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P17735

- ATTY_HUMAN

UniProt

P17735 - ATTY_HUMAN

Protein

Tyrosine aminotransferase

Gene

TAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine.2 Publications

    Catalytic activityi

    L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate.2 Publications

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    GO - Molecular functioni

    1. amino acid binding Source: Ensembl
    2. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
    3. L-tyrosine:2-oxoglutarate aminotransferase activity Source: UniProtKB
    4. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: UniProtKB
    2. biosynthetic process Source: InterPro
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. glutamate metabolic process Source: UniProtKB
    5. L-phenylalanine catabolic process Source: Reactome
    6. response to glucocorticoid Source: Ensembl
    7. response to mercury ion Source: Ensembl
    8. response to oxidative stress Source: Ensembl
    9. small molecule metabolic process Source: Reactome
    10. tyrosine catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Phenylalanine catabolism, Tyrosine catabolism

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06761-MONOMER.
    ReactomeiREACT_1786. Phenylalanine and tyrosine catabolism.
    UniPathwayiUPA00139; UER00338.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine aminotransferase (EC:2.6.1.5)
    Short name:
    TAT
    Alternative name(s):
    L-tyrosine:2-oxoglutarate aminotransferase
    Gene namesi
    Name:TAT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:11573. TAT.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Tyrosinemia 2 (TYRSN2) [MIM:276600]: An inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, and oculocutaneous manifestations. Typical features include palmoplantar keratosis, painful corneal ulcers, and mental retardation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti362 – 3621G → V in TYRSN2. 1 Publication
    Corresponds to variant rs28934277 [ dbSNP | Ensembl ].
    VAR_000560

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi294 – 2941I → A: Reduced catalytic activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Mental retardation, Palmoplantar keratoderma

    Organism-specific databases

    MIMi276600. phenotype.
    Orphaneti28378. Tyrosinemia type 2.
    PharmGKBiPA36338.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 454454Tyrosine aminotransferasePRO_0000123887Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei280 – 2801N6-(pyridoxal phosphate)lysine

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP17735.
    PaxDbiP17735.
    PRIDEiP17735.

    PTM databases

    PhosphoSiteiP17735.

    Expressioni

    Gene expression databases

    BgeeiP17735.
    CleanExiHS_TAT.
    GenevestigatoriP17735.

    Organism-specific databases

    HPAiHPA029316.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi112761. 1 interaction.
    STRINGi9606.ENSP00000348234.

    Structurei

    Secondary structure

    1
    454
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni81 – 844
    Beta strandi85 – 873
    Helixi91 – 10313
    Beta strandi106 – 1083
    Helixi116 – 12611
    Helixi135 – 1373
    Beta strandi138 – 1436
    Helixi144 – 15512
    Beta strandi161 – 1677
    Helixi171 – 1788
    Beta strandi182 – 1887
    Helixi190 – 1923
    Helixi198 – 2025
    Beta strandi209 – 2179
    Turni219 – 2213
    Helixi227 – 23913
    Beta strandi244 – 2474
    Turni249 – 2524
    Helixi263 – 2664
    Beta strandi272 – 2787
    Turni279 – 2813
    Helixi285 – 2873
    Beta strandi290 – 2956
    Helixi302 – 31615
    Helixi321 – 33313
    Helixi336 – 35924
    Beta strandi363 – 3664
    Beta strandi373 – 3786
    Helixi380 – 3823
    Helixi389 – 40012
    Helixi407 – 4104
    Beta strandi415 – 4206
    Helixi424 – 44118

