CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016635
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ethanolamine-phosphate phospho-lyase 
Protein Synonyms/Alias
 Alanine--glyoxylate aminotransferase 2-like 1 
Gene Name
 Etnppl 
Gene Synonyms/Alias
 Agxt2l1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
23RHIGPSCKIFFAADPacetylation[1]
32FFAADPIKIMRAQGQubiquitination[2]
45GQYMFDEKGERYLDCubiquitination[2]
72EVVKAAAKQMELLNTubiquitination[2]
93DNIIEFAKRLTATLPubiquitination[2]
177APDTYRGKYREDHEDubiquitination[2]
351MELLSEQKAKHPLIGubiquitination[2]
460AYRTKMPKEIQVELPubiquitination[2]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde (By similarity). 
Sequence Annotation
 MOD_RES 278 278 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Aminotransferase; Complete proteome; Lyase; Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 499 AA 
Protein Sequence
MCELYSKQDT LALRERHIGP SCKIFFAADP IKIMRAQGQY MFDEKGERYL DCINNVAHVG 60
HCHPEVVKAA AKQMELLNTN SRFLHDNIIE FAKRLTATLP QELSVCYFTN SGSEANDLAL 120
RLARQFRGHQ DVITLDHAYH GHLSSLIEIS PYKFQKGKDV KRETVHVAPA PDTYRGKYRE 180
DHEDPSTAYA DEVKKIIEEA HSSGRKIAAF IAESMQSCGG QIIPPAGYFQ KVAEHIHKAG 240
GVFIADEVQV GFGRVGRYFW SFQMYGEDFV PDIVTMGKPM GNGHPISCVV TTKEIAEAFS 300
SSGMEYFNTY GGNPVSCAVG LAVLDVIEKE NLQGNAVRVG TYLMELLSEQ KAKHPLIGDI 360
RGVGLFIGID LVKDREKRTP ATAEAQHIIY EMKGKGVLLS ADGPHRNVLK IKPPMCFTED 420
DAKFLVDHLD GILTVLEEAM DSKSGTVFSE NTAYRTKMPK EIQVELPNLS ATEAREIPRG 480
KRNGVCSDQQ ALLSKRLKT 499 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0050459; F:ethanolamine-phosphate phospho-lyase activity; IEA:EC.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
 GO:0008152; P:metabolic process; IEA:GOC. 
Interpro
 IPR005814; Aminotrans_3.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00202; Aminotran_3 
SMART
  
PROSITE
 PS00600; AA_TRANSFER_CLASS_3 
PRINTS