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O43708

- MAAI_HUMAN

UniProt

O43708 - MAAI_HUMAN

Protein

Maleylacetoacetate isomerase

Gene

GSTZ1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 3 (24 Nov 2009)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.1 Publication

    Catalytic activityi

    4-maleylacetoacetate = 4-fumarylacetoacetate.1 Publication
    RX + glutathione = HX + R-S-glutathione.1 Publication

    Cofactori

    Glutathione. Required for the MAAI activity.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei45 – 451Glutathione1 Publication
    Binding sitei59 – 591Glutathione; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei111 – 1111Glutathione1 Publication

    GO - Molecular functioni

    1. glutathione peroxidase activity Source: ProtInc
    2. glutathione transferase activity Source: UniProtKB
    3. maleylacetoacetate isomerase activity Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. glutathione derivative biosynthetic process Source: Reactome
    3. glutathione metabolic process Source: UniProtKB
    4. L-phenylalanine catabolic process Source: Reactome
    5. oxidation-reduction process Source: GOC
    6. small molecule metabolic process Source: Reactome
    7. tyrosine catabolic process Source: UniProtKB-KW
    8. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Isomerase, Transferase

    Keywords - Biological processi

    Phenylalanine catabolism, Tyrosine catabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02114-MONOMER.
    BRENDAi5.2.1.2. 2681.
    ReactomeiREACT_1786. Phenylalanine and tyrosine catabolism.
    REACT_6926. Glutathione conjugation.
    UniPathwayiUPA00139; UER00340.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Maleylacetoacetate isomerase (EC:5.2.1.2)
    Short name:
    MAAI
    Alternative name(s):
    GSTZ1-1
    Glutathione S-transferase zeta 1 (EC:2.5.1.18)
    Gene namesi
    Name:GSTZ1
    Synonyms:MAAI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:4643. GSTZ1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29031.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 216216Maleylacetoacetate isomerasePRO_0000186022Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei32 – 321N6-acetyllysine1 Publication
    Modified residuei57 – 571N6-succinyllysineBy similarity
    Modified residuei136 – 1361PhosphothreonineBy similarity
    Modified residuei177 – 1771N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO43708.
    PaxDbiO43708.
    PRIDEiO43708.

    PTM databases

    PhosphoSiteiO43708.

    Expressioni

    Tissue specificityi

    Mostly expressed in liver followed by kidney, skeletal muscle and brain. Also expressed in melanocytes, synovium, placenta, breast and fetal liver and heart.

    Gene expression databases

    ArrayExpressiO43708.
    BgeeiO43708.
    CleanExiHS_GSTZ1.
    GenevestigatoriO43708.

    Organism-specific databases

    HPAiHPA004701.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK1P163332EBI-748043,EBI-389883

    Protein-protein interaction databases

    BioGridi109209. 5 interactions.
    IntActiO43708. 5 interactions.
    MINTiMINT-1444642.
    STRINGi9606.ENSP00000216465.

    Structurei

    Secondary structure

    1
    216
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Helixi15 – 2612
    Beta strandi32 – 354
    Helixi44 – 463
    Helixi48 – 536
    Beta strandi61 – 644
    Beta strandi67 – 715
    Helixi72 – 8211
    Helixi93 – 10917
    Helixi111 – 1144
    Helixi116 – 1227
    Helixi124 – 14926
    Beta strandi150 – 1567
    Helixi161 – 17515
    Helixi184 – 19411
    Helixi197 – 1993
    Turni200 – 2023
    Helixi204 – 2063

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FW1X-ray1.90A1-216[»]
    ProteinModelPortaliO43708.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43708.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 8784GST N-terminalAdd
    BLAST
    Domaini92 – 212121GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 196Glutathione binding
    Regioni71 – 722Glutathione binding
    Regioni115 – 1173Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Zeta family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG0625.
    HOVERGENiHBG001501.
    KOiK01800.
    OrthoDBiEOG7TF79P.
    PhylomeDBiO43708.
    TreeFamiTF105324.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR005955. Mal_ac_isom.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    TIGRFAMsiTIGR01262. maiA. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43708-1) [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

    MQAGKPILYS YFRSSCSWRV RIALALKGID YKTVPINLIK DRGQQFSKDF    50
    QALNPMKQVP TLKIDGITIH QSLAIIEYLE EMRPTPRLLP QDPKKRASVR 100
    MISDLIAGGI QPLQNLSVLK QVGEEMQLTW AQNAITCGFN ALEQILQSTA 150
    GIYCVGDEVT MADLCLVPQV ANAERFKVDL TPYPTISSIN KRLLVLEAFQ 200
    VSHPCRQPDT PTELRA 216
    Length:216
    Mass (Da):24,212
    Last modified:November 24, 2009 - v3
    Checksum:i2B3112B8AE6B55E0
    GO
    Isoform 2 (identifier: O43708-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-55: Missing.

    Show »
    Length:161
    Mass (Da):17,896
    Checksum:i8EF7E58223F1C0E3
    GO
    Isoform 3 (identifier: O43708-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         73-114: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:174
    Mass (Da):19,472
    Checksum:i9C4636C87F67ADED
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321K → E in allele GSTZ1*C. 6 Publications
    Corresponds to variant rs7975 [ dbSNP | Ensembl ].
    VAR_009705
    Natural varianti42 – 421R → G in allele GSTZ1*B and allele GSTZ1*C. 9 Publications
    Corresponds to variant rs7972 [ dbSNP | Ensembl ].
    VAR_009706
    Natural varianti82 – 821M → T.7 Publications
    Corresponds to variant rs1046428 [ dbSNP | Ensembl ].
    VAR_009707
    Natural varianti133 – 1331N → H.1 Publication
    Corresponds to variant rs2234955 [ dbSNP | Ensembl ].
    VAR_014505

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5555Missing in isoform 2. 1 PublicationVSP_039862Add
    BLAST
    Alternative sequencei73 – 11442Missing in isoform 3. CuratedVSP_047392Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001838 mRNA. Translation: CAA05045.1.
    U86529 mRNA. Translation: AAB96392.1.
    AF053545
    , AF053539, AF053540, AF053541, AF053542, AF053543, AF053544 Genomic DNA. Translation: AAC33591.1.
    AF098318
    , AF095582, AF098311, AF098312, AF098313, AF098314, AF098315, AF098316, AF098317 Genomic DNA. Translation: AAD43007.1.
    AK315154 mRNA. Translation: BAG37600.1.
    CR456987 mRNA. Translation: CAG33268.1.
    AY316305 Genomic DNA. Translation: AAP69526.1.
    AC007954 Genomic DNA. Translation: AAF62559.1.
    CH471061 Genomic DNA. Translation: EAW81278.1.
    CH471061 Genomic DNA. Translation: EAW81279.1.
    BC001453 mRNA. Translation: AAH01453.1.
    CCDSiCCDS9858.1. [O43708-1]
    CCDS9859.1. [O43708-3]
    CCDS9860.1. [O43708-2]
    RefSeqiNP_001504.2. NM_001513.3. [O43708-2]
    NP_665877.1. NM_145870.2.
    NP_665878.2. NM_145871.2.
    XP_005267616.1. XM_005267559.1. [O43708-2]
    UniGeneiHs.655292.

    Genome annotation databases

    EnsembliENST00000216465; ENSP00000216465; ENSG00000100577.
    ENST00000361389; ENSP00000354959; ENSG00000100577. [O43708-2]
    ENST00000393734; ENSP00000377335; ENSG00000100577. [O43708-2]
    ENST00000557639; ENSP00000451927; ENSG00000100577. [O43708-2]
    GeneIDi2954.
    KEGGihsa:2954.
    UCSCiuc001xtk.3. human.
    uc001xtm.3. human. [O43708-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001838 mRNA. Translation: CAA05045.1 .
    U86529 mRNA. Translation: AAB96392.1 .
    AF053545
    , AF053539 , AF053540 , AF053541 , AF053542 , AF053543 , AF053544 Genomic DNA. Translation: AAC33591.1 .
    AF098318
    , AF095582 , AF098311 , AF098312 , AF098313 , AF098314 , AF098315 , AF098316 , AF098317 Genomic DNA. Translation: AAD43007.1 .
    AK315154 mRNA. Translation: BAG37600.1 .
    CR456987 mRNA. Translation: CAG33268.1 .
    AY316305 Genomic DNA. Translation: AAP69526.1 .
    AC007954 Genomic DNA. Translation: AAF62559.1 .
    CH471061 Genomic DNA. Translation: EAW81278.1 .
    CH471061 Genomic DNA. Translation: EAW81279.1 .
    BC001453 mRNA. Translation: AAH01453.1 .
    CCDSi CCDS9858.1. [O43708-1 ]
    CCDS9859.1. [O43708-3 ]
    CCDS9860.1. [O43708-2 ]
    RefSeqi NP_001504.2. NM_001513.3. [O43708-2 ]
    NP_665877.1. NM_145870.2.
    NP_665878.2. NM_145871.2.
    XP_005267616.1. XM_005267559.1. [O43708-2 ]
    UniGenei Hs.655292.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FW1 X-ray 1.90 A 1-216 [» ]
    ProteinModelPortali O43708.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109209. 5 interactions.
    IntActi O43708. 5 interactions.
    MINTi MINT-1444642.
    STRINGi 9606.ENSP00000216465.

