CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016966
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 5-phosphohydroxy-L-lysine phospho-lyase 
Protein Synonyms/Alias
 Alanine--glyoxylate aminotransferase 2-like 2 
Gene Name
 PHYKPL 
Gene Synonyms/Alias
 AGXT2L2; PP9286 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MAADQRPKADTLALRubiquitination[1]
33FFPEDPVKIVRAQGQacetylation[2]
33FFPEDPVKIVRAQGQubiquitination[1]
278PDIVTMGKSIGNGHPubiquitination[1]
353LLGQQKIKHPIVGDVubiquitination[1]
393AYLVSRLKENYVLLSubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
 Catalyzes the pyridoxal-phosphate-dependent breakdown of 5-phosphohydroxy-L-lysine, converting it to ammonia, inorganic phosphate and 2-aminoadipate semialdehyde. 
Sequence Annotation
 MOD_RES 278 278 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Alternative splicing; Aminotransferase; Complete proteome; Disease mutation; Lyase; Mitochondrion; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 450 AA 
Protein Sequence
MAADQRPKAD TLALRQRLIS SSCRLFFPED PVKIVRAQGQ YMYDEQGAEY IDCISNVAHV 60
GHCHPLVVQA AHEQNQVLNT NSRYLHDNIV DYAQRLSETL PEQLCVFYFL NSGSEANDLA 120
LRLARHYTGH QDVVVLDHAY HGHLSSLIDI SPYKFRNLDG QKEWVHVAPL PDTYRGPYRE 180
DHPNPAMAYA NEVKRVVSSA QEKGRKIAAF FAESLPSVGG QIIPPAGYFS QVAEHIRKAG 240
GVFVADEIQV GFGRVGKHFW AFQLQGKDFV PDIVTMGKSI GNGHPVACVA ATQPVARAFE 300
ATGVEYFNTF GGSPVSCAVG LAVLNVLEKE QLQDHATSVG SFLMQLLGQQ KIKHPIVGDV 360
RGVGLFIGVD LIKDEATRTP ATEEAAYLVS RLKENYVLLS TDGPGRNILK FKPPMCFSLD 420
NARQVVAKLD AILTDMEEKV RSCETLRLQP 450 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
 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