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Protein

Fumarylacetoacetase

Gene

FAH

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

Functioni

Catalytic activityi

4-fumarylacetoacetate + H2O = acetoacetate + fumarate.By similarity

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarity
  • Mg2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi126 – 1261CalciumBy similarity
Binding sitei128 – 1281SubstrateBy similarity
Active sitei133 – 1331Proton acceptorCurated
Binding sitei142 – 1421SubstrateBy similarity
Metal bindingi199 – 1991CalciumBy similarity
Metal bindingi201 – 2011CalciumBy similarity
Metal bindingi233 – 2331CalciumBy similarity
Metal bindingi233 – 2331MagnesiumBy similarity
Binding sitei240 – 2401SubstrateBy similarity
Binding sitei244 – 2441SubstrateBy similarity
Metal bindingi253 – 2531MagnesiumBy similarity
Metal bindingi257 – 2571MagnesiumBy similarity
Binding sitei350 – 3501SubstrateBy similarity

GO - Molecular functioni

  1. fumarylacetoacetase activity Source: Reactome
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine catabolic process Source: Ensembl
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. L-phenylalanine catabolic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
  5. tyrosine catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Phenylalanine catabolism, Tyrosine catabolism

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS02536-MONOMER.
ReactomeiREACT_1786. Phenylalanine and tyrosine catabolism.
UniPathwayiUPA00139; UER00341.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarylacetoacetase (EC:3.7.1.2By similarity)
Short name:
FAA
Alternative name(s):
Beta-diketonase
Fumarylacetoacetate hydrolase
Gene namesi
Name:FAH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:3579. FAH.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Tyrosinemia 113 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, and hepatorenal manifestations. Typical features include hepatic necrosis, renal tubular injury, episodic weakness, self-mutilation, and seizures. Renal tubular dysfunction is associated with phosphate loss and hypophosphataemic rickets. Progressive liver disease can lead to the development of hepatocellular carcinoma. Dietary treatment with restriction of tyrosine and phenylalanine alleviates the rickets, but liver transplantation has so far been the only definite treatment.

See also OMIM:276700
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161N → I in TYRSN1; loss of activity. 2 Publications
VAR_005205
Natural varianti35 – 351A → T in TYRSN1; atypical mild phenotype. 1 Publication
VAR_065454
Natural varianti62 – 621F → C in TYRSN1; loss of activity. 1 Publication
VAR_005206
Natural varianti64 – 641Q → H in TYRSN1.
VAR_005207
Natural varianti134 – 1341A → D in TYRSN1; loss of activity. 3 Publications
VAR_005208
Natural varianti158 – 1581G → D in TYRSN1. 1 Publication
VAR_005209
Natural varianti166 – 1661V → G in TYRSN1. 1 Publication
VAR_005210
Natural varianti193 – 1931C → R in TYRSN1; loss of activity. 2 Publications
VAR_005211
Natural varianti207 – 2071G → D in TYRSN1.
VAR_005212
Natural varianti233 – 2331D → V in TYRSN1; loss of activity. 2 Publications
VAR_005213
Natural varianti234 – 2341W → G in TYRSN1; loss of activity. 2 Publications
VAR_005214
Natural varianti249 – 2491P → T in TYRSN1.
VAR_005215
Natural varianti261 – 2611P → L in TYRSN1. 1 Publication
VAR_005216
Natural varianti279 – 2791Q → R in TYRSN1; may affect splicing resulting in skipping of exon 8 alone or together with exon 9; lower activity as compared to wild type. 3 Publications
VAR_065455
Natural varianti294 – 2941T → P in TYRSN1.
VAR_005217
Natural varianti337 – 3371G → S in TYRSN1. 1 Publication
VAR_005218
Natural varianti341 – 3411R → W in TYRSN1; pseudo-deficient phenotype; lower activity. 2 Publications
Corresponds to variant rs11555096 [ dbSNP | Ensembl ].
VAR_005219
Natural varianti342 – 3421P → L in TYRSN1; loss of activity. 1 Publication
VAR_005220
Natural varianti366 – 3661Missing in TYRSN1. 1 Publication
VAR_005221
Natural varianti369 – 3691G → V in TYRSN1. 1 Publication
VAR_005222
Natural varianti381 – 3811R → G in TYRSN1; loss of activity. 1 Publication
VAR_005223
Natural varianti405 – 4051F → H in TYRSN1; requires 2 nucleotide substitutions. 1 Publication
VAR_005224

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi276700. phenotype.
Orphaneti882. Tyrosinemia type 1.
PharmGKBiPA27977.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 419418FumarylacetoacetasePRO_0000156825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP16930.
PaxDbiP16930.
PeptideAtlasiP16930.
PRIDEiP16930.

2D gel databases

OGPiP16930.
REPRODUCTION-2DPAGEIPI00031708.

PTM databases

PhosphoSiteiP16930.

Expressioni

Tissue specificityi

Mainly expressed in liver and kidney. Lower levels are also detected in many other tissues.

Gene expression databases

BgeeiP16930.
CleanExiHS_FAH.
ExpressionAtlasiP16930. baseline and differential.
GenevestigatoriP16930.

Organism-specific databases

HPAiHPA041370.
HPA044093.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi108479. 7 interactions.
IntActiP16930. 1 interaction.
STRINGi9606.ENSP00000261755.

Structurei

3D structure databases

ProteinModelPortaliP16930.
SMRiP16930. Positions 1-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FAH family.Curated

Phylogenomic databases

eggNOGiCOG0179.
GeneTreeiENSGT00390000008646.
HOGENOMiHOG000256845.
HOVERGENiHBG001919.
InParanoidiP16930.
KOiK01555.
OMAiLSWKGTK.
PhylomeDBiP16930.
TreeFamiTF315211.

Family and domain databases

Gene3Di2.30.30.230. 1 hit.
3.90.850.10. 1 hit.
InterProiIPR005959. Fumarylacetoacetase.
IPR002529. Fumarylacetoacetase_C.
IPR011234. Fumarylacetoacetase_C-rel.
IPR015377. Fumarylacetoacetase_N.
[Graphical view]
PANTHERiPTHR11820:SF1. PTHR11820:SF1. 1 hit.
PfamiPF01557. FAA_hydrolase. 1 hit.
PF09298. FAA_hydrolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56529. SSF56529. 1 hit.
SSF63433. SSF63433. 1 hit.
TIGRFAMsiTIGR01266. fum_ac_acetase. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P16930-1) [UniParc]FASTAAdd to Basket

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
MSFIPVAEDS DFPIHNLPYG VFSTRGDPRP RIGVAIGDQI LDLSIIKHLF
60 70 80 90 100
TGPVLSKHQD VFNQPTLNSF MGLGQAAWKE ARVFLQNLLS VSQARLRDDT
110 120 130 140 150
ELRKCAFISQ ASATMHLPAT IGDYTDFYSS RQHATNVGIM FRDKENALMP
160 170 180 190 200
NWLHLPVGYH GRASSVVVSG TPIRRPMGQM KPDDSKPPVY GACKLLDMEL
210 220 230 240 250
EMAFFVGPGN RLGEPIPISK AHEHIFGMVL MNDWSARDIQ KWEYVPLGPF
260 270 280 290 300
LGKSFGTTVS PWVVPMDALM PFAVPNPKQD PRPLPYLCHD EPYTFDINLS
310 320 330 340 350
VNLKGEGMSQ AATICKSNFK YMYWTMLQQL THHSVNGCNL RPGDLLASGT
360 370 380 390 400
ISGPEPENFG SMLELSWKGT KPIDLGNGQT RKFLLDGDEV IITGYCQGDG
410
YRIGFGQCAG KVLPALLPS
Length:419
Mass (Da):46,374
Last modified:August 1, 1992 - v2
Checksum:i12EA8D8074C55BB2
GO
Isoform 2 (identifier: P16930-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.

Note: No experimental confirmation available.

Show »
Length:349
Mass (Da):38,614
Checksum:i76484AD16731BE21
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161N → I in TYRSN1; loss of activity. 2 Publications
VAR_005205
Natural varianti35 – 351A → T in TYRSN1; atypical mild phenotype. 1 Publication
VAR_065454
Natural varianti62 – 621F → C in TYRSN1; loss of activity. 1 Publication
VAR_005206
Natural varianti64 – 641Q → H in TYRSN1.
VAR_005207
Natural varianti134 – 1341A → D in TYRSN1; loss of activity. 3 Publications
VAR_005208
Natural varianti158 – 1581G → D in TYRSN1. 1 Publication
VAR_005209
Natural varianti166 – 1661V → G in TYRSN1. 1 Publication
VAR_005210
Natural varianti193 – 1931C → R in TYRSN1; loss of activity. 2 Publications
VAR_005211
Natural varianti207 – 2071G → D in TYRSN1.
VAR_005212
Natural varianti233 – 2331D → V in TYRSN1; loss of activity. 2 Publications
VAR_005213
Natural varianti234 – 2341W → G in TYRSN1; loss of activity. 2 Publications
VAR_005214
Natural varianti249 – 2491P → T in TYRSN1.
VAR_005215
Natural varianti261 – 2611P → L in TYRSN1. 1 Publication
VAR_005216
Natural varianti279 – 2791Q → R in TYRSN1; may affect splicing resulting in skipping of exon 8 alone or together with exon 9; lower activity as compared to wild type. 3 Publications
VAR_065455
Natural varianti294 – 2941T → P in TYRSN1.
VAR_005217
Natural varianti337 – 3371G → S in TYRSN1. 1 Publication
VAR_005218
Natural varianti341 – 3411R → W in TYRSN1; pseudo-deficient phenotype; lower activity. 2 Publications
Corresponds to variant rs11555096 [ dbSNP | Ensembl ].
VAR_005219
Natural varianti342 – 3421P → L in TYRSN1; loss of activity. 1 Publication
VAR_005220
Natural varianti366 – 3661Missing in TYRSN1. 1 Publication
VAR_005221
Natural varianti369 – 3691G → V in TYRSN1. 1 Publication
VAR_005222
Natural varianti381 – 3811R → G in TYRSN1; loss of activity. 1 Publication
VAR_005223
Natural varianti405 – 4051F → H in TYRSN1; requires 2 nucleotide substitutions. 1 Publication
VAR_005224

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7070Missing in isoform 2. 1 PublicationVSP_055491Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55150 mRNA. Translation: AAA52422.1.
BT007160 mRNA. Translation: AAP35824.1.
AK313951 mRNA. Translation: BAG36668.1.
BX537608 mRNA. Translation: CAD97795.1.
AC087761 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99120.1.
CH471136 Genomic DNA. Translation: EAW99121.1.
BC002527 mRNA. Translation: AAH02527.1.
X51728 mRNA. Translation: CAA36016.1.
CCDSiCCDS10314.1. [P16930-1]
PIRiA37926.
RefSeqiNP_000128.1. NM_000137.2. [P16930-1]
UniGeneiHs.73875.

Genome annotation databases

EnsembliENST00000261755; ENSP00000261755; ENSG00000103876. [P16930-1]
ENST00000407106; ENSP00000385080; ENSG00000103876. [P16930-1]
ENST00000539156; ENSP00000454271; ENSG00000103876. [P16930-2]
ENST00000561421; ENSP00000453347; ENSG00000103876. [P16930-1]
GeneIDi2184.
KEGGihsa:2184.
UCSCiuc002bfm.2. human. [P16930-1]

Polymorphism databases

DMDMi119778.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55150 mRNA. Translation: AAA52422.1.
BT007160 mRNA. Translation: AAP35824.1.
AK313951 mRNA. Translation: BAG36668.1.
BX537608 mRNA. Translation: CAD97795.1.
AC087761 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99120.1.
CH471136 Genomic DNA. Translation: EAW99121.1.
BC002527 mRNA. Translation: AAH02527.1.
X51728 mRNA. Translation: CAA36016.1.
CCDSiCCDS10314.1. [P16930-1]
PIRiA37926.
RefSeqiNP_000128.1. NM_000137.2. [P16930-1]
UniGeneiHs.73875.

3D structure databases

ProteinModelPortaliP16930.
SMRiP16930. Positions 1-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108479. 7 interactions.
IntActiP16930. 1 interaction.
STRINGi9606.ENSP00000261755.

