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Reviewed, UniProtKB/Swiss-Prot P17735 (ATTY_HUMAN)

Last modified November 24, 2009. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Pathway

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

Subunit structure

Homodimer By similarity.

Involvement in disease

Defects in TAT are the cause of tyrosinemia type 2 (TYRO2) [MIM:276600]; also known as Richner-Hanhart syndrome. TYRO2 is 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. Ref.7

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Tyrosine aminotransferase
PRO_0000123887

Amino acid modifications

Modified residue2801N6-(pyridoxal phosphate)lysine

Natural variations

Natural variant701N → D: dbSNP rs16973344.
VAR_048226
Natural variant3621G → V in TYRO2. dbSNP rs28934277.
VAR_000560

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P17735-1 [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: 1973834] [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: 7908801] [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: 7999802] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 14702039] [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]"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.
[7]"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: 1357662] [Abstract]
Cited for: VARIANT TYRO2 VAL-362.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

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.
IPIIPI00016764.
PIRS10887.
RefSeqNP_000344.1.
UniGeneHs.161640

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3DYDX-ray2.30A/B41-444[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP17735.

Proteomic databases

PRIDEP17735.

Genome annotation databases

EnsemblENST00000355962; ENSP00000348234; ENSG00000198650; Homo sapiens. [Genome view]
GeneID6898.
KEGGhsa:6898.
UCSCuc002fap.2. human.

Organism-specific databases

CTD6898.
GeneCardsGC16M070158.
H-InvDBHIX0038602.
HGNCHGNC:11573. TAT.
MIM276600. gene+phenotype.
Orphanet28378. Tyrosinemia, type 2.
PharmGKBPA36338.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP17735.
HOVERGENP17735.
OMACVPILAD
OrthoDBEOG9MSGJ9

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12018.
BRENDA2.6.1.5. 247.
Pathway_Interaction_DBhnf3bpathway. FOXA2 and FOXA3 transcription factor networks.
ReactomeREACT_13. Metabolism of amino acids.

Gene expression databases

ArrayExpressP17735.
BgeeP17735.
CleanExHS_TAT.
GenevestigatorP17735.
GermOnlineENSG00000198650. Homo sapiens.

Family and domain databases

InterProIPR001176. ACC_synthase.
IPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase_major.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR011715. Tyr_aa_trans_ubi.
IPR005958. TyrNic_aminoTrfase.
IPR005957. Tyrosine_aminoTrfase.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
PF07706. TAT_ubiq. 1 hit.
[Graphical view]
PRINTSPR00753. ACCSYNTHASE.
TIGRFAMsTIGR01264. tyr_amTase_E. 1 hit.
TIGR01265. tyr_nico_aTase. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00142. L-Glutamic Acid.
DB00120. L-Phenylalanine.
DB00135. L-Tyrosine.
DB00114. Pyridoxal Phosphate.
NextBio26963.
SOURCESearch...

Entry information

Entry nameATTY_HUMAN
AccessionPrimary (citable) accession number: P17735
Secondary accession number(s): B2R8I1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 24, 2009
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents