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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

Pathwayi: L-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

  • 2-oxoglutarate metabolic process Source: UniProtKB
  • biosynthetic process Source: InterPro
  • glutamate metabolic process Source: UniProtKB
  • L-phenylalanine catabolic process Source: Reactome
  • response to glucocorticoid Source: Ensembl
  • response to mercury ion Source: Ensembl
  • response to oxidative stress Source: Ensembl
  • tyrosine catabolic process Source: UniProtKB

Keywordsi

Molecular functionAminotransferase, Transferase
Biological processPhenylalanine catabolism, Tyrosine catabolism
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS06761-MONOMER.
ReactomeiR-HSA-71182. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:11573. TAT.

Subcellular locationi

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_000560362G → V in TYRSN2. 1 PublicationCorresponds to variant dbSNP:rs587776511Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi294I → A: Reduced catalytic activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation, Palmoplantar keratoderma

Organism-specific databases

DisGeNETi6898.
MalaCardsiTAT.
MIMi276600. phenotype.
OpenTargetsiENSG00000198650.
Orphaneti28378. Tyrosinemia type 2.
PharmGKBiPA36338.

Chemistry databases

ChEMBLiCHEMBL3043.
DrugBankiDB00142. L-Glutamic Acid.
DB00120. L-Phenylalanine.
DB00135. L-Tyrosine.
DB00114. Pyridoxal Phosphate.

Polymorphism and mutation databases

BioMutaiTAT.
DMDMi114713.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001238871 – 454Tyrosine aminotransferaseAdd BLAST454

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei280N6-(pyridoxal phosphate)lysine1
Modified residuei448PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP17735.
PaxDbiP17735.
PeptideAtlasiP17735.
PRIDEiP17735.

PTM databases

iPTMnetiP17735.
PhosphoSitePlusiP17735.

Expressioni

Gene expression databases

BgeeiENSG00000198650.
CleanExiHS_TAT.
ExpressionAtlasiP17735. baseline and differential.
GenevisibleiP17735. HS.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi112761. 4 interactors.
IntActiP17735. 4 interactors.
STRINGi9606.ENSP00000348234.

Structurei

Secondary structure

1454
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni81 – 84Combined sources4
Beta strandi85 – 87Combined sources3
Helixi91 – 103Combined sources13
Beta strandi106 – 108Combined sources3
Helixi116 – 126Combined sources11
Helixi135 – 137Combined sources3
Beta strandi138 – 143Combined sources6
Helixi144 – 155Combined sources12
Beta strandi161 – 167Combined sources7
Helixi171 – 178Combined sources8
Beta strandi182 – 188Combined sources7
Helixi190 – 192Combined sources3
Helixi198 – 202Combined sources5
Beta strandi209 – 217Combined sources9
Turni219 – 221Combined sources3
Helixi227 – 239Combined sources13
Beta strandi244 – 247Combined sources4
Turni249 – 252Combined sources4
Helixi263 – 266Combined sources4
Beta strandi272 – 278Combined sources7
Turni279 – 281Combined sources3
Helixi285 – 287Combined sources3
Beta strandi290 – 295Combined sources6
Helixi302 – 316Combined sources15
Helixi321 – 333Combined sources13
Helixi336 – 359Combined sources24
Beta strandi363 – 366Combined sources4
Beta strandi373 – 378Combined sources6
Helixi380 – 382Combined sources3
Helixi389 – 400Combined sources12
Helixi407 – 410Combined sources4
Beta strandi415 – 420Combined sources6
Helixi424 – 441Combined sources18

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP17735.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0259. Eukaryota.
COG0436. LUCA.
GeneTreeiENSGT00650000093238.
HOGENOMiHOG000239005.
HOVERGENiHBG004318.
InParanoidiP17735.
KOiK00815.
OMAiFRVVITV.
OrthoDBiEOG091G06R8.
PhylomeDBiP17735.
TreeFamiTF105999.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiView protein in InterPro
IPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_sub2.
IPR011715. Tyr_aminoTrfase_ubiquitination.
IPR005958. TyrNic_aminoTrfase.
IPR005957. Tyrosine_aminoTrfase.
PfamiView protein in Pfam
PF00155. Aminotran_1_2. 1 hit.
PF07706. TAT_ubiq. 1 hit.
PIRSFiPIRSF000517. Tyr_transaminase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01264. tyr_amTase_E. 1 hit.
TIGR01265. tyr_nico_aTase. 1 hit.
PROSITEiView protein in PROSITE
PS00105. AA_TRANSFER_CLASS_1. 1 hit.

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_04822670N → D. Corresponds to variant dbSNP:rs16973344Ensembl.1
Natural variantiVAR_000560362G → V in TYRSN2. 1 PublicationCorresponds to variant dbSNP:rs587776511Ensembl.1

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.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiATTY_HUMAN
AccessioniPrimary (citable) accession number: P17735
Secondary accession number(s): B2R8I1, D3DWS2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: August 30, 2017
This is version 177 of the entry and version 1 of the sequence. See 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