CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006207
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 4-hydroxyphenylpyruvate dioxygenase 
Protein Synonyms/Alias
 4-hydroxyphenylpyruvic acid oxidase; 4HPPD; HPD; HPPDase 
Gene Name
 HPD 
Gene Synonyms/Alias
 PPD 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
39AASFYCSKMGFEPLAubiquitination[1]
63EVVSHVIKQGKIVFVubiquitination[1]
80SALNPWNKEMGDHLVubiquitination[1]
94VKHGDGVKDIAFEVEubiquitination[1]
109DCDYIVQKARERGAKubiquitination[1]
127EPWVEQDKFGKVKFAubiquitination[1]
175PLLPKLPKCSLEMIDubiquitination[1]
202SASEWYLKNLQFHRFubiquitination[1]
237ANYEESIKMPINEPAubiquitination[1]
247INEPAPGKKKSQIQEubiquitination[1]
249EPAPGKKKSQIQEYVubiquitination[1]
270GVQHIALKTEDIITAubiquitination[1]
297SVPSTYYKQLREKLKubiquitination[1, 2, 3]
311KTAKIKVKENIDALEubiquitination[1]
369GNFNSLFKAFEEEQNubiquitination[1]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 Key enzyme in the degradation of tyrosine. 
Sequence Annotation
 METAL 183 183 Iron (Probable).
 METAL 266 266 Iron (Probable).
 METAL 349 349 Iron (Probable).
 MOD_RES 2 2 N-acetylthreonine (By similarity).
 MOD_RES 250 250 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Dioxygenase; Disease mutation; Iron; Mental retardation; Metal-binding; Oxidoreductase; Phenylalanine catabolism; Phosphoprotein; Polymorphism; Reference proteome; Tyrosine catabolism. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 393 AA 
Protein Sequence
MTTYSDKGAK PERGRFLHFH SVTFWVGNAK QAASFYCSKM GFEPLAYRGL ETGSREVVSH 60
VIKQGKIVFV LSSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDYIVQKA RERGAKIMRE 120
PWVEQDKFGK VKFAVLQTYG DTTHTLVEKM NYIGQFLPGY EAPAFMDPLL PKLPKCSLEM 180
IDHIVGNQPD QEMVSASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSIVVA NYEESIKMPI 240
NEPAPGKKKS QIQEYVDYNG GAGVQHIALK TEDIITAIRH LRERGLEFLS VPSTYYKQLR 300
EKLKTAKIKV KENIDALEEL KILVDYDEKG YLLQIFTKPV QDRPTLFLEV IQRHNHQGFG 360
AGNFNSLFKA FEEEQNLRGN LTNMETNGVV PGM 393 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0006559; P:L-phenylalanine catabolic process; TAS:Reactome.
 GO:0006572; P:tyrosine catabolic process; ISS:UniProtKB. 
Interpro
 IPR005956; 4OHPhenylPyrv_dOase.
 IPR004360; Glyas_Fos-R_dOase_dom. 
Pfam
 PF00903; Glyoxalase 
SMART
  
PROSITE
  
PRINTS