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P17735

- ATTY_HUMAN

UniProt

P17735 - ATTY_HUMAN

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Protein

Tyrosine aminotransferase

Gene

TAT

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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
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: Chromosome 16

Organism-specific databases

HGNCiHGNC:11573. TAT.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: Ensembl
Complete GO annotation...

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. 3 interactions.
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.
GeneTreeiENSGT00650000093238.
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

        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:
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. 3 interactions.
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.
GeneTreei ENSGT00650000093238.
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

« 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. "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 29, 2014
This is version 151 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