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DYDX-ray2.30A/B41-444[»]
    ProteinModelPortaliP17735.
    SMRiP17735. Positions 41-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17735.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0436.
    HOGENOMiHOG000239005.
    HOVERGENiHBG004318.
    InParanoidiP17735.
    KOiK00815.
    OMAiHCAEGSQ.
    OrthoDBiEOG7PVWP7.
    PhylomeDBiP17735.
    TreeFamiTF105999.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR011715. Tyr_aminoTrfase_ubiquitination.
    IPR005958. TyrNic_aminoTrfase.
    IPR005957. Tyrosine_aminoTrfase.
    IPR021178. Tyrosine_transaminase.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    PF07706. TAT_ubiq. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000517. Tyr_transaminase. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01264. tyr_amTase_E. 1 hit.
    TIGR01265. tyr_nico_aTase. 1 hit.
    PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P17735-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDPYMIQMSS KGNLPSILDV HVNVGGRSSV PGKMKGRKAR WSVRPSDMAK    50
    KTFNPIRAIV DNMKVKPNPN KTMISLSIGD PTVFGNLPTD PEVTQAMKDA 100
    LDSGKYNGYA PSIGFLSSRE EIASYYHCPE APLEAKDVIL TSGCSQAIDL 150
    CLAVLANPGQ NILVPRPGFS LYKTLAESMG IEVKLYNLLP EKSWEIDLKQ 200
    LEYLIDEKTA CLIVNNPSNP CGSVFSKRHL QKILAVAARQ CVPILADEIY 250
    GDMVFSDCKY EPLATLSTDV PILSCGGLAK RWLVPGWRLG WILIHDRRDI 300
    FGNEIRDGLV KLSQRILGPC TIVQGALKSI LCRTPGEFYH NTLSFLKSNA 350
    DLCYGALAAI PGLRPVRPSG AMYLMVGIEM EHFPEFENDV EFTERLVAEQ 400
    SVHCLPATCF EYPNFIRVVI TVPEVMMLEA CSRIQEFCEQ HYHCAEGSQE 450
    ECDK 454
    Length:454
    Mass (Da):50,399
    Last modified:August 1, 1990 - v1
    Checksum:i82B5B24F3B2CE489
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti70 – 701N → D.
    Corresponds to variant rs16973344 [ dbSNP | Ensembl ].
    VAR_048226
    Natural varianti362 – 3621G → V in TYRSN2. 1 Publication
    Corresponds to variant rs28934277 [ dbSNP | Ensembl ].
    VAR_000560

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52520 mRNA. Translation: CAA36750.1.
    X52509
    , X52510, X52511, X52512, X52513, X52514, X52515, X52516, X52517, X52518, X52519 Genomic DNA. Translation: CAA36749.1.
    X55675 mRNA. Translation: CAA39210.1.
    AK313380 mRNA. Translation: BAG36178.1.
    CH471166 Genomic DNA. Translation: EAW59230.1.
    CH471166 Genomic DNA. Translation: EAW59231.1.
    CCDSiCCDS10903.1.
    PIRiS10887.
    RefSeqiNP_000344.1. NM_000353.2.
    UniGeneiHs.161640.

    Genome annotation databases

    EnsembliENST00000355962; ENSP00000348234; ENSG00000198650.
    GeneIDi6898.
    KEGGihsa:6898.
    UCSCiuc002fap.2. human.

    Polymorphism databases

    DMDMi114713.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52520 mRNA. Translation: CAA36750.1 .
    X52509
    , X52510 , X52511 , X52512 , X52513 , X52514 , X52515 , X52516 , X52517 , X52518 , X52519 Genomic DNA. Translation: CAA36749.1 .
    X55675 mRNA. Translation: CAA39210.1 .
    AK313380 mRNA. Translation: BAG36178.1 .
    CH471166 Genomic DNA. Translation: EAW59230.1 .
    CH471166 Genomic DNA. Translation: EAW59231.1 .
    CCDSi CCDS10903.1.
    PIRi S10887.
    RefSeqi NP_000344.1. NM_000353.2.
    UniGenei Hs.161640.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DYD X-ray 2.30 A/B 41-444 [» ]
    ProteinModelPortali P17735.
    SMRi P17735. Positions 41-444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112761. 1 interaction.
    STRINGi 9606.ENSP00000348234.