PTM databases

PhosphoSiteiP16930.

Polymorphism databases

DMDMi119778.

2D gel databases

OGPiP16930.
REPRODUCTION-2DPAGEIPI00031708.

Proteomic databases

MaxQBiP16930.
PaxDbiP16930.
PeptideAtlasiP16930.
PRIDEiP16930.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261755; ENSP00000261755; ENSG00000103876. [P16930-1]
ENST00000407106; ENSP00000385080; ENSG00000103876. [P16930-1]
ENST00000539156; ENSP00000454271; ENSG00000103876. [P16930-2]
ENST00000561421; ENSP00000453347; ENSG00000103876. [P16930-1]
GeneIDi2184.
KEGGihsa:2184.
UCSCiuc002bfm.2. human. [P16930-1]

Organism-specific databases

CTDi2184.
GeneCardsiGC15P080445.
HGNCiHGNC:3579. FAH.
HPAiHPA041370.
HPA044093.
MIMi276700. phenotype.
613871. gene.
neXtProtiNX_P16930.
Orphaneti882. Tyrosinemia type 1.
PharmGKBiPA27977.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0179.
GeneTreeiENSGT00390000008646.
HOGENOMiHOG000256845.
HOVERGENiHBG001919.
InParanoidiP16930.
KOiK01555.
OMAiLSWKGTK.
PhylomeDBiP16930.
TreeFamiTF315211.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00341.
BioCyciMetaCyc:HS02536-MONOMER.
ReactomeiREACT_1786. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

ChiTaRSiFAH. human.
GeneWikiiFumarylacetoacetate_hydrolase.
GenomeRNAii2184.
NextBioi8817.
PROiP16930.
SOURCEiSearch...

Gene expression databases

BgeeiP16930.
CleanExiHS_FAH.
ExpressionAtlasiP16930. baseline and differential.
GenevestigatoriP16930.

