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P11586

- C1TC_HUMAN

UniProt

P11586 - C1TC_HUMAN

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Protein

C-1-tetrahydrofolate synthase, cytoplasmic

Gene
MTHFD1, MTHFC, MTHFD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.UniRule annotation
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.UniRule annotation
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei197 – 1971NADP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi172 – 1743NADPUniRule annotation
Nucleotide bindingi380 – 3878ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. formate-tetrahydrofolate ligase activity Source: RefGenome
  3. methenyltetrahydrofolate cyclohydrolase activity Source: RefGenome
  4. methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: RefGenome
  5. methylenetetrahydrofolate dehydrogenase [NAD(P)+] activity Source: Reactome

GO - Biological processi

  1. folic acid-containing compound biosynthetic process Source: InterPro
  2. folic acid metabolic process Source: Reactome
  3. histidine biosynthetic process Source: UniProtKB-KW
  4. methionine biosynthetic process Source: UniProtKB-KW
  5. one-carbon metabolic process Source: RefGenome
  6. purine nucleotide biosynthetic process Source: UniProtKB-KW
  7. small molecule metabolic process Source: Reactome
  8. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
  9. vitamin metabolic process Source: Reactome
  10. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis, Methionine biosynthesis, One-carbon metabolism, Purine biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS02138-MONOMER.
BRENDAi6.3.4.3. 2681.
ReactomeiREACT_11167. Metabolism of folate and pterines.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
C-1-tetrahydrofolate synthase, cytoplasmic
Short name:
C1-THF synthase
Cleaved into the following chain:
Including the following 3 domains:
Methylenetetrahydrofolate dehydrogenase (EC:1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase (EC:3.5.4.9)
Formyltetrahydrofolate synthetase (EC:6.3.4.3)
Gene namesi
Name:MTHFD1
Synonyms:MTHFC, MTHFD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:7432. MTHFD1.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytosol Source: RefGenome
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Folate-sensitive neural tube defects (FS-NTD) [MIM:601634]: The most common NTDs are open spina bifida (myelomeningocele) and anencephaly.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti293 – 2931R → H Associated with susceptibility to FS-NTD. 1 Publication
Corresponds to variant rs34181110 [ dbSNP | Ensembl ].
VAR_010241
Natural varianti653 – 6531R → Q May be associated with susceptibility to FS-NTD; decreases enzyme stability and increases risk for congenital heart defects. 7 Publications
Corresponds to variant rs2236225 [ dbSNP | Ensembl ].
VAR_010251
Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491S → A: No effect on dehydrogenase and cyclohydrolase activity. Strong increase of Km for NADP. 1 Publication
Mutagenesisi49 – 491S → Q: Reduces dehydrogenase by 75% and cyclohydrolase activity by 99%. No effect on Km for NADP and for 5,10-methenyltetrahydrofolate. 1 Publication
Mutagenesisi52 – 521Y → A or S: Reduces dehydrogenase activity by 99%. Reduces cyclohydrolase activity by 70%. No effect on Km for NADP and for 5,10-methenyltetrahydrofolate. 1 Publication
Mutagenesisi52 – 521Y → F: Slightly reduces dehydrogenase and cyclohydrolase activity. Increase of Km for NADP and for 5,10-methenyltetrahydrofolate. 1 Publication
Mutagenesisi56 – 561K → A, I, S or T: Decreases dehydrogenase activity over 90%. Loss of cyclohydrolase activity. 1 Publication
Mutagenesisi56 – 561K → E, M or Q: Moderate decrease of dehydrogenase activity. Loss of cyclohydrolase activity. Strong increase of Km for NADP. Decrease of Km for 5,10-methenyltetrahydrofolate. 1 Publication
Mutagenesisi56 – 561K → R: Reduces dehydrogenase and cyclohydrolase activity by 99%. No effect on Km for NADP and for 5,10-methenyltetrahydrofolate. 1 Publication
Mutagenesisi147 – 1471C → Q: Reduces dehydrogenase activity by 50% and cyclohydrolase activity by 87%. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi114500. phenotype.
172460. gene+phenotype.
601634. phenotype.
Orphaneti268392. Cervical spina bifida aperta.
268762. Cervical spina bifida cystica.
268397. Cervicothoracic spina bifida aperta.
268766. Cervicothoracic spina bifida cystica.
268388. Lumbosacral spina bifida aperta.
268758. Lumbosacral spina bifida cystica.
268384. Thoracolumbosacral spina bifida aperta.
268752. Thoracolumbosacral spina bifida cystica.
268377. Total spina bifida aperta.
268748. Total spina bifida cystica.
268740. Upper thoracic spina bifida aperta.
268770. Upper thoracic spina bifida cystica.
PharmGKBiPA31236.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 935935C-1-tetrahydrofolate synthase, cytoplasmicUniRule annotationPRO_0000423280Add
BLAST
Initiator methioninei1 – 11Removed; alternate3 Publications
Chaini2 – 935934C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processedUniRule annotationPRO_0000199321Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP11586.
PaxDbiP11586.
PRIDEiP11586.

