CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005167
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycine dehydrogenase [decarboxylating], mitochondrial 
Protein Synonyms/Alias
 Glycine cleavage system P protein; Glycine decarboxylase 
Gene Name
 GLDC 
Gene Synonyms/Alias
 GCSP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
272QYPDTEGKVEDFTELubiquitination[1]
358VTRDATGKEVYRLALubiquitination[1, 2]
423LILSEGLKRAGHQLQubiquitination[1]
447IQCGCSVKEVLGRAAubiquitination[1, 2]
514GIPGSVFKRTSPFLTubiquitination[1]
636IRAYLNQKGEGHRTVubiquitination[2]
672IQPVEVDKYGNIDAVubiquitination[1, 2]
773GMGPIGVKKHLAPFLubiquitination[3]
774MGPIGVKKHLAPFLPubiquitination[1]
789NHPVISLKRNEDACPubiquitination[1]
871ILDTRPFKKSANIEAubiquitination[1]
872LDTRPFKKSANIEAVubiquitination[1]
883IEAVDVAKRLQDYGFubiquitination[1, 2]
977AFPLPFVKPENKFWPubiquitination[1]
981PFVKPENKFWPTIARubiquitination[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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. 
Sequence Annotation
 MOD_RES 754 754 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Complete proteome; Disease mutation; Mitochondrion; Oxidoreductase; Pyridoxal phosphate; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1020 AA 
Protein Sequence
MQSCARAWGL RLGRGVGGGR RLAGGSGPCW APRSRDSSSG GGDSAAAGAS RLLERLLPRH 60
DDFARRHIGP GDKDQREMLQ TLGLASIDEL IEKTVPANIR LKRPLKMEDP VCENEILATL 120
HAISSKNQIW RSYIGMGYYN CSVPQTILRN LLENSGWITQ YTPYQPEVSQ GRLESLLNYQ 180
TMVCDITGLD MANASLLDEG TAAAEALQLC YRHNKRRKFL VDPRCHPQTI AVVQTRAKYT 240
GVLTELKLPC EMDFSGKDVS GVLFQYPDTE GKVEDFTELV ERAHQSGSLA CCATDLLALC 300
ILRPPGEFGV DIALGSSQRF GVPLGYGGPH AAFFAVRESL VRMMPGRMVG VTRDATGKEV 360
YRLALQTREQ HIRRDKATSN ICTAQALLAN MAAMFAIYHG SHGLEHIARR VHNATLILSE 420
GLKRAGHQLQ HDLFFDTLKI QCGCSVKEVL GRAAQRQINF RLFEDGTLGI SLDETVNEKD 480
LDDLLWIFGC ESSAELVAES MGEECRGIPG SVFKRTSPFL THQVFNSYHS ETNIVRYMKK 540
LENKDISLVH SMIPLGSCTM KLNSSSELAP ITWKEFANIH PFVPLDQAQG YQQLFRELEK 600
DLCELTGYDQ VCFQPNSGAQ GEYAGLATIR AYLNQKGEGH RTVCLIPKSA HGTNPASAHM 660
AGMKIQPVEV DKYGNIDAVH LKAMVDKHKE NLAAIMITYP STNGVFEENI SDVCDLIHQH 720
GGQVYLDGAN MNAQVGICRP GDFGSDVSHL NLHKTFCIPH GGGGPGMGPI GVKKHLAPFL 780
PNHPVISLKR NEDACPVGTV SAAPWGSSSI LPISWAYIKM MGGKGLKQAT ETAILNANYM 840
AKRLETHYRI LFRGARGYVG HEFILDTRPF KKSANIEAVD VAKRLQDYGF HAPTMSWPVA 900
GTLMVEPTES EDKAELDRFC DAMISIRQEI ADIEEGRIDP RVNPLKMSPH SLTCVTSSHW 960
DRPYSREVAA FPLPFVKPEN KFWPTIARID DIYGDQHLVC TCPPMEVYES PFSEQKRASS 1020 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0009055; F:electron carrier activity; TAS:UniProtKB.
 GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; TAS:ProtInc.
 GO:0016829; F:lyase activity; IEA:InterPro.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006546; P:glycine catabolic process; TAS:ProtInc. 
Interpro
 IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
 IPR020580; GDC-P_N.
 IPR020581; GDC_P.
 IPR003437; GDC_P_homo.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1. 
Pfam
 PF01212; Beta_elim_lyase
 PF02347; GDC-P 
SMART
  
PROSITE
  
PRINTS