Family and domain databases

Gene3Di2.30.30.230. 1 hit.
3.90.850.10. 1 hit.
InterProiIPR005959. Fumarylacetoacetase.
IPR002529. Fumarylacetoacetase_C.
IPR011234. Fumarylacetoacetase_C-rel.
IPR015377. Fumarylacetoacetase_N.
[Graphical view]
PANTHERiPTHR11820:SF1. PTHR11820:SF1. 1 hit.
PfamiPF01557. FAA_hydrolase. 1 hit.
PF09298. FAA_hydrolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56529. SSF56529. 1 hit.
SSF63433. SSF63433. 1 hit.
TIGRFAMsiTIGR01266. fum_ac_acetase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the cDNA encoding human fumarylacetoacetate hydrolase, the enzyme deficient in hereditary tyrosinemia: assignment of the gene to chromosome 15."
    Phaneuf D., Labelle Y., Berube D., Arden K., Cavenee W., Gagne R., Tanguay R.M.
    Am. J. Hum. Genet. 48:525-535(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "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 1).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Small intestine.
  5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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).
    Tissue: Placenta.
  8. Bienvenut W.V.
    Submitted (JAN-2010) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-25; 32-47; 83-95 AND 195-211, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  9. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 71-419 (ISOFORM 1).
    Tissue: Liver.
  10. "Mutations in the fumarylacetoacetate hydrolase gene causing hereditary tyrosinemia type I: overview."
    St Louis M., Tanguay R.M.
    Hum. Mutat. 9:291-299(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Type 1 hereditary tyrosinemia. Evidence for molecular heterogeneity and identification of a causal mutation in a French Canadian patient."
    Phaneuf D., Lambert M., Laframboise R., Mitchell G., Lettre F., Tanguay R.M.
    J. Clin. Invest. 90:1185-1192(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TYRSN1 ILE-16.
  13. "Characterization of the human fumarylacetoacetate hydrolase gene and identification of a missense mutation abolishing enzymatic activity."
    Labelle Y., Phaneuf D., Leclerc B., Tanguay R.M.
    Hum. Mol. Genet. 2:941-946(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TYRSN1 ASP-134.
  14. "Mutations of the fumarylacetoacetate hydrolase gene in four patients with tyrosinemia, type I."
    Grompe M., Al-Dhalimy M.
    Hum. Mutat. 2:85-93(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TYRSN1 GLY-166.
  15. "Novel splice, missense, and nonsense mutations in the fumarylacetoacetase gene causing tyrosinemia type 1."
    Rootwelt H., Berger R., Gray G., Kelly D.A., Coskun T., Kvittingen E.A.
    Am. J. Hum. Genet. 55:653-658(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TYRSN1 VAL-233.
  16. "Identification of a frequent pseudodeficiency mutation in the fumarylacetoacetase gene, with implications for diagnosis of tyrosinemia type I."
    Rootwelt H., Brodtkorb E., Kvittingen E.A.
    Am. J. Hum. Genet. 55:1122-1127(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TYRSN1 TRP-341.
  17. "Two missense mutations causing tyrosinemia type 1 with presence and absence of immunoreactive fumarylacetoacetase."
    Rootwelt H., Chou J., Gahl W.A., Berger R., Coskun T., Brodtkorb E., Kvittingen E.A.
    Hum. Genet. 93:615-619(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TYRSN1 ASP-134 AND LEU-342.
  18. "Two novel mutations involved in hereditary tyrosinemia type I."
    St Louis M., Poudrier J., Phaneuf D., Leclerc B., Laframboise R., Tanguay R.M.
    Hum. Mol. Genet. 4:319-320(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TYRSN1 SER-337 AND GLY-381.
  19. "Heterozygosity for an exon 12 splicing mutation and a W234G missense mutation in an American child with chronic tyrosinemia type 1."
    Hahn S.H., Krasnewich D., Brantly M., Kvittingen E.A., Gahl W.A.
    Hum. Mutat. 6:66-73(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TYRSN1 GLY-234.
  20. "Hereditary tyrosinemia type 1: novel missense, nonsense and splice consensus mutations in the human fumarylacetoacetate hydrolase gene; variability of the genotype-phenotype relationship."
    Ploos van Amstel J.K., Bergman A.J.I.W., van Beurden E.A.C.M., Roijers J.F.M., Peelen T., van den Berg I.E.T., Poll-The B.T., Kvittingen E.A., Berger R.
    Hum. Genet. 97:51-59(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TYRSN1 ARG-193 AND VAL-369.
  21. "Spectrum of mutations in the fumarylacetoacetate hydrolase gene of tyrosinemia type 1 patients in northwestern Europe and Mediterranean countries."
    Bergman A.J.I.W., van den Berg I.E.T., Brink W., Poll-The B.T., Ploos van Amstel J.K., Berger R.
    Hum. Mutat. 12:19-26(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TYRSN1 ASP-158; LEU-261; SER-366 DEL AND HIS-405.
  22. Cited for: VARIANT TYRSN1 ARG-279.
  23. "A missense mutation (Q279R) in the fumarylacetoacetate hydrolase gene, responsible for hereditary tyrosinemia, acts as a splicing mutation."
    Dreumont N., Poudrier J.A., Bergeron A., Levy H.L., Baklouti F., Tanguay R.M.
    BMC Genet. 2:9-9(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TYRSN1 ARG-279.
  24. "Structural and functional analysis of missense mutations in fumarylacetoacetate hydrolase, the gene deficient in hereditary tyrosinemia type 1."
    Bergeron A., D'Astous M., Timm D.E., Tanguay R.M.
    J. Biol. Chem. 276:15225-15231(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS TYRSN1 ILE-16; CYS-62; ASP-134; ARG-193; VAL-233; GLY-234; ARG-279 AND TRP-341.
  25. "A novel mutation causing mild, atypical fumarylacetoacetase deficiency (Tyrosinemia type I): a case report."
    Cassiman D., Zeevaert R., Holme E., Kvittingen E.A., Jaeken J.
    Orphanet J. Rare Dis. 4:28-28(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TYRSN1 THR-35.

Entry informationi

Entry nameiFAAA_HUMAN
AccessioniPrimary (citable) accession number: P16930
Secondary accession number(s): B2R9X1, D3DW95, Q53XA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1992
Last modified: February 4, 2015
This is version 153 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.