2D gel databases

REPRODUCTION-2DPAGEIPI00218342.
SWISS-2DPAGEP11586.

PTM databases

PhosphoSiteiP11586.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiP11586.
BgeeiP11586.
CleanExiHS_MTHFD1.
GenevestigatoriP11586.

Organism-specific databases

HPAiHPA000704.
HPA001290.
HPA015006.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MCCP235081EBI-709638,EBI-307531
TRAF6Q9Y4K31EBI-709638,EBI-359276
WDR8Q9P2S51EBI-709638,EBI-1054904

Protein-protein interaction databases

BioGridi110622. 50 interactions.
IntActiP11586. 7 interactions.
MINTiMINT-5000922.
STRINGi9606.ENSP00000216605.

Structurei

Secondary structure

1
935
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 3022
Beta strandi37 – 448
Helixi47 – 6317
Beta strandi66 – 727
Helixi78 – 9013
Beta strandi96 – 994
Helixi111 – 1166
Helixi120 – 1223
Helixi129 – 1368
Helixi147 – 15711
Turni158 – 1603
Beta strandi167 – 1715
Turni175 – 1773
Helixi178 – 18710
Beta strandi191 – 1955
Helixi202 – 2065
Beta strandi210 – 2145
Helixi224 – 2263
Beta strandi232 – 2354
Helixi258 – 2614
Turni262 – 2643
Beta strandi266 – 2683
Beta strandi271 – 2744
Helixi275 – 29521

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4IX-ray1.50A/B1-301[»]
1DIAX-ray2.20A/B1-306[»]
1DIBX-ray2.70A/B1-306[»]
1DIGX-ray2.20A/B1-306[»]
ProteinModelPortaliP11586.
SMRiP11586. Positions 2-296, 317-935.

Miscellaneous databases

EvolutionaryTraceiP11586.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 305304Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseUniRule annotationAdd
BLAST
Regioni52 – 565Substrate bindingUniRule annotation
Regioni99 – 1013Substrate bindingUniRule annotation
Regioni272 – 2765Substrate bindingUniRule annotation
Regioni306 – 935630Formyltetrahydrofolate synthetaseUniRule annotationAdd
BLAST

Domaini

This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity.UniRule annotation

Sequence similaritiesi

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.

Phylogenomic databases

eggNOGiCOG0190.
HOVERGENiHBG004916.
InParanoidiP11586.
KOiK00288.
PhylomeDBiP11586.
TreeFamiTF300623.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPiMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProiIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P11586-1 [UniParc]FASTAAdd to Basket

« Hide

MAPAEILNGK EISAQIRARL KNQVTQLKEQ VPGFTPRLAI LQVGNRDDSN    50
LYINVKLKAA EEIGIKATHI KLPRTTTESE VMKYITSLNE DSTVHGFLVQ 100
LPLDSENSIN TEEVINAIAP EKDVDGLTSI NAGRLARGDL NDCFIPCTPK 150
GCLELIKETG VPIAGRHAVV VGRSKIVGAP MHDLLLWNNA TVTTCHSKTA 200
HLDEEVNKGD ILVVATGQPE MVKGEWIKPG AIVIDCGINY VPDDKKPNGR 250
KVVGDVAYDE AKERASFITP VPGGVGPMTV AMLMQSTVES AKRFLEKFKP 300
GKWMIQYNNL NLKTPVPSDI DISRSCKPKP IGKLAREIGL LSEEVELYGE 350
TKAKVLLSAL ERLKHRPDGK YVVVTGITPT PLGEGKSTTT IGLVQALGAH 400
LYQNVFACVR QPSQGPTFGI KGGAAGGGYS QVIPMEEFNL HLTGDIHAIT 450
AANNLVAAAI DARIFHELTQ TDKALFNRLV PSVNGVRRFS DIQIRRLKRL 500
GIEKTDPTTL TDEEINRFAR LDIDPETITW QRVLDTNDRF LRKITIGQAP 550
TEKGHTRTAQ FDISVASEIM AVLALTTSLE DMRERLGKMV VASSKKGEPV 600
SAEDLGVSGA LTVLMKDAIK PNLMQTLEGT PVFVHAGPFA NIAHGNSSII 650
ADRIALKLVG PEGFVVTEAG FGADIGMEKF FNIKCRYSGL CPHVVVLVAT 700
VRALKMHGGG PTVTAGLPLP KAYIQENLEL VEKGFSNLKK QIENARMFGI 750
PVVVAVNAFK TDTESELDLI SRLSREHGAF DAVKCTHWAE GGKGALALAQ 800
AVQRAAQAPS SFQLLYDLKL PVEDKIRIIA QKIYGADDIE LLPEAQHKAE 850
VYTKQGFGNL PICMAKTHLS LSHNPEQKGV PTGFILPIRD IRASVGAGFL 900
YPLVGTMSTM PGLPTRPCFY DIDLDPETEQ VNGLF 935
Length:935
Mass (Da):101,559
Last modified:January 23, 2007 - v3
Checksum:i29AE1C04B4922885
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti134 – 1341R → K Associated with increased risk of colorectal cancer. 3 Publications
Corresponds to variant rs1950902 [ dbSNP | Ensembl ].
VAR_016232
Natural varianti162 – 1621P → L.
Corresponds to variant rs4902283 [ dbSNP | Ensembl ].
VAR_055458
Natural varianti293 – 2931R → H Associated with susceptibility to FS-NTD. 1 Publication
Corresponds to variant rs34181110 [ dbSNP | Ensembl ].
VAR_010241
Natural varianti653 – 6531R → Q May be associated with susceptibility to FS-NTD; decreases enzyme stability and increases risk for congenital heart defects. 7 Publications
Corresponds to variant rs2236225 [ dbSNP | Ensembl ].
VAR_010251
Natural varianti761 – 7611T → M.
Corresponds to variant rs10813 [ dbSNP | Ensembl ].
VAR_032789
Natural varianti769 – 7691L → F.1 Publication
Corresponds to variant rs17857382 [ dbSNP | Ensembl ].
VAR_032790

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04031 mRNA. Translation: AAA59574.1.
AK312361 mRNA. Translation: BAG35279.1.
AL122035 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80857.1.
BC001014 mRNA. Translation: AAH01014.2.
BC009806 mRNA. Translation: AAH09806.1.
BC050420 mRNA. Translation: AAH50420.1.
CCDSiCCDS9763.1.
PIRiA31903.
RefSeqiNP_005947.3. NM_005956.3.
UniGeneiHs.652308.

Genome annotation databases

EnsembliENST00000216605; ENSP00000216605; ENSG00000100714.
ENST00000555709; ENSP00000450560; ENSG00000100714.
GeneIDi4522.
KEGGihsa:4522.

