CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005312
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Inosine-5'-monophosphate dehydrogenase 2 
Protein Synonyms/Alias
 IMP dehydrogenase 2; IMPD 2; IMPDH 2; IMPDH-II 
Gene Name
 Impdh2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
109NEVRKVKKYEQGFITacetylation[1]
109NEVRKVKKYEQGFITubiquitination[2]
134VRDVFEAKARHGFCGubiquitination[2]
195APAGVTLKEANEILQubiquitination[2]
206EILQRSKKGKLPIVNubiquitination[2]
208LQRSKKGKLPIVNENubiquitination[2]
242LASKDAKKQLLCGAAubiquitination[2]
257IGTHEDDKYRLDLLAacetylation[3]
293MIKYIKEKYPSLQVIubiquitination[2]
450VSGAVQDKGSIHKFVubiquitination[2]
474SCQDIGAKSLTQVRAubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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
Functional Description
 Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism (By similarity). It may also have a role in the development of malignancy and the growth progression of some tumors. 
Sequence Annotation
 DOMAIN 114 173 CBS 1.
 DOMAIN 179 237 CBS 2.
 NP_BIND 274 276 NAD (By similarity).
 NP_BIND 324 326 NAD (By similarity).
 REGION 364 366 IMP binding (By similarity).
 REGION 387 388 IMP binding (By similarity).
 REGION 411 415 IMP binding (By similarity).
 ACT_SITE 331 331 Thioimidate intermediate (By similarity).
 METAL 326 326 Potassium; via carbonyl oxygen (By
 METAL 328 328 Potassium; via carbonyl oxygen (By
 METAL 331 331 Potassium; via carbonyl oxygen (By
 METAL 500 500 Potassium; via carbonyl oxygen; shared
 METAL 501 501 Potassium; via carbonyl oxygen; shared
 METAL 502 502 Potassium; via carbonyl oxygen; shared
 BINDING 329 329 IMP (By similarity).
 BINDING 441 441 IMP (By similarity).
 MOD_RES 122 122 Phosphoserine (By similarity).
 MOD_RES 400 400 Phosphotyrosine (By similarity).
 MOD_RES 416 416 Phosphoserine (By similarity).
 MOD_RES 511 511 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; CBS domain; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; GMP biosynthesis; Metal-binding; NAD; Nucleus; Oxidoreductase; Phosphoprotein; Potassium; Purine biosynthesis; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 514 AA 
Protein Sequence
MADYLISGGT SYVPDDGLTA QQLFNCGDGL TYNDFLILPG YIDFTADQVD LTSALTKKIT 60
LKTPLVSSPM DTVTEAGMAI AMALTGGIGF IHHNCTPEFQ ANEVRKVKKY EQGFITDPVV 120
LSPKDRVRDV FEAKARHGFC GIPITDTGRM GSRLVGIISS RDIDFLKEEE HDRFLEEIMT 180
KREDLVVAPA GVTLKEANEI LQRSKKGKLP IVNENDELVA IIARTDLKKN RDYPLASKDA 240
KKQLLCGAAI GTHEDDKYRL DLLALAGVDV VVLDSSQGNS IFQINMIKYI KEKYPSLQVI 300
GGNVVTAAQA KNLIDAGVDA LRVGMGSGSI CITQEVLACG RPQATAVYKV SEYARRFGVP 360
VIADGGIQNV GHIAKALALG ASTVMMGSLL AATTEAPGEY FFSDGIRLKK YRGMGSLDAM 420
DKHLSSQNRY FSEADKIKVA QGVSGAVQDK GSIHKFVPYL IAGIQHSCQD IGAKSLTQVR 480
AMMYSGELKF EKRTSSAQVE GGVHSLHSYE KRLF 514 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0005778; C:peroxisomal membrane; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003938; F:IMP dehydrogenase activity; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:HAMAP.
 GO:0000166; F:nucleotide binding; ISS:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
 GO:0006177; P:GMP biosynthetic process; IEA:HAMAP.
 GO:0046651; P:lymphocyte proliferation; IMP:MGI.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 GO:0006164; P:purine nucleotide biosynthetic process; IMP:MGI.
 GO:0060041; P:retina development in camera-type eye; IEA:Compara. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR000644; Cysta_beta_synth_core.
 IPR005990; IMP_DH.
 IPR015875; IMP_DH/GMP_Rdtase_CS.
 IPR001093; IMP_DH_GMPRt. 
Pfam
 PF00571; CBS
 PF00478; IMPDH 
SMART
 SM00116; CBS 
PROSITE
 PS51371; CBS
 PS00487; IMP_DH_GMP_RED 
PRINTS