CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000165
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 D-3-phosphoglycerate dehydrogenase 
Protein Synonyms/Alias
 3-PGDH 
Gene Name
 Phgdh 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
58LIVRSATKVTADVINacetylation[1]
58LIVRSATKVTADVINubiquitination[2]
132TASMKDGKWDRKKFMacetylation[1]
137DGKWDRKKFMGTELNubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113
Functional Description
  
Sequence Annotation
 NP_BIND 155 156 NAD (By similarity).
 NP_BIND 234 236 NAD (By similarity).
 NP_BIND 283 286 NAD (By similarity).
 ACT_SITE 236 236 By similarity.
 ACT_SITE 265 265 By similarity.
 ACT_SITE 283 283 Proton donor (By similarity).
 BINDING 78 78 NAD (By similarity).
 BINDING 175 175 NAD (By similarity).
 BINDING 207 207 NAD; via carbonyl oxygen (By similarity).
 BINDING 260 260 NAD (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).  
Keyword
 Acetylation; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; NAD; Oxidoreductase; Reference proteome; Serine biosynthesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 533 AA 
Protein Sequence
MAFANLRKIL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT 60
ADVINAAEKL QVVGRAGTGV DNVDLEAATR KGVLVMNTPN GNSLSAAELT CGMLMCLARQ 120
IPQATASMKD GKWDRKKFMG TELNGKTLGI LGLGRIGREV AARMQAFGMK TVGYDPIISP 180
EVAASFGVQQ LPLEEIWPLC DFITVHTPLL PSTTGLLNDS TFAQCKKGVR VVNCARGGIV 240
DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVDHENVIS CPHLGASTKE AQSRCGEEIA 300
VQFVDMVKGK SLTGVVNAQA LTSAFSPHTK PWIGLAEALG TLMHAWAGSP KGTIQVVTQG 360
TSLKNAGTCL SPAVIVGLLR EASKQADVNL VNAKLLVKEA GLNVTTSHSP GVPGEQGIGE 420
CLLTVALAGA PYQAVGLVQG TTPMLQMLNG AVFRPEVPLR RGQPLLLFRA QPSDPVMLPT 480
MIGLLAEAGV QLLSYQTSKV SDGDTWHVMG LSSLLPSLDA WKQHVSEAFQ FCF 533 
Gene Ontology
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0004617; F:phosphoglycerate dehydrogenase activity; IDA:RGD.
 GO:0022402; P:cell cycle process; IEA:Compara.
 GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:Compara.
 GO:0021782; P:glial cell development; IEA:Compara.
 GO:0006541; P:glutamine metabolic process; IEA:Compara.
 GO:0006544; P:glycine metabolic process; IEA:Compara.
 GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
 GO:0021915; P:neural tube development; IEA:Compara.
 GO:0031175; P:neuron projection development; IEA:Compara.
 GO:0010468; P:regulation of gene expression; IEA:Compara.
 GO:0009070; P:serine family amino acid biosynthetic process; TAS:RGD.
 GO:0021510; P:spinal cord development; IEA:Compara.
 GO:0019530; P:taurine metabolic process; IEA:Compara.
 GO:0006566; P:threonine metabolic process; IEA:Compara. 
Interpro
 IPR006236; D-3-Phosphoglycerate_DH.
 IPR006139; D-isomer_2_OHA_DH_cat_dom.
 IPR006140; D-isomer_2_OHA_DH_NAD-bd.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF00389; 2-Hacid_dh
 PF02826; 2-Hacid_dh_C 
SMART
  
PROSITE
 PS00065; D_2_HYDROXYACID_DH_1
 PS00670; D_2_HYDROXYACID_DH_2
 PS00671; D_2_HYDROXYACID_DH_3 
PRINTS