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P17735 (ATTY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine aminotransferase

Short name=TAT
EC=2.6.1.5
Alternative name(s):
L-tyrosine:2-oxoglutarate aminotransferase
Gene names
Name:TAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.6

Catalytic activity

L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate. Ref.3 Ref.6

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 2/6.

Subunit structure

Homodimer Probable.

Involvement in disease

Tyrosinemia 2 (TYRO2) [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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Biological processPhenylalanine catabolism
Tyrosine catabolism
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Mental retardation
Palmoplantar keratoderma
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

L-phenylalanine catabolic process

Traceable author statement. Source: Reactome

biosynthetic process

Inferred from electronic annotation. Source: InterPro

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

glutamate metabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to mercury ion

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

tyrosine catabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionL-phenylalanine:2-oxoglutarate aminotransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

L-tyrosine:2-oxoglutarate aminotransferase activity

Inferred from direct assay Ref.3. Source: UniProtKB

amino acid binding

Inferred from electronic annotation. Source: Ensembl

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Tyrosine aminotransferase
PRO_0000123887

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2801N6-(pyridoxal phosphate)lysine

Natural variations

Natural variant701N → D.
Corresponds to variant rs16973344 [ dbSNP | Ensembl ].
VAR_048226
Natural variant3621G → V in TYRO2. Ref.8
Corresponds to variant rs28934277 [ dbSNP | Ensembl ].
VAR_000560

Experimental info

Mutagenesis2941I → A: Reduced catalytic activity. Ref.6

Secondary structure

............................................................... 454
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17735 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 82B5B24F3B2CE489

FASTA45450,399
        10         20         30         40         50         60 
MDPYMIQMSS KGNLPSILDV HVNVGGRSSV PGKMKGRKAR WSVRPSDMAK KTFNPIRAIV 

        70         80         90        100        110        120 
DNMKVKPNPN KTMISLSIGD PTVFGNLPTD PEVTQAMKDA LDSGKYNGYA PSIGFLSSRE 

       130        140        150        160        170        180 
EIASYYHCPE APLEAKDVIL TSGCSQAIDL CLAVLANPGQ NILVPRPGFS LYKTLAESMG 

       190        200        210        220        230        240 
IEVKLYNLLP EKSWEIDLKQ LEYLIDEKTA CLIVNNPSNP CGSVFSKRHL QKILAVAARQ 

       250        260        270        280        290        300 
CVPILADEIY GDMVFSDCKY EPLATLSTDV PILSCGGLAK RWLVPGWRLG WILIHDRRDI 

       310        320        330        340        350        360 
FGNEIRDGLV KLSQRILGPC TIVQGALKSI LCRTPGEFYH NTLSFLKSNA DLCYGALAAI 

       370        380        390        400        410        420 
PGLRPVRPSG AMYLMVGIEM EHFPEFENDV EFTERLVAEQ SVHCLPATCF EYPNFIRVVI 

       430        440        450 
TVPEVMMLEA CSRIQEFCEQ HYHCAEGSQE ECDK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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 TYRO2 VAL-362.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52520 mRNA. Translation: CAA36750.1.
X52509 expand/collapse EMBL AC list , 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.
PIRS10887.
RefSeqNP_000344.1. NM_000353.2.
UniGeneHs.161640.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DYDX-ray2.30A/B41-444[»]
ProteinModelPortalP17735.
SMRP17735. Positions 41-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112761. 1 interaction.
STRING9606.ENSP00000348234.

Chemistry

ChEMBLCHEMBL3043.
DrugBankDB00142. L-Glutamic Acid.
DB00120. L-Phenylalanine.
DB00135. L-Tyrosine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteP17735.

Polymorphism databases

DMDM114713.

Proteomic databases

PaxDbP17735.
PRIDEP17735.

Protocols and materials databases

DNASU6898.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355962; ENSP00000348234; ENSG00000198650.
GeneID6898.
KEGGhsa:6898.
UCSCuc002fap.2. human.

Organism-specific databases

CTD6898.
GeneCardsGC16M071599.
HGNCHGNC:11573. TAT.
HPAHPA029316.
MIM276600. phenotype.
613018. gene.
neXtProtNX_P17735.
Orphanet28378. Tyrosinemia type 2.
PharmGKBPA36338.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000239005.
HOVERGENHBG004318.
InParanoidP17735.
KOK00815.
OMAFRVVITV.
OrthoDBEOG7PVWP7.
PhylomeDBP17735.
TreeFamTF105999.

Enzyme and pathway databases

BioCycMetaCyc:HS06761-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00139; UER00338.

Gene expression databases

BgeeP17735.
CleanExHS_TAT.
GenevestigatorP17735.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. 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]
PfamPF00155. Aminotran_1_2. 1 hit.
PF07706. TAT_ubiq. 1 hit.
[Graphical view]
PIRSFPIRSF000517. Tyr_transaminase. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01264. tyr_amTase_E. 1 hit.
TIGR01265. tyr_nico_aTase. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTAT. human.
EvolutionaryTraceP17735.
GenomeRNAi6898.
NextBio26963.
PROP17735.
SOURCESearch...

Entry information

Entry nameATTY_HUMAN
AccessionPrimary (citable) accession number: P17735
Secondary accession number(s): B2R8I1, D3DWS2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM