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Protein

Tyrosine aminotransferase

Gene

TAT

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

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

Pathway:iL-phenylalanine degradation

This protein is involved in step 2 of the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Phenylalanine-4-hydroxylase (PAH)
  2. Tyrosine aminotransferase (TAT)
  3. 4-hydroxyphenylpyruvate dioxygenase (HPD)
  4. Homogentisate 1,2-dioxygenase (HGD)
  5. Maleylacetoacetate isomerase (GSTZ1)
  6. Fumarylacetoacetase (FAH)
This subpathway is part of the pathway L-phenylalanine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine, the pathway L-phenylalanine degradation and in Amino-acid degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:11573. TAT.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Tyrosinemia 2 (TYRSN2)1 Publication

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 oculocutaneous manifestations. Typical features include palmoplantar keratosis, painful corneal ulcers, and mental retardation.

See also OMIM:276600
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.

Chemistry

DrugBankiDB00120. L-Phenylalanine.
DB00135. L-Tyrosine.

Polymorphism and mutation databases

BioMutaiTAT.
DMDMi114713.

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
Modified residuei448 – 4481Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP17735.
PaxDbiP17735.
PRIDEiP17735.

PTM databases

PhosphoSiteiP17735.

Expressioni

Gene expression databases

BgeeiP17735.
CleanExiHS_TAT.
GenevisibleiP17735. HS.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi112761. 4 interactions.
STRINGi9606.ENSP00000348234.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00650000093238.
HOGENOMiHOG000239005.
HOVERGENiHBG004318.
InParanoidiP17735.
KOiK00815.
OMAiNADLCYA.
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.
[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

        10         20         30         40         50
MDPYMIQMSS KGNLPSILDV HVNVGGRSSV PGKMKGRKAR WSVRPSDMAK
60 70 80 90 100
KTFNPIRAIV DNMKVKPNPN KTMISLSIGD PTVFGNLPTD PEVTQAMKDA
110 120 130 140 150
LDSGKYNGYA PSIGFLSSRE EIASYYHCPE APLEAKDVIL TSGCSQAIDL
160 170 180 190 200
CLAVLANPGQ NILVPRPGFS LYKTLAESMG IEVKLYNLLP EKSWEIDLKQ
210 220 230 240 250
LEYLIDEKTA CLIVNNPSNP CGSVFSKRHL QKILAVAARQ CVPILADEIY
260 270 280 290 300
GDMVFSDCKY EPLATLSTDV PILSCGGLAK RWLVPGWRLG WILIHDRRDI
310 320 330 340 350
FGNEIRDGLV KLSQRILGPC TIVQGALKSI LCRTPGEFYH NTLSFLKSNA
360 370 380 390 400
DLCYGALAAI PGLRPVRPSG AMYLMVGIEM EHFPEFENDV EFTERLVAEQ
410 420 430 440 450
SVHCLPATCF EYPNFIRVVI TVPEVMMLEA CSRIQEFCEQ HYHCAEGSQE

ECDK
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi112761. 4 interactions.
STRINGi9606.ENSP00000348234.

Chemistry

ChEMBLiCHEMBL3043.
DrugBankiDB00120. L-Phenylalanine.
DB00135. L-Tyrosine.

PTM databases

PhosphoSiteiP17735.

Polymorphism and mutation databases

BioMutaiTAT.
DMDMi114713.

Proteomic databases

MaxQBiP17735.
PaxDbiP17735.
PRIDEiP17735.

Protocols and materials databases

DNASUi6898.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6898.
GeneCardsiGC16M071599.
HGNCiHGNC:11573. TAT.
MIMi276600. phenotype.
613018. gene.
neXtProtiNX_P17735.
Orphaneti28378. Tyrosinemia type 2.
PharmGKBiPA36338.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0436.
GeneTreeiENSGT00650000093238.
HOGENOMiHOG000239005.
HOVERGENiHBG004318.
InParanoidiP17735.
KOiK00815.
OMAiNADLCYA.
OrthoDBiEOG7PVWP7.
PhylomeDBiP17735.
TreeFamiTF105999.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiTAT. human.
EvolutionaryTraceiP17735.
GenomeRNAii6898.
NextBioi26963.
PROiP17735.
SOURCEiSearch...

Gene expression databases

BgeeiP17735.
CleanExiHS_TAT.
GenevisibleiP17735. HS.

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.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "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.
  9. "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: July 22, 2015
This is version 159 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

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.