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Protein

Folylpolyglutamate synthase, mitochondrial

Gene

FPGS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Unsubstituted reduced folates are the preferred substrates. Metabolizes methotrexate (MTX) to polyglutamates.4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by 10 mM sodium bicarbonate.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)1 Publication
  23. KM=52.6 µM for methotrexate (isoform 1, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)1 Publication
  24. KM=71 µM for methotrexate (Glu-1) (isoform 2, at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)1 Publication
  25. KM=50 µM for methotrexate (Glu-2) (isoform 2, at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)1 Publication
  26. KM=148 µM for methotrexate (Glu-3) (isoform 2, at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)1 Publication
  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)1 Publication
  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)1 Publication
  29. KM=1702 µM for glutamic acid (isoform 2, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)1 Publication
  30. KM=2068 µM for glutamic acid (isoform 1, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)1 Publication
  1. Vmax=0.34 µmol/h/mg enzyme with methotrexate as substrate (isoform 2, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)1 Publication
  2. Vmax=0.05 µmol/h/mg enzyme with methotrexate as substrate (isoform 1, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)1 Publication
  3. Vmax=1.26 µmol/h/mg enzyme with glutamic acid as substrate (isoform 2, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)1 Publication
  4. Vmax=0.25 µmol/h/mg enzyme with glutamic acid as substrate (isoform 1, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)1 Publication

pH dependencei

Optimum pH is 9.6 (isoform 2).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tetrahydrofolylpolyglutamate biosynthesis

This protein is involved in the pathway tetrahydrofolylpolyglutamate biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolylpolyglutamate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi130Magnesium 1By similarity1
Metal bindingi200Magnesium 1By similarity1
Metal bindingi228Magnesium 2By similarity1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei363ATPBy similarity1
Binding sitei377ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi106 – 109ATPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLigase
Biological processOne-carbon metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS06237-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-196757 Metabolism of folate and pterines

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00850

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FPGS
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000136877.14

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3824 FPGS

Online Mendelian Inheritance in Man (OMIM)

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MIMi
136510 gene+phenotype

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q05932

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

DisGeNET

More...
DisGeNETi
2356
MIMi136510 gene+phenotype

Open Targets

More...
OpenTargetsi
ENSG00000136877

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA167

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3171

Drug and drug target database

More...
DrugBanki
DB00142 L-Glutamic Acid
DB00563 Methotrexate
DB06813 Pralatrexate
DB00293 Raltitrexed

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
FPGS

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1706884

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 42MitochondrionCombined sourcesAdd BLAST42
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001009743 – 587Folylpolyglutamate synthase, mitochondrialAdd BLAST545

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei43N-acetylmethionineCombined sources1
Modified residuei539PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q05932

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q05932

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q05932

PeptideAtlas

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PeptideAtlasi
Q05932

PRoteomics IDEntifications database

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PRIDEi
Q05932

ProteomicsDB human proteome resource

More...
ProteomicsDBi
58358
58359 [Q05932-2]
58360 [Q05932-3]
58361 [Q05932-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q05932

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q05932

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000136877 Expressed in 181 organ(s), highest expression level in right adrenal gland

CleanEx database of gene expression profiles

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CleanExi
HS_FPGS

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q05932 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q05932 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA050488

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108639, 9 interactors

Protein interaction database and analysis system

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IntActi
Q05932, 1 interactor

STRING: functional protein association networks

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STRINGi
9606.ENSP00000362344

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q05932

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q05932

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the folylpolyglutamate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2525 Eukaryota
COG0285 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000016526

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000181278

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG003086

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q05932

KEGG Orthology (KO)

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KOi
K01930

Identification of Orthologs from Complete Genome Data

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OMAi
HTFMLGN

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0DO0

Database for complete collections of gene phylogenies

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PhylomeDBi
Q05932

TreeFam database of animal gene trees

More...
TreeFami
TF313956

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1190.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001645 Folylpolyglutamate_synth
IPR018109 Folylpolyglutamate_synth_CS
IPR023600 Folylpolyglutamate_synth_euk
IPR036565 Mur-like_cat_sf
IPR036615 Mur_ligase_C_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11136 PTHR11136, 1 hit
PTHR11136:SF5 PTHR11136:SF5, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF038895 FPGS, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53244 SSF53244, 1 hit
SSF53623 SSF53623, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01499 folC, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01011 FOLYLPOLYGLU_SYNT_1, 1 hit
PS01012 FOLYLPOLYGLU_SYNT_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

