Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q05932

- FOLC_HUMAN

UniProt

Q05932 - FOLC_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Folylpolyglutamate synthase, mitochondrial

Gene

FPGS

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

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
Complete GO annotation...

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-KW
  4. mitochondrial matrix Source: Reactome
  5. mitochondrion Source: ProtInc
Complete GO annotation...

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

BgeeiQ05932.
CleanExiHS_FPGS.
ExpressionAtlasiQ05932. baseline.
GenevestigatoriQ05932.

Organism-specific databases

HPAiHPA050488.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi108639. 4 interactions.
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.
GeneTreeiENSGT00390000016526.
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) [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
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]
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.

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 ]
CCDS75905.1. [Q05932-4 ]
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. 4 interactions.
STRINGi 9606.ENSP00000362344.

Chemistry

BindingDBi Q05932.
ChEMBLi CHEMBL3171.
DrugBanki DB00563. Methotrexate.
DB06813. Pralatrexate.
DB00293. Raltitrexed.

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.
GeneTreei ENSGT00390000016526.
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

Bgeei Q05932.
CleanExi HS_FPGS.
ExpressionAtlasi Q05932. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 148 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