    Chemistry

    ChEMBLi CHEMBL4949.
    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei O43708.

    Proteomic databases

    MaxQBi O43708.
    PaxDbi O43708.
    PRIDEi O43708.

    Protocols and materials databases

    DNASUi 2954.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216465 ; ENSP00000216465 ; ENSG00000100577 .
    ENST00000361389 ; ENSP00000354959 ; ENSG00000100577 . [O43708-2 ]
    ENST00000393734 ; ENSP00000377335 ; ENSG00000100577 . [O43708-2 ]
    ENST00000557639 ; ENSP00000451927 ; ENSG00000100577 . [O43708-2 ]
    GeneIDi 2954.
    KEGGi hsa:2954.
    UCSCi uc001xtk.3. human.
    uc001xtm.3. human. [O43708-1 ]

    Organism-specific databases

    CTDi 2954.
    GeneCardsi GC14P077787.
    HGNCi HGNC:4643. GSTZ1.
    HPAi HPA004701.
    MIMi 603758. gene.
    neXtProti NX_O43708.
    PharmGKBi PA29031.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0625.
    HOVERGENi HBG001501.
    KOi K01800.
    OrthoDBi EOG7TF79P.
    PhylomeDBi O43708.
    TreeFami TF105324.

    Enzyme and pathway databases

    UniPathwayi UPA00139 ; UER00340 .
    BioCyci MetaCyc:HS02114-MONOMER.
    BRENDAi 5.2.1.2. 2681.
    Reactomei REACT_1786. Phenylalanine and tyrosine catabolism.
    REACT_6926. Glutathione conjugation.

    Miscellaneous databases

    ChiTaRSi GSTZ1. human.
    EvolutionaryTracei O43708.
    GeneWikii GSTZ1.
    GenomeRNAii 2954.
    NextBioi 11706.
    PROi O43708.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43708.
    Bgeei O43708.
    CleanExi HS_GSTZ1.
    Genevestigatori O43708.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR005955. Mal_ac_isom.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    TIGRFAMsi TIGR01262. maiA. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue."
      Fernandez-Canon J.M., Penalva M.A.
      J. Biol. Chem. 273:329-337(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, VARIANTS GLY-42 AND THR-82.
    2. "Zeta, a novel class of glutathione transferases in a range of species from plants to humans."
      Board P.G., Baker R.T., Chelvanayagam G., Jermiin L.S.
      Biochem. J. 328:929-935(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT THR-82, CHARACTERIZATION.
    3. "Characterization and chromosome location of the gene GSTZ1 encoding the human zeta class glutathione transferase and maleylacetoacetate isomerase."
      Blackburn A.C., Woollatt E., Sutherland G.R., Board P.G.
      Cytogenet. Cell Genet. 83:109-114(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS GLU-32; GLY-42 AND THR-82.
    4. "Gene structure, chromosomal location, and expression pattern of maleylacetoacetate isomerase."
      Fernandez-Canon J.M., Hejna J., Reifsteck C., Olson S., Grompe M.
      Genomics 58:263-269(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS GLY-42 AND THR-82.
    5. "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), VARIANT THR-82.
      Tissue: Skeletal muscle.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLY-42 AND THR-82.
    7. NIEHS SNPs program
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS GLU-32; GLY-42; THR-82 AND HIS-133.
    8. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLU-32 AND GLY-42.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLU-32 AND GLY-42.
    10. "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), VARIANTS GLU-32 AND GLY-42.
      Tissue: Placenta.
    11. "Glutathione transferase zeta catalyses the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid."
      Tong Z., Board P.G., Anders M.W.
      Biochem. J. 331:371-374(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Discovery of a functional polymorphism in human glutathione transferase zeta by expressed sequence tag database analysis."
      Blackburn A.C., Tzeng H.F., Anders M.W., Board P.G.
      Pharmacogenetics 10:49-57(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLU-32 AND GLY-42, FUNCTION, CATALYTIC ACTIVITY.
    16. "Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity."
      Polekhina G., Board P.G., Blackburn A.C., Parker M.W.
      Biochemistry 40:1567-1576(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.

    Entry informationi

    Entry nameiMAAI_HUMAN
    AccessioniPrimary (citable) accession number: O43708
    Secondary accession number(s): A6NED0
    , A6NNB8, A8MWD7, B2RCK3, O15308, O75430, Q6IB17, Q7Z610, Q9BV63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 160 of the entry and version 3 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

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3