Polymorphism databases

DMDMi115206.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04031 mRNA. Translation: AAA59574.1 .
AK312361 mRNA. Translation: BAG35279.1 .
AL122035 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80857.1 .
BC001014 mRNA. Translation: AAH01014.2 .
BC009806 mRNA. Translation: AAH09806.1 .
BC050420 mRNA. Translation: AAH50420.1 .
CCDSi CCDS9763.1.
PIRi A31903.
RefSeqi NP_005947.3. NM_005956.3.
UniGenei Hs.652308.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A4I X-ray 1.50 A/B 1-301 [» ]
1DIA X-ray 2.20 A/B 1-306 [» ]
1DIB X-ray 2.70 A/B 1-306 [» ]
1DIG X-ray 2.20 A/B 1-306 [» ]
ProteinModelPortali P11586.
SMRi P11586. Positions 2-296, 317-935.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110622. 50 interactions.
IntActi P11586. 7 interactions.
MINTi MINT-5000922.
STRINGi 9606.ENSP00000216605.

Chemistry

BindingDBi P11586.
ChEMBLi CHEMBL2541.
DrugBanki DB00157. NADH.
DB00116. Tetrahydrofolic acid.

PTM databases

PhosphoSitei P11586.

Polymorphism databases

DMDMi 115206.

2D gel databases

REPRODUCTION-2DPAGE IPI00218342.
SWISS-2DPAGE P11586.

Proteomic databases

MaxQBi P11586.
PaxDbi P11586.
PRIDEi P11586.

Protocols and materials databases

DNASUi 4522.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216605 ; ENSP00000216605 ; ENSG00000100714 .
ENST00000555709 ; ENSP00000450560 ; ENSG00000100714 .
GeneIDi 4522.
KEGGi hsa:4522.

Organism-specific databases

CTDi 4522.
GeneCardsi GC14P064854.
H-InvDB HIX0011731.
HGNCi HGNC:7432. MTHFD1.
HPAi HPA000704.
HPA001290.
HPA015006.
MIMi 114500. phenotype.
172460. gene+phenotype.
601634. phenotype.
neXtProti NX_P11586.
Orphaneti 268392. Cervical spina bifida aperta.
268762. Cervical spina bifida cystica.
268397. Cervicothoracic spina bifida aperta.
268766. Cervicothoracic spina bifida cystica.
268388. Lumbosacral spina bifida aperta.
268758. Lumbosacral spina bifida cystica.
268384. Thoracolumbosacral spina bifida aperta.
268752. Thoracolumbosacral spina bifida cystica.
268377. Total spina bifida aperta.
268748. Total spina bifida cystica.
268740. Upper thoracic spina bifida aperta.
268770. Upper thoracic spina bifida cystica.
PharmGKBi PA31236.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0190.
HOVERGENi HBG004916.
InParanoidi P11586.
KOi K00288.
PhylomeDBi P11586.
TreeFami TF300623.

Enzyme and pathway databases

UniPathwayi UPA00193 .
BioCyci MetaCyc:HS02138-MONOMER.
BRENDAi 6.3.4.3. 2681.
Reactomei REACT_11167. Metabolism of folate and pterines.

Miscellaneous databases

ChiTaRSi MTHFD1. human.
EvolutionaryTracei P11586.
GeneWikii MTHFD1.
GenomeRNAii 4522.
NextBioi 17468.
PROi P11586.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11586.
Bgeei P11586.
CleanExi HS_MTHFD1.
Genevestigatori P11586.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPi MF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProi IPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view ]
Pfami PF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view ]
PRINTSi PR00085. THFDHDRGNASE.
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase."
    Hum D.W., Bell A.W., Rozen R., Mackenzie R.E.
    J. Biol. Chem. 263:15946-15950(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-31.
    Tissue: Liver.
  2. "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], VARIANT GLN-653.
    Tissue: Amygdala.
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-653.
  5. "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], VARIANTS GLN-653 AND PHE-769.
    Tissue: Brain, Eye and Lymph.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-17.
    Tissue: Platelet.
  7. Bienvenut W.V., Gao M., Leug H., Campbell A., Ozanne B.W.
    Submitted (JUL-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17; 251-264; 314-324; 355-362; 596-616 AND 722-733, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Foreskin fibroblast and Prostatic carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5-A resolution."
    Allaire M., Li Y., Mackenzie R.E., Cygler M.
    Structure 6:173-182(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-302.
  13. "Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase."
    Schmidt A., Wu H., MacKenzie R.E., Chen V.J., Bewly J.R., Ray J.E., Toth J.E., Cygler M.
    Biochemistry 39:6325-6335(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-306 IN COMPLEX WITH NADP AND SUBSTRATE ANALOGS, SUBUNIT, MUTAGENESIS OF SER-49; TYR-52; LYS-56 AND CYS-147.
  14. "Molecular genetic analysis of the gene encoding the trifunctional enzyme MTHFD (methylenetetrahydrofolate-dehydrogenase, methenyltetrahydrofolate-cyclohydrolase, formyltetrahydrofolate synthetase) in patients with neural tube defects."
    Hol F.A., van der Put N.M.J., Geurds M.P.A., Heil S.G., Trijbels F.J.M., Hamel B.C.J., Mariman E.C.M., Blom H.J.
    Clin. Genet. 53:119-125(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF VARIANT HIS-293 WITH SUSCEPTIBILITY TO FS-NTD, VARIANT GLN-653.
  15. "A polymorphism, R653Q, in the trifunctional enzyme methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase is a maternal genetic risk factor for neural tube defects: report of the Birth Defects Research Group."
    Brody L.C., Conley M., Cox C., Kirke P.N., McKeever M.P., Mills J.L., Molloy A.M., O'Leary V.B., Parle-McDermott A., Scott J.M., Swanson D.A.
    Am. J. Hum. Genet. 71:1207-1215(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF VARIANT GLN-653 WITH SUSCEPTIBILITY TO FS-NTD, VARIANT LYS-134.
  16. "Confirmation of the R653Q polymorphism of the trifunctional C1-synthase enzyme as a maternal risk for neural tube defects in the Irish population."
    Parle-McDermott A., Kirke P.N., Mills J.L., Molloy A.M., Cox C., O'Leary V.B., Pangilinan F., Conley M., Cleary L., Brody L.C., Scott J.M.
    Eur. J. Hum. Genet. 14:768-772(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF VARIANT GLN-653 WITH SUSCEPTIBILITY TO FS-NTD, VARIANT LYS-134.
  17. "Search for low penetrance alleles for colorectal cancer through a scan of 1467 non-synonymous SNPs in 2575 cases and 2707 controls with validation by kin-cohort analysis of 14 704 first-degree relatives."
    Webb E.L., Rudd M.F., Sellick G.S., El Galta R., Bethke L., Wood W., Fletcher O., Penegar S., Withey L., Qureshi M., Johnson N., Tomlinson I., Gray R., Peto J., Houlston R.S.
    Hum. Mol. Genet. 15:3263-3271(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LYS-134, ASSOCIATION WITH COLORECTAL CANCER SUSCEPTIBILITY.
  18. "The MTHFD1 p.Arg653Gln variant alters enzyme function and increases risk for congenital heart defects."
    Christensen K.E., Rohlicek C.V., Andelfinger G.U., Michaud J., Bigras J.-L., Richter A., Mackenzie R.E., Rozen R.
    Hum. Mutat. 30:212-220(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT GLN-653, ASSOCIATION WITH RISK OF CONGENITAL HEART DEFECTS.

Entry informationi

Entry nameiC1TC_HUMAN
AccessioniPrimary (citable) accession number: P11586
Secondary accession number(s): B2R5Y2
, G3V2B8, Q86VC9, Q9BVP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 168 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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