CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015216
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyridoxal-dependent decarboxylase domain-containing protein 1 
Protein Synonyms/Alias
  
Gene Name
 PDXDC1 
Gene Synonyms/Alias
 KIAA0251 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
226AFLEKLIKDDIERGRubiquitination[1]
331VAGLTSNKPTDKLRAubiquitination[1]
406PGSDPVFKAVPVPNMubiquitination[1, 2]
536NDDKSSLKSDPEGENubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
  
Sequence Annotation
 MOD_RES 212 212 Phosphoserine (By similarity).
 MOD_RES 652 652 Phosphoserine.
 MOD_RES 687 687 Phosphothreonine (By similarity).
 MOD_RES 691 691 Phosphothreonine.
 MOD_RES 710 710 Phosphoserine.
 MOD_RES 718 718 Phosphoserine.
 MOD_RES 722 722 Phosphoserine (By similarity).
 MOD_RES 757 757 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Decarboxylase; Lyase; Phosphoprotein; Polymorphism; Pyridoxal phosphate; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 788 AA 
Protein Sequence
MDASLEKIAD PTLAEMGKNL KEAVKMLEDS QRRTEEENGK KLISGDIPGP LQGSGQDMVS 60
ILQLVQNLMH GDEDEEPQSP RIQNIGEQGH MALLGHSLGA YISTLDKEKL RKLTTRILSD 120
TTLWLCRIFR YENGCAYFHE EEREGLAKIC RLAIHSRYED FVVDGFNVLY NKKPVIYLSA 180
AARPGLGQYL CNQLGLPFPC LCRVPCNTVF GSQHQMDVAF LEKLIKDDIE RGRLPLLLVA 240
NAGTAAVGHT DKIGRLKELC EQYGIWLHVE GVNLATLALG YVSSSVLAAA KCDSMTMTPG 300
PWLGLPAVPA VTLYKHDDPA LTLVAGLTSN KPTDKLRALP LWLSLQYLGL DGFVERIKHA 360
CQLSQRLQES LKKVNYIKIL VEDELSSPVV VFRFFQELPG SDPVFKAVPV PNMTPSGVGR 420
ERHSCDALNR WLGEQLKQLV PASGLTVMDL EAEGTCLRFS PLMTAAVLGT RGEDVDQLVA 480
CIESKLPVLC CTLQLREEFK QEVEATAGLL YVDDPNWSGI GVVRYEHAND DKSSLKSDPE 540
GENIHAGLLK KLNELESDLT FKIGPEYKSM KSCLYVGMAS DNVDAAELVE TIAATAREIE 600
ENSRLLENMT EVVRKGIQEA QVELQKASEE RLLEEGVLRQ IPVVGSVLNW FSPVQALQKG 660
RTFNLTAGSL ESTEPIYVYK AQGAGVTLPP TPSGSRTKQR LPGQKPFKRS LRGSDALSET 720
SSVSHIEDLE KVERLSSGPE QITLEASSTE GHPGAPSPQH TDQTEAFQKG VPHPEDDHSQ 780
VEGPESLR 788 
Gene Ontology
 GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro. 
Interpro
 IPR002129; PyrdxlP-dep_de-COase.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00282; Pyridoxal_deC 
SMART
  
PROSITE
 PS00392; DDC_GAD_HDC_YDC 
PRINTS