CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007219
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 D-lactate dehydrogenase [cytochrome] 3 
Protein Synonyms/Alias
 D-lactate ferricytochrome C oxidoreductase; D-LCR 
Gene Name
 DLD3 
Gene Synonyms/Alias
 YEL071W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
17LTAEAYPKVKRNPNFubiquitination[1, 2, 3]
329EKLTAFLKDTTDSKLacetylation[4]
335LKDTTDSKLISEGMMacetylation[4]
357DRLWTWRKSVPTACNubiquitination[5]
461EHGIGFHKKGKLHYTacetylation[4]
481IRFMKDIKNHYDPNGacetylation[4]
Reference
 [1] A proteomics approach to understanding protein ubiquitination.
 Peng J, Schwartz D, Elias JE, Thoreen CC, Cheng D, Marsischky G, Roelofs J, Finley D, Gygi SP.
 Nat Biotechnol. 2003 Aug;21(8):921-6. [PMID: 12872131]
 [2] Computational identification of ubiquitylation sites from protein sequences.
 Tung CW, Ho SY.
 BMC Bioinformatics. 2008 Jul 15;9:310. [PMID: 18625080]
 [3] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
 [4] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [5] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
  
Sequence Annotation
 DOMAIN 64 243 FAD-binding PCMH-type.
 CROSSLNK 17 17 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; Cytoplasm; FAD; Flavoprotein; Isopeptide bond; Oxidoreductase; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 496 AA 
Protein Sequence
MTAAHPVAQL TAEAYPKVKR NPNFKVLDSE DLAYFRSILS NDEILNSQAP EELASFNQDW 60
MKKYRGQSNL ILLPNSTDKV SKIMKYCNDK KLAVVPQGGN TDLVGASVPV FDEIVLSLRN 120
MNKVRDFDPV SGTFKCDAGV VMRDAHQFLH DHDHIFPLDL PSRNNCQVGG VVSTNAGGLN 180
FLRYGSLHGN VLGLEVVLPN GEIISNINAL RKDNTGYDLK QLFIGAEGTI GVVTGVSIVA 240
AAKPKALNAV FFGIENFDTV QKLFVKAKSE LSEILSAFEF MDRGSIECTI EYLKDLPFPL 300
ENQHNFYVLI ETSGSNKRHD DEKLTAFLKD TTDSKLISEG MMAKDKADFD RLWTWRKSVP 360
TACNSYGGMY KYDMSLQLKD LYSVSAAVTE RLNAAGLIGD APKPVVKSCG YGHVGDGNIH 420
LNIAVREFTK QIEDLLEPFV YEYIASKKGS ISAEHGIGFH KKGKLHYTRS DIEIRFMKDI 480
KNHYDPNGIL NPYKYI 496 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IDA:SGD.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro.
 GO:0030447; P:filamentous growth; IMP:SGD.
 GO:0006089; P:lactate metabolic process; ISS:SGD. 
Interpro
 IPR016169; CO_DH_flavot_FAD-bd_sub2.
 IPR016166; FAD-bd_2.
 IPR016167; FAD-bd_2_sub1.
 IPR016164; FAD-linked_Oxase-like_C.
 IPR004113; FAD-linked_oxidase_C.
 IPR006094; Oxid_FAD_bind_N.
 IPR016171; Vanillyl_alc_oxidase_C-sub2. 
Pfam
 PF02913; FAD-oxidase_C
 PF01565; FAD_binding_4 
SMART
  
PROSITE
 PS51387; FAD_PCMH 
PRINTS