Skip Header

Contribute Send feedback
Read comments (?) or add your own

O75891 (AL1L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosolic 10-formyltetrahydrofolate dehydrogenase

Short name=10-FTHFDH
Short name=FDH
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 lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length902 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH.

Subcellular location

Cytoplasm.

Tissue specificity

Highly expressed in liver, pancreas and kidney. Ref.4

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.

Sequence caution

The sequence CAH18667.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 902902Cytosolic 10-formyltetrahydrofolate dehydrogenase
PRO_0000199419

Regions

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

Sites

Active site1061Proton donor By similarity
Active site6731 By similarity
Active site7071 By similarity
Site1421Essential for catalytic activity By similarity

Amino acid modifications

Modified residue3541O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residue6131Phosphothreonine Ref.3

Natural variations

Natural variant2541L → P.
Corresponds to variant rs3796191 [ dbSNP | Ensembl ].
VAR_052290
Natural variant3301V → F.
Corresponds to variant rs2886059 [ dbSNP | Ensembl ].
VAR_052291
Natural variant4291E → A.
Corresponds to variant rs9282691 [ dbSNP | Ensembl ].
VAR_052292
Natural variant4361A → T.
Corresponds to variant rs9282692 [ dbSNP | Ensembl ].
VAR_052293
Natural variant4361A → V.
Corresponds to variant rs9282693 [ dbSNP | Ensembl ].
VAR_052294
Natural variant4481S → N.
Corresponds to variant rs9282697 [ dbSNP | Ensembl ].
VAR_052295
Natural variant4811S → G.
Corresponds to variant rs2276724 [ dbSNP | Ensembl ].
VAR_052296
Natural variant5111A → V in a colorectal cancer sample; somatic mutation. Ref.7
VAR_036101
Natural variant7931D → G.
Corresponds to variant rs1127717 [ dbSNP | Ensembl ].
VAR_052297
Natural variant8031E → K.
Corresponds to variant rs9282689 [ dbSNP | Ensembl ].
VAR_052298
Natural variant8121I → V.
Corresponds to variant rs4646750 [ dbSNP | Ensembl ].
VAR_052299

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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
O75891 [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

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 full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon carcinoma.
[3]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-613, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[4]"ALDH1L2 is the mitochondrial homolog of 10-formyltetrahydrofolate dehydrogenase."
Krupenko N.I., Dubard M.E., Strickland K.C., Moxley K.M., Oleinik N.V., Krupenko S.A.
J. Biol. Chem. 285:23056-23063(2010) [PubMed: 20498374] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"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.
[6]"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.
[7]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF052732 mRNA. Translation: AAC35000.1.
CR749807 mRNA. Translation: CAH18667.1. Different initiation.
IPIIPI00290553.
RefSeqNP_036322.2. NM_012190.2.
UniGeneHs.434435.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BW0X-ray1.70A1-307[»]
2CFIX-ray1.85A1-307[»]
2CQ8NMR-A305-401[»]
ProteinModelPortalO75891.
SMRO75891. Positions 1-401, 406-902.
ModBaseSearch...

Protein-protein interaction databases

STRINGO75891.

PTM databases

PhosphoSiteO75891.

Proteomic databases

PRIDEO75891.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273450; ENSP00000273450; ENSG00000144908.
ENST00000393434; ENSP00000377083; ENSG00000144908.
ENST00000472186; ENSP00000420293; ENSG00000144908.
GeneID10840.
KEGGhsa:10840.
NMPDRfig|9606.3.peg.23112.
UCSCuc003eim.1. human.

Organism-specific databases

CTD10840.
GeneCardsGC03M125822.
H-InvDBHIX0003632.
HIX0017226.
HGNCHGNC:3978. ALDH1L1.
HPAHPA036900.
MIM600249. gene.
neXtProtNX_O75891.
PharmGKBPA28393.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12626.
HOVERGENHBG051668.
InParanoidO75891.
OrthoDBEOG45TCMG.
PhylomeDBO75891.

Gene expression databases

ArrayExpressO75891.
BgeeO75891.
CleanExHS_ALDH1L1.
GenevestigatorO75891.
GermOnlineENSG00000144908. Homo sapiens.

Family and domain databases

InterProIPR011407. 10_FTHF_DH.
IPR009081. Acyl_carrier_prot-like.
IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
IPR006163. Phsphopanteth-bd.
[Graphical view]
Gene3DG3DSA:1.10.1200.10. ACP_like. 1 hit.
G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA: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.
KOK00289.
PfamPF00171. Aldedh. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
PIRSFPIRSF036489. 10-FTHFDH. 1 hit.
SUPFAMSSF47336. ACP_like. 1 hit.
SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
SSF50486. FMT_C_like. 1 hit.
SSF53328. formyl_transf. 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]
ProtoNetSearch...

Other

DrugBankDB00116. Tetrahydrofolic acid.
NextBio41156.
SOURCESearch...

Entry information

Entry nameAL1L1_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: January 25, 2012
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

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

SIMILARITY comments

Index of protein domains and families