Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot O75891 (FTHFD_HUMAN)

Last modified September 23, 2008. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    10-formyltetrahydrofolate dehydrogenase
      Short name=10-FTHFDH
    EC=1.5.1.6
Alternative name(s):
    Aldehyde dehydrogenase family 1 member L1
Gene names
Name: ALDH1L1
Synonyms: FTHFD
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length902 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + NADP(+) + H(2)O = tetrahydrofolate + CO(2) + NADPH.

Subcellular location

Cytoplasm.

Sequence similarities

In the N-terminal section; belongs to the GART family.

In the C-terminal section; belongs to the aldehyde dehydrogenase family. ALDH1L subfamily.

Contains 1 acyl carrier domain.

Hide | Top

Ontologies

Keywords

   Biological processOne-carbon metabolism
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandNADP
Phosphopantetheine
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological process10-formyltetrahydrofolate catabolic process

Traceable author statement. Source: ProtInc

   Molecular functioncatalytic activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 90290210-formyltetrahydrofolate dehydrogenase

Regions

Domain323 – 39270Acyl carrier
Region1 – 203203GART
Region417 – 902486Aldehyde dehydrogenase

Sites

Active site1061Proton donor By similarity
Active site6731 By similarity
Active site7071 By similarity
Binding site3541Phosphopantetheine (covalent) By similarity
Site1421Essential for catalytic activity By similarity

Amino acid modifications

Modified residue3541Phosphoserine By similarity

Natural variations

Natural variant5111A → V in a colorectal cancer sample; somatic mutation.

Experimental info

Sequence conflict631G → A in AAC35000. Ref.1
Sequence conflict851F → S in AAC35000. Ref.1
Sequence conflict1761M → V in AAC35000. Ref.1
Sequence conflict1951E → K in AAC35000. Ref.1
Sequence conflict4701D → G in AAC35000. Ref.1
Sequence conflict6771K → E in AAC35000. Ref.1
Sequence conflict6801L → F in AAC35000. Ref.1
Sequence conflict7021N → S in AAC35000. Ref.1

Secondary structure

1 ................................................................ 902
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
O75891-1 [UniParc].

Last modified February 15, 2005. Version 2.
Checksum: D92CB2930617F7CF

FASTA90298,829
        10         20         30         40         50         60 
MKIAVIGQSL FGQEVYCHLR KEGHEVVGVF TVPDKDGKAD PLGLEAEKDG VPVFKYSRWR 

        70         80         90        100        110        120 
AKGQALPDVV AKYQALGAEL NVLPFCSQFI PMEIISAPRH GSIIYHPSLL PRHRGASAIN 

       130        140        150        160        170        180 
WTLIHGDKKG GFSIFWADDG LDTGDLLLQK ECEVLPDDTV STLYNRFLFP EGIKGMVQAV 

       190        200        210        220        230        240 
RLIAEGKAPR LPQPEEGATY EGIQKKETAK INWDQPAEAI HNWIRGNDKV PGAWTEACEQ 

       250        260        270        280        290        300 
KLTFFNSTLN TSGLVPEGDA LPIPGAHRPG VVTKAGLILF GNDDKMLLVK NIQLEDGKMI 

       310        320        330        340        350        360 
LASNFFKGAA SSVLELTEAE LVTAEAVRSV WQRILPKVLE VEDSTDFFKS GAASVDVVRL 

       370        380        390        400        410        420 
VEEVKELCDG LELENEDVYM ASTFGDFIQL LVRKLRGDDE EGECSIDYVE MAVNKRTVRM 

       430        440        450        460        470        480 
PHQLFIGGEF VDAEGAKTSE TINPTDGSVI CQVSLAQVTD VDKAVAAAKD AFENGRWGKI 

       490        500        510        520        530        540 
SARDRGRLMY RLADLMEQHQ EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI 

       550        560        570        580        590        600 
QGSTIPINQA RPNRNLTLTR KEPVGVCGII IPWNYPLMML SWKTAACLAA GNTVVIKPAQ 

       610        620        630        640        650        660 
VTPLTALKFA ELTLKAGIPK GVVNVLPGSG SLVGQRLSDH PDVRKIGFTG STEVGKHIMK 

       670        680        690        700        710        720 
SCAISNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF FNKGENCIAA GRLFVEDSIH 

       730        740        750        760        770        780 
DEFVRRVVEE VRKMKVGNPL DRDTDHGPQN HHAHLVKLME YCQHGVKEGA TLVCGGNQVP 

       790        800        810        820        830        840 
RPGFFFEPTV FTDVEDHMFI AKEESFGPVM IISRFADGDL DAVLSRANAT EFGLASGVFT 

       850        860        870        880        890        900 
RDINKALYVS DKLQAGTVFV NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRVKTVTF 


EY

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]Hong M.H., Lee Y., Kim J.W., Kang B.S., Choe I.S.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]The German cDNA consortium
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon carcinoma.
[3]"Crystal structure of human 10-formyltetrahydrofolate dehydrogenase."
Ogg D.J., Stenmark P., Arrowsmith C., Edwards A., Ehn M., Graslund S., Hammarstrom M., Hallberg M., Kotenyova T., Nilsson-Ehle P., Nordlund P., Persson C., Sagemark J., Schuler H., Sundstrom M., Thorsell A., Weigelt J.
Submitted (JUL-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-307.
[4]"Solution structure of RSGI RUH-033, a PP-binding domain of 10-FTHFDH from human cDNA."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 303-405.
[5]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-511.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

AF052732 mRNA. Translation: AAC35000.1.
CR749807 mRNA. Translation: CAH18667.1. Different initiation.
RefSeqNP_036322.2.
UniGeneHs.434435

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2BW0X-ray1.70A1-307[»]
2CFIX-ray1.85A1-307[»]
2CQ8NMR-A303-401[»]
SMRO75891. Positions 406-902.
ModBaseSearch...

PTM databases

PhosphoSiteO75891.

Genome annotation databases

EnsemblENSG00000144908. Homo sapiens. [Contig view]
GeneID10840.
KEGGhsa:10840.
NMPDRfig|9606.3.peg.23112.

Organism-specific databases

HGNCHGNC:3978. ALDH1L1.
MIM600249. gene.
PharmGKBPA28393.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENO75891.

Gene expression databases

ArrayExpressO75891.
CleanExHS_ALDH1L1.
GermOnlineENSG00000144908. Homo sapiens.

Family and domain databases

InterProIPR011407. 10_FTHF_DHase.
IPR016160. Ald_DHase_CS.
IPR016162. Ald_DHase_N.
IPR015590. Aldehyde_DHase.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR006163. Phsphopanteth_bd.
IPR006162. Ppantne_S.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
G3DSA:3.10.25.10. Formyl_trans_C. 1 hit.
G3DSA:3.40.50.170. Formyl_transf_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
PIRSFPIRSF036489. 10-FTHFDH. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
PS00373. GART. 1 hit.
PS00012. PHOSPHOPANTETHEINE. False negative.
[Graphical view]
ProDomO75891.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

DrugBankDB00116. Tetrahydrofolic acid.
LinkHubO75891.
SOURCESearch...
ProtoNetSearch...

Hide | Top

Entry information

Entry nameFTHFD_HUMAN
AccessionPrimary (citable) accession number: O75891
Secondary accession number(s): Q68CS1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 15, 2005
Last modified: September 23, 2008
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents