O75891 (AL1L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	902 AA.
Sequence status	Complete.
Protein existence	Evidence 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.5
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.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	NADP Phosphopantetheine
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	10-formyltetrahydrofolate catabolic process Traceable author statement PubMed 10204077. Source: ProtInc biosynthetic process Inferred from electronic annotation. Source: InterPro methylation Inferred from electronic annotation. Source: GOC one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	catalytic activity Traceable author statement PubMed 10204077. Source: ProtInc formyltetrahydrofolate dehydrogenase activity Inferred from electronic annotation. Source: EC hydroxymethyl-, formyl- and related transferase activity Inferred from electronic annotation. Source: InterPro methyltransferase activity Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75891-1)

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.

Isoform 2 (identifier: O75891-2)

The sequence of this isoform differs from the canonical sequence as follows:
     118-218: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 902

902

Cytosolic 10-formyltetrahydrofolate dehydrogenase

PRO_0000199419

Regions

Domain

323 – 392

70

Acyl carrier

Nucleotide binding

571 – 573

3

NADP By similarity

Nucleotide binding

597 – 600

4

NADP By similarity

Nucleotide binding

630 – 635

6

NADP By similarity

Nucleotide binding

650 – 651

2

NADP By similarity

Nucleotide binding

804 – 806

3

NADP By similarity

Region

1 – 203

203

GART

Region

88 – 90

3

Substrate binding

Region

417 – 902

486

Aldehyde dehydrogenase

Sites

Active site

106

1

Proton donor By similarity

Active site

673

1

Proton acceptor By similarity

Active site

707

1

Proton donor By similarity

Binding site

142

1

Substrate

Binding site

757

1

NADP By similarity

Site

142

1

Essential for catalytic activity By similarity

Amino acid modifications

Modified residue

354

1

O-(pantetheine 4'-phosphoryl)serine By similarity

Natural variations

Alternative sequence

118 – 218

101

Missing in isoform 2.

VSP_045569

Natural variant

254

1

L → P.
Corresponds to variant rs3796191 [ dbSNP | Ensembl ].

VAR_052290

Natural variant

330

1

V → F.
Corresponds to variant rs2886059 [ dbSNP | Ensembl ].

VAR_052291

Natural variant

429

1

E → A.
Corresponds to variant rs9282691 [ dbSNP | Ensembl ].

VAR_052292

Natural variant

436

1

A → T.
Corresponds to variant rs9282692 [ dbSNP | Ensembl ].

VAR_052293

Natural variant

436

1

A → V.
Corresponds to variant rs9282693 [ dbSNP | Ensembl ].

VAR_052294

Natural variant

448

1

S → N.
Corresponds to variant rs9282697 [ dbSNP | Ensembl ].

VAR_052295

Natural variant

481

1

S → G.
Corresponds to variant rs2276724 [ dbSNP | Ensembl ].

VAR_052296

Natural variant

511

1

A → V in a colorectal cancer sample; somatic mutation. Ref.8

VAR_036101

Natural variant

793

1

D → G.
Corresponds to variant rs1127717 [ dbSNP | Ensembl ].

VAR_052297

Natural variant

803

1

E → K.
Corresponds to variant rs9282689 [ dbSNP | Ensembl ].

VAR_052298

Natural variant

812

1

I → V.
Corresponds to variant rs4646750 [ dbSNP | Ensembl ].

VAR_052299

Experimental info

Sequence conflict

63

1

G → A in AAC35000. Ref.1

Sequence conflict

85

1

F → S in AAC35000. Ref.1

Sequence conflict

176

1

M → V in AAC35000. Ref.1

Sequence conflict

195

1

E → K in AAC35000. Ref.1

Sequence conflict

470

1

D → G in AAC35000. Ref.1

Sequence conflict

472

1

F → L in BAG57647. Ref.2

Sequence conflict

677

1

K → E in AAC35000. Ref.1

Sequence conflict

680

1

L → F in AAC35000. Ref.1

Sequence conflict

702

1

N → S in AAC35000. Ref.1

Secondary structure

1

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902

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

9 – 21

13

Beta strand

25 – 31

7

Helix

41 – 49

9

Beta strand

53 – 55

3

Helix

67 – 74

8

Beta strand

79 – 85

7

Helix

92 – 95

4

Beta strand

102 – 108

7

Turn

110 – 113

4

Beta strand

114 – 116

3

Helix

118 – 124

7

Beta strand

128 – 136

9

Beta strand

139 – 142

4

Beta strand

146 – 153

8

Helix

160 – 166

7

Turn

167 – 169

3

Helix

170 – 185

16

Helix

206 – 209

4

Helix

217 – 225

9

Turn

226 – 231

6

Beta strand

234 – 237

4

Beta strand

240 – 249

10

Beta strand

258 – 261

4

Beta strand

270 – 273

4

Beta strand

276 – 280

5

Beta strand

286 – 293

8

Beta strand

299 – 301

3

Helix

302 – 304

3

Helix

320 – 334

15

Helix

347 – 351

5

Helix

356 – 367

12

Helix

375 – 380

6

Helix

384 – 397

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 15, 2005. Version 2. Checksum: D92CB2930617F7CF	FASTA	902	98,829
	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
	Isoform 2 [UniParc]. Checksum: 2749168F3D76D548	FASTA	801	87,602
	10 20 30 40 50 60 MKIAVIGQSL FGQEVYCHLR KEGHEVVGVF TVPDKDGKAD PLGLEAEKDG VPVFKYSRWR 70 80 90 100 110 120 AKGQALPDVV AKYQALGAEL NVLPFCSQFI PMEIISAPRH GSIIYHPSLL PRHRGASAIH 130 140 150 160 170 180 NWIRGNDKVP GAWTEACEQK LTFFNSTLNT SGLVPEGDAL PIPGAHRPGV VTKAGLILFG 190 200 210 220 230 240 NDDKMLLVKN IQLEDGKMIL ASNFFKGAAS SVLELTEAEL VTAEAVRSVW QRILPKVLEV 250 260 270 280 290 300 EDSTDFFKSG AASVDVVRLV EEVKELCDGL ELENEDVYMA STFGDFIQLL VRKLRGDDEE 310 320 330 340 350 360 GECSIDYVEM AVNKRTVRMP HQLFIGGEFV DAEGAKTSET INPTDGSVIC QVSLAQVTDV 370 380 390 400 410 420 DKAVAAAKDA FENGRWGKIS ARDRGRLMYR LADLMEQHQE ELATIEALDA GAVYTLALKT 430 440 450 460 470 480 HVGMSIQTFR YFAGWCDKIQ GSTIPINQAR PNRNLTLTRK EPVGVCGIII PWNYPLMMLS 490 500 510 520 530 540 WKTAACLAAG NTVVIKPAQV TPLTALKFAE LTLKAGIPKG VVNVLPGSGS LVGQRLSDHP 550 560 570 580 590 600 DVRKIGFTGS TEVGKHIMKS CAISNVKKVS LELGGKSPLI IFADCDLNKA VQMGMSSVFF 610 620 630 640 650 660 NKGENCIAAG RLFVEDSIHD EFVRRVVEEV RKMKVGNPLD RDTDHGPQNH HAHLVKLMEY 670 680 690 700 710 720 CQHGVKEGAT LVCGGNQVPR PGFFFEPTVF TDVEDHMFIA KEESFGPVMI ISRFADGDLD 730 740 750 760 770 780 AVLSRANATE FGLASGVFTR DINKALYVSD KLQAGTVFVN TYNKTDVAAP FGGFKQSGFG 790 800 KDLGEAALNE YLRVKTVTFE Y

References

	« Hide 'large scale' referencesShow '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] (ISOFORM 1).
[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] (ISOFORM 2). Tissue: Amygdala.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Colon carcinoma.
[4]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[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]	"Structures of the hydrolase domain of human 10-formyltetrahydrofolate dehydrogenase and its complex with a substrate analogue." Kursula P., Schuler H., Flodin S., Nilsson-Ehle P., Ogg D.J., Savitsky P., Nordlund P., Stenmark P. Acta Crystallogr. D 62:1294-1299(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-307 IN COMPLEX WITH 6-FORMYLTETRAHYDROPTERIN, ACTIVE SITE.
[8]	"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. , 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] [Europe PMC] [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.
AK294392 mRNA. Translation: BAG57647.1.
CR749807 mRNA. Translation: CAH18667.1. Different initiation.
AC079848 Genomic DNA. No translation available.

IPI

IPI00290553.
IPI00966217.

RefSeq

NP_001257293.1. NM_001270364.1.
NP_001257294.1. NM_001270365.1.
NP_036322.2. NM_012190.3.

UniGene

Hs.434435.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BW0	X-ray	1.70	A	1-307	[»]
2CFI	X-ray	1.85	A	1-307	[»]
2CQ8	NMR	-	A	305-401	[»]

ProteinModelPortal

O75891.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000377083.

PTM databases

PhosphoSite

O75891.

Proteomic databases

PaxDb

O75891.

PRIDE

O75891.

Protocols and materials databases

DNASU

10840.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000273450; ENSP00000273450; ENSG00000144908.
ENST00000393434; ENSP00000377083; ENSG00000144908.
ENST00000452905; ENSP00000395881; ENSG00000144908.
ENST00000472186; ENSP00000420293; ENSG00000144908.

GeneID

10840.

KEGG

hsa:10840.

UCSC

uc003eim.1. human.

Organism-specific databases

CTD

10840.

GeneCards

GC03M125822.

HGNC

HGNC:3978. ALDH1L1.

HPA

HPA036900.

MIM

600249. gene.

neXtProt

NX_O75891.

PharmGKB

PA28393.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1012.

HOVERGEN

HBG051668.

InParanoid

O75891.

KO

K00289.

OrthoDB

EOG45TCMG.

PhylomeDB

O75891.

Gene expression databases

ArrayExpress

O75891.

Bgee

O75891.

CleanEx

HS_ALDH1L1.

Genevestigator

O75891.

GermOnline

ENSG00000144908. Homo sapiens.

Family and domain databases

Gene3D

1.10.1200.10. 1 hit.
3.10.25.10. 1 hit.
3.40.309.10. 1 hit.
3.40.50.170. 1 hit.
3.40.605.10. 1 hit.

InterPro

IPR011407. 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.
[Graphical view]

Pfam

PF00171. Aldedh. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]

PIRSF

PIRSF036489. 10-FTHFDH. 1 hit.

SUPFAM

SSF47336. ACP_like. 1 hit.
SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
SSF50486. FMT_C_like. 1 hit.
SSF53328. formyl_transf. 1 hit.

PROSITE

PS50075. 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]

ProtoNet

Search...

Other

DrugBank

DB00116. Tetrahydrofolic acid.

EvolutionaryTrace

O75891.

GenomeRNAi

10840.

NextBio

41156.

SOURCE

Search...

Entry information

Entry name

AL1L1_HUMAN

Accession

Primary (citable) accession number: O75891
Secondary accession number(s): B4DG36, E9PBX3, Q68CS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 15, 2005
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.