CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014378
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 D-3-phosphoglycerate dehydrogenase 
Protein Synonyms/Alias
 3-PGDH; A10 
Gene Name
 Phgdh 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
8MAFANLRKVLISDSLacetylation[1, 2]
8MAFANLRKVLISDSLsuccinylation[2]
21SLDPCCRKILQDGGLacetylation[1, 2]
21SLDPCCRKILQDGGLubiquitination[3]
33GGLQVVEKQNLSKEEacetylation[1, 4]
58LIVRSATKVTADVINubiquitination[3]
289PHLGASTKEAQSRCGacetylation[4]
394DVNLVNAKLLVKEAGacetylation[1, 2, 4]
394DVNLVNAKLLVKEAGsuccinylation[2]
394DVNLVNAKLLVKEAGubiquitination[3]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] 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]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
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
MAFANLRKVL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT 60
ADVINAAEKL QVVGRAGTGV DNVDLEAATR KGILVMNTPN GNSLSAAELT CGMIMCLARQ 120
IPQATASMKD GKWDRKKFMG TELNGKTLGI LGLGRIGREV ATRMQSFGMK TVGYDPIISP 180
EVAASFGVQQ LPLEEIWPLC DFITVHTPLL PSTTGLLNDS TFAQCKKGVR VVNCARGGIV 240
DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVDHENVIS CPHLGASTKE AQSRCGEEIA 300
VQFVDMVKGK SLTGVVNAQA LTSAFSPHTK PWIGLAEAMG TLMHAWAGSP KGTIQVVTQG 360
TSLKNAGTCL SPAVIVGLLR EASKQADVNL VNAKLLVKEA GLNVTTSHNP GVPGEQGSGE 420
CLLTVALAGA PYQAVGLVQG TTPMLQMLNG AVFRPEVPLR RGQPLLVFRA QPSDPGMLPT 480
MIGLLAEAGV QLLSYQTSMV SDGEPWHVMG LSSLLPSLET WKQHVLEAFQ FCF 533 
Gene Ontology
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0004617; F:phosphoglycerate dehydrogenase activity; TAS:MGI.
 GO:0070314; P:G1 to G0 transition; IMP:MGI.
 GO:0009448; P:gamma-aminobutyric acid metabolic process; IMP:MGI.
 GO:0021782; P:glial cell development; IMP:MGI.
 GO:0006541; P:glutamine metabolic process; IMP:MGI.
 GO:0006544; P:glycine metabolic process; IMP:MGI.
 GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
 GO:0006563; P:L-serine metabolic process; IMP:MGI.
 GO:0021915; P:neural tube development; IMP:MGI.
 GO:0031175; P:neuron projection development; IMP:MGI.
 GO:0010468; P:regulation of gene expression; IMP:MGI.
 GO:0021510; P:spinal cord development; IMP:MGI.
 GO:0019530; P:taurine metabolic process; IMP:MGI.
 GO:0006566; P:threonine metabolic process; IMP:MGI. 
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