This entry has 4 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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
        10         20         30         40         50
MSRARSHLRA ALFLAAASAR GITTQVAARR GLSAWPVPQE PSMEYQDAVR
60 70 80 90 100
MLNTLQTNAG YLEQVKRQRG DPQTQLEAME LYLARSGLQV EDLDRLNIIH
110 120 130 140 150
VTGTKGKGST CAFTECILRS YGLKTGFFSS PHLVQVRERI RINGQPISPE
160 170 180 190 200
LFTKYFWRLY HRLEETKDGS CVSMPPYFRF LTLMAFHVFL QEKVDLAVVE
210 220 230 240 250
VGIGGAYDCT NIIRKPVVCG VSSLGIDHTS LLGDTVEKIA WQKGGIFKQG
260 270 280 290 300
VPAFTVLQPE GPLAVLRDRA QQISCPLYLC PMLEALEEGG PPLTLGLEGE
310 320 330 340 350
HQRSNAALAL QLAHCWLQRQ DRHGAGEPKA SRPGLLWQLP LAPVFQPTSH
360 370 380 390 400
MRLGLRNTEW PGRTQVLRRG PLTWYLDGAH TASSAQACVR WFRQALQGRE
410 420 430 440 450
RPSGGPEVRV LLFNATGDRD PAALLKLLQP CQFDYAVFCP NLTEVSSTGN
460 470 480 490 500
ADQQNFTVTL DQVLLRCLEH QQHWNHLDEE QASPDLWSAP SPEPGGSASL
510 520 530 540 550
LLAPHPPHTC SASSLVFSCI SHALQWISQG RDPIFQPPSP PKGLLTHPVA
560 570 580
HSGASILREA AAIHVLVTGS LHLVGGVLKL LEPALSQ
Length:587
Mass (Da):64,609
Last modified:October 1, 1996 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5JU23Q5JU23_HUMAN
Folylpolyglutamate synthase, mitoch...
FPGS
375Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5JU21Q5JU21_HUMAN
Folylpolyglutamate synthase, mitoch...
FPGS
194Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5JU20Q5JU20_HUMAN
Folylpolyglutamate synthase, mitoch...
FPGS
264Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti101V → A in BAG51826 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06601613F → L1 PublicationCorresponds to variants dbSNP:rs1034635821 and dbSNP:rs759336102EnsemblEnsembl.1
Natural variantiVAR_05930522I → V3 PublicationsCorresponds to variant dbSNP:rs10760502Ensembl.1
Natural variantiVAR_043929437V → D. Corresponds to variant dbSNP:rs12686275Ensembl.1
Natural variantiVAR_066017466R → C Expression is reduced by 1.86-fold; Vmax with methotrexate as substrate is significantly reduced resulting in significantly decreased intrinsic clearance of methotrexate; 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 PublicationCorresponds to variant dbSNP:rs35789560Ensembl.1
Natural variantiVAR_043930489A → V2 PublicationsCorresponds to variant dbSNP:rs17855900Ensembl.1
Natural variantiVAR_066018499S → F Expression reduced by 2.11-fold; Vmax with methotrexate as substrate is significantly reduced resulting in significantly decreased intrinsic clearance of methotrexate; 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 PublicationCorresponds to variant dbSNP:rs200314440Ensembl.1
Natural variantiVAR_043931528S → T. Corresponds to variant dbSNP:rs34354111Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0187331 – 42Missing in isoform 2 and isoform 3. 1 PublicationAdd BLAST42
Alternative sequenceiVSP_04195943 – 50Missing in isoform 3. 1 Publication8
Alternative sequenceiVSP_041960168 – 193Missing in isoform 4. 1 PublicationAdd BLAST26

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AK056920 mRNA Translation: BAG51826.1
AK295309 mRNA Translation: BAH12029.1
AL162586 Genomic DNA No translation available.
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

The Consensus CDS (CCDS) project

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CCDSi
CCDS35148.1 [Q05932-1]
CCDS35149.1 [Q05932-3]
CCDS75905.1 [Q05932-4]

Protein sequence database of the Protein Information Resource

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PIRi
A46281

NCBI Reference Sequences

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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]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.335084

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000373225; ENSP00000362322; ENSG00000136877 [Q05932-3]
ENST00000373247; ENSP00000362344; ENSG00000136877 [Q05932-1]
ENST00000393706; ENSP00000377309; ENSG00000136877 [Q05932-4]

Database of genes from NCBI RefSeq genomes

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GeneIDi
2356

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2356

UCSC genome browser

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UCSCi
uc004bsg.3 human [Q05932-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056920 mRNA Translation: BAG51826.1
AK295309 mRNA Translation: BAH12029.1
AL162586 Genomic DNA No translation available.
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]
CCDS75905.1 [Q05932-4]
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

3D structure databases

ProteinModelPortaliQ05932
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108639, 9 interactors
IntActiQ05932, 1 interactor
STRINGi9606.ENSP00000362344

Chemistry databases

BindingDBiQ05932
ChEMBLiCHEMBL3171
DrugBankiDB00142 L-Glutamic Acid
DB00563 Methotrexate
DB06813 Pralatrexate
DB00293 Raltitrexed

PTM databases

iPTMnetiQ05932
PhosphoSitePlusiQ05932

Polymorphism and mutation databases

BioMutaiFPGS
DMDMi1706884

Proteomic databases

EPDiQ05932
MaxQBiQ05932
PaxDbiQ05932
PeptideAtlasiQ05932
PRIDEiQ05932
ProteomicsDBi58358
58359 [Q05932-2]
58360 [Q05932-3]
58361 [Q05932-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2356
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2356
DisGeNETi2356
EuPathDBiHostDB:ENSG00000136877.14

GeneCards: human genes, protein and diseases

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GeneCardsi
FPGS
HGNCiHGNC:3824 FPGS
HPAiHPA050488
MIMi136510 gene+phenotype
neXtProtiNX_Q05932
OpenTargetsiENSG00000136877
PharmGKBiPA167

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2525 Eukaryota
COG0285 LUCA
GeneTreeiENSGT00390000016526
HOGENOMiHOG000181278
HOVERGENiHBG003086
InParanoidiQ05932
KOiK01930
OMAiHTFMLGN
OrthoDBiEOG091G0DO0
PhylomeDBiQ05932
TreeFamiTF313956

Enzyme and pathway databases

UniPathwayi
UPA00850

BioCyciMetaCyc:HS06237-MONOMER
ReactomeiR-HSA-196757 Metabolism of folate and pterines

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
FPGS human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
FPGS

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
2356

Protein Ontology

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PROi
PR:Q05932

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000136877 Expressed in 181 organ(s), highest expression level in right adrenal gland
CleanExiHS_FPGS
ExpressionAtlasiQ05932 baseline and differential
GenevisibleiQ05932 HS

Family and domain databases

Gene3Di3.40.1190.10, 1 hit
InterProiView protein in InterPro
IPR001645 Folylpolyglutamate_synth
IPR018109 Folylpolyglutamate_synth_CS
IPR023600 Folylpolyglutamate_synth_euk
IPR036565 Mur-like_cat_sf
IPR036615 Mur_ligase_C_dom_sf
PANTHERiPTHR11136 PTHR11136, 1 hit
PTHR11136:SF5 PTHR11136:SF5, 1 hit
PIRSFiPIRSF038895 FPGS, 1 hit
SUPFAMiSSF53244 SSF53244, 1 hit
SSF53623 SSF53623, 1 hit
TIGRFAMsiTIGR01499 folC, 1 hit
PROSITEiView protein in PROSITE
PS01011 FOLYLPOLYGLU_SYNT_1, 1 hit
PS01012 FOLYLPOLYGLU_SYNT_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFOLC_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q05932
Secondary accession number(s): B3KPW4
, B7Z2Z3, F5H0K6, Q5JU19, Q5JU22, Q6P2P6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 1, 1996
Last modified: December 5, 2018
This is version 183 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. SIMILARITY comments
    Index of protein domains and families
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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