    Chemistry

    ChEMBLi CHEMBL3043.
    DrugBanki DB00120. L-Phenylalanine.
    DB00135. L-Tyrosine.

    PTM databases

    PhosphoSitei P17735.

    Polymorphism databases

    DMDMi 114713.

    Proteomic databases

    MaxQBi P17735.
    PaxDbi P17735.
    PRIDEi P17735.

    Protocols and materials databases

    DNASUi 6898.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355962 ; ENSP00000348234 ; ENSG00000198650 .
    GeneIDi 6898.
    KEGGi hsa:6898.
    UCSCi uc002fap.2. human.

    Organism-specific databases

    CTDi 6898.
    GeneCardsi GC16M071599.
    HGNCi HGNC:11573. TAT.
    HPAi HPA029316.
    MIMi 276600. phenotype.
    613018. gene.
    neXtProti NX_P17735.
    Orphaneti 28378. Tyrosinemia type 2.
    PharmGKBi PA36338.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0436.
    HOGENOMi HOG000239005.
    HOVERGENi HBG004318.
    InParanoidi P17735.
    KOi K00815.
    OMAi HCAEGSQ.
    OrthoDBi EOG7PVWP7.
    PhylomeDBi P17735.
    TreeFami TF105999.

    Enzyme and pathway databases

    UniPathwayi UPA00139 ; UER00338 .
    BioCyci MetaCyc:HS06761-MONOMER.
    Reactomei REACT_1786. Phenylalanine and tyrosine catabolism.

    Miscellaneous databases

    ChiTaRSi TAT. human.
    EvolutionaryTracei P17735.
    GenomeRNAii 6898.
    NextBioi 26963.
    PROi P17735.
    SOURCEi Search...

    Gene expression databases

    Bgeei P17735.
    CleanExi HS_TAT.
    Genevestigatori P17735.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR004839. Aminotransferase_I/II.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR011715. Tyr_aminoTrfase_ubiquitination.
    IPR005958. TyrNic_aminoTrfase.
    IPR005957. Tyrosine_aminoTrfase.
    IPR021178. Tyrosine_transaminase.
    [Graphical view ]
    Pfami PF00155. Aminotran_1_2. 1 hit.
    PF07706. TAT_ubiq. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000517. Tyr_transaminase. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01264. tyr_amTase_E. 1 hit.
    TIGR01265. tyr_nico_aTase. 1 hit.
    PROSITEi PS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of the human tyrosine aminotransferase gene."
      Rettenmeier R., Natt E., Zentgraf H., Scherer G.
      Nucleic Acids Res. 18:3853-3861(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Nucleotide sequence of the human tyrosine aminotransferase gene."
      Zelenin S.M., Mertvetsov N.P.
      Bioorg. Khim. 20:196-204(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning and expression of human tyrosine aminotransferase cDNA."
      Seralini G.E., Luu-The V., Labrie F.
      Biochim. Biophys. Acta 1260:97-101(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
      Tissue: Liver.
    4. "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].
      Tissue: Liver.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The narrow substrate specificity of human tyrosine aminotransferase -- the enzyme deficient in tyrosinemia type II."
      Sivaraman S., Kirsch J.F.
      FEBS J. 273:1920-1929(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-294.
    7. "Human tyrosine aminotransferase."
      Structural genomics consortium (SGC)
      Submitted (AUG-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-444 IN COMPLEX WITH PYRIDOXAL PHOSPHATE.
    8. "Point mutations in the tyrosine aminotransferase gene in tyrosinemia type II."
      Natt E., Kida K., Odievre M., di Rocco M., Scherer G.
      Proc. Natl. Acad. Sci. U.S.A. 89:9297-9301(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TYRSN2 VAL-362.

    Entry informationi

    Entry nameiATTY_HUMAN
    AccessioniPrimary (citable) accession number: P17735
    Secondary accession number(s): B2R8I1, D3DWS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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