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P16930

- FAAA_HUMAN

UniProt

P16930 - FAAA_HUMAN

Protein

Fumarylacetoacetase

Gene

FAH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    4-fumarylacetoacetate + H2O = acetoacetate + fumarate.

    Cofactori

    Calcium.By similarity
    Magnesium.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. aromatic amino acid family metabolic process Source: InterPro
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. L-phenylalanine catabolic process Source: Reactome
    5. small molecule metabolic process Source: Reactome
    6. tyrosine catabolic process Source: ProtInc

    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:3.7.1.2)
    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: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    Tyrosinemia 1 (TYRSN1) [MIM:276700]: An 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.13 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161N → I in TYRSN1; loss of activity. 1 Publication
    VAR_005205
    Natural varianti35 – 351A → T in TYRSN1; atypical mild phenotype. 1 Publication
    VAR_065454
    Natural varianti62 – 621F → C in TYRSN1; loss of activity.
    VAR_005206
    Natural varianti64 – 641Q → H in TYRSN1.
    VAR_005207
    Natural varianti134 – 1341A → D in TYRSN1; loss of activity. 2 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. 1 Publication
    VAR_005211
    Natural varianti207 – 2071G → D in TYRSN1.
    VAR_005212
    Natural varianti233 – 2331D → V in TYRSN1; loss of activity. 1 Publication
    VAR_005213
    Natural varianti234 – 2341W → G in TYRSN1; loss of activity. 1 Publication
    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. 2 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. 1 Publication
    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

    ArrayExpressiP16930.
    BgeeiP16930.
    CleanExiHS_FAH.
    GenevestigatoriP16930.

    Organism-specific databases

    HPAiHPA041370.
    HPA044093.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi108479. 2 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.
    HOGENOMiHOG000256845.
    HOVERGENiHBG001919.
    InParanoidiP16930.
    KOiK01555.
    OMAiFVGPGNK.
    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

    MSFIPVAEDS DFPIHNLPYG VFSTRGDPRP RIGVAIGDQI LDLSIIKHLF    50
    TGPVLSKHQD VFNQPTLNSF MGLGQAAWKE ARVFLQNLLS VSQARLRDDT 100
    ELRKCAFISQ ASATMHLPAT IGDYTDFYSS RQHATNVGIM FRDKENALMP 150
    NWLHLPVGYH GRASSVVVSG TPIRRPMGQM KPDDSKPPVY GACKLLDMEL 200
    EMAFFVGPGN RLGEPIPISK AHEHIFGMVL MNDWSARDIQ KWEYVPLGPF 250
    LGKSFGTTVS PWVVPMDALM PFAVPNPKQD PRPLPYLCHD EPYTFDINLS 300
    VNLKGEGMSQ AATICKSNFK YMYWTMLQQL THHSVNGCNL RPGDLLASGT 350
    ISGPEPENFG SMLELSWKGT KPIDLGNGQT RKFLLDGDEV IITGYCQGDG 400
    YRIGFGQCAG KVLPALLPS 419
    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. 1 Publication
    VAR_005205
    Natural varianti35 – 351A → T in TYRSN1; atypical mild phenotype. 1 Publication
    VAR_065454
    Natural varianti62 – 621F → C in TYRSN1; loss of activity.
    VAR_005206
    Natural varianti64 – 641Q → H in TYRSN1.
    VAR_005207
    Natural varianti134 – 1341A → D in TYRSN1; loss of activity. 2 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. 1 Publication
    VAR_005211
    Natural varianti207 – 2071G → D in TYRSN1.
    VAR_005212
    Natural varianti233 – 2331D → V in TYRSN1; loss of activity. 1 Publication
    VAR_005213
    Natural varianti234 – 2341W → G in TYRSN1; loss of activity. 1 Publication
    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. 2 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. 1 Publication
    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:
    EMBL
    GenBank
    DDBJ
    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.
    PIRiA37926.
    RefSeqiNP_000128.1. NM_000137.2.
    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.

    Polymorphism databases

    DMDMi119778.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS10314.1.
    PIRi A37926.
    RefSeqi NP_000128.1. NM_000137.2.
    UniGenei Hs.73875.

    3D structure databases

    ProteinModelPortali P16930.
    SMRi P16930. Positions 1-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108479. 2 interactions.
    IntActi P16930. 1 interaction.
    STRINGi 9606.ENSP00000261755.

    PTM databases

    PhosphoSitei P16930.

    Polymorphism databases

    DMDMi 119778.

    2D gel databases

    OGPi P16930.
    REPRODUCTION-2DPAGE IPI00031708.

    Proteomic databases

    MaxQBi P16930.
    PaxDbi P16930.
    PeptideAtlasi P16930.
    PRIDEi P16930.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261755 ; ENSP00000261755 ; ENSG00000103876 . [P16930-1 ]
    ENST00000407106 ; ENSP00000385080 ; ENSG00000103876 . [P16930-1 ]
    ENST00000539156 ; ENSP00000454271 ; ENSG00000103876 . [P16930-2 ]
    ENST00000561421 ; ENSP00000453347 ; ENSG00000103876 . [P16930-1 ]
    GeneIDi 2184.
    KEGGi hsa:2184.
    UCSCi uc002bfm.2. human.

    Organism-specific databases

    CTDi 2184.
    GeneCardsi GC15P080445.
    HGNCi HGNC:3579. FAH.
    HPAi HPA041370.
    HPA044093.
    MIMi 276700. phenotype.
    613871. gene.
    neXtProti NX_P16930.
    Orphaneti 882. Tyrosinemia type 1.
    PharmGKBi PA27977.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0179.
    HOGENOMi HOG000256845.
    HOVERGENi HBG001919.
    InParanoidi P16930.
    KOi K01555.
    OMAi FVGPGNK.
    PhylomeDBi P16930.
    TreeFami TF315211.

    Enzyme and pathway databases

    UniPathwayi UPA00139 ; UER00341 .
    BioCyci MetaCyc:HS02536-MONOMER.
    Reactomei REACT_1786. Phenylalanine and tyrosine catabolism.

    Miscellaneous databases

    ChiTaRSi FAH. human.
    GeneWikii Fumarylacetoacetate_hydrolase.
    GenomeRNAii 2184.
    NextBioi 8817.
    PROi P16930.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16930.
    Bgeei P16930.
    CleanExi HS_FAH.
    Genevestigatori P16930.

    Family and domain databases

    Gene3Di 2.30.30.230. 1 hit.
    3.90.850.10. 1 hit.
    InterProi IPR005959. Fumarylacetoacetase.
    IPR002529. Fumarylacetoacetase_C.
    IPR011234. Fumarylacetoacetase_C-rel.
    IPR015377. Fumarylacetoacetase_N.
    [Graphical view ]
    PANTHERi PTHR11820:SF1. PTHR11820:SF1. 1 hit.
    Pfami PF01557. FAA_hydrolase. 1 hit.
    PF09298. FAA_hydrolase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56529. SSF56529. 1 hit.
    SSF63433. SSF63433. 1 hit.
    TIGRFAMsi TIGR01266. fum_ac_acetase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 149 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