

    BindingDBi Q05932.
    ChEMBLi CHEMBL3171.
    DrugBanki DB00142. L-Glutamic Acid.

    PTM databases

    PhosphoSitei Q05932.

    Polymorphism databases

    DMDMi 1706884.

    Proteomic databases

    MaxQBi Q05932.
    PaxDbi Q05932.
    PRIDEi Q05932.

    Protocols and materials databases

    DNASUi 2356.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373225 ; ENSP00000362322 ; ENSG00000136877 . [Q05932-3 ]
    ENST00000373247 ; ENSP00000362344 ; ENSG00000136877 . [Q05932-1 ]
    ENST00000393706 ; ENSP00000377309 ; ENSG00000136877 . [Q05932-4 ]
    GeneIDi 2356.
    KEGGi hsa:2356.
    UCSCi uc004bsg.1. human. [Q05932-1 ]
    uc011mal.1. human. [Q05932-4 ]

    Organism-specific databases

    CTDi 2356.
    GeneCardsi GC09P130556.
    HGNCi HGNC:3824. FPGS.
    HPAi HPA050488.
    MIMi 136510. gene+phenotype.
    neXtProti NX_Q05932.
    PharmGKBi PA167.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0285.
    HOGENOMi HOG000181278.
    HOVERGENi HBG003086.
    InParanoidi Q05932.
    KOi K01930.
    OMAi IPEMVEY.
    OrthoDBi EOG7T7GTN.
    PhylomeDBi Q05932.
    TreeFami TF313956.

    Enzyme and pathway databases

    UniPathwayi UPA00850 .
    BioCyci MetaCyc:HS06237-MONOMER.
    Reactomei REACT_11167. Metabolism of folate and pterines.

    Miscellaneous databases

    GeneWikii FPGS.
    GenomeRNAii 2356.
    NextBioi 9555.
    PROi Q05932.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05932.
    Bgeei Q05932.
    CleanExi HS_FPGS.
    Genevestigatori Q05932.

    Family and domain databases

    Gene3Di 3.40.1190.10. 1 hit.
    3.90.190.20. 3 hits.
    InterProi IPR001645. Folylpolyglutamate_synth.
    IPR018109. Folylpolyglutamate_synth_CS.
    IPR023600. Folylpolyglutamate_synth_euk.
    IPR004101. Mur_ligase_C.
    IPR013221. Mur_ligase_cen.
    [Graphical view ]
    PANTHERi PTHR11136. PTHR11136. 1 hit.
    PIRSFi PIRSF038895. FPGS. 1 hit.
    SUPFAMi SSF53244. SSF53244. 1 hit.
    SSF53623. SSF53623. 1 hit.
    TIGRFAMsi TIGR01499. folC. 1 hit.
    PROSITEi PS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
    PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), VARIANT VAL-22.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] (ISOFORM 1), VARIANTS VAL-22 AND VAL-489.
      Tissue: Lung.
    4. "Purification and properties of human cytosolic folylpoly-gamma-glutamate synthetase and organization, localization, and differential splicing of its gene."
      Chen L., Qi H., Korenberg J., Garrow T.A., Choi Y.J., Shane B.
      J. Biol. Chem. 271:13077-13087(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-353, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
      Tissue: Fibroblast.
    5. "Upstream organization of and multiple transcripts from the human folylpoly-gamma-glutamate synthetase gene."
      Freemantle S.J., Taylor S.M., Krystal G., Moran R.G.
      J. Biol. Chem. 270:9579-9584(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107, ALTERNATIVE INITIATION, VARIANT VAL-22.
      Tissue: Placenta.
    6. "Expression cloning of a human cDNA encoding folylpoly(gamma-glutamate) synthetase and determination of its primary structure."
      Garrow T.A., Admon A., Shane B.
      Proc. Natl. Acad. Sci. U.S.A. 89:9151-9155(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-587 (ISOFORM 1), CATALYTIC ACTIVITY.
      Tissue: Lymphocyte.
    7. "Structural organization of the human folypoly-gamma-glutamate synthetase gene: evidence for a single genomic locus."
      Taylor S.M., Freemantle S.J., Moran R.G.
      Cancer Res. 55:6030-6034(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 102-587.
      Tissue: Placenta.
    8. "Regulation of folate and one-carbon metabolism in mammalian cells. I. Folate metabolism in Chinese hamster ovary cells expressing Escherichia coli or human folylpoly-gamma-glutamate synthetase activity."
      Osborne C.B., Lowe K.E., Shane B.
      J. Biol. Chem. 268:21657-21664(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    9. "Regulation of folate and one-carbon metabolism in mammalian cells. II. Effect of folylpoly-gamma-glutamate synthetase substrate specificity and level on folate metabolism and folylpoly-gamma-glutamate specificity of metabolic cycles of one-carbon metabolism."
      Lowe K.E., Osborne C.B., Lin B.F., Kim J.S., Hsu J.C., Shane B.
      J. Biol. Chem. 268:21665-21673(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Regulation of folate and one-carbon metabolism in mammalian cells. III. Role of mitochondrial folylpoly-gamma-glutamate synthetase."
      Lin B.F., Huang R.F., Shane B.
      J. Biol. Chem. 268:21674-21679(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    11. "Regulation of folate and one-carbon metabolism in mammalian cells. IV. Role of folylpoly-gamma-glutamate synthetase in methotrexate metabolism and cytotoxicity."
      Kim J.S., Lowe K.E., Shane B.
      J. Biol. Chem. 268:21680-21685(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Submitochondrial localization of the mitochondrial isoform of folylpolyglutamate synthetase in CCRF-CEM human T-lymphoblastic leukemia cells."
      Nair J.R., McGuire J.J.
      Biochim. Biophys. Acta 1746:38-44(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "Identification and characterization of genetic variation in the folylpolyglutamate synthase gene."
      Leil T.A., Endo C., Adjei A.A., Dy G.K., Salavaggione O.E., Reid J.R., Ames M.M., Adjei A.A.
      Cancer Res. 67:8772-8782(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, VARIANTS LEU-13; CYS-466; VAL-489 AND PHE-499.
    14. "Concentration-dependent processivity of multiple glutamate ligations catalyzed by folylpoly-gamma-glutamate synthetase."
      Tomsho J.W., Moran R.G., Coward J.K.
      Biochemistry 47:9040-9050(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, REACTION MECHANISM.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFOLC_HUMAN
    AccessioniPrimary (citable) accession number: Q05932
    Secondary accession number(s): B3KPW4
    , B7Z2Z3, F5H0K6, Q5JU19, Q5JU22, Q6P2P